data_5MSA
# 
_entry.id   5MSA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.397 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   5MSA         pdb_00005msa 10.2210/pdb5msa/pdb 
WWPDB D_1200002927 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2018-01-17 
2 'Structure model' 1 1 2024-01-17 
3 'Structure model' 1 2 2024-10-09 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 2 'Structure model' 'Refinement description' 
5 3 'Structure model' 'Structure summary'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' diffrn_radiation_wavelength   
5 2 'Structure model' pdbx_initial_refinement_model 
6 2 'Structure model' struct_conn                   
7 3 'Structure model' pdbx_entry_details            
8 3 'Structure model' pdbx_modification_feature     
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_database_2.pdbx_DOI'                    
2  2 'Structure model' '_database_2.pdbx_database_accession'     
3  2 'Structure model' '_diffrn_radiation_wavelength.wavelength' 
4  2 'Structure model' '_struct_conn.pdbx_dist_value'            
5  2 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'    
6  2 'Structure model' '_struct_conn.ptnr1_auth_asym_id'         
7  2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'         
8  2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'          
9  2 'Structure model' '_struct_conn.ptnr1_label_asym_id'        
10 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'        
11 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'        
12 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'         
13 2 'Structure model' '_struct_conn.ptnr2_auth_asym_id'         
14 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'         
15 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'          
16 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'        
17 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'        
18 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'        
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5MSA 
_pdbx_database_status.recvd_initial_deposition_date   2017-01-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'Human carbonic anhydrase isozyme II with ligand'   5LLC unspecified 
PDB 'Human carbonic anhydrase isozyme II with ligand'   5LLE unspecified 
PDB 'Human carbonic anhydrase isozyme II with ligand'   5LLG unspecified 
PDB 'Human carbonic anhydrase isozyme II with ligand'   5LLH unspecified 
PDB 'Human carbonic anhydrase isozyme XIII with ligand' 5LLN unspecified 
PDB 'Human carbonic anhydrase isozyme XII with ligand'  5LLO unspecified 
PDB 'Human carbonic anhydrase isozyme XII with ligand'  5LLP unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 ? 
'Manakova, E.' 2 ? 
'Grazulis, S.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Crystal structure of human carbonic anhydrase
isozyme XII with 2,3,5,6-Tetrafluoro-4-(propylthio)benzenesulfonamide
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnov, A.'   1 ? 
primary 'Manakova, E.'  2 ? 
primary 'Grazulis, S.'  3 ? 
primary 'Matulis, D.'   4 ? 
primary 'Dudutiene, V.' 5 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 12'                                    29917.318 4    4.2.1.1 ? 
'human carbonic anhydrase XII'                         ? 
2 non-polymer syn 'ZINC ION'                                                 65.409    4    ?       ? 
'2,3,5,6-Tetrafluoro-4-(propylthio)benzenesulfonamide' ? 
3 non-polymer syn '2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' 303.297   4    ?       ? Zn ? 
4 non-polymer syn 1,2-ETHANEDIOL                                             62.068    12   ?       ? 1,2-ETHANEDIOL ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                    106.120   4    ?       ? CITRATE ? 
6 non-polymer syn 'CITRIC ACID'                                              192.124   3    ?       ? 'DI(HYDROXYETHYL)ETHER' ? 
7 water       nat water                                                      18.015    1442 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase XII,Carbonic anhydrase XII,CA-XII,Tumor antigen HOM-RCC-3.1.3' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQG
LQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFS
HLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPR
EMINNFRQVQKFDERLVYTSFSQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQG
LQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFS
HLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPR
EMINNFRQVQKFDERLVYTSFSQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                 ZN  
3 '2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' 3TV 
4 1,2-ETHANEDIOL                                             EDO 
5 'DI(HYDROXYETHYL)ETHER'                                    PEG 
6 'CITRIC ACID'                                              CIT 
7 water                                                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   TRP n 
1 5   THR n 
1 6   TYR n 
1 7   PHE n 
1 8   GLY n 
1 9   PRO n 
1 10  ASP n 
1 11  GLY n 
1 12  GLU n 
1 13  ASN n 
1 14  SER n 
1 15  TRP n 
1 16  SER n 
1 17  LYS n 
1 18  LYS n 
1 19  TYR n 
1 20  PRO n 
1 21  SER n 
1 22  CYS n 
1 23  GLY n 
1 24  GLY n 
1 25  LEU n 
1 26  LEU n 
1 27  GLN n 
1 28  SER n 
1 29  PRO n 
1 30  ILE n 
1 31  ASP n 
1 32  LEU n 
1 33  HIS n 
1 34  SER n 
1 35  ASP n 
1 36  ILE n 
1 37  LEU n 
1 38  GLN n 
1 39  TYR n 
1 40  ASP n 
1 41  ALA n 
1 42  SER n 
1 43  LEU n 
1 44  THR n 
1 45  PRO n 
1 46  LEU n 
1 47  GLU n 
1 48  PHE n 
1 49  GLN n 
1 50  GLY n 
1 51  TYR n 
1 52  ASN n 
1 53  LEU n 
1 54  SER n 
1 55  ALA n 
1 56  ASN n 
1 57  LYS n 
1 58  GLN n 
1 59  PHE n 
1 60  LEU n 
1 61  LEU n 
1 62  THR n 
1 63  ASN n 
1 64  ASN n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  VAL n 
1 69  LYS n 
1 70  LEU n 
1 71  ASN n 
1 72  LEU n 
1 73  PRO n 
1 74  SER n 
1 75  ASP n 
1 76  MET n 
1 77  HIS n 
1 78  ILE n 
1 79  GLN n 
1 80  GLY n 
1 81  LEU n 
1 82  GLN n 
1 83  SER n 
1 84  ARG n 
1 85  TYR n 
1 86  SER n 
1 87  ALA n 
1 88  THR n 
1 89  GLN n 
1 90  LEU n 
1 91  HIS n 
1 92  LEU n 
1 93  HIS n 
1 94  TRP n 
1 95  GLY n 
1 96  ASN n 
1 97  PRO n 
1 98  ASN n 
1 99  ASP n 
1 100 PRO n 
1 101 HIS n 
1 102 GLY n 
1 103 SER n 
1 104 GLU n 
1 105 HIS n 
1 106 THR n 
1 107 VAL n 
1 108 SER n 
1 109 GLY n 
1 110 GLN n 
1 111 HIS n 
1 112 PHE n 
1 113 ALA n 
1 114 ALA n 
1 115 GLU n 
1 116 LEU n 
1 117 HIS n 
1 118 ILE n 
1 119 VAL n 
1 120 HIS n 
1 121 TYR n 
1 122 ASN n 
1 123 SER n 
1 124 ASP n 
1 125 LEU n 
1 126 TYR n 
1 127 PRO n 
1 128 ASP n 
1 129 ALA n 
1 130 SER n 
1 131 THR n 
1 132 ALA n 
1 133 SER n 
1 134 ASN n 
1 135 LYS n 
1 136 SER n 
1 137 GLU n 
1 138 GLY n 
1 139 LEU n 
1 140 ALA n 
1 141 VAL n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 LEU n 
1 146 ILE n 
1 147 GLU n 
1 148 MET n 
1 149 GLY n 
1 150 SER n 
1 151 PHE n 
1 152 ASN n 
1 153 PRO n 
1 154 SER n 
1 155 TYR n 
1 156 ASP n 
1 157 LYS n 
1 158 ILE n 
1 159 PHE n 
1 160 SER n 
1 161 HIS n 
1 162 LEU n 
1 163 GLN n 
1 164 HIS n 
1 165 VAL n 
1 166 LYS n 
1 167 TYR n 
1 168 LYS n 
1 169 GLY n 
1 170 GLN n 
1 171 GLU n 
1 172 ALA n 
1 173 PHE n 
1 174 VAL n 
1 175 PRO n 
1 176 GLY n 
1 177 PHE n 
1 178 ASN n 
1 179 ILE n 
1 180 GLU n 
1 181 GLU n 
1 182 LEU n 
1 183 LEU n 
1 184 PRO n 
1 185 GLU n 
1 186 ARG n 
1 187 THR n 
1 188 ALA n 
1 189 GLU n 
1 190 TYR n 
1 191 TYR n 
1 192 ARG n 
1 193 TYR n 
1 194 ARG n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 CYS n 
1 203 ASN n 
1 204 PRO n 
1 205 THR n 
1 206 VAL n 
1 207 LEU n 
1 208 TRP n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 ARG n 
1 213 ASN n 
1 214 PRO n 
1 215 VAL n 
1 216 GLN n 
1 217 ILE n 
1 218 SER n 
1 219 GLN n 
1 220 GLU n 
1 221 GLN n 
1 222 LEU n 
1 223 LEU n 
1 224 ALA n 
1 225 LEU n 
1 226 GLU n 
1 227 THR n 
1 228 ALA n 
1 229 LEU n 
1 230 TYR n 
1 231 CYS n 
1 232 THR n 
1 233 HIS n 
1 234 MET n 
1 235 ASP n 
1 236 ASP n 
1 237 PRO n 
1 238 SER n 
1 239 PRO n 
1 240 ARG n 
1 241 GLU n 
1 242 MET n 
1 243 ILE n 
1 244 ASN n 
1 245 ASN n 
1 246 PHE n 
1 247 ARG n 
1 248 GLN n 
1 249 VAL n 
1 250 GLN n 
1 251 LYS n 
1 252 PHE n 
1 253 ASP n 
1 254 GLU n 
1 255 ARG n 
1 256 LEU n 
1 257 VAL n 
1 258 TYR n 
1 259 THR n 
1 260 SER n 
1 261 PHE n 
1 262 SER n 
1 263 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   263 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA12 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              Rosetta 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET21a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
3TV non-polymer         . '2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' ?                 'C9 H9 F4 N O2 S2' 303.297 
ALA 'L-peptide linking' y ALANINE                                                    ?                 'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                                                   ?                 'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                 ?                 'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                            ?                 'C4 H7 N O4'       133.103 
CIT non-polymer         . 'CITRIC ACID'                                              ?                 'C6 H8 O7'         192.124 
CYS 'L-peptide linking' y CYSTEINE                                                   ?                 'C3 H7 N O2 S'     121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                             'ETHYLENE GLYCOL' 'C2 H6 O2'         62.068  
GLN 'L-peptide linking' y GLUTAMINE                                                  ?                 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                            ?                 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                                                    ?                 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                                                  ?                 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                                                      ?                 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                 ?                 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                                                    ?                 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                                                     ?                 'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                                                 ?                 'C5 H11 N O2 S'    149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                    ?                 'C4 H10 O3'        106.120 
PHE 'L-peptide linking' y PHENYLALANINE                                              ?                 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                                    ?                 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                                                     ?                 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                                                  ?                 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                 ?                 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                                                   ?                 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                                                     ?                 'C5 H11 N O2'      117.146 
ZN  non-polymer         . 'ZINC ION'                                                 ?                 'Zn 2'             65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   TRP 4   4   4   TRP TRP A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  TRP 15  15  15  TRP TRP A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 MET 148 148 148 MET MET A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 CYS 231 231 231 CYS CYS A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 GLN 263 263 263 GLN GLN A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   TRP 4   4   4   TRP TRP B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   TYR 6   6   6   TYR TYR B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  TRP 15  15  15  TRP TRP B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  TYR 19  19  19  TYR TYR B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASN 52  52  52  ASN ASN B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  MET 76  76  76  MET MET B . n 
B 1 77  HIS 77  77  77  HIS HIS B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  GLN 89  89  89  GLN GLN B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  TRP 94  94  94  TRP TRP B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 HIS 101 101 101 HIS HIS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ASN 122 122 122 ASN ASN B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 SER 130 130 130 SER SER B . n 
B 1 131 THR 131 131 131 THR THR B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 MET 148 148 148 MET MET B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 PHE 151 151 151 PHE PHE B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 TYR 155 155 155 TYR TYR B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 ILE 158 158 158 ILE ILE B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 HIS 161 161 161 HIS HIS B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 GLN 163 163 163 GLN GLN B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLN 170 170 170 GLN GLN B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 THR 187 187 187 THR THR B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 TYR 191 191 191 TYR TYR B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 ARG 194 194 194 ARG ARG B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 CYS 202 202 202 CYS CYS B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 TRP 208 208 208 TRP TRP B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 PHE 211 211 211 PHE PHE B . n 
B 1 212 ARG 212 212 212 ARG ARG B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 CYS 231 231 231 CYS CYS B . n 
B 1 232 THR 232 232 232 THR THR B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 ASP 235 235 235 ASP ASP B . n 
B 1 236 ASP 236 236 236 ASP ASP B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 ARG 240 240 240 ARG ARG B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 MET 242 242 242 MET MET B . n 
B 1 243 ILE 243 243 243 ILE ILE B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 ARG 247 247 247 ARG ARG B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 VAL 249 249 249 VAL VAL B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 PHE 252 252 252 PHE PHE B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 TYR 258 258 258 TYR TYR B . n 
B 1 259 THR 259 259 259 THR THR B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 SER 262 262 262 SER SER B . n 
B 1 263 GLN 263 263 263 GLN GLN B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   2   SER SER C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   TRP 4   4   4   TRP TRP C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   TYR 6   6   6   TYR TYR C . n 
C 1 7   PHE 7   7   7   PHE PHE C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   PRO 9   9   9   PRO PRO C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  GLY 11  11  11  GLY GLY C . n 
C 1 12  GLU 12  12  12  GLU GLU C . n 
C 1 13  ASN 13  13  13  ASN ASN C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  TRP 15  15  15  TRP TRP C . n 
C 1 16  SER 16  16  16  SER SER C . n 
C 1 17  LYS 17  17  17  LYS LYS C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  TYR 19  19  19  TYR TYR C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  CYS 22  22  22  CYS CYS C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLY 24  24  24  GLY GLY C . n 
C 1 25  LEU 25  25  25  LEU LEU C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ASP 35  35  35  ASP ASP C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  LEU 37  37  37  LEU LEU C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  ALA 41  41  41  ALA ALA C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  THR 44  44  44  THR THR C . n 
C 1 45  PRO 45  45  45  PRO PRO C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  GLN 49  49  49  GLN GLN C . n 
C 1 50  GLY 50  50  50  GLY GLY C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ASN 52  52  52  ASN ASN C . n 
C 1 53  LEU 53  53  53  LEU LEU C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  ASN 56  56  56  ASN ASN C . n 
C 1 57  LYS 57  57  57  LYS LYS C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  PHE 59  59  59  PHE PHE C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  THR 62  62  62  THR THR C . n 
C 1 63  ASN 63  63  63  ASN ASN C . n 
C 1 64  ASN 64  64  64  ASN ASN C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  HIS 66  66  66  HIS HIS C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  ASN 71  71  71  ASN ASN C . n 
C 1 72  LEU 72  72  72  LEU LEU C . n 
C 1 73  PRO 73  73  73  PRO PRO C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  MET 76  76  76  MET MET C . n 
C 1 77  HIS 77  77  77  HIS HIS C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  GLY 80  80  80  GLY GLY C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  GLN 82  82  82  GLN GLN C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  TYR 85  85  85  TYR TYR C . n 
C 1 86  SER 86  86  86  SER SER C . n 
C 1 87  ALA 87  87  87  ALA ALA C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  GLN 89  89  89  GLN GLN C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  HIS 91  91  91  HIS HIS C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  HIS 93  93  93  HIS HIS C . n 
C 1 94  TRP 94  94  94  TRP TRP C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  PRO 97  97  97  PRO PRO C . n 
C 1 98  ASN 98  98  98  ASN ASN C . n 
C 1 99  ASP 99  99  99  ASP ASP C . n 
C 1 100 PRO 100 100 100 PRO PRO C . n 
C 1 101 HIS 101 101 101 HIS HIS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 SER 103 103 103 SER SER C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 HIS 105 105 105 HIS HIS C . n 
C 1 106 THR 106 106 106 THR THR C . n 
C 1 107 VAL 107 107 107 VAL VAL C . n 
C 1 108 SER 108 108 108 SER SER C . n 
C 1 109 GLY 109 109 109 GLY GLY C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 HIS 111 111 111 HIS HIS C . n 
C 1 112 PHE 112 112 112 PHE PHE C . n 
C 1 113 ALA 113 113 113 ALA ALA C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 HIS 117 117 117 HIS HIS C . n 
C 1 118 ILE 118 118 118 ILE ILE C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 TYR 121 121 121 TYR TYR C . n 
C 1 122 ASN 122 122 122 ASN ASN C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 TYR 126 126 126 TYR TYR C . n 
C 1 127 PRO 127 127 127 PRO PRO C . n 
C 1 128 ASP 128 128 128 ASP ASP C . n 
C 1 129 ALA 129 129 129 ALA ALA C . n 
C 1 130 SER 130 130 130 SER SER C . n 
C 1 131 THR 131 131 131 THR THR C . n 
C 1 132 ALA 132 132 132 ALA ALA C . n 
C 1 133 SER 133 133 133 SER SER C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 LYS 135 135 135 LYS LYS C . n 
C 1 136 SER 136 136 136 SER SER C . n 
C 1 137 GLU 137 137 137 GLU GLU C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 ALA 143 143 143 ALA ALA C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 LEU 145 145 145 LEU LEU C . n 
C 1 146 ILE 146 146 146 ILE ILE C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 MET 148 148 148 MET MET C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 SER 150 150 150 SER SER C . n 
C 1 151 PHE 151 151 151 PHE PHE C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 SER 154 154 154 SER SER C . n 
C 1 155 TYR 155 155 155 TYR TYR C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 LYS 157 157 157 LYS LYS C . n 
C 1 158 ILE 158 158 158 ILE ILE C . n 
C 1 159 PHE 159 159 159 PHE PHE C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 HIS 161 161 161 HIS HIS C . n 
C 1 162 LEU 162 162 162 LEU LEU C . n 
C 1 163 GLN 163 163 163 GLN GLN C . n 
C 1 164 HIS 164 164 164 HIS HIS C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 TYR 167 167 167 TYR TYR C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 GLY 169 169 169 GLY GLY C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 GLU 171 171 171 GLU GLU C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 PHE 173 173 173 PHE PHE C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 PRO 175 175 175 PRO PRO C . n 
C 1 176 GLY 176 176 176 GLY GLY C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 GLU 180 180 180 GLU GLU C . n 
C 1 181 GLU 181 181 181 GLU GLU C . n 
C 1 182 LEU 182 182 182 LEU LEU C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 ARG 186 186 186 ARG ARG C . n 
C 1 187 THR 187 187 187 THR THR C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 TYR 191 191 191 TYR TYR C . n 
C 1 192 ARG 192 192 192 ARG ARG C . n 
C 1 193 TYR 193 193 193 TYR TYR C . n 
C 1 194 ARG 194 194 194 ARG ARG C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 PRO 201 201 201 PRO PRO C . n 
C 1 202 CYS 202 202 202 CYS CYS C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 VAL 206 206 206 VAL VAL C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 TRP 208 208 208 TRP TRP C . n 
C 1 209 THR 209 209 209 THR THR C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 ARG 212 212 212 ARG ARG C . n 
C 1 213 ASN 213 213 213 ASN ASN C . n 
C 1 214 PRO 214 214 214 PRO PRO C . n 
C 1 215 VAL 215 215 215 VAL VAL C . n 
C 1 216 GLN 216 216 216 GLN GLN C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 GLN 219 219 219 GLN GLN C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 GLN 221 221 221 GLN GLN C . n 
C 1 222 LEU 222 222 222 LEU LEU C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 LEU 225 225 225 LEU LEU C . n 
C 1 226 GLU 226 226 226 GLU GLU C . n 
C 1 227 THR 227 227 227 THR THR C . n 
C 1 228 ALA 228 228 228 ALA ALA C . n 
C 1 229 LEU 229 229 229 LEU LEU C . n 
C 1 230 TYR 230 230 230 TYR TYR C . n 
C 1 231 CYS 231 231 231 CYS CYS C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 MET 234 234 234 MET MET C . n 
C 1 235 ASP 235 235 235 ASP ASP C . n 
C 1 236 ASP 236 236 236 ASP ASP C . n 
C 1 237 PRO 237 237 237 PRO PRO C . n 
C 1 238 SER 238 238 238 SER SER C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 ARG 240 240 240 ARG ARG C . n 
C 1 241 GLU 241 241 241 GLU GLU C . n 
C 1 242 MET 242 242 242 MET MET C . n 
C 1 243 ILE 243 243 243 ILE ILE C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 ASN 245 245 245 ASN ASN C . n 
C 1 246 PHE 246 246 246 PHE PHE C . n 
C 1 247 ARG 247 247 247 ARG ARG C . n 
C 1 248 GLN 248 248 248 GLN GLN C . n 
C 1 249 VAL 249 249 249 VAL VAL C . n 
C 1 250 GLN 250 250 250 GLN GLN C . n 
C 1 251 LYS 251 251 251 LYS LYS C . n 
C 1 252 PHE 252 252 252 PHE PHE C . n 
C 1 253 ASP 253 253 253 ASP ASP C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 ARG 255 255 255 ARG ARG C . n 
C 1 256 LEU 256 256 256 LEU LEU C . n 
C 1 257 VAL 257 257 257 VAL VAL C . n 
C 1 258 TYR 258 258 258 TYR TYR C . n 
C 1 259 THR 259 259 259 THR THR C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 PHE 261 261 261 PHE PHE C . n 
C 1 262 SER 262 262 262 SER SER C . n 
C 1 263 GLN 263 263 263 GLN GLN C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   SER 2   2   ?   ?   ?   D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   TRP 4   4   4   TRP TRP D . n 
D 1 5   THR 5   5   5   THR THR D . n 
D 1 6   TYR 6   6   6   TYR TYR D . n 
D 1 7   PHE 7   7   7   PHE PHE D . n 
D 1 8   GLY 8   8   8   GLY GLY D . n 
D 1 9   PRO 9   9   9   PRO PRO D . n 
D 1 10  ASP 10  10  10  ASP ASP D . n 
D 1 11  GLY 11  11  11  GLY GLY D . n 
D 1 12  GLU 12  12  12  GLU GLU D . n 
D 1 13  ASN 13  13  13  ASN ASN D . n 
D 1 14  SER 14  14  14  SER SER D . n 
D 1 15  TRP 15  15  15  TRP TRP D . n 
D 1 16  SER 16  16  16  SER SER D . n 
D 1 17  LYS 17  17  17  LYS LYS D . n 
D 1 18  LYS 18  18  18  LYS LYS D . n 
D 1 19  TYR 19  19  19  TYR TYR D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  SER 21  21  21  SER SER D . n 
D 1 22  CYS 22  22  22  CYS CYS D . n 
D 1 23  GLY 23  23  23  GLY GLY D . n 
D 1 24  GLY 24  24  24  GLY GLY D . n 
D 1 25  LEU 25  25  25  LEU LEU D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  GLN 27  27  27  GLN GLN D . n 
D 1 28  SER 28  28  28  SER SER D . n 
D 1 29  PRO 29  29  29  PRO PRO D . n 
D 1 30  ILE 30  30  30  ILE ILE D . n 
D 1 31  ASP 31  31  31  ASP ASP D . n 
D 1 32  LEU 32  32  32  LEU LEU D . n 
D 1 33  HIS 33  33  33  HIS HIS D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ASP 35  35  35  ASP ASP D . n 
D 1 36  ILE 36  36  36  ILE ILE D . n 
D 1 37  LEU 37  37  37  LEU LEU D . n 
D 1 38  GLN 38  38  38  GLN GLN D . n 
D 1 39  TYR 39  39  39  TYR TYR D . n 
D 1 40  ASP 40  40  40  ASP ASP D . n 
D 1 41  ALA 41  41  41  ALA ALA D . n 
D 1 42  SER 42  42  42  SER SER D . n 
D 1 43  LEU 43  43  43  LEU LEU D . n 
D 1 44  THR 44  44  44  THR THR D . n 
D 1 45  PRO 45  45  45  PRO PRO D . n 
D 1 46  LEU 46  46  46  LEU LEU D . n 
D 1 47  GLU 47  47  47  GLU GLU D . n 
D 1 48  PHE 48  48  48  PHE PHE D . n 
D 1 49  GLN 49  49  49  GLN GLN D . n 
D 1 50  GLY 50  50  50  GLY GLY D . n 
D 1 51  TYR 51  51  51  TYR TYR D . n 
D 1 52  ASN 52  52  52  ASN ASN D . n 
D 1 53  LEU 53  53  53  LEU LEU D . n 
D 1 54  SER 54  54  54  SER SER D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  ASN 56  56  56  ASN ASN D . n 
D 1 57  LYS 57  57  57  LYS LYS D . n 
D 1 58  GLN 58  58  58  GLN GLN D . n 
D 1 59  PHE 59  59  59  PHE PHE D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  THR 62  62  62  THR THR D . n 
D 1 63  ASN 63  63  63  ASN ASN D . n 
D 1 64  ASN 64  64  64  ASN ASN D . n 
D 1 65  GLY 65  65  65  GLY GLY D . n 
D 1 66  HIS 66  66  66  HIS HIS D . n 
D 1 67  SER 67  67  67  SER SER D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  LEU 70  70  70  LEU LEU D . n 
D 1 71  ASN 71  71  71  ASN ASN D . n 
D 1 72  LEU 72  72  72  LEU LEU D . n 
D 1 73  PRO 73  73  73  PRO PRO D . n 
D 1 74  SER 74  74  74  SER SER D . n 
D 1 75  ASP 75  75  75  ASP ASP D . n 
D 1 76  MET 76  76  76  MET MET D . n 
D 1 77  HIS 77  77  77  HIS HIS D . n 
D 1 78  ILE 78  78  78  ILE ILE D . n 
D 1 79  GLN 79  79  79  GLN GLN D . n 
D 1 80  GLY 80  80  80  GLY GLY D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  GLN 82  82  82  GLN GLN D . n 
D 1 83  SER 83  83  83  SER SER D . n 
D 1 84  ARG 84  84  84  ARG ARG D . n 
D 1 85  TYR 85  85  85  TYR TYR D . n 
D 1 86  SER 86  86  86  SER SER D . n 
D 1 87  ALA 87  87  87  ALA ALA D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  GLN 89  89  89  GLN GLN D . n 
D 1 90  LEU 90  90  90  LEU LEU D . n 
D 1 91  HIS 91  91  91  HIS HIS D . n 
D 1 92  LEU 92  92  92  LEU LEU D . n 
D 1 93  HIS 93  93  93  HIS HIS D . n 
D 1 94  TRP 94  94  94  TRP TRP D . n 
D 1 95  GLY 95  95  95  GLY GLY D . n 
D 1 96  ASN 96  96  96  ASN ASN D . n 
D 1 97  PRO 97  97  97  PRO PRO D . n 
D 1 98  ASN 98  98  98  ASN ASN D . n 
D 1 99  ASP 99  99  99  ASP ASP D . n 
D 1 100 PRO 100 100 100 PRO PRO D . n 
D 1 101 HIS 101 101 101 HIS HIS D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 SER 103 103 103 SER SER D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 HIS 105 105 105 HIS HIS D . n 
D 1 106 THR 106 106 106 THR THR D . n 
D 1 107 VAL 107 107 107 VAL VAL D . n 
D 1 108 SER 108 108 108 SER SER D . n 
D 1 109 GLY 109 109 109 GLY GLY D . n 
D 1 110 GLN 110 110 110 GLN GLN D . n 
D 1 111 HIS 111 111 111 HIS HIS D . n 
D 1 112 PHE 112 112 112 PHE PHE D . n 
D 1 113 ALA 113 113 113 ALA ALA D . n 
D 1 114 ALA 114 114 114 ALA ALA D . n 
D 1 115 GLU 115 115 115 GLU GLU D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 HIS 117 117 117 HIS HIS D . n 
D 1 118 ILE 118 118 118 ILE ILE D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 TYR 121 121 121 TYR TYR D . n 
D 1 122 ASN 122 122 122 ASN ASN D . n 
D 1 123 SER 123 123 123 SER SER D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 LEU 125 125 125 LEU LEU D . n 
D 1 126 TYR 126 126 126 TYR TYR D . n 
D 1 127 PRO 127 127 127 PRO PRO D . n 
D 1 128 ASP 128 128 128 ASP ASP D . n 
D 1 129 ALA 129 129 129 ALA ALA D . n 
D 1 130 SER 130 130 130 SER SER D . n 
D 1 131 THR 131 131 131 THR THR D . n 
D 1 132 ALA 132 132 132 ALA ALA D . n 
D 1 133 SER 133 133 133 SER SER D . n 
D 1 134 ASN 134 134 134 ASN ASN D . n 
D 1 135 LYS 135 135 135 LYS LYS D . n 
D 1 136 SER 136 136 136 SER SER D . n 
D 1 137 GLU 137 137 137 GLU GLU D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 LEU 139 139 139 LEU LEU D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 VAL 141 141 141 VAL VAL D . n 
D 1 142 LEU 142 142 142 LEU LEU D . n 
D 1 143 ALA 143 143 143 ALA ALA D . n 
D 1 144 VAL 144 144 144 VAL VAL D . n 
D 1 145 LEU 145 145 145 LEU LEU D . n 
D 1 146 ILE 146 146 146 ILE ILE D . n 
D 1 147 GLU 147 147 147 GLU GLU D . n 
D 1 148 MET 148 148 148 MET MET D . n 
D 1 149 GLY 149 149 149 GLY GLY D . n 
D 1 150 SER 150 150 150 SER SER D . n 
D 1 151 PHE 151 151 151 PHE PHE D . n 
D 1 152 ASN 152 152 152 ASN ASN D . n 
D 1 153 PRO 153 153 153 PRO PRO D . n 
D 1 154 SER 154 154 154 SER SER D . n 
D 1 155 TYR 155 155 155 TYR TYR D . n 
D 1 156 ASP 156 156 156 ASP ASP D . n 
D 1 157 LYS 157 157 157 LYS LYS D . n 
D 1 158 ILE 158 158 158 ILE ILE D . n 
D 1 159 PHE 159 159 159 PHE PHE D . n 
D 1 160 SER 160 160 160 SER SER D . n 
D 1 161 HIS 161 161 161 HIS HIS D . n 
D 1 162 LEU 162 162 162 LEU LEU D . n 
D 1 163 GLN 163 163 163 GLN GLN D . n 
D 1 164 HIS 164 164 164 HIS HIS D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 LYS 166 166 166 LYS LYS D . n 
D 1 167 TYR 167 167 167 TYR TYR D . n 
D 1 168 LYS 168 168 168 LYS LYS D . n 
D 1 169 GLY 169 169 169 GLY GLY D . n 
D 1 170 GLN 170 170 170 GLN GLN D . n 
D 1 171 GLU 171 171 171 GLU GLU D . n 
D 1 172 ALA 172 172 172 ALA ALA D . n 
D 1 173 PHE 173 173 173 PHE PHE D . n 
D 1 174 VAL 174 174 174 VAL VAL D . n 
D 1 175 PRO 175 175 175 PRO PRO D . n 
D 1 176 GLY 176 176 176 GLY GLY D . n 
D 1 177 PHE 177 177 177 PHE PHE D . n 
D 1 178 ASN 178 178 178 ASN ASN D . n 
D 1 179 ILE 179 179 179 ILE ILE D . n 
D 1 180 GLU 180 180 180 GLU GLU D . n 
D 1 181 GLU 181 181 181 GLU GLU D . n 
D 1 182 LEU 182 182 182 LEU LEU D . n 
D 1 183 LEU 183 183 183 LEU LEU D . n 
D 1 184 PRO 184 184 184 PRO PRO D . n 
D 1 185 GLU 185 185 185 GLU GLU D . n 
D 1 186 ARG 186 186 186 ARG ARG D . n 
D 1 187 THR 187 187 187 THR THR D . n 
D 1 188 ALA 188 188 188 ALA ALA D . n 
D 1 189 GLU 189 189 189 GLU GLU D . n 
D 1 190 TYR 190 190 190 TYR TYR D . n 
D 1 191 TYR 191 191 191 TYR TYR D . n 
D 1 192 ARG 192 192 192 ARG ARG D . n 
D 1 193 TYR 193 193 193 TYR TYR D . n 
D 1 194 ARG 194 194 194 ARG ARG D . n 
D 1 195 GLY 195 195 195 GLY GLY D . n 
D 1 196 SER 196 196 196 SER SER D . n 
D 1 197 LEU 197 197 197 LEU LEU D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 THR 199 199 199 THR THR D . n 
D 1 200 PRO 200 200 200 PRO PRO D . n 
D 1 201 PRO 201 201 201 PRO PRO D . n 
D 1 202 CYS 202 202 202 CYS CYS D . n 
D 1 203 ASN 203 203 203 ASN ASN D . n 
D 1 204 PRO 204 204 204 PRO PRO D . n 
D 1 205 THR 205 205 205 THR THR D . n 
D 1 206 VAL 206 206 206 VAL VAL D . n 
D 1 207 LEU 207 207 207 LEU LEU D . n 
D 1 208 TRP 208 208 208 TRP TRP D . n 
D 1 209 THR 209 209 209 THR THR D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 PHE 211 211 211 PHE PHE D . n 
D 1 212 ARG 212 212 212 ARG ARG D . n 
D 1 213 ASN 213 213 213 ASN ASN D . n 
D 1 214 PRO 214 214 214 PRO PRO D . n 
D 1 215 VAL 215 215 215 VAL VAL D . n 
D 1 216 GLN 216 216 216 GLN GLN D . n 
D 1 217 ILE 217 217 217 ILE ILE D . n 
D 1 218 SER 218 218 218 SER SER D . n 
D 1 219 GLN 219 219 219 GLN GLN D . n 
D 1 220 GLU 220 220 220 GLU GLU D . n 
D 1 221 GLN 221 221 221 GLN GLN D . n 
D 1 222 LEU 222 222 222 LEU LEU D . n 
D 1 223 LEU 223 223 223 LEU LEU D . n 
D 1 224 ALA 224 224 224 ALA ALA D . n 
D 1 225 LEU 225 225 225 LEU LEU D . n 
D 1 226 GLU 226 226 226 GLU GLU D . n 
D 1 227 THR 227 227 227 THR THR D . n 
D 1 228 ALA 228 228 228 ALA ALA D . n 
D 1 229 LEU 229 229 229 LEU LEU D . n 
D 1 230 TYR 230 230 230 TYR TYR D . n 
D 1 231 CYS 231 231 231 CYS CYS D . n 
D 1 232 THR 232 232 232 THR THR D . n 
D 1 233 HIS 233 233 233 HIS HIS D . n 
D 1 234 MET 234 234 234 MET MET D . n 
D 1 235 ASP 235 235 235 ASP ASP D . n 
D 1 236 ASP 236 236 236 ASP ASP D . n 
D 1 237 PRO 237 237 237 PRO PRO D . n 
D 1 238 SER 238 238 238 SER SER D . n 
D 1 239 PRO 239 239 239 PRO PRO D . n 
D 1 240 ARG 240 240 240 ARG ARG D . n 
D 1 241 GLU 241 241 241 GLU GLU D . n 
D 1 242 MET 242 242 242 MET MET D . n 
D 1 243 ILE 243 243 243 ILE ILE D . n 
D 1 244 ASN 244 244 244 ASN ASN D . n 
D 1 245 ASN 245 245 245 ASN ASN D . n 
D 1 246 PHE 246 246 246 PHE PHE D . n 
D 1 247 ARG 247 247 247 ARG ARG D . n 
D 1 248 GLN 248 248 248 GLN GLN D . n 
D 1 249 VAL 249 249 249 VAL VAL D . n 
D 1 250 GLN 250 250 250 GLN GLN D . n 
D 1 251 LYS 251 251 251 LYS LYS D . n 
D 1 252 PHE 252 252 252 PHE PHE D . n 
D 1 253 ASP 253 253 253 ASP ASP D . n 
D 1 254 GLU 254 254 254 GLU GLU D . n 
D 1 255 ARG 255 255 255 ARG ARG D . n 
D 1 256 LEU 256 256 256 LEU LEU D . n 
D 1 257 VAL 257 257 257 VAL VAL D . n 
D 1 258 TYR 258 258 258 TYR TYR D . n 
D 1 259 THR 259 259 259 THR THR D . n 
D 1 260 SER 260 260 260 SER SER D . n 
D 1 261 PHE 261 261 261 PHE PHE D . n 
D 1 262 SER 262 262 262 SER SER D . n 
D 1 263 GLN 263 263 263 GLN GLN D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 ZN  1   301 1    ZN  ZN  A . 
F  3 3TV 1   302 1    3TV V05 A . 
G  4 EDO 1   303 8    EDO EDO A . 
H  4 EDO 1   304 9    EDO EDO A . 
I  4 EDO 1   305 10   EDO EDO A . 
J  5 PEG 1   306 12   PEG PEG A . 
K  4 EDO 1   307 15   EDO EDO A . 
L  4 EDO 1   308 16   EDO EDO A . 
M  4 EDO 1   309 17   EDO EDO A . 
N  4 EDO 1   310 18   EDO EDO A . 
O  2 ZN  1   301 2    ZN  ZN  B . 
P  3 3TV 1   302 2    3TV V05 B . 
Q  4 EDO 1   303 3    EDO EDO B . 
R  5 PEG 1   304 4    PEG PEG B . 
S  6 CIT 1   305 14   CIT CIT B . 
T  2 ZN  1   301 3    ZN  ZN  C . 
U  3 3TV 1   302 3    3TV V05 C . 
V  4 EDO 1   303 1    EDO EDO C . 
W  5 PEG 1   304 11   PEG PEG C . 
X  4 EDO 1   305 19   EDO EDO C . 
Y  2 ZN  1   301 4    ZN  ZN  D . 
Z  3 3TV 1   302 4    3TV V05 D . 
AA 5 PEG 1   303 5    PEG PEG D . 
BA 6 CIT 1   304 6    CIT CIT D . 
CA 4 EDO 1   305 7    EDO EDO D . 
DA 6 CIT 1   306 13   CIT CIT D . 
EA 4 EDO 1   307 20   EDO EDO D . 
FA 7 HOH 1   401 1075 HOH HOH A . 
FA 7 HOH 2   402 446  HOH HOH A . 
FA 7 HOH 3   403 707  HOH HOH A . 
FA 7 HOH 4   404 1377 HOH HOH A . 
FA 7 HOH 5   405 1258 HOH HOH A . 
FA 7 HOH 6   406 1342 HOH HOH A . 
FA 7 HOH 7   407 860  HOH HOH A . 
FA 7 HOH 8   408 1029 HOH HOH A . 
FA 7 HOH 9   409 660  HOH HOH A . 
FA 7 HOH 10  410 1338 HOH HOH A . 
FA 7 HOH 11  411 159  HOH HOH A . 
FA 7 HOH 12  412 1343 HOH HOH A . 
FA 7 HOH 13  413 926  HOH HOH A . 
FA 7 HOH 14  414 1021 HOH HOH A . 
FA 7 HOH 15  415 1002 HOH HOH A . 
FA 7 HOH 16  416 938  HOH HOH A . 
FA 7 HOH 17  417 1320 HOH HOH A . 
FA 7 HOH 18  418 491  HOH HOH A . 
FA 7 HOH 19  419 351  HOH HOH A . 
FA 7 HOH 20  420 720  HOH HOH A . 
FA 7 HOH 21  421 1393 HOH HOH A . 
FA 7 HOH 22  422 166  HOH HOH A . 
FA 7 HOH 23  423 206  HOH HOH A . 
FA 7 HOH 24  424 1058 HOH HOH A . 
FA 7 HOH 25  425 248  HOH HOH A . 
FA 7 HOH 26  426 1063 HOH HOH A . 
FA 7 HOH 27  427 371  HOH HOH A . 
FA 7 HOH 28  428 832  HOH HOH A . 
FA 7 HOH 29  429 299  HOH HOH A . 
FA 7 HOH 30  430 936  HOH HOH A . 
FA 7 HOH 31  431 37   HOH HOH A . 
FA 7 HOH 32  432 1348 HOH HOH A . 
FA 7 HOH 33  433 934  HOH HOH A . 
FA 7 HOH 34  434 531  HOH HOH A . 
FA 7 HOH 35  435 134  HOH HOH A . 
FA 7 HOH 36  436 1106 HOH HOH A . 
FA 7 HOH 37  437 241  HOH HOH A . 
FA 7 HOH 38  438 511  HOH HOH A . 
FA 7 HOH 39  439 1337 HOH HOH A . 
FA 7 HOH 40  440 1247 HOH HOH A . 
FA 7 HOH 41  441 23   HOH HOH A . 
FA 7 HOH 42  442 1300 HOH HOH A . 
FA 7 HOH 43  443 298  HOH HOH A . 
FA 7 HOH 44  444 1098 HOH HOH A . 
FA 7 HOH 45  445 215  HOH HOH A . 
FA 7 HOH 46  446 824  HOH HOH A . 
FA 7 HOH 47  447 1004 HOH HOH A . 
FA 7 HOH 48  448 619  HOH HOH A . 
FA 7 HOH 49  449 72   HOH HOH A . 
FA 7 HOH 50  450 1140 HOH HOH A . 
FA 7 HOH 51  451 212  HOH HOH A . 
FA 7 HOH 52  452 98   HOH HOH A . 
FA 7 HOH 53  453 1239 HOH HOH A . 
FA 7 HOH 54  454 426  HOH HOH A . 
FA 7 HOH 55  455 552  HOH HOH A . 
FA 7 HOH 56  456 15   HOH HOH A . 
FA 7 HOH 57  457 382  HOH HOH A . 
FA 7 HOH 58  458 1006 HOH HOH A . 
FA 7 HOH 59  459 953  HOH HOH A . 
FA 7 HOH 60  460 133  HOH HOH A . 
FA 7 HOH 61  461 418  HOH HOH A . 
FA 7 HOH 62  462 347  HOH HOH A . 
FA 7 HOH 63  463 663  HOH HOH A . 
FA 7 HOH 64  464 297  HOH HOH A . 
FA 7 HOH 65  465 64   HOH HOH A . 
FA 7 HOH 66  466 990  HOH HOH A . 
FA 7 HOH 67  467 846  HOH HOH A . 
FA 7 HOH 68  468 221  HOH HOH A . 
FA 7 HOH 69  469 59   HOH HOH A . 
FA 7 HOH 70  470 624  HOH HOH A . 
FA 7 HOH 71  471 305  HOH HOH A . 
FA 7 HOH 72  472 151  HOH HOH A . 
FA 7 HOH 73  473 1078 HOH HOH A . 
FA 7 HOH 74  474 77   HOH HOH A . 
FA 7 HOH 75  475 104  HOH HOH A . 
FA 7 HOH 76  476 249  HOH HOH A . 
FA 7 HOH 77  477 180  HOH HOH A . 
FA 7 HOH 78  478 359  HOH HOH A . 
FA 7 HOH 79  479 1100 HOH HOH A . 
FA 7 HOH 80  480 361  HOH HOH A . 
FA 7 HOH 81  481 182  HOH HOH A . 
FA 7 HOH 82  482 362  HOH HOH A . 
FA 7 HOH 83  483 8    HOH HOH A . 
FA 7 HOH 84  484 618  HOH HOH A . 
FA 7 HOH 85  485 346  HOH HOH A . 
FA 7 HOH 86  486 743  HOH HOH A . 
FA 7 HOH 87  487 1298 HOH HOH A . 
FA 7 HOH 88  488 183  HOH HOH A . 
FA 7 HOH 89  489 38   HOH HOH A . 
FA 7 HOH 90  490 142  HOH HOH A . 
FA 7 HOH 91  491 557  HOH HOH A . 
FA 7 HOH 92  492 397  HOH HOH A . 
FA 7 HOH 93  493 61   HOH HOH A . 
FA 7 HOH 94  494 136  HOH HOH A . 
FA 7 HOH 95  495 822  HOH HOH A . 
FA 7 HOH 96  496 512  HOH HOH A . 
FA 7 HOH 97  497 1383 HOH HOH A . 
FA 7 HOH 98  498 1389 HOH HOH A . 
FA 7 HOH 99  499 983  HOH HOH A . 
FA 7 HOH 100 500 438  HOH HOH A . 
FA 7 HOH 101 501 238  HOH HOH A . 
FA 7 HOH 102 502 19   HOH HOH A . 
FA 7 HOH 103 503 725  HOH HOH A . 
FA 7 HOH 104 504 951  HOH HOH A . 
FA 7 HOH 105 505 865  HOH HOH A . 
FA 7 HOH 106 506 843  HOH HOH A . 
FA 7 HOH 107 507 124  HOH HOH A . 
FA 7 HOH 108 508 401  HOH HOH A . 
FA 7 HOH 109 509 542  HOH HOH A . 
FA 7 HOH 110 510 193  HOH HOH A . 
FA 7 HOH 111 511 1296 HOH HOH A . 
FA 7 HOH 112 512 208  HOH HOH A . 
FA 7 HOH 113 513 57   HOH HOH A . 
FA 7 HOH 114 514 1099 HOH HOH A . 
FA 7 HOH 115 515 647  HOH HOH A . 
FA 7 HOH 116 516 1097 HOH HOH A . 
FA 7 HOH 117 517 440  HOH HOH A . 
FA 7 HOH 118 518 190  HOH HOH A . 
FA 7 HOH 119 519 1246 HOH HOH A . 
FA 7 HOH 120 520 1033 HOH HOH A . 
FA 7 HOH 121 521 668  HOH HOH A . 
FA 7 HOH 122 522 948  HOH HOH A . 
FA 7 HOH 123 523 389  HOH HOH A . 
FA 7 HOH 124 524 373  HOH HOH A . 
FA 7 HOH 125 525 289  HOH HOH A . 
FA 7 HOH 126 526 1110 HOH HOH A . 
FA 7 HOH 127 527 24   HOH HOH A . 
FA 7 HOH 128 528 575  HOH HOH A . 
FA 7 HOH 129 529 46   HOH HOH A . 
FA 7 HOH 130 530 902  HOH HOH A . 
FA 7 HOH 131 531 125  HOH HOH A . 
FA 7 HOH 132 532 669  HOH HOH A . 
FA 7 HOH 133 533 274  HOH HOH A . 
FA 7 HOH 134 534 258  HOH HOH A . 
FA 7 HOH 135 535 1381 HOH HOH A . 
FA 7 HOH 136 536 240  HOH HOH A . 
FA 7 HOH 137 537 506  HOH HOH A . 
FA 7 HOH 138 538 432  HOH HOH A . 
FA 7 HOH 139 539 554  HOH HOH A . 
FA 7 HOH 140 540 1248 HOH HOH A . 
FA 7 HOH 141 541 73   HOH HOH A . 
FA 7 HOH 142 542 1388 HOH HOH A . 
FA 7 HOH 143 543 82   HOH HOH A . 
FA 7 HOH 144 544 1378 HOH HOH A . 
FA 7 HOH 145 545 414  HOH HOH A . 
FA 7 HOH 146 546 116  HOH HOH A . 
FA 7 HOH 147 547 755  HOH HOH A . 
FA 7 HOH 148 548 616  HOH HOH A . 
FA 7 HOH 149 549 974  HOH HOH A . 
FA 7 HOH 150 550 119  HOH HOH A . 
FA 7 HOH 151 551 503  HOH HOH A . 
FA 7 HOH 152 552 48   HOH HOH A . 
FA 7 HOH 153 553 247  HOH HOH A . 
FA 7 HOH 154 554 604  HOH HOH A . 
FA 7 HOH 155 555 103  HOH HOH A . 
FA 7 HOH 156 556 962  HOH HOH A . 
FA 7 HOH 157 557 31   HOH HOH A . 
FA 7 HOH 158 558 1252 HOH HOH A . 
FA 7 HOH 159 559 353  HOH HOH A . 
FA 7 HOH 160 560 213  HOH HOH A . 
FA 7 HOH 161 561 681  HOH HOH A . 
FA 7 HOH 162 562 463  HOH HOH A . 
FA 7 HOH 163 563 535  HOH HOH A . 
FA 7 HOH 164 564 981  HOH HOH A . 
FA 7 HOH 165 565 1130 HOH HOH A . 
FA 7 HOH 166 566 386  HOH HOH A . 
FA 7 HOH 167 567 796  HOH HOH A . 
FA 7 HOH 168 568 265  HOH HOH A . 
FA 7 HOH 169 569 1322 HOH HOH A . 
FA 7 HOH 170 570 127  HOH HOH A . 
FA 7 HOH 171 571 387  HOH HOH A . 
FA 7 HOH 172 572 767  HOH HOH A . 
FA 7 HOH 173 573 473  HOH HOH A . 
FA 7 HOH 174 574 1025 HOH HOH A . 
FA 7 HOH 175 575 996  HOH HOH A . 
FA 7 HOH 176 576 423  HOH HOH A . 
FA 7 HOH 177 577 788  HOH HOH A . 
FA 7 HOH 178 578 504  HOH HOH A . 
FA 7 HOH 179 579 205  HOH HOH A . 
FA 7 HOH 180 580 9    HOH HOH A . 
FA 7 HOH 181 581 1334 HOH HOH A . 
FA 7 HOH 182 582 457  HOH HOH A . 
FA 7 HOH 183 583 1232 HOH HOH A . 
FA 7 HOH 184 584 942  HOH HOH A . 
FA 7 HOH 185 585 309  HOH HOH A . 
FA 7 HOH 186 586 661  HOH HOH A . 
FA 7 HOH 187 587 122  HOH HOH A . 
FA 7 HOH 188 588 666  HOH HOH A . 
FA 7 HOH 189 589 112  HOH HOH A . 
FA 7 HOH 190 590 553  HOH HOH A . 
FA 7 HOH 191 591 577  HOH HOH A . 
FA 7 HOH 192 592 1147 HOH HOH A . 
FA 7 HOH 193 593 90   HOH HOH A . 
FA 7 HOH 194 594 1254 HOH HOH A . 
FA 7 HOH 195 595 1052 HOH HOH A . 
FA 7 HOH 196 596 897  HOH HOH A . 
FA 7 HOH 197 597 479  HOH HOH A . 
FA 7 HOH 198 598 546  HOH HOH A . 
FA 7 HOH 199 599 172  HOH HOH A . 
FA 7 HOH 200 600 1157 HOH HOH A . 
FA 7 HOH 201 601 1173 HOH HOH A . 
FA 7 HOH 202 602 896  HOH HOH A . 
FA 7 HOH 203 603 285  HOH HOH A . 
FA 7 HOH 204 604 229  HOH HOH A . 
FA 7 HOH 205 605 1398 HOH HOH A . 
FA 7 HOH 206 606 164  HOH HOH A . 
FA 7 HOH 207 607 676  HOH HOH A . 
FA 7 HOH 208 608 1297 HOH HOH A . 
FA 7 HOH 209 609 462  HOH HOH A . 
FA 7 HOH 210 610 219  HOH HOH A . 
FA 7 HOH 211 611 1027 HOH HOH A . 
FA 7 HOH 212 612 4    HOH HOH A . 
FA 7 HOH 213 613 398  HOH HOH A . 
FA 7 HOH 214 614 1238 HOH HOH A . 
FA 7 HOH 215 615 757  HOH HOH A . 
FA 7 HOH 216 616 513  HOH HOH A . 
FA 7 HOH 217 617 145  HOH HOH A . 
FA 7 HOH 218 618 753  HOH HOH A . 
FA 7 HOH 219 619 493  HOH HOH A . 
FA 7 HOH 220 620 458  HOH HOH A . 
FA 7 HOH 221 621 187  HOH HOH A . 
FA 7 HOH 222 622 132  HOH HOH A . 
FA 7 HOH 223 623 179  HOH HOH A . 
FA 7 HOH 224 624 455  HOH HOH A . 
FA 7 HOH 225 625 1134 HOH HOH A . 
FA 7 HOH 226 626 1245 HOH HOH A . 
FA 7 HOH 227 627 1237 HOH HOH A . 
FA 7 HOH 228 628 267  HOH HOH A . 
FA 7 HOH 229 629 940  HOH HOH A . 
FA 7 HOH 230 630 1311 HOH HOH A . 
FA 7 HOH 231 631 1259 HOH HOH A . 
FA 7 HOH 232 632 360  HOH HOH A . 
FA 7 HOH 233 633 591  HOH HOH A . 
FA 7 HOH 234 634 227  HOH HOH A . 
FA 7 HOH 235 635 345  HOH HOH A . 
FA 7 HOH 236 636 225  HOH HOH A . 
FA 7 HOH 237 637 1333 HOH HOH A . 
FA 7 HOH 238 638 519  HOH HOH A . 
FA 7 HOH 239 639 178  HOH HOH A . 
FA 7 HOH 240 640 783  HOH HOH A . 
FA 7 HOH 241 641 1244 HOH HOH A . 
FA 7 HOH 242 642 1007 HOH HOH A . 
FA 7 HOH 243 643 137  HOH HOH A . 
FA 7 HOH 244 644 25   HOH HOH A . 
FA 7 HOH 245 645 1293 HOH HOH A . 
FA 7 HOH 246 646 958  HOH HOH A . 
FA 7 HOH 247 647 408  HOH HOH A . 
FA 7 HOH 248 648 525  HOH HOH A . 
FA 7 HOH 249 649 710  HOH HOH A . 
FA 7 HOH 250 650 246  HOH HOH A . 
FA 7 HOH 251 651 906  HOH HOH A . 
FA 7 HOH 252 652 1392 HOH HOH A . 
FA 7 HOH 253 653 727  HOH HOH A . 
FA 7 HOH 254 654 827  HOH HOH A . 
FA 7 HOH 255 655 1102 HOH HOH A . 
FA 7 HOH 256 656 835  HOH HOH A . 
FA 7 HOH 257 657 1241 HOH HOH A . 
FA 7 HOH 258 658 1323 HOH HOH A . 
FA 7 HOH 259 659 903  HOH HOH A . 
FA 7 HOH 260 660 1336 HOH HOH A . 
FA 7 HOH 261 661 300  HOH HOH A . 
FA 7 HOH 262 662 1292 HOH HOH A . 
FA 7 HOH 263 663 594  HOH HOH A . 
FA 7 HOH 264 664 1294 HOH HOH A . 
FA 7 HOH 265 665 1108 HOH HOH A . 
FA 7 HOH 266 666 1017 HOH HOH A . 
FA 7 HOH 267 667 1054 HOH HOH A . 
FA 7 HOH 268 668 1346 HOH HOH A . 
FA 7 HOH 269 669 1153 HOH HOH A . 
FA 7 HOH 270 670 598  HOH HOH A . 
FA 7 HOH 271 671 1242 HOH HOH A . 
FA 7 HOH 272 672 917  HOH HOH A . 
FA 7 HOH 273 673 898  HOH HOH A . 
FA 7 HOH 274 674 769  HOH HOH A . 
FA 7 HOH 275 675 1345 HOH HOH A . 
FA 7 HOH 276 676 470  HOH HOH A . 
FA 7 HOH 277 677 1372 HOH HOH A . 
FA 7 HOH 278 678 1379 HOH HOH A . 
FA 7 HOH 279 679 1385 HOH HOH A . 
FA 7 HOH 280 680 1397 HOH HOH A . 
FA 7 HOH 281 681 855  HOH HOH A . 
FA 7 HOH 282 682 1152 HOH HOH A . 
FA 7 HOH 283 683 374  HOH HOH A . 
FA 7 HOH 284 684 807  HOH HOH A . 
FA 7 HOH 285 685 844  HOH HOH A . 
FA 7 HOH 286 686 1382 HOH HOH A . 
FA 7 HOH 287 687 685  HOH HOH A . 
FA 7 HOH 288 688 779  HOH HOH A . 
FA 7 HOH 289 689 950  HOH HOH A . 
FA 7 HOH 290 690 659  HOH HOH A . 
FA 7 HOH 291 691 1250 HOH HOH A . 
FA 7 HOH 292 692 1335 HOH HOH A . 
FA 7 HOH 293 693 1076 HOH HOH A . 
FA 7 HOH 294 694 640  HOH HOH A . 
FA 7 HOH 295 695 644  HOH HOH A . 
FA 7 HOH 296 696 1396 HOH HOH A . 
FA 7 HOH 297 697 818  HOH HOH A . 
FA 7 HOH 298 698 1257 HOH HOH A . 
FA 7 HOH 299 699 1390 HOH HOH A . 
FA 7 HOH 300 700 337  HOH HOH A . 
FA 7 HOH 301 701 667  HOH HOH A . 
FA 7 HOH 302 702 904  HOH HOH A . 
FA 7 HOH 303 703 1374 HOH HOH A . 
FA 7 HOH 304 704 1295 HOH HOH A . 
FA 7 HOH 305 705 472  HOH HOH A . 
FA 7 HOH 306 706 1120 HOH HOH A . 
FA 7 HOH 307 707 1299 HOH HOH A . 
FA 7 HOH 308 708 858  HOH HOH A . 
FA 7 HOH 309 709 610  HOH HOH A . 
FA 7 HOH 310 710 1047 HOH HOH A . 
FA 7 HOH 311 711 499  HOH HOH A . 
FA 7 HOH 312 712 1107 HOH HOH A . 
FA 7 HOH 313 713 1253 HOH HOH A . 
FA 7 HOH 314 714 804  HOH HOH A . 
FA 7 HOH 315 715 1240 HOH HOH A . 
FA 7 HOH 316 716 699  HOH HOH A . 
FA 7 HOH 317 717 1243 HOH HOH A . 
FA 7 HOH 318 718 329  HOH HOH A . 
FA 7 HOH 319 719 944  HOH HOH A . 
FA 7 HOH 320 720 752  HOH HOH A . 
FA 7 HOH 321 721 709  HOH HOH A . 
FA 7 HOH 322 722 1339 HOH HOH A . 
FA 7 HOH 323 723 1306 HOH HOH A . 
FA 7 HOH 324 724 1236 HOH HOH A . 
FA 7 HOH 325 725 1380 HOH HOH A . 
FA 7 HOH 326 726 979  HOH HOH A . 
FA 7 HOH 327 727 355  HOH HOH A . 
FA 7 HOH 328 728 665  HOH HOH A . 
FA 7 HOH 329 729 1394 HOH HOH A . 
FA 7 HOH 330 730 1043 HOH HOH A . 
FA 7 HOH 331 731 584  HOH HOH A . 
FA 7 HOH 332 732 1386 HOH HOH A . 
FA 7 HOH 333 733 780  HOH HOH A . 
FA 7 HOH 334 734 1347 HOH HOH A . 
FA 7 HOH 335 735 369  HOH HOH A . 
FA 7 HOH 336 736 815  HOH HOH A . 
FA 7 HOH 337 737 1340 HOH HOH A . 
FA 7 HOH 338 738 1384 HOH HOH A . 
FA 7 HOH 339 739 1249 HOH HOH A . 
FA 7 HOH 340 740 1145 HOH HOH A . 
FA 7 HOH 341 741 1391 HOH HOH A . 
FA 7 HOH 342 742 1089 HOH HOH A . 
FA 7 HOH 343 743 1000 HOH HOH A . 
FA 7 HOH 344 744 1344 HOH HOH A . 
FA 7 HOH 345 745 1055 HOH HOH A . 
FA 7 HOH 346 746 1387 HOH HOH A . 
FA 7 HOH 347 747 866  HOH HOH A . 
FA 7 HOH 348 748 1056 HOH HOH A . 
FA 7 HOH 349 749 1321 HOH HOH A . 
FA 7 HOH 350 750 496  HOH HOH A . 
FA 7 HOH 351 751 1255 HOH HOH A . 
FA 7 HOH 352 752 871  HOH HOH A . 
FA 7 HOH 353 753 582  HOH HOH A . 
FA 7 HOH 354 754 391  HOH HOH A . 
FA 7 HOH 355 755 1008 HOH HOH A . 
FA 7 HOH 356 756 480  HOH HOH A . 
FA 7 HOH 357 757 602  HOH HOH A . 
FA 7 HOH 358 758 985  HOH HOH A . 
FA 7 HOH 359 759 1319 HOH HOH A . 
FA 7 HOH 360 760 878  HOH HOH A . 
FA 7 HOH 361 761 1160 HOH HOH A . 
FA 7 HOH 362 762 1341 HOH HOH A . 
FA 7 HOH 363 763 799  HOH HOH A . 
FA 7 HOH 364 764 1233 HOH HOH A . 
FA 7 HOH 365 765 831  HOH HOH A . 
FA 7 HOH 366 766 781  HOH HOH A . 
FA 7 HOH 367 767 409  HOH HOH A . 
FA 7 HOH 368 768 1395 HOH HOH A . 
FA 7 HOH 369 769 572  HOH HOH A . 
FA 7 HOH 370 770 1280 HOH HOH A . 
FA 7 HOH 371 771 217  HOH HOH A . 
FA 7 HOH 372 772 1251 HOH HOH A . 
FA 7 HOH 373 773 882  HOH HOH A . 
FA 7 HOH 374 774 823  HOH HOH A . 
FA 7 HOH 375 775 1438 HOH HOH A . 
FA 7 HOH 376 776 1256 HOH HOH A . 
FA 7 HOH 377 777 930  HOH HOH A . 
FA 7 HOH 378 778 813  HOH HOH A . 
FA 7 HOH 379 779 964  HOH HOH A . 
FA 7 HOH 380 780 886  HOH HOH A . 
GA 7 HOH 1   401 1011 HOH HOH B . 
GA 7 HOH 2   402 1095 HOH HOH B . 
GA 7 HOH 3   403 1050 HOH HOH B . 
GA 7 HOH 4   404 468  HOH HOH B . 
GA 7 HOH 5   405 1286 HOH HOH B . 
GA 7 HOH 6   406 721  HOH HOH B . 
GA 7 HOH 7   407 914  HOH HOH B . 
GA 7 HOH 8   408 428  HOH HOH B . 
GA 7 HOH 9   409 466  HOH HOH B . 
GA 7 HOH 10  410 777  HOH HOH B . 
GA 7 HOH 11  411 586  HOH HOH B . 
GA 7 HOH 12  412 949  HOH HOH B . 
GA 7 HOH 13  413 662  HOH HOH B . 
GA 7 HOH 14  414 1094 HOH HOH B . 
GA 7 HOH 15  415 489  HOH HOH B . 
GA 7 HOH 16  416 402  HOH HOH B . 
GA 7 HOH 17  417 1351 HOH HOH B . 
GA 7 HOH 18  418 1014 HOH HOH B . 
GA 7 HOH 19  419 595  HOH HOH B . 
GA 7 HOH 20  420 1125 HOH HOH B . 
GA 7 HOH 21  421 1144 HOH HOH B . 
GA 7 HOH 22  422 199  HOH HOH B . 
GA 7 HOH 23  423 895  HOH HOH B . 
GA 7 HOH 24  424 1399 HOH HOH B . 
GA 7 HOH 25  425 656  HOH HOH B . 
GA 7 HOH 26  426 1077 HOH HOH B . 
GA 7 HOH 27  427 1355 HOH HOH B . 
GA 7 HOH 28  428 1174 HOH HOH B . 
GA 7 HOH 29  429 730  HOH HOH B . 
GA 7 HOH 30  430 16   HOH HOH B . 
GA 7 HOH 31  431 395  HOH HOH B . 
GA 7 HOH 32  432 760  HOH HOH B . 
GA 7 HOH 33  433 603  HOH HOH B . 
GA 7 HOH 34  434 420  HOH HOH B . 
GA 7 HOH 35  435 1126 HOH HOH B . 
GA 7 HOH 36  436 43   HOH HOH B . 
GA 7 HOH 37  437 991  HOH HOH B . 
GA 7 HOH 38  438 287  HOH HOH B . 
GA 7 HOH 39  439 1281 HOH HOH B . 
GA 7 HOH 40  440 510  HOH HOH B . 
GA 7 HOH 41  441 1317 HOH HOH B . 
GA 7 HOH 42  442 1376 HOH HOH B . 
GA 7 HOH 43  443 417  HOH HOH B . 
GA 7 HOH 44  444 1283 HOH HOH B . 
GA 7 HOH 45  445 529  HOH HOH B . 
GA 7 HOH 46  446 332  HOH HOH B . 
GA 7 HOH 47  447 1262 HOH HOH B . 
GA 7 HOH 48  448 920  HOH HOH B . 
GA 7 HOH 49  449 138  HOH HOH B . 
GA 7 HOH 50  450 992  HOH HOH B . 
GA 7 HOH 51  451 1402 HOH HOH B . 
GA 7 HOH 52  452 120  HOH HOH B . 
GA 7 HOH 53  453 130  HOH HOH B . 
GA 7 HOH 54  454 1086 HOH HOH B . 
GA 7 HOH 55  455 352  HOH HOH B . 
GA 7 HOH 56  456 186  HOH HOH B . 
GA 7 HOH 57  457 564  HOH HOH B . 
GA 7 HOH 58  458 278  HOH HOH B . 
GA 7 HOH 59  459 892  HOH HOH B . 
GA 7 HOH 60  460 317  HOH HOH B . 
GA 7 HOH 61  461 1176 HOH HOH B . 
GA 7 HOH 62  462 319  HOH HOH B . 
GA 7 HOH 63  463 498  HOH HOH B . 
GA 7 HOH 64  464 642  HOH HOH B . 
GA 7 HOH 65  465 291  HOH HOH B . 
GA 7 HOH 66  466 561  HOH HOH B . 
GA 7 HOH 67  467 1178 HOH HOH B . 
GA 7 HOH 68  468 785  HOH HOH B . 
GA 7 HOH 69  469 1354 HOH HOH B . 
GA 7 HOH 70  470 1171 HOH HOH B . 
GA 7 HOH 71  471 315  HOH HOH B . 
GA 7 HOH 72  472 288  HOH HOH B . 
GA 7 HOH 73  473 84   HOH HOH B . 
GA 7 HOH 74  474 811  HOH HOH B . 
GA 7 HOH 75  475 35   HOH HOH B . 
GA 7 HOH 76  476 143  HOH HOH B . 
GA 7 HOH 77  477 1352 HOH HOH B . 
GA 7 HOH 78  478 91   HOH HOH B . 
GA 7 HOH 79  479 411  HOH HOH B . 
GA 7 HOH 80  480 569  HOH HOH B . 
GA 7 HOH 81  481 253  HOH HOH B . 
GA 7 HOH 82  482 150  HOH HOH B . 
GA 7 HOH 83  483 495  HOH HOH B . 
GA 7 HOH 84  484 344  HOH HOH B . 
GA 7 HOH 85  485 87   HOH HOH B . 
GA 7 HOH 86  486 261  HOH HOH B . 
GA 7 HOH 87  487 431  HOH HOH B . 
GA 7 HOH 88  488 1375 HOH HOH B . 
GA 7 HOH 89  489 157  HOH HOH B . 
GA 7 HOH 90  490 539  HOH HOH B . 
GA 7 HOH 91  491 705  HOH HOH B . 
GA 7 HOH 92  492 415  HOH HOH B . 
GA 7 HOH 93  493 126  HOH HOH B . 
GA 7 HOH 94  494 1070 HOH HOH B . 
GA 7 HOH 95  495 497  HOH HOH B . 
GA 7 HOH 96  496 101  HOH HOH B . 
GA 7 HOH 97  497 276  HOH HOH B . 
GA 7 HOH 98  498 44   HOH HOH B . 
GA 7 HOH 99  499 502  HOH HOH B . 
GA 7 HOH 100 500 27   HOH HOH B . 
GA 7 HOH 101 501 518  HOH HOH B . 
GA 7 HOH 102 502 211  HOH HOH B . 
GA 7 HOH 103 503 654  HOH HOH B . 
GA 7 HOH 104 504 1263 HOH HOH B . 
GA 7 HOH 105 505 1040 HOH HOH B . 
GA 7 HOH 106 506 935  HOH HOH B . 
GA 7 HOH 107 507 83   HOH HOH B . 
GA 7 HOH 108 508 282  HOH HOH B . 
GA 7 HOH 109 509 1169 HOH HOH B . 
GA 7 HOH 110 510 255  HOH HOH B . 
GA 7 HOH 111 511 312  HOH HOH B . 
GA 7 HOH 112 512 55   HOH HOH B . 
GA 7 HOH 113 513 1015 HOH HOH B . 
GA 7 HOH 114 514 155  HOH HOH B . 
GA 7 HOH 115 515 1071 HOH HOH B . 
GA 7 HOH 116 516 1079 HOH HOH B . 
GA 7 HOH 117 517 272  HOH HOH B . 
GA 7 HOH 118 518 801  HOH HOH B . 
GA 7 HOH 119 519 184  HOH HOH B . 
GA 7 HOH 120 520 175  HOH HOH B . 
GA 7 HOH 121 521 354  HOH HOH B . 
GA 7 HOH 122 522 695  HOH HOH B . 
GA 7 HOH 123 523 536  HOH HOH B . 
GA 7 HOH 124 524 223  HOH HOH B . 
GA 7 HOH 125 525 384  HOH HOH B . 
GA 7 HOH 126 526 946  HOH HOH B . 
GA 7 HOH 127 527 269  HOH HOH B . 
GA 7 HOH 128 528 49   HOH HOH B . 
GA 7 HOH 129 529 209  HOH HOH B . 
GA 7 HOH 130 530 830  HOH HOH B . 
GA 7 HOH 131 531 628  HOH HOH B . 
GA 7 HOH 132 532 761  HOH HOH B . 
GA 7 HOH 133 533 766  HOH HOH B . 
GA 7 HOH 134 534 573  HOH HOH B . 
GA 7 HOH 135 535 1158 HOH HOH B . 
GA 7 HOH 136 536 10   HOH HOH B . 
GA 7 HOH 137 537 52   HOH HOH B . 
GA 7 HOH 138 538 328  HOH HOH B . 
GA 7 HOH 139 539 168  HOH HOH B . 
GA 7 HOH 140 540 1373 HOH HOH B . 
GA 7 HOH 141 541 5    HOH HOH B . 
GA 7 HOH 142 542 47   HOH HOH B . 
GA 7 HOH 143 543 739  HOH HOH B . 
GA 7 HOH 144 544 841  HOH HOH B . 
GA 7 HOH 145 545 80   HOH HOH B . 
GA 7 HOH 146 546 901  HOH HOH B . 
GA 7 HOH 147 547 828  HOH HOH B . 
GA 7 HOH 148 548 1163 HOH HOH B . 
GA 7 HOH 149 549 310  HOH HOH B . 
GA 7 HOH 150 550 198  HOH HOH B . 
GA 7 HOH 151 551 478  HOH HOH B . 
GA 7 HOH 152 552 1182 HOH HOH B . 
GA 7 HOH 153 553 1260 HOH HOH B . 
GA 7 HOH 154 554 585  HOH HOH B . 
GA 7 HOH 155 555 1268 HOH HOH B . 
GA 7 HOH 156 556 257  HOH HOH B . 
GA 7 HOH 157 557 325  HOH HOH B . 
GA 7 HOH 158 558 623  HOH HOH B . 
GA 7 HOH 159 559 925  HOH HOH B . 
GA 7 HOH 160 560 453  HOH HOH B . 
GA 7 HOH 161 561 993  HOH HOH B . 
GA 7 HOH 162 562 678  HOH HOH B . 
GA 7 HOH 163 563 673  HOH HOH B . 
GA 7 HOH 164 564 723  HOH HOH B . 
GA 7 HOH 165 565 1267 HOH HOH B . 
GA 7 HOH 166 566 1271 HOH HOH B . 
GA 7 HOH 167 567 273  HOH HOH B . 
GA 7 HOH 168 568 340  HOH HOH B . 
GA 7 HOH 169 569 314  HOH HOH B . 
GA 7 HOH 170 570 732  HOH HOH B . 
GA 7 HOH 171 571 483  HOH HOH B . 
GA 7 HOH 172 572 893  HOH HOH B . 
GA 7 HOH 173 573 599  HOH HOH B . 
GA 7 HOH 174 574 45   HOH HOH B . 
GA 7 HOH 175 575 449  HOH HOH B . 
GA 7 HOH 176 576 848  HOH HOH B . 
GA 7 HOH 177 577 933  HOH HOH B . 
GA 7 HOH 178 578 93   HOH HOH B . 
GA 7 HOH 179 579 194  HOH HOH B . 
GA 7 HOH 180 580 406  HOH HOH B . 
GA 7 HOH 181 581 338  HOH HOH B . 
GA 7 HOH 182 582 390  HOH HOH B . 
GA 7 HOH 183 583 370  HOH HOH B . 
GA 7 HOH 184 584 1177 HOH HOH B . 
GA 7 HOH 185 585 729  HOH HOH B . 
GA 7 HOH 186 586 694  HOH HOH B . 
GA 7 HOH 187 587 1141 HOH HOH B . 
GA 7 HOH 188 588 1314 HOH HOH B . 
GA 7 HOH 189 589 652  HOH HOH B . 
GA 7 HOH 190 590 1217 HOH HOH B . 
GA 7 HOH 191 591 78   HOH HOH B . 
GA 7 HOH 192 592 461  HOH HOH B . 
GA 7 HOH 193 593 161  HOH HOH B . 
GA 7 HOH 194 594 3    HOH HOH B . 
GA 7 HOH 195 595 18   HOH HOH B . 
GA 7 HOH 196 596 192  HOH HOH B . 
GA 7 HOH 197 597 281  HOH HOH B . 
GA 7 HOH 198 598 214  HOH HOH B . 
GA 7 HOH 199 599 839  HOH HOH B . 
GA 7 HOH 200 600 231  HOH HOH B . 
GA 7 HOH 201 601 605  HOH HOH B . 
GA 7 HOH 202 602 144  HOH HOH B . 
GA 7 HOH 203 603 558  HOH HOH B . 
GA 7 HOH 204 604 900  HOH HOH B . 
GA 7 HOH 205 605 680  HOH HOH B . 
GA 7 HOH 206 606 736  HOH HOH B . 
GA 7 HOH 207 607 286  HOH HOH B . 
GA 7 HOH 208 608 952  HOH HOH B . 
GA 7 HOH 209 609 195  HOH HOH B . 
GA 7 HOH 210 610 448  HOH HOH B . 
GA 7 HOH 211 611 66   HOH HOH B . 
GA 7 HOH 212 612 160  HOH HOH B . 
GA 7 HOH 213 613 42   HOH HOH B . 
GA 7 HOH 214 614 1264 HOH HOH B . 
GA 7 HOH 215 615 1440 HOH HOH B . 
GA 7 HOH 216 616 334  HOH HOH B . 
GA 7 HOH 217 617 203  HOH HOH B . 
GA 7 HOH 218 618 1179 HOH HOH B . 
GA 7 HOH 219 619 149  HOH HOH B . 
GA 7 HOH 220 620 1164 HOH HOH B . 
GA 7 HOH 221 621 596  HOH HOH B . 
GA 7 HOH 222 622 162  HOH HOH B . 
GA 7 HOH 223 623 106  HOH HOH B . 
GA 7 HOH 224 624 698  HOH HOH B . 
GA 7 HOH 225 625 887  HOH HOH B . 
GA 7 HOH 226 626 485  HOH HOH B . 
GA 7 HOH 227 627 1186 HOH HOH B . 
GA 7 HOH 228 628 771  HOH HOH B . 
GA 7 HOH 229 629 341  HOH HOH B . 
GA 7 HOH 230 630 713  HOH HOH B . 
GA 7 HOH 231 631 748  HOH HOH B . 
GA 7 HOH 232 632 1270 HOH HOH B . 
GA 7 HOH 233 633 1325 HOH HOH B . 
GA 7 HOH 234 634 117  HOH HOH B . 
GA 7 HOH 235 635 691  HOH HOH B . 
GA 7 HOH 236 636 96   HOH HOH B . 
GA 7 HOH 237 637 986  HOH HOH B . 
GA 7 HOH 238 638 551  HOH HOH B . 
GA 7 HOH 239 639 875  HOH HOH B . 
GA 7 HOH 240 640 738  HOH HOH B . 
GA 7 HOH 241 641 1350 HOH HOH B . 
GA 7 HOH 242 642 1326 HOH HOH B . 
GA 7 HOH 243 643 562  HOH HOH B . 
GA 7 HOH 244 644 649  HOH HOH B . 
GA 7 HOH 245 645 937  HOH HOH B . 
GA 7 HOH 246 646 224  HOH HOH B . 
GA 7 HOH 247 647 874  HOH HOH B . 
GA 7 HOH 248 648 704  HOH HOH B . 
GA 7 HOH 249 649 836  HOH HOH B . 
GA 7 HOH 250 650 1403 HOH HOH B . 
GA 7 HOH 251 651 1261 HOH HOH B . 
GA 7 HOH 252 652 590  HOH HOH B . 
GA 7 HOH 253 653 627  HOH HOH B . 
GA 7 HOH 254 654 1175 HOH HOH B . 
GA 7 HOH 255 655 1041 HOH HOH B . 
GA 7 HOH 256 656 429  HOH HOH B . 
GA 7 HOH 257 657 516  HOH HOH B . 
GA 7 HOH 258 658 1082 HOH HOH B . 
GA 7 HOH 259 659 343  HOH HOH B . 
GA 7 HOH 260 660 702  HOH HOH B . 
GA 7 HOH 261 661 1180 HOH HOH B . 
GA 7 HOH 262 662 1088 HOH HOH B . 
GA 7 HOH 263 663 1266 HOH HOH B . 
GA 7 HOH 264 664 1315 HOH HOH B . 
GA 7 HOH 265 665 960  HOH HOH B . 
GA 7 HOH 266 666 1139 HOH HOH B . 
GA 7 HOH 267 667 716  HOH HOH B . 
GA 7 HOH 268 668 1353 HOH HOH B . 
GA 7 HOH 269 669 859  HOH HOH B . 
GA 7 HOH 270 670 600  HOH HOH B . 
GA 7 HOH 271 671 1117 HOH HOH B . 
GA 7 HOH 272 672 976  HOH HOH B . 
GA 7 HOH 273 673 683  HOH HOH B . 
GA 7 HOH 274 674 965  HOH HOH B . 
GA 7 HOH 275 675 688  HOH HOH B . 
GA 7 HOH 276 676 632  HOH HOH B . 
GA 7 HOH 277 677 433  HOH HOH B . 
GA 7 HOH 278 678 620  HOH HOH B . 
GA 7 HOH 279 679 1159 HOH HOH B . 
GA 7 HOH 280 680 1124 HOH HOH B . 
GA 7 HOH 281 681 856  HOH HOH B . 
GA 7 HOH 282 682 524  HOH HOH B . 
GA 7 HOH 283 683 1104 HOH HOH B . 
GA 7 HOH 284 684 268  HOH HOH B . 
GA 7 HOH 285 685 877  HOH HOH B . 
GA 7 HOH 286 686 1155 HOH HOH B . 
GA 7 HOH 287 687 657  HOH HOH B . 
GA 7 HOH 288 688 1048 HOH HOH B . 
GA 7 HOH 289 689 481  HOH HOH B . 
GA 7 HOH 290 690 626  HOH HOH B . 
GA 7 HOH 291 691 1136 HOH HOH B . 
GA 7 HOH 292 692 1170 HOH HOH B . 
GA 7 HOH 293 693 816  HOH HOH B . 
GA 7 HOH 294 694 883  HOH HOH B . 
GA 7 HOH 295 695 1282 HOH HOH B . 
GA 7 HOH 296 696 220  HOH HOH B . 
GA 7 HOH 297 697 782  HOH HOH B . 
GA 7 HOH 298 698 842  HOH HOH B . 
GA 7 HOH 299 699 907  HOH HOH B . 
GA 7 HOH 300 700 538  HOH HOH B . 
GA 7 HOH 301 701 921  HOH HOH B . 
GA 7 HOH 302 702 140  HOH HOH B . 
GA 7 HOH 303 703 477  HOH HOH B . 
GA 7 HOH 304 704 356  HOH HOH B . 
GA 7 HOH 305 705 1123 HOH HOH B . 
GA 7 HOH 306 706 1165 HOH HOH B . 
GA 7 HOH 307 707 635  HOH HOH B . 
GA 7 HOH 308 708 488  HOH HOH B . 
GA 7 HOH 309 709 350  HOH HOH B . 
GA 7 HOH 310 710 1016 HOH HOH B . 
GA 7 HOH 311 711 567  HOH HOH B . 
GA 7 HOH 312 712 808  HOH HOH B . 
GA 7 HOH 313 713 547  HOH HOH B . 
GA 7 HOH 314 714 968  HOH HOH B . 
GA 7 HOH 315 715 1181 HOH HOH B . 
GA 7 HOH 316 716 994  HOH HOH B . 
GA 7 HOH 317 717 1090 HOH HOH B . 
GA 7 HOH 318 718 1045 HOH HOH B . 
GA 7 HOH 319 719 1072 HOH HOH B . 
GA 7 HOH 320 720 471  HOH HOH B . 
GA 7 HOH 321 721 515  HOH HOH B . 
GA 7 HOH 322 722 1132 HOH HOH B . 
GA 7 HOH 323 723 579  HOH HOH B . 
GA 7 HOH 324 724 1168 HOH HOH B . 
GA 7 HOH 325 725 1324 HOH HOH B . 
GA 7 HOH 326 726 543  HOH HOH B . 
GA 7 HOH 327 727 1166 HOH HOH B . 
GA 7 HOH 328 728 235  HOH HOH B . 
GA 7 HOH 329 729 189  HOH HOH B . 
GA 7 HOH 330 730 1291 HOH HOH B . 
GA 7 HOH 331 731 326  HOH HOH B . 
GA 7 HOH 332 732 1023 HOH HOH B . 
GA 7 HOH 333 733 999  HOH HOH B . 
GA 7 HOH 334 734 1031 HOH HOH B . 
GA 7 HOH 335 735 1269 HOH HOH B . 
GA 7 HOH 336 736 392  HOH HOH B . 
GA 7 HOH 337 737 1439 HOH HOH B . 
GA 7 HOH 338 738 379  HOH HOH B . 
GA 7 HOH 339 739 1187 HOH HOH B . 
GA 7 HOH 340 740 1265 HOH HOH B . 
GA 7 HOH 341 741 1284 HOH HOH B . 
GA 7 HOH 342 742 1349 HOH HOH B . 
GA 7 HOH 343 743 806  HOH HOH B . 
GA 7 HOH 344 744 613  HOH HOH B . 
GA 7 HOH 345 745 851  HOH HOH B . 
GA 7 HOH 346 746 776  HOH HOH B . 
GA 7 HOH 347 747 928  HOH HOH B . 
GA 7 HOH 348 748 1412 HOH HOH B . 
GA 7 HOH 349 749 1413 HOH HOH B . 
GA 7 HOH 350 750 1404 HOH HOH B . 
GA 7 HOH 351 751 724  HOH HOH B . 
GA 7 HOH 352 752 588  HOH HOH B . 
GA 7 HOH 353 753 803  HOH HOH B . 
GA 7 HOH 354 754 1184 HOH HOH B . 
GA 7 HOH 355 755 425  HOH HOH B . 
GA 7 HOH 356 756 637  HOH HOH B . 
GA 7 HOH 357 757 1183 HOH HOH B . 
GA 7 HOH 358 758 800  HOH HOH B . 
GA 7 HOH 359 759 880  HOH HOH B . 
GA 7 HOH 360 760 869  HOH HOH B . 
GA 7 HOH 361 761 464  HOH HOH B . 
GA 7 HOH 362 762 1406 HOH HOH B . 
GA 7 HOH 363 763 1162 HOH HOH B . 
GA 7 HOH 364 764 1172 HOH HOH B . 
GA 7 HOH 365 765 1407 HOH HOH B . 
GA 7 HOH 366 766 1290 HOH HOH B . 
GA 7 HOH 367 767 834  HOH HOH B . 
GA 7 HOH 368 768 1185 HOH HOH B . 
GA 7 HOH 369 769 1400 HOH HOH B . 
GA 7 HOH 370 770 754  HOH HOH B . 
GA 7 HOH 371 771 1405 HOH HOH B . 
GA 7 HOH 372 772 927  HOH HOH B . 
GA 7 HOH 373 773 622  HOH HOH B . 
GA 7 HOH 374 774 1064 HOH HOH B . 
GA 7 HOH 375 775 1161 HOH HOH B . 
GA 7 HOH 376 776 966  HOH HOH B . 
GA 7 HOH 377 777 1167 HOH HOH B . 
GA 7 HOH 378 778 1038 HOH HOH B . 
GA 7 HOH 379 779 1401 HOH HOH B . 
GA 7 HOH 380 780 802  HOH HOH B . 
GA 7 HOH 381 781 1285 HOH HOH B . 
HA 7 HOH 1   401 474  HOH HOH C . 
HA 7 HOH 2   402 1360 HOH HOH C . 
HA 7 HOH 3   403 445  HOH HOH C . 
HA 7 HOH 4   404 568  HOH HOH C . 
HA 7 HOH 5   405 957  HOH HOH C . 
HA 7 HOH 6   406 905  HOH HOH C . 
HA 7 HOH 7   407 1022 HOH HOH C . 
HA 7 HOH 8   408 1200 HOH HOH C . 
HA 7 HOH 9   409 540  HOH HOH C . 
HA 7 HOH 10  410 1423 HOH HOH C . 
HA 7 HOH 11  411 829  HOH HOH C . 
HA 7 HOH 12  412 689  HOH HOH C . 
HA 7 HOH 13  413 188  HOH HOH C . 
HA 7 HOH 14  414 734  HOH HOH C . 
HA 7 HOH 15  415 593  HOH HOH C . 
HA 7 HOH 16  416 508  HOH HOH C . 
HA 7 HOH 17  417 1332 HOH HOH C . 
HA 7 HOH 18  418 697  HOH HOH C . 
HA 7 HOH 19  419 1273 HOH HOH C . 
HA 7 HOH 20  420 1150 HOH HOH C . 
HA 7 HOH 21  421 1143 HOH HOH C . 
HA 7 HOH 22  422 1111 HOH HOH C . 
HA 7 HOH 23  423 1365 HOH HOH C . 
HA 7 HOH 24  424 107  HOH HOH C . 
HA 7 HOH 25  425 592  HOH HOH C . 
HA 7 HOH 26  426 1151 HOH HOH C . 
HA 7 HOH 27  427 327  HOH HOH C . 
HA 7 HOH 28  428 1422 HOH HOH C . 
HA 7 HOH 29  429 365  HOH HOH C . 
HA 7 HOH 30  430 1287 HOH HOH C . 
HA 7 HOH 31  431 283  HOH HOH C . 
HA 7 HOH 32  432 687  HOH HOH C . 
HA 7 HOH 33  433 982  HOH HOH C . 
HA 7 HOH 34  434 1194 HOH HOH C . 
HA 7 HOH 35  435 89   HOH HOH C . 
HA 7 HOH 36  436 505  HOH HOH C . 
HA 7 HOH 37  437 74   HOH HOH C . 
HA 7 HOH 38  438 765  HOH HOH C . 
HA 7 HOH 39  439 708  HOH HOH C . 
HA 7 HOH 40  440 772  HOH HOH C . 
HA 7 HOH 41  441 156  HOH HOH C . 
HA 7 HOH 42  442 416  HOH HOH C . 
HA 7 HOH 43  443 894  HOH HOH C . 
HA 7 HOH 44  444 320  HOH HOH C . 
HA 7 HOH 45  445 1121 HOH HOH C . 
HA 7 HOH 46  446 636  HOH HOH C . 
HA 7 HOH 47  447 201  HOH HOH C . 
HA 7 HOH 48  448 243  HOH HOH C . 
HA 7 HOH 49  449 128  HOH HOH C . 
HA 7 HOH 50  450 113  HOH HOH C . 
HA 7 HOH 51  451 357  HOH HOH C . 
HA 7 HOH 52  452 181  HOH HOH C . 
HA 7 HOH 53  453 377  HOH HOH C . 
HA 7 HOH 54  454 692  HOH HOH C . 
HA 7 HOH 55  455 1146 HOH HOH C . 
HA 7 HOH 56  456 277  HOH HOH C . 
HA 7 HOH 57  457 1009 HOH HOH C . 
HA 7 HOH 58  458 731  HOH HOH C . 
HA 7 HOH 59  459 1274 HOH HOH C . 
HA 7 HOH 60  460 534  HOH HOH C . 
HA 7 HOH 61  461 482  HOH HOH C . 
HA 7 HOH 62  462 684  HOH HOH C . 
HA 7 HOH 63  463 139  HOH HOH C . 
HA 7 HOH 64  464 12   HOH HOH C . 
HA 7 HOH 65  465 545  HOH HOH C . 
HA 7 HOH 66  466 434  HOH HOH C . 
HA 7 HOH 67  467 63   HOH HOH C . 
HA 7 HOH 68  468 639  HOH HOH C . 
HA 7 HOH 69  469 756  HOH HOH C . 
HA 7 HOH 70  470 671  HOH HOH C . 
HA 7 HOH 71  471 293  HOH HOH C . 
HA 7 HOH 72  472 146  HOH HOH C . 
HA 7 HOH 73  473 6    HOH HOH C . 
HA 7 HOH 74  474 913  HOH HOH C . 
HA 7 HOH 75  475 648  HOH HOH C . 
HA 7 HOH 76  476 99   HOH HOH C . 
HA 7 HOH 77  477 607  HOH HOH C . 
HA 7 HOH 78  478 625  HOH HOH C . 
HA 7 HOH 79  479 121  HOH HOH C . 
HA 7 HOH 80  480 476  HOH HOH C . 
HA 7 HOH 81  481 617  HOH HOH C . 
HA 7 HOH 82  482 251  HOH HOH C . 
HA 7 HOH 83  483 76   HOH HOH C . 
HA 7 HOH 84  484 250  HOH HOH C . 
HA 7 HOH 85  485 50   HOH HOH C . 
HA 7 HOH 86  486 239  HOH HOH C . 
HA 7 HOH 87  487 528  HOH HOH C . 
HA 7 HOH 88  488 419  HOH HOH C . 
HA 7 HOH 89  489 615  HOH HOH C . 
HA 7 HOH 90  490 1018 HOH HOH C . 
HA 7 HOH 91  491 967  HOH HOH C . 
HA 7 HOH 92  492 1196 HOH HOH C . 
HA 7 HOH 93  493 88   HOH HOH C . 
HA 7 HOH 94  494 233  HOH HOH C . 
HA 7 HOH 95  495 1001 HOH HOH C . 
HA 7 HOH 96  496 197  HOH HOH C . 
HA 7 HOH 97  497 200  HOH HOH C . 
HA 7 HOH 98  498 148  HOH HOH C . 
HA 7 HOH 99  499 630  HOH HOH C . 
HA 7 HOH 100 500 174  HOH HOH C . 
HA 7 HOH 101 501 167  HOH HOH C . 
HA 7 HOH 102 502 1304 HOH HOH C . 
HA 7 HOH 103 503 550  HOH HOH C . 
HA 7 HOH 104 504 571  HOH HOH C . 
HA 7 HOH 105 505 881  HOH HOH C . 
HA 7 HOH 106 506 54   HOH HOH C . 
HA 7 HOH 107 507 1059 HOH HOH C . 
HA 7 HOH 108 508 435  HOH HOH C . 
HA 7 HOH 109 509 670  HOH HOH C . 
HA 7 HOH 110 510 775  HOH HOH C . 
HA 7 HOH 111 511 889  HOH HOH C . 
HA 7 HOH 112 512 294  HOH HOH C . 
HA 7 HOH 113 513 22   HOH HOH C . 
HA 7 HOH 114 514 969  HOH HOH C . 
HA 7 HOH 115 515 447  HOH HOH C . 
HA 7 HOH 116 516 1276 HOH HOH C . 
HA 7 HOH 117 517 653  HOH HOH C . 
HA 7 HOH 118 518 152  HOH HOH C . 
HA 7 HOH 119 519 14   HOH HOH C . 
HA 7 HOH 120 520 339  HOH HOH C . 
HA 7 HOH 121 521 30   HOH HOH C . 
HA 7 HOH 122 522 385  HOH HOH C . 
HA 7 HOH 123 523 737  HOH HOH C . 
HA 7 HOH 124 524 1356 HOH HOH C . 
HA 7 HOH 125 525 890  HOH HOH C . 
HA 7 HOH 126 526 75   HOH HOH C . 
HA 7 HOH 127 527 313  HOH HOH C . 
HA 7 HOH 128 528 862  HOH HOH C . 
HA 7 HOH 129 529 28   HOH HOH C . 
HA 7 HOH 130 530 459  HOH HOH C . 
HA 7 HOH 131 531 1206 HOH HOH C . 
HA 7 HOH 132 532 631  HOH HOH C . 
HA 7 HOH 133 533 988  HOH HOH C . 
HA 7 HOH 134 534 1046 HOH HOH C . 
HA 7 HOH 135 535 759  HOH HOH C . 
HA 7 HOH 136 536 973  HOH HOH C . 
HA 7 HOH 137 537 202  HOH HOH C . 
HA 7 HOH 138 538 396  HOH HOH C . 
HA 7 HOH 139 539 643  HOH HOH C . 
HA 7 HOH 140 540 530  HOH HOH C . 
HA 7 HOH 141 541 939  HOH HOH C . 
HA 7 HOH 142 542 11   HOH HOH C . 
HA 7 HOH 143 543 108  HOH HOH C . 
HA 7 HOH 144 544 204  HOH HOH C . 
HA 7 HOH 145 545 58   HOH HOH C . 
HA 7 HOH 146 546 601  HOH HOH C . 
HA 7 HOH 147 547 956  HOH HOH C . 
HA 7 HOH 148 548 322  HOH HOH C . 
HA 7 HOH 149 549 280  HOH HOH C . 
HA 7 HOH 150 550 21   HOH HOH C . 
HA 7 HOH 151 551 26   HOH HOH C . 
HA 7 HOH 152 552 1195 HOH HOH C . 
HA 7 HOH 153 553 404  HOH HOH C . 
HA 7 HOH 154 554 20   HOH HOH C . 
HA 7 HOH 155 555 987  HOH HOH C . 
HA 7 HOH 156 556 228  HOH HOH C . 
HA 7 HOH 157 557 349  HOH HOH C . 
HA 7 HOH 158 558 65   HOH HOH C . 
HA 7 HOH 159 559 1414 HOH HOH C . 
HA 7 HOH 160 560 1328 HOH HOH C . 
HA 7 HOH 161 561 1083 HOH HOH C . 
HA 7 HOH 162 562 290  HOH HOH C . 
HA 7 HOH 163 563 475  HOH HOH C . 
HA 7 HOH 164 564 169  HOH HOH C . 
HA 7 HOH 165 565 1129 HOH HOH C . 
HA 7 HOH 166 566 578  HOH HOH C . 
HA 7 HOH 167 567 222  HOH HOH C . 
HA 7 HOH 168 568 41   HOH HOH C . 
HA 7 HOH 169 569 170  HOH HOH C . 
HA 7 HOH 170 570 301  HOH HOH C . 
HA 7 HOH 171 571 614  HOH HOH C . 
HA 7 HOH 172 572 888  HOH HOH C . 
HA 7 HOH 173 573 778  HOH HOH C . 
HA 7 HOH 174 574 304  HOH HOH C . 
HA 7 HOH 175 575 559  HOH HOH C . 
HA 7 HOH 176 576 364  HOH HOH C . 
HA 7 HOH 177 577 36   HOH HOH C . 
HA 7 HOH 178 578 324  HOH HOH C . 
HA 7 HOH 179 579 60   HOH HOH C . 
HA 7 HOH 180 580 234  HOH HOH C . 
HA 7 HOH 181 581 407  HOH HOH C . 
HA 7 HOH 182 582 185  HOH HOH C . 
HA 7 HOH 183 583 672  HOH HOH C . 
HA 7 HOH 184 584 207  HOH HOH C . 
HA 7 HOH 185 585 650  HOH HOH C . 
HA 7 HOH 186 586 1198 HOH HOH C . 
HA 7 HOH 187 587 1032 HOH HOH C . 
HA 7 HOH 188 588 722  HOH HOH C . 
HA 7 HOH 189 589 726  HOH HOH C . 
HA 7 HOH 190 590 978  HOH HOH C . 
HA 7 HOH 191 591 655  HOH HOH C . 
HA 7 HOH 192 592 68   HOH HOH C . 
HA 7 HOH 193 593 1062 HOH HOH C . 
HA 7 HOH 194 594 1101 HOH HOH C . 
HA 7 HOH 195 595 1085 HOH HOH C . 
HA 7 HOH 196 596 441  HOH HOH C . 
HA 7 HOH 197 597 768  HOH HOH C . 
HA 7 HOH 198 598 1112 HOH HOH C . 
HA 7 HOH 199 599 311  HOH HOH C . 
HA 7 HOH 200 600 560  HOH HOH C . 
HA 7 HOH 201 601 693  HOH HOH C . 
HA 7 HOH 202 602 1418 HOH HOH C . 
HA 7 HOH 203 603 279  HOH HOH C . 
HA 7 HOH 204 604 1081 HOH HOH C . 
HA 7 HOH 205 605 1318 HOH HOH C . 
HA 7 HOH 206 606 762  HOH HOH C . 
HA 7 HOH 207 607 924  HOH HOH C . 
HA 7 HOH 208 608 1307 HOH HOH C . 
HA 7 HOH 209 609 745  HOH HOH C . 
HA 7 HOH 210 610 400  HOH HOH C . 
HA 7 HOH 211 611 454  HOH HOH C . 
HA 7 HOH 212 612 424  HOH HOH C . 
HA 7 HOH 213 613 677  HOH HOH C . 
HA 7 HOH 214 614 1039 HOH HOH C . 
HA 7 HOH 215 615 1302 HOH HOH C . 
HA 7 HOH 216 616 1437 HOH HOH C . 
HA 7 HOH 217 617 918  HOH HOH C . 
HA 7 HOH 218 618 1363 HOH HOH C . 
HA 7 HOH 219 619 1067 HOH HOH C . 
HA 7 HOH 220 620 1366 HOH HOH C . 
HA 7 HOH 221 621 638  HOH HOH C . 
HA 7 HOH 222 622 645  HOH HOH C . 
HA 7 HOH 223 623 696  HOH HOH C . 
HA 7 HOH 224 624 1154 HOH HOH C . 
HA 7 HOH 225 625 911  HOH HOH C . 
HA 7 HOH 226 626 1199 HOH HOH C . 
HA 7 HOH 227 627 1362 HOH HOH C . 
HA 7 HOH 228 628 1114 HOH HOH C . 
HA 7 HOH 229 629 814  HOH HOH C . 
HA 7 HOH 230 630 1442 HOH HOH C . 
HA 7 HOH 231 631 1303 HOH HOH C . 
HA 7 HOH 232 632 943  HOH HOH C . 
HA 7 HOH 233 633 1417 HOH HOH C . 
HA 7 HOH 234 634 1190 HOH HOH C . 
HA 7 HOH 235 635 1358 HOH HOH C . 
HA 7 HOH 236 636 931  HOH HOH C . 
HA 7 HOH 237 637 1191 HOH HOH C . 
HA 7 HOH 238 638 682  HOH HOH C . 
HA 7 HOH 239 639 758  HOH HOH C . 
HA 7 HOH 240 640 1068 HOH HOH C . 
HA 7 HOH 241 641 1359 HOH HOH C . 
HA 7 HOH 242 642 421  HOH HOH C . 
HA 7 HOH 243 643 812  HOH HOH C . 
HA 7 HOH 244 644 995  HOH HOH C . 
HA 7 HOH 245 645 719  HOH HOH C . 
HA 7 HOH 246 646 484  HOH HOH C . 
HA 7 HOH 247 647 817  HOH HOH C . 
HA 7 HOH 248 648 1192 HOH HOH C . 
HA 7 HOH 249 649 861  HOH HOH C . 
HA 7 HOH 250 650 465  HOH HOH C . 
HA 7 HOH 251 651 873  HOH HOH C . 
HA 7 HOH 252 652 712  HOH HOH C . 
HA 7 HOH 253 653 517  HOH HOH C . 
HA 7 HOH 254 654 1361 HOH HOH C . 
HA 7 HOH 255 655 728  HOH HOH C . 
HA 7 HOH 256 656 1371 HOH HOH C . 
HA 7 HOH 257 657 527  HOH HOH C . 
HA 7 HOH 258 658 1331 HOH HOH C . 
HA 7 HOH 259 659 919  HOH HOH C . 
HA 7 HOH 260 660 581  HOH HOH C . 
HA 7 HOH 261 661 521  HOH HOH C . 
HA 7 HOH 262 662 410  HOH HOH C . 
HA 7 HOH 263 663 1020 HOH HOH C . 
HA 7 HOH 264 664 706  HOH HOH C . 
HA 7 HOH 265 665 891  HOH HOH C . 
HA 7 HOH 266 666 980  HOH HOH C . 
HA 7 HOH 267 667 1197 HOH HOH C . 
HA 7 HOH 268 668 1421 HOH HOH C . 
HA 7 HOH 269 669 1235 HOH HOH C . 
HA 7 HOH 270 670 1415 HOH HOH C . 
HA 7 HOH 271 671 1105 HOH HOH C . 
HA 7 HOH 272 672 1156 HOH HOH C . 
HA 7 HOH 273 673 1416 HOH HOH C . 
HA 7 HOH 274 674 1189 HOH HOH C . 
HA 7 HOH 275 675 348  HOH HOH C . 
HA 7 HOH 276 676 1330 HOH HOH C . 
HA 7 HOH 277 677 537  HOH HOH C . 
HA 7 HOH 278 678 998  HOH HOH C . 
HA 7 HOH 279 679 714  HOH HOH C . 
HA 7 HOH 280 680 863  HOH HOH C . 
HA 7 HOH 281 681 1034 HOH HOH C . 
HA 7 HOH 282 682 795  HOH HOH C . 
HA 7 HOH 283 683 746  HOH HOH C . 
HA 7 HOH 284 684 1275 HOH HOH C . 
HA 7 HOH 285 685 955  HOH HOH C . 
HA 7 HOH 286 686 606  HOH HOH C . 
HA 7 HOH 287 687 1364 HOH HOH C . 
HA 7 HOH 288 688 158  HOH HOH C . 
HA 7 HOH 289 689 442  HOH HOH C . 
HA 7 HOH 290 690 1272 HOH HOH C . 
HA 7 HOH 291 691 1420 HOH HOH C . 
HA 7 HOH 292 692 1028 HOH HOH C . 
HA 7 HOH 293 693 1193 HOH HOH C . 
HA 7 HOH 294 694 1327 HOH HOH C . 
HA 7 HOH 295 695 422  HOH HOH C . 
HA 7 HOH 296 696 885  HOH HOH C . 
HA 7 HOH 297 697 487  HOH HOH C . 
HA 7 HOH 298 698 565  HOH HOH C . 
HA 7 HOH 299 699 263  HOH HOH C . 
HA 7 HOH 300 700 1051 HOH HOH C . 
HA 7 HOH 301 701 1305 HOH HOH C . 
HA 7 HOH 302 702 853  HOH HOH C . 
HA 7 HOH 303 703 450  HOH HOH C . 
HA 7 HOH 304 704 634  HOH HOH C . 
HA 7 HOH 305 705 703  HOH HOH C . 
HA 7 HOH 306 706 621  HOH HOH C . 
HA 7 HOH 307 707 1234 HOH HOH C . 
HA 7 HOH 308 708 790  HOH HOH C . 
HA 7 HOH 309 709 1312 HOH HOH C . 
HA 7 HOH 310 710 1116 HOH HOH C . 
HA 7 HOH 311 711 372  HOH HOH C . 
HA 7 HOH 312 712 1030 HOH HOH C . 
HA 7 HOH 313 713 899  HOH HOH C . 
HA 7 HOH 314 714 1301 HOH HOH C . 
IA 7 HOH 1   401 1367 HOH HOH D . 
IA 7 HOH 2   402 674  HOH HOH D . 
IA 7 HOH 3   403 486  HOH HOH D . 
IA 7 HOH 4   404 1313 HOH HOH D . 
IA 7 HOH 5   405 264  HOH HOH D . 
IA 7 HOH 6   406 1148 HOH HOH D . 
IA 7 HOH 7   407 376  HOH HOH D . 
IA 7 HOH 8   408 367  HOH HOH D . 
IA 7 HOH 9   409 1005 HOH HOH D . 
IA 7 HOH 10  410 1430 HOH HOH D . 
IA 7 HOH 11  411 378  HOH HOH D . 
IA 7 HOH 12  412 923  HOH HOH D . 
IA 7 HOH 13  413 763  HOH HOH D . 
IA 7 HOH 14  414 196  HOH HOH D . 
IA 7 HOH 15  415 774  HOH HOH D . 
IA 7 HOH 16  416 1224 HOH HOH D . 
IA 7 HOH 17  417 1057 HOH HOH D . 
IA 7 HOH 18  418 1231 HOH HOH D . 
IA 7 HOH 19  419 366  HOH HOH D . 
IA 7 HOH 20  420 533  HOH HOH D . 
IA 7 HOH 21  421 403  HOH HOH D . 
IA 7 HOH 22  422 1426 HOH HOH D . 
IA 7 HOH 23  423 909  HOH HOH D . 
IA 7 HOH 24  424 838  HOH HOH D . 
IA 7 HOH 25  425 1044 HOH HOH D . 
IA 7 HOH 26  426 849  HOH HOH D . 
IA 7 HOH 27  427 555  HOH HOH D . 
IA 7 HOH 28  428 700  HOH HOH D . 
IA 7 HOH 29  429 1092 HOH HOH D . 
IA 7 HOH 30  430 633  HOH HOH D . 
IA 7 HOH 31  431 13   HOH HOH D . 
IA 7 HOH 32  432 1053 HOH HOH D . 
IA 7 HOH 33  433 793  HOH HOH D . 
IA 7 HOH 34  434 296  HOH HOH D . 
IA 7 HOH 35  435 490  HOH HOH D . 
IA 7 HOH 36  436 1223 HOH HOH D . 
IA 7 HOH 37  437 526  HOH HOH D . 
IA 7 HOH 38  438 1308 HOH HOH D . 
IA 7 HOH 39  439 451  HOH HOH D . 
IA 7 HOH 40  440 115  HOH HOH D . 
IA 7 HOH 41  441 1207 HOH HOH D . 
IA 7 HOH 42  442 333  HOH HOH D . 
IA 7 HOH 43  443 171  HOH HOH D . 
IA 7 HOH 44  444 735  HOH HOH D . 
IA 7 HOH 45  445 123  HOH HOH D . 
IA 7 HOH 46  446 1065 HOH HOH D . 
IA 7 HOH 47  447 1289 HOH HOH D . 
IA 7 HOH 48  448 358  HOH HOH D . 
IA 7 HOH 49  449 770  HOH HOH D . 
IA 7 HOH 50  450 501  HOH HOH D . 
IA 7 HOH 51  451 733  HOH HOH D . 
IA 7 HOH 52  452 1227 HOH HOH D . 
IA 7 HOH 53  453 242  HOH HOH D . 
IA 7 HOH 54  454 910  HOH HOH D . 
IA 7 HOH 55  455 541  HOH HOH D . 
IA 7 HOH 56  456 912  HOH HOH D . 
IA 7 HOH 57  457 576  HOH HOH D . 
IA 7 HOH 58  458 254  HOH HOH D . 
IA 7 HOH 59  459 715  HOH HOH D . 
IA 7 HOH 60  460 1278 HOH HOH D . 
IA 7 HOH 61  461 71   HOH HOH D . 
IA 7 HOH 62  462 105  HOH HOH D . 
IA 7 HOH 63  463 1215 HOH HOH D . 
IA 7 HOH 64  464 947  HOH HOH D . 
IA 7 HOH 65  465 494  HOH HOH D . 
IA 7 HOH 66  466 163  HOH HOH D . 
IA 7 HOH 67  467 81   HOH HOH D . 
IA 7 HOH 68  468 970  HOH HOH D . 
IA 7 HOH 69  469 237  HOH HOH D . 
IA 7 HOH 70  470 945  HOH HOH D . 
IA 7 HOH 71  471 789  HOH HOH D . 
IA 7 HOH 72  472 664  HOH HOH D . 
IA 7 HOH 73  473 1118 HOH HOH D . 
IA 7 HOH 74  474 1419 HOH HOH D . 
IA 7 HOH 75  475 173  HOH HOH D . 
IA 7 HOH 76  476 500  HOH HOH D . 
IA 7 HOH 77  477 556  HOH HOH D . 
IA 7 HOH 78  478 252  HOH HOH D . 
IA 7 HOH 79  479 109  HOH HOH D . 
IA 7 HOH 80  480 176  HOH HOH D . 
IA 7 HOH 81  481 260  HOH HOH D . 
IA 7 HOH 82  482 270  HOH HOH D . 
IA 7 HOH 83  483 1409 HOH HOH D . 
IA 7 HOH 84  484 102  HOH HOH D . 
IA 7 HOH 85  485 40   HOH HOH D . 
IA 7 HOH 86  486 1218 HOH HOH D . 
IA 7 HOH 87  487 165  HOH HOH D . 
IA 7 HOH 88  488 1441 HOH HOH D . 
IA 7 HOH 89  489 32   HOH HOH D . 
IA 7 HOH 90  490 963  HOH HOH D . 
IA 7 HOH 91  491 316  HOH HOH D . 
IA 7 HOH 92  492 583  HOH HOH D . 
IA 7 HOH 93  493 908  HOH HOH D . 
IA 7 HOH 94  494 94   HOH HOH D . 
IA 7 HOH 95  495 857  HOH HOH D . 
IA 7 HOH 96  496 56   HOH HOH D . 
IA 7 HOH 97  497 876  HOH HOH D . 
IA 7 HOH 98  498 854  HOH HOH D . 
IA 7 HOH 99  499 611  HOH HOH D . 
IA 7 HOH 100 500 764  HOH HOH D . 
IA 7 HOH 101 501 436  HOH HOH D . 
IA 7 HOH 102 502 750  HOH HOH D . 
IA 7 HOH 103 503 1212 HOH HOH D . 
IA 7 HOH 104 504 845  HOH HOH D . 
IA 7 HOH 105 505 114  HOH HOH D . 
IA 7 HOH 106 506 266  HOH HOH D . 
IA 7 HOH 107 507 34   HOH HOH D . 
IA 7 HOH 108 508 147  HOH HOH D . 
IA 7 HOH 109 509 307  HOH HOH D . 
IA 7 HOH 110 510 17   HOH HOH D . 
IA 7 HOH 111 511 850  HOH HOH D . 
IA 7 HOH 112 512 177  HOH HOH D . 
IA 7 HOH 113 513 932  HOH HOH D . 
IA 7 HOH 114 514 786  HOH HOH D . 
IA 7 HOH 115 515 381  HOH HOH D . 
IA 7 HOH 116 516 118  HOH HOH D . 
IA 7 HOH 117 517 1210 HOH HOH D . 
IA 7 HOH 118 518 997  HOH HOH D . 
IA 7 HOH 119 519 1370 HOH HOH D . 
IA 7 HOH 120 520 62   HOH HOH D . 
IA 7 HOH 121 521 563  HOH HOH D . 
IA 7 HOH 122 522 399  HOH HOH D . 
IA 7 HOH 123 523 1    HOH HOH D . 
IA 7 HOH 124 524 7    HOH HOH D . 
IA 7 HOH 125 525 1222 HOH HOH D . 
IA 7 HOH 126 526 1436 HOH HOH D . 
IA 7 HOH 127 527 92   HOH HOH D . 
IA 7 HOH 128 528 1073 HOH HOH D . 
IA 7 HOH 129 529 522  HOH HOH D . 
IA 7 HOH 130 530 394  HOH HOH D . 
IA 7 HOH 131 531 1087 HOH HOH D . 
IA 7 HOH 132 532 548  HOH HOH D . 
IA 7 HOH 133 533 1003 HOH HOH D . 
IA 7 HOH 134 534 79   HOH HOH D . 
IA 7 HOH 135 535 191  HOH HOH D . 
IA 7 HOH 136 536 825  HOH HOH D . 
IA 7 HOH 137 537 430  HOH HOH D . 
IA 7 HOH 138 538 129  HOH HOH D . 
IA 7 HOH 139 539 210  HOH HOH D . 
IA 7 HOH 140 540 1113 HOH HOH D . 
IA 7 HOH 141 541 658  HOH HOH D . 
IA 7 HOH 142 542 33   HOH HOH D . 
IA 7 HOH 143 543 262  HOH HOH D . 
IA 7 HOH 144 544 321  HOH HOH D . 
IA 7 HOH 145 545 295  HOH HOH D . 
IA 7 HOH 146 546 1188 HOH HOH D . 
IA 7 HOH 147 547 232  HOH HOH D . 
IA 7 HOH 148 548 439  HOH HOH D . 
IA 7 HOH 149 549 520  HOH HOH D . 
IA 7 HOH 150 550 867  HOH HOH D . 
IA 7 HOH 151 551 1201 HOH HOH D . 
IA 7 HOH 152 552 597  HOH HOH D . 
IA 7 HOH 153 553 443  HOH HOH D . 
IA 7 HOH 154 554 1074 HOH HOH D . 
IA 7 HOH 155 555 1431 HOH HOH D . 
IA 7 HOH 156 556 791  HOH HOH D . 
IA 7 HOH 157 557 1133 HOH HOH D . 
IA 7 HOH 158 558 69   HOH HOH D . 
IA 7 HOH 159 559 111  HOH HOH D . 
IA 7 HOH 160 560 342  HOH HOH D . 
IA 7 HOH 161 561 256  HOH HOH D . 
IA 7 HOH 162 562 1208 HOH HOH D . 
IA 7 HOH 163 563 405  HOH HOH D . 
IA 7 HOH 164 564 1149 HOH HOH D . 
IA 7 HOH 165 565 86   HOH HOH D . 
IA 7 HOH 166 566 271  HOH HOH D . 
IA 7 HOH 167 567 330  HOH HOH D . 
IA 7 HOH 168 568 259  HOH HOH D . 
IA 7 HOH 169 569 1026 HOH HOH D . 
IA 7 HOH 170 570 413  HOH HOH D . 
IA 7 HOH 171 571 1069 HOH HOH D . 
IA 7 HOH 172 572 53   HOH HOH D . 
IA 7 HOH 173 573 837  HOH HOH D . 
IA 7 HOH 174 574 97   HOH HOH D . 
IA 7 HOH 175 575 131  HOH HOH D . 
IA 7 HOH 176 576 718  HOH HOH D . 
IA 7 HOH 177 577 1309 HOH HOH D . 
IA 7 HOH 178 578 954  HOH HOH D . 
IA 7 HOH 179 579 742  HOH HOH D . 
IA 7 HOH 180 580 141  HOH HOH D . 
IA 7 HOH 181 581 29   HOH HOH D . 
IA 7 HOH 182 582 95   HOH HOH D . 
IA 7 HOH 183 583 226  HOH HOH D . 
IA 7 HOH 184 584 245  HOH HOH D . 
IA 7 HOH 185 585 1432 HOH HOH D . 
IA 7 HOH 186 586 368  HOH HOH D . 
IA 7 HOH 187 587 275  HOH HOH D . 
IA 7 HOH 188 588 363  HOH HOH D . 
IA 7 HOH 189 589 1035 HOH HOH D . 
IA 7 HOH 190 590 306  HOH HOH D . 
IA 7 HOH 191 591 1013 HOH HOH D . 
IA 7 HOH 192 592 380  HOH HOH D . 
IA 7 HOH 193 593 135  HOH HOH D . 
IA 7 HOH 194 594 85   HOH HOH D . 
IA 7 HOH 195 595 509  HOH HOH D . 
IA 7 HOH 196 596 153  HOH HOH D . 
IA 7 HOH 197 597 51   HOH HOH D . 
IA 7 HOH 198 598 244  HOH HOH D . 
IA 7 HOH 199 599 467  HOH HOH D . 
IA 7 HOH 200 600 284  HOH HOH D . 
IA 7 HOH 201 601 929  HOH HOH D . 
IA 7 HOH 202 602 972  HOH HOH D . 
IA 7 HOH 203 603 230  HOH HOH D . 
IA 7 HOH 204 604 2    HOH HOH D . 
IA 7 HOH 205 605 67   HOH HOH D . 
IA 7 HOH 206 606 1410 HOH HOH D . 
IA 7 HOH 207 607 39   HOH HOH D . 
IA 7 HOH 208 608 747  HOH HOH D . 
IA 7 HOH 209 609 1211 HOH HOH D . 
IA 7 HOH 210 610 1135 HOH HOH D . 
IA 7 HOH 211 611 218  HOH HOH D . 
IA 7 HOH 212 612 110  HOH HOH D . 
IA 7 HOH 213 613 1425 HOH HOH D . 
IA 7 HOH 214 614 1036 HOH HOH D . 
IA 7 HOH 215 615 679  HOH HOH D . 
IA 7 HOH 216 616 154  HOH HOH D . 
IA 7 HOH 217 617 507  HOH HOH D . 
IA 7 HOH 218 618 864  HOH HOH D . 
IA 7 HOH 219 619 984  HOH HOH D . 
IA 7 HOH 220 620 100  HOH HOH D . 
IA 7 HOH 221 621 580  HOH HOH D . 
IA 7 HOH 222 622 701  HOH HOH D . 
IA 7 HOH 223 623 1128 HOH HOH D . 
IA 7 HOH 224 624 549  HOH HOH D . 
IA 7 HOH 225 625 784  HOH HOH D . 
IA 7 HOH 226 626 690  HOH HOH D . 
IA 7 HOH 227 627 427  HOH HOH D . 
IA 7 HOH 228 628 870  HOH HOH D . 
IA 7 HOH 229 629 916  HOH HOH D . 
IA 7 HOH 230 630 587  HOH HOH D . 
IA 7 HOH 231 631 302  HOH HOH D . 
IA 7 HOH 232 632 331  HOH HOH D . 
IA 7 HOH 233 633 523  HOH HOH D . 
IA 7 HOH 234 634 383  HOH HOH D . 
IA 7 HOH 235 635 335  HOH HOH D . 
IA 7 HOH 236 636 787  HOH HOH D . 
IA 7 HOH 237 637 1357 HOH HOH D . 
IA 7 HOH 238 638 1060 HOH HOH D . 
IA 7 HOH 239 639 336  HOH HOH D . 
IA 7 HOH 240 640 393  HOH HOH D . 
IA 7 HOH 241 641 70   HOH HOH D . 
IA 7 HOH 242 642 308  HOH HOH D . 
IA 7 HOH 243 643 833  HOH HOH D . 
IA 7 HOH 244 644 1277 HOH HOH D . 
IA 7 HOH 245 645 1433 HOH HOH D . 
IA 7 HOH 246 646 469  HOH HOH D . 
IA 7 HOH 247 647 589  HOH HOH D . 
IA 7 HOH 248 648 236  HOH HOH D . 
IA 7 HOH 249 649 1138 HOH HOH D . 
IA 7 HOH 250 650 961  HOH HOH D . 
IA 7 HOH 251 651 1310 HOH HOH D . 
IA 7 HOH 252 652 456  HOH HOH D . 
IA 7 HOH 253 653 492  HOH HOH D . 
IA 7 HOH 254 654 629  HOH HOH D . 
IA 7 HOH 255 655 574  HOH HOH D . 
IA 7 HOH 256 656 1131 HOH HOH D . 
IA 7 HOH 257 657 915  HOH HOH D . 
IA 7 HOH 258 658 641  HOH HOH D . 
IA 7 HOH 259 659 1369 HOH HOH D . 
IA 7 HOH 260 660 1216 HOH HOH D . 
IA 7 HOH 261 661 847  HOH HOH D . 
IA 7 HOH 262 662 1434 HOH HOH D . 
IA 7 HOH 263 663 751  HOH HOH D . 
IA 7 HOH 264 664 1288 HOH HOH D . 
IA 7 HOH 265 665 570  HOH HOH D . 
IA 7 HOH 266 666 544  HOH HOH D . 
IA 7 HOH 267 667 318  HOH HOH D . 
IA 7 HOH 268 668 1229 HOH HOH D . 
IA 7 HOH 269 669 1435 HOH HOH D . 
IA 7 HOH 270 670 1109 HOH HOH D . 
IA 7 HOH 271 671 975  HOH HOH D . 
IA 7 HOH 272 672 1219 HOH HOH D . 
IA 7 HOH 273 673 1137 HOH HOH D . 
IA 7 HOH 274 674 792  HOH HOH D . 
IA 7 HOH 275 675 740  HOH HOH D . 
IA 7 HOH 276 676 460  HOH HOH D . 
IA 7 HOH 277 677 1213 HOH HOH D . 
IA 7 HOH 278 678 1368 HOH HOH D . 
IA 7 HOH 279 679 1316 HOH HOH D . 
IA 7 HOH 280 680 868  HOH HOH D . 
IA 7 HOH 281 681 805  HOH HOH D . 
IA 7 HOH 282 682 216  HOH HOH D . 
IA 7 HOH 283 683 1220 HOH HOH D . 
IA 7 HOH 284 684 1228 HOH HOH D . 
IA 7 HOH 285 685 821  HOH HOH D . 
IA 7 HOH 286 686 292  HOH HOH D . 
IA 7 HOH 287 687 612  HOH HOH D . 
IA 7 HOH 288 688 717  HOH HOH D . 
IA 7 HOH 289 689 609  HOH HOH D . 
IA 7 HOH 290 690 879  HOH HOH D . 
IA 7 HOH 291 691 388  HOH HOH D . 
IA 7 HOH 292 692 872  HOH HOH D . 
IA 7 HOH 293 693 1091 HOH HOH D . 
IA 7 HOH 294 694 959  HOH HOH D . 
IA 7 HOH 295 695 437  HOH HOH D . 
IA 7 HOH 296 696 303  HOH HOH D . 
IA 7 HOH 297 697 977  HOH HOH D . 
IA 7 HOH 298 698 741  HOH HOH D . 
IA 7 HOH 299 699 1142 HOH HOH D . 
IA 7 HOH 300 700 1119 HOH HOH D . 
IA 7 HOH 301 701 514  HOH HOH D . 
IA 7 HOH 302 702 852  HOH HOH D . 
IA 7 HOH 303 703 444  HOH HOH D . 
IA 7 HOH 304 704 1096 HOH HOH D . 
IA 7 HOH 305 705 1061 HOH HOH D . 
IA 7 HOH 306 706 1427 HOH HOH D . 
IA 7 HOH 307 707 773  HOH HOH D . 
IA 7 HOH 308 708 1205 HOH HOH D . 
IA 7 HOH 309 709 323  HOH HOH D . 
IA 7 HOH 310 710 1127 HOH HOH D . 
IA 7 HOH 311 711 1093 HOH HOH D . 
IA 7 HOH 312 712 566  HOH HOH D . 
IA 7 HOH 313 713 922  HOH HOH D . 
IA 7 HOH 314 714 749  HOH HOH D . 
IA 7 HOH 315 715 797  HOH HOH D . 
IA 7 HOH 316 716 1019 HOH HOH D . 
IA 7 HOH 317 717 744  HOH HOH D . 
IA 7 HOH 318 718 794  HOH HOH D . 
IA 7 HOH 319 719 1329 HOH HOH D . 
IA 7 HOH 320 720 646  HOH HOH D . 
IA 7 HOH 321 721 941  HOH HOH D . 
IA 7 HOH 322 722 1049 HOH HOH D . 
IA 7 HOH 323 723 651  HOH HOH D . 
IA 7 HOH 324 724 819  HOH HOH D . 
IA 7 HOH 325 725 1408 HOH HOH D . 
IA 7 HOH 326 726 884  HOH HOH D . 
IA 7 HOH 327 727 989  HOH HOH D . 
IA 7 HOH 328 728 412  HOH HOH D . 
IA 7 HOH 329 729 1221 HOH HOH D . 
IA 7 HOH 330 730 375  HOH HOH D . 
IA 7 HOH 331 731 1428 HOH HOH D . 
IA 7 HOH 332 732 840  HOH HOH D . 
IA 7 HOH 333 733 1230 HOH HOH D . 
IA 7 HOH 334 734 1214 HOH HOH D . 
IA 7 HOH 335 735 1103 HOH HOH D . 
IA 7 HOH 336 736 608  HOH HOH D . 
IA 7 HOH 337 737 1122 HOH HOH D . 
IA 7 HOH 338 738 1042 HOH HOH D . 
IA 7 HOH 339 739 971  HOH HOH D . 
IA 7 HOH 340 740 452  HOH HOH D . 
IA 7 HOH 341 741 1084 HOH HOH D . 
IA 7 HOH 342 742 1279 HOH HOH D . 
IA 7 HOH 343 743 1209 HOH HOH D . 
IA 7 HOH 344 744 809  HOH HOH D . 
IA 7 HOH 345 745 1225 HOH HOH D . 
IA 7 HOH 346 746 532  HOH HOH D . 
IA 7 HOH 347 747 675  HOH HOH D . 
IA 7 HOH 348 748 1429 HOH HOH D . 
IA 7 HOH 349 749 1037 HOH HOH D . 
IA 7 HOH 350 750 826  HOH HOH D . 
IA 7 HOH 351 751 1010 HOH HOH D . 
IA 7 HOH 352 752 711  HOH HOH D . 
IA 7 HOH 353 753 1424 HOH HOH D . 
IA 7 HOH 354 754 686  HOH HOH D . 
IA 7 HOH 355 755 1203 HOH HOH D . 
IA 7 HOH 356 756 820  HOH HOH D . 
IA 7 HOH 357 757 1204 HOH HOH D . 
IA 7 HOH 358 758 1226 HOH HOH D . 
IA 7 HOH 359 759 1411 HOH HOH D . 
IA 7 HOH 360 760 1066 HOH HOH D . 
IA 7 HOH 361 761 1115 HOH HOH D . 
IA 7 HOH 362 762 1080 HOH HOH D . 
IA 7 HOH 363 763 810  HOH HOH D . 
IA 7 HOH 364 764 1024 HOH HOH D . 
IA 7 HOH 365 765 798  HOH HOH D . 
IA 7 HOH 366 766 1202 HOH HOH D . 
IA 7 HOH 367 767 1012 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A PHE 7   ? CG  ? A PHE 7   CG  
2  1 Y 1 A PHE 7   ? CD1 ? A PHE 7   CD1 
3  1 Y 1 A PHE 7   ? CD2 ? A PHE 7   CD2 
4  1 Y 1 A PHE 7   ? CE1 ? A PHE 7   CE1 
5  1 Y 1 A PHE 7   ? CE2 ? A PHE 7   CE2 
6  1 Y 1 A PHE 7   ? CZ  ? A PHE 7   CZ  
7  1 Y 1 A ASP 35  ? CG  ? A ASP 35  CG  
8  1 Y 1 A ASP 35  ? OD1 ? A ASP 35  OD1 
9  1 Y 1 A ASP 35  ? OD2 ? A ASP 35  OD2 
10 1 Y 1 A GLU 137 ? CD  ? A GLU 137 CD  
11 1 Y 1 A GLU 137 ? OE1 ? A GLU 137 OE1 
12 1 Y 1 A GLU 137 ? OE2 ? A GLU 137 OE2 
13 1 Y 1 B LYS 18  ? CE  ? B LYS 18  CE  
14 1 Y 1 B LYS 18  ? NZ  ? B LYS 18  NZ  
15 1 Y 1 B LYS 135 ? CD  ? B LYS 135 CD  
16 1 Y 1 B LYS 135 ? CE  ? B LYS 135 CE  
17 1 Y 1 B LYS 135 ? NZ  ? B LYS 135 NZ  
18 1 Y 1 B SER 136 ? CB  ? B SER 136 CB  
19 1 Y 1 B SER 136 ? OG  ? B SER 136 OG  
20 1 Y 1 B GLU 254 ? CB  ? B GLU 254 CB  
21 1 Y 1 B GLU 254 ? CG  ? B GLU 254 CG  
22 1 Y 1 B GLU 254 ? CD  ? B GLU 254 CD  
23 1 Y 1 B GLU 254 ? OE1 ? B GLU 254 OE1 
24 1 Y 1 B GLU 254 ? OE2 ? B GLU 254 OE2 
25 1 Y 1 C LYS 3   ? CG  ? C LYS 3   CG  
26 1 Y 1 C LYS 3   ? CD  ? C LYS 3   CD  
27 1 Y 1 C LYS 3   ? CE  ? C LYS 3   CE  
28 1 Y 1 C LYS 3   ? NZ  ? C LYS 3   NZ  
29 1 Y 1 C PHE 7   ? CG  ? C PHE 7   CG  
30 1 Y 1 C PHE 7   ? CD1 ? C PHE 7   CD1 
31 1 Y 1 C PHE 7   ? CD2 ? C PHE 7   CD2 
32 1 Y 1 C PHE 7   ? CE1 ? C PHE 7   CE1 
33 1 Y 1 C PHE 7   ? CE2 ? C PHE 7   CE2 
34 1 Y 1 C PHE 7   ? CZ  ? C PHE 7   CZ  
35 1 Y 1 C ASN 56  ? CB  ? C ASN 56  CB  
36 1 Y 1 C ASN 56  ? CG  ? C ASN 56  CG  
37 1 Y 1 C ASN 56  ? OD1 ? C ASN 56  OD1 
38 1 Y 1 C ASN 56  ? ND2 ? C ASN 56  ND2 
39 1 Y 1 C LYS 57  ? CD  ? C LYS 57  CD  
40 1 Y 1 C LYS 57  ? CE  ? C LYS 57  CE  
41 1 Y 1 C LYS 57  ? NZ  ? C LYS 57  NZ  
42 1 Y 1 C GLN 79  ? CG  ? C GLN 79  CG  
43 1 Y 1 C GLN 79  ? CD  ? C GLN 79  CD  
44 1 Y 1 C GLN 79  ? OE1 ? C GLN 79  OE1 
45 1 Y 1 C GLN 79  ? NE2 ? C GLN 79  NE2 
46 1 Y 1 C GLN 82  ? CG  ? C GLN 82  CG  
47 1 Y 1 C GLN 82  ? CD  ? C GLN 82  CD  
48 1 Y 1 C GLN 82  ? OE1 ? C GLN 82  OE1 
49 1 Y 1 C GLN 82  ? NE2 ? C GLN 82  NE2 
50 1 Y 1 C GLN 219 ? CG  ? C GLN 219 CG  
51 1 Y 1 C GLN 219 ? CD  ? C GLN 219 CD  
52 1 Y 1 C GLN 219 ? OE1 ? C GLN 219 OE1 
53 1 Y 1 C GLN 219 ? NE2 ? C GLN 219 NE2 
54 1 Y 1 C ASP 235 ? CB  ? C ASP 235 CB  
55 1 Y 1 C ASP 235 ? CG  ? C ASP 235 CG  
56 1 Y 1 C ASP 235 ? OD1 ? C ASP 235 OD1 
57 1 Y 1 C ASP 235 ? OD2 ? C ASP 235 OD2 
58 1 Y 1 C ARG 240 ? CG  ? C ARG 240 CG  
59 1 Y 1 C ARG 240 ? CD  ? C ARG 240 CD  
60 1 Y 1 C ARG 240 ? NE  ? C ARG 240 NE  
61 1 Y 1 C ARG 240 ? CZ  ? C ARG 240 CZ  
62 1 Y 1 C ARG 240 ? NH1 ? C ARG 240 NH1 
63 1 Y 1 C ARG 240 ? NH2 ? C ARG 240 NH2 
64 1 Y 1 D GLN 79  ? CD  ? D GLN 79  CD  
65 1 Y 1 D GLN 79  ? OE1 ? D GLN 79  OE1 
66 1 Y 1 D GLN 79  ? NE2 ? D GLN 79  NE2 
67 1 Y 1 D GLN 263 ? C   ? D GLN 263 C   
68 1 Y 1 D GLN 263 ? O   ? D GLN 263 O   
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.6.0117 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.850 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5MSA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.170 
_cell.length_a_esd                 ? 
_cell.length_b                     74.157 
_cell.length_b_esd                 ? 
_cell.length_c                     91.559 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         5MSA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   5MSA 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.07 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.3 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.2 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer: 0.1M ammonium citrate (pH 7.2), 0.2 M ammonium sulfate and 26% PEG4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-23 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.826606 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5MSA 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.200 
_reflns.d_resolution_low                 73.032 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       294981 
_reflns.number_obs                       294981 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             97.200 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.900 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.057 
_reflns.pdbx_netI_over_av_sigmaI         2.903 
_reflns.pdbx_netI_over_sigmaI            19.900 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.068 
_reflns.pdbx_Rpim_I_all                  0.026 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         2029753 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.200 1.260  ? 3.700  ? ? ? ? ? 94.400 ? ? ? ? 0.195 ? ? ? ? ? ? ? ? 6.600 ? ? ? ? ? ? ? 1  1 ? ? 
1.260 1.340  ? 5.000  ? ? ? ? ? 95.800 ? ? ? ? 0.147 ? ? ? ? ? ? ? ? 6.900 ? ? ? ? ? ? ? 2  1 ? ? 
1.340 1.430  ? 6.800  ? ? ? ? ? 96.400 ? ? ? ? 0.107 ? ? ? ? ? ? ? ? 6.900 ? ? ? ? ? ? ? 3  1 ? ? 
1.430 1.550  ? 9.100  ? ? ? ? ? 96.900 ? ? ? ? 0.076 ? ? ? ? ? ? ? ? 6.900 ? ? ? ? ? ? ? 4  1 ? ? 
1.550 1.700  ? 11.300 ? ? ? ? ? 98.000 ? ? ? ? 0.058 ? ? ? ? ? ? ? ? 6.800 ? ? ? ? ? ? ? 5  1 ? ? 
1.700 1.900  ? 12.100 ? ? ? ? ? 97.900 ? ? ? ? 0.048 ? ? ? ? ? ? ? ? 7.000 ? ? ? ? ? ? ? 6  1 ? ? 
1.900 2.190  ? 13.100 ? ? ? ? ? 99.100 ? ? ? ? 0.042 ? ? ? ? ? ? ? ? 7.100 ? ? ? ? ? ? ? 7  1 ? ? 
2.190 2.680  ? 12.900 ? ? ? ? ? 99.200 ? ? ? ? 0.041 ? ? ? ? ? ? ? ? 7.000 ? ? ? ? ? ? ? 8  1 ? ? 
2.680 3.790  ? 6.600  ? ? ? ? ? 99.800 ? ? ? ? 0.051 ? ? ? ? ? ? ? ? 7.000 ? ? ? ? ? ? ? 9  1 ? ? 
3.790 73.032 ? 5.700  ? ? ? ? ? 99.600 ? ? ? ? 0.069 ? ? ? ? ? ? ? ? 6.700 ? ? ? ? ? ? ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            -0.5200 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -0.2900 
_refine.aniso_B[2][2]                            0.2200 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.1200 
_refine.B_iso_max                                302.940 
_refine.B_iso_mean                               19.5750 
_refine.B_iso_min                                4.720 
_refine.correlation_coeff_Fo_to_Fc               0.9760 
_refine.correlation_coeff_Fo_to_Fc_free          0.9660 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 5MSA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.2000 
_refine.ls_d_res_low                             67.6400 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     265539 
_refine.ls_number_reflns_R_free                  29410 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.9600 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1445 
_refine.ls_R_factor_R_free                       0.1779 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1408 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5LL9 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0440 
_refine.pdbx_overall_ESU_R_Free                  0.0440 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.0437 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.2000 
_refine_hist.d_res_low                        67.6400 
_refine_hist.pdbx_number_atoms_ligand         245 
_refine_hist.number_atoms_solvent             1442 
_refine_hist.number_atoms_total               10083 
_refine_hist.pdbx_number_residues_total       1045 
_refine_hist.pdbx_B_iso_mean_ligand           27.78 
_refine_hist.pdbx_B_iso_mean_solvent          30.88 
_refine_hist.pdbx_number_atoms_protein        8396 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.022  0.020  9299  ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.225  1.967  12731 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.386  5.000  1148  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 37.226 24.698 447   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.559 15.000 1416  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 17.630 15.000 33    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.155  0.200  1310  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.021  7413  ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 8.803  3.000  9299  ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 30.620 5.000  1446  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 24.184 5.000  9010  ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.2000 
_refine_ls_shell.d_res_low                        1.2310 
_refine_ls_shell.number_reflns_all                21012 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             2082 
_refine_ls_shell.number_reflns_R_work             18930 
_refine_ls_shell.percent_reflns_obs               93.6500 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.2080 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.1650 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     5MSA 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme XII with 2,3,5,6-Tetrafluoro-4-(propylthio)benzenesulfonamide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        5MSA 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, Lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 4 ? 
H  N N 4 ? 
I  N N 4 ? 
J  N N 5 ? 
K  N N 4 ? 
L  N N 4 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 2 ? 
P  N N 3 ? 
Q  N N 4 ? 
R  N N 5 ? 
S  N N 6 ? 
T  N N 2 ? 
U  N N 3 ? 
V  N N 4 ? 
W  N N 5 ? 
X  N N 4 ? 
Y  N N 2 ? 
Z  N N 3 ? 
AA N N 5 ? 
BA N N 6 ? 
CA N N 4 ? 
DA N N 6 ? 
EA N N 4 ? 
FA N N 7 ? 
GA N N 7 ? 
HA N N 7 ? 
IA N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH12_HUMAN 
_struct_ref.pdbx_db_accession          O43570 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGL
QSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSH
LQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPRE
MINNFRQVQKFDERLVYTSFSQ
;
_struct_ref.pdbx_align_begin           30 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5MSA A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 5MSA B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 5MSA C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 5MSA D 2 ? 263 ? O43570 30 ? 291 ? 2 263 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 5MSA MET A 1 ? UNP O43570 ? ? 'initiating methionine' 1 1 
2 5MSA MET B 1 ? UNP O43570 ? ? 'initiating methionine' 1 2 
3 5MSA MET C 1 ? UNP O43570 ? ? 'initiating methionine' 1 3 
4 5MSA MET D 1 ? UNP O43570 ? ? 'initiating methionine' 1 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,FA,GA 
2 1 C,D,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,HA,IA  
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PHE A 7   ? LYS A 18  ? PHE A 7   LYS A 18  5 ? 12 
HELX_P HELX_P2  AA2 TYR A 19  ? GLY A 24  ? TYR A 19  GLY A 24  5 ? 6  
HELX_P HELX_P3  AA3 HIS A 33  ? ASP A 35  ? HIS A 33  ASP A 35  5 ? 3  
HELX_P HELX_P4  AA4 ASP A 128 ? SER A 133 ? ASP A 128 SER A 133 1 ? 6  
HELX_P HELX_P5  AA5 ASN A 152 ? SER A 160 ? ASN A 152 SER A 160 1 ? 9  
HELX_P HELX_P6  AA6 HIS A 161 ? VAL A 165 ? HIS A 161 VAL A 165 5 ? 5  
HELX_P HELX_P7  AA7 ASN A 178 ? LEU A 183 ? ASN A 178 LEU A 183 5 ? 6  
HELX_P HELX_P8  AA8 SER A 218 ? ALA A 228 ? SER A 218 ALA A 228 1 ? 11 
HELX_P HELX_P9  AA9 GLY B 11  ? LYS B 18  ? GLY B 11  LYS B 18  5 ? 8  
HELX_P HELX_P10 AB1 TYR B 19  ? GLY B 24  ? TYR B 19  GLY B 24  5 ? 6  
HELX_P HELX_P11 AB2 HIS B 33  ? ASP B 35  ? HIS B 33  ASP B 35  5 ? 3  
HELX_P HELX_P12 AB3 ASP B 128 ? SER B 133 ? ASP B 128 SER B 133 1 ? 6  
HELX_P HELX_P13 AB4 ASN B 152 ? SER B 160 ? ASN B 152 SER B 160 1 ? 9  
HELX_P HELX_P14 AB5 HIS B 161 ? VAL B 165 ? HIS B 161 VAL B 165 5 ? 5  
HELX_P HELX_P15 AB6 ASN B 178 ? LEU B 183 ? ASN B 178 LEU B 183 5 ? 6  
HELX_P HELX_P16 AB7 SER B 218 ? ALA B 228 ? SER B 218 ALA B 228 1 ? 11 
HELX_P HELX_P17 AB8 PHE C 7   ? LYS C 18  ? PHE C 7   LYS C 18  5 ? 12 
HELX_P HELX_P18 AB9 TYR C 19  ? GLY C 24  ? TYR C 19  GLY C 24  5 ? 6  
HELX_P HELX_P19 AC1 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P20 AC2 ASP C 128 ? SER C 133 ? ASP C 128 SER C 133 1 ? 6  
HELX_P HELX_P21 AC3 ASN C 152 ? SER C 160 ? ASN C 152 SER C 160 1 ? 9  
HELX_P HELX_P22 AC4 HIS C 161 ? LYS C 166 ? HIS C 161 LYS C 166 5 ? 6  
HELX_P HELX_P23 AC5 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P24 AC6 GLN C 219 ? ALA C 228 ? GLN C 219 ALA C 228 1 ? 10 
HELX_P HELX_P25 AC7 GLY D 11  ? LYS D 18  ? GLY D 11  LYS D 18  5 ? 8  
HELX_P HELX_P26 AC8 TYR D 19  ? GLY D 24  ? TYR D 19  GLY D 24  5 ? 6  
HELX_P HELX_P27 AC9 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P28 AD1 ASP D 128 ? SER D 133 ? ASP D 128 SER D 133 1 ? 6  
HELX_P HELX_P29 AD2 ASN D 152 ? SER D 160 ? ASN D 152 SER D 160 1 ? 9  
HELX_P HELX_P30 AD3 HIS D 161 ? LYS D 166 ? HIS D 161 LYS D 166 5 ? 6  
HELX_P HELX_P31 AD4 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P32 AD5 SER D 218 ? LEU D 229 ? SER D 218 LEU D 229 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 22  SG  ? ? ? 1_555 A CYS 202 SG ? ? A CYS 22  A CYS 202 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf2  disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
disulf4  disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 202 SG ? ? D CYS 22  D CYS 202 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc1  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 1.988 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.017 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F 3TV .   N2 A ? A ZN  301 A 3TV 302 1_555 ? ? ? ? ? ? ? 1.833 ? ? 
metalc5  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F 3TV .   N2 B ? A ZN  301 A 3TV 302 1_555 ? ? ? ? ? ? ? 2.071 ? ? 
metalc6  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 O ZN  .   ZN ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
metalc7  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 O ZN  .   ZN ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 2.012 ? ? 
metalc8  metalc ? ? B HIS 117 ND1 ? ? ? 1_555 O ZN  .   ZN ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 2.016 ? ? 
metalc9  metalc ? ? O ZN  .   ZN  ? ? ? 1_555 P 3TV .   S1 A ? B ZN  301 B 3TV 302 1_555 ? ? ? ? ? ? ? 2.982 ? ? 
metalc10 metalc ? ? O ZN  .   ZN  ? ? ? 1_555 P 3TV .   N2 A ? B ZN  301 B 3TV 302 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc11 metalc ? ? O ZN  .   ZN  ? ? ? 1_555 P 3TV .   N2 B ? B ZN  301 B 3TV 302 1_555 ? ? ? ? ? ? ? 1.873 ? ? 
metalc12 metalc ? ? C HIS 91  NE2 ? ? ? 1_555 T ZN  .   ZN ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc13 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 T ZN  .   ZN ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 1.994 ? ? 
metalc14 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 T ZN  .   ZN ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc15 metalc ? ? T ZN  .   ZN  ? ? ? 1_555 U 3TV .   N2 ? ? C ZN  301 C 3TV 302 1_555 ? ? ? ? ? ? ? 1.932 ? ? 
metalc16 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 Y ZN  .   ZN ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 2.008 ? ? 
metalc17 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 Y ZN  .   ZN ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 1.997 ? ? 
metalc18 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 Y ZN  .   ZN ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc19 metalc ? ? Y ZN  .   ZN  ? ? ? 1_555 Z 3TV .   N2 A ? D ZN  301 D 3TV 302 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc20 metalc ? ? Y ZN  .   ZN  ? ? ? 1_555 Z 3TV .   N2 B ? D ZN  301 D 3TV 302 1_555 ? ? ? ? ? ? ? 1.903 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 93  ? A HIS 93  ? 1_555 102.7 ? 
2  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 112.7 ? 
3  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 100.2 ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N2  A F 3TV .   ? A 3TV 302 ? 1_555 111.2 ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N2  A F 3TV .   ? A 3TV 302 ? 1_555 116.8 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N2  A F 3TV .   ? A 3TV 302 ? 1_555 112.4 ? 
7  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N2  B F 3TV .   ? A 3TV 302 ? 1_555 111.4 ? 
8  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N2  B F 3TV .   ? A 3TV 302 ? 1_555 115.3 ? 
9  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N2  B F 3TV .   ? A 3TV 302 ? 1_555 113.5 ? 
10 N2  A F 3TV .   ? A 3TV 302 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N2  B F 3TV .   ? A 3TV 302 ? 1_555 1.5   ? 
11 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 103.9 ? 
12 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 111.8 ? 
13 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 99.1  ? 
14 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 S1  A P 3TV .   ? B 3TV 302 ? 1_555 99.3  ? 
15 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 S1  A P 3TV .   ? B 3TV 302 ? 1_555 141.8 ? 
16 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 S1  A P 3TV .   ? B 3TV 302 ? 1_555 99.9  ? 
17 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 N2  A P 3TV .   ? B 3TV 302 ? 1_555 114.3 ? 
18 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 N2  A P 3TV .   ? B 3TV 302 ? 1_555 113.3 ? 
19 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 N2  A P 3TV .   ? B 3TV 302 ? 1_555 113.1 ? 
20 S1  A P 3TV .   ? B 3TV 302 ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 N2  A P 3TV .   ? B 3TV 302 ? 1_555 28.5  ? 
21 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 N2  B P 3TV .   ? B 3TV 302 ? 1_555 110.7 ? 
22 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 N2  B P 3TV .   ? B 3TV 302 ? 1_555 112.2 ? 
23 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 N2  B P 3TV .   ? B 3TV 302 ? 1_555 117.9 ? 
24 S1  A P 3TV .   ? B 3TV 302 ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 N2  B P 3TV .   ? B 3TV 302 ? 1_555 30.0  ? 
25 N2  A P 3TV .   ? B 3TV 302 ? 1_555 ZN ? O ZN . ? B ZN 301 ? 1_555 N2  B P 3TV .   ? B 3TV 302 ? 1_555 4.8   ? 
26 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? T ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 102.2 ? 
27 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? T ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 113.0 ? 
28 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? T ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 98.9  ? 
29 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? T ZN . ? C ZN 301 ? 1_555 N2  ? U 3TV .   ? C 3TV 302 ? 1_555 111.1 ? 
30 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? T ZN . ? C ZN 301 ? 1_555 N2  ? U 3TV .   ? C 3TV 302 ? 1_555 118.0 ? 
31 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? T ZN . ? C ZN 301 ? 1_555 N2  ? U 3TV .   ? C 3TV 302 ? 1_555 112.8 ? 
32 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? Y ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 103.7 ? 
33 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? Y ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 112.1 ? 
34 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? Y ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 99.7  ? 
35 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? Y ZN . ? D ZN 301 ? 1_555 N2  A Z 3TV .   ? D 3TV 302 ? 1_555 116.0 ? 
36 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? Y ZN . ? D ZN 301 ? 1_555 N2  A Z 3TV .   ? D 3TV 302 ? 1_555 113.7 ? 
37 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? Y ZN . ? D ZN 301 ? 1_555 N2  A Z 3TV .   ? D 3TV 302 ? 1_555 110.4 ? 
38 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? Y ZN . ? D ZN 301 ? 1_555 N2  B Z 3TV .   ? D 3TV 302 ? 1_555 107.8 ? 
39 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? Y ZN . ? D ZN 301 ? 1_555 N2  B Z 3TV .   ? D 3TV 302 ? 1_555 115.2 ? 
40 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? Y ZN . ? D ZN 301 ? 1_555 N2  B Z 3TV .   ? D 3TV 302 ? 1_555 117.4 ? 
41 N2  A Z 3TV .   ? D 3TV 302 ? 1_555 ZN ? Y ZN . ? D ZN 301 ? 1_555 N2  B Z 3TV .   ? D 3TV 302 ? 1_555 8.5   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 22 ? CYS A 202 ? CYS A 22 ? 1_555 CYS A 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 22 ? CYS B 202 ? CYS B 22 ? 1_555 CYS B 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS C 22 ? CYS C 202 ? CYS C 22 ? 1_555 CYS C 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS D 22 ? CYS D 202 ? CYS D 22 ? 1_555 CYS D 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  SER 28  A . ? SER 28  A PRO 29  A ? PRO 29  A 1 -2.19 
2  PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 9.07  
3  SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 -2.48 
4  PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 8.66  
5  PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 11.42 
6  SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 -1.13 
7  PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 8.53  
8  SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 0.16  
9  PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 9.67  
10 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 9.07  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 6  ? 
AA7 ? 2  ? 
AA8 ? 10 ? 
AA9 ? 6  ? 
AB1 ? 2  ? 
AB2 ? 10 ? 
AB3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? parallel      
AA7 1 2  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA8 3 4  ? anti-parallel 
AA8 4 5  ? parallel      
AA8 5 6  ? anti-parallel 
AA8 6 7  ? anti-parallel 
AA8 7 8  ? anti-parallel 
AA8 8 9  ? anti-parallel 
AA8 9 10 ? anti-parallel 
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AA9 4 5  ? anti-parallel 
AA9 5 6  ? parallel      
AB1 1 2  ? parallel      
AB2 1 2  ? parallel      
AB2 2 3  ? anti-parallel 
AB2 3 4  ? anti-parallel 
AB2 4 5  ? parallel      
AB2 5 6  ? anti-parallel 
AB2 6 7  ? anti-parallel 
AB2 7 8  ? anti-parallel 
AB2 8 9  ? anti-parallel 
AB2 9 10 ? anti-parallel 
AB3 1 2  ? anti-parallel 
AB3 2 3  ? anti-parallel 
AB3 3 4  ? anti-parallel 
AB3 4 5  ? anti-parallel 
AB3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 31  ? LEU A 32  ? ASP A 31  LEU A 32  
AA1 2  THR A 106 ? VAL A 107 ? THR A 106 VAL A 107 
AA2 1  LEU A 37  ? TYR A 39  ? LEU A 37  TYR A 39  
AA2 2  VAL A 257 ? THR A 259 ? VAL A 257 THR A 259 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? PHE A 211 ? VAL A 206 PHE A 211 
AA2 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
AA2 6  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
AA2 7  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
AA2 8  VAL A 68  ? ASN A 71  ? VAL A 68  ASN A 71  
AA2 9  GLN A 58  ? ASN A 63  ? GLN A 58  ASN A 63  
AA2 10 GLU A 171 ? PRO A 175 ? GLU A 171 PRO A 175 
AA3 1  GLU A 47  ? GLN A 49  ? GLU A 47  GLN A 49  
AA3 2  HIS A 77  ? GLN A 79  ? HIS A 77  GLN A 79  
AA3 3  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
AA3 4  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
AA3 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
AA3 6  VAL A 215 ? ILE A 217 ? VAL A 215 ILE A 217 
AA4 1  ASP B 31  ? LEU B 32  ? ASP B 31  LEU B 32  
AA4 2  THR B 106 ? VAL B 107 ? THR B 106 VAL B 107 
AA5 1  LEU B 37  ? TYR B 39  ? LEU B 37  TYR B 39  
AA5 2  VAL B 257 ? THR B 259 ? VAL B 257 THR B 259 
AA5 3  TYR B 190 ? GLY B 195 ? TYR B 190 GLY B 195 
AA5 4  VAL B 206 ? PHE B 211 ? VAL B 206 PHE B 211 
AA5 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
AA5 6  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
AA5 7  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
AA5 8  VAL B 68  ? ASN B 71  ? VAL B 68  ASN B 71  
AA5 9  GLN B 58  ? ASN B 63  ? GLN B 58  ASN B 63  
AA5 10 GLU B 171 ? PRO B 175 ? GLU B 171 PRO B 175 
AA6 1  GLU B 47  ? GLN B 49  ? GLU B 47  GLN B 49  
AA6 2  HIS B 77  ? GLN B 79  ? HIS B 77  GLN B 79  
AA6 3  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
AA6 4  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
AA6 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
AA6 6  VAL B 215 ? ILE B 217 ? VAL B 215 ILE B 217 
AA7 1  ASP C 31  ? LEU C 32  ? ASP C 31  LEU C 32  
AA7 2  THR C 106 ? VAL C 107 ? THR C 106 VAL C 107 
AA8 1  LEU C 37  ? TYR C 39  ? LEU C 37  TYR C 39  
AA8 2  VAL C 257 ? THR C 259 ? VAL C 257 THR C 259 
AA8 3  TYR C 190 ? GLY C 195 ? TYR C 190 GLY C 195 
AA8 4  VAL C 206 ? PHE C 211 ? VAL C 206 PHE C 211 
AA8 5  LEU C 139 ? GLY C 149 ? LEU C 139 GLY C 149 
AA8 6  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
AA8 7  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
AA8 8  VAL C 68  ? ASN C 71  ? VAL C 68  ASN C 71  
AA8 9  GLN C 58  ? ASN C 63  ? GLN C 58  ASN C 63  
AA8 10 GLU C 171 ? PRO C 175 ? GLU C 171 PRO C 175 
AA9 1  GLU C 47  ? GLN C 49  ? GLU C 47  GLN C 49  
AA9 2  HIS C 77  ? GLN C 79  ? HIS C 77  GLN C 79  
AA9 3  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
AA9 4  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
AA9 5  LEU C 139 ? GLY C 149 ? LEU C 139 GLY C 149 
AA9 6  VAL C 215 ? SER C 218 ? VAL C 215 SER C 218 
AB1 1  ASP D 31  ? LEU D 32  ? ASP D 31  LEU D 32  
AB1 2  THR D 106 ? VAL D 107 ? THR D 106 VAL D 107 
AB2 1  LEU D 37  ? TYR D 39  ? LEU D 37  TYR D 39  
AB2 2  VAL D 257 ? THR D 259 ? VAL D 257 THR D 259 
AB2 3  TYR D 190 ? GLY D 195 ? TYR D 190 GLY D 195 
AB2 4  VAL D 206 ? PHE D 211 ? VAL D 206 PHE D 211 
AB2 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB2 6  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB2 7  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB2 8  VAL D 68  ? ASN D 71  ? VAL D 68  ASN D 71  
AB2 9  GLN D 58  ? ASN D 63  ? GLN D 58  ASN D 63  
AB2 10 GLU D 171 ? PRO D 175 ? GLU D 171 PRO D 175 
AB3 1  GLU D 47  ? GLN D 49  ? GLU D 47  GLN D 49  
AB3 2  HIS D 77  ? GLN D 79  ? HIS D 77  GLN D 79  
AB3 3  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB3 4  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB3 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB3 6  VAL D 215 ? ILE D 217 ? VAL D 215 ILE D 217 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N LEU A 32  ? N LEU A 32  O THR A 106 ? O THR A 106 
AA2 1 2  N GLN A 38  ? N GLN A 38  O THR A 259 ? O THR A 259 
AA2 2 3  O TYR A 258 ? O TYR A 258 N ARG A 192 ? N ARG A 192 
AA2 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
AA2 4 5  O THR A 209 ? O THR A 209 N ALA A 143 ? N ALA A 143 
AA2 5 6  O VAL A 144 ? O VAL A 144 N LEU A 116 ? N LEU A 116 
AA2 6 7  O HIS A 117 ? O HIS A 117 N HIS A 91  ? N HIS A 91  
AA2 7 8  O LEU A 90  ? O LEU A 90  N LEU A 70  ? N LEU A 70  
AA2 8 9  O LYS A 69  ? O LYS A 69  N THR A 62  ? N THR A 62  
AA2 9 10 N LEU A 61  ? N LEU A 61  O ALA A 172 ? O ALA A 172 
AA3 1 2  N GLN A 49  ? N GLN A 49  O HIS A 77  ? O HIS A 77  
AA3 2 3  N ILE A 78  ? N ILE A 78  O TYR A 85  ? O TYR A 85  
AA3 3 4  N HIS A 91  ? N HIS A 91  O HIS A 117 ? O HIS A 117 
AA3 4 5  N LEU A 116 ? N LEU A 116 O VAL A 144 ? O VAL A 144 
AA3 5 6  N GLU A 147 ? N GLU A 147 O VAL A 215 ? O VAL A 215 
AA4 1 2  N LEU B 32  ? N LEU B 32  O THR B 106 ? O THR B 106 
AA5 1 2  N GLN B 38  ? N GLN B 38  O THR B 259 ? O THR B 259 
AA5 2 3  O TYR B 258 ? O TYR B 258 N ARG B 192 ? N ARG B 192 
AA5 3 4  N GLY B 195 ? N GLY B 195 O VAL B 206 ? O VAL B 206 
AA5 4 5  O THR B 209 ? O THR B 209 N ALA B 143 ? N ALA B 143 
AA5 5 6  O LEU B 142 ? O LEU B 142 N ILE B 118 ? N ILE B 118 
AA5 6 7  O VAL B 119 ? O VAL B 119 N GLN B 89  ? N GLN B 89  
AA5 7 8  O LEU B 90  ? O LEU B 90  N LEU B 70  ? N LEU B 70  
AA5 8 9  O ASN B 71  ? O ASN B 71  N LEU B 60  ? N LEU B 60  
AA5 9 10 N LEU B 61  ? N LEU B 61  O ALA B 172 ? O ALA B 172 
AA6 1 2  N GLN B 49  ? N GLN B 49  O HIS B 77  ? O HIS B 77  
AA6 2 3  N ILE B 78  ? N ILE B 78  O TYR B 85  ? O TYR B 85  
AA6 3 4  N GLN B 89  ? N GLN B 89  O VAL B 119 ? O VAL B 119 
AA6 4 5  N ILE B 118 ? N ILE B 118 O LEU B 142 ? O LEU B 142 
AA6 5 6  N GLU B 147 ? N GLU B 147 O VAL B 215 ? O VAL B 215 
AA7 1 2  N LEU C 32  ? N LEU C 32  O THR C 106 ? O THR C 106 
AA8 1 2  N GLN C 38  ? N GLN C 38  O THR C 259 ? O THR C 259 
AA8 2 3  O TYR C 258 ? O TYR C 258 N ARG C 192 ? N ARG C 192 
AA8 3 4  N GLY C 195 ? N GLY C 195 O VAL C 206 ? O VAL C 206 
AA8 4 5  O THR C 209 ? O THR C 209 N ALA C 143 ? N ALA C 143 
AA8 5 6  O VAL C 144 ? O VAL C 144 N LEU C 116 ? N LEU C 116 
AA8 6 7  O VAL C 119 ? O VAL C 119 N GLN C 89  ? N GLN C 89  
AA8 7 8  O LEU C 90  ? O LEU C 90  N LEU C 70  ? N LEU C 70  
AA8 8 9  O LYS C 69  ? O LYS C 69  N THR C 62  ? N THR C 62  
AA8 9 10 N LEU C 61  ? N LEU C 61  O ALA C 172 ? O ALA C 172 
AA9 1 2  N GLN C 49  ? N GLN C 49  O HIS C 77  ? O HIS C 77  
AA9 2 3  N ILE C 78  ? N ILE C 78  O TYR C 85  ? O TYR C 85  
AA9 3 4  N GLN C 89  ? N GLN C 89  O VAL C 119 ? O VAL C 119 
AA9 4 5  N LEU C 116 ? N LEU C 116 O VAL C 144 ? O VAL C 144 
AA9 5 6  N GLY C 149 ? N GLY C 149 O ILE C 217 ? O ILE C 217 
AB1 1 2  N LEU D 32  ? N LEU D 32  O THR D 106 ? O THR D 106 
AB2 1 2  N GLN D 38  ? N GLN D 38  O THR D 259 ? O THR D 259 
AB2 2 3  O TYR D 258 ? O TYR D 258 N ARG D 192 ? N ARG D 192 
AB2 3 4  N GLY D 195 ? N GLY D 195 O VAL D 206 ? O VAL D 206 
AB2 4 5  O THR D 209 ? O THR D 209 N ALA D 143 ? N ALA D 143 
AB2 5 6  O LEU D 142 ? O LEU D 142 N ILE D 118 ? N ILE D 118 
AB2 6 7  O HIS D 117 ? O HIS D 117 N HIS D 91  ? N HIS D 91  
AB2 7 8  O LEU D 90  ? O LEU D 90  N LEU D 70  ? N LEU D 70  
AB2 8 9  O ASN D 71  ? O ASN D 71  N LEU D 60  ? N LEU D 60  
AB2 9 10 N LEU D 61  ? N LEU D 61  O ALA D 172 ? O ALA D 172 
AB3 1 2  N GLN D 49  ? N GLN D 49  O HIS D 77  ? O HIS D 77  
AB3 2 3  N ILE D 78  ? N ILE D 78  O TYR D 85  ? O TYR D 85  
AB3 3 4  N HIS D 91  ? N HIS D 91  O HIS D 117 ? O HIS D 117 
AB3 4 5  N ILE D 118 ? N ILE D 118 O LEU D 142 ? O LEU D 142 
AB3 5 6  N GLU D 147 ? N GLU D 147 O VAL D 215 ? O VAL D 215 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A 3TV 302 ? 17 'binding site for residue 3TV A 302' 
AC3 Software A EDO 303 ? 6  'binding site for residue EDO A 303' 
AC4 Software A EDO 304 ? 5  'binding site for residue EDO A 304' 
AC5 Software A EDO 305 ? 3  'binding site for residue EDO A 305' 
AC6 Software A PEG 306 ? 4  'binding site for residue PEG A 306' 
AC7 Software A EDO 307 ? 8  'binding site for residue EDO A 307' 
AC8 Software A EDO 308 ? 5  'binding site for residue EDO A 308' 
AC9 Software A EDO 309 ? 9  'binding site for residue EDO A 309' 
AD1 Software A EDO 310 ? 4  'binding site for residue EDO A 310' 
AD2 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AD3 Software B 3TV 302 ? 18 'binding site for residue 3TV B 302' 
AD4 Software B EDO 303 ? 8  'binding site for residue EDO B 303' 
AD5 Software B PEG 304 ? 4  'binding site for residue PEG B 304' 
AD6 Software B CIT 305 ? 10 'binding site for residue CIT B 305' 
AD7 Software C ZN  301 ? 4  'binding site for residue ZN C 301'  
AD8 Software C 3TV 302 ? 14 'binding site for residue 3TV C 302' 
AD9 Software C EDO 303 ? 6  'binding site for residue EDO C 303' 
AE1 Software C PEG 304 ? 3  'binding site for residue PEG C 304' 
AE2 Software C EDO 305 ? 8  'binding site for residue EDO C 305' 
AE3 Software D ZN  301 ? 4  'binding site for residue ZN D 301'  
AE4 Software D 3TV 302 ? 17 'binding site for residue 3TV D 302' 
AE5 Software D PEG 303 ? 5  'binding site for residue PEG D 303' 
AE6 Software D CIT 304 ? 8  'binding site for residue CIT D 304' 
AE7 Software D EDO 305 ? 1  'binding site for residue EDO D 305' 
AE8 Software D CIT 306 ? 10 'binding site for residue CIT D 306' 
AE9 Software D EDO 307 ? 6  'binding site for residue EDO D 307' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 4  HIS A  91  ? HIS A 91  . ? 1_555 ? 
2   AC1 4  HIS A  93  ? HIS A 93  . ? 1_555 ? 
3   AC1 4  HIS A  117 ? HIS A 117 . ? 1_555 ? 
4   AC1 4  3TV F  .   ? 3TV A 302 . ? 1_555 ? 
5   AC2 17 HIS A  91  ? HIS A 91  . ? 1_555 ? 
6   AC2 17 HIS A  93  ? HIS A 93  . ? 1_555 ? 
7   AC2 17 HIS A  117 ? HIS A 117 . ? 1_555 ? 
8   AC2 17 VAL A  119 ? VAL A 119 . ? 1_555 ? 
9   AC2 17 LEU A  139 ? LEU A 139 . ? 1_555 ? 
10  AC2 17 VAL A  141 ? VAL A 141 . ? 1_555 ? 
11  AC2 17 LEU A  197 ? LEU A 197 . ? 1_555 ? 
12  AC2 17 THR A  198 ? THR A 198 . ? 1_555 ? 
13  AC2 17 THR A  199 ? THR A 199 . ? 1_555 ? 
14  AC2 17 PRO A  200 ? PRO A 200 . ? 1_555 ? 
15  AC2 17 TRP A  208 ? TRP A 208 . ? 1_555 ? 
16  AC2 17 ZN  E  .   ? ZN  A 301 . ? 1_555 ? 
17  AC2 17 HOH FA .   ? HOH A 428 . ? 1_555 ? 
18  AC2 17 HOH FA .   ? HOH A 681 . ? 1_555 ? 
19  AC2 17 HOH FA .   ? HOH A 702 . ? 1_555 ? 
20  AC2 17 HOH FA .   ? HOH A 745 . ? 1_555 ? 
21  AC2 17 HOH FA .   ? HOH A 775 . ? 1_555 ? 
22  AC3 6  ASN A  71  ? ASN A 71  . ? 1_555 ? 
23  AC3 6  LEU A  72  ? LEU A 72  . ? 1_555 ? 
24  AC3 6  THR A  88  ? THR A 88  . ? 1_555 ? 
25  AC3 6  HOH FA .   ? HOH A 419 . ? 1_555 ? 
26  AC3 6  HOH FA .   ? HOH A 450 . ? 1_555 ? 
27  AC3 6  HOH FA .   ? HOH A 488 . ? 1_555 ? 
28  AC4 5  THR A  62  ? THR A 62  . ? 1_555 ? 
29  AC4 5  ASN A  63  ? ASN A 63  . ? 1_555 ? 
30  AC4 5  ASN A  64  ? ASN A 64  . ? 1_555 ? 
31  AC4 5  GLY A  169 ? GLY A 169 . ? 1_555 ? 
32  AC4 5  GLU A  171 ? GLU A 171 . ? 1_555 ? 
33  AC5 3  ASP A  156 ? ASP A 156 . ? 1_555 ? 
34  AC5 3  SER A  160 ? SER A 160 . ? 1_555 ? 
35  AC5 3  HOH FA .   ? HOH A 423 . ? 1_555 ? 
36  AC6 4  SER A  150 ? SER A 150 . ? 1_555 ? 
37  AC6 4  PHE A  151 ? PHE A 151 . ? 1_555 ? 
38  AC6 4  HOH FA .   ? HOH A 421 . ? 1_555 ? 
39  AC6 4  HOH FA .   ? HOH A 451 . ? 1_555 ? 
40  AC7 8  ASP A  31  ? ASP A 31  . ? 1_555 ? 
41  AC7 8  HIS A  33  ? HIS A 33  . ? 1_555 ? 
42  AC7 8  SER A  108 ? SER A 108 . ? 1_555 ? 
43  AC7 8  GLY A  109 ? GLY A 109 . ? 1_555 ? 
44  AC7 8  HOH FA .   ? HOH A 447 . ? 1_555 ? 
45  AC7 8  HOH FA .   ? HOH A 656 . ? 1_555 ? 
46  AC7 8  GLY B  109 ? GLY B 109 . ? 1_555 ? 
47  AC7 8  HIS B  111 ? HIS B 111 . ? 1_555 ? 
48  AC8 5  TYR A  39  ? TYR A 39  . ? 1_555 ? 
49  AC8 5  ALA A  41  ? ALA A 41  . ? 1_555 ? 
50  AC8 5  SER A  260 ? SER A 260 . ? 1_555 ? 
51  AC8 5  HOH FA .   ? HOH A 406 . ? 1_555 ? 
52  AC8 5  HOH FA .   ? HOH A 522 . ? 1_555 ? 
53  AC9 9  LEU A  53  ? LEU A 53  . ? 1_555 ? 
54  AC9 9  SER A  54  ? SER A 54  . ? 1_555 ? 
55  AC9 9  LYS A  57  ? LYS A 57  . ? 1_555 ? 
56  AC9 9  PHE A  59  ? PHE A 59  . ? 1_555 ? 
57  AC9 9  PRO A  73  ? PRO A 73  . ? 1_555 ? 
58  AC9 9  ASP A  75  ? ASP A 75  . ? 1_555 ? 
59  AC9 9  HOH FA .   ? HOH A 407 . ? 1_555 ? 
60  AC9 9  HOH FA .   ? HOH A 425 . ? 1_555 ? 
61  AC9 9  GLN B  49  ? GLN B 49  . ? 1_655 ? 
62  AD1 4  ALA A  224 ? ALA A 224 . ? 1_555 ? 
63  AD1 4  THR A  227 ? THR A 227 . ? 1_555 ? 
64  AD1 4  HOH FA .   ? HOH A 492 . ? 1_555 ? 
65  AD1 4  HOH FA .   ? HOH A 619 . ? 1_555 ? 
66  AD2 4  HIS B  91  ? HIS B 91  . ? 1_555 ? 
67  AD2 4  HIS B  93  ? HIS B 93  . ? 1_555 ? 
68  AD2 4  HIS B  117 ? HIS B 117 . ? 1_555 ? 
69  AD2 4  3TV P  .   ? 3TV B 302 . ? 1_555 ? 
70  AD3 18 GLN B  89  ? GLN B 89  . ? 1_555 ? 
71  AD3 18 HIS B  91  ? HIS B 91  . ? 1_555 ? 
72  AD3 18 HIS B  93  ? HIS B 93  . ? 1_555 ? 
73  AD3 18 HIS B  117 ? HIS B 117 . ? 1_555 ? 
74  AD3 18 VAL B  119 ? VAL B 119 . ? 1_555 ? 
75  AD3 18 ALA B  129 ? ALA B 129 . ? 1_555 ? 
76  AD3 18 SER B  133 ? SER B 133 . ? 1_555 ? 
77  AD3 18 LEU B  139 ? LEU B 139 . ? 1_555 ? 
78  AD3 18 VAL B  141 ? VAL B 141 . ? 1_555 ? 
79  AD3 18 LEU B  197 ? LEU B 197 . ? 1_555 ? 
80  AD3 18 THR B  198 ? THR B 198 . ? 1_555 ? 
81  AD3 18 THR B  199 ? THR B 199 . ? 1_555 ? 
82  AD3 18 PRO B  200 ? PRO B 200 . ? 1_555 ? 
83  AD3 18 TRP B  208 ? TRP B 208 . ? 1_555 ? 
84  AD3 18 ZN  O  .   ? ZN  B 301 . ? 1_555 ? 
85  AD3 18 CIT S  .   ? CIT B 305 . ? 1_555 ? 
86  AD3 18 HOH GA .   ? HOH B 422 . ? 1_555 ? 
87  AD3 18 HOH GA .   ? HOH B 669 . ? 1_555 ? 
88  AD4 8  LEU B  43  ? LEU B 43  . ? 1_555 ? 
89  AD4 8  THR B  44  ? THR B 44  . ? 1_555 ? 
90  AD4 8  LEU B  46  ? LEU B 46  . ? 1_555 ? 
91  AD4 8  GLY B  80  ? GLY B 80  . ? 1_555 ? 
92  AD4 8  TYR B  190 ? TYR B 190 . ? 1_555 ? 
93  AD4 8  ARG B  192 ? ARG B 192 . ? 1_555 ? 
94  AD4 8  HOH GA .   ? HOH B 469 . ? 1_555 ? 
95  AD4 8  HOH GA .   ? HOH B 555 . ? 1_555 ? 
96  AD5 4  PHE B  151 ? PHE B 151 . ? 1_555 ? 
97  AD5 4  PRO B  153 ? PRO B 153 . ? 1_555 ? 
98  AD5 4  HOH GA .   ? HOH B 461 . ? 1_555 ? 
99  AD5 4  HOH GA .   ? HOH B 663 . ? 1_555 ? 
100 AD6 10 ASN B  64  ? ASN B 64  . ? 1_555 ? 
101 AD6 10 LYS B  69  ? LYS B 69  . ? 1_555 ? 
102 AD6 10 GLN B  89  ? GLN B 89  . ? 1_555 ? 
103 AD6 10 3TV P  .   ? 3TV B 302 . ? 1_555 ? 
104 AD6 10 HOH GA .   ? HOH B 402 . ? 1_555 ? 
105 AD6 10 HOH GA .   ? HOH B 406 . ? 1_555 ? 
106 AD6 10 HOH GA .   ? HOH B 408 . ? 1_555 ? 
107 AD6 10 HOH GA .   ? HOH B 411 . ? 1_555 ? 
108 AD6 10 HOH GA .   ? HOH B 422 . ? 1_555 ? 
109 AD6 10 HOH GA .   ? HOH B 439 . ? 1_555 ? 
110 AD7 4  HIS C  91  ? HIS C 91  . ? 1_555 ? 
111 AD7 4  HIS C  93  ? HIS C 93  . ? 1_555 ? 
112 AD7 4  HIS C  117 ? HIS C 117 . ? 1_555 ? 
113 AD7 4  3TV U  .   ? 3TV C 302 . ? 1_555 ? 
114 AD8 14 HIS C  91  ? HIS C 91  . ? 1_555 ? 
115 AD8 14 HIS C  93  ? HIS C 93  . ? 1_555 ? 
116 AD8 14 HIS C  117 ? HIS C 117 . ? 1_555 ? 
117 AD8 14 VAL C  119 ? VAL C 119 . ? 1_555 ? 
118 AD8 14 ALA C  129 ? ALA C 129 . ? 1_555 ? 
119 AD8 14 LEU C  139 ? LEU C 139 . ? 1_555 ? 
120 AD8 14 VAL C  141 ? VAL C 141 . ? 1_555 ? 
121 AD8 14 LEU C  197 ? LEU C 197 . ? 1_555 ? 
122 AD8 14 THR C  198 ? THR C 198 . ? 1_555 ? 
123 AD8 14 THR C  199 ? THR C 199 . ? 1_555 ? 
124 AD8 14 TRP C  208 ? TRP C 208 . ? 1_555 ? 
125 AD8 14 ZN  T  .   ? ZN  C 301 . ? 1_555 ? 
126 AD8 14 HOH HA .   ? HOH C 632 . ? 1_555 ? 
127 AD8 14 HOH HA .   ? HOH C 669 . ? 1_555 ? 
128 AD9 6  ASN C  71  ? ASN C 71  . ? 1_555 ? 
129 AD9 6  LEU C  72  ? LEU C 72  . ? 1_555 ? 
130 AD9 6  THR C  88  ? THR C 88  . ? 1_555 ? 
131 AD9 6  HOH HA .   ? HOH C 444 . ? 1_555 ? 
132 AD9 6  HOH HA .   ? HOH C 465 . ? 1_555 ? 
133 AD9 6  HOH HA .   ? HOH C 494 . ? 1_555 ? 
134 AE1 3  LYS C  17  ? LYS C 17  . ? 1_555 ? 
135 AE1 3  LYS C  18  ? LYS C 18  . ? 1_555 ? 
136 AE1 3  PRO C  20  ? PRO C 20  . ? 1_555 ? 
137 AE2 8  GLN A  82  ? GLN A 82  . ? 1_555 ? 
138 AE2 8  GLU C  220 ? GLU C 220 . ? 1_555 ? 
139 AE2 8  LEU C  223 ? LEU C 223 . ? 1_555 ? 
140 AE2 8  ALA C  224 ? ALA C 224 . ? 1_555 ? 
141 AE2 8  THR C  227 ? THR C 227 . ? 1_555 ? 
142 AE2 8  HOH HA .   ? HOH C 421 . ? 1_555 ? 
143 AE2 8  HOH HA .   ? HOH C 426 . ? 1_555 ? 
144 AE2 8  HOH HA .   ? HOH C 428 . ? 1_555 ? 
145 AE3 4  HIS D  91  ? HIS D 91  . ? 1_555 ? 
146 AE3 4  HIS D  93  ? HIS D 93  . ? 1_555 ? 
147 AE3 4  HIS D  117 ? HIS D 117 . ? 1_555 ? 
148 AE3 4  3TV Z  .   ? 3TV D 302 . ? 1_555 ? 
149 AE4 17 GLN D  89  ? GLN D 89  . ? 1_555 ? 
150 AE4 17 HIS D  91  ? HIS D 91  . ? 1_555 ? 
151 AE4 17 HIS D  93  ? HIS D 93  . ? 1_555 ? 
152 AE4 17 HIS D  117 ? HIS D 117 . ? 1_555 ? 
153 AE4 17 VAL D  119 ? VAL D 119 . ? 1_555 ? 
154 AE4 17 SER D  133 ? SER D 133 . ? 1_555 ? 
155 AE4 17 LEU D  139 ? LEU D 139 . ? 1_555 ? 
156 AE4 17 VAL D  141 ? VAL D 141 . ? 1_555 ? 
157 AE4 17 LEU D  197 ? LEU D 197 . ? 1_555 ? 
158 AE4 17 THR D  198 ? THR D 198 . ? 1_555 ? 
159 AE4 17 THR D  199 ? THR D 199 . ? 1_555 ? 
160 AE4 17 PRO D  200 ? PRO D 200 . ? 1_555 ? 
161 AE4 17 TRP D  208 ? TRP D 208 . ? 1_555 ? 
162 AE4 17 ZN  Y  .   ? ZN  D 301 . ? 1_555 ? 
163 AE4 17 CIT DA .   ? CIT D 306 . ? 1_555 ? 
164 AE4 17 HOH IA .   ? HOH D 473 . ? 1_555 ? 
165 AE4 17 HOH IA .   ? HOH D 488 . ? 1_555 ? 
166 AE5 5  THR D  62  ? THR D 62  . ? 1_555 ? 
167 AE5 5  LYS D  168 ? LYS D 168 . ? 1_555 ? 
168 AE5 5  GLY D  169 ? GLY D 169 . ? 1_555 ? 
169 AE5 5  HIS D  233 ? HIS D 233 . ? 1_555 ? 
170 AE5 5  HOH IA .   ? HOH D 463 . ? 1_555 ? 
171 AE6 8  SER D  133 ? SER D 133 . ? 1_555 ? 
172 AE6 8  ASN D  134 ? ASN D 134 . ? 1_555 ? 
173 AE6 8  PRO D  201 ? PRO D 201 . ? 1_555 ? 
174 AE6 8  ASN D  203 ? ASN D 203 . ? 1_555 ? 
175 AE6 8  HOH IA .   ? HOH D 401 . ? 1_555 ? 
176 AE6 8  HOH IA .   ? HOH D 404 . ? 1_555 ? 
177 AE6 8  HOH IA .   ? HOH D 414 . ? 1_555 ? 
178 AE6 8  HOH IA .   ? HOH D 488 . ? 1_555 ? 
179 AE7 1  ASP D  235 ? ASP D 235 . ? 1_555 ? 
180 AE8 10 ASN D  64  ? ASN D 64  . ? 1_555 ? 
181 AE8 10 LYS D  69  ? LYS D 69  . ? 1_555 ? 
182 AE8 10 GLN D  89  ? GLN D 89  . ? 1_555 ? 
183 AE8 10 3TV Z  .   ? 3TV D 302 . ? 1_555 ? 
184 AE8 10 HOH IA .   ? HOH D 405 . ? 1_555 ? 
185 AE8 10 HOH IA .   ? HOH D 419 . ? 1_555 ? 
186 AE8 10 HOH IA .   ? HOH D 447 . ? 1_555 ? 
187 AE8 10 HOH IA .   ? HOH D 463 . ? 1_555 ? 
188 AE8 10 HOH IA .   ? HOH D 481 . ? 1_555 ? 
189 AE8 10 HOH IA .   ? HOH D 650 . ? 1_555 ? 
190 AE9 6  GLU A  171 ? GLU A 171 . ? 1_454 ? 
191 AE9 6  PHE A  173 ? PHE A 173 . ? 1_454 ? 
192 AE9 6  HIS D  164 ? HIS D 164 . ? 1_555 ? 
193 AE9 6  ALA D  172 ? ALA D 172 . ? 1_555 ? 
194 AE9 6  PHE D  173 ? PHE D 173 . ? 1_555 ? 
195 AE9 6  HOH IA .   ? HOH D 472 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   5MSA 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O7  D CIT 304 ? ? O   D HOH 401 ? ? 1.68 
2  1 O   B HOH 479 ? ? O   B HOH 710 ? ? 1.75 
3  1 O   D HOH 499 ? ? O   D HOH 702 ? ? 1.84 
4  1 O   A HOH 447 ? ? O   B HOH 636 ? ? 1.89 
5  1 F17 B 3TV 302 ? B O   B HOH 669 ? ? 1.91 
6  1 OE1 A GLN 219 ? B O   A HOH 401 ? ? 1.92 
7  1 OG1 D THR 199 ? ? F15 D 3TV 302 ? B 1.92 
8  1 OG1 D THR 199 ? ? F16 D 3TV 302 ? B 1.96 
9  1 OG  B SER 16  ? ? O   B HOH 401 ? ? 2.03 
10 1 CE  A LYS 18  ? A O   A HOH 672 ? ? 2.04 
11 1 O   D SER 42  ? ? O   D HOH 402 ? ? 2.09 
12 1 O   B HOH 669 ? ? O   B HOH 679 ? ? 2.11 
13 1 O2  B CIT 305 ? ? O   B HOH 402 ? ? 2.14 
14 1 O   D HOH 441 ? ? O   D HOH 452 ? ? 2.15 
15 1 O   B HOH 566 ? ? O   B HOH 632 ? ? 2.16 
16 1 OE1 B GLU 189 ? B O   B HOH 403 ? ? 2.18 
17 1 O   B HOH 442 ? ? O   B HOH 488 ? ? 2.18 
18 1 O   A HOH 517 ? ? O   A HOH 712 ? ? 2.18 
19 1 O   B HOH 745 ? ? O   B HOH 758 ? ? 2.18 
20 1 O   A HOH 679 ? ? O   A HOH 732 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB B SER 67  ? B OG  B SER 67  ? B 1.502 1.418 0.084 0.013 N 
2 1 CG B HIS 164 ? ? CD2 B HIS 164 ? ? 1.415 1.354 0.061 0.009 N 
3 1 CG C HIS 66  ? ? CD2 C HIS 66  ? ? 1.417 1.354 0.063 0.009 N 
4 1 CG C HIS 161 ? ? CD2 C HIS 161 ? ? 1.410 1.354 0.056 0.009 N 
5 1 CG C HIS 164 ? ? CD2 C HIS 164 ? ? 1.420 1.354 0.066 0.009 N 
6 1 CB D SER 67  ? B OG  D SER 67  ? B 1.513 1.418 0.095 0.013 N 
7 1 CG D HIS 233 ? B CD2 D HIS 233 ? B 1.418 1.354 0.064 0.009 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CG A MET 148 ? B SD A MET 148 ? B CE A MET 148 ? B 115.68 100.20 15.48 1.60 N 
2 1 CA D SER 67  ? B CB D SER 67  ? B OG D SER 67  ? B 128.44 111.20 17.24 2.70 N 
3 1 C  D SER 262 ? ? N  D GLN 263 ? ? CA D GLN 263 ? ? 137.05 121.70 15.35 2.50 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 99  ? ? -152.48 76.46  
2  1 ASP A 99  ? ? -153.73 76.46  
3  1 ASN A 245 ? ? -93.21  55.10  
4  1 ASP B 99  ? ? -151.69 80.53  
5  1 GLU B 137 ? ? 57.65   18.80  
6  1 ASN B 245 ? ? -92.89  56.97  
7  1 GLU B 254 ? ? 64.98   -35.83 
8  1 LYS C 3   ? ? 35.44   47.52  
9  1 ASP C 99  ? ? -154.39 79.33  
10 1 MET C 234 ? ? -38.39  -37.28 
11 1 ASN C 245 ? ? -95.29  56.47  
12 1 ASP D 99  ? ? -151.70 79.07  
13 1 SER D 136 ? B -33.42  128.35 
14 1 ASN D 245 ? ? -95.78  55.63  
15 1 GLU D 254 ? ? 88.27   -3.06  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   SER 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    262 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLN 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    263 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -129.75 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? C HOH 714 ? 6.46 . 
2 1 O ? D HOH 767 ? 5.98 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 B MET 1 ? B MET 1 
4 1 Y 1 B SER 2 ? B SER 2 
5 1 Y 1 C MET 1 ? C MET 1 
6 1 Y 1 D MET 1 ? D MET 1 
7 1 Y 1 D SER 2 ? D SER 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
3TV F18  F  N N 1   
3TV C7   C  Y N 2   
3TV C6   C  Y N 3   
3TV F17  F  N N 4   
3TV C8   C  Y N 5   
3TV S11  S  N N 6   
3TV C12  C  N N 7   
3TV C13  C  N N 8   
3TV C14  C  N N 9   
3TV C9   C  Y N 10  
3TV F15  F  N N 11  
3TV C10  C  Y N 12  
3TV F16  F  N N 13  
3TV C5   C  Y N 14  
3TV S1   S  N N 15  
3TV O3   O  N N 16  
3TV O4   O  N N 17  
3TV N2   N  N N 18  
3TV H1   H  N N 19  
3TV H2   H  N N 20  
3TV H3   H  N N 21  
3TV H4   H  N N 22  
3TV H5   H  N N 23  
3TV H6   H  N N 24  
3TV H7   H  N N 25  
3TV H8   H  N N 26  
3TV H9   H  N N 27  
ALA N    N  N N 28  
ALA CA   C  N S 29  
ALA C    C  N N 30  
ALA O    O  N N 31  
ALA CB   C  N N 32  
ALA OXT  O  N N 33  
ALA H    H  N N 34  
ALA H2   H  N N 35  
ALA HA   H  N N 36  
ALA HB1  H  N N 37  
ALA HB2  H  N N 38  
ALA HB3  H  N N 39  
ALA HXT  H  N N 40  
ARG N    N  N N 41  
ARG CA   C  N S 42  
ARG C    C  N N 43  
ARG O    O  N N 44  
ARG CB   C  N N 45  
ARG CG   C  N N 46  
ARG CD   C  N N 47  
ARG NE   N  N N 48  
ARG CZ   C  N N 49  
ARG NH1  N  N N 50  
ARG NH2  N  N N 51  
ARG OXT  O  N N 52  
ARG H    H  N N 53  
ARG H2   H  N N 54  
ARG HA   H  N N 55  
ARG HB2  H  N N 56  
ARG HB3  H  N N 57  
ARG HG2  H  N N 58  
ARG HG3  H  N N 59  
ARG HD2  H  N N 60  
ARG HD3  H  N N 61  
ARG HE   H  N N 62  
ARG HH11 H  N N 63  
ARG HH12 H  N N 64  
ARG HH21 H  N N 65  
ARG HH22 H  N N 66  
ARG HXT  H  N N 67  
ASN N    N  N N 68  
ASN CA   C  N S 69  
ASN C    C  N N 70  
ASN O    O  N N 71  
ASN CB   C  N N 72  
ASN CG   C  N N 73  
ASN OD1  O  N N 74  
ASN ND2  N  N N 75  
ASN OXT  O  N N 76  
ASN H    H  N N 77  
ASN H2   H  N N 78  
ASN HA   H  N N 79  
ASN HB2  H  N N 80  
ASN HB3  H  N N 81  
ASN HD21 H  N N 82  
ASN HD22 H  N N 83  
ASN HXT  H  N N 84  
ASP N    N  N N 85  
ASP CA   C  N S 86  
ASP C    C  N N 87  
ASP O    O  N N 88  
ASP CB   C  N N 89  
ASP CG   C  N N 90  
ASP OD1  O  N N 91  
ASP OD2  O  N N 92  
ASP OXT  O  N N 93  
ASP H    H  N N 94  
ASP H2   H  N N 95  
ASP HA   H  N N 96  
ASP HB2  H  N N 97  
ASP HB3  H  N N 98  
ASP HD2  H  N N 99  
ASP HXT  H  N N 100 
CIT C1   C  N N 101 
CIT O1   O  N N 102 
CIT O2   O  N N 103 
CIT C2   C  N N 104 
CIT C3   C  N N 105 
CIT O7   O  N N 106 
CIT C4   C  N N 107 
CIT C5   C  N N 108 
CIT O3   O  N N 109 
CIT O4   O  N N 110 
CIT C6   C  N N 111 
CIT O5   O  N N 112 
CIT O6   O  N N 113 
CIT HO2  H  N N 114 
CIT H21  H  N N 115 
CIT H22  H  N N 116 
CIT HO7  H  N N 117 
CIT H41  H  N N 118 
CIT H42  H  N N 119 
CIT HO4  H  N N 120 
CIT HO6  H  N N 121 
CYS N    N  N N 122 
CYS CA   C  N R 123 
CYS C    C  N N 124 
CYS O    O  N N 125 
CYS CB   C  N N 126 
CYS SG   S  N N 127 
CYS OXT  O  N N 128 
CYS H    H  N N 129 
CYS H2   H  N N 130 
CYS HA   H  N N 131 
CYS HB2  H  N N 132 
CYS HB3  H  N N 133 
CYS HG   H  N N 134 
CYS HXT  H  N N 135 
EDO C1   C  N N 136 
EDO O1   O  N N 137 
EDO C2   C  N N 138 
EDO O2   O  N N 139 
EDO H11  H  N N 140 
EDO H12  H  N N 141 
EDO HO1  H  N N 142 
EDO H21  H  N N 143 
EDO H22  H  N N 144 
EDO HO2  H  N N 145 
GLN N    N  N N 146 
GLN CA   C  N S 147 
GLN C    C  N N 148 
GLN O    O  N N 149 
GLN CB   C  N N 150 
GLN CG   C  N N 151 
GLN CD   C  N N 152 
GLN OE1  O  N N 153 
GLN NE2  N  N N 154 
GLN OXT  O  N N 155 
GLN H    H  N N 156 
GLN H2   H  N N 157 
GLN HA   H  N N 158 
GLN HB2  H  N N 159 
GLN HB3  H  N N 160 
GLN HG2  H  N N 161 
GLN HG3  H  N N 162 
GLN HE21 H  N N 163 
GLN HE22 H  N N 164 
GLN HXT  H  N N 165 
GLU N    N  N N 166 
GLU CA   C  N S 167 
GLU C    C  N N 168 
GLU O    O  N N 169 
GLU CB   C  N N 170 
GLU CG   C  N N 171 
GLU CD   C  N N 172 
GLU OE1  O  N N 173 
GLU OE2  O  N N 174 
GLU OXT  O  N N 175 
GLU H    H  N N 176 
GLU H2   H  N N 177 
GLU HA   H  N N 178 
GLU HB2  H  N N 179 
GLU HB3  H  N N 180 
GLU HG2  H  N N 181 
GLU HG3  H  N N 182 
GLU HE2  H  N N 183 
GLU HXT  H  N N 184 
GLY N    N  N N 185 
GLY CA   C  N N 186 
GLY C    C  N N 187 
GLY O    O  N N 188 
GLY OXT  O  N N 189 
GLY H    H  N N 190 
GLY H2   H  N N 191 
GLY HA2  H  N N 192 
GLY HA3  H  N N 193 
GLY HXT  H  N N 194 
HIS N    N  N N 195 
HIS CA   C  N S 196 
HIS C    C  N N 197 
HIS O    O  N N 198 
HIS CB   C  N N 199 
HIS CG   C  Y N 200 
HIS ND1  N  Y N 201 
HIS CD2  C  Y N 202 
HIS CE1  C  Y N 203 
HIS NE2  N  Y N 204 
HIS OXT  O  N N 205 
HIS H    H  N N 206 
HIS H2   H  N N 207 
HIS HA   H  N N 208 
HIS HB2  H  N N 209 
HIS HB3  H  N N 210 
HIS HD1  H  N N 211 
HIS HD2  H  N N 212 
HIS HE1  H  N N 213 
HIS HE2  H  N N 214 
HIS HXT  H  N N 215 
HOH O    O  N N 216 
HOH H1   H  N N 217 
HOH H2   H  N N 218 
ILE N    N  N N 219 
ILE CA   C  N S 220 
ILE C    C  N N 221 
ILE O    O  N N 222 
ILE CB   C  N S 223 
ILE CG1  C  N N 224 
ILE CG2  C  N N 225 
ILE CD1  C  N N 226 
ILE OXT  O  N N 227 
ILE H    H  N N 228 
ILE H2   H  N N 229 
ILE HA   H  N N 230 
ILE HB   H  N N 231 
ILE HG12 H  N N 232 
ILE HG13 H  N N 233 
ILE HG21 H  N N 234 
ILE HG22 H  N N 235 
ILE HG23 H  N N 236 
ILE HD11 H  N N 237 
ILE HD12 H  N N 238 
ILE HD13 H  N N 239 
ILE HXT  H  N N 240 
LEU N    N  N N 241 
LEU CA   C  N S 242 
LEU C    C  N N 243 
LEU O    O  N N 244 
LEU CB   C  N N 245 
LEU CG   C  N N 246 
LEU CD1  C  N N 247 
LEU CD2  C  N N 248 
LEU OXT  O  N N 249 
LEU H    H  N N 250 
LEU H2   H  N N 251 
LEU HA   H  N N 252 
LEU HB2  H  N N 253 
LEU HB3  H  N N 254 
LEU HG   H  N N 255 
LEU HD11 H  N N 256 
LEU HD12 H  N N 257 
LEU HD13 H  N N 258 
LEU HD21 H  N N 259 
LEU HD22 H  N N 260 
LEU HD23 H  N N 261 
LEU HXT  H  N N 262 
LYS N    N  N N 263 
LYS CA   C  N S 264 
LYS C    C  N N 265 
LYS O    O  N N 266 
LYS CB   C  N N 267 
LYS CG   C  N N 268 
LYS CD   C  N N 269 
LYS CE   C  N N 270 
LYS NZ   N  N N 271 
LYS OXT  O  N N 272 
LYS H    H  N N 273 
LYS H2   H  N N 274 
LYS HA   H  N N 275 
LYS HB2  H  N N 276 
LYS HB3  H  N N 277 
LYS HG2  H  N N 278 
LYS HG3  H  N N 279 
LYS HD2  H  N N 280 
LYS HD3  H  N N 281 
LYS HE2  H  N N 282 
LYS HE3  H  N N 283 
LYS HZ1  H  N N 284 
LYS HZ2  H  N N 285 
LYS HZ3  H  N N 286 
LYS HXT  H  N N 287 
MET N    N  N N 288 
MET CA   C  N S 289 
MET C    C  N N 290 
MET O    O  N N 291 
MET CB   C  N N 292 
MET CG   C  N N 293 
MET SD   S  N N 294 
MET CE   C  N N 295 
MET OXT  O  N N 296 
MET H    H  N N 297 
MET H2   H  N N 298 
MET HA   H  N N 299 
MET HB2  H  N N 300 
MET HB3  H  N N 301 
MET HG2  H  N N 302 
MET HG3  H  N N 303 
MET HE1  H  N N 304 
MET HE2  H  N N 305 
MET HE3  H  N N 306 
MET HXT  H  N N 307 
PEG C1   C  N N 308 
PEG O1   O  N N 309 
PEG C2   C  N N 310 
PEG O2   O  N N 311 
PEG C3   C  N N 312 
PEG C4   C  N N 313 
PEG O4   O  N N 314 
PEG H11  H  N N 315 
PEG H12  H  N N 316 
PEG HO1  H  N N 317 
PEG H21  H  N N 318 
PEG H22  H  N N 319 
PEG H31  H  N N 320 
PEG H32  H  N N 321 
PEG H41  H  N N 322 
PEG H42  H  N N 323 
PEG HO4  H  N N 324 
PHE N    N  N N 325 
PHE CA   C  N S 326 
PHE C    C  N N 327 
PHE O    O  N N 328 
PHE CB   C  N N 329 
PHE CG   C  Y N 330 
PHE CD1  C  Y N 331 
PHE CD2  C  Y N 332 
PHE CE1  C  Y N 333 
PHE CE2  C  Y N 334 
PHE CZ   C  Y N 335 
PHE OXT  O  N N 336 
PHE H    H  N N 337 
PHE H2   H  N N 338 
PHE HA   H  N N 339 
PHE HB2  H  N N 340 
PHE HB3  H  N N 341 
PHE HD1  H  N N 342 
PHE HD2  H  N N 343 
PHE HE1  H  N N 344 
PHE HE2  H  N N 345 
PHE HZ   H  N N 346 
PHE HXT  H  N N 347 
PRO N    N  N N 348 
PRO CA   C  N S 349 
PRO C    C  N N 350 
PRO O    O  N N 351 
PRO CB   C  N N 352 
PRO CG   C  N N 353 
PRO CD   C  N N 354 
PRO OXT  O  N N 355 
PRO H    H  N N 356 
PRO HA   H  N N 357 
PRO HB2  H  N N 358 
PRO HB3  H  N N 359 
PRO HG2  H  N N 360 
PRO HG3  H  N N 361 
PRO HD2  H  N N 362 
PRO HD3  H  N N 363 
PRO HXT  H  N N 364 
SER N    N  N N 365 
SER CA   C  N S 366 
SER C    C  N N 367 
SER O    O  N N 368 
SER CB   C  N N 369 
SER OG   O  N N 370 
SER OXT  O  N N 371 
SER H    H  N N 372 
SER H2   H  N N 373 
SER HA   H  N N 374 
SER HB2  H  N N 375 
SER HB3  H  N N 376 
SER HG   H  N N 377 
SER HXT  H  N N 378 
THR N    N  N N 379 
THR CA   C  N S 380 
THR C    C  N N 381 
THR O    O  N N 382 
THR CB   C  N R 383 
THR OG1  O  N N 384 
THR CG2  C  N N 385 
THR OXT  O  N N 386 
THR H    H  N N 387 
THR H2   H  N N 388 
THR HA   H  N N 389 
THR HB   H  N N 390 
THR HG1  H  N N 391 
THR HG21 H  N N 392 
THR HG22 H  N N 393 
THR HG23 H  N N 394 
THR HXT  H  N N 395 
TRP N    N  N N 396 
TRP CA   C  N S 397 
TRP C    C  N N 398 
TRP O    O  N N 399 
TRP CB   C  N N 400 
TRP CG   C  Y N 401 
TRP CD1  C  Y N 402 
TRP CD2  C  Y N 403 
TRP NE1  N  Y N 404 
TRP CE2  C  Y N 405 
TRP CE3  C  Y N 406 
TRP CZ2  C  Y N 407 
TRP CZ3  C  Y N 408 
TRP CH2  C  Y N 409 
TRP OXT  O  N N 410 
TRP H    H  N N 411 
TRP H2   H  N N 412 
TRP HA   H  N N 413 
TRP HB2  H  N N 414 
TRP HB3  H  N N 415 
TRP HD1  H  N N 416 
TRP HE1  H  N N 417 
TRP HE3  H  N N 418 
TRP HZ2  H  N N 419 
TRP HZ3  H  N N 420 
TRP HH2  H  N N 421 
TRP HXT  H  N N 422 
TYR N    N  N N 423 
TYR CA   C  N S 424 
TYR C    C  N N 425 
TYR O    O  N N 426 
TYR CB   C  N N 427 
TYR CG   C  Y N 428 
TYR CD1  C  Y N 429 
TYR CD2  C  Y N 430 
TYR CE1  C  Y N 431 
TYR CE2  C  Y N 432 
TYR CZ   C  Y N 433 
TYR OH   O  N N 434 
TYR OXT  O  N N 435 
TYR H    H  N N 436 
TYR H2   H  N N 437 
TYR HA   H  N N 438 
TYR HB2  H  N N 439 
TYR HB3  H  N N 440 
TYR HD1  H  N N 441 
TYR HD2  H  N N 442 
TYR HE1  H  N N 443 
TYR HE2  H  N N 444 
TYR HH   H  N N 445 
TYR HXT  H  N N 446 
VAL N    N  N N 447 
VAL CA   C  N S 448 
VAL C    C  N N 449 
VAL O    O  N N 450 
VAL CB   C  N N 451 
VAL CG1  C  N N 452 
VAL CG2  C  N N 453 
VAL OXT  O  N N 454 
VAL H    H  N N 455 
VAL H2   H  N N 456 
VAL HA   H  N N 457 
VAL HB   H  N N 458 
VAL HG11 H  N N 459 
VAL HG12 H  N N 460 
VAL HG13 H  N N 461 
VAL HG21 H  N N 462 
VAL HG22 H  N N 463 
VAL HG23 H  N N 464 
VAL HXT  H  N N 465 
ZN  ZN   ZN N N 466 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
3TV C14 C13  sing N N 1   
3TV C13 C12  sing N N 2   
3TV S11 C12  sing N N 3   
3TV S11 C8   sing N N 4   
3TV F18 C7   sing N N 5   
3TV C8  C7   doub Y N 6   
3TV C8  C9   sing Y N 7   
3TV C7  C6   sing Y N 8   
3TV F15 C9   sing N N 9   
3TV C9  C10  doub Y N 10  
3TV C6  F17  sing N N 11  
3TV C6  C5   doub Y N 12  
3TV C10 C5   sing Y N 13  
3TV C10 F16  sing N N 14  
3TV C5  S1   sing N N 15  
3TV N2  S1   sing N N 16  
3TV S1  O4   doub N N 17  
3TV S1  O3   doub N N 18  
3TV C12 H1   sing N N 19  
3TV C12 H2   sing N N 20  
3TV C13 H3   sing N N 21  
3TV C13 H4   sing N N 22  
3TV C14 H5   sing N N 23  
3TV C14 H6   sing N N 24  
3TV C14 H7   sing N N 25  
3TV N2  H8   sing N N 26  
3TV N2  H9   sing N N 27  
ALA N   CA   sing N N 28  
ALA N   H    sing N N 29  
ALA N   H2   sing N N 30  
ALA CA  C    sing N N 31  
ALA CA  CB   sing N N 32  
ALA CA  HA   sing N N 33  
ALA C   O    doub N N 34  
ALA C   OXT  sing N N 35  
ALA CB  HB1  sing N N 36  
ALA CB  HB2  sing N N 37  
ALA CB  HB3  sing N N 38  
ALA OXT HXT  sing N N 39  
ARG N   CA   sing N N 40  
ARG N   H    sing N N 41  
ARG N   H2   sing N N 42  
ARG CA  C    sing N N 43  
ARG CA  CB   sing N N 44  
ARG CA  HA   sing N N 45  
ARG C   O    doub N N 46  
ARG C   OXT  sing N N 47  
ARG CB  CG   sing N N 48  
ARG CB  HB2  sing N N 49  
ARG CB  HB3  sing N N 50  
ARG CG  CD   sing N N 51  
ARG CG  HG2  sing N N 52  
ARG CG  HG3  sing N N 53  
ARG CD  NE   sing N N 54  
ARG CD  HD2  sing N N 55  
ARG CD  HD3  sing N N 56  
ARG NE  CZ   sing N N 57  
ARG NE  HE   sing N N 58  
ARG CZ  NH1  sing N N 59  
ARG CZ  NH2  doub N N 60  
ARG NH1 HH11 sing N N 61  
ARG NH1 HH12 sing N N 62  
ARG NH2 HH21 sing N N 63  
ARG NH2 HH22 sing N N 64  
ARG OXT HXT  sing N N 65  
ASN N   CA   sing N N 66  
ASN N   H    sing N N 67  
ASN N   H2   sing N N 68  
ASN CA  C    sing N N 69  
ASN CA  CB   sing N N 70  
ASN CA  HA   sing N N 71  
ASN C   O    doub N N 72  
ASN C   OXT  sing N N 73  
ASN CB  CG   sing N N 74  
ASN CB  HB2  sing N N 75  
ASN CB  HB3  sing N N 76  
ASN CG  OD1  doub N N 77  
ASN CG  ND2  sing N N 78  
ASN ND2 HD21 sing N N 79  
ASN ND2 HD22 sing N N 80  
ASN OXT HXT  sing N N 81  
ASP N   CA   sing N N 82  
ASP N   H    sing N N 83  
ASP N   H2   sing N N 84  
ASP CA  C    sing N N 85  
ASP CA  CB   sing N N 86  
ASP CA  HA   sing N N 87  
ASP C   O    doub N N 88  
ASP C   OXT  sing N N 89  
ASP CB  CG   sing N N 90  
ASP CB  HB2  sing N N 91  
ASP CB  HB3  sing N N 92  
ASP CG  OD1  doub N N 93  
ASP CG  OD2  sing N N 94  
ASP OD2 HD2  sing N N 95  
ASP OXT HXT  sing N N 96  
CIT C1  O1   doub N N 97  
CIT C1  O2   sing N N 98  
CIT C1  C2   sing N N 99  
CIT O2  HO2  sing N N 100 
CIT C2  C3   sing N N 101 
CIT C2  H21  sing N N 102 
CIT C2  H22  sing N N 103 
CIT C3  O7   sing N N 104 
CIT C3  C4   sing N N 105 
CIT C3  C6   sing N N 106 
CIT O7  HO7  sing N N 107 
CIT C4  C5   sing N N 108 
CIT C4  H41  sing N N 109 
CIT C4  H42  sing N N 110 
CIT C5  O3   doub N N 111 
CIT C5  O4   sing N N 112 
CIT O4  HO4  sing N N 113 
CIT C6  O5   doub N N 114 
CIT C6  O6   sing N N 115 
CIT O6  HO6  sing N N 116 
CYS N   CA   sing N N 117 
CYS N   H    sing N N 118 
CYS N   H2   sing N N 119 
CYS CA  C    sing N N 120 
CYS CA  CB   sing N N 121 
CYS CA  HA   sing N N 122 
CYS C   O    doub N N 123 
CYS C   OXT  sing N N 124 
CYS CB  SG   sing N N 125 
CYS CB  HB2  sing N N 126 
CYS CB  HB3  sing N N 127 
CYS SG  HG   sing N N 128 
CYS OXT HXT  sing N N 129 
EDO C1  O1   sing N N 130 
EDO C1  C2   sing N N 131 
EDO C1  H11  sing N N 132 
EDO C1  H12  sing N N 133 
EDO O1  HO1  sing N N 134 
EDO C2  O2   sing N N 135 
EDO C2  H21  sing N N 136 
EDO C2  H22  sing N N 137 
EDO O2  HO2  sing N N 138 
GLN N   CA   sing N N 139 
GLN N   H    sing N N 140 
GLN N   H2   sing N N 141 
GLN CA  C    sing N N 142 
GLN CA  CB   sing N N 143 
GLN CA  HA   sing N N 144 
GLN C   O    doub N N 145 
GLN C   OXT  sing N N 146 
GLN CB  CG   sing N N 147 
GLN CB  HB2  sing N N 148 
GLN CB  HB3  sing N N 149 
GLN CG  CD   sing N N 150 
GLN CG  HG2  sing N N 151 
GLN CG  HG3  sing N N 152 
GLN CD  OE1  doub N N 153 
GLN CD  NE2  sing N N 154 
GLN NE2 HE21 sing N N 155 
GLN NE2 HE22 sing N N 156 
GLN OXT HXT  sing N N 157 
GLU N   CA   sing N N 158 
GLU N   H    sing N N 159 
GLU N   H2   sing N N 160 
GLU CA  C    sing N N 161 
GLU CA  CB   sing N N 162 
GLU CA  HA   sing N N 163 
GLU C   O    doub N N 164 
GLU C   OXT  sing N N 165 
GLU CB  CG   sing N N 166 
GLU CB  HB2  sing N N 167 
GLU CB  HB3  sing N N 168 
GLU CG  CD   sing N N 169 
GLU CG  HG2  sing N N 170 
GLU CG  HG3  sing N N 171 
GLU CD  OE1  doub N N 172 
GLU CD  OE2  sing N N 173 
GLU OE2 HE2  sing N N 174 
GLU OXT HXT  sing N N 175 
GLY N   CA   sing N N 176 
GLY N   H    sing N N 177 
GLY N   H2   sing N N 178 
GLY CA  C    sing N N 179 
GLY CA  HA2  sing N N 180 
GLY CA  HA3  sing N N 181 
GLY C   O    doub N N 182 
GLY C   OXT  sing N N 183 
GLY OXT HXT  sing N N 184 
HIS N   CA   sing N N 185 
HIS N   H    sing N N 186 
HIS N   H2   sing N N 187 
HIS CA  C    sing N N 188 
HIS CA  CB   sing N N 189 
HIS CA  HA   sing N N 190 
HIS C   O    doub N N 191 
HIS C   OXT  sing N N 192 
HIS CB  CG   sing N N 193 
HIS CB  HB2  sing N N 194 
HIS CB  HB3  sing N N 195 
HIS CG  ND1  sing Y N 196 
HIS CG  CD2  doub Y N 197 
HIS ND1 CE1  doub Y N 198 
HIS ND1 HD1  sing N N 199 
HIS CD2 NE2  sing Y N 200 
HIS CD2 HD2  sing N N 201 
HIS CE1 NE2  sing Y N 202 
HIS CE1 HE1  sing N N 203 
HIS NE2 HE2  sing N N 204 
HIS OXT HXT  sing N N 205 
HOH O   H1   sing N N 206 
HOH O   H2   sing N N 207 
ILE N   CA   sing N N 208 
ILE N   H    sing N N 209 
ILE N   H2   sing N N 210 
ILE CA  C    sing N N 211 
ILE CA  CB   sing N N 212 
ILE CA  HA   sing N N 213 
ILE C   O    doub N N 214 
ILE C   OXT  sing N N 215 
ILE CB  CG1  sing N N 216 
ILE CB  CG2  sing N N 217 
ILE CB  HB   sing N N 218 
ILE CG1 CD1  sing N N 219 
ILE CG1 HG12 sing N N 220 
ILE CG1 HG13 sing N N 221 
ILE CG2 HG21 sing N N 222 
ILE CG2 HG22 sing N N 223 
ILE CG2 HG23 sing N N 224 
ILE CD1 HD11 sing N N 225 
ILE CD1 HD12 sing N N 226 
ILE CD1 HD13 sing N N 227 
ILE OXT HXT  sing N N 228 
LEU N   CA   sing N N 229 
LEU N   H    sing N N 230 
LEU N   H2   sing N N 231 
LEU CA  C    sing N N 232 
LEU CA  CB   sing N N 233 
LEU CA  HA   sing N N 234 
LEU C   O    doub N N 235 
LEU C   OXT  sing N N 236 
LEU CB  CG   sing N N 237 
LEU CB  HB2  sing N N 238 
LEU CB  HB3  sing N N 239 
LEU CG  CD1  sing N N 240 
LEU CG  CD2  sing N N 241 
LEU CG  HG   sing N N 242 
LEU CD1 HD11 sing N N 243 
LEU CD1 HD12 sing N N 244 
LEU CD1 HD13 sing N N 245 
LEU CD2 HD21 sing N N 246 
LEU CD2 HD22 sing N N 247 
LEU CD2 HD23 sing N N 248 
LEU OXT HXT  sing N N 249 
LYS N   CA   sing N N 250 
LYS N   H    sing N N 251 
LYS N   H2   sing N N 252 
LYS CA  C    sing N N 253 
LYS CA  CB   sing N N 254 
LYS CA  HA   sing N N 255 
LYS C   O    doub N N 256 
LYS C   OXT  sing N N 257 
LYS CB  CG   sing N N 258 
LYS CB  HB2  sing N N 259 
LYS CB  HB3  sing N N 260 
LYS CG  CD   sing N N 261 
LYS CG  HG2  sing N N 262 
LYS CG  HG3  sing N N 263 
LYS CD  CE   sing N N 264 
LYS CD  HD2  sing N N 265 
LYS CD  HD3  sing N N 266 
LYS CE  NZ   sing N N 267 
LYS CE  HE2  sing N N 268 
LYS CE  HE3  sing N N 269 
LYS NZ  HZ1  sing N N 270 
LYS NZ  HZ2  sing N N 271 
LYS NZ  HZ3  sing N N 272 
LYS OXT HXT  sing N N 273 
MET N   CA   sing N N 274 
MET N   H    sing N N 275 
MET N   H2   sing N N 276 
MET CA  C    sing N N 277 
MET CA  CB   sing N N 278 
MET CA  HA   sing N N 279 
MET C   O    doub N N 280 
MET C   OXT  sing N N 281 
MET CB  CG   sing N N 282 
MET CB  HB2  sing N N 283 
MET CB  HB3  sing N N 284 
MET CG  SD   sing N N 285 
MET CG  HG2  sing N N 286 
MET CG  HG3  sing N N 287 
MET SD  CE   sing N N 288 
MET CE  HE1  sing N N 289 
MET CE  HE2  sing N N 290 
MET CE  HE3  sing N N 291 
MET OXT HXT  sing N N 292 
PEG C1  O1   sing N N 293 
PEG C1  C2   sing N N 294 
PEG C1  H11  sing N N 295 
PEG C1  H12  sing N N 296 
PEG O1  HO1  sing N N 297 
PEG C2  O2   sing N N 298 
PEG C2  H21  sing N N 299 
PEG C2  H22  sing N N 300 
PEG O2  C3   sing N N 301 
PEG C3  C4   sing N N 302 
PEG C3  H31  sing N N 303 
PEG C3  H32  sing N N 304 
PEG C4  O4   sing N N 305 
PEG C4  H41  sing N N 306 
PEG C4  H42  sing N N 307 
PEG O4  HO4  sing N N 308 
PHE N   CA   sing N N 309 
PHE N   H    sing N N 310 
PHE N   H2   sing N N 311 
PHE CA  C    sing N N 312 
PHE CA  CB   sing N N 313 
PHE CA  HA   sing N N 314 
PHE C   O    doub N N 315 
PHE C   OXT  sing N N 316 
PHE CB  CG   sing N N 317 
PHE CB  HB2  sing N N 318 
PHE CB  HB3  sing N N 319 
PHE CG  CD1  doub Y N 320 
PHE CG  CD2  sing Y N 321 
PHE CD1 CE1  sing Y N 322 
PHE CD1 HD1  sing N N 323 
PHE CD2 CE2  doub Y N 324 
PHE CD2 HD2  sing N N 325 
PHE CE1 CZ   doub Y N 326 
PHE CE1 HE1  sing N N 327 
PHE CE2 CZ   sing Y N 328 
PHE CE2 HE2  sing N N 329 
PHE CZ  HZ   sing N N 330 
PHE OXT HXT  sing N N 331 
PRO N   CA   sing N N 332 
PRO N   CD   sing N N 333 
PRO N   H    sing N N 334 
PRO CA  C    sing N N 335 
PRO CA  CB   sing N N 336 
PRO CA  HA   sing N N 337 
PRO C   O    doub N N 338 
PRO C   OXT  sing N N 339 
PRO CB  CG   sing N N 340 
PRO CB  HB2  sing N N 341 
PRO CB  HB3  sing N N 342 
PRO CG  CD   sing N N 343 
PRO CG  HG2  sing N N 344 
PRO CG  HG3  sing N N 345 
PRO CD  HD2  sing N N 346 
PRO CD  HD3  sing N N 347 
PRO OXT HXT  sing N N 348 
SER N   CA   sing N N 349 
SER N   H    sing N N 350 
SER N   H2   sing N N 351 
SER CA  C    sing N N 352 
SER CA  CB   sing N N 353 
SER CA  HA   sing N N 354 
SER C   O    doub N N 355 
SER C   OXT  sing N N 356 
SER CB  OG   sing N N 357 
SER CB  HB2  sing N N 358 
SER CB  HB3  sing N N 359 
SER OG  HG   sing N N 360 
SER OXT HXT  sing N N 361 
THR N   CA   sing N N 362 
THR N   H    sing N N 363 
THR N   H2   sing N N 364 
THR CA  C    sing N N 365 
THR CA  CB   sing N N 366 
THR CA  HA   sing N N 367 
THR C   O    doub N N 368 
THR C   OXT  sing N N 369 
THR CB  OG1  sing N N 370 
THR CB  CG2  sing N N 371 
THR CB  HB   sing N N 372 
THR OG1 HG1  sing N N 373 
THR CG2 HG21 sing N N 374 
THR CG2 HG22 sing N N 375 
THR CG2 HG23 sing N N 376 
THR OXT HXT  sing N N 377 
TRP N   CA   sing N N 378 
TRP N   H    sing N N 379 
TRP N   H2   sing N N 380 
TRP CA  C    sing N N 381 
TRP CA  CB   sing N N 382 
TRP CA  HA   sing N N 383 
TRP C   O    doub N N 384 
TRP C   OXT  sing N N 385 
TRP CB  CG   sing N N 386 
TRP CB  HB2  sing N N 387 
TRP CB  HB3  sing N N 388 
TRP CG  CD1  doub Y N 389 
TRP CG  CD2  sing Y N 390 
TRP CD1 NE1  sing Y N 391 
TRP CD1 HD1  sing N N 392 
TRP CD2 CE2  doub Y N 393 
TRP CD2 CE3  sing Y N 394 
TRP NE1 CE2  sing Y N 395 
TRP NE1 HE1  sing N N 396 
TRP CE2 CZ2  sing Y N 397 
TRP CE3 CZ3  doub Y N 398 
TRP CE3 HE3  sing N N 399 
TRP CZ2 CH2  doub Y N 400 
TRP CZ2 HZ2  sing N N 401 
TRP CZ3 CH2  sing Y N 402 
TRP CZ3 HZ3  sing N N 403 
TRP CH2 HH2  sing N N 404 
TRP OXT HXT  sing N N 405 
TYR N   CA   sing N N 406 
TYR N   H    sing N N 407 
TYR N   H2   sing N N 408 
TYR CA  C    sing N N 409 
TYR CA  CB   sing N N 410 
TYR CA  HA   sing N N 411 
TYR C   O    doub N N 412 
TYR C   OXT  sing N N 413 
TYR CB  CG   sing N N 414 
TYR CB  HB2  sing N N 415 
TYR CB  HB3  sing N N 416 
TYR CG  CD1  doub Y N 417 
TYR CG  CD2  sing Y N 418 
TYR CD1 CE1  sing Y N 419 
TYR CD1 HD1  sing N N 420 
TYR CD2 CE2  doub Y N 421 
TYR CD2 HD2  sing N N 422 
TYR CE1 CZ   doub Y N 423 
TYR CE1 HE1  sing N N 424 
TYR CE2 CZ   sing Y N 425 
TYR CE2 HE2  sing N N 426 
TYR CZ  OH   sing N N 427 
TYR OH  HH   sing N N 428 
TYR OXT HXT  sing N N 429 
VAL N   CA   sing N N 430 
VAL N   H    sing N N 431 
VAL N   H2   sing N N 432 
VAL CA  C    sing N N 433 
VAL CA  CB   sing N N 434 
VAL CA  HA   sing N N 435 
VAL C   O    doub N N 436 
VAL C   OXT  sing N N 437 
VAL CB  CG1  sing N N 438 
VAL CB  CG2  sing N N 439 
VAL CB  HB   sing N N 440 
VAL CG1 HG11 sing N N 441 
VAL CG1 HG12 sing N N 442 
VAL CG1 HG13 sing N N 443 
VAL CG2 HG21 sing N N 444 
VAL CG2 HG22 sing N N 445 
VAL CG2 HG23 sing N N 446 
VAL OXT HXT  sing N N 447 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5LL9 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    5MSA 
_atom_sites.fract_transf_matrix[1][1]   0.012958 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004424 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013485 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.011541 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . LYS A  1 3   ? 17.401  16.720  19.330  1.00 65.21  ? 3   LYS A N   1 
ATOM   2     C  CA  . LYS A  1 3   ? 17.849  15.959  18.140  1.00 34.63  ? 3   LYS A CA  1 
ATOM   3     C  C   . LYS A  1 3   ? 16.822  14.876  17.817  1.00 45.00  ? 3   LYS A C   1 
ATOM   4     O  O   . LYS A  1 3   ? 15.666  14.891  18.306  1.00 49.56  ? 3   LYS A O   1 
ATOM   5     C  CB  . LYS A  1 3   ? 19.337  15.438  18.289  1.00 40.58  ? 3   LYS A CB  1 
ATOM   6     C  CG  . LYS A  1 3   ? 19.663  13.941  18.565  1.00 42.61  ? 3   LYS A CG  1 
ATOM   7     C  CD  . LYS A  1 3   ? 21.103  13.756  19.022  1.00 43.34  ? 3   LYS A CD  1 
ATOM   8     C  CE  . LYS A  1 3   ? 22.088  14.589  18.202  1.00 52.80  ? 3   LYS A CE  1 
ATOM   9     N  NZ  . LYS A  1 3   ? 22.105  14.109  16.795  1.00 66.52  ? 3   LYS A NZ  1 
ATOM   10    N  N   . TRP A  1 4   ? 17.270  13.964  17.009  1.00 20.93  ? 4   TRP A N   1 
ATOM   11    C  CA  . TRP A  1 4   ? 16.404  12.923  16.517  1.00 17.51  ? 4   TRP A CA  1 
ATOM   12    C  C   . TRP A  1 4   ? 16.328  11.807  17.524  1.00 13.69  ? 4   TRP A C   1 
ATOM   13    O  O   . TRP A  1 4   ? 17.252  11.571  18.309  1.00 17.00  ? 4   TRP A O   1 
ATOM   14    C  CB  . TRP A  1 4   ? 16.901  12.491  15.173  1.00 16.99  ? 4   TRP A CB  1 
ATOM   15    C  CG  . TRP A  1 4   ? 18.225  11.868  15.143  1.00 14.47  ? 4   TRP A CG  1 
ATOM   16    C  CD1 . TRP A  1 4   ? 19.428  12.458  14.945  1.00 16.33  ? 4   TRP A CD1 1 
ATOM   17    C  CD2 . TRP A  1 4   ? 18.487  10.458  15.273  1.00 13.81  ? 4   TRP A CD2 1 
ATOM   18    N  NE1 . TRP A  1 4   ? 20.418  11.551  14.884  1.00 16.51  ? 4   TRP A NE1 1 
ATOM   19    C  CE2 . TRP A  1 4   ? 19.910  10.306  15.119  1.00 13.58  ? 4   TRP A CE2 1 
ATOM   20    C  CE3 . TRP A  1 4   ? 17.673  9.326   15.458  1.00 13.33  ? 4   TRP A CE3 1 
ATOM   21    C  CZ2 . TRP A  1 4   ? 20.528  9.074   15.185  1.00 16.55  ? 4   TRP A CZ2 1 
ATOM   22    C  CZ3 . TRP A  1 4   ? 18.280  8.093   15.499  1.00 14.18  ? 4   TRP A CZ3 1 
ATOM   23    C  CH2 . TRP A  1 4   ? 19.666  7.966   15.362  1.00 15.47  ? 4   TRP A CH2 1 
ATOM   24    N  N   . THR A  1 5   ? 15.230  11.095  17.488  1.00 14.53  ? 5   THR A N   1 
ATOM   25    C  CA  . THR A  1 5   ? 15.009  9.976   18.400  1.00 15.59  ? 5   THR A CA  1 
ATOM   26    C  C   . THR A  1 5   ? 14.274  8.869   17.614  1.00 11.88  ? 5   THR A C   1 
ATOM   27    O  O   . THR A  1 5   ? 13.970  8.997   16.451  1.00 13.26  ? 5   THR A O   1 
ATOM   28    C  CB  . THR A  1 5   ? 14.119  10.318  19.633  1.00 16.34  ? 5   THR A CB  1 
ATOM   29    O  OG1 . THR A  1 5   ? 12.797  10.525  19.120  1.00 18.48  ? 5   THR A OG1 1 
ATOM   30    C  CG2 . THR A  1 5   ? 14.653  11.540  20.437  1.00 20.39  ? 5   THR A CG2 1 
ATOM   31    N  N   . TYR A  1 6   ? 14.021  7.746   18.286  1.00 14.54  ? 6   TYR A N   1 
ATOM   32    C  CA  . TYR A  1 6   ? 13.178  6.686   17.746  1.00 13.46  ? 6   TYR A CA  1 
ATOM   33    C  C   . TYR A  1 6   ? 11.752  6.689   18.318  1.00 14.43  ? 6   TYR A C   1 
ATOM   34    O  O   . TYR A  1 6   ? 10.970  5.734   18.110  1.00 15.22  ? 6   TYR A O   1 
ATOM   35    C  CB  . TYR A  1 6   ? 13.775  5.338   18.011  1.00 16.49  ? 6   TYR A CB  1 
ATOM   36    C  CG  . TYR A  1 6   ? 15.000  5.045   17.223  1.00 12.58  ? 6   TYR A CG  1 
ATOM   37    C  CD1 . TYR A  1 6   ? 16.288  5.276   17.772  1.00 14.16  ? 6   TYR A CD1 1 
ATOM   38    C  CD2 . TYR A  1 6   ? 14.924  4.548   15.936  1.00 12.43  ? 6   TYR A CD2 1 
ATOM   39    C  CE1 . TYR A  1 6   ? 17.443  4.954   17.082  1.00 13.72  ? 6   TYR A CE1 1 
ATOM   40    C  CE2 . TYR A  1 6   ? 16.107  4.194   15.225  1.00 10.23  ? 6   TYR A CE2 1 
ATOM   41    C  CZ  . TYR A  1 6   ? 17.339  4.402   15.802  1.00 11.91  ? 6   TYR A CZ  1 
ATOM   42    O  OH  . TYR A  1 6   ? 18.463  4.096   15.140  1.00 12.62  ? 6   TYR A OH  1 
ATOM   43    N  N   . PHE A  1 7   ? 11.377  7.684   19.078  1.00 20.95  ? 7   PHE A N   1 
ATOM   44    C  CA  . PHE A  1 7   ? 10.093  7.647   19.779  1.00 21.75  ? 7   PHE A CA  1 
ATOM   45    C  C   . PHE A  1 7   ? 9.601   9.081   19.856  1.00 30.01  ? 7   PHE A C   1 
ATOM   46    O  O   . PHE A  1 7   ? 10.341  10.019  19.919  1.00 41.13  ? 7   PHE A O   1 
ATOM   47    C  CB  . PHE A  1 7   ? 10.233  7.035   21.224  1.00 32.61  ? 7   PHE A CB  1 
ATOM   48    N  N   . GLY A  1 8   ? 8.292   9.265   19.915  1.00 27.98  ? 8   GLY A N   1 
ATOM   49    C  CA  . GLY A  1 8   ? 7.723   10.557  20.341  1.00 24.51  ? 8   GLY A CA  1 
ATOM   50    C  C   . GLY A  1 8   ? 7.921   11.544  19.200  1.00 25.78  ? 8   GLY A C   1 
ATOM   51    O  O   . GLY A  1 8   ? 8.087   11.186  18.043  1.00 27.47  ? 8   GLY A O   1 
ATOM   52    N  N   . PRO A  1 9   ? 7.841   12.807  19.484  1.00 24.76  ? 9   PRO A N   1 
ATOM   53    C  CA  . PRO A  1 9   ? 7.764   13.863  18.487  1.00 24.93  ? 9   PRO A CA  1 
ATOM   54    C  C   . PRO A  1 9   ? 8.927   13.921  17.528  1.00 22.92  ? 9   PRO A C   1 
ATOM   55    O  O   . PRO A  1 9   ? 8.769   14.422  16.408  1.00 21.53  ? 9   PRO A O   1 
ATOM   56    C  CB  . PRO A  1 9   ? 7.724   15.165  19.327  1.00 35.49  ? 9   PRO A CB  1 
ATOM   57    C  CG  . PRO A  1 9   ? 7.290   14.764  20.673  1.00 39.87  ? 9   PRO A CG  1 
ATOM   58    C  CD  . PRO A  1 9   ? 7.642   13.326  20.854  1.00 30.94  ? 9   PRO A CD  1 
ATOM   59    N  N   . ASP A  1 10  ? 10.083  13.448  17.970  1.00 21.70  ? 10  ASP A N   1 
ATOM   60    C  CA  . ASP A  1 10  ? 11.288  13.544  17.168  1.00 19.37  ? 10  ASP A CA  1 
ATOM   61    C  C   . ASP A  1 10  ? 11.662  12.228  16.501  1.00 15.39  ? 10  ASP A C   1 
ATOM   62    O  O   . ASP A  1 10  ? 12.817  12.026  16.055  1.00 17.75  ? 10  ASP A O   1 
ATOM   63    C  CB  . ASP A  1 10  ? 12.456  14.101  18.042  1.00 22.00  ? 10  ASP A CB  1 
ATOM   64    C  CG  . ASP A  1 10  ? 12.181  15.487  18.517  1.00 32.12  ? 10  ASP A CG  1 
ATOM   65    O  OD1 . ASP A  1 10  ? 11.743  16.324  17.701  1.00 33.91  ? 10  ASP A OD1 1 
ATOM   66    O  OD2 . ASP A  1 10  ? 12.416  15.752  19.740  1.00 45.66  ? 10  ASP A OD2 1 
ATOM   67    N  N   . GLY A  1 11  ? 10.706  11.297  16.524  1.00 16.68  ? 11  GLY A N   1 
ATOM   68    C  CA  . GLY A  1 11  ? 10.818  9.973   15.963  1.00 13.11  ? 11  GLY A CA  1 
ATOM   69    C  C   . GLY A  1 11  ? 10.907  9.939   14.432  1.00 11.13  ? 11  GLY A C   1 
ATOM   70    O  O   . GLY A  1 11  ? 10.916  10.962  13.727  1.00 11.62  ? 11  GLY A O   1 
ATOM   71    N  N   . GLU A  1 12  ? 10.909  8.710   13.895  1.00 10.70  ? 12  GLU A N   1 
ATOM   72    C  CA  . GLU A  1 12  ? 11.381  8.533   12.554  1.00 9.74   ? 12  GLU A CA  1 
ATOM   73    C  C   . GLU A  1 12  ? 10.475  9.178   11.487  1.00 9.07   ? 12  GLU A C   1 
ATOM   74    O  O   . GLU A  1 12  ? 10.990  9.502   10.401  1.00 9.88   ? 12  GLU A O   1 
ATOM   75    C  CB  . GLU A  1 12  ? 11.565  7.031   12.257  1.00 10.16  ? 12  GLU A CB  1 
ATOM   76    C  CG  . GLU A  1 12  ? 10.231  6.271   12.207  1.00 9.67   ? 12  GLU A CG  1 
ATOM   77    C  CD  . GLU A  1 12  ? 10.523  4.803   12.331  1.00 9.84   ? 12  GLU A CD  1 
ATOM   78    O  OE1 . GLU A  1 12  ? 10.797  4.110   11.328  1.00 9.09   ? 12  GLU A OE1 1 
ATOM   79    O  OE2 . GLU A  1 12  ? 10.541  4.303   13.500  1.00 11.03  ? 12  GLU A OE2 1 
ATOM   80    N  N   . ASN A  1 13  ? 9.170   9.353   11.759  1.00 9.77   ? 13  ASN A N   1 
ATOM   81    C  CA  . ASN A  1 13  ? 8.337   9.972   10.740  1.00 9.53   ? 13  ASN A CA  1 
ATOM   82    C  C   . ASN A  1 13  ? 8.667   11.478  10.548  1.00 9.41   ? 13  ASN A C   1 
ATOM   83    O  O   . ASN A  1 13  ? 8.258   12.084  9.597   1.00 10.69  ? 13  ASN A O   1 
ATOM   84    C  CB  . ASN A  1 13  ? 6.884   9.856   11.049  1.00 9.90   ? 13  ASN A CB  1 
ATOM   85    C  CG  . ASN A  1 13  ? 6.371   8.443   10.866  1.00 8.90   ? 13  ASN A CG  1 
ATOM   86    O  OD1 . ASN A  1 13  ? 7.074   7.573   10.386  1.00 10.17  ? 13  ASN A OD1 1 
ATOM   87    N  ND2 . ASN A  1 13  ? 5.156   8.220   11.308  1.00 9.20   ? 13  ASN A ND2 1 
ATOM   88    N  N   . SER A  1 14  ? 9.388   12.055  11.555  1.00 10.17  ? 14  SER A N   1 
ATOM   89    C  CA  . SER A  1 14  ? 9.793   13.461  11.536  1.00 10.95  ? 14  SER A CA  1 
ATOM   90    C  C   . SER A  1 14  ? 11.227  13.660  11.111  1.00 10.78  ? 14  SER A C   1 
ATOM   91    O  O   . SER A  1 14  ? 11.600  14.858  10.928  1.00 10.97  ? 14  SER A O   1 
ATOM   92    C  CB  . SER A  1 14  ? 9.614   14.042  12.964  1.00 13.05  ? 14  SER A CB  1 
ATOM   93    O  OG  . SER A  1 14  ? 8.172   14.188  13.147  1.00 19.09  ? 14  SER A OG  1 
ATOM   94    N  N   . TRP A  1 15  ? 12.036  12.621  10.924  1.00 9.67   ? 15  TRP A N   1 
ATOM   95    C  CA  . TRP A  1 15  ? 13.418  12.842  10.585  1.00 10.35  ? 15  TRP A CA  1 
ATOM   96    C  C   . TRP A  1 15  ? 13.576  13.656  9.289   1.00 9.99   ? 15  TRP A C   1 
ATOM   97    O  O   . TRP A  1 15  ? 14.555  14.458  9.196   1.00 10.55  ? 15  TRP A O   1 
ATOM   98    C  CB  . TRP A  1 15  ? 14.122  11.501  10.345  1.00 10.67  ? 15  TRP A CB  1 
ATOM   99    C  CG  . TRP A  1 15  ? 14.258  10.647  11.574  1.00 9.83   ? 15  TRP A CG  1 
ATOM   100   C  CD1 . TRP A  1 15  ? 14.046  10.976  12.897  1.00 10.66  ? 15  TRP A CD1 1 
ATOM   101   C  CD2 . TRP A  1 15  ? 14.737  9.285   11.575  1.00 10.17  ? 15  TRP A CD2 1 
ATOM   102   N  NE1 . TRP A  1 15  ? 14.322  9.913   13.736  1.00 10.50  ? 15  TRP A NE1 1 
ATOM   103   C  CE2 . TRP A  1 15  ? 14.778  8.872   12.965  1.00 9.87   ? 15  TRP A CE2 1 
ATOM   104   C  CE3 . TRP A  1 15  ? 15.129  8.416   10.595  1.00 9.70   ? 15  TRP A CE3 1 
ATOM   105   C  CZ2 . TRP A  1 15  ? 15.169  7.556   13.334  1.00 10.06  ? 15  TRP A CZ2 1 
ATOM   106   C  CZ3 . TRP A  1 15  ? 15.554  7.127   10.944  1.00 10.04  ? 15  TRP A CZ3 1 
ATOM   107   C  CH2 . TRP A  1 15  ? 15.575  6.734   12.302  1.00 9.92   ? 15  TRP A CH2 1 
ATOM   108   N  N   . SER A  1 16  ? 12.687  13.519  8.339   1.00 10.01  ? 16  SER A N   1 
ATOM   109   C  CA  . SER A  1 16  ? 12.867  14.179  7.048   1.00 10.55  ? 16  SER A CA  1 
ATOM   110   C  C   . SER A  1 16  ? 12.792  15.687  7.140   1.00 10.60  ? 16  SER A C   1 
ATOM   111   O  O   . SER A  1 16  ? 13.195  16.363  6.197   1.00 10.95  ? 16  SER A O   1 
ATOM   112   C  CB  . SER A  1 16  ? 11.809  13.673  6.097   1.00 10.62  ? 16  SER A CB  1 
ATOM   113   O  OG  . SER A  1 16  ? 10.544  14.072  6.545   1.00 12.01  ? 16  SER A OG  1 
ATOM   114   N  N   A LYS A  1 17  ? 12.234  16.250  8.195   0.50 10.91  ? 17  LYS A N   1 
ATOM   115   N  N   B LYS A  1 17  ? 12.290  16.205  8.287   0.50 10.49  ? 17  LYS A N   1 
ATOM   116   C  CA  A LYS A  1 17  ? 12.197  17.732  8.231   0.50 9.74   ? 17  LYS A CA  1 
ATOM   117   C  CA  B LYS A  1 17  ? 12.200  17.701  8.490   0.50 11.24  ? 17  LYS A CA  1 
ATOM   118   C  C   A LYS A  1 17  ? 13.672  18.247  8.173   0.50 9.70   ? 17  LYS A C   1 
ATOM   119   C  C   B LYS A  1 17  ? 13.576  18.339  8.595   0.50 9.98   ? 17  LYS A C   1 
ATOM   120   O  O   A LYS A  1 17  ? 14.027  19.053  7.366   0.50 9.75   ? 17  LYS A O   1 
ATOM   121   O  O   B LYS A  1 17  ? 13.812  19.344  7.931   0.50 9.21   ? 17  LYS A O   1 
ATOM   122   C  CB  A LYS A  1 17  ? 11.482  18.109  9.517   0.50 11.30  ? 17  LYS A CB  1 
ATOM   123   C  CB  B LYS A  1 17  ? 11.354  18.124  9.688   0.50 12.91  ? 17  LYS A CB  1 
ATOM   124   C  CG  A LYS A  1 17  ? 10.052  17.592  9.638   0.50 13.16  ? 17  LYS A CG  1 
ATOM   125   C  CG  B LYS A  1 17  ? 11.278  19.680  9.723   0.50 13.66  ? 17  LYS A CG  1 
ATOM   126   C  CD  A LYS A  1 17  ? 9.495   17.737  11.047  0.50 14.26  ? 17  LYS A CD  1 
ATOM   127   C  CD  B LYS A  1 17  ? 10.485  20.107  10.942  0.50 15.01  ? 17  LYS A CD  1 
ATOM   128   C  CE  A LYS A  1 17  ? 8.203   17.003  11.113  0.50 18.38  ? 17  LYS A CE  1 
ATOM   129   C  CE  B LYS A  1 17  ? 9.007   19.965  10.641  0.50 18.20  ? 17  LYS A CE  1 
ATOM   130   N  NZ  A LYS A  1 17  ? 7.564   17.270  12.488  0.50 20.11  ? 17  LYS A NZ  1 
ATOM   131   N  NZ  B LYS A  1 17  ? 8.254   20.263  11.857  0.50 16.55  ? 17  LYS A NZ  1 
ATOM   132   N  N   A LYS A  1 18  ? 14.520  17.729  9.068   0.50 9.99   ? 18  LYS A N   1 
ATOM   133   N  N   B LYS A  1 18  ? 14.431  17.790  9.462   0.50 9.94   ? 18  LYS A N   1 
ATOM   134   C  CA  A LYS A  1 18  ? 15.833  18.333  9.248   0.50 12.38  ? 18  LYS A CA  1 
ATOM   135   C  CA  B LYS A  1 18  ? 15.813  18.226  9.498   0.50 11.58  ? 18  LYS A CA  1 
ATOM   136   C  C   A LYS A  1 18  ? 16.859  17.478  8.542   0.50 12.23  ? 18  LYS A C   1 
ATOM   137   C  C   B LYS A  1 18  ? 16.722  17.549  8.430   0.50 11.53  ? 18  LYS A C   1 
ATOM   138   O  O   A LYS A  1 18  ? 18.048  17.885  8.462   0.50 12.10  ? 18  LYS A O   1 
ATOM   139   O  O   B LYS A  1 18  ? 17.649  18.192  7.912   0.50 12.36  ? 18  LYS A O   1 
ATOM   140   C  CB  A LYS A  1 18  ? 16.221  18.378  10.737  0.50 13.68  ? 18  LYS A CB  1 
ATOM   141   C  CB  B LYS A  1 18  ? 16.338  18.025  10.911  0.50 12.83  ? 18  LYS A CB  1 
ATOM   142   C  CG  A LYS A  1 18  ? 15.543  19.396  11.639  0.50 22.04  ? 18  LYS A CG  1 
ATOM   143   C  CG  B LYS A  1 18  ? 17.741  18.514  11.052  0.50 15.33  ? 18  LYS A CG  1 
ATOM   144   C  CD  A LYS A  1 18  ? 16.145  20.761  11.389  0.50 22.26  ? 18  LYS A CD  1 
ATOM   145   C  CE  A LYS A  1 18  ? 15.582  21.839  12.292  0.50 22.94  ? 18  LYS A CE  1 
ATOM   146   N  NZ  A LYS A  1 18  ? 16.473  22.995  12.472  0.50 29.19  ? 18  LYS A NZ  1 
ATOM   147   N  N   . TYR A  1 19  ? 16.421  16.302  8.080   1.00 11.74  ? 19  TYR A N   1 
ATOM   148   C  CA  . TYR A  1 19  ? 17.316  15.408  7.355   1.00 11.40  ? 19  TYR A CA  1 
ATOM   149   C  C   . TYR A  1 19  ? 16.628  14.975  6.079   1.00 11.00  ? 19  TYR A C   1 
ATOM   150   O  O   . TYR A  1 19  ? 15.990  13.924  6.036   1.00 10.86  ? 19  TYR A O   1 
ATOM   151   C  CB  . TYR A  1 19  ? 17.727  14.205  8.208   1.00 11.64  ? 19  TYR A CB  1 
ATOM   152   C  CG  . TYR A  1 19  ? 18.388  14.593  9.496   1.00 12.21  ? 19  TYR A CG  1 
ATOM   153   C  CD1 . TYR A  1 19  ? 19.761  14.938  9.520   1.00 13.74  ? 19  TYR A CD1 1 
ATOM   154   C  CD2 . TYR A  1 19  ? 17.677  14.625  10.693  1.00 13.28  ? 19  TYR A CD2 1 
ATOM   155   C  CE1 . TYR A  1 19  ? 20.375  15.232  10.732  1.00 16.65  ? 19  TYR A CE1 1 
ATOM   156   C  CE2 . TYR A  1 19  ? 18.283  14.932  11.901  1.00 15.48  ? 19  TYR A CE2 1 
ATOM   157   C  CZ  . TYR A  1 19  ? 19.647  15.225  11.913  1.00 18.37  ? 19  TYR A CZ  1 
ATOM   158   O  OH  . TYR A  1 19  ? 20.258  15.525  13.101  1.00 19.93  ? 19  TYR A OH  1 
ATOM   159   N  N   A PRO A  1 20  ? 16.631  15.852  5.074   0.50 12.50  ? 20  PRO A N   1 
ATOM   160   N  N   B PRO A  1 20  ? 16.684  15.778  4.975   0.50 12.72  ? 20  PRO A N   1 
ATOM   161   C  CA  A PRO A  1 20  ? 15.784  15.548  3.970   0.50 12.34  ? 20  PRO A CA  1 
ATOM   162   C  CA  B PRO A  1 20  ? 15.835  15.540  3.799   0.50 12.47  ? 20  PRO A CA  1 
ATOM   163   C  C   A PRO A  1 20  ? 16.007  14.197  3.303   0.50 10.24  ? 20  PRO A C   1 
ATOM   164   C  C   B PRO A  1 20  ? 16.052  14.189  3.132   0.50 11.68  ? 20  PRO A C   1 
ATOM   165   O  O   A PRO A  1 20  ? 15.045  13.692  2.723   0.50 10.29  ? 20  PRO A O   1 
ATOM   166   O  O   B PRO A  1 20  ? 15.153  13.635  2.450   0.50 12.41  ? 20  PRO A O   1 
ATOM   167   C  CB  A PRO A  1 20  ? 16.052  16.691  2.989   0.50 10.66  ? 20  PRO A CB  1 
ATOM   168   C  CB  B PRO A  1 20  ? 16.204  16.695  2.843   0.50 17.49  ? 20  PRO A CB  1 
ATOM   169   C  CG  A PRO A  1 20  ? 16.592  17.787  3.810   0.50 11.63  ? 20  PRO A CG  1 
ATOM   170   C  CG  B PRO A  1 20  ? 17.505  17.145  3.327   0.50 16.42  ? 20  PRO A CG  1 
ATOM   171   C  CD  A PRO A  1 20  ? 17.312  17.173  4.964   0.50 11.52  ? 20  PRO A CD  1 
ATOM   172   C  CD  B PRO A  1 20  ? 17.597  16.936  4.791   0.50 12.42  ? 20  PRO A CD  1 
ATOM   173   N  N   . SER A  1 21  ? 17.247  13.625  3.296   1.00 10.57  ? 21  SER A N   1 
ATOM   174   C  CA  . SER A  1 21  ? 17.435  12.355  2.649   1.00 11.63  ? 21  SER A CA  1 
ATOM   175   C  C   . SER A  1 21  ? 16.604  11.221  3.281   1.00 9.89   ? 21  SER A C   1 
ATOM   176   O  O   . SER A  1 21  ? 16.367  10.205  2.642   1.00 9.99   ? 21  SER A O   1 
ATOM   177   C  CB  . SER A  1 21  ? 18.927  11.905  2.679   1.00 11.62  ? 21  SER A CB  1 
ATOM   178   O  OG  . SER A  1 21  ? 19.664  12.764  1.785   1.00 13.90  ? 21  SER A OG  1 
ATOM   179   N  N   . CYS A  1 22  ? 16.118  11.445  4.514   1.00 10.34  ? 22  CYS A N   1 
ATOM   180   C  CA  . CYS A  1 22  ? 15.279  10.434  5.142   1.00 9.87   ? 22  CYS A CA  1 
ATOM   181   C  C   . CYS A  1 22  ? 13.944  10.267  4.461   1.00 9.89   ? 22  CYS A C   1 
ATOM   182   O  O   . CYS A  1 22  ? 13.293  9.252   4.710   1.00 10.29  ? 22  CYS A O   1 
ATOM   183   C  CB  . CYS A  1 22  ? 15.118  10.728  6.621   1.00 11.10  ? 22  CYS A CB  1 
ATOM   184   S  SG  . CYS A  1 22  ? 16.639  10.800  7.597   1.00 10.97  ? 22  CYS A SG  1 
ATOM   185   N  N   . GLY A  1 23  ? 13.560  11.227  3.603   1.00 10.73  ? 23  GLY A N   1 
ATOM   186   C  CA  . GLY A  1 23  ? 12.397  11.096  2.783   1.00 10.76  ? 23  GLY A CA  1 
ATOM   187   C  C   . GLY A  1 23  ? 12.694  10.923  1.301   1.00 11.06  ? 23  GLY A C   1 
ATOM   188   O  O   . GLY A  1 23  ? 11.796  11.019  0.453   1.00 11.73  ? 23  GLY A O   1 
ATOM   189   N  N   . GLY A  1 24  ? 13.937  10.582  0.963   1.00 11.99  ? 24  GLY A N   1 
ATOM   190   C  CA  . GLY A  1 24  ? 14.367  10.436  -0.413  1.00 12.86  ? 24  GLY A CA  1 
ATOM   191   C  C   . GLY A  1 24  ? 14.465  9.011   -0.849  1.00 12.65  ? 24  GLY A C   1 
ATOM   192   O  O   . GLY A  1 24  ? 13.800  8.115   -0.299  1.00 14.09  ? 24  GLY A O   1 
ATOM   193   N  N   . LEU A  1 25  ? 15.277  8.790   -1.881  1.00 13.44  ? 25  LEU A N   1 
ATOM   194   C  CA  . LEU A  1 25  ? 15.413  7.498   -2.510  1.00 14.97  ? 25  LEU A CA  1 
ATOM   195   C  C   . LEU A  1 25  ? 16.323  6.570   -1.692  1.00 12.51  ? 25  LEU A C   1 
ATOM   196   O  O   . LEU A  1 25  ? 17.081  6.987   -0.831  1.00 12.34  ? 25  LEU A O   1 
ATOM   197   C  CB  . LEU A  1 25  ? 16.010  7.657   -3.926  1.00 18.78  ? 25  LEU A CB  1 
ATOM   198   C  CG  . LEU A  1 25  ? 15.232  8.557   -4.869  1.00 21.69  ? 25  LEU A CG  1 
ATOM   199   C  CD1 . LEU A  1 25  ? 15.995  8.745   -6.159  1.00 27.84  ? 25  LEU A CD1 1 
ATOM   200   C  CD2 . LEU A  1 25  ? 13.848  7.981   -5.082  1.00 28.94  ? 25  LEU A CD2 1 
ATOM   201   N  N   . LEU A  1 26  ? 16.194  5.288   -2.016  1.00 13.94  ? 26  LEU A N   1 
ATOM   202   C  CA  . LEU A  1 26  ? 17.093  4.205   -1.606  1.00 13.59  ? 26  LEU A CA  1 
ATOM   203   C  C   . LEU A  1 26  ? 17.111  4.023   -0.083  1.00 10.92  ? 26  LEU A C   1 
ATOM   204   O  O   . LEU A  1 26  ? 18.152  3.632   0.455   1.00 12.56  ? 26  LEU A O   1 
ATOM   205   C  CB  . LEU A  1 26  ? 18.574  4.470   -2.153  1.00 15.29  ? 26  LEU A CB  1 
ATOM   206   C  CG  . LEU A  1 26  ? 18.777  4.408   -3.653  1.00 22.40  ? 26  LEU A CG  1 
ATOM   207   C  CD1 . LEU A  1 26  ? 20.288  4.313   -3.861  1.00 25.72  ? 26  LEU A CD1 1 
ATOM   208   C  CD2 . LEU A  1 26  ? 17.993  3.358   -4.391  1.00 23.33  ? 26  LEU A CD2 1 
ATOM   209   N  N   . GLN A  1 27  ? 15.982  4.217   0.568   1.00 10.55  ? 27  GLN A N   1 
ATOM   210   C  CA  . GLN A  1 27  ? 16.020  4.141   2.035   1.00 8.18   ? 27  GLN A CA  1 
ATOM   211   C  C   . GLN A  1 27  ? 16.043  2.695   2.553   1.00 8.67   ? 27  GLN A C   1 
ATOM   212   O  O   . GLN A  1 27  ? 15.404  1.800   2.024   1.00 11.10  ? 27  GLN A O   1 
ATOM   213   C  CB  . GLN A  1 27  ? 14.846  4.865   2.629   1.00 9.13   ? 27  GLN A CB  1 
ATOM   214   C  CG  . GLN A  1 27  ? 14.919  6.351   2.333   1.00 9.96   ? 27  GLN A CG  1 
ATOM   215   C  CD  . GLN A  1 27  ? 16.084  6.978   3.068   1.00 9.45   ? 27  GLN A CD  1 
ATOM   216   O  OE1 . GLN A  1 27  ? 16.055  7.173   4.286   1.00 9.26   ? 27  GLN A OE1 1 
ATOM   217   N  NE2 . GLN A  1 27  ? 17.155  7.261   2.306   1.00 9.79   ? 27  GLN A NE2 1 
ATOM   218   N  N   . SER A  1 28  ? 16.786  2.516   3.626   1.00 7.93   ? 28  SER A N   1 
ATOM   219   C  CA  . SER A  1 28  ? 16.915  1.280   4.373   1.00 7.48   ? 28  SER A CA  1 
ATOM   220   C  C   . SER A  1 28  ? 16.321  1.505   5.773   1.00 7.90   ? 28  SER A C   1 
ATOM   221   O  O   . SER A  1 28  ? 16.227  2.623   6.275   1.00 8.25   ? 28  SER A O   1 
ATOM   222   C  CB  . SER A  1 28  ? 18.386  0.988   4.515   1.00 8.65   ? 28  SER A CB  1 
ATOM   223   O  OG  . SER A  1 28  ? 18.945  0.667   3.242   1.00 8.61   ? 28  SER A OG  1 
ATOM   224   N  N   . PRO A  1 29  ? 15.996  0.388   6.481   1.00 7.67   ? 29  PRO A N   1 
ATOM   225   C  CA  . PRO A  1 29  ? 16.081  -1.009  6.109   1.00 7.66   ? 29  PRO A CA  1 
ATOM   226   C  C   . PRO A  1 29  ? 14.865  -1.436  5.274   1.00 7.46   ? 29  PRO A C   1 
ATOM   227   O  O   . PRO A  1 29  ? 13.943  -0.657  5.061   1.00 8.24   ? 29  PRO A O   1 
ATOM   228   C  CB  . PRO A  1 29  ? 16.110  -1.702  7.489   1.00 8.34   ? 29  PRO A CB  1 
ATOM   229   C  CG  . PRO A  1 29  ? 15.124  -0.857  8.302   1.00 8.11   ? 29  PRO A CG  1 
ATOM   230   C  CD  . PRO A  1 29  ? 15.428  0.553   7.849   1.00 8.10   ? 29  PRO A CD  1 
ATOM   231   N  N   . ILE A  1 30  ? 14.879  -2.685  4.854   1.00 8.42   ? 30  ILE A N   1 
ATOM   232   C  CA  . ILE A  1 30  ? 13.855  -3.258  4.002   1.00 8.43   ? 30  ILE A CA  1 
ATOM   233   C  C   . ILE A  1 30  ? 13.546  -4.683  4.473   1.00 8.35   ? 30  ILE A C   1 
ATOM   234   O  O   . ILE A  1 30  ? 14.337  -5.310  5.213   1.00 9.25   ? 30  ILE A O   1 
ATOM   235   C  CB  . ILE A  1 30  ? 14.276  -3.243  2.532   1.00 9.38   ? 30  ILE A CB  1 
ATOM   236   C  CG1 . ILE A  1 30  ? 15.512  -4.150  2.276   1.00 10.20  ? 30  ILE A CG1 1 
ATOM   237   C  CG2 . ILE A  1 30  ? 14.497  -1.812  2.080   1.00 11.67  ? 30  ILE A CG2 1 
ATOM   238   C  CD1 . ILE A  1 30  ? 15.823  -4.392  0.811   1.00 12.75  ? 30  ILE A CD1 1 
ATOM   239   N  N   . ASP A  1 31  ? 12.412  -5.166  4.029   1.00 9.38   ? 31  ASP A N   1 
ATOM   240   C  CA  . ASP A  1 31  ? 12.062  -6.560  4.190   1.00 9.46   ? 31  ASP A CA  1 
ATOM   241   C  C   . ASP A  1 31  ? 12.662  -7.359  3.069   1.00 9.23   ? 31  ASP A C   1 
ATOM   242   O  O   . ASP A  1 31  ? 12.462  -7.096  1.876   1.00 13.41  ? 31  ASP A O   1 
ATOM   243   C  CB  . ASP A  1 31  ? 10.534  -6.695  4.173   1.00 11.61  ? 31  ASP A CB  1 
ATOM   244   C  CG  . ASP A  1 31  ? 10.057  -8.131  4.374   1.00 11.80  ? 31  ASP A CG  1 
ATOM   245   O  OD1 . ASP A  1 31  ? 10.641  -8.835  5.217   1.00 10.69  ? 31  ASP A OD1 1 
ATOM   246   O  OD2 . ASP A  1 31  ? 9.150   -8.531  3.684   1.00 17.03  ? 31  ASP A OD2 1 
ATOM   247   N  N   . LEU A  1 32  ? 13.369  -8.381  3.440   1.00 10.13  ? 32  LEU A N   1 
ATOM   248   C  CA  . LEU A  1 32  ? 14.042  -9.290  2.491   1.00 10.79  ? 32  LEU A CA  1 
ATOM   249   C  C   . LEU A  1 32  ? 13.125  -10.480 2.249   1.00 13.07  ? 32  LEU A C   1 
ATOM   250   O  O   . LEU A  1 32  ? 12.945  -11.341 3.110   1.00 13.60  ? 32  LEU A O   1 
ATOM   251   C  CB  . LEU A  1 32  ? 15.348  -9.755  3.104   1.00 11.81  ? 32  LEU A CB  1 
ATOM   252   C  CG  . LEU A  1 32  ? 16.300  -8.624  3.496   1.00 10.84  ? 32  LEU A CG  1 
ATOM   253   C  CD1 . LEU A  1 32  ? 17.464  -9.085  4.348   1.00 12.72  ? 32  LEU A CD1 1 
ATOM   254   C  CD2 . LEU A  1 32  ? 16.847  -7.860  2.316   1.00 13.62  ? 32  LEU A CD2 1 
ATOM   255   N  N   . HIS A  1 33  ? 12.408  -10.506 1.161   1.00 20.41  ? 33  HIS A N   1 
ATOM   256   C  CA  . HIS A  1 33  ? 11.454  -11.629 0.985   1.00 22.92  ? 33  HIS A CA  1 
ATOM   257   C  C   . HIS A  1 33  ? 11.569  -12.177 -0.365  1.00 22.91  ? 33  HIS A C   1 
ATOM   258   O  O   . HIS A  1 33  ? 12.114  -11.515 -1.235  1.00 20.68  ? 33  HIS A O   1 
ATOM   259   C  CB  . HIS A  1 33  ? 10.088  -11.128 1.297   1.00 20.88  ? 33  HIS A CB  1 
ATOM   260   C  CG  . HIS A  1 33  ? 9.641   -10.078 0.324   1.00 21.21  ? 33  HIS A CG  1 
ATOM   261   N  ND1 . HIS A  1 33  ? 9.894   -8.769  0.442   1.00 29.37  ? 33  HIS A ND1 1 
ATOM   262   C  CD2 . HIS A  1 33  ? 8.871   -10.231 -0.833  1.00 29.38  ? 33  HIS A CD2 1 
ATOM   263   C  CE1 . HIS A  1 33  ? 9.291   -8.112  -0.615  1.00 35.15  ? 33  HIS A CE1 1 
ATOM   264   N  NE2 . HIS A  1 33  ? 8.696   -9.019  -1.377  1.00 38.49  ? 33  HIS A NE2 1 
ATOM   265   N  N   . SER A  1 34  ? 11.032  -13.394 -0.539  1.00 23.33  ? 34  SER A N   1 
ATOM   266   C  CA  . SER A  1 34  ? 11.436  -14.240 -1.667  1.00 33.44  ? 34  SER A CA  1 
ATOM   267   C  C   . SER A  1 34  ? 11.177  -13.592 -3.028  1.00 31.92  ? 34  SER A C   1 
ATOM   268   O  O   . SER A  1 34  ? 12.028  -13.722 -3.911  1.00 35.13  ? 34  SER A O   1 
ATOM   269   C  CB  . SER A  1 34  ? 10.843  -15.672 -1.559  1.00 47.13  ? 34  SER A CB  1 
ATOM   270   O  OG  . SER A  1 34  ? 9.476   -15.652 -1.858  1.00 49.87  ? 34  SER A OG  1 
ATOM   271   N  N   . ASP A  1 35  ? 10.047  -12.858 -3.178  1.00 28.02  ? 35  ASP A N   1 
ATOM   272   C  CA  . ASP A  1 35  ? 9.643   -12.234 -4.440  1.00 30.05  ? 35  ASP A CA  1 
ATOM   273   C  C   . ASP A  1 35  ? 10.630  -11.260 -5.014  1.00 28.65  ? 35  ASP A C   1 
ATOM   274   O  O   . ASP A  1 35  ? 10.567  -10.964 -6.187  1.00 35.33  ? 35  ASP A O   1 
ATOM   275   C  CB  . ASP A  1 35  ? 8.234   -11.593 -4.310  1.00 38.32  ? 35  ASP A CB  1 
ATOM   276   N  N   . ILE A  1 36  ? 11.550  -10.741 -4.210  1.00 23.26  ? 36  ILE A N   1 
ATOM   277   C  CA  . ILE A  1 36  ? 12.454  -9.688  -4.657  1.00 21.05  ? 36  ILE A CA  1 
ATOM   278   C  C   . ILE A  1 36  ? 13.885  -10.160 -4.599  1.00 20.48  ? 36  ILE A C   1 
ATOM   279   O  O   . ILE A  1 36  ? 14.802  -9.361  -4.793  1.00 22.86  ? 36  ILE A O   1 
ATOM   280   C  CB  . ILE A  1 36  ? 12.255  -8.371  -3.874  1.00 21.69  ? 36  ILE A CB  1 
ATOM   281   C  CG1 . ILE A  1 36  ? 12.609  -8.682  -2.400  1.00 23.44  ? 36  ILE A CG1 1 
ATOM   282   C  CG2 . ILE A  1 36  ? 10.908  -7.720  -4.200  1.00 24.45  ? 36  ILE A CG2 1 
ATOM   283   C  CD1 . ILE A  1 36  ? 12.899  -7.476  -1.603  1.00 26.89  ? 36  ILE A CD1 1 
ATOM   284   N  N   . LEU A  1 37  ? 14.106  -11.440 -4.318  1.00 20.88  ? 37  LEU A N   1 
ATOM   285   C  CA  . LEU A  1 37  ? 15.497  -12.008 -4.219  1.00 20.03  ? 37  LEU A CA  1 
ATOM   286   C  C   . LEU A  1 37  ? 15.917  -12.533 -5.562  1.00 23.08  ? 37  LEU A C   1 
ATOM   287   O  O   . LEU A  1 37  ? 15.120  -13.182 -6.282  1.00 28.20  ? 37  LEU A O   1 
ATOM   288   C  CB  . LEU A  1 37  ? 15.565  -13.140 -3.221  1.00 21.76  ? 37  LEU A CB  1 
ATOM   289   C  CG  . LEU A  1 37  ? 15.129  -12.798 -1.792  1.00 22.25  ? 37  LEU A CG  1 
ATOM   290   C  CD1 . LEU A  1 37  ? 15.312  -14.018 -0.878  1.00 28.24  ? 37  LEU A CD1 1 
ATOM   291   C  CD2 . LEU A  1 37  ? 15.943  -11.639 -1.200  1.00 18.74  ? 37  LEU A CD2 1 
ATOM   292   N  N   . GLN A  1 38  ? 17.173  -12.316 -5.901  1.00 21.82  ? 38  GLN A N   1 
ATOM   293   C  CA  . GLN A  1 38  ? 17.656  -12.824 -7.173  1.00 21.59  ? 38  GLN A CA  1 
ATOM   294   C  C   . GLN A  1 38  ? 19.079  -13.266 -6.966  1.00 18.45  ? 38  GLN A C   1 
ATOM   295   O  O   . GLN A  1 38  ? 19.917  -12.478 -6.547  1.00 19.01  ? 38  GLN A O   1 
ATOM   296   C  CB  . GLN A  1 38  ? 17.601  -11.778 -8.274  1.00 26.53  ? 38  GLN A CB  1 
ATOM   297   C  CG  . GLN A  1 38  ? 17.970  -12.366 -9.648  1.00 31.39  ? 38  GLN A CG  1 
ATOM   298   C  CD  . GLN A  1 38  ? 17.761  -11.373 -10.737 1.00 30.55  ? 38  GLN A CD  1 
ATOM   299   O  OE1 . GLN A  1 38  ? 16.612  -11.132 -11.146 1.00 43.42  ? 38  GLN A OE1 1 
ATOM   300   N  NE2 . GLN A  1 38  ? 18.847  -10.759 -11.200 1.00 32.13  ? 38  GLN A NE2 1 
ATOM   301   N  N   . TYR A  1 39  ? 19.338  -14.534 -7.193  1.00 21.52  ? 39  TYR A N   1 
ATOM   302   C  CA  . TYR A  1 39  ? 20.692  -15.068 -7.129  1.00 20.56  ? 39  TYR A CA  1 
ATOM   303   C  C   . TYR A  1 39  ? 21.542  -14.336 -8.164  1.00 20.24  ? 39  TYR A C   1 
ATOM   304   O  O   . TYR A  1 39  ? 21.119  -14.074 -9.330  1.00 21.84  ? 39  TYR A O   1 
ATOM   305   C  CB  . TYR A  1 39  ? 20.691  -16.593 -7.430  1.00 19.33  ? 39  TYR A CB  1 
ATOM   306   C  CG  . TYR A  1 39  ? 22.079  -17.224 -7.517  1.00 20.82  ? 39  TYR A CG  1 
ATOM   307   C  CD1 . TYR A  1 39  ? 22.984  -17.152 -6.449  1.00 19.82  ? 39  TYR A CD1 1 
ATOM   308   C  CD2 . TYR A  1 39  ? 22.481  -17.860 -8.677  1.00 22.98  ? 39  TYR A CD2 1 
ATOM   309   C  CE1 . TYR A  1 39  ? 24.202  -17.747 -6.477  1.00 24.66  ? 39  TYR A CE1 1 
ATOM   310   C  CE2 . TYR A  1 39  ? 23.732  -18.465 -8.741  1.00 30.70  ? 39  TYR A CE2 1 
ATOM   311   C  CZ  . TYR A  1 39  ? 24.568  -18.448 -7.615  1.00 24.88  ? 39  TYR A CZ  1 
ATOM   312   O  OH  . TYR A  1 39  ? 25.843  -18.993 -7.641  1.00 36.39  ? 39  TYR A OH  1 
ATOM   313   N  N   . ASP A  1 40  ? 22.747  -14.005 -7.723  1.00 18.04  ? 40  ASP A N   1 
ATOM   314   C  CA  . ASP A  1 40  ? 23.712  -13.344 -8.567  1.00 19.27  ? 40  ASP A CA  1 
ATOM   315   C  C   . ASP A  1 40  ? 25.017  -14.057 -8.320  1.00 20.24  ? 40  ASP A C   1 
ATOM   316   O  O   . ASP A  1 40  ? 25.657  -13.912 -7.255  1.00 19.08  ? 40  ASP A O   1 
ATOM   317   C  CB  . ASP A  1 40  ? 23.748  -11.836 -8.305  1.00 22.16  ? 40  ASP A CB  1 
ATOM   318   C  CG  . ASP A  1 40  ? 24.731  -11.106 -9.166  1.00 28.20  ? 40  ASP A CG  1 
ATOM   319   O  OD1 . ASP A  1 40  ? 25.597  -11.718 -9.759  1.00 27.25  ? 40  ASP A OD1 1 
ATOM   320   O  OD2 . ASP A  1 40  ? 24.687  -9.874  -9.204  1.00 39.63  ? 40  ASP A OD2 1 
ATOM   321   N  N   . ALA A  1 41  ? 25.380  -14.924 -9.279  1.00 25.22  ? 41  ALA A N   1 
ATOM   322   C  CA  . ALA A  1 41  ? 26.620  -15.700 -9.175  1.00 26.92  ? 41  ALA A CA  1 
ATOM   323   C  C   . ALA A  1 41  ? 27.863  -14.796 -9.035  1.00 24.86  ? 41  ALA A C   1 
ATOM   324   O  O   . ALA A  1 41  ? 28.930  -15.253 -8.668  1.00 34.44  ? 41  ALA A O   1 
ATOM   325   C  CB  . ALA A  1 41  ? 26.788  -16.569 -10.418 1.00 37.15  ? 41  ALA A CB  1 
ATOM   326   N  N   . SER A  1 42  ? 27.753  -13.517 -9.411  1.00 26.85  ? 42  SER A N   1 
ATOM   327   C  CA  . SER A  1 42  ? 28.883  -12.616 -9.264  1.00 29.98  ? 42  SER A CA  1 
ATOM   328   C  C   . SER A  1 42  ? 29.271  -12.210 -7.840  1.00 34.18  ? 42  SER A C   1 
ATOM   329   O  O   . SER A  1 42  ? 30.365  -11.694 -7.619  1.00 40.11  ? 42  SER A O   1 
ATOM   330   C  CB  . SER A  1 42  ? 28.727  -11.432 -10.184 1.00 33.21  ? 42  SER A CB  1 
ATOM   331   O  OG  . SER A  1 42  ? 27.945  -10.382 -9.638  1.00 40.55  ? 42  SER A OG  1 
ATOM   332   N  N   . LEU A  1 43  ? 28.400  -12.495 -6.890  1.00 21.85  ? 43  LEU A N   1 
ATOM   333   C  CA  . LEU A  1 43  ? 28.605  -12.124 -5.440  1.00 21.21  ? 43  LEU A CA  1 
ATOM   334   C  C   . LEU A  1 43  ? 29.473  -13.163 -4.652  1.00 19.24  ? 43  LEU A C   1 
ATOM   335   O  O   . LEU A  1 43  ? 29.019  -14.145 -4.028  1.00 22.14  ? 43  LEU A O   1 
ATOM   336   C  CB  . LEU A  1 43  ? 27.269  -11.999 -4.793  1.00 16.83  ? 43  LEU A CB  1 
ATOM   337   C  CG  . LEU A  1 43  ? 26.399  -10.900 -5.363  1.00 16.01  ? 43  LEU A CG  1 
ATOM   338   C  CD1 . LEU A  1 43  ? 25.038  -10.929 -4.669  1.00 15.42  ? 43  LEU A CD1 1 
ATOM   339   C  CD2 . LEU A  1 43  ? 26.992  -9.534  -5.182  1.00 17.94  ? 43  LEU A CD2 1 
ATOM   340   N  N   . THR A  1 44  ? 30.759  -12.913 -4.715  1.00 20.54  ? 44  THR A N   1 
ATOM   341   C  CA  . THR A  1 44  ? 31.765  -13.812 -4.194  1.00 22.00  ? 44  THR A CA  1 
ATOM   342   C  C   . THR A  1 44  ? 32.005  -13.467 -2.716  1.00 20.10  ? 44  THR A C   1 
ATOM   343   O  O   . THR A  1 44  ? 31.527  -12.457 -2.210  1.00 18.21  ? 44  THR A O   1 
ATOM   344   C  CB  . THR A  1 44  ? 33.074  -13.666 -4.963  1.00 29.72  ? 44  THR A CB  1 
ATOM   345   O  OG1 . THR A  1 44  ? 33.419  -12.284 -4.977  1.00 30.27  ? 44  THR A OG1 1 
ATOM   346   C  CG2 . THR A  1 44  ? 32.928  -14.216 -6.382  1.00 41.88  ? 44  THR A CG2 1 
ATOM   347   N  N   A PRO A  1 45  ? 32.655  -14.370 -1.987  0.50 20.79  ? 45  PRO A N   1 
ATOM   348   N  N   B PRO A  1 45  ? 32.786  -14.305 -2.014  0.50 21.18  ? 45  PRO A N   1 
ATOM   349   C  CA  A PRO A  1 45  ? 32.824  -14.067 -0.582  0.50 17.86  ? 45  PRO A CA  1 
ATOM   350   C  CA  B PRO A  1 45  ? 32.982  -14.182 -0.562  0.50 17.61  ? 45  PRO A CA  1 
ATOM   351   C  C   A PRO A  1 45  ? 33.705  -12.839 -0.377  0.50 15.44  ? 45  PRO A C   1 
ATOM   352   C  C   B PRO A  1 45  ? 33.844  -12.972 -0.223  0.50 17.94  ? 45  PRO A C   1 
ATOM   353   O  O   A PRO A  1 45  ? 34.661  -12.571 -1.098  0.50 16.63  ? 45  PRO A O   1 
ATOM   354   O  O   B PRO A  1 45  ? 34.968  -12.845 -0.735  0.50 18.78  ? 45  PRO A O   1 
ATOM   355   C  CB  A PRO A  1 45  ? 33.496  -15.334 -0.032  0.50 21.31  ? 45  PRO A CB  1 
ATOM   356   C  CB  B PRO A  1 45  ? 33.764  -15.465 -0.209  0.50 21.40  ? 45  PRO A CB  1 
ATOM   357   C  CG  A PRO A  1 45  ? 33.056  -16.439 -0.997  0.50 20.04  ? 45  PRO A CG  1 
ATOM   358   C  CG  B PRO A  1 45  ? 33.540  -16.407 -1.385  0.50 26.36  ? 45  PRO A CG  1 
ATOM   359   C  CD  A PRO A  1 45  ? 33.058  -15.752 -2.332  0.50 21.18  ? 45  PRO A CD  1 
ATOM   360   C  CD  B PRO A  1 45  ? 33.490  -15.482 -2.571  0.50 22.89  ? 45  PRO A CD  1 
ATOM   361   N  N   . LEU A  1 46  ? 33.332  -12.094 0.649   1.00 15.09  ? 46  LEU A N   1 
ATOM   362   C  CA  . LEU A  1 46  ? 34.137  -11.004 1.160   1.00 13.79  ? 46  LEU A CA  1 
ATOM   363   C  C   . LEU A  1 46  ? 35.298  -11.551 1.949   1.00 14.48  ? 46  LEU A C   1 
ATOM   364   O  O   . LEU A  1 46  ? 35.192  -12.597 2.600   1.00 17.20  ? 46  LEU A O   1 
ATOM   365   C  CB  . LEU A  1 46  ? 33.331  -10.047 2.001   1.00 14.65  ? 46  LEU A CB  1 
ATOM   366   C  CG  . LEU A  1 46  ? 32.210  -9.299  1.280   1.00 17.08  ? 46  LEU A CG  1 
ATOM   367   C  CD1 . LEU A  1 46  ? 31.406  -8.515  2.274   1.00 18.62  ? 46  LEU A CD1 1 
ATOM   368   C  CD2 . LEU A  1 46  ? 32.793  -8.385  0.198   1.00 20.90  ? 46  LEU A CD2 1 
ATOM   369   N  N   . GLU A  1 47  ? 36.384  -10.775 1.995   1.00 14.80  ? 47  GLU A N   1 
ATOM   370   C  CA  . GLU A  1 47  ? 37.509  -11.114 2.830   1.00 15.19  ? 47  GLU A CA  1 
ATOM   371   C  C   . GLU A  1 47  ? 37.632  -10.058 3.911   1.00 15.18  ? 47  GLU A C   1 
ATOM   372   O  O   . GLU A  1 47  ? 37.521  -8.853  3.660   1.00 16.74  ? 47  GLU A O   1 
ATOM   373   C  CB  . GLU A  1 47  ? 38.801  -11.149 2.005   1.00 20.63  ? 47  GLU A CB  1 
ATOM   374   C  CG  . GLU A  1 47  ? 38.774  -12.178 0.904   1.00 31.41  ? 47  GLU A CG  1 
ATOM   375   C  CD  . GLU A  1 47  ? 40.029  -12.069 0.028   1.00 40.14  ? 47  GLU A CD  1 
ATOM   376   O  OE1 . GLU A  1 47  ? 39.881  -11.955 -1.208  1.00 65.38  ? 47  GLU A OE1 1 
ATOM   377   O  OE2 . GLU A  1 47  ? 41.134  -12.059 0.603   1.00 58.41  ? 47  GLU A OE2 1 
ATOM   378   N  N   . PHE A  1 48  ? 37.775  -10.502 5.156   1.00 14.83  ? 48  PHE A N   1 
ATOM   379   C  CA  . PHE A  1 48  ? 37.767  -9.597  6.297   1.00 13.88  ? 48  PHE A CA  1 
ATOM   380   C  C   . PHE A  1 48  ? 39.200  -9.443  6.750   1.00 14.61  ? 48  PHE A C   1 
ATOM   381   O  O   . PHE A  1 48  ? 39.787  -10.398 7.246   1.00 19.05  ? 48  PHE A O   1 
ATOM   382   C  CB  . PHE A  1 48  ? 36.844  -10.184 7.399   1.00 15.65  ? 48  PHE A CB  1 
ATOM   383   C  CG  . PHE A  1 48  ? 35.515  -10.568 6.870   1.00 12.59  ? 48  PHE A CG  1 
ATOM   384   C  CD1 . PHE A  1 48  ? 34.624  -9.581  6.508   1.00 13.76  ? 48  PHE A CD1 1 
ATOM   385   C  CD2 . PHE A  1 48  ? 35.192  -11.916 6.684   1.00 15.81  ? 48  PHE A CD2 1 
ATOM   386   C  CE1 . PHE A  1 48  ? 33.373  -9.952  5.937   1.00 14.13  ? 48  PHE A CE1 1 
ATOM   387   C  CE2 . PHE A  1 48  ? 33.990  -12.257 6.109   1.00 16.22  ? 48  PHE A CE2 1 
ATOM   388   C  CZ  . PHE A  1 48  ? 33.062  -11.252 5.736   1.00 15.75  ? 48  PHE A CZ  1 
ATOM   389   N  N   . GLN A  1 49  ? 39.786  -8.280  6.536   1.00 14.95  ? 49  GLN A N   1 
ATOM   390   C  CA  . GLN A  1 49  ? 41.224  -8.088  6.743   1.00 14.57  ? 49  GLN A CA  1 
ATOM   391   C  C   . GLN A  1 49  ? 41.450  -7.202  7.919   1.00 12.59  ? 49  GLN A C   1 
ATOM   392   O  O   . GLN A  1 49  ? 40.765  -6.190  8.078   1.00 12.72  ? 49  GLN A O   1 
ATOM   393   C  CB  . GLN A  1 49  ? 41.769  -7.359  5.510   1.00 16.36  ? 49  GLN A CB  1 
ATOM   394   C  CG  . GLN A  1 49  ? 41.687  -8.193  4.263   1.00 20.53  ? 49  GLN A CG  1 
ATOM   395   C  CD  . GLN A  1 49  ? 42.943  -8.939  4.011   1.00 41.67  ? 49  GLN A CD  1 
ATOM   396   O  OE1 . GLN A  1 49  ? 43.832  -9.020  4.891   1.00 44.48  ? 49  GLN A OE1 1 
ATOM   397   N  NE2 . GLN A  1 49  ? 43.061  -9.490  2.816   1.00 38.38  ? 49  GLN A NE2 1 
ATOM   398   N  N   . GLY A  1 50  ? 42.390  -7.531  8.760   1.00 13.76  ? 50  GLY A N   1 
ATOM   399   C  CA  . GLY A  1 50  ? 42.680  -6.692  9.890   1.00 14.19  ? 50  GLY A CA  1 
ATOM   400   C  C   . GLY A  1 50  ? 41.573  -6.762  10.947  1.00 14.31  ? 50  GLY A C   1 
ATOM   401   O  O   . GLY A  1 50  ? 41.507  -5.858  11.793  1.00 14.81  ? 50  GLY A O   1 
ATOM   402   N  N   . TYR A  1 51  ? 40.689  -7.753  10.886  1.00 13.06  ? 51  TYR A N   1 
ATOM   403   C  CA  . TYR A  1 51  ? 39.620  -7.871  11.912  1.00 12.56  ? 51  TYR A CA  1 
ATOM   404   C  C   . TYR A  1 51  ? 40.149  -8.424  13.218  1.00 14.03  ? 51  TYR A C   1 
ATOM   405   O  O   . TYR A  1 51  ? 39.450  -8.287  14.250  1.00 13.04  ? 51  TYR A O   1 
ATOM   406   C  CB  . TYR A  1 51  ? 38.474  -8.781  11.379  1.00 12.06  ? 51  TYR A CB  1 
ATOM   407   C  CG  . TYR A  1 51  ? 37.464  -8.102  10.522  1.00 11.09  ? 51  TYR A CG  1 
ATOM   408   C  CD1 . TYR A  1 51  ? 37.813  -7.235  9.473   1.00 11.29  ? 51  TYR A CD1 1 
ATOM   409   C  CD2 . TYR A  1 51  ? 36.104  -8.351  10.725  1.00 11.17  ? 51  TYR A CD2 1 
ATOM   410   C  CE1 . TYR A  1 51  ? 36.811  -6.604  8.690   1.00 11.42  ? 51  TYR A CE1 1 
ATOM   411   C  CE2 . TYR A  1 51  ? 35.105  -7.753  9.973   1.00 10.35  ? 51  TYR A CE2 1 
ATOM   412   C  CZ  . TYR A  1 51  ? 35.447  -6.841  9.004   1.00 11.43  ? 51  TYR A CZ  1 
ATOM   413   O  OH  . TYR A  1 51  ? 34.477  -6.231  8.317   1.00 11.98  ? 51  TYR A OH  1 
ATOM   414   N  N   . ASN A  1 52  ? 41.312  -9.072  13.211  1.00 14.21  ? 52  ASN A N   1 
ATOM   415   C  CA  . ASN A  1 52  ? 41.844  -9.606  14.432  1.00 15.23  ? 52  ASN A CA  1 
ATOM   416   C  C   . ASN A  1 52  ? 42.584  -8.501  15.168  1.00 16.80  ? 52  ASN A C   1 
ATOM   417   O  O   . ASN A  1 52  ? 43.825  -8.317  15.015  1.00 20.61  ? 52  ASN A O   1 
ATOM   418   C  CB  . ASN A  1 52  ? 42.735  -10.796 14.156  1.00 17.15  ? 52  ASN A CB  1 
ATOM   419   C  CG  . ASN A  1 52  ? 43.162  -11.473 15.421  1.00 21.10  ? 52  ASN A CG  1 
ATOM   420   O  OD1 . ASN A  1 52  ? 42.453  -11.444 16.413  1.00 21.86  ? 52  ASN A OD1 1 
ATOM   421   N  ND2 . ASN A  1 52  ? 44.341  -12.071 15.390  1.00 28.75  ? 52  ASN A ND2 1 
ATOM   422   N  N   . LEU A  1 53  ? 41.839  -7.695  15.911  1.00 16.48  ? 53  LEU A N   1 
ATOM   423   C  CA  . LEU A  1 53  ? 42.378  -6.497  16.539  1.00 16.48  ? 53  LEU A CA  1 
ATOM   424   C  C   . LEU A  1 53  ? 43.391  -6.828  17.595  1.00 20.55  ? 53  LEU A C   1 
ATOM   425   O  O   . LEU A  1 53  ? 43.150  -7.709  18.460  1.00 25.93  ? 53  LEU A O   1 
ATOM   426   C  CB  . LEU A  1 53  ? 41.327  -5.590  17.126  1.00 16.04  ? 53  LEU A CB  1 
ATOM   427   C  CG  . LEU A  1 53  ? 40.213  -5.231  16.142  1.00 14.24  ? 53  LEU A CG  1 
ATOM   428   C  CD1 . LEU A  1 53  ? 39.267  -4.288  16.904  1.00 15.93  ? 53  LEU A CD1 1 
ATOM   429   C  CD2 . LEU A  1 53  ? 40.807  -4.530  14.966  1.00 17.24  ? 53  LEU A CD2 1 
ATOM   430   N  N   . SER A  1 54  ? 44.470  -6.042  17.614  1.00 23.58  ? 54  SER A N   1 
ATOM   431   C  CA  . SER A  1 54  ? 45.518  -6.264  18.578  1.00 27.77  ? 54  SER A CA  1 
ATOM   432   C  C   . SER A  1 54  ? 44.983  -6.343  20.030  1.00 22.79  ? 54  SER A C   1 
ATOM   433   O  O   . SER A  1 54  ? 44.317  -5.392  20.505  1.00 23.48  ? 54  SER A O   1 
ATOM   434   C  CB  . SER A  1 54  ? 46.526  -5.118  18.463  1.00 29.61  ? 54  SER A CB  1 
ATOM   435   O  OG  . SER A  1 54  ? 47.558  -5.248  19.406  1.00 33.93  ? 54  SER A OG  1 
ATOM   436   N  N   . ALA A  1 55  ? 45.263  -7.449  20.710  1.00 33.58  ? 55  ALA A N   1 
ATOM   437   C  CA  . ALA A  1 55  ? 44.959  -7.565  22.134  1.00 32.80  ? 55  ALA A CA  1 
ATOM   438   C  C   . ALA A  1 55  ? 45.621  -6.461  22.917  1.00 26.90  ? 55  ALA A C   1 
ATOM   439   O  O   . ALA A  1 55  ? 45.217  -6.163  24.045  1.00 26.85  ? 55  ALA A O   1 
ATOM   440   C  CB  . ALA A  1 55  ? 45.483  -8.902  22.643  1.00 37.32  ? 55  ALA A CB  1 
ATOM   441   N  N   . ASN A  1 56  ? 46.663  -5.848  22.321  1.00 22.84  ? 56  ASN A N   1 
ATOM   442   C  CA  . ASN A  1 56  ? 47.486  -4.794  22.961  1.00 22.04  ? 56  ASN A CA  1 
ATOM   443   C  C   . ASN A  1 56  ? 47.031  -3.363  22.712  1.00 25.16  ? 56  ASN A C   1 
ATOM   444   O  O   . ASN A  1 56  ? 47.698  -2.393  23.127  1.00 30.48  ? 56  ASN A O   1 
ATOM   445   C  CB  . ASN A  1 56  ? 48.979  -4.989  22.551  1.00 22.85  ? 56  ASN A CB  1 
ATOM   446   C  CG  . ASN A  1 56  ? 49.535  -6.270  23.091  1.00 31.22  ? 56  ASN A CG  1 
ATOM   447   O  OD1 . ASN A  1 56  ? 49.366  -6.556  24.285  1.00 35.19  ? 56  ASN A OD1 1 
ATOM   448   N  ND2 . ASN A  1 56  ? 50.211  -7.031  22.265  1.00 36.34  ? 56  ASN A ND2 1 
ATOM   449   N  N   A LYS A  1 57  ? 45.912  -3.222  22.001  0.50 20.08  ? 57  LYS A N   1 
ATOM   450   N  N   B LYS A  1 57  ? 45.888  -3.253  22.053  0.50 29.99  ? 57  LYS A N   1 
ATOM   451   C  CA  A LYS A  1 57  ? 45.346  -1.907  21.611  0.50 19.93  ? 57  LYS A CA  1 
ATOM   452   C  CA  B LYS A  1 57  ? 45.296  -1.962  21.757  0.50 28.81  ? 57  LYS A CA  1 
ATOM   453   C  C   A LYS A  1 57  ? 43.978  -1.857  22.267  0.50 17.34  ? 57  LYS A C   1 
ATOM   454   C  C   B LYS A  1 57  ? 43.949  -1.906  22.464  0.50 25.80  ? 57  LYS A C   1 
ATOM   455   O  O   A LYS A  1 57  ? 43.314  -2.872  22.408  0.50 16.97  ? 57  LYS A O   1 
ATOM   456   O  O   B LYS A  1 57  ? 43.332  -2.930  22.777  0.50 25.60  ? 57  LYS A O   1 
ATOM   457   C  CB  A LYS A  1 57  ? 45.223  -1.811  20.065  0.50 21.04  ? 57  LYS A CB  1 
ATOM   458   C  CB  B LYS A  1 57  ? 45.121  -1.813  20.261  0.50 28.88  ? 57  LYS A CB  1 
ATOM   459   C  CG  A LYS A  1 57  ? 46.359  -1.119  19.275  0.50 18.17  ? 57  LYS A CG  1 
ATOM   460   C  CG  B LYS A  1 57  ? 44.956  -0.381  19.746  0.50 27.92  ? 57  LYS A CG  1 
ATOM   461   C  CD  A LYS A  1 57  ? 45.913  -0.760  17.853  0.50 17.99  ? 57  LYS A CD  1 
ATOM   462   C  CD  B LYS A  1 57  ? 45.145  -0.392  18.220  0.50 20.02  ? 57  LYS A CD  1 
ATOM   463   C  CE  A LYS A  1 57  ? 44.995  0.452   17.911  0.50 29.65  ? 57  LYS A CE  1 
ATOM   464   C  CE  B LYS A  1 57  ? 44.744  0.904   17.542  0.50 27.05  ? 57  LYS A CE  1 
ATOM   465   N  NZ  A LYS A  1 57  ? 44.063  0.538   16.756  0.50 31.02  ? 57  LYS A NZ  1 
ATOM   466   N  NZ  B LYS A  1 57  ? 45.179  0.866   16.118  0.50 32.87  ? 57  LYS A NZ  1 
ATOM   467   N  N   . GLN A  1 58  ? 43.496  -0.693  22.693  1.00 21.08  ? 58  GLN A N   1 
ATOM   468   C  CA  . GLN A  1 58  ? 42.150  -0.515  23.247  1.00 21.09  ? 58  GLN A CA  1 
ATOM   469   C  C   . GLN A  1 58  ? 41.317  0.277   22.275  1.00 19.58  ? 58  GLN A C   1 
ATOM   470   O  O   . GLN A  1 58  ? 41.857  1.183   21.602  1.00 23.19  ? 58  GLN A O   1 
ATOM   471   C  CB  . GLN A  1 58  ? 42.185  0.191   24.594  1.00 25.14  ? 58  GLN A CB  1 
ATOM   472   C  CG  . GLN A  1 58  ? 42.869  -0.662  25.601  1.00 27.90  ? 58  GLN A CG  1 
ATOM   473   C  CD  . GLN A  1 58  ? 43.033  0.014   26.872  1.00 28.80  ? 58  GLN A CD  1 
ATOM   474   O  OE1 . GLN A  1 58  ? 43.625  -0.575  27.759  1.00 29.89  ? 58  GLN A OE1 1 
ATOM   475   N  NE2 . GLN A  1 58  ? 42.644  1.264   26.957  1.00 29.55  ? 58  GLN A NE2 1 
ATOM   476   N  N   . PHE A  1 59  ? 40.027  -0.056  22.219  1.00 18.00  ? 59  PHE A N   1 
ATOM   477   C  CA  . PHE A  1 59  ? 39.115  0.539   21.259  1.00 17.87  ? 59  PHE A CA  1 
ATOM   478   C  C   . PHE A  1 59  ? 37.986  1.212   21.995  1.00 16.64  ? 59  PHE A C   1 
ATOM   479   O  O   . PHE A  1 59  ? 37.452  0.680   22.975  1.00 17.25  ? 59  PHE A O   1 
ATOM   480   C  CB  . PHE A  1 59  ? 38.644  -0.564  20.286  1.00 16.15  ? 59  PHE A CB  1 
ATOM   481   C  CG  . PHE A  1 59  ? 39.800  -1.090  19.469  1.00 16.33  ? 59  PHE A CG  1 
ATOM   482   C  CD1 . PHE A  1 59  ? 40.212  -0.460  18.280  1.00 17.70  ? 59  PHE A CD1 1 
ATOM   483   C  CD2 . PHE A  1 59  ? 40.554  -2.142  20.006  1.00 16.86  ? 59  PHE A CD2 1 
ATOM   484   C  CE1 . PHE A  1 59  ? 41.343  -0.872  17.628  1.00 18.60  ? 59  PHE A CE1 1 
ATOM   485   C  CE2 . PHE A  1 59  ? 41.702  -2.556  19.302  1.00 17.30  ? 59  PHE A CE2 1 
ATOM   486   C  CZ  . PHE A  1 59  ? 42.084  -1.901  18.143  1.00 18.62  ? 59  PHE A CZ  1 
ATOM   487   N  N   . LEU A  1 60  ? 37.633  2.406   21.609  1.00 16.95  ? 60  LEU A N   1 
ATOM   488   C  CA  . LEU A  1 60  ? 36.699  3.248   22.358  1.00 14.43  ? 60  LEU A CA  1 
ATOM   489   C  C   . LEU A  1 60  ? 35.241  2.822   22.147  1.00 14.42  ? 60  LEU A C   1 
ATOM   490   O  O   . LEU A  1 60  ? 34.765  2.768   21.036  1.00 15.12  ? 60  LEU A O   1 
ATOM   491   C  CB  . LEU A  1 60  ? 36.816  4.685   21.928  1.00 17.14  ? 60  LEU A CB  1 
ATOM   492   C  CG  . LEU A  1 60  ? 36.047  5.735   22.731  1.00 20.87  ? 60  LEU A CG  1 
ATOM   493   C  CD1 . LEU A  1 60  ? 36.642  5.784   24.150  1.00 24.56  ? 60  LEU A CD1 1 
ATOM   494   C  CD2 . LEU A  1 60  ? 36.099  7.091   22.063  1.00 24.00  ? 60  LEU A CD2 1 
ATOM   495   N  N   . LEU A  1 61  ? 34.539  2.508   23.240  1.00 14.74  ? 61  LEU A N   1 
ATOM   496   C  CA  . LEU A  1 61  ? 33.162  2.200   23.246  1.00 14.88  ? 61  LEU A CA  1 
ATOM   497   C  C   . LEU A  1 61  ? 32.427  3.394   23.770  1.00 13.76  ? 61  LEU A C   1 
ATOM   498   O  O   . LEU A  1 61  ? 32.798  3.944   24.778  1.00 15.37  ? 61  LEU A O   1 
ATOM   499   C  CB  . LEU A  1 61  ? 32.982  1.016   24.167  1.00 16.78  ? 61  LEU A CB  1 
ATOM   500   C  CG  . LEU A  1 61  ? 31.561  0.401   24.180  1.00 17.27  ? 61  LEU A CG  1 
ATOM   501   C  CD1 . LEU A  1 61  ? 31.399  -0.463  22.931  1.00 17.28  ? 61  LEU A CD1 1 
ATOM   502   C  CD2 . LEU A  1 61  ? 31.414  -0.450  25.417  1.00 18.31  ? 61  LEU A CD2 1 
ATOM   503   N  N   A THR A  1 62  ? 31.326  3.728   23.101  0.50 14.11  ? 62  THR A N   1 
ATOM   504   N  N   B THR A  1 62  ? 31.412  3.872   23.057  0.50 16.68  ? 62  THR A N   1 
ATOM   505   C  CA  A THR A  1 62  ? 30.569  4.941   23.405  0.50 13.72  ? 62  THR A CA  1 
ATOM   506   C  CA  B THR A  1 62  ? 30.641  5.018   23.553  0.50 16.36  ? 62  THR A CA  1 
ATOM   507   C  C   A THR A  1 62  ? 29.096  4.632   23.425  0.50 12.44  ? 62  THR A C   1 
ATOM   508   C  C   B THR A  1 62  ? 29.152  4.824   23.364  0.50 18.24  ? 62  THR A C   1 
ATOM   509   O  O   A THR A  1 62  ? 28.589  3.845   22.648  0.50 14.81  ? 62  THR A O   1 
ATOM   510   O  O   B THR A  1 62  ? 28.672  4.329   22.365  0.50 13.41  ? 62  THR A O   1 
ATOM   511   C  CB  A THR A  1 62  ? 30.871  6.085   22.363  0.50 14.35  ? 62  THR A CB  1 
ATOM   512   C  CB  B THR A  1 62  ? 30.970  6.283   22.742  0.50 21.52  ? 62  THR A CB  1 
ATOM   513   O  OG1 A THR A  1 62  ? 32.282  6.308   22.276  0.50 14.90  ? 62  THR A OG1 1 
ATOM   514   O  OG1 B THR A  1 62  ? 30.681  6.022   21.358  0.50 19.91  ? 62  THR A OG1 1 
ATOM   515   C  CG2 A THR A  1 62  ? 30.189  7.446   22.698  0.50 19.40  ? 62  THR A CG2 1 
ATOM   516   C  CG2 B THR A  1 62  ? 32.448  6.691   22.902  0.50 24.37  ? 62  THR A CG2 1 
ATOM   517   N  N   . ASN A  1 63  ? 28.403  5.297   24.350  1.00 15.13  ? 63  ASN A N   1 
ATOM   518   C  CA  . ASN A  1 63  ? 26.952  5.439   24.258  1.00 14.74  ? 63  ASN A CA  1 
ATOM   519   C  C   . ASN A  1 63  ? 26.716  6.798   23.637  1.00 15.19  ? 63  ASN A C   1 
ATOM   520   O  O   . ASN A  1 63  ? 27.030  7.807   24.226  1.00 15.05  ? 63  ASN A O   1 
ATOM   521   C  CB  . ASN A  1 63  ? 26.346  5.351   25.625  1.00 14.18  ? 63  ASN A CB  1 
ATOM   522   C  CG  . ASN A  1 63  ? 24.869  5.681   25.678  1.00 13.19  ? 63  ASN A CG  1 
ATOM   523   O  OD1 . ASN A  1 63  ? 24.276  6.307   24.812  1.00 15.11  ? 63  ASN A OD1 1 
ATOM   524   N  ND2 . ASN A  1 63  ? 24.240  5.110   26.694  1.00 14.73  ? 63  ASN A ND2 1 
ATOM   525   N  N   . ASN A  1 64  ? 26.209  6.859   22.406  1.00 14.12  ? 64  ASN A N   1 
ATOM   526   C  CA  . ASN A  1 64  ? 26.016  8.151   21.751  1.00 15.02  ? 64  ASN A CA  1 
ATOM   527   C  C   . ASN A  1 64  ? 24.558  8.651   21.830  1.00 15.15  ? 64  ASN A C   1 
ATOM   528   O  O   . ASN A  1 64  ? 24.159  9.619   21.100  1.00 18.03  ? 64  ASN A O   1 
ATOM   529   C  CB  . ASN A  1 64  ? 26.484  8.127   20.283  1.00 16.60  ? 64  ASN A CB  1 
ATOM   530   C  CG  . ASN A  1 64  ? 25.668  7.175   19.418  1.00 17.10  ? 64  ASN A CG  1 
ATOM   531   O  OD1 . ASN A  1 64  ? 24.644  6.639   19.898  1.00 14.95  ? 64  ASN A OD1 1 
ATOM   532   N  ND2 . ASN A  1 64  ? 26.036  6.960   18.173  1.00 30.19  ? 64  ASN A ND2 1 
ATOM   533   N  N   . GLY A  1 65  ? 23.740  8.041   22.705  1.00 15.35  ? 65  GLY A N   1 
ATOM   534   C  CA  . GLY A  1 65  ? 22.384  8.492   22.861  1.00 16.02  ? 65  GLY A CA  1 
ATOM   535   C  C   . GLY A  1 65  ? 21.421  7.772   21.914  1.00 17.90  ? 65  GLY A C   1 
ATOM   536   O  O   . GLY A  1 65  ? 20.240  7.946   22.056  1.00 24.20  ? 65  GLY A O   1 
ATOM   537   N  N   . HIS A  1 66  ? 21.959  7.041   20.928  1.00 13.96  ? 66  HIS A N   1 
ATOM   538   C  CA  . HIS A  1 66  ? 21.154  6.342   19.908  1.00 13.35  ? 66  HIS A CA  1 
ATOM   539   C  C   . HIS A  1 66  ? 21.435  4.862   19.914  1.00 13.18  ? 66  HIS A C   1 
ATOM   540   O  O   . HIS A  1 66  ? 20.534  4.101   19.583  1.00 16.77  ? 66  HIS A O   1 
ATOM   541   C  CB  . HIS A  1 66  ? 21.416  6.921   18.526  1.00 15.33  ? 66  HIS A CB  1 
ATOM   542   C  CG  . HIS A  1 66  ? 21.190  8.442   18.430  1.00 17.08  ? 66  HIS A CG  1 
ATOM   543   N  ND1 . HIS A  1 66  ? 19.954  9.039   18.509  1.00 17.75  ? 66  HIS A ND1 1 
ATOM   544   C  CD2 . HIS A  1 66  ? 22.107  9.454   18.244  1.00 16.85  ? 66  HIS A CD2 1 
ATOM   545   C  CE1 . HIS A  1 66  ? 20.116  10.396  18.404  1.00 18.65  ? 66  HIS A CE1 1 
ATOM   546   N  NE2 . HIS A  1 66  ? 21.449  10.618  18.202  1.00 19.31  ? 66  HIS A NE2 1 
ATOM   547   N  N   . SER A  1 67  ? 22.680  4.487   20.180  1.00 13.47  ? 67  SER A N   1 
ATOM   548   C  CA  . SER A  1 67  ? 23.146  3.086   20.208  1.00 12.95  ? 67  SER A CA  1 
ATOM   549   C  C   . SER A  1 67  ? 24.394  3.024   21.081  1.00 12.62  ? 67  SER A C   1 
ATOM   550   O  O   . SER A  1 67  ? 24.785  4.032   21.676  1.00 14.47  ? 67  SER A O   1 
ATOM   551   C  CB  . SER A  1 67  ? 23.445  2.597   18.784  1.00 12.44  ? 67  SER A CB  1 
ATOM   552   O  OG  . SER A  1 67  ? 23.805  1.231   18.768  1.00 14.05  ? 67  SER A OG  1 
ATOM   553   N  N   . VAL A  1 68  ? 24.967  1.847   21.183  1.00 12.74  ? 68  VAL A N   1 
ATOM   554   C  CA  . VAL A  1 68  ? 26.308  1.700   21.696  1.00 12.14  ? 68  VAL A CA  1 
ATOM   555   C  C   . VAL A  1 68  ? 27.199  1.410   20.491  1.00 12.10  ? 68  VAL A C   1 
ATOM   556   O  O   . VAL A  1 68  ? 26.865  0.534   19.692  1.00 13.19  ? 68  VAL A O   1 
ATOM   557   C  CB  . VAL A  1 68  ? 26.374  0.612   22.797  1.00 13.60  ? 68  VAL A CB  1 
ATOM   558   C  CG1 . VAL A  1 68  ? 25.806  -0.755  22.325  1.00 15.77  ? 68  VAL A CG1 1 
ATOM   559   C  CG2 . VAL A  1 68  ? 27.782  0.544   23.307  1.00 18.93  ? 68  VAL A CG2 1 
ATOM   560   N  N   . LYS A  1 69  ? 28.316  2.169   20.402  1.00 13.58  ? 69  LYS A N   1 
ATOM   561   C  CA  . LYS A  1 69  ? 29.215  2.068   19.252  1.00 12.66  ? 69  LYS A CA  1 
ATOM   562   C  C   . LYS A  1 69  ? 30.636  1.760   19.738  1.00 12.61  ? 69  LYS A C   1 
ATOM   563   O  O   . LYS A  1 69  ? 31.060  2.227   20.769  1.00 15.87  ? 69  LYS A O   1 
ATOM   564   C  CB  . LYS A  1 69  ? 29.175  3.276   18.355  1.00 16.42  ? 69  LYS A CB  1 
ATOM   565   C  CG  . LYS A  1 69  ? 29.656  4.547   18.842  1.00 19.98  ? 69  LYS A CG  1 
ATOM   566   C  CD  . LYS A  1 69  ? 29.876  5.479   17.641  1.00 25.26  ? 69  LYS A CD  1 
ATOM   567   C  CE  . LYS A  1 69  ? 30.376  6.727   18.305  1.00 27.23  ? 69  LYS A CE  1 
ATOM   568   N  NZ  . LYS A  1 69  ? 30.569  7.754   17.270  1.00 30.60  ? 69  LYS A NZ  1 
ATOM   569   N  N   . LEU A  1 70  ? 31.309  0.909   18.972  1.00 10.86  ? 70  LEU A N   1 
ATOM   570   C  CA  . LEU A  1 70  ? 32.708  0.604   19.163  1.00 11.63  ? 70  LEU A CA  1 
ATOM   571   C  C   . LEU A  1 70  ? 33.488  1.212   18.007  1.00 11.15  ? 70  LEU A C   1 
ATOM   572   O  O   . LEU A  1 70  ? 33.212  0.830   16.859  1.00 11.20  ? 70  LEU A O   1 
ATOM   573   C  CB  . LEU A  1 70  ? 32.917  -0.920  19.260  1.00 12.27  ? 70  LEU A CB  1 
ATOM   574   C  CG  . LEU A  1 70  ? 34.359  -1.346  19.551  1.00 12.19  ? 70  LEU A CG  1 
ATOM   575   C  CD1 . LEU A  1 70  ? 34.892  -0.772  20.865  1.00 16.78  ? 70  LEU A CD1 1 
ATOM   576   C  CD2 . LEU A  1 70  ? 34.421  -2.876  19.431  1.00 16.15  ? 70  LEU A CD2 1 
ATOM   577   N  N   . ASN A  1 71  ? 34.476  2.060   18.290  1.00 11.98  ? 71  ASN A N   1 
ATOM   578   C  CA  . ASN A  1 71  ? 35.318  2.589   17.223  1.00 12.50  ? 71  ASN A CA  1 
ATOM   579   C  C   . ASN A  1 71  ? 36.240  1.479   16.733  1.00 13.12  ? 71  ASN A C   1 
ATOM   580   O  O   . ASN A  1 71  ? 36.752  0.690   17.526  1.00 15.25  ? 71  ASN A O   1 
ATOM   581   C  CB  . ASN A  1 71  ? 36.116  3.784   17.717  1.00 15.60  ? 71  ASN A CB  1 
ATOM   582   C  CG  . ASN A  1 71  ? 35.275  4.991   17.803  1.00 20.02  ? 71  ASN A CG  1 
ATOM   583   O  OD1 . ASN A  1 71  ? 34.057  4.986   17.565  1.00 21.82  ? 71  ASN A OD1 1 
ATOM   584   N  ND2 . ASN A  1 71  ? 35.886  6.034   18.215  1.00 22.92  ? 71  ASN A ND2 1 
ATOM   585   N  N   . LEU A  1 72  ? 36.506  1.484   15.432  1.00 12.39  ? 72  LEU A N   1 
ATOM   586   C  CA  . LEU A  1 72  ? 37.368  0.468   14.793  1.00 11.80  ? 72  LEU A CA  1 
ATOM   587   C  C   . LEU A  1 72  ? 38.458  1.183   14.012  1.00 13.62  ? 72  LEU A C   1 
ATOM   588   O  O   . LEU A  1 72  ? 38.254  2.315   13.552  1.00 14.58  ? 72  LEU A O   1 
ATOM   589   C  CB  . LEU A  1 72  ? 36.520  -0.384  13.873  1.00 12.19  ? 72  LEU A CB  1 
ATOM   590   C  CG  . LEU A  1 72  ? 35.419  -1.163  14.563  1.00 11.57  ? 72  LEU A CG  1 
ATOM   591   C  CD1 . LEU A  1 72  ? 34.473  -1.740  13.503  1.00 11.79  ? 72  LEU A CD1 1 
ATOM   592   C  CD2 . LEU A  1 72  ? 35.987  -2.225  15.475  1.00 14.44  ? 72  LEU A CD2 1 
ATOM   593   N  N   . PRO A  1 73  ? 39.627  0.490   13.844  1.00 13.75  ? 73  PRO A N   1 
ATOM   594   C  CA  . PRO A  1 73  ? 40.777  1.162   13.205  1.00 15.73  ? 73  PRO A CA  1 
ATOM   595   C  C   . PRO A  1 73  ? 40.695  1.081   11.693  1.00 14.51  ? 73  PRO A C   1 
ATOM   596   O  O   . PRO A  1 73  ? 40.190  0.110   11.140  1.00 15.33  ? 73  PRO A O   1 
ATOM   597   C  CB  . PRO A  1 73  ? 41.950  0.340   13.789  1.00 15.77  ? 73  PRO A CB  1 
ATOM   598   C  CG  . PRO A  1 73  ? 41.398  -1.042  13.911  1.00 13.83  ? 73  PRO A CG  1 
ATOM   599   C  CD  . PRO A  1 73  ? 39.924  -0.842  14.353  1.00 14.63  ? 73  PRO A CD  1 
ATOM   600   N  N   . SER A  1 74  ? 41.298  2.034   10.993  1.00 18.05  ? 74  SER A N   1 
ATOM   601   C  CA  . SER A  1 74  ? 41.094  2.083   9.546   1.00 18.85  ? 74  SER A CA  1 
ATOM   602   C  C   . SER A  1 74  ? 41.972  1.040   8.824   1.00 15.88  ? 74  SER A C   1 
ATOM   603   O  O   . SER A  1 74  ? 41.794  0.911   7.627   1.00 19.57  ? 74  SER A O   1 
ATOM   604   C  CB  . SER A  1 74  ? 41.386  3.477   8.992   1.00 28.22  ? 74  SER A CB  1 
ATOM   605   O  OG  . SER A  1 74  ? 42.738  3.779   9.339   1.00 25.81  ? 74  SER A OG  1 
ATOM   606   N  N   . ASP A  1 75  ? 42.921  0.337   9.520   1.00 15.86  ? 75  ASP A N   1 
ATOM   607   C  CA  . ASP A  1 75  ? 43.583  -0.775  8.820   1.00 15.89  ? 75  ASP A CA  1 
ATOM   608   C  C   . ASP A  1 75  ? 42.684  -1.997  8.742   1.00 13.60  ? 75  ASP A C   1 
ATOM   609   O  O   . ASP A  1 75  ? 42.953  -2.881  7.983   1.00 16.38  ? 75  ASP A O   1 
ATOM   610   C  CB  . ASP A  1 75  ? 44.922  -1.148  9.507   1.00 18.67  ? 75  ASP A CB  1 
ATOM   611   C  CG  . ASP A  1 75  ? 44.685  -1.589  10.959  1.00 19.28  ? 75  ASP A CG  1 
ATOM   612   O  OD1 . ASP A  1 75  ? 44.263  -0.735  11.790  1.00 24.88  ? 75  ASP A OD1 1 
ATOM   613   O  OD2 . ASP A  1 75  ? 44.932  -2.741  11.305  1.00 25.81  ? 75  ASP A OD2 1 
ATOM   614   N  N   . MET A  1 76  ? 41.588  -2.057  9.507   1.00 12.61  ? 76  MET A N   1 
ATOM   615   C  CA  . MET A  1 76  ? 40.590  -3.101  9.344   1.00 11.67  ? 76  MET A CA  1 
ATOM   616   C  C   . MET A  1 76  ? 39.753  -2.784  8.105   1.00 11.87  ? 76  MET A C   1 
ATOM   617   O  O   . MET A  1 76  ? 39.296  -1.632  7.956   1.00 12.39  ? 76  MET A O   1 
ATOM   618   C  CB  . MET A  1 76  ? 39.769  -3.081  10.605  1.00 12.94  ? 76  MET A CB  1 
ATOM   619   C  CG  . MET A  1 76  ? 38.576  -4.015  10.581  1.00 12.28  ? 76  MET A CG  1 
ATOM   620   S  SD  . MET A  1 76  ? 37.737  -3.989  12.177  1.00 12.89  ? 76  MET A SD  1 
ATOM   621   C  CE  . MET A  1 76  ? 36.183  -4.716  11.696  1.00 13.60  ? 76  MET A CE  1 
ATOM   622   N  N   . HIS A  1 77  ? 39.548  -3.747  7.247   1.00 11.04  ? 77  HIS A N   1 
ATOM   623   C  CA  . HIS A  1 77  ? 38.843  -3.452  6.023   1.00 12.01  ? 77  HIS A CA  1 
ATOM   624   C  C   . HIS A  1 77  ? 38.244  -4.680  5.383   1.00 11.16  ? 77  HIS A C   1 
ATOM   625   O  O   . HIS A  1 77  ? 38.583  -5.807  5.706   1.00 12.43  ? 77  HIS A O   1 
ATOM   626   C  CB  . HIS A  1 77  ? 39.764  -2.684  5.021   1.00 13.69  ? 77  HIS A CB  1 
ATOM   627   C  CG  . HIS A  1 77  ? 40.931  -3.476  4.540   1.00 14.16  ? 77  HIS A CG  1 
ATOM   628   N  ND1 . HIS A  1 77  ? 42.112  -3.468  5.177   1.00 16.33  ? 77  HIS A ND1 1 
ATOM   629   C  CD2 . HIS A  1 77  ? 41.096  -4.289  3.425   1.00 16.43  ? 77  HIS A CD2 1 
ATOM   630   C  CE1 . HIS A  1 77  ? 43.008  -4.201  4.458   1.00 15.84  ? 77  HIS A CE1 1 
ATOM   631   N  NE2 . HIS A  1 77  ? 42.377  -4.739  3.428   1.00 16.86  ? 77  HIS A NE2 1 
ATOM   632   N  N   A ILE A  1 78  ? 37.299  -4.479  4.463   0.50 11.58  ? 78  ILE A N   1 
ATOM   633   N  N   B ILE A  1 78  ? 37.382  -4.399  4.411   0.50 12.07  ? 78  ILE A N   1 
ATOM   634   C  CA  A ILE A  1 78  ? 36.748  -5.536  3.616   0.50 11.74  ? 78  ILE A CA  1 
ATOM   635   C  CA  B ILE A  1 78  ? 36.748  -5.362  3.536   0.50 14.12  ? 78  ILE A CA  1 
ATOM   636   C  C   A ILE A  1 78  ? 37.508  -5.440  2.307   0.50 12.88  ? 78  ILE A C   1 
ATOM   637   C  C   B ILE A  1 78  ? 37.511  -5.415  2.223   0.50 13.50  ? 78  ILE A C   1 
ATOM   638   O  O   A ILE A  1 78  ? 37.669  -4.328  1.760   0.50 13.16  ? 78  ILE A O   1 
ATOM   639   O  O   B ILE A  1 78  ? 37.725  -4.379  1.596   0.50 14.75  ? 78  ILE A O   1 
ATOM   640   C  CB  A ILE A  1 78  ? 35.212  -5.194  3.319   0.50 15.60  ? 78  ILE A CB  1 
ATOM   641   C  CB  B ILE A  1 78  ? 35.312  -4.804  3.246   0.50 20.34  ? 78  ILE A CB  1 
ATOM   642   C  CG1 A ILE A  1 78  ? 34.357  -5.113  4.560   0.50 12.40  ? 78  ILE A CG1 1 
ATOM   643   C  CG1 B ILE A  1 78  ? 34.293  -5.633  3.935   0.50 26.03  ? 78  ILE A CG1 1 
ATOM   644   C  CG2 A ILE A  1 78  ? 34.690  -6.010  2.183   0.50 14.22  ? 78  ILE A CG2 1 
ATOM   645   C  CG2 B ILE A  1 78  ? 35.057  -4.713  1.763   0.50 29.13  ? 78  ILE A CG2 1 
ATOM   646   C  CD1 A ILE A  1 78  ? 33.041  -4.378  4.280   0.50 12.62  ? 78  ILE A CD1 1 
ATOM   647   C  CD1 B ILE A  1 78  ? 34.923  -6.312  5.074   0.50 20.93  ? 78  ILE A CD1 1 
ATOM   648   N  N   . GLN A  1 79  ? 37.853  -6.633  1.799   1.00 14.70  ? 79  GLN A N   1 
ATOM   649   C  CA  . GLN A  1 79  ? 38.410  -6.827  0.467   1.00 15.92  ? 79  GLN A CA  1 
ATOM   650   C  C   . GLN A  1 79  ? 37.367  -7.609  -0.350  1.00 16.53  ? 79  GLN A C   1 
ATOM   651   O  O   . GLN A  1 79  ? 36.663  -8.478  0.202   1.00 16.72  ? 79  GLN A O   1 
ATOM   652   C  CB  . GLN A  1 79  ? 39.771  -7.530  0.587   1.00 22.01  ? 79  GLN A CB  1 
ATOM   653   C  CG  . GLN A  1 79  ? 40.405  -7.877  -0.746  1.00 24.95  ? 79  GLN A CG  1 
ATOM   654   C  CD  . GLN A  1 79  ? 41.787  -8.442  -0.564  1.00 36.23  ? 79  GLN A CD  1 
ATOM   655   O  OE1 . GLN A  1 79  ? 42.266  -8.635  0.559   1.00 53.74  ? 79  GLN A OE1 1 
ATOM   656   N  NE2 . GLN A  1 79  ? 42.449  -8.713  -1.680  1.00 65.48  ? 79  GLN A NE2 1 
ATOM   657   N  N   . GLY A  1 80  ? 37.188  -7.217  -1.591  1.00 18.45  ? 80  GLY A N   1 
ATOM   658   C  CA  . GLY A  1 80  ? 36.236  -7.876  -2.472  1.00 18.56  ? 80  GLY A CA  1 
ATOM   659   C  C   . GLY A  1 80  ? 35.317  -6.878  -3.165  1.00 17.35  ? 80  GLY A C   1 
ATOM   660   O  O   . GLY A  1 80  ? 34.656  -7.264  -4.136  1.00 21.56  ? 80  GLY A O   1 
ATOM   661   N  N   . LEU A  1 81  ? 35.124  -5.693  -2.614  1.00 18.87  ? 81  LEU A N   1 
ATOM   662   C  CA  . LEU A  1 81  ? 34.195  -4.698  -3.224  1.00 17.08  ? 81  LEU A CA  1 
ATOM   663   C  C   . LEU A  1 81  ? 34.970  -3.854  -4.253  1.00 17.67  ? 81  LEU A C   1 
ATOM   664   O  O   . LEU A  1 81  ? 36.215  -4.109  -4.449  1.00 22.04  ? 81  LEU A O   1 
ATOM   665   C  CB  . LEU A  1 81  ? 33.542  -3.863  -2.182  1.00 16.92  ? 81  LEU A CB  1 
ATOM   666   C  CG  . LEU A  1 81  ? 32.651  -4.655  -1.196  1.00 16.02  ? 81  LEU A CG  1 
ATOM   667   C  CD1 . LEU A  1 81  ? 32.205  -3.729  -0.087  1.00 19.39  ? 81  LEU A CD1 1 
ATOM   668   C  CD2 . LEU A  1 81  ? 31.504  -5.302  -1.941  1.00 20.34  ? 81  LEU A CD2 1 
ATOM   669   N  N   . GLN A  1 82  ? 34.300  -2.912  -4.951  1.00 17.88  ? 82  GLN A N   1 
ATOM   670   C  CA  . GLN A  1 82  ? 34.969  -2.123  -6.028  1.00 19.26  ? 82  GLN A CA  1 
ATOM   671   C  C   . GLN A  1 82  ? 36.022  -1.173  -5.506  1.00 18.73  ? 82  GLN A C   1 
ATOM   672   O  O   . GLN A  1 82  ? 36.835  -0.630  -6.286  1.00 29.30  ? 82  GLN A O   1 
ATOM   673   C  CB  . GLN A  1 82  ? 33.968  -1.356  -6.827  1.00 22.28  ? 82  GLN A CB  1 
ATOM   674   C  CG  . GLN A  1 82  ? 33.063  -2.272  -7.635  1.00 23.74  ? 82  GLN A CG  1 
ATOM   675   C  CD  . GLN A  1 82  ? 33.697  -2.775  -8.944  1.00 40.77  ? 82  GLN A CD  1 
ATOM   676   O  OE1 . GLN A  1 82  ? 34.729  -2.242  -9.447  1.00 32.31  ? 82  GLN A OE1 1 
ATOM   677   N  NE2 . GLN A  1 82  ? 33.008  -3.765  -9.566  1.00 29.93  ? 82  GLN A NE2 1 
ATOM   678   N  N   . SER A  1 83  ? 36.007  -0.870  -4.274  1.00 19.23  ? 83  SER A N   1 
ATOM   679   C  CA  . SER A  1 83  ? 37.005  -0.084  -3.602  1.00 17.40  ? 83  SER A CA  1 
ATOM   680   C  C   . SER A  1 83  ? 37.283  -0.821  -2.314  1.00 15.15  ? 83  SER A C   1 
ATOM   681   O  O   . SER A  1 83  ? 36.450  -1.649  -1.869  1.00 15.20  ? 83  SER A O   1 
ATOM   682   C  CB  . SER A  1 83  ? 36.412  1.297   -3.319  1.00 19.48  ? 83  SER A CB  1 
ATOM   683   O  OG  . SER A  1 83  ? 36.223  1.937   -4.543  1.00 21.56  ? 83  SER A OG  1 
ATOM   684   N  N   . ARG A  1 84  ? 38.394  -0.506  -1.661  1.00 17.14  ? 84  ARG A N   1 
ATOM   685   C  CA  . ARG A  1 84  ? 38.612  -0.920  -0.291  1.00 14.51  ? 84  ARG A CA  1 
ATOM   686   C  C   . ARG A  1 84  ? 37.657  -0.131  0.587   1.00 13.32  ? 84  ARG A C   1 
ATOM   687   O  O   . ARG A  1 84  ? 37.553  1.057   0.440   1.00 14.68  ? 84  ARG A O   1 
ATOM   688   C  CB  . ARG A  1 84  ? 40.030  -0.621  0.133   1.00 15.58  ? 84  ARG A CB  1 
ATOM   689   C  CG  . ARG A  1 84  ? 40.226  -1.026  1.611   1.00 13.07  ? 84  ARG A CG  1 
ATOM   690   C  CD  . ARG A  1 84  ? 41.589  -0.854  2.112   1.00 14.48  ? 84  ARG A CD  1 
ATOM   691   N  NE  . ARG A  1 84  ? 42.495  -1.873  1.526   1.00 15.11  ? 84  ARG A NE  1 
ATOM   692   C  CZ  . ARG A  1 84  ? 43.767  -1.988  1.880   1.00 13.72  ? 84  ARG A CZ  1 
ATOM   693   N  NH1 . ARG A  1 84  ? 44.291  -1.112  2.702   1.00 16.99  ? 84  ARG A NH1 1 
ATOM   694   N  NH2 . ARG A  1 84  ? 44.470  -2.934  1.341   1.00 16.19  ? 84  ARG A NH2 1 
ATOM   695   N  N   . TYR A  1 85  ? 36.964  -0.862  1.481   1.00 12.42  ? 85  TYR A N   1 
ATOM   696   C  CA  . TYR A  1 85  ? 36.148  -0.193  2.466   1.00 11.44  ? 85  TYR A CA  1 
ATOM   697   C  C   . TYR A  1 85  ? 36.727  -0.489  3.838   1.00 10.73  ? 85  TYR A C   1 
ATOM   698   O  O   . TYR A  1 85  ? 36.852  -1.640  4.248   1.00 11.56  ? 85  TYR A O   1 
ATOM   699   C  CB  . TYR A  1 85  ? 34.688  -0.674  2.414   1.00 12.07  ? 85  TYR A CB  1 
ATOM   700   C  CG  . TYR A  1 85  ? 33.940  -0.083  1.253   1.00 12.38  ? 85  TYR A CG  1 
ATOM   701   C  CD1 . TYR A  1 85  ? 34.022  -0.650  -0.027  1.00 14.98  ? 85  TYR A CD1 1 
ATOM   702   C  CD2 . TYR A  1 85  ? 33.148  1.047   1.409   1.00 13.08  ? 85  TYR A CD2 1 
ATOM   703   C  CE1 . TYR A  1 85  ? 33.309  -0.041  -1.109  1.00 15.09  ? 85  TYR A CE1 1 
ATOM   704   C  CE2 . TYR A  1 85  ? 32.420  1.600   0.332   1.00 13.80  ? 85  TYR A CE2 1 
ATOM   705   C  CZ  . TYR A  1 85  ? 32.521  1.055   -0.888  1.00 14.23  ? 85  TYR A CZ  1 
ATOM   706   O  OH  . TYR A  1 85  ? 31.867  1.593   -1.938  1.00 19.30  ? 85  TYR A OH  1 
ATOM   707   N  N   . SER A  1 86  ? 37.156  0.559   4.507   1.00 11.23  ? 86  SER A N   1 
ATOM   708   C  CA  . SER A  1 86  ? 37.871  0.491   5.795   1.00 11.70  ? 86  SER A CA  1 
ATOM   709   C  C   . SER A  1 86  ? 36.882  0.722   6.917   1.00 11.20  ? 86  SER A C   1 
ATOM   710   O  O   . SER A  1 86  ? 35.952  1.493   6.801   1.00 11.30  ? 86  SER A O   1 
ATOM   711   C  CB  . SER A  1 86  ? 38.981  1.514   5.885   1.00 12.95  ? 86  SER A CB  1 
ATOM   712   O  OG  . SER A  1 86  ? 39.978  1.263   4.908   1.00 13.89  ? 86  SER A OG  1 
ATOM   713   N  N   . ALA A  1 87  ? 37.052  -0.057  7.995   1.00 11.18  ? 87  ALA A N   1 
ATOM   714   C  CA  . ALA A  1 87  ? 36.154  0.045   9.107   1.00 10.41  ? 87  ALA A CA  1 
ATOM   715   C  C   . ALA A  1 87  ? 36.229  1.358   9.782   1.00 10.10  ? 87  ALA A C   1 
ATOM   716   O  O   . ALA A  1 87  ? 37.303  1.995   9.886   1.00 12.68  ? 87  ALA A O   1 
ATOM   717   C  CB  . ALA A  1 87  ? 36.460  -1.073  10.098  1.00 12.48  ? 87  ALA A CB  1 
ATOM   718   N  N   . THR A  1 88  ? 35.087  1.786   10.359  1.00 11.30  ? 88  THR A N   1 
ATOM   719   C  CA  . THR A  1 88  ? 35.053  2.955   11.218  1.00 11.49  ? 88  THR A CA  1 
ATOM   720   C  C   . THR A  1 88  ? 34.399  2.712   12.539  1.00 9.43   ? 88  THR A C   1 
ATOM   721   O  O   . THR A  1 88  ? 34.869  3.243   13.559  1.00 11.89  ? 88  THR A O   1 
ATOM   722   C  CB  . THR A  1 88  ? 34.392  4.148   10.497  1.00 11.65  ? 88  THR A CB  1 
ATOM   723   O  OG1 . THR A  1 88  ? 34.398  5.289   11.333  1.00 15.23  ? 88  THR A OG1 1 
ATOM   724   C  CG2 . THR A  1 88  ? 32.990  3.889   10.010  1.00 13.28  ? 88  THR A CG2 1 
ATOM   725   N  N   . GLN A  1 89  ? 33.328  1.910   12.644  1.00 10.28  ? 89  GLN A N   1 
ATOM   726   C  CA  . GLN A  1 89  ? 32.679  1.631   13.918  1.00 10.88  ? 89  GLN A CA  1 
ATOM   727   C  C   . GLN A  1 89  ? 31.729  0.492   13.715  1.00 9.64   ? 89  GLN A C   1 
ATOM   728   O  O   . GLN A  1 89  ? 31.340  0.174   12.622  1.00 9.99   ? 89  GLN A O   1 
ATOM   729   C  CB  . GLN A  1 89  ? 31.946  2.833   14.444  1.00 11.37  ? 89  GLN A CB  1 
ATOM   730   C  CG  . GLN A  1 89  ? 30.917  3.467   13.517  1.00 13.68  ? 89  GLN A CG  1 
ATOM   731   C  CD  . GLN A  1 89  ? 29.545  3.265   13.982  1.00 13.50  ? 89  GLN A CD  1 
ATOM   732   O  OE1 . GLN A  1 89  ? 29.155  2.107   14.231  1.00 12.60  ? 89  GLN A OE1 1 
ATOM   733   N  NE2 . GLN A  1 89  ? 28.743  4.243   13.982  1.00 20.76  ? 89  GLN A NE2 1 
ATOM   734   N  N   . LEU A  1 90  ? 31.369  -0.131  14.855  1.00 9.97   ? 90  LEU A N   1 
ATOM   735   C  CA  . LEU A  1 90  ? 30.230  -1.047  14.874  1.00 8.96   ? 90  LEU A CA  1 
ATOM   736   C  C   . LEU A  1 90  ? 29.255  -0.596  15.921  1.00 8.99   ? 90  LEU A C   1 
ATOM   737   O  O   . LEU A  1 90  ? 29.601  0.054   16.860  1.00 9.81   ? 90  LEU A O   1 
ATOM   738   C  CB  . LEU A  1 90  ? 30.642  -2.505  14.959  1.00 9.74   ? 90  LEU A CB  1 
ATOM   739   C  CG  . LEU A  1 90  ? 31.439  -2.974  16.222  1.00 10.69  ? 90  LEU A CG  1 
ATOM   740   C  CD1 . LEU A  1 90  ? 30.552  -3.052  17.458  1.00 11.70  ? 90  LEU A CD1 1 
ATOM   741   C  CD2 . LEU A  1 90  ? 32.054  -4.346  15.928  1.00 13.50  ? 90  LEU A CD2 1 
ATOM   742   N  N   . HIS A  1 91  ? 28.007  -1.046  15.779  1.00 8.54   ? 91  HIS A N   1 
ATOM   743   C  CA  . HIS A  1 91  ? 26.941  -0.703  16.751  1.00 8.22   ? 91  HIS A CA  1 
ATOM   744   C  C   . HIS A  1 91  ? 25.793  -1.656  16.567  1.00 7.81   ? 91  HIS A C   1 
ATOM   745   O  O   . HIS A  1 91  ? 25.818  -2.481  15.657  1.00 8.26   ? 91  HIS A O   1 
ATOM   746   C  CB  . HIS A  1 91  ? 26.484  0.774   16.569  1.00 9.20   ? 91  HIS A CB  1 
ATOM   747   C  CG  . HIS A  1 91  ? 25.860  0.979   15.221  1.00 8.72   ? 91  HIS A CG  1 
ATOM   748   N  ND1 . HIS A  1 91  ? 26.556  1.391   14.133  1.00 8.68   ? 91  HIS A ND1 1 
ATOM   749   C  CD2 . HIS A  1 91  ? 24.604  0.723   14.771  1.00 8.92   ? 91  HIS A CD2 1 
ATOM   750   C  CE1 . HIS A  1 91  ? 25.740  1.396   13.068  1.00 8.87   ? 91  HIS A CE1 1 
ATOM   751   N  NE2 . HIS A  1 91  ? 24.559  0.964   13.439  1.00 7.76   ? 91  HIS A NE2 1 
ATOM   752   N  N   . LEU A  1 92  ? 24.772  -1.554  17.432  1.00 8.15   ? 92  LEU A N   1 
ATOM   753   C  CA  . LEU A  1 92  ? 23.670  -2.468  17.426  1.00 7.97   ? 92  LEU A CA  1 
ATOM   754   C  C   . LEU A  1 92  ? 22.308  -1.788  17.423  1.00 7.50   ? 92  LEU A C   1 
ATOM   755   O  O   . LEU A  1 92  ? 22.191  -0.613  17.768  1.00 8.52   ? 92  LEU A O   1 
ATOM   756   C  CB  . LEU A  1 92  ? 23.750  -3.449  18.599  1.00 9.98   ? 92  LEU A CB  1 
ATOM   757   C  CG  . LEU A  1 92  ? 24.989  -4.368  18.607  1.00 9.57   ? 92  LEU A CG  1 
ATOM   758   C  CD1 . LEU A  1 92  ? 26.084  -3.813  19.484  1.00 15.13  ? 92  LEU A CD1 1 
ATOM   759   C  CD2 . LEU A  1 92  ? 24.630  -5.777  18.923  1.00 13.35  ? 92  LEU A CD2 1 
ATOM   760   N  N   . HIS A  1 93  ? 21.280  -2.537  17.075  1.00 7.75   ? 93  HIS A N   1 
ATOM   761   C  CA  . HIS A  1 93  ? 19.891  -2.081  17.148  1.00 8.01   ? 93  HIS A CA  1 
ATOM   762   C  C   . HIS A  1 93  ? 19.112  -3.222  17.793  1.00 7.59   ? 93  HIS A C   1 
ATOM   763   O  O   . HIS A  1 93  ? 19.386  -4.409  17.522  1.00 8.18   ? 93  HIS A O   1 
ATOM   764   C  CB  . HIS A  1 93  ? 19.321  -1.874  15.742  1.00 8.72   ? 93  HIS A CB  1 
ATOM   765   C  CG  . HIS A  1 93  ? 20.085  -0.845  14.932  1.00 7.70   ? 93  HIS A CG  1 
ATOM   766   N  ND1 . HIS A  1 93  ? 19.766  0.482   14.951  1.00 8.62   ? 93  HIS A ND1 1 
ATOM   767   C  CD2 . HIS A  1 93  ? 21.169  -0.948  14.142  1.00 7.91   ? 93  HIS A CD2 1 
ATOM   768   C  CE1 . HIS A  1 93  ? 20.622  1.157   14.165  1.00 8.49   ? 93  HIS A CE1 1 
ATOM   769   N  NE2 . HIS A  1 93  ? 21.491  0.298   13.625  1.00 8.06   ? 93  HIS A NE2 1 
ATOM   770   N  N   . TRP A  1 94  ? 18.152  -2.866  18.661  1.00 7.70   ? 94  TRP A N   1 
ATOM   771   C  CA  . TRP A  1 94  ? 17.406  -3.898  19.391  1.00 7.78   ? 94  TRP A CA  1 
ATOM   772   C  C   . TRP A  1 94  ? 16.022  -3.342  19.747  1.00 8.35   ? 94  TRP A C   1 
ATOM   773   O  O   . TRP A  1 94  ? 15.684  -2.168  19.530  1.00 8.51   ? 94  TRP A O   1 
ATOM   774   C  CB  . TRP A  1 94  ? 18.190  -4.317  20.643  1.00 8.87   ? 94  TRP A CB  1 
ATOM   775   C  CG  . TRP A  1 94  ? 18.477  -3.172  21.582  1.00 8.48   ? 94  TRP A CG  1 
ATOM   776   C  CD1 . TRP A  1 94  ? 17.669  -2.679  22.600  1.00 9.31   ? 94  TRP A CD1 1 
ATOM   777   C  CD2 . TRP A  1 94  ? 19.680  -2.359  21.599  1.00 8.81   ? 94  TRP A CD2 1 
ATOM   778   N  NE1 . TRP A  1 94  ? 18.288  -1.642  23.228  1.00 10.05  ? 94  TRP A NE1 1 
ATOM   779   C  CE2 . TRP A  1 94  ? 19.523  -1.431  22.651  1.00 9.50   ? 94  TRP A CE2 1 
ATOM   780   C  CE3 . TRP A  1 94  ? 20.849  -2.292  20.822  1.00 8.70   ? 94  TRP A CE3 1 
ATOM   781   C  CZ2 . TRP A  1 94  ? 20.496  -0.493  22.968  1.00 10.52  ? 94  TRP A CZ2 1 
ATOM   782   C  CZ3 . TRP A  1 94  ? 21.804  -1.376  21.112  1.00 8.99   ? 94  TRP A CZ3 1 
ATOM   783   C  CH2 . TRP A  1 94  ? 21.643  -0.471  22.141  1.00 9.82   ? 94  TRP A CH2 1 
ATOM   784   N  N   . GLY A  1 95  ? 15.206  -4.234  20.313  1.00 8.81   ? 95  GLY A N   1 
ATOM   785   C  CA  . GLY A  1 95  ? 13.822  -3.955  20.694  1.00 9.50   ? 95  GLY A CA  1 
ATOM   786   C  C   . GLY A  1 95  ? 13.702  -3.666  22.174  1.00 9.20   ? 95  GLY A C   1 
ATOM   787   O  O   . GLY A  1 95  ? 14.363  -2.767  22.712  1.00 10.16  ? 95  GLY A O   1 
ATOM   788   N  N   . ASN A  1 96  ? 12.870  -4.439  22.843  1.00 9.80   ? 96  ASN A N   1 
ATOM   789   C  CA  . ASN A  1 96  ? 12.696  -4.258  24.280  1.00 10.33  ? 96  ASN A CA  1 
ATOM   790   C  C   . ASN A  1 96  ? 12.221  -5.583  24.846  1.00 10.44  ? 96  ASN A C   1 
ATOM   791   O  O   . ASN A  1 96  ? 11.770  -6.460  24.124  1.00 10.43  ? 96  ASN A O   1 
ATOM   792   C  CB  . ASN A  1 96  ? 11.739  -3.120  24.564  1.00 12.24  ? 96  ASN A CB  1 
ATOM   793   C  CG  . ASN A  1 96  ? 10.320  -3.497  24.326  1.00 11.94  ? 96  ASN A CG  1 
ATOM   794   O  OD1 . ASN A  1 96  ? 9.657   -4.016  25.207  1.00 16.80  ? 96  ASN A OD1 1 
ATOM   795   N  ND2 . ASN A  1 96  ? 9.797   -3.160  23.133  1.00 15.00  ? 96  ASN A ND2 1 
ATOM   796   N  N   . PRO A  1 97  ? 12.264  -5.733  26.190  1.00 10.89  ? 97  PRO A N   1 
ATOM   797   C  CA  . PRO A  1 97  ? 11.967  -7.084  26.696  1.00 11.92  ? 97  PRO A CA  1 
ATOM   798   C  C   . PRO A  1 97  ? 10.526  -7.544  26.487  1.00 11.46  ? 97  PRO A C   1 
ATOM   799   O  O   . PRO A  1 97  ? 10.272  -8.742  26.491  1.00 13.75  ? 97  PRO A O   1 
ATOM   800   C  CB  . PRO A  1 97  ? 12.290  -6.925  28.244  1.00 13.95  ? 97  PRO A CB  1 
ATOM   801   C  CG  . PRO A  1 97  ? 13.395  -5.871  28.255  1.00 13.52  ? 97  PRO A CG  1 
ATOM   802   C  CD  . PRO A  1 97  ? 12.913  -4.912  27.206  1.00 12.95  ? 97  PRO A CD  1 
ATOM   803   N  N   A ASN A  1 98  ? 9.588   -6.605  26.353  0.50 10.97  ? 98  ASN A N   1 
ATOM   804   N  N   B ASN A  1 98  ? 9.575   -6.604  26.351  0.50 11.08  ? 98  ASN A N   1 
ATOM   805   C  CA  A ASN A  1 98  ? 8.234   -7.004  26.077  0.50 11.20  ? 98  ASN A CA  1 
ATOM   806   C  CA  B ASN A  1 98  ? 8.183   -6.949  26.062  0.50 12.59  ? 98  ASN A CA  1 
ATOM   807   C  C   A ASN A  1 98  ? 7.985   -7.321  24.620  0.50 11.73  ? 98  ASN A C   1 
ATOM   808   C  C   B ASN A  1 98  ? 7.963   -7.307  24.601  0.50 12.27  ? 98  ASN A C   1 
ATOM   809   O  O   A ASN A  1 98  ? 6.952   -7.925  24.296  0.50 14.60  ? 98  ASN A O   1 
ATOM   810   O  O   B ASN A  1 98  ? 6.935   -7.913  24.251  0.50 14.52  ? 98  ASN A O   1 
ATOM   811   C  CB  A ASN A  1 98  ? 7.268   -5.889  26.521  0.50 11.29  ? 98  ASN A CB  1 
ATOM   812   C  CB  B ASN A  1 98  ? 7.274   -5.747  26.425  0.50 16.28  ? 98  ASN A CB  1 
ATOM   813   C  CG  A ASN A  1 98  ? 7.171   -5.788  27.999  0.50 14.24  ? 98  ASN A CG  1 
ATOM   814   C  CG  B ASN A  1 98  ? 5.876   -6.157  26.791  0.50 27.82  ? 98  ASN A CG  1 
ATOM   815   O  OD1 A ASN A  1 98  ? 7.249   -6.776  28.726  0.50 18.53  ? 98  ASN A OD1 1 
ATOM   816   O  OD1 B ASN A  1 98  ? 5.620   -7.312  27.069  0.50 38.13  ? 98  ASN A OD1 1 
ATOM   817   N  ND2 A ASN A  1 98  ? 6.887   -4.599  28.476  0.50 21.94  ? 98  ASN A ND2 1 
ATOM   818   N  ND2 B ASN A  1 98  ? 4.969   -5.194  26.854  0.50 39.69  ? 98  ASN A ND2 1 
ATOM   819   N  N   . ASP A  1 99  ? 8.897   -6.964  23.706  1.00 11.47  ? 99  ASP A N   1 
ATOM   820   C  CA  . ASP A  1 99  ? 8.746   -7.241  22.293  1.00 11.41  ? 99  ASP A CA  1 
ATOM   821   C  C   . ASP A  1 99  ? 10.165  -7.338  21.747  1.00 10.21  ? 99  ASP A C   1 
ATOM   822   O  O   . ASP A  1 99  ? 10.694  -6.365  21.126  1.00 10.91  ? 99  ASP A O   1 
ATOM   823   C  CB  . ASP A  1 99  ? 7.908   -6.140  21.633  1.00 11.92  ? 99  ASP A CB  1 
ATOM   824   C  CG  . ASP A  1 99  ? 7.344   -6.521  20.322  1.00 12.26  ? 99  ASP A CG  1 
ATOM   825   O  OD1 . ASP A  1 99  ? 7.735   -7.532  19.730  1.00 15.60  ? 99  ASP A OD1 1 
ATOM   826   O  OD2 . ASP A  1 99  ? 6.474   -5.812  19.818  1.00 16.79  ? 99  ASP A OD2 1 
ATOM   827   N  N   . PRO A  1 100 ? 10.829  -8.449  22.004  1.00 10.37  ? 100 PRO A N   1 
ATOM   828   C  CA  . PRO A  1 100 ? 12.301  -8.562  21.779  1.00 10.76  ? 100 PRO A CA  1 
ATOM   829   C  C   . PRO A  1 100 ? 12.619  -8.905  20.324  1.00 9.51   ? 100 PRO A C   1 
ATOM   830   O  O   . PRO A  1 100 ? 13.212  -9.900  20.035  1.00 12.32  ? 100 PRO A O   1 
ATOM   831   C  CB  . PRO A  1 100 ? 12.684  -9.648  22.767  1.00 11.50  ? 100 PRO A CB  1 
ATOM   832   C  CG  . PRO A  1 100 ? 11.488  -10.521 22.759  1.00 11.86  ? 100 PRO A CG  1 
ATOM   833   C  CD  . PRO A  1 100 ? 10.312  -9.585  22.793  1.00 11.65  ? 100 PRO A CD  1 
ATOM   834   N  N   . HIS A  1 101 ? 12.220  -7.983  19.439  1.00 9.90   ? 101 HIS A N   1 
ATOM   835   C  CA  . HIS A  1 101 ? 12.269  -8.203  17.965  1.00 11.43  ? 101 HIS A CA  1 
ATOM   836   C  C   . HIS A  1 101 ? 12.673  -6.955  17.271  1.00 10.10  ? 101 HIS A C   1 
ATOM   837   O  O   . HIS A  1 101 ? 11.884  -6.445  16.484  1.00 14.11  ? 101 HIS A O   1 
ATOM   838   C  CB  . HIS A  1 101 ? 10.910  -8.723  17.448  1.00 13.20  ? 101 HIS A CB  1 
ATOM   839   C  CG  . HIS A  1 101 ? 10.376  -9.906  18.215  1.00 13.51  ? 101 HIS A CG  1 
ATOM   840   N  ND1 . HIS A  1 101 ? 10.869  -11.167 18.143  1.00 16.31  ? 101 HIS A ND1 1 
ATOM   841   C  CD2 . HIS A  1 101 ? 9.382   -9.919  19.171  1.00 12.74  ? 101 HIS A CD2 1 
ATOM   842   C  CE1 . HIS A  1 101 ? 10.148  -11.946 19.004  1.00 16.30  ? 101 HIS A CE1 1 
ATOM   843   N  NE2 . HIS A  1 101 ? 9.275   -11.158 19.628  1.00 16.01  ? 101 HIS A NE2 1 
ATOM   844   N  N   . GLY A  1 102 ? 13.855  -6.510  17.512  1.00 9.14   ? 102 GLY A N   1 
ATOM   845   C  CA  . GLY A  1 102 ? 14.316  -5.173  17.151  1.00 9.77   ? 102 GLY A CA  1 
ATOM   846   C  C   . GLY A  1 102 ? 15.392  -5.112  16.070  1.00 8.16   ? 102 GLY A C   1 
ATOM   847   O  O   . GLY A  1 102 ? 16.098  -4.124  15.999  1.00 9.18   ? 102 GLY A O   1 
ATOM   848   N  N   . SER A  1 103 ? 15.522  -6.167  15.242  1.00 8.14   ? 103 SER A N   1 
ATOM   849   C  CA  . SER A  1 103 ? 16.386  -6.001  14.065  1.00 7.72   ? 103 SER A CA  1 
ATOM   850   C  C   . SER A  1 103 ? 15.806  -4.903  13.181  1.00 8.05   ? 103 SER A C   1 
ATOM   851   O  O   . SER A  1 103 ? 14.603  -4.590  13.243  1.00 10.08  ? 103 SER A O   1 
ATOM   852   C  CB  . SER A  1 103 ? 16.544  -7.275  13.277  1.00 8.01   ? 103 SER A CB  1 
ATOM   853   O  OG  . SER A  1 103 ? 15.296  -7.694  12.693  1.00 8.42   ? 103 SER A OG  1 
ATOM   854   N  N   . GLU A  1 104 ? 16.644  -4.359  12.335  1.00 7.24   ? 104 GLU A N   1 
ATOM   855   C  CA  . GLU A  1 104 ? 16.171  -3.395  11.313  1.00 7.70   ? 104 GLU A CA  1 
ATOM   856   C  C   . GLU A  1 104 ? 15.692  -4.075  10.068  1.00 7.62   ? 104 GLU A C   1 
ATOM   857   O  O   . GLU A  1 104 ? 14.542  -3.872  9.643   1.00 7.78   ? 104 GLU A O   1 
ATOM   858   C  CB  . GLU A  1 104 ? 17.332  -2.428  10.996  1.00 8.17   ? 104 GLU A CB  1 
ATOM   859   C  CG  . GLU A  1 104 ? 17.869  -1.735  12.242  1.00 9.11   ? 104 GLU A CG  1 
ATOM   860   C  CD  . GLU A  1 104 ? 18.247  -0.299  11.944  1.00 7.90   ? 104 GLU A CD  1 
ATOM   861   O  OE1 . GLU A  1 104 ? 19.298  -0.105  11.352  1.00 8.99   ? 104 GLU A OE1 1 
ATOM   862   O  OE2 . GLU A  1 104 ? 17.413  0.613   12.199  1.00 9.49   ? 104 GLU A OE2 1 
ATOM   863   N  N   . HIS A  1 105 ? 16.533  -4.895  9.451   1.00 7.55   ? 105 HIS A N   1 
ATOM   864   C  CA  . HIS A  1 105 ? 16.043  -5.716  8.341   1.00 7.61   ? 105 HIS A CA  1 
ATOM   865   C  C   . HIS A  1 105 ? 15.129  -6.783  8.854   1.00 7.74   ? 105 HIS A C   1 
ATOM   866   O  O   . HIS A  1 105 ? 15.318  -7.312  9.969   1.00 8.59   ? 105 HIS A O   1 
ATOM   867   C  CB  . HIS A  1 105 ? 17.238  -6.303  7.595   1.00 8.47   ? 105 HIS A CB  1 
ATOM   868   C  CG  . HIS A  1 105 ? 18.029  -5.269  6.876   1.00 7.38   ? 105 HIS A CG  1 
ATOM   869   N  ND1 . HIS A  1 105 ? 19.077  -4.588  7.455   1.00 8.62   ? 105 HIS A ND1 1 
ATOM   870   C  CD2 . HIS A  1 105 ? 17.853  -4.716  5.632   1.00 7.77   ? 105 HIS A CD2 1 
ATOM   871   C  CE1 . HIS A  1 105 ? 19.503  -3.656  6.557   1.00 8.52   ? 105 HIS A CE1 1 
ATOM   872   N  NE2 . HIS A  1 105 ? 18.798  -3.743  5.463   1.00 8.62   ? 105 HIS A NE2 1 
ATOM   873   N  N   . THR A  1 106 ? 14.190  -7.184  8.049   1.00 7.72   ? 106 THR A N   1 
ATOM   874   C  CA  . THR A  1 106 ? 13.331  -8.334  8.330   1.00 8.25   ? 106 THR A CA  1 
ATOM   875   C  C   . THR A  1 106 ? 13.506  -9.326  7.209   1.00 8.31   ? 106 THR A C   1 
ATOM   876   O  O   . THR A  1 106 ? 13.984  -8.996  6.097   1.00 8.66   ? 106 THR A O   1 
ATOM   877   C  CB  . THR A  1 106 ? 11.864  -7.934  8.462   1.00 8.78   ? 106 THR A CB  1 
ATOM   878   O  OG1 . THR A  1 106 ? 11.411  -7.294  7.263   1.00 9.50   ? 106 THR A OG1 1 
ATOM   879   C  CG2 . THR A  1 106 ? 11.692  -6.962  9.568   1.00 9.52   ? 106 THR A CG2 1 
ATOM   880   N  N   . VAL A  1 107 ? 13.163  -10.594 7.478   1.00 8.61   ? 107 VAL A N   1 
ATOM   881   C  CA  . VAL A  1 107 ? 13.258  -11.671 6.495   1.00 9.41   ? 107 VAL A CA  1 
ATOM   882   C  C   . VAL A  1 107 ? 11.877  -12.293 6.403   1.00 9.64   ? 107 VAL A C   1 
ATOM   883   O  O   . VAL A  1 107 ? 11.368  -12.765 7.414   1.00 10.69  ? 107 VAL A O   1 
ATOM   884   C  CB  . VAL A  1 107 ? 14.291  -12.733 6.800   1.00 10.41  ? 107 VAL A CB  1 
ATOM   885   C  CG1 . VAL A  1 107 ? 14.263  -13.829 5.768   1.00 12.72  ? 107 VAL A CG1 1 
ATOM   886   C  CG2 . VAL A  1 107 ? 15.696  -12.082 6.922   1.00 12.75  ? 107 VAL A CG2 1 
ATOM   887   N  N   . SER A  1 108 ? 11.246  -12.186 5.229   1.00 10.54  ? 108 SER A N   1 
ATOM   888   C  CA  . SER A  1 108 ? 9.903   -12.690 5.042   1.00 11.19  ? 108 SER A CA  1 
ATOM   889   C  C   . SER A  1 108 ? 9.002   -12.129 6.120   1.00 10.56  ? 108 SER A C   1 
ATOM   890   O  O   . SER A  1 108 ? 8.110   -12.815 6.687   1.00 12.18  ? 108 SER A O   1 
ATOM   891   C  CB  . SER A  1 108 ? 9.890   -14.241 5.058   1.00 14.96  ? 108 SER A CB  1 
ATOM   892   O  OG  . SER A  1 108 ? 10.685  -14.754 4.006   1.00 19.22  ? 108 SER A OG  1 
ATOM   893   N  N   . GLY A  1 109 ? 9.150   -10.832 6.371   1.00 10.19  ? 109 GLY A N   1 
ATOM   894   C  CA  . GLY A  1 109 ? 8.311   -10.102 7.274   1.00 10.54  ? 109 GLY A CA  1 
ATOM   895   C  C   . GLY A  1 109 ? 8.655   -10.244 8.746   1.00 11.88  ? 109 GLY A C   1 
ATOM   896   O  O   . GLY A  1 109 ? 7.979   -9.577  9.551   1.00 13.90  ? 109 GLY A O   1 
ATOM   897   N  N   . GLN A  1 110 ? 9.643   -11.063 9.093   1.00 10.43  ? 110 GLN A N   1 
ATOM   898   C  CA  . GLN A  1 110 ? 9.977   -11.323 10.463  1.00 10.53  ? 110 GLN A CA  1 
ATOM   899   C  C   . GLN A  1 110 ? 11.206  -10.614 10.918  1.00 8.83   ? 110 GLN A C   1 
ATOM   900   O  O   . GLN A  1 110 ? 12.223  -10.620 10.266  1.00 9.40   ? 110 GLN A O   1 
ATOM   901   C  CB  . GLN A  1 110 ? 10.217  -12.804 10.703  1.00 11.34  ? 110 GLN A CB  1 
ATOM   902   C  CG  . GLN A  1 110 ? 9.101   -13.662 10.088  1.00 13.13  ? 110 GLN A CG  1 
ATOM   903   C  CD  . GLN A  1 110 ? 7.712   -13.255 10.473  1.00 14.60  ? 110 GLN A CD  1 
ATOM   904   O  OE1 . GLN A  1 110 ? 7.407   -13.212 11.664  1.00 15.42  ? 110 GLN A OE1 1 
ATOM   905   N  NE2 . GLN A  1 110 ? 6.847   -12.925 9.484   1.00 16.08  ? 110 GLN A NE2 1 
ATOM   906   N  N   . HIS A  1 111 ? 11.101  -9.936  12.078  1.00 9.94   ? 111 HIS A N   1 
ATOM   907   C  CA  . HIS A  1 111 ? 12.250  -9.376  12.745  1.00 9.86   ? 111 HIS A CA  1 
ATOM   908   C  C   . HIS A  1 111 ? 13.060  -10.469 13.414  1.00 10.84  ? 111 HIS A C   1 
ATOM   909   O  O   . HIS A  1 111 ? 12.559  -11.527 13.785  1.00 16.32  ? 111 HIS A O   1 
ATOM   910   C  CB  . HIS A  1 111 ? 11.885  -8.411  13.835  1.00 11.93  ? 111 HIS A CB  1 
ATOM   911   C  CG  . HIS A  1 111 ? 11.386  -7.087  13.347  1.00 10.63  ? 111 HIS A CG  1 
ATOM   912   N  ND1 . HIS A  1 111 ? 10.123  -6.733  12.958  1.00 16.04  ? 111 HIS A ND1 1 
ATOM   913   C  CD2 . HIS A  1 111 ? 12.172  -5.990  13.154  1.00 9.91   ? 111 HIS A CD2 1 
ATOM   914   C  CE1 . HIS A  1 111 ? 10.141  -5.476  12.577  1.00 14.45  ? 111 HIS A CE1 1 
ATOM   915   N  NE2 . HIS A  1 111 ? 11.413  -5.032  12.616  1.00 15.79  ? 111 HIS A NE2 1 
ATOM   916   N  N   . PHE A  1 112 ? 14.324  -10.209 13.570  1.00 9.55   ? 112 PHE A N   1 
ATOM   917   C  CA  . PHE A  1 112 ? 15.191  -10.919 14.486  1.00 9.44   ? 112 PHE A CA  1 
ATOM   918   C  C   . PHE A  1 112 ? 15.259  -10.118 15.779  1.00 8.55   ? 112 PHE A C   1 
ATOM   919   O  O   . PHE A  1 112 ? 14.746  -8.979  15.847  1.00 9.24   ? 112 PHE A O   1 
ATOM   920   C  CB  . PHE A  1 112 ? 16.569  -11.148 13.832  1.00 9.59   ? 112 PHE A CB  1 
ATOM   921   C  CG  . PHE A  1 112 ? 16.513  -12.222 12.776  1.00 10.86  ? 112 PHE A CG  1 
ATOM   922   C  CD1 . PHE A  1 112 ? 15.936  -11.988 11.517  1.00 14.23  ? 112 PHE A CD1 1 
ATOM   923   C  CD2 . PHE A  1 112 ? 16.920  -13.511 13.120  1.00 13.95  ? 112 PHE A CD2 1 
ATOM   924   C  CE1 . PHE A  1 112 ? 15.870  -13.043 10.569  1.00 16.69  ? 112 PHE A CE1 1 
ATOM   925   C  CE2 . PHE A  1 112 ? 16.889  -14.556 12.167  1.00 17.95  ? 112 PHE A CE2 1 
ATOM   926   C  CZ  . PHE A  1 112 ? 16.327  -14.312 10.939  1.00 21.76  ? 112 PHE A CZ  1 
ATOM   927   N  N   . ALA A  1 113 ? 15.859  -10.701 16.786  1.00 8.71   ? 113 ALA A N   1 
ATOM   928   C  CA  . ALA A  1 113 ? 15.937  -10.022 18.095  1.00 9.00   ? 113 ALA A CA  1 
ATOM   929   C  C   . ALA A  1 113 ? 16.691  -8.726  18.024  1.00 8.76   ? 113 ALA A C   1 
ATOM   930   O  O   . ALA A  1 113 ? 16.330  -7.739  18.686  1.00 8.57   ? 113 ALA A O   1 
ATOM   931   C  CB  . ALA A  1 113 ? 16.509  -10.945 19.155  1.00 10.98  ? 113 ALA A CB  1 
ATOM   932   N  N   . ALA A  1 114 ? 17.816  -8.705  17.272  1.00 8.57   ? 114 ALA A N   1 
ATOM   933   C  CA  . ALA A  1 114 ? 18.671  -7.503  17.248  1.00 8.19   ? 114 ALA A CA  1 
ATOM   934   C  C   . ALA A  1 114 ? 19.452  -7.557  15.945  1.00 7.33   ? 114 ALA A C   1 
ATOM   935   O  O   . ALA A  1 114 ? 19.387  -8.562  15.212  1.00 7.89   ? 114 ALA A O   1 
ATOM   936   C  CB  . ALA A  1 114 ? 19.589  -7.470  18.485  1.00 9.20   ? 114 ALA A CB  1 
ATOM   937   N  N   . GLU A  1 115 ? 20.282  -6.555  15.741  1.00 7.62   ? 115 GLU A N   1 
ATOM   938   C  CA  . GLU A  1 115 ? 21.078  -6.503  14.505  1.00 7.57   ? 115 GLU A CA  1 
ATOM   939   C  C   . GLU A  1 115 ? 22.363  -5.743  14.803  1.00 7.89   ? 115 GLU A C   1 
ATOM   940   O  O   . GLU A  1 115 ? 22.306  -4.656  15.435  1.00 9.00   ? 115 GLU A O   1 
ATOM   941   C  CB  . GLU A  1 115 ? 20.256  -5.880  13.380  1.00 7.75   ? 115 GLU A CB  1 
ATOM   942   C  CG  . GLU A  1 115 ? 20.895  -5.896  12.016  1.00 8.61   ? 115 GLU A CG  1 
ATOM   943   C  CD  . GLU A  1 115 ? 19.948  -5.513  10.904  1.00 7.99   ? 115 GLU A CD  1 
ATOM   944   O  OE1 . GLU A  1 115 ? 18.733  -5.738  11.036  1.00 8.56   ? 115 GLU A OE1 1 
ATOM   945   O  OE2 . GLU A  1 115 ? 20.411  -4.970  9.856   1.00 8.42   ? 115 GLU A OE2 1 
ATOM   946   N  N   . LEU A  1 116 ? 23.494  -6.291  14.373  1.00 7.77   ? 116 LEU A N   1 
ATOM   947   C  CA  . LEU A  1 116 ? 24.777  -5.663  14.495  1.00 7.89   ? 116 LEU A CA  1 
ATOM   948   C  C   . LEU A  1 116 ? 25.113  -5.079  13.105  1.00 7.22   ? 116 LEU A C   1 
ATOM   949   O  O   . LEU A  1 116 ? 24.994  -5.764  12.091  1.00 7.57   ? 116 LEU A O   1 
ATOM   950   C  CB  . LEU A  1 116 ? 25.839  -6.696  14.889  1.00 8.88   ? 116 LEU A CB  1 
ATOM   951   C  CG  . LEU A  1 116 ? 27.333  -6.269  14.770  1.00 10.30  ? 116 LEU A CG  1 
ATOM   952   C  CD1 . LEU A  1 116 ? 27.668  -5.383  15.883  1.00 13.21  ? 116 LEU A CD1 1 
ATOM   953   C  CD2 . LEU A  1 116 ? 28.248  -7.514  14.697  1.00 13.30  ? 116 LEU A CD2 1 
ATOM   954   N  N   . HIS A  1 117 ? 25.666  -3.857  13.140  1.00 7.35   ? 117 HIS A N   1 
ATOM   955   C  CA  . HIS A  1 117 ? 26.184  -3.207  11.921  1.00 7.12   ? 117 HIS A CA  1 
ATOM   956   C  C   . HIS A  1 117 ? 27.617  -2.887  12.089  1.00 7.27   ? 117 HIS A C   1 
ATOM   957   O  O   . HIS A  1 117 ? 28.000  -2.250  13.064  1.00 8.33   ? 117 HIS A O   1 
ATOM   958   C  CB  . HIS A  1 117 ? 25.392  -1.903  11.691  1.00 8.17   ? 117 HIS A CB  1 
ATOM   959   C  CG  . HIS A  1 117 ? 23.993  -2.143  11.259  1.00 7.40   ? 117 HIS A CG  1 
ATOM   960   N  ND1 . HIS A  1 117 ? 22.980  -1.222  11.407  1.00 7.61   ? 117 HIS A ND1 1 
ATOM   961   C  CD2 . HIS A  1 117 ? 23.451  -3.276  10.696  1.00 8.20   ? 117 HIS A CD2 1 
ATOM   962   C  CE1 . HIS A  1 117 ? 21.860  -1.789  10.915  1.00 7.67   ? 117 HIS A CE1 1 
ATOM   963   N  NE2 . HIS A  1 117 ? 22.124  -3.024  10.491  1.00 8.09   ? 117 HIS A NE2 1 
ATOM   964   N  N   . ILE A  1 118 ? 28.435  -3.298  11.102  1.00 8.39   ? 118 ILE A N   1 
ATOM   965   C  CA  . ILE A  1 118 ? 29.861  -2.957  11.087  1.00 8.59   ? 118 ILE A CA  1 
ATOM   966   C  C   . ILE A  1 118 ? 30.006  -2.041  9.874   1.00 8.97   ? 118 ILE A C   1 
ATOM   967   O  O   . ILE A  1 118 ? 29.868  -2.425  8.708   1.00 8.66   ? 118 ILE A O   1 
ATOM   968   C  CB  . ILE A  1 118 ? 30.758  -4.201  10.940  1.00 9.03   ? 118 ILE A CB  1 
ATOM   969   C  CG1 . ILE A  1 118 ? 30.381  -5.285  11.956  1.00 10.00  ? 118 ILE A CG1 1 
ATOM   970   C  CG2 . ILE A  1 118 ? 32.218  -3.733  11.094  1.00 10.81  ? 118 ILE A CG2 1 
ATOM   971   C  CD1 . ILE A  1 118 ? 31.220  -6.522  11.854  1.00 12.48  ? 118 ILE A CD1 1 
ATOM   972   N  N   . VAL A  1 119 ? 30.260  -0.775  10.198  1.00 9.11   ? 119 VAL A N   1 
ATOM   973   C  CA  . VAL A  1 119 ? 30.270  0.333   9.224   1.00 9.46   ? 119 VAL A CA  1 
ATOM   974   C  C   . VAL A  1 119 ? 31.667  0.531   8.693   1.00 8.65   ? 119 VAL A C   1 
ATOM   975   O  O   . VAL A  1 119 ? 32.621  0.663   9.439   1.00 10.63  ? 119 VAL A O   1 
ATOM   976   C  CB  . VAL A  1 119 ? 29.797  1.637   9.896   1.00 10.32  ? 119 VAL A CB  1 
ATOM   977   C  CG1 . VAL A  1 119 ? 29.710  2.795   8.892   1.00 12.00  ? 119 VAL A CG1 1 
ATOM   978   C  CG2 . VAL A  1 119 ? 28.415  1.444   10.577  1.00 10.91  ? 119 VAL A CG2 1 
ATOM   979   N  N   . HIS A  1 120 ? 31.732  0.576   7.368   1.00 9.96   ? 120 HIS A N   1 
ATOM   980   C  CA  . HIS A  1 120 ? 33.024  0.842   6.633   1.00 10.54  ? 120 HIS A CA  1 
ATOM   981   C  C   . HIS A  1 120 ? 32.797  1.973   5.666   1.00 9.96   ? 120 HIS A C   1 
ATOM   982   O  O   . HIS A  1 120 ? 31.694  2.252   5.238   1.00 10.70  ? 120 HIS A O   1 
ATOM   983   C  CB  . HIS A  1 120 ? 33.429  -0.411  5.853   1.00 11.24  ? 120 HIS A CB  1 
ATOM   984   C  CG  . HIS A  1 120 ? 33.568  -1.670  6.626   1.00 10.19  ? 120 HIS A CG  1 
ATOM   985   N  ND1 . HIS A  1 120 ? 32.492  -2.374  7.193   1.00 10.34  ? 120 HIS A ND1 1 
ATOM   986   C  CD2 . HIS A  1 120 ? 34.652  -2.427  6.908   1.00 11.06  ? 120 HIS A CD2 1 
ATOM   987   C  CE1 . HIS A  1 120 ? 32.965  -3.498  7.738   1.00 10.31  ? 120 HIS A CE1 1 
ATOM   988   N  NE2 . HIS A  1 120 ? 34.252  -3.563  7.614   1.00 10.44  ? 120 HIS A NE2 1 
ATOM   989   N  N   . TYR A  1 121 ? 33.896  2.643   5.297   1.00 12.04  ? 121 TYR A N   1 
ATOM   990   C  CA  . TYR A  1 121 ? 33.859  3.738   4.340   1.00 12.22  ? 121 TYR A CA  1 
ATOM   991   C  C   . TYR A  1 121 ? 34.841  3.511   3.223   1.00 12.59  ? 121 TYR A C   1 
ATOM   992   O  O   . TYR A  1 121 ? 35.846  2.798   3.378   1.00 12.47  ? 121 TYR A O   1 
ATOM   993   C  CB  . TYR A  1 121 ? 34.110  5.124   4.993   1.00 13.90  ? 121 TYR A CB  1 
ATOM   994   C  CG  . TYR A  1 121 ? 35.530  5.307   5.503   1.00 13.57  ? 121 TYR A CG  1 
ATOM   995   C  CD1 . TYR A  1 121 ? 35.948  4.715   6.719   1.00 13.90  ? 121 TYR A CD1 1 
ATOM   996   C  CD2 . TYR A  1 121 ? 36.457  6.026   4.766   1.00 16.64  ? 121 TYR A CD2 1 
ATOM   997   C  CE1 . TYR A  1 121 ? 37.220  4.834   7.201   1.00 16.95  ? 121 TYR A CE1 1 
ATOM   998   C  CE2 . TYR A  1 121 ? 37.791  6.140   5.242   1.00 17.41  ? 121 TYR A CE2 1 
ATOM   999   C  CZ  . TYR A  1 121 ? 38.154  5.534   6.449   1.00 18.92  ? 121 TYR A CZ  1 
ATOM   1000  O  OH  . TYR A  1 121 ? 39.450  5.701   6.905   1.00 21.64  ? 121 TYR A OH  1 
ATOM   1001  N  N   . ASN A  1 122 ? 34.624  4.141   2.067   1.00 13.60  ? 122 ASN A N   1 
ATOM   1002  C  CA  . ASN A  1 122 ? 35.441  3.973   0.924   1.00 15.62  ? 122 ASN A CA  1 
ATOM   1003  C  C   . ASN A  1 122 ? 36.726  4.786   1.127   1.00 16.51  ? 122 ASN A C   1 
ATOM   1004  O  O   . ASN A  1 122 ? 36.756  6.037   0.906   1.00 16.74  ? 122 ASN A O   1 
ATOM   1005  C  CB  . ASN A  1 122 ? 34.703  4.489   -0.304  1.00 16.21  ? 122 ASN A CB  1 
ATOM   1006  C  CG  . ASN A  1 122 ? 35.395  4.113   -1.546  1.00 20.58  ? 122 ASN A CG  1 
ATOM   1007  O  OD1 . ASN A  1 122 ? 36.660  4.101   -1.596  1.00 20.33  ? 122 ASN A OD1 1 
ATOM   1008  N  ND2 . ASN A  1 122 ? 34.627  3.808   -2.597  1.00 23.93  ? 122 ASN A ND2 1 
ATOM   1009  N  N   . SER A  1 123 ? 37.772  4.129   1.605   1.00 14.44  ? 123 SER A N   1 
ATOM   1010  C  CA  . SER A  1 123 ? 39.032  4.814   1.913   1.00 15.64  ? 123 SER A CA  1 
ATOM   1011  C  C   . SER A  1 123 ? 39.865  4.979   0.690   1.00 17.09  ? 123 SER A C   1 
ATOM   1012  O  O   . SER A  1 123 ? 40.877  5.717   0.752   1.00 18.10  ? 123 SER A O   1 
ATOM   1013  C  CB  . SER A  1 123 ? 39.800  3.952   2.969   1.00 15.38  ? 123 SER A CB  1 
ATOM   1014  O  OG  . SER A  1 123 ? 39.821  2.608   2.606   1.00 15.37  ? 123 SER A OG  1 
ATOM   1015  N  N   . ASP A  1 124 ? 39.539  4.352   -0.440  1.00 16.23  ? 124 ASP A N   1 
ATOM   1016  C  CA  . ASP A  1 124 ? 40.235  4.708   -1.640  1.00 19.64  ? 124 ASP A CA  1 
ATOM   1017  C  C   . ASP A  1 124 ? 39.823  6.066   -2.165  1.00 23.43  ? 124 ASP A C   1 
ATOM   1018  O  O   . ASP A  1 124 ? 40.626  6.704   -2.770  1.00 28.64  ? 124 ASP A O   1 
ATOM   1019  C  CB  . ASP A  1 124 ? 39.918  3.718   -2.719  1.00 18.87  ? 124 ASP A CB  1 
ATOM   1020  C  CG  . ASP A  1 124 ? 40.595  2.341   -2.507  1.00 18.28  ? 124 ASP A CG  1 
ATOM   1021  O  OD1 . ASP A  1 124 ? 41.617  2.233   -1.768  1.00 18.94  ? 124 ASP A OD1 1 
ATOM   1022  O  OD2 . ASP A  1 124 ? 40.045  1.348   -3.023  1.00 20.67  ? 124 ASP A OD2 1 
ATOM   1023  N  N   . LEU A  1 125 ? 38.587  6.455   -1.926  1.00 21.82  ? 125 LEU A N   1 
ATOM   1024  C  CA  . LEU A  1 125 ? 38.056  7.746   -2.395  1.00 22.13  ? 125 LEU A CA  1 
ATOM   1025  C  C   . LEU A  1 125 ? 38.061  8.860   -1.363  1.00 26.09  ? 125 LEU A C   1 
ATOM   1026  O  O   . LEU A  1 125 ? 38.242  10.020  -1.785  1.00 33.50  ? 125 LEU A O   1 
ATOM   1027  C  CB  . LEU A  1 125 ? 36.616  7.564   -2.911  1.00 28.02  ? 125 LEU A CB  1 
ATOM   1028  C  CG  . LEU A  1 125 ? 36.340  6.895   -4.258  1.00 32.06  ? 125 LEU A CG  1 
ATOM   1029  C  CD1 . LEU A  1 125 ? 37.019  5.539   -4.350  1.00 42.02  ? 125 LEU A CD1 1 
ATOM   1030  C  CD2 . LEU A  1 125 ? 34.840  6.756   -4.480  1.00 41.07  ? 125 LEU A CD2 1 
ATOM   1031  N  N   . TYR A  1 126 ? 37.871  8.548   -0.062  1.00 22.48  ? 126 TYR A N   1 
ATOM   1032  C  CA  . TYR A  1 126 ? 37.685  9.564   0.976   1.00 23.87  ? 126 TYR A CA  1 
ATOM   1033  C  C   . TYR A  1 126 ? 38.637  9.419   2.162   1.00 18.84  ? 126 TYR A C   1 
ATOM   1034  O  O   . TYR A  1 126 ? 39.046  8.259   2.413   1.00 23.13  ? 126 TYR A O   1 
ATOM   1035  C  CB  . TYR A  1 126 ? 36.223  9.527   1.441   1.00 21.49  ? 126 TYR A CB  1 
ATOM   1036  C  CG  . TYR A  1 126 ? 35.231  9.540   0.257   1.00 23.32  ? 126 TYR A CG  1 
ATOM   1037  C  CD1 . TYR A  1 126 ? 35.165  10.637  -0.601  1.00 26.74  ? 126 TYR A CD1 1 
ATOM   1038  C  CD2 . TYR A  1 126 ? 34.423  8.436   -0.060  1.00 24.15  ? 126 TYR A CD2 1 
ATOM   1039  C  CE1 . TYR A  1 126 ? 34.314  10.629  -1.718  1.00 29.35  ? 126 TYR A CE1 1 
ATOM   1040  C  CE2 . TYR A  1 126 ? 33.540  8.452   -1.163  1.00 24.87  ? 126 TYR A CE2 1 
ATOM   1041  C  CZ  . TYR A  1 126 ? 33.464  9.566   -1.999  1.00 32.27  ? 126 TYR A CZ  1 
ATOM   1042  O  OH  . TYR A  1 126 ? 32.596  9.573   -3.117  1.00 50.19  ? 126 TYR A OH  1 
ATOM   1043  N  N   . PRO A  1 127 ? 38.861  10.514  2.905   1.00 23.13  ? 127 PRO A N   1 
ATOM   1044  C  CA  . PRO A  1 127 ? 39.889  10.411  3.905   1.00 25.64  ? 127 PRO A CA  1 
ATOM   1045  C  C   . PRO A  1 127 ? 39.385  9.831   5.195   1.00 23.88  ? 127 PRO A C   1 
ATOM   1046  O  O   . PRO A  1 127 ? 40.150  9.324   5.997   1.00 28.76  ? 127 PRO A O   1 
ATOM   1047  C  CB  . PRO A  1 127 ? 40.299  11.872  4.124   1.00 31.11  ? 127 PRO A CB  1 
ATOM   1048  C  CG  . PRO A  1 127 ? 39.106  12.677  3.755   1.00 30.50  ? 127 PRO A CG  1 
ATOM   1049  C  CD  . PRO A  1 127 ? 38.623  11.954  2.552   1.00 24.33  ? 127 PRO A CD  1 
ATOM   1050  N  N   . ASP A  1 128 ? 38.072  9.858   5.381   1.00 20.72  ? 128 ASP A N   1 
ATOM   1051  C  CA  . ASP A  1 128 ? 37.470  9.397   6.648   1.00 22.78  ? 128 ASP A CA  1 
ATOM   1052  C  C   . ASP A  1 128 ? 35.981  9.155   6.394   1.00 17.15  ? 128 ASP A C   1 
ATOM   1053  O  O   . ASP A  1 128 ? 35.422  9.490   5.337   1.00 18.87  ? 128 ASP A O   1 
ATOM   1054  C  CB  . ASP A  1 128 ? 37.731  10.397  7.786   1.00 26.07  ? 128 ASP A CB  1 
ATOM   1055  C  CG  . ASP A  1 128 ? 37.383  11.785  7.422   1.00 32.67  ? 128 ASP A CG  1 
ATOM   1056  O  OD1 . ASP A  1 128 ? 38.209  12.697  7.609   1.00 44.51  ? 128 ASP A OD1 1 
ATOM   1057  O  OD2 . ASP A  1 128 ? 36.295  11.994  6.920   1.00 28.77  ? 128 ASP A OD2 1 
ATOM   1058  N  N   . ALA A  1 129 ? 35.341  8.529   7.349   1.00 18.71  ? 129 ALA A N   1 
ATOM   1059  C  CA  . ALA A  1 129 ? 33.977  8.150   7.192   1.00 17.77  ? 129 ALA A CA  1 
ATOM   1060  C  C   . ALA A  1 129 ? 33.018  9.305   7.157   1.00 20.71  ? 129 ALA A C   1 
ATOM   1061  O  O   . ALA A  1 129 ? 32.038  9.259   6.428   1.00 20.10  ? 129 ALA A O   1 
ATOM   1062  C  CB  . ALA A  1 129 ? 33.568  7.188   8.311   1.00 21.26  ? 129 ALA A CB  1 
ATOM   1063  N  N   A SER A  1 130 ? 33.350  10.366  7.873   0.50 20.40  ? 130 SER A N   1 
ATOM   1064  N  N   B SER A  1 130 ? 33.233  10.336  7.959   0.50 21.22  ? 130 SER A N   1 
ATOM   1065  C  CA  A SER A  1 130 ? 32.448  11.472  8.005   0.50 24.52  ? 130 SER A CA  1 
ATOM   1066  C  CA  B SER A  1 130 ? 32.270  11.402  7.898   0.50 22.33  ? 130 SER A CA  1 
ATOM   1067  C  C   A SER A  1 130 ? 32.373  12.210  6.667   0.50 24.02  ? 130 SER A C   1 
ATOM   1068  C  C   B SER A  1 130 ? 32.284  11.955  6.472   0.50 23.20  ? 130 SER A C   1 
ATOM   1069  O  O   A SER A  1 130 ? 31.331  12.774  6.319   0.50 21.75  ? 130 SER A O   1 
ATOM   1070  O  O   B SER A  1 130 ? 31.219  12.115  5.863   0.50 19.34  ? 130 SER A O   1 
ATOM   1071  C  CB  A SER A  1 130 ? 32.934  12.397  9.118   0.50 25.47  ? 130 SER A CB  1 
ATOM   1072  C  CB  B SER A  1 130 ? 32.544  12.509  8.936   0.50 23.29  ? 130 SER A CB  1 
ATOM   1073  O  OG  A SER A  1 130 ? 32.333  13.663  8.980   0.50 31.78  ? 130 SER A OG  1 
ATOM   1074  O  OG  B SER A  1 130 ? 33.928  12.684  9.190   0.50 28.48  ? 130 SER A OG  1 
ATOM   1075  N  N   . THR A  1 131 ? 33.485  12.158  5.908   1.00 20.11  ? 131 THR A N   1 
ATOM   1076  C  CA  . THR A  1 131 ? 33.540  12.809  4.581   1.00 21.81  ? 131 THR A CA  1 
ATOM   1077  C  C   . THR A  1 131 ? 32.854  11.879  3.601   1.00 18.41  ? 131 THR A C   1 
ATOM   1078  O  O   . THR A  1 131 ? 32.155  12.339  2.712   1.00 22.23  ? 131 THR A O   1 
ATOM   1079  C  CB  . THR A  1 131 ? 35.012  13.047  4.146   1.00 21.81  ? 131 THR A CB  1 
ATOM   1080  O  OG1 . THR A  1 131 ? 35.653  13.863  5.134   1.00 28.06  ? 131 THR A OG1 1 
ATOM   1081  C  CG2 . THR A  1 131 ? 35.048  13.684  2.757   1.00 23.68  ? 131 THR A CG2 1 
ATOM   1082  N  N   . ALA A  1 132 ? 33.109  10.574  3.723   1.00 19.03  ? 132 ALA A N   1 
ATOM   1083  C  CA  . ALA A  1 132 ? 32.483  9.631   2.795   1.00 17.23  ? 132 ALA A CA  1 
ATOM   1084  C  C   . ALA A  1 132 ? 30.973  9.533   2.884   1.00 18.37  ? 132 ALA A C   1 
ATOM   1085  O  O   . ALA A  1 132 ? 30.319  9.114   1.911   1.00 18.00  ? 132 ALA A O   1 
ATOM   1086  C  CB  . ALA A  1 132 ? 33.022  8.221   3.008   1.00 17.94  ? 132 ALA A CB  1 
ATOM   1087  N  N   . SER A  1 133 ? 30.390  9.850   4.038   1.00 18.22  ? 133 SER A N   1 
ATOM   1088  C  CA  . SER A  1 133 ? 29.038  9.363   4.357   1.00 19.24  ? 133 SER A CA  1 
ATOM   1089  C  C   . SER A  1 133 ? 27.974  9.985   3.457   1.00 16.94  ? 133 SER A C   1 
ATOM   1090  O  O   . SER A  1 133 ? 26.929  9.377   3.263   1.00 18.26  ? 133 SER A O   1 
ATOM   1091  C  CB  . SER A  1 133 ? 28.746  9.579   5.838   1.00 22.57  ? 133 SER A CB  1 
ATOM   1092  O  OG  . SER A  1 133 ? 28.593  10.966  6.113   1.00 24.13  ? 133 SER A OG  1 
ATOM   1093  N  N   . ASN A  1 134 ? 28.223  11.183  2.926   1.00 21.51  ? 134 ASN A N   1 
ATOM   1094  C  CA  . ASN A  1 134 ? 27.254  11.772  2.064   1.00 22.19  ? 134 ASN A CA  1 
ATOM   1095  C  C   . ASN A  1 134 ? 27.712  11.754  0.593   1.00 21.69  ? 134 ASN A C   1 
ATOM   1096  O  O   . ASN A  1 134 ? 27.193  12.507  -0.239  1.00 31.43  ? 134 ASN A O   1 
ATOM   1097  C  CB  . ASN A  1 134 ? 26.883  13.176  2.538   1.00 27.79  ? 134 ASN A CB  1 
ATOM   1098  C  CG  . ASN A  1 134 ? 27.995  14.171  2.278   1.00 31.44  ? 134 ASN A CG  1 
ATOM   1099  O  OD1 . ASN A  1 134 ? 29.160  13.801  2.140   1.00 32.65  ? 134 ASN A OD1 1 
ATOM   1100  N  ND2 . ASN A  1 134 ? 27.656  15.415  2.256   1.00 32.29  ? 134 ASN A ND2 1 
ATOM   1101  N  N   . LYS A  1 135 ? 28.659  10.881  0.279   1.00 21.03  ? 135 LYS A N   1 
ATOM   1102  C  CA  . LYS A  1 135 ? 29.208  10.852  -1.058  1.00 23.44  ? 135 LYS A CA  1 
ATOM   1103  C  C   . LYS A  1 135 ? 28.895  9.561   -1.771  1.00 23.97  ? 135 LYS A C   1 
ATOM   1104  O  O   . LYS A  1 135 ? 28.709  8.489   -1.133  1.00 20.51  ? 135 LYS A O   1 
ATOM   1105  C  CB  . LYS A  1 135 ? 30.730  11.195  -1.036  1.00 29.22  ? 135 LYS A CB  1 
ATOM   1106  C  CG  . LYS A  1 135 ? 30.945  12.656  -0.613  1.00 36.08  ? 135 LYS A CG  1 
ATOM   1107  C  CD  . LYS A  1 135 ? 32.362  13.121  -0.713  1.00 37.64  ? 135 LYS A CD  1 
ATOM   1108  C  CE  . LYS A  1 135 ? 32.561  14.480  -0.083  1.00 44.19  ? 135 LYS A CE  1 
ATOM   1109  N  NZ  . LYS A  1 135 ? 31.819  14.731  1.186   1.00 34.61  ? 135 LYS A NZ  1 
ATOM   1110  N  N   . SER A  1 136 ? 28.963  9.647   -3.093  1.00 27.37  ? 136 SER A N   1 
ATOM   1111  C  CA  . SER A  1 136 ? 28.849  8.487   -3.927  1.00 27.64  ? 136 SER A CA  1 
ATOM   1112  C  C   . SER A  1 136 ? 29.738  7.302   -3.503  1.00 19.37  ? 136 SER A C   1 
ATOM   1113  O  O   . SER A  1 136 ? 30.961  7.422   -3.315  1.00 26.08  ? 136 SER A O   1 
ATOM   1114  C  CB  . SER A  1 136 ? 29.182  8.874   -5.373  1.00 32.85  ? 136 SER A CB  1 
ATOM   1115  O  OG  . SER A  1 136 ? 28.897  7.794   -6.249  1.00 41.50  ? 136 SER A OG  1 
ATOM   1116  N  N   . GLU A  1 137 ? 29.118  6.154   -3.346  1.00 24.47  ? 137 GLU A N   1 
ATOM   1117  C  CA  . GLU A  1 137 ? 29.871  4.958   -2.977  1.00 22.01  ? 137 GLU A CA  1 
ATOM   1118  C  C   . GLU A  1 137 ? 30.580  5.083   -1.682  1.00 19.07  ? 137 GLU A C   1 
ATOM   1119  O  O   . GLU A  1 137 ? 31.626  4.409   -1.454  1.00 20.14  ? 137 GLU A O   1 
ATOM   1120  C  CB  . GLU A  1 137 ? 30.802  4.523   -4.077  1.00 23.80  ? 137 GLU A CB  1 
ATOM   1121  C  CG  . GLU A  1 137 ? 30.014  4.350   -5.333  1.00 32.87  ? 137 GLU A CG  1 
ATOM   1122  N  N   . GLY A  1 138 ? 30.016  5.887   -0.787  1.00 18.08  ? 138 GLY A N   1 
ATOM   1123  C  CA  . GLY A  1 138 ? 30.782  6.218   0.346   1.00 16.89  ? 138 GLY A CA  1 
ATOM   1124  C  C   . GLY A  1 138 ? 30.939  5.146   1.370   1.00 14.63  ? 138 GLY A C   1 
ATOM   1125  O  O   . GLY A  1 138 ? 31.954  5.129   2.060   1.00 15.11  ? 138 GLY A O   1 
ATOM   1126  N  N   . LEU A  1 139 ? 29.883  4.315   1.580   1.00 12.63  ? 139 LEU A N   1 
ATOM   1127  C  CA  . LEU A  1 139 ? 29.851  3.468   2.740   1.00 11.42  ? 139 LEU A CA  1 
ATOM   1128  C  C   . LEU A  1 139 ? 29.492  2.022   2.364   1.00 10.49  ? 139 LEU A C   1 
ATOM   1129  O  O   . LEU A  1 139 ? 28.801  1.752   1.364   1.00 11.18  ? 139 LEU A O   1 
ATOM   1130  C  CB  . LEU A  1 139 ? 28.799  3.957   3.764   1.00 12.05  ? 139 LEU A CB  1 
ATOM   1131  C  CG  . LEU A  1 139 ? 29.020  5.375   4.331   1.00 13.46  ? 139 LEU A CG  1 
ATOM   1132  C  CD1 . LEU A  1 139 ? 27.795  5.770   5.160   1.00 13.80  ? 139 LEU A CD1 1 
ATOM   1133  C  CD2 . LEU A  1 139 ? 30.297  5.474   5.120   1.00 15.30  ? 139 LEU A CD2 1 
ATOM   1134  N  N   . ALA A  1 140 ? 29.945  1.078   3.200   1.00 10.59  ? 140 ALA A N   1 
ATOM   1135  C  CA  . ALA A  1 140 ? 29.526  -0.322  3.090   1.00 9.58   ? 140 ALA A CA  1 
ATOM   1136  C  C   . ALA A  1 140 ? 29.284  -0.750  4.504   1.00 8.91   ? 140 ALA A C   1 
ATOM   1137  O  O   . ALA A  1 140 ? 30.144  -0.592  5.378   1.00 10.39  ? 140 ALA A O   1 
ATOM   1138  C  CB  . ALA A  1 140 ? 30.577  -1.161  2.407   1.00 10.67  ? 140 ALA A CB  1 
ATOM   1139  N  N   . VAL A  1 141 ? 28.116  -1.363  4.762   1.00 9.15   ? 141 VAL A N   1 
ATOM   1140  C  CA  . VAL A  1 141 ? 27.787  -1.872  6.088   1.00 8.14   ? 141 VAL A CA  1 
ATOM   1141  C  C   . VAL A  1 141 ? 27.566  -3.361  5.999   1.00 8.04   ? 141 VAL A C   1 
ATOM   1142  O  O   . VAL A  1 141 ? 26.873  -3.851  5.093   1.00 8.81   ? 141 VAL A O   1 
ATOM   1143  C  CB  . VAL A  1 141 ? 26.576  -1.133  6.685   1.00 8.39   ? 141 VAL A CB  1 
ATOM   1144  C  CG1 . VAL A  1 141 ? 26.275  -1.642  8.078   1.00 10.09  ? 141 VAL A CG1 1 
ATOM   1145  C  CG2 . VAL A  1 141 ? 26.829  0.357   6.750   1.00 10.08  ? 141 VAL A CG2 1 
ATOM   1146  N  N   . LEU A  1 142 ? 28.128  -4.075  6.969   1.00 7.90   ? 142 LEU A N   1 
ATOM   1147  C  CA  . LEU A  1 142 ? 27.842  -5.489  7.149   1.00 8.21   ? 142 LEU A CA  1 
ATOM   1148  C  C   . LEU A  1 142 ? 26.794  -5.586  8.271   1.00 8.00   ? 142 LEU A C   1 
ATOM   1149  O  O   . LEU A  1 142 ? 26.968  -4.985  9.329   1.00 9.14   ? 142 LEU A O   1 
ATOM   1150  C  CB  . LEU A  1 142 ? 29.097  -6.229  7.609   1.00 9.15   ? 142 LEU A CB  1 
ATOM   1151  C  CG  . LEU A  1 142 ? 30.315  -6.156  6.712   1.00 10.61  ? 142 LEU A CG  1 
ATOM   1152  C  CD1 . LEU A  1 142 ? 31.417  -6.974  7.331   1.00 11.15  ? 142 LEU A CD1 1 
ATOM   1153  C  CD2 . LEU A  1 142 ? 29.958  -6.591  5.296   1.00 11.53  ? 142 LEU A CD2 1 
ATOM   1154  N  N   . ALA A  1 143 ? 25.764  -6.378  8.003   1.00 7.85   ? 143 ALA A N   1 
ATOM   1155  C  CA  . ALA A  1 143 ? 24.683  -6.562  8.999   1.00 7.38   ? 143 ALA A CA  1 
ATOM   1156  C  C   . ALA A  1 143 ? 24.608  -8.035  9.380   1.00 7.24   ? 143 ALA A C   1 
ATOM   1157  O  O   . ALA A  1 143 ? 24.578  -8.936  8.531   1.00 8.07   ? 143 ALA A O   1 
ATOM   1158  C  CB  . ALA A  1 143 ? 23.367  -6.125  8.446   1.00 8.71   ? 143 ALA A CB  1 
ATOM   1159  N  N   . VAL A  1 144 ? 24.586  -8.261  10.721  1.00 7.55   ? 144 VAL A N   1 
ATOM   1160  C  CA  . VAL A  1 144 ? 24.424  -9.570  11.288  1.00 7.88   ? 144 VAL A CA  1 
ATOM   1161  C  C   . VAL A  1 144 ? 23.121  -9.590  12.039  1.00 7.67   ? 144 VAL A C   1 
ATOM   1162  O  O   . VAL A  1 144 ? 22.920  -8.762  12.972  1.00 8.39   ? 144 VAL A O   1 
ATOM   1163  C  CB  . VAL A  1 144 ? 25.607  -9.904  12.266  1.00 8.89   ? 144 VAL A CB  1 
ATOM   1164  C  CG1 . VAL A  1 144 ? 25.407  -11.306 12.810  1.00 10.39  ? 144 VAL A CG1 1 
ATOM   1165  C  CG2 . VAL A  1 144 ? 26.966  -9.765  11.551  1.00 9.65   ? 144 VAL A CG2 1 
ATOM   1166  N  N   . LEU A  1 145 ? 22.260  -10.527 11.679  1.00 8.02   ? 145 LEU A N   1 
ATOM   1167  C  CA  . LEU A  1 145 ? 21.028  -10.720 12.394  1.00 7.98   ? 145 LEU A CA  1 
ATOM   1168  C  C   . LEU A  1 145 ? 21.296  -11.557 13.635  1.00 8.16   ? 145 LEU A C   1 
ATOM   1169  O  O   . LEU A  1 145 ? 22.062  -12.502 13.602  1.00 9.35   ? 145 LEU A O   1 
ATOM   1170  C  CB  . LEU A  1 145 ? 20.056  -11.443 11.440  1.00 9.02   ? 145 LEU A CB  1 
ATOM   1171  C  CG  . LEU A  1 145 ? 19.736  -10.655 10.155  1.00 10.65  ? 145 LEU A CG  1 
ATOM   1172  C  CD1 . LEU A  1 145 ? 19.081  -11.553 9.111   1.00 12.72  ? 145 LEU A CD1 1 
ATOM   1173  C  CD2 . LEU A  1 145 ? 18.892  -9.398  10.478  1.00 13.70  ? 145 LEU A CD2 1 
ATOM   1174  N  N   . ILE A  1 146 ? 20.636  -11.198 14.747  1.00 7.90   ? 146 ILE A N   1 
ATOM   1175  C  CA  . ILE A  1 146 ? 20.863  -11.806 16.029  1.00 8.54   ? 146 ILE A CA  1 
ATOM   1176  C  C   . ILE A  1 146 ? 19.590  -12.385 16.582  1.00 8.75   ? 146 ILE A C   1 
ATOM   1177  O  O   . ILE A  1 146 ? 18.573  -11.689 16.592  1.00 9.64   ? 146 ILE A O   1 
ATOM   1178  C  CB  . ILE A  1 146 ? 21.428  -10.738 17.041  1.00 8.58   ? 146 ILE A CB  1 
ATOM   1179  C  CG1 . ILE A  1 146 ? 22.749  -10.147 16.546  1.00 9.51   ? 146 ILE A CG1 1 
ATOM   1180  C  CG2 . ILE A  1 146 ? 21.575  -11.336 18.435  1.00 10.71  ? 146 ILE A CG2 1 
ATOM   1181  C  CD1 . ILE A  1 146 ? 23.154  -8.900  17.274  1.00 10.51  ? 146 ILE A CD1 1 
ATOM   1182  N  N   . GLU A  1 147 ? 19.641  -13.636 17.033  1.00 9.69   ? 147 GLU A N   1 
ATOM   1183  C  CA  . GLU A  1 147 ? 18.501  -14.286 17.687  1.00 10.62  ? 147 GLU A CA  1 
ATOM   1184  C  C   . GLU A  1 147 ? 18.933  -14.821 19.046  1.00 10.45  ? 147 GLU A C   1 
ATOM   1185  O  O   . GLU A  1 147 ? 20.103  -15.008 19.308  1.00 10.65  ? 147 GLU A O   1 
ATOM   1186  C  CB  . GLU A  1 147 ? 17.949  -15.353 16.806  1.00 12.95  ? 147 GLU A CB  1 
ATOM   1187  C  CG  . GLU A  1 147 ? 18.848  -16.526 16.560  1.00 13.16  ? 147 GLU A CG  1 
ATOM   1188  C  CD  . GLU A  1 147 ? 18.380  -17.539 15.503  1.00 15.32  ? 147 GLU A CD  1 
ATOM   1189  O  OE1 . GLU A  1 147 ? 17.442  -17.267 14.741  1.00 18.23  ? 147 GLU A OE1 1 
ATOM   1190  O  OE2 . GLU A  1 147 ? 19.063  -18.575 15.399  1.00 21.83  ? 147 GLU A OE2 1 
ATOM   1191  N  N   A MET A  1 148 ? 17.985  -14.922 19.980  0.50 11.80  ? 148 MET A N   1 
ATOM   1192  N  N   B MET A  1 148 ? 17.884  -15.254 19.774  0.50 12.13  ? 148 MET A N   1 
ATOM   1193  C  CA  A MET A  1 148 ? 18.278  -15.577 21.246  0.50 12.71  ? 148 MET A CA  1 
ATOM   1194  C  CA  B MET A  1 148 ? 18.078  -15.883 21.058  0.50 14.32  ? 148 MET A CA  1 
ATOM   1195  C  C   A MET A  1 148 ? 18.506  -17.118 21.059  0.50 13.88  ? 148 MET A C   1 
ATOM   1196  C  C   B MET A  1 148 ? 18.590  -17.292 20.839  0.50 13.95  ? 148 MET A C   1 
ATOM   1197  O  O   A MET A  1 148 ? 17.720  -17.793 20.389  0.50 14.10  ? 148 MET A O   1 
ATOM   1198  O  O   B MET A  1 148 ? 18.149  -18.001 19.890  0.50 16.09  ? 148 MET A O   1 
ATOM   1199  C  CB  A MET A  1 148 ? 17.080  -15.356 22.182  0.50 12.84  ? 148 MET A CB  1 
ATOM   1200  C  CB  B MET A  1 148 ? 16.764  -15.860 21.879  0.50 15.13  ? 148 MET A CB  1 
ATOM   1201  C  CG  A MET A  1 148 ? 17.361  -15.869 23.614  0.50 18.65  ? 148 MET A CG  1 
ATOM   1202  C  CG  B MET A  1 148 ? 17.092  -16.238 23.321  0.50 15.70  ? 148 MET A CG  1 
ATOM   1203  S  SD  A MET A  1 148 ? 16.955  -17.602 23.765  0.50 28.25  ? 148 MET A SD  1 
ATOM   1204  S  SD  B MET A  1 148 ? 15.986  -15.815 24.683  0.50 17.75  ? 148 MET A SD  1 
ATOM   1205  C  CE  A MET A  1 148 ? 15.149  -17.396 23.623  0.50 33.47  ? 148 MET A CE  1 
ATOM   1206  C  CE  B MET A  1 148 ? 15.637  -14.154 24.864  0.50 18.40  ? 148 MET A CE  1 
ATOM   1207  N  N   . GLY A  1 149 ? 19.551  -17.663 21.687  1.00 14.12  ? 149 GLY A N   1 
ATOM   1208  C  CA  . GLY A  1 149 ? 19.938  -19.083 21.676  1.00 15.09  ? 149 GLY A CA  1 
ATOM   1209  C  C   . GLY A  1 149 ? 21.009  -19.241 22.701  1.00 13.54  ? 149 GLY A C   1 
ATOM   1210  O  O   . GLY A  1 149 ? 20.898  -18.801 23.828  1.00 14.32  ? 149 GLY A O   1 
ATOM   1211  N  N   . SER A  1 150 ? 22.102  -19.859 22.305  1.00 15.63  ? 150 SER A N   1 
ATOM   1212  C  CA  . SER A  1 150 ? 23.170  -20.128 23.239  1.00 17.30  ? 150 SER A CA  1 
ATOM   1213  C  C   . SER A  1 150 ? 24.011  -18.886 23.565  1.00 16.24  ? 150 SER A C   1 
ATOM   1214  O  O   . SER A  1 150 ? 24.132  -17.986 22.753  1.00 15.80  ? 150 SER A O   1 
ATOM   1215  C  CB  . SER A  1 150 ? 24.031  -21.305 22.801  1.00 28.54  ? 150 SER A CB  1 
ATOM   1216  O  OG  . SER A  1 150 ? 24.592  -21.002 21.567  1.00 28.40  ? 150 SER A OG  1 
ATOM   1217  N  N   . PHE A  1 151 ? 24.595  -18.884 24.761  1.00 15.42  ? 151 PHE A N   1 
ATOM   1218  C  CA  . PHE A  1 151 ? 25.536  -17.867 25.133  1.00 15.65  ? 151 PHE A CA  1 
ATOM   1219  C  C   . PHE A  1 151 ? 26.629  -17.699 24.110  1.00 13.86  ? 151 PHE A C   1 
ATOM   1220  O  O   . PHE A  1 151 ? 27.223  -18.684 23.624  1.00 16.58  ? 151 PHE A O   1 
ATOM   1221  C  CB  . PHE A  1 151 ? 26.147  -18.186 26.501  1.00 15.90  ? 151 PHE A CB  1 
ATOM   1222  C  CG  . PHE A  1 151 ? 27.096  -17.216 27.023  1.00 16.17  ? 151 PHE A CG  1 
ATOM   1223  C  CD1 . PHE A  1 151 ? 26.639  -15.990 27.553  1.00 18.96  ? 151 PHE A CD1 1 
ATOM   1224  C  CD2 . PHE A  1 151 ? 28.451  -17.440 26.961  1.00 18.29  ? 151 PHE A CD2 1 
ATOM   1225  C  CE1 . PHE A  1 151 ? 27.554  -15.009 27.980  1.00 18.13  ? 151 PHE A CE1 1 
ATOM   1226  C  CE2 . PHE A  1 151 ? 29.368  -16.497 27.425  1.00 19.63  ? 151 PHE A CE2 1 
ATOM   1227  C  CZ  . PHE A  1 151 ? 28.941  -15.265 27.922  1.00 21.16  ? 151 PHE A CZ  1 
ATOM   1228  N  N   . ASN A  1 152 ? 26.985  -16.451 23.850  1.00 14.88  ? 152 ASN A N   1 
ATOM   1229  C  CA  . ASN A  1 152 ? 27.990  -16.143 22.814  1.00 13.99  ? 152 ASN A CA  1 
ATOM   1230  C  C   . ASN A  1 152 ? 29.130  -15.445 23.517  1.00 15.69  ? 152 ASN A C   1 
ATOM   1231  O  O   . ASN A  1 152 ? 29.065  -14.246 23.769  1.00 13.76  ? 152 ASN A O   1 
ATOM   1232  C  CB  . ASN A  1 152 ? 27.291  -15.316 21.778  1.00 13.80  ? 152 ASN A CB  1 
ATOM   1233  C  CG  . ASN A  1 152 ? 28.170  -15.170 20.554  1.00 12.19  ? 152 ASN A CG  1 
ATOM   1234  O  OD1 . ASN A  1 152 ? 29.397  -14.819 20.660  1.00 13.90  ? 152 ASN A OD1 1 
ATOM   1235  N  ND2 . ASN A  1 152 ? 27.580  -15.366 19.401  1.00 12.50  ? 152 ASN A ND2 1 
ATOM   1236  N  N   . PRO A  1 153 ? 30.259  -16.174 23.772  1.00 15.01  ? 153 PRO A N   1 
ATOM   1237  C  CA  . PRO A  1 153 ? 31.394  -15.505 24.421  1.00 16.78  ? 153 PRO A CA  1 
ATOM   1238  C  C   . PRO A  1 153 ? 31.907  -14.294 23.649  1.00 15.31  ? 153 PRO A C   1 
ATOM   1239  O  O   . PRO A  1 153 ? 32.382  -13.341 24.237  1.00 17.96  ? 153 PRO A O   1 
ATOM   1240  C  CB  . PRO A  1 153 ? 32.448  -16.630 24.437  1.00 22.81  ? 153 PRO A CB  1 
ATOM   1241  C  CG  . PRO A  1 153 ? 31.596  -17.866 24.562  1.00 22.01  ? 153 PRO A CG  1 
ATOM   1242  C  CD  . PRO A  1 153 ? 30.422  -17.637 23.635  1.00 16.42  ? 153 PRO A CD  1 
ATOM   1243  N  N   . SER A  1 154 ? 31.861  -14.341 22.328  1.00 14.59  ? 154 SER A N   1 
ATOM   1244  C  CA  . SER A  1 154 ? 32.438  -13.224 21.552  1.00 14.13  ? 154 SER A CA  1 
ATOM   1245  C  C   . SER A  1 154 ? 31.637  -11.970 21.719  1.00 13.16  ? 154 SER A C   1 
ATOM   1246  O  O   . SER A  1 154 ? 32.190  -10.913 21.843  1.00 13.72  ? 154 SER A O   1 
ATOM   1247  C  CB  . SER A  1 154 ? 32.602  -13.657 20.090  1.00 15.30  ? 154 SER A CB  1 
ATOM   1248  O  OG  . SER A  1 154 ? 33.470  -14.800 19.992  1.00 18.68  ? 154 SER A OG  1 
ATOM   1249  N  N   . TYR A  1 155 ? 30.299  -12.093 21.611  1.00 13.06  ? 155 TYR A N   1 
ATOM   1250  C  CA  . TYR A  1 155 ? 29.516  -10.885 21.866  1.00 12.25  ? 155 TYR A CA  1 
ATOM   1251  C  C   . TYR A  1 155 ? 29.711  -10.378 23.255  1.00 12.51  ? 155 TYR A C   1 
ATOM   1252  O  O   . TYR A  1 155 ? 29.585  -9.143  23.486  1.00 12.78  ? 155 TYR A O   1 
ATOM   1253  C  CB  . TYR A  1 155 ? 28.043  -11.111 21.559  1.00 13.01  ? 155 TYR A CB  1 
ATOM   1254  C  CG  . TYR A  1 155 ? 27.741  -10.954 20.051  1.00 12.49  ? 155 TYR A CG  1 
ATOM   1255  C  CD1 . TYR A  1 155 ? 28.067  -11.927 19.111  1.00 10.91  ? 155 TYR A CD1 1 
ATOM   1256  C  CD2 . TYR A  1 155 ? 27.165  -9.740  19.572  1.00 11.28  ? 155 TYR A CD2 1 
ATOM   1257  C  CE1 . TYR A  1 155 ? 27.863  -11.741 17.769  1.00 10.89  ? 155 TYR A CE1 1 
ATOM   1258  C  CE2 . TYR A  1 155 ? 26.974  -9.579  18.210  1.00 11.18  ? 155 TYR A CE2 1 
ATOM   1259  C  CZ  . TYR A  1 155 ? 27.347  -10.571 17.311  1.00 9.85   ? 155 TYR A CZ  1 
ATOM   1260  O  OH  . TYR A  1 155 ? 27.094  -10.371 15.965  1.00 10.94  ? 155 TYR A OH  1 
ATOM   1261  N  N   . ASP A  1 156 ? 29.991  -11.267 24.227  1.00 12.54  ? 156 ASP A N   1 
ATOM   1262  C  CA  . ASP A  1 156 ? 30.249  -10.793 25.553  1.00 13.93  ? 156 ASP A CA  1 
ATOM   1263  C  C   . ASP A  1 156 ? 31.516  -9.928  25.687  1.00 13.89  ? 156 ASP A C   1 
ATOM   1264  O  O   . ASP A  1 156 ? 31.614  -9.178  26.664  1.00 16.43  ? 156 ASP A O   1 
ATOM   1265  C  CB  . ASP A  1 156 ? 30.200  -11.929 26.536  1.00 16.53  ? 156 ASP A CB  1 
ATOM   1266  C  CG  . ASP A  1 156 ? 29.138  -11.617 27.621  1.00 19.48  ? 156 ASP A CG  1 
ATOM   1267  O  OD1 . ASP A  1 156 ? 27.963  -11.116 27.313  1.00 16.00  ? 156 ASP A OD1 1 
ATOM   1268  O  OD2 . ASP A  1 156 ? 29.493  -11.736 28.830  1.00 25.61  ? 156 ASP A OD2 1 
ATOM   1269  N  N   . LYS A  1 157 ? 32.423  -9.975  24.728  1.00 14.49  ? 157 LYS A N   1 
ATOM   1270  C  CA  . LYS A  1 157 ? 33.625  -9.121  24.756  1.00 14.83  ? 157 LYS A CA  1 
ATOM   1271  C  C   . LYS A  1 157 ? 33.173  -7.675  24.630  1.00 13.99  ? 157 LYS A C   1 
ATOM   1272  O  O   . LYS A  1 157 ? 33.922  -6.785  25.074  1.00 19.02  ? 157 LYS A O   1 
ATOM   1273  C  CB  . LYS A  1 157 ? 34.606  -9.583  23.665  1.00 14.25  ? 157 LYS A CB  1 
ATOM   1274  C  CG  . LYS A  1 157 ? 35.136  -11.037 23.951  1.00 16.25  ? 157 LYS A CG  1 
ATOM   1275  C  CD  . LYS A  1 157 ? 36.110  -11.509 22.873  1.00 17.83  ? 157 LYS A CD  1 
ATOM   1276  C  CE  . LYS A  1 157 ? 36.442  -12.962 23.121  1.00 22.33  ? 157 LYS A CE  1 
ATOM   1277  N  NZ  . LYS A  1 157 ? 37.332  -13.480 22.094  1.00 21.66  ? 157 LYS A NZ  1 
ATOM   1278  N  N   . ILE A  1 158 ? 32.014  -7.445  24.015  1.00 14.90  ? 158 ILE A N   1 
ATOM   1279  C  CA  . ILE A  1 158 ? 31.434  -6.098  23.985  1.00 14.94  ? 158 ILE A CA  1 
ATOM   1280  C  C   . ILE A  1 158 ? 30.483  -5.907  25.154  1.00 14.75  ? 158 ILE A C   1 
ATOM   1281  O  O   . ILE A  1 158 ? 30.555  -4.948  25.904  1.00 16.04  ? 158 ILE A O   1 
ATOM   1282  C  CB  . ILE A  1 158 ? 30.632  -5.853  22.676  1.00 17.15  ? 158 ILE A CB  1 
ATOM   1283  C  CG1 . ILE A  1 158 ? 31.568  -5.833  21.477  1.00 21.28  ? 158 ILE A CG1 1 
ATOM   1284  C  CG2 . ILE A  1 158 ? 29.893  -4.535  22.781  1.00 17.78  ? 158 ILE A CG2 1 
ATOM   1285  C  CD1 . ILE A  1 158 ? 30.786  -5.939  20.194  1.00 28.82  ? 158 ILE A CD1 1 
ATOM   1286  N  N   . PHE A  1 159 ? 29.576  -6.870  25.346  1.00 13.08  ? 159 PHE A N   1 
ATOM   1287  C  CA  . PHE A  1 159 ? 28.504  -6.663  26.327  1.00 14.48  ? 159 PHE A CA  1 
ATOM   1288  C  C   . PHE A  1 159 ? 29.007  -6.558  27.743  1.00 14.33  ? 159 PHE A C   1 
ATOM   1289  O  O   . PHE A  1 159 ? 28.346  -5.917  28.526  1.00 14.72  ? 159 PHE A O   1 
ATOM   1290  C  CB  . PHE A  1 159 ? 27.413  -7.741  26.257  1.00 14.17  ? 159 PHE A CB  1 
ATOM   1291  C  CG  . PHE A  1 159 ? 26.702  -7.858  24.929  1.00 13.36  ? 159 PHE A CG  1 
ATOM   1292  C  CD1 . PHE A  1 159 ? 26.633  -6.834  23.988  1.00 15.88  ? 159 PHE A CD1 1 
ATOM   1293  C  CD2 . PHE A  1 159 ? 26.027  -9.046  24.658  1.00 16.28  ? 159 PHE A CD2 1 
ATOM   1294  C  CE1 . PHE A  1 159 ? 25.933  -6.994  22.778  1.00 18.74  ? 159 PHE A CE1 1 
ATOM   1295  C  CE2 . PHE A  1 159 ? 25.317  -9.216  23.467  1.00 17.48  ? 159 PHE A CE2 1 
ATOM   1296  C  CZ  . PHE A  1 159 ? 25.243  -8.147  22.548  1.00 16.48  ? 159 PHE A CZ  1 
ATOM   1297  N  N   . SER A  1 160 ? 30.162  -7.139  28.093  1.00 14.08  ? 160 SER A N   1 
ATOM   1298  C  CA  . SER A  1 160 ? 30.697  -7.020  29.492  1.00 15.56  ? 160 SER A CA  1 
ATOM   1299  C  C   . SER A  1 160 ? 31.088  -5.595  29.802  1.00 15.90  ? 160 SER A C   1 
ATOM   1300  O  O   . SER A  1 160 ? 31.284  -5.271  30.981  1.00 18.84  ? 160 SER A O   1 
ATOM   1301  C  CB  . SER A  1 160 ? 31.848  -7.970  29.636  1.00 17.75  ? 160 SER A CB  1 
ATOM   1302  O  OG  . SER A  1 160 ? 32.918  -7.617  28.805  1.00 22.08  ? 160 SER A OG  1 
ATOM   1303  N  N   . HIS A  1 161 ? 31.220  -4.733  28.786  1.00 15.17  ? 161 HIS A N   1 
ATOM   1304  C  CA  . HIS A  1 161 ? 31.490  -3.334  29.031  1.00 15.42  ? 161 HIS A CA  1 
ATOM   1305  C  C   . HIS A  1 161 ? 30.303  -2.439  29.085  1.00 15.69  ? 161 HIS A C   1 
ATOM   1306  O  O   . HIS A  1 161 ? 30.469  -1.239  29.325  1.00 16.76  ? 161 HIS A O   1 
ATOM   1307  C  CB  . HIS A  1 161 ? 32.517  -2.853  28.008  1.00 16.90  ? 161 HIS A CB  1 
ATOM   1308  C  CG  . HIS A  1 161 ? 33.804  -3.572  28.082  1.00 16.14  ? 161 HIS A CG  1 
ATOM   1309  N  ND1 . HIS A  1 161 ? 34.860  -3.123  28.865  1.00 18.92  ? 161 HIS A ND1 1 
ATOM   1310  C  CD2 . HIS A  1 161 ? 34.236  -4.729  27.463  1.00 18.99  ? 161 HIS A CD2 1 
ATOM   1311  C  CE1 . HIS A  1 161 ? 35.916  -3.974  28.716  1.00 24.59  ? 161 HIS A CE1 1 
ATOM   1312  N  NE2 . HIS A  1 161 ? 35.532  -4.952  27.856  1.00 19.87  ? 161 HIS A NE2 1 
ATOM   1313  N  N   . LEU A  1 162 ? 29.098  -2.968  28.861  1.00 14.78  ? 162 LEU A N   1 
ATOM   1314  C  CA  . LEU A  1 162 ? 27.901  -2.093  28.826  1.00 16.05  ? 162 LEU A CA  1 
ATOM   1315  C  C   . LEU A  1 162 ? 27.710  -1.353  30.121  1.00 15.98  ? 162 LEU A C   1 
ATOM   1316  O  O   . LEU A  1 162 ? 27.222  -0.212  30.080  1.00 16.51  ? 162 LEU A O   1 
ATOM   1317  C  CB  . LEU A  1 162 ? 26.617  -2.835  28.508  1.00 15.90  ? 162 LEU A CB  1 
ATOM   1318  C  CG  . LEU A  1 162 ? 26.581  -3.443  27.078  1.00 17.49  ? 162 LEU A CG  1 
ATOM   1319  C  CD1 . LEU A  1 162 ? 25.290  -4.265  26.945  1.00 22.72  ? 162 LEU A CD1 1 
ATOM   1320  C  CD2 . LEU A  1 162 ? 26.759  -2.383  25.995  1.00 22.12  ? 162 LEU A CD2 1 
ATOM   1321  N  N   . GLN A  1 163 ? 28.107  -1.966  31.251  1.00 16.23  ? 163 GLN A N   1 
ATOM   1322  C  CA  . GLN A  1 163 ? 28.081  -1.342  32.581  1.00 18.18  ? 163 GLN A CA  1 
ATOM   1323  C  C   . GLN A  1 163 ? 28.750  -0.004  32.665  1.00 18.94  ? 163 GLN A C   1 
ATOM   1324  O  O   . GLN A  1 163 ? 28.452  0.777   33.571  1.00 23.26  ? 163 GLN A O   1 
ATOM   1325  C  CB  . GLN A  1 163 ? 28.704  -2.296  33.621  1.00 19.40  ? 163 GLN A CB  1 
ATOM   1326  C  CG  . GLN A  1 163 ? 30.152  -2.706  33.336  1.00 25.60  ? 163 GLN A CG  1 
ATOM   1327  C  CD  . GLN A  1 163 ? 30.787  -3.346  34.571  1.00 34.72  ? 163 GLN A CD  1 
ATOM   1328  O  OE1 . GLN A  1 163 ? 30.235  -3.244  35.668  1.00 29.23  ? 163 GLN A OE1 1 
ATOM   1329  N  NE2 . GLN A  1 163 ? 31.968  -3.968  34.402  1.00 35.75  ? 163 GLN A NE2 1 
ATOM   1330  N  N   . HIS A  1 164 ? 29.684  0.264   31.770  1.00 15.82  ? 164 HIS A N   1 
ATOM   1331  C  CA  . HIS A  1 164 ? 30.510  1.503   31.808  1.00 16.20  ? 164 HIS A CA  1 
ATOM   1332  C  C   . HIS A  1 164 ? 30.064  2.508   30.820  1.00 15.09  ? 164 HIS A C   1 
ATOM   1333  O  O   . HIS A  1 164 ? 30.681  3.623   30.775  1.00 18.93  ? 164 HIS A O   1 
ATOM   1334  C  CB  . HIS A  1 164 ? 31.981  1.178   31.642  1.00 19.08  ? 164 HIS A CB  1 
ATOM   1335  C  CG  . HIS A  1 164 ? 32.562  0.334   32.771  1.00 15.80  ? 164 HIS A CG  1 
ATOM   1336  N  ND1 . HIS A  1 164 ? 32.229  0.393   34.106  1.00 18.45  ? 164 HIS A ND1 1 
ATOM   1337  C  CD2 . HIS A  1 164 ? 33.624  -0.571  32.668  1.00 18.68  ? 164 HIS A CD2 1 
ATOM   1338  C  CE1 . HIS A  1 164 ? 33.030  -0.475  34.766  1.00 15.81  ? 164 HIS A CE1 1 
ATOM   1339  N  NE2 . HIS A  1 164 ? 33.884  -1.023  33.903  1.00 24.66  ? 164 HIS A NE2 1 
ATOM   1340  N  N   . VAL A  1 165 ? 29.067  2.201   29.983  1.00 14.31  ? 165 VAL A N   1 
ATOM   1341  C  CA  . VAL A  1 165 ? 28.561  3.199   29.033  1.00 15.20  ? 165 VAL A CA  1 
ATOM   1342  C  C   . VAL A  1 165 ? 27.044  3.330   29.141  1.00 13.66  ? 165 VAL A C   1 
ATOM   1343  O  O   . VAL A  1 165 ? 26.318  3.525   28.207  1.00 14.62  ? 165 VAL A O   1 
ATOM   1344  C  CB  . VAL A  1 165 ? 28.979  2.841   27.575  1.00 16.29  ? 165 VAL A CB  1 
ATOM   1345  C  CG1 . VAL A  1 165 ? 30.519  2.959   27.444  1.00 18.38  ? 165 VAL A CG1 1 
ATOM   1346  C  CG2 . VAL A  1 165 ? 28.495  1.422   27.152  1.00 15.46  ? 165 VAL A CG2 1 
ATOM   1347  N  N   . LYS A  1 166 ? 26.553  3.277   30.383  1.00 14.69  ? 166 LYS A N   1 
ATOM   1348  C  CA  . LYS A  1 166 ? 25.171  3.311   30.681  1.00 13.76  ? 166 LYS A CA  1 
ATOM   1349  C  C   . LYS A  1 166 ? 24.417  4.533   30.119  1.00 13.43  ? 166 LYS A C   1 
ATOM   1350  O  O   . LYS A  1 166 ? 23.281  4.405   29.640  1.00 15.20  ? 166 LYS A O   1 
ATOM   1351  C  CB  . LYS A  1 166 ? 24.981  3.197   32.211  1.00 15.88  ? 166 LYS A CB  1 
ATOM   1352  C  CG  . LYS A  1 166 ? 23.560  3.148   32.663  1.00 16.62  ? 166 LYS A CG  1 
ATOM   1353  C  CD  . LYS A  1 166 ? 23.458  2.837   34.179  1.00 24.76  ? 166 LYS A CD  1 
ATOM   1354  C  CE  . LYS A  1 166 ? 24.736  2.145   34.600  1.00 41.95  ? 166 LYS A CE  1 
ATOM   1355  N  NZ  . LYS A  1 166 ? 24.791  0.667   34.521  1.00 42.22  ? 166 LYS A NZ  1 
ATOM   1356  N  N   . TYR A  1 167 ? 25.035  5.712   30.229  1.00 14.28  ? 167 TYR A N   1 
ATOM   1357  C  CA  . TYR A  1 167 ? 24.379  6.962   29.855  1.00 14.52  ? 167 TYR A CA  1 
ATOM   1358  C  C   . TYR A  1 167 ? 25.026  7.630   28.663  1.00 14.41  ? 167 TYR A C   1 
ATOM   1359  O  O   . TYR A  1 167 ? 26.210  7.430   28.339  1.00 15.84  ? 167 TYR A O   1 
ATOM   1360  C  CB  . TYR A  1 167 ? 24.419  7.978   31.053  1.00 16.52  ? 167 TYR A CB  1 
ATOM   1361  C  CG  . TYR A  1 167 ? 23.663  7.436   32.216  1.00 15.20  ? 167 TYR A CG  1 
ATOM   1362  C  CD1 . TYR A  1 167 ? 22.279  7.484   32.242  1.00 17.40  ? 167 TYR A CD1 1 
ATOM   1363  C  CD2 . TYR A  1 167 ? 24.342  6.932   33.330  1.00 18.35  ? 167 TYR A CD2 1 
ATOM   1364  C  CE1 . TYR A  1 167 ? 21.555  7.026   33.324  1.00 18.53  ? 167 TYR A CE1 1 
ATOM   1365  C  CE2 . TYR A  1 167 ? 23.632  6.447   34.421  1.00 19.79  ? 167 TYR A CE2 1 
ATOM   1366  C  CZ  . TYR A  1 167 ? 22.252  6.496   34.390  1.00 18.89  ? 167 TYR A CZ  1 
ATOM   1367  O  OH  . TYR A  1 167 ? 21.578  6.022   35.523  1.00 23.96  ? 167 TYR A OH  1 
ATOM   1368  N  N   . LYS A  1 168 ? 24.240  8.467   28.021  1.00 16.45  ? 168 LYS A N   1 
ATOM   1369  C  CA  . LYS A  1 168 ? 24.754  9.149   26.870  1.00 16.40  ? 168 LYS A CA  1 
ATOM   1370  C  C   . LYS A  1 168 ? 25.987  9.921   27.204  1.00 17.64  ? 168 LYS A C   1 
ATOM   1371  O  O   . LYS A  1 168 ? 26.078  10.669  28.189  1.00 18.62  ? 168 LYS A O   1 
ATOM   1372  C  CB  . LYS A  1 168 ? 23.657  10.140  26.412  1.00 19.29  ? 168 LYS A CB  1 
ATOM   1373  C  CG  . LYS A  1 168 ? 24.003  10.946  25.177  1.00 22.65  ? 168 LYS A CG  1 
ATOM   1374  C  CD  . LYS A  1 168 ? 22.839  11.825  24.714  1.00 24.25  ? 168 LYS A CD  1 
ATOM   1375  C  CE  . LYS A  1 168 ? 23.310  12.660  23.550  1.00 34.89  ? 168 LYS A CE  1 
ATOM   1376  N  NZ  . LYS A  1 168 ? 22.182  13.403  22.922  1.00 40.66  ? 168 LYS A NZ  1 
ATOM   1377  N  N   . GLY A  1 169 ? 26.962  9.828   26.316  1.00 19.38  ? 169 GLY A N   1 
ATOM   1378  C  CA  . GLY A  1 169 ? 28.192  10.534  26.494  1.00 21.65  ? 169 GLY A CA  1 
ATOM   1379  C  C   . GLY A  1 169 ? 29.286  9.710   27.170  1.00 21.59  ? 169 GLY A C   1 
ATOM   1380  O  O   . GLY A  1 169 ? 30.439  10.024  27.037  1.00 28.01  ? 169 GLY A O   1 
ATOM   1381  N  N   . GLN A  1 170 ? 28.925  8.656   27.879  1.00 17.30  ? 170 GLN A N   1 
ATOM   1382  C  CA  . GLN A  1 170 ? 29.900  7.850   28.571  1.00 16.10  ? 170 GLN A CA  1 
ATOM   1383  C  C   . GLN A  1 170 ? 30.711  6.998   27.569  1.00 15.56  ? 170 GLN A C   1 
ATOM   1384  O  O   . GLN A  1 170 ? 30.222  6.591   26.505  1.00 17.57  ? 170 GLN A O   1 
ATOM   1385  C  CB  . GLN A  1 170 ? 29.228  7.014   29.642  1.00 14.96  ? 170 GLN A CB  1 
ATOM   1386  C  CG  . GLN A  1 170 ? 28.637  7.875   30.748  1.00 15.40  ? 170 GLN A CG  1 
ATOM   1387  C  CD  . GLN A  1 170 ? 28.076  7.116   31.877  1.00 17.39  ? 170 GLN A CD  1 
ATOM   1388  O  OE1 . GLN A  1 170 ? 27.517  6.067   31.699  1.00 17.44  ? 170 GLN A OE1 1 
ATOM   1389  N  NE2 . GLN A  1 170 ? 28.173  7.679   33.081  1.00 19.87  ? 170 GLN A NE2 1 
ATOM   1390  N  N   A GLU A  1 171 ? 31.967  6.748   27.954  0.50 18.19  ? 171 GLU A N   1 
ATOM   1391  N  N   B GLU A  1 171 ? 31.880  6.615   28.043  0.50 16.06  ? 171 GLU A N   1 
ATOM   1392  C  CA  A GLU A  1 171 ? 32.967  6.092   27.121  0.50 15.72  ? 171 GLU A CA  1 
ATOM   1393  C  CA  B GLU A  1 171 ? 32.786  5.895   27.236  0.50 18.97  ? 171 GLU A CA  1 
ATOM   1394  C  C   A GLU A  1 171 ? 33.748  5.116   27.930  0.50 16.10  ? 171 GLU A C   1 
ATOM   1395  C  C   B GLU A  1 171 ? 33.496  4.868   28.059  0.50 15.70  ? 171 GLU A C   1 
ATOM   1396  O  O   A GLU A  1 171 ? 34.068  5.423   29.092  0.50 15.80  ? 171 GLU A O   1 
ATOM   1397  O  O   B GLU A  1 171 ? 33.571  4.881   29.311  0.50 18.02  ? 171 GLU A O   1 
ATOM   1398  C  CB  A GLU A  1 171 ? 33.898  7.128   26.478  0.50 17.56  ? 171 GLU A CB  1 
ATOM   1399  C  CB  B GLU A  1 171 ? 33.803  6.844   26.573  0.50 18.50  ? 171 GLU A CB  1 
ATOM   1400  C  CG  A GLU A  1 171 ? 33.206  7.950   25.417  0.50 22.84  ? 171 GLU A CG  1 
ATOM   1401  C  CG  B GLU A  1 171 ? 34.808  7.447   27.543  0.50 22.30  ? 171 GLU A CG  1 
ATOM   1402  C  CD  A GLU A  1 171 ? 34.026  9.121   24.957  0.50 21.98  ? 171 GLU A CD  1 
ATOM   1403  C  CD  B GLU A  1 171 ? 35.811  8.335   26.852  0.50 26.13  ? 171 GLU A CD  1 
ATOM   1404  O  OE1 A GLU A  1 171 ? 35.162  9.301   25.409  0.50 23.65  ? 171 GLU A OE1 1 
ATOM   1405  O  OE1 B GLU A  1 171 ? 35.523  8.803   25.722  0.50 21.06  ? 171 GLU A OE1 1 
ATOM   1406  O  OE2 A GLU A  1 171 ? 33.503  9.868   24.127  0.50 27.06  ? 171 GLU A OE2 1 
ATOM   1407  O  OE2 B GLU A  1 171 ? 36.908  8.539   27.424  0.50 22.20  ? 171 GLU A OE2 1 
ATOM   1408  N  N   . ALA A  1 172 ? 34.093  3.962   27.329  1.00 16.14  ? 172 ALA A N   1 
ATOM   1409  C  CA  . ALA A  1 172 ? 34.904  2.956   27.975  1.00 18.33  ? 172 ALA A CA  1 
ATOM   1410  C  C   . ALA A  1 172 ? 35.867  2.395   26.923  1.00 17.57  ? 172 ALA A C   1 
ATOM   1411  O  O   . ALA A  1 172 ? 35.717  2.663   25.771  1.00 22.23  ? 172 ALA A O   1 
ATOM   1412  C  CB  . ALA A  1 172 ? 34.031  1.857   28.517  1.00 20.40  ? 172 ALA A CB  1 
ATOM   1413  N  N   . PHE A  1 173 ? 36.845  1.626   27.349  1.00 20.41  ? 173 PHE A N   1 
ATOM   1414  C  CA  . PHE A  1 173 ? 37.824  1.030   26.421  1.00 19.14  ? 173 PHE A CA  1 
ATOM   1415  C  C   . PHE A  1 173 ? 37.663  -0.470  26.430  1.00 19.60  ? 173 PHE A C   1 
ATOM   1416  O  O   . PHE A  1 173 ? 37.568  -1.101  27.508  1.00 31.80  ? 173 PHE A O   1 
ATOM   1417  C  CB  . PHE A  1 173 ? 39.229  1.477   26.840  1.00 23.82  ? 173 PHE A CB  1 
ATOM   1418  C  CG  . PHE A  1 173 ? 39.487  2.927   26.527  1.00 24.16  ? 173 PHE A CG  1 
ATOM   1419  C  CD1 . PHE A  1 173 ? 39.752  3.354   25.196  1.00 28.25  ? 173 PHE A CD1 1 
ATOM   1420  C  CD2 . PHE A  1 173 ? 39.358  3.893   27.521  1.00 36.79  ? 173 PHE A CD2 1 
ATOM   1421  C  CE1 . PHE A  1 173 ? 39.928  4.717   24.895  1.00 34.47  ? 173 PHE A CE1 1 
ATOM   1422  C  CE2 . PHE A  1 173 ? 39.583  5.231   27.246  1.00 36.56  ? 173 PHE A CE2 1 
ATOM   1423  C  CZ  . PHE A  1 173 ? 39.853  5.648   25.934  1.00 48.42  ? 173 PHE A CZ  1 
ATOM   1424  N  N   . VAL A  1 174 ? 37.638  -1.021  25.204  1.00 16.72  ? 174 VAL A N   1 
ATOM   1425  C  CA  . VAL A  1 174 ? 37.548  -2.487  24.938  1.00 17.31  ? 174 VAL A CA  1 
ATOM   1426  C  C   . VAL A  1 174 ? 38.848  -2.978  24.323  1.00 16.85  ? 174 VAL A C   1 
ATOM   1427  O  O   . VAL A  1 174 ? 39.255  -2.474  23.308  1.00 19.44  ? 174 VAL A O   1 
ATOM   1428  C  CB  . VAL A  1 174 ? 36.353  -2.858  24.016  1.00 16.30  ? 174 VAL A CB  1 
ATOM   1429  C  CG1 . VAL A  1 174 ? 36.289  -4.354  23.713  1.00 20.74  ? 174 VAL A CG1 1 
ATOM   1430  C  CG2 . VAL A  1 174 ? 35.058  -2.270  24.563  1.00 19.53  ? 174 VAL A CG2 1 
ATOM   1431  N  N   . PRO A  1 175 ? 39.527  -3.923  24.994  1.00 18.14  ? 175 PRO A N   1 
ATOM   1432  C  CA  . PRO A  1 175 ? 40.743  -4.503  24.402  1.00 18.28  ? 175 PRO A CA  1 
ATOM   1433  C  C   . PRO A  1 175 ? 40.459  -5.175  23.059  1.00 17.38  ? 175 PRO A C   1 
ATOM   1434  O  O   . PRO A  1 175 ? 39.380  -5.753  22.904  1.00 18.20  ? 175 PRO A O   1 
ATOM   1435  C  CB  . PRO A  1 175 ? 41.140  -5.547  25.426  1.00 23.15  ? 175 PRO A CB  1 
ATOM   1436  C  CG  . PRO A  1 175 ? 40.541  -5.055  26.738  1.00 28.36  ? 175 PRO A CG  1 
ATOM   1437  C  CD  . PRO A  1 175 ? 39.196  -4.495  26.280  1.00 19.53  ? 175 PRO A CD  1 
ATOM   1438  N  N   . GLY A  1 176 ? 41.377  -5.069  22.141  1.00 17.54  ? 176 GLY A N   1 
ATOM   1439  C  CA  . GLY A  1 176 ? 41.140  -5.687  20.854  1.00 16.92  ? 176 GLY A CA  1 
ATOM   1440  C  C   . GLY A  1 176 ? 40.804  -7.164  20.949  1.00 17.74  ? 176 GLY A C   1 
ATOM   1441  O  O   . GLY A  1 176 ? 41.411  -7.904  21.730  1.00 19.28  ? 176 GLY A O   1 
ATOM   1442  N  N   . PHE A  1 177 ? 39.903  -7.606  20.099  1.00 16.60  ? 177 PHE A N   1 
ATOM   1443  C  CA  . PHE A  1 177 ? 39.605  -9.002  19.869  1.00 16.45  ? 177 PHE A CA  1 
ATOM   1444  C  C   . PHE A  1 177 ? 39.230  -9.192  18.413  1.00 14.66  ? 177 PHE A C   1 
ATOM   1445  O  O   . PHE A  1 177 ? 39.204  -8.204  17.662  1.00 15.38  ? 177 PHE A O   1 
ATOM   1446  C  CB  . PHE A  1 177 ? 38.462  -9.447  20.790  1.00 17.18  ? 177 PHE A CB  1 
ATOM   1447  C  CG  . PHE A  1 177 ? 37.090  -8.893  20.445  1.00 15.25  ? 177 PHE A CG  1 
ATOM   1448  C  CD1 . PHE A  1 177 ? 36.741  -7.613  20.929  1.00 15.82  ? 177 PHE A CD1 1 
ATOM   1449  C  CD2 . PHE A  1 177 ? 36.147  -9.650  19.693  1.00 16.84  ? 177 PHE A CD2 1 
ATOM   1450  C  CE1 . PHE A  1 177 ? 35.470  -7.088  20.643  1.00 16.93  ? 177 PHE A CE1 1 
ATOM   1451  C  CE2 . PHE A  1 177 ? 34.909  -9.128  19.443  1.00 16.41  ? 177 PHE A CE2 1 
ATOM   1452  C  CZ  . PHE A  1 177 ? 34.593  -7.852  19.880  1.00 14.98  ? 177 PHE A CZ  1 
ATOM   1453  N  N   . ASN A  1 178 ? 39.082  -10.461 18.005  1.00 16.03  ? 178 ASN A N   1 
ATOM   1454  C  CA  . ASN A  1 178 ? 38.811  -10.732 16.613  1.00 15.56  ? 178 ASN A CA  1 
ATOM   1455  C  C   . ASN A  1 178 ? 37.357  -10.461 16.261  1.00 13.50  ? 178 ASN A C   1 
ATOM   1456  O  O   . ASN A  1 178 ? 36.444  -11.238 16.595  1.00 13.57  ? 178 ASN A O   1 
ATOM   1457  C  CB  . ASN A  1 178 ? 39.182  -12.184 16.298  1.00 16.60  ? 178 ASN A CB  1 
ATOM   1458  C  CG  . ASN A  1 178 ? 39.026  -12.558 14.855  1.00 15.70  ? 178 ASN A CG  1 
ATOM   1459  O  OD1 . ASN A  1 178 ? 38.719  -11.706 13.995  1.00 16.78  ? 178 ASN A OD1 1 
ATOM   1460  N  ND2 . ASN A  1 178 ? 39.139  -13.825 14.565  1.00 21.07  ? 178 ASN A ND2 1 
ATOM   1461  N  N   . ILE A  1 179 ? 37.103  -9.358  15.595  1.00 13.14  ? 179 ILE A N   1 
ATOM   1462  C  CA  . ILE A  1 179 ? 35.754  -8.947  15.245  1.00 11.91  ? 179 ILE A CA  1 
ATOM   1463  C  C   . ILE A  1 179 ? 35.090  -9.989  14.338  1.00 11.57  ? 179 ILE A C   1 
ATOM   1464  O  O   . ILE A  1 179 ? 33.847  -10.066 14.298  1.00 11.75  ? 179 ILE A O   1 
ATOM   1465  C  CB  . ILE A  1 179 ? 35.788  -7.566  14.555  1.00 12.26  ? 179 ILE A CB  1 
ATOM   1466  C  CG1 . ILE A  1 179 ? 36.414  -6.520  15.434  1.00 12.63  ? 179 ILE A CG1 1 
ATOM   1467  C  CG2 . ILE A  1 179 ? 34.397  -7.108  14.111  1.00 12.35  ? 179 ILE A CG2 1 
ATOM   1468  C  CD1 . ILE A  1 179 ? 35.819  -6.315  16.843  1.00 13.91  ? 179 ILE A CD1 1 
ATOM   1469  N  N   . GLU A  1 180 ? 35.861  -10.799 13.586  1.00 12.05  ? 180 GLU A N   1 
ATOM   1470  C  CA  . GLU A  1 180 ? 35.245  -11.810 12.751  1.00 12.48  ? 180 GLU A CA  1 
ATOM   1471  C  C   . GLU A  1 180 ? 34.439  -12.812 13.600  1.00 11.72  ? 180 GLU A C   1 
ATOM   1472  O  O   . GLU A  1 180 ? 33.542  -13.485 13.084  1.00 13.01  ? 180 GLU A O   1 
ATOM   1473  C  CB  . GLU A  1 180 ? 36.281  -12.491 11.887  1.00 15.82  ? 180 GLU A CB  1 
ATOM   1474  C  CG  . GLU A  1 180 ? 35.623  -13.292 10.754  1.00 19.28  ? 180 GLU A CG  1 
ATOM   1475  C  CD  . GLU A  1 180 ? 36.663  -13.728 9.750   1.00 21.34  ? 180 GLU A CD  1 
ATOM   1476  O  OE1 . GLU A  1 180 ? 37.881  -13.360 9.842   1.00 21.27  ? 180 GLU A OE1 1 
ATOM   1477  O  OE2 . GLU A  1 180 ? 36.228  -14.462 8.863   1.00 23.08  ? 180 GLU A OE2 1 
ATOM   1478  N  N   . GLU A  1 181 ? 34.778  -12.928 14.894  1.00 11.95  ? 181 GLU A N   1 
ATOM   1479  C  CA  . GLU A  1 181 ? 34.000  -13.773 15.782  1.00 12.43  ? 181 GLU A CA  1 
ATOM   1480  C  C   . GLU A  1 181 ? 32.569  -13.340 15.924  1.00 11.42  ? 181 GLU A C   1 
ATOM   1481  O  O   . GLU A  1 181 ? 31.749  -14.123 16.389  1.00 13.20  ? 181 GLU A O   1 
ATOM   1482  C  CB  . GLU A  1 181 ? 34.625  -13.778 17.181  1.00 14.13  ? 181 GLU A CB  1 
ATOM   1483  C  CG  . GLU A  1 181 ? 36.021  -14.435 17.263  1.00 15.27  ? 181 GLU A CG  1 
ATOM   1484  C  CD  . GLU A  1 181 ? 36.671  -14.274 18.630  1.00 16.69  ? 181 GLU A CD  1 
ATOM   1485  O  OE1 . GLU A  1 181 ? 36.038  -13.784 19.606  1.00 18.04  ? 181 GLU A OE1 1 
ATOM   1486  O  OE2 . GLU A  1 181 ? 37.881  -14.522 18.728  1.00 19.73  ? 181 GLU A OE2 1 
ATOM   1487  N  N   . LEU A  1 182 ? 32.231  -12.110 15.558  1.00 10.92  ? 182 LEU A N   1 
ATOM   1488  C  CA  . LEU A  1 182 ? 30.876  -11.625 15.644  1.00 10.07  ? 182 LEU A CA  1 
ATOM   1489  C  C   . LEU A  1 182 ? 30.048  -11.995 14.437  1.00 10.33  ? 182 LEU A C   1 
ATOM   1490  O  O   . LEU A  1 182 ? 28.833  -11.794 14.398  1.00 10.68  ? 182 LEU A O   1 
ATOM   1491  C  CB  . LEU A  1 182 ? 30.863  -10.105 15.813  1.00 10.29  ? 182 LEU A CB  1 
ATOM   1492  C  CG  . LEU A  1 182 ? 31.644  -9.590  16.992  1.00 10.14  ? 182 LEU A CG  1 
ATOM   1493  C  CD1 . LEU A  1 182 ? 31.556  -8.075  16.975  1.00 12.05  ? 182 LEU A CD1 1 
ATOM   1494  C  CD2 . LEU A  1 182 ? 31.151  -10.130 18.325  1.00 11.99  ? 182 LEU A CD2 1 
ATOM   1495  N  N   . LEU A  1 183 ? 30.699  -12.499 13.385  1.00 11.00  ? 183 LEU A N   1 
ATOM   1496  C  CA  . LEU A  1 183 ? 30.036  -12.841 12.148  1.00 10.37  ? 183 LEU A CA  1 
ATOM   1497  C  C   . LEU A  1 183 ? 29.444  -14.225 12.256  1.00 11.13  ? 183 LEU A C   1 
ATOM   1498  O  O   . LEU A  1 183 ? 29.962  -15.075 12.991  1.00 12.11  ? 183 LEU A O   1 
ATOM   1499  C  CB  . LEU A  1 183 ? 30.999  -12.750 10.977  1.00 11.79  ? 183 LEU A CB  1 
ATOM   1500  C  CG  . LEU A  1 183 ? 31.643  -11.368 10.772  1.00 12.84  ? 183 LEU A CG  1 
ATOM   1501  C  CD1 . LEU A  1 183 ? 32.485  -11.347 9.511   1.00 17.06  ? 183 LEU A CD1 1 
ATOM   1502  C  CD2 . LEU A  1 183 ? 30.585  -10.270 10.746  1.00 13.02  ? 183 LEU A CD2 1 
ATOM   1503  N  N   . PRO A  1 184 ? 28.377  -14.520 11.510  1.00 10.76  ? 184 PRO A N   1 
ATOM   1504  C  CA  . PRO A  1 184 ? 27.734  -15.831 11.538  1.00 12.23  ? 184 PRO A CA  1 
ATOM   1505  C  C   . PRO A  1 184 ? 28.451  -16.877 10.762  1.00 15.04  ? 184 PRO A C   1 
ATOM   1506  O  O   . PRO A  1 184 ? 29.486  -16.562 10.101  1.00 15.65  ? 184 PRO A O   1 
ATOM   1507  C  CB  . PRO A  1 184 ? 26.311  -15.496 10.959  1.00 14.21  ? 184 PRO A CB  1 
ATOM   1508  C  CG  . PRO A  1 184 ? 26.695  -14.460 9.903   1.00 13.33  ? 184 PRO A CG  1 
ATOM   1509  C  CD  . PRO A  1 184 ? 27.691  -13.583 10.589  1.00 11.70  ? 184 PRO A CD  1 
ATOM   1510  N  N   . GLU A  1 185 ? 27.842  -18.080 10.780  1.00 16.10  ? 185 GLU A N   1 
ATOM   1511  C  CA  . GLU A  1 185 ? 28.284  -19.148 9.898   1.00 16.97  ? 185 GLU A CA  1 
ATOM   1512  C  C   . GLU A  1 185 ? 28.041  -18.819 8.458   1.00 17.37  ? 185 GLU A C   1 
ATOM   1513  O  O   . GLU A  1 185 ? 27.081  -18.119 8.100   1.00 16.67  ? 185 GLU A O   1 
ATOM   1514  C  CB  . GLU A  1 185 ? 27.530  -20.477 10.247  1.00 20.44  ? 185 GLU A CB  1 
ATOM   1515  C  CG  . GLU A  1 185 ? 27.958  -20.917 11.648  1.00 25.39  ? 185 GLU A CG  1 
ATOM   1516  C  CD  . GLU A  1 185 ? 29.473  -21.133 11.781  1.00 38.18  ? 185 GLU A CD  1 
ATOM   1517  O  OE1 . GLU A  1 185 ? 30.010  -21.979 11.044  1.00 42.31  ? 185 GLU A OE1 1 
ATOM   1518  O  OE2 . GLU A  1 185 ? 30.129  -20.460 12.591  1.00 47.44  ? 185 GLU A OE2 1 
ATOM   1519  N  N   . ARG A  1 186 ? 28.964  -19.310 7.592   1.00 16.09  ? 186 ARG A N   1 
ATOM   1520  C  CA  . ARG A  1 186 ? 28.761  -19.265 6.120   1.00 17.32  ? 186 ARG A CA  1 
ATOM   1521  C  C   . ARG A  1 186 ? 28.562  -17.801 5.723   1.00 15.83  ? 186 ARG A C   1 
ATOM   1522  O  O   . ARG A  1 186 ? 27.597  -17.431 5.039   1.00 15.29  ? 186 ARG A O   1 
ATOM   1523  C  CB  . ARG A  1 186 ? 27.621  -20.220 5.619   1.00 21.68  ? 186 ARG A CB  1 
ATOM   1524  C  CG  . ARG A  1 186 ? 27.924  -21.664 5.927   1.00 25.01  ? 186 ARG A CG  1 
ATOM   1525  C  CD  . ARG A  1 186 ? 26.936  -22.664 5.391   1.00 28.59  ? 186 ARG A CD  1 
ATOM   1526  N  NE  . ARG A  1 186 ? 25.587  -22.450 5.890   1.00 27.26  ? 186 ARG A NE  1 
ATOM   1527  C  CZ  . ARG A  1 186 ? 25.176  -22.737 7.099   1.00 29.89  ? 186 ARG A CZ  1 
ATOM   1528  N  NH1 . ARG A  1 186 ? 26.023  -23.129 8.018   1.00 38.22  ? 186 ARG A NH1 1 
ATOM   1529  N  NH2 . ARG A  1 186 ? 23.915  -22.473 7.448   1.00 37.81  ? 186 ARG A NH2 1 
ATOM   1530  N  N   . THR A  1 187 ? 29.579  -17.011 6.033   1.00 13.63  ? 187 THR A N   1 
ATOM   1531  C  CA  . THR A  1 187 ? 29.543  -15.659 5.569   1.00 14.24  ? 187 THR A CA  1 
ATOM   1532  C  C   . THR A  1 187 ? 29.524  -15.522 4.075   1.00 15.26  ? 187 THR A C   1 
ATOM   1533  O  O   . THR A  1 187 ? 29.217  -14.436 3.585   1.00 15.02  ? 187 THR A O   1 
ATOM   1534  C  CB  . THR A  1 187 ? 30.651  -14.789 6.169   1.00 13.82  ? 187 THR A CB  1 
ATOM   1535  O  OG1 . THR A  1 187 ? 31.904  -15.471 6.023   1.00 17.94  ? 187 THR A OG1 1 
ATOM   1536  C  CG2 . THR A  1 187 ? 30.458  -14.513 7.659   1.00 15.03  ? 187 THR A CG2 1 
ATOM   1537  N  N   . ALA A  1 188 ? 29.848  -16.563 3.328   1.00 16.03  ? 188 ALA A N   1 
ATOM   1538  C  CA  . ALA A  1 188 ? 29.646  -16.542 1.870   1.00 16.01  ? 188 ALA A CA  1 
ATOM   1539  C  C   . ALA A  1 188 ? 28.228  -16.277 1.432   1.00 14.05  ? 188 ALA A C   1 
ATOM   1540  O  O   . ALA A  1 188 ? 28.018  -15.840 0.319   1.00 14.63  ? 188 ALA A O   1 
ATOM   1541  C  CB  . ALA A  1 188 ? 30.134  -17.876 1.223   1.00 20.95  ? 188 ALA A CB  1 
ATOM   1542  N  N   . GLU A  1 189 ? 27.289  -16.587 2.340   1.00 13.51  ? 189 GLU A N   1 
ATOM   1543  C  CA  . GLU A  1 189 ? 25.848  -16.476 2.007   1.00 12.89  ? 189 GLU A CA  1 
ATOM   1544  C  C   . GLU A  1 189 ? 25.331  -15.114 2.540   1.00 11.29  ? 189 GLU A C   1 
ATOM   1545  O  O   . GLU A  1 189 ? 25.310  -14.909 3.761   1.00 10.86  ? 189 GLU A O   1 
ATOM   1546  C  CB  . GLU A  1 189 ? 25.051  -17.635 2.701   1.00 14.35  ? 189 GLU A CB  1 
ATOM   1547  C  CG  . GLU A  1 189 ? 25.497  -19.023 2.163   1.00 18.90  ? 189 GLU A CG  1 
ATOM   1548  C  CD  . GLU A  1 189 ? 24.953  -20.230 2.968   1.00 24.68  ? 189 GLU A CD  1 
ATOM   1549  O  OE1 . GLU A  1 189 ? 24.246  -20.091 3.990   1.00 20.70  ? 189 GLU A OE1 1 
ATOM   1550  O  OE2 . GLU A  1 189 ? 25.432  -21.335 2.647   1.00 32.90  ? 189 GLU A OE2 1 
ATOM   1551  N  N   . TYR A  1 190 ? 24.894  -14.220 1.630   1.00 10.50  ? 190 TYR A N   1 
ATOM   1552  C  CA  . TYR A  1 190 ? 24.449  -12.927 2.051   1.00 9.13   ? 190 TYR A CA  1 
ATOM   1553  C  C   . TYR A  1 190 ? 23.487  -12.362 1.033   1.00 10.51  ? 190 TYR A C   1 
ATOM   1554  O  O   . TYR A  1 190 ? 23.448  -12.798 -0.151  1.00 11.15  ? 190 TYR A O   1 
ATOM   1555  C  CB  . TYR A  1 190 ? 25.632  -11.965 2.255   1.00 10.51  ? 190 TYR A CB  1 
ATOM   1556  C  CG  . TYR A  1 190 ? 26.578  -11.822 1.075   1.00 11.14  ? 190 TYR A CG  1 
ATOM   1557  C  CD1 . TYR A  1 190 ? 26.288  -10.921 0.049   1.00 12.41  ? 190 TYR A CD1 1 
ATOM   1558  C  CD2 . TYR A  1 190 ? 27.772  -12.576 1.015   1.00 12.69  ? 190 TYR A CD2 1 
ATOM   1559  C  CE1 . TYR A  1 190 ? 27.176  -10.740 -1.039  1.00 12.74  ? 190 TYR A CE1 1 
ATOM   1560  C  CE2 . TYR A  1 190 ? 28.646  -12.388 -0.062  1.00 13.35  ? 190 TYR A CE2 1 
ATOM   1561  C  CZ  . TYR A  1 190 ? 28.349  -11.476 -1.052  1.00 13.45  ? 190 TYR A CZ  1 
ATOM   1562  O  OH  . TYR A  1 190 ? 29.177  -11.258 -2.157  1.00 15.55  ? 190 TYR A OH  1 
ATOM   1563  N  N   . TYR A  1 191 ? 22.754  -11.343 1.490   1.00 9.84   ? 191 TYR A N   1 
ATOM   1564  C  CA  . TYR A  1 191 ? 21.932  -10.471 0.710   1.00 9.87   ? 191 TYR A CA  1 
ATOM   1565  C  C   . TYR A  1 191 ? 22.695  -9.175  0.426   1.00 9.48   ? 191 TYR A C   1 
ATOM   1566  O  O   . TYR A  1 191 ? 23.401  -8.707  1.300   1.00 10.79  ? 191 TYR A O   1 
ATOM   1567  C  CB  . TYR A  1 191 ? 20.682  -10.097 1.490   1.00 10.40  ? 191 TYR A CB  1 
ATOM   1568  C  CG  . TYR A  1 191 ? 19.820  -11.189 2.027   1.00 11.04  ? 191 TYR A CG  1 
ATOM   1569  C  CD1 . TYR A  1 191 ? 18.784  -11.779 1.308   1.00 11.59  ? 191 TYR A CD1 1 
ATOM   1570  C  CD2 . TYR A  1 191 ? 20.052  -11.659 3.337   1.00 10.43  ? 191 TYR A CD2 1 
ATOM   1571  C  CE1 . TYR A  1 191 ? 17.959  -12.769 1.870   1.00 12.63  ? 191 TYR A CE1 1 
ATOM   1572  C  CE2 . TYR A  1 191 ? 19.243  -12.631 3.921   1.00 11.67  ? 191 TYR A CE2 1 
ATOM   1573  C  CZ  . TYR A  1 191 ? 18.213  -13.187 3.193   1.00 12.09  ? 191 TYR A CZ  1 
ATOM   1574  O  OH  . TYR A  1 191 ? 17.435  -14.151 3.722   1.00 14.26  ? 191 TYR A OH  1 
ATOM   1575  N  N   . ARG A  1 192 ? 22.516  -8.612  -0.767  1.00 10.48  ? 192 ARG A N   1 
ATOM   1576  C  CA  . ARG A  1 192 ? 23.217  -7.394  -1.165  1.00 10.17  ? 192 ARG A CA  1 
ATOM   1577  C  C   . ARG A  1 192 ? 22.282  -6.462  -1.841  1.00 10.61  ? 192 ARG A C   1 
ATOM   1578  O  O   . ARG A  1 192 ? 21.557  -6.824  -2.779  1.00 12.10  ? 192 ARG A O   1 
ATOM   1579  C  CB  . ARG A  1 192 ? 24.366  -7.800  -2.134  1.00 11.52  ? 192 ARG A CB  1 
ATOM   1580  C  CG  . ARG A  1 192 ? 24.987  -6.687  -2.977  1.00 12.75  ? 192 ARG A CG  1 
ATOM   1581  C  CD  . ARG A  1 192 ? 25.760  -5.724  -2.080  1.00 12.86  ? 192 ARG A CD  1 
ATOM   1582  N  NE  . ARG A  1 192 ? 26.774  -6.341  -1.195  1.00 14.22  ? 192 ARG A NE  1 
ATOM   1583  C  CZ  . ARG A  1 192 ? 27.886  -6.977  -1.583  1.00 13.00  ? 192 ARG A CZ  1 
ATOM   1584  N  NH1 . ARG A  1 192 ? 28.279  -6.899  -2.878  1.00 14.62  ? 192 ARG A NH1 1 
ATOM   1585  N  NH2 . ARG A  1 192 ? 28.722  -7.513  -0.691  1.00 14.20  ? 192 ARG A NH2 1 
ATOM   1586  N  N   . TYR A  1 193 ? 22.306  -5.195  -1.440  1.00 9.90   ? 193 TYR A N   1 
ATOM   1587  C  CA  . TYR A  1 193 ? 21.499  -4.149  -2.116  1.00 10.58  ? 193 TYR A CA  1 
ATOM   1588  C  C   . TYR A  1 193 ? 22.073  -2.803  -1.792  1.00 10.54  ? 193 TYR A C   1 
ATOM   1589  O  O   . TYR A  1 193 ? 22.821  -2.604  -0.830  1.00 11.10  ? 193 TYR A O   1 
ATOM   1590  C  CB  . TYR A  1 193 ? 19.996  -4.265  -1.775  1.00 10.92  ? 193 TYR A CB  1 
ATOM   1591  C  CG  . TYR A  1 193 ? 19.642  -3.754  -0.393  1.00 9.93   ? 193 TYR A CG  1 
ATOM   1592  C  CD1 . TYR A  1 193 ? 19.855  -4.498  0.734   1.00 9.51   ? 193 TYR A CD1 1 
ATOM   1593  C  CD2 . TYR A  1 193 ? 19.081  -2.486  -0.245  1.00 10.71  ? 193 TYR A CD2 1 
ATOM   1594  C  CE1 . TYR A  1 193 ? 19.520  -3.971  2.004   1.00 9.08   ? 193 TYR A CE1 1 
ATOM   1595  C  CE2 . TYR A  1 193 ? 18.745  -1.924  0.978   1.00 10.84  ? 193 TYR A CE2 1 
ATOM   1596  C  CZ  . TYR A  1 193 ? 18.993  -2.687  2.102   1.00 8.94   ? 193 TYR A CZ  1 
ATOM   1597  O  OH  . TYR A  1 193 ? 18.679  -2.134  3.327   1.00 8.64   ? 193 TYR A OH  1 
ATOM   1598  N  N   . ARG A  1 194 ? 21.740  -1.841  -2.662  1.00 11.17  ? 194 ARG A N   1 
ATOM   1599  C  CA  . ARG A  1 194 ? 22.119  -0.439  -2.444  1.00 10.81  ? 194 ARG A CA  1 
ATOM   1600  C  C   . ARG A  1 194 ? 21.021  0.232   -1.640  1.00 11.23  ? 194 ARG A C   1 
ATOM   1601  O  O   . ARG A  1 194 ? 19.866  0.246   -2.011  1.00 12.28  ? 194 ARG A O   1 
ATOM   1602  C  CB  . ARG A  1 194 ? 22.287  0.297   -3.784  1.00 15.21  ? 194 ARG A CB  1 
ATOM   1603  C  CG  . ARG A  1 194 ? 23.435  -0.270  -4.531  1.00 18.08  ? 194 ARG A CG  1 
ATOM   1604  C  CD  . ARG A  1 194 ? 24.750  0.215   -3.991  1.00 34.18  ? 194 ARG A CD  1 
ATOM   1605  N  NE  . ARG A  1 194 ? 25.845  -0.348  -4.789  1.00 46.26  ? 194 ARG A NE  1 
ATOM   1606  C  CZ  . ARG A  1 194 ? 27.013  0.245   -4.989  1.00 37.97  ? 194 ARG A CZ  1 
ATOM   1607  N  NH1 . ARG A  1 194 ? 27.244  1.437   -4.449  1.00 50.71  ? 194 ARG A NH1 1 
ATOM   1608  N  NH2 . ARG A  1 194 ? 27.919  -0.372  -5.746  1.00 49.29  ? 194 ARG A NH2 1 
ATOM   1609  N  N   . GLY A  1 195 ? 21.420  0.836   -0.530  1.00 9.28   ? 195 GLY A N   1 
ATOM   1610  C  CA  . GLY A  1 195 ? 20.485  1.600   0.313   1.00 10.15  ? 195 GLY A CA  1 
ATOM   1611  C  C   . GLY A  1 195 ? 21.106  2.712   1.029   1.00 9.43   ? 195 GLY A C   1 
ATOM   1612  O  O   . GLY A  1 195 ? 21.949  3.442   0.468   1.00 10.39  ? 195 GLY A O   1 
ATOM   1613  N  N   . SER A  1 196 ? 20.671  2.929   2.257   1.00 8.60   ? 196 SER A N   1 
ATOM   1614  C  CA  . SER A  1 196 ? 20.976  4.169   2.939   1.00 9.61   ? 196 SER A CA  1 
ATOM   1615  C  C   . SER A  1 196 ? 21.420  3.907   4.369   1.00 9.33   ? 196 SER A C   1 
ATOM   1616  O  O   . SER A  1 196 ? 21.262  2.774   4.903   1.00 9.67   ? 196 SER A O   1 
ATOM   1617  C  CB  . SER A  1 196 ? 19.733  5.068   2.991   1.00 9.79   ? 196 SER A CB  1 
ATOM   1618  O  OG  . SER A  1 196 ? 18.756  4.607   3.980   1.00 9.31   ? 196 SER A OG  1 
ATOM   1619  N  N   . LEU A  1 197 ? 21.932  4.950   5.029   1.00 9.53   ? 197 LEU A N   1 
ATOM   1620  C  CA  . LEU A  1 197 ? 21.962  4.907   6.443   1.00 9.18   ? 197 LEU A CA  1 
ATOM   1621  C  C   . LEU A  1 197 ? 20.566  4.701   6.981   1.00 8.92   ? 197 LEU A C   1 
ATOM   1622  O  O   . LEU A  1 197 ? 19.625  5.307   6.462   1.00 9.12   ? 197 LEU A O   1 
ATOM   1623  C  CB  . LEU A  1 197 ? 22.516  6.187   7.069   1.00 11.00  ? 197 LEU A CB  1 
ATOM   1624  C  CG  . LEU A  1 197 ? 23.999  6.490   6.917   1.00 14.02  ? 197 LEU A CG  1 
ATOM   1625  C  CD1 . LEU A  1 197 ? 24.372  6.903   5.537   1.00 18.90  ? 197 LEU A CD1 1 
ATOM   1626  C  CD2 . LEU A  1 197 ? 24.358  7.577   7.950   1.00 21.04  ? 197 LEU A CD2 1 
ATOM   1627  N  N   . THR A  1 198 ? 20.401  3.927   8.063   1.00 9.26   ? 198 THR A N   1 
ATOM   1628  C  CA  . THR A  1 198 ? 19.111  3.750   8.675   1.00 8.90   ? 198 THR A CA  1 
ATOM   1629  C  C   . THR A  1 198 ? 18.824  4.764   9.795   1.00 9.08   ? 198 THR A C   1 
ATOM   1630  O  O   . THR A  1 198 ? 17.787  4.709   10.429  1.00 9.30   ? 198 THR A O   1 
ATOM   1631  C  CB  . THR A  1 198 ? 18.944  2.338   9.257   1.00 9.08   ? 198 THR A CB  1 
ATOM   1632  O  OG1 . THR A  1 198 ? 19.864  2.234   10.348  1.00 8.82   ? 198 THR A OG1 1 
ATOM   1633  C  CG2 . THR A  1 198 ? 19.175  1.297   8.239   1.00 9.09   ? 198 THR A CG2 1 
ATOM   1634  N  N   . THR A  1 199 ? 19.773  5.674   9.989   1.00 10.33  ? 199 THR A N   1 
ATOM   1635  C  CA  . THR A  1 199 ? 19.648  6.750   10.951  1.00 11.95  ? 199 THR A CA  1 
ATOM   1636  C  C   . THR A  1 199 ? 19.850  8.047   10.193  1.00 10.84  ? 199 THR A C   1 
ATOM   1637  O  O   . THR A  1 199 ? 20.558  8.039   9.163   1.00 11.47  ? 199 THR A O   1 
ATOM   1638  C  CB  . THR A  1 199 ? 20.873  6.649   11.965  1.00 15.20  ? 199 THR A CB  1 
ATOM   1639  O  OG1 . THR A  1 199 ? 22.132  6.459   11.240  1.00 20.82  ? 199 THR A OG1 1 
ATOM   1640  C  CG2 . THR A  1 199 ? 20.630  5.355   12.846  1.00 15.37  ? 199 THR A CG2 1 
ATOM   1641  N  N   . PRO A  1 200 ? 19.369  9.164   10.736  1.00 10.69  ? 200 PRO A N   1 
ATOM   1642  C  CA  . PRO A  1 200 ? 19.712  10.462  10.166  1.00 10.81  ? 200 PRO A CA  1 
ATOM   1643  C  C   . PRO A  1 200 ? 21.235  10.562  10.018  1.00 11.59  ? 200 PRO A C   1 
ATOM   1644  O  O   . PRO A  1 200 ? 21.938  10.149  10.969  1.00 13.74  ? 200 PRO A O   1 
ATOM   1645  C  CB  . PRO A  1 200 ? 19.170  11.422  11.203  1.00 12.09  ? 200 PRO A CB  1 
ATOM   1646  C  CG  . PRO A  1 200 ? 17.967  10.701  11.707  1.00 12.40  ? 200 PRO A CG  1 
ATOM   1647  C  CD  . PRO A  1 200 ? 18.432  9.263   11.874  1.00 12.51  ? 200 PRO A CD  1 
ATOM   1648  N  N   . PRO A  1 201 ? 21.764  11.107  8.917   1.00 11.54  ? 201 PRO A N   1 
ATOM   1649  C  CA  . PRO A  1 201 ? 21.007  11.811  7.873   1.00 11.24  ? 201 PRO A CA  1 
ATOM   1650  C  C   . PRO A  1 201 ? 20.416  10.952  6.781   1.00 10.85  ? 201 PRO A C   1 
ATOM   1651  O  O   . PRO A  1 201 ? 19.944  11.535  5.821   1.00 12.12  ? 201 PRO A O   1 
ATOM   1652  C  CB  . PRO A  1 201 ? 22.065  12.793  7.232   1.00 13.77  ? 201 PRO A CB  1 
ATOM   1653  C  CG  . PRO A  1 201 ? 23.120  12.845  8.268   1.00 17.02  ? 201 PRO A CG  1 
ATOM   1654  C  CD  . PRO A  1 201 ? 23.184  11.440  8.825   1.00 13.85  ? 201 PRO A CD  1 
ATOM   1655  N  N   . CYS A  1 202 ? 20.449  9.640   6.914   1.00 10.48  ? 202 CYS A N   1 
ATOM   1656  C  CA  . CYS A  1 202 ? 19.771  8.733   5.947   1.00 9.95   ? 202 CYS A CA  1 
ATOM   1657  C  C   . CYS A  1 202 ? 20.343  8.788   4.546   1.00 9.42   ? 202 CYS A C   1 
ATOM   1658  O  O   . CYS A  1 202 ? 19.644  8.532   3.583   1.00 10.11  ? 202 CYS A O   1 
ATOM   1659  C  CB  . CYS A  1 202 ? 18.268  8.947   5.873   1.00 10.24  ? 202 CYS A CB  1 
ATOM   1660  S  SG  . CYS A  1 202 ? 17.378  8.902   7.451   1.00 10.45  ? 202 CYS A SG  1 
ATOM   1661  N  N   . ASN A  1 203 ? 21.628  9.152   4.416   1.00 10.29  ? 203 ASN A N   1 
ATOM   1662  C  CA  . ASN A  1 203 ? 22.165  9.315   3.092   1.00 11.90  ? 203 ASN A CA  1 
ATOM   1663  C  C   . ASN A  1 203 ? 22.089  8.041   2.307   1.00 11.12  ? 203 ASN A C   1 
ATOM   1664  O  O   . ASN A  1 203 ? 22.381  6.957   2.837   1.00 10.23  ? 203 ASN A O   1 
ATOM   1665  C  CB  . ASN A  1 203 ? 23.642  9.756   3.161   1.00 13.62  ? 203 ASN A CB  1 
ATOM   1666  C  CG  . ASN A  1 203 ? 23.795  10.955  4.012   1.00 15.48  ? 203 ASN A CG  1 
ATOM   1667  O  OD1 . ASN A  1 203 ? 23.829  10.822  5.212   1.00 15.80  ? 203 ASN A OD1 1 
ATOM   1668  N  ND2 . ASN A  1 203 ? 23.774  12.101  3.411   1.00 19.24  ? 203 ASN A ND2 1 
ATOM   1669  N  N   . PRO A  1 204 ? 21.751  8.123   1.002   1.00 11.03  ? 204 PRO A N   1 
ATOM   1670  C  CA  . PRO A  1 204 ? 21.600  6.914   0.184   1.00 11.64  ? 204 PRO A CA  1 
ATOM   1671  C  C   . PRO A  1 204 ? 22.922  6.398   -0.391  1.00 10.88  ? 204 PRO A C   1 
ATOM   1672  O  O   . PRO A  1 204 ? 23.079  6.281   -1.602  1.00 13.61  ? 204 PRO A O   1 
ATOM   1673  C  CB  . PRO A  1 204 ? 20.594  7.313   -0.884  1.00 12.76  ? 204 PRO A CB  1 
ATOM   1674  C  CG  . PRO A  1 204 ? 20.969  8.779   -1.087  1.00 14.94  ? 204 PRO A CG  1 
ATOM   1675  C  CD  . PRO A  1 204 ? 21.199  9.318   0.296   1.00 13.80  ? 204 PRO A CD  1 
ATOM   1676  N  N   . THR A  1 205 ? 23.865  6.158   0.511   1.00 11.75  ? 205 THR A N   1 
ATOM   1677  C  CA  . THR A  1 205 ? 25.261  5.983   0.117   1.00 12.09  ? 205 THR A CA  1 
ATOM   1678  C  C   . THR A  1 205 ? 25.840  4.639   0.653   1.00 11.87  ? 205 THR A C   1 
ATOM   1679  O  O   . THR A  1 205 ? 27.042  4.426   0.631   1.00 12.87  ? 205 THR A O   1 
ATOM   1680  C  CB  . THR A  1 205 ? 26.104  7.106   0.711   1.00 13.27  ? 205 THR A CB  1 
ATOM   1681  O  OG1 . THR A  1 205 ? 25.839  7.142   2.106   1.00 13.32  ? 205 THR A OG1 1 
ATOM   1682  C  CG2 . THR A  1 205 ? 25.696  8.426   0.041   1.00 15.76  ? 205 THR A CG2 1 
ATOM   1683  N  N   . VAL A  1 206 ? 24.936  3.719   1.093   1.00 10.66  ? 206 VAL A N   1 
ATOM   1684  C  CA  . VAL A  1 206 ? 25.400  2.465   1.697   1.00 10.44  ? 206 VAL A CA  1 
ATOM   1685  C  C   . VAL A  1 206 ? 25.190  1.295   0.761   1.00 10.50  ? 206 VAL A C   1 
ATOM   1686  O  O   . VAL A  1 206 ? 24.097  1.005   0.327   1.00 11.67  ? 206 VAL A O   1 
ATOM   1687  C  CB  . VAL A  1 206 ? 24.628  2.218   3.035   1.00 10.49  ? 206 VAL A CB  1 
ATOM   1688  C  CG1 . VAL A  1 206 ? 25.049  0.862   3.591   1.00 10.94  ? 206 VAL A CG1 1 
ATOM   1689  C  CG2 . VAL A  1 206 ? 24.876  3.323   4.013   1.00 11.01  ? 206 VAL A CG2 1 
ATOM   1690  N  N   . LEU A  1 207 ? 26.278  0.550   0.535   1.00 10.39  ? 207 LEU A N   1 
ATOM   1691  C  CA  . LEU A  1 207 ? 26.209  -0.801  -0.005  1.00 11.06  ? 207 LEU A CA  1 
ATOM   1692  C  C   . LEU A  1 207 ? 25.987  -1.762  1.162   1.00 9.11   ? 207 LEU A C   1 
ATOM   1693  O  O   . LEU A  1 207 ? 26.873  -1.897  2.033   1.00 10.03  ? 207 LEU A O   1 
ATOM   1694  C  CB  . LEU A  1 207 ? 27.483  -1.097  -0.786  1.00 13.17  ? 207 LEU A CB  1 
ATOM   1695  C  CG  . LEU A  1 207 ? 27.383  -2.411  -1.593  1.00 17.04  ? 207 LEU A CG  1 
ATOM   1696  C  CD1 . LEU A  1 207 ? 26.312  -2.345  -2.742  1.00 22.09  ? 207 LEU A CD1 1 
ATOM   1697  C  CD2 . LEU A  1 207 ? 28.675  -2.879  -2.231  1.00 26.40  ? 207 LEU A CD2 1 
ATOM   1698  N  N   . TRP A  1 208 ? 24.802  -2.351  1.203   1.00 8.87   ? 208 TRP A N   1 
ATOM   1699  C  CA  . TRP A  1 208 ? 24.440  -3.289  2.302   1.00 8.42   ? 208 TRP A CA  1 
ATOM   1700  C  C   . TRP A  1 208 ? 24.810  -4.698  1.981   1.00 8.32   ? 208 TRP A C   1 
ATOM   1701  O  O   . TRP A  1 208 ? 24.561  -5.191  0.867   1.00 9.92   ? 208 TRP A O   1 
ATOM   1702  C  CB  . TRP A  1 208 ? 22.946  -3.207  2.542   1.00 8.88   ? 208 TRP A CB  1 
ATOM   1703  C  CG  . TRP A  1 208 ? 22.549  -2.034  3.382   1.00 8.91   ? 208 TRP A CG  1 
ATOM   1704  C  CD1 . TRP A  1 208 ? 22.078  -0.807  2.943   1.00 9.51   ? 208 TRP A CD1 1 
ATOM   1705  C  CD2 . TRP A  1 208 ? 22.671  -1.916  4.791   1.00 8.41   ? 208 TRP A CD2 1 
ATOM   1706  N  NE1 . TRP A  1 208 ? 21.918  0.067   3.987   1.00 9.80   ? 208 TRP A NE1 1 
ATOM   1707  C  CE2 . TRP A  1 208 ? 22.274  -0.568  5.149   1.00 8.19   ? 208 TRP A CE2 1 
ATOM   1708  C  CE3 . TRP A  1 208 ? 23.086  -2.778  5.802   1.00 8.55   ? 208 TRP A CE3 1 
ATOM   1709  C  CZ2 . TRP A  1 208 ? 22.297  -0.113  6.455   1.00 9.06   ? 208 TRP A CZ2 1 
ATOM   1710  C  CZ3 . TRP A  1 208 ? 23.051  -2.297  7.109   1.00 8.76   ? 208 TRP A CZ3 1 
ATOM   1711  C  CH2 . TRP A  1 208 ? 22.708  -0.992  7.418   1.00 8.96   ? 208 TRP A CH2 1 
ATOM   1712  N  N   . THR A  1 209 ? 25.347  -5.381  2.972   1.00 8.06   ? 209 THR A N   1 
ATOM   1713  C  CA  . THR A  1 209 ? 25.562  -6.833  2.945   1.00 8.54   ? 209 THR A CA  1 
ATOM   1714  C  C   . THR A  1 209 ? 24.926  -7.351  4.205   1.00 8.21   ? 209 THR A C   1 
ATOM   1715  O  O   . THR A  1 209 ? 25.398  -7.007  5.308   1.00 9.89   ? 209 THR A O   1 
ATOM   1716  C  CB  . THR A  1 209 ? 27.037  -7.189  2.904   1.00 9.10   ? 209 THR A CB  1 
ATOM   1717  O  OG1 . THR A  1 209 ? 27.628  -6.600  1.728   1.00 10.86  ? 209 THR A OG1 1 
ATOM   1718  C  CG2 . THR A  1 209 ? 27.216  -8.697  2.854   1.00 10.24  ? 209 THR A CG2 1 
ATOM   1719  N  N   . VAL A  1 210 ? 23.836  -8.100  4.083   1.00 8.13   ? 210 VAL A N   1 
ATOM   1720  C  CA  . VAL A  1 210 ? 23.179  -8.702  5.233   1.00 7.84   ? 210 VAL A CA  1 
ATOM   1721  C  C   . VAL A  1 210 ? 23.439  -10.185 5.189   1.00 8.07   ? 210 VAL A C   1 
ATOM   1722  O  O   . VAL A  1 210 ? 23.079  -10.861 4.229   1.00 9.15   ? 210 VAL A O   1 
ATOM   1723  C  CB  . VAL A  1 210 ? 21.642  -8.410  5.218   1.00 8.90   ? 210 VAL A CB  1 
ATOM   1724  C  CG1 . VAL A  1 210 ? 20.992  -9.036  6.462   1.00 9.46   ? 210 VAL A CG1 1 
ATOM   1725  C  CG2 . VAL A  1 210 ? 21.342  -6.942  5.074   1.00 9.71   ? 210 VAL A CG2 1 
ATOM   1726  N  N   . PHE A  1 211 ? 24.142  -10.720 6.163   1.00 8.14   ? 211 PHE A N   1 
ATOM   1727  C  CA  . PHE A  1 211 ? 24.441  -12.137 6.113   1.00 8.89   ? 211 PHE A CA  1 
ATOM   1728  C  C   . PHE A  1 211 ? 23.195  -12.932 6.212   1.00 9.25   ? 211 PHE A C   1 
ATOM   1729  O  O   . PHE A  1 211 ? 22.257  -12.621 6.979   1.00 9.44   ? 211 PHE A O   1 
ATOM   1730  C  CB  . PHE A  1 211 ? 25.472  -12.474 7.175   1.00 9.21   ? 211 PHE A CB  1 
ATOM   1731  C  CG  . PHE A  1 211 ? 26.815  -11.868 6.889   1.00 9.57   ? 211 PHE A CG  1 
ATOM   1732  C  CD1 . PHE A  1 211 ? 27.588  -12.296 5.789   1.00 10.55  ? 211 PHE A CD1 1 
ATOM   1733  C  CD2 . PHE A  1 211 ? 27.275  -10.808 7.670   1.00 9.66   ? 211 PHE A CD2 1 
ATOM   1734  C  CE1 . PHE A  1 211 ? 28.795  -11.683 5.496   1.00 12.52  ? 211 PHE A CE1 1 
ATOM   1735  C  CE2 . PHE A  1 211 ? 28.533  -10.245 7.417   1.00 10.16  ? 211 PHE A CE2 1 
ATOM   1736  C  CZ  . PHE A  1 211 ? 29.273  -10.660 6.307   1.00 12.00  ? 211 PHE A CZ  1 
ATOM   1737  N  N   . ARG A  1 212 ? 23.124  -14.063 5.492   1.00 9.50   ? 212 ARG A N   1 
ATOM   1738  C  CA  . ARG A  1 212 ? 21.943  -14.897 5.509   1.00 9.40   ? 212 ARG A CA  1 
ATOM   1739  C  C   . ARG A  1 212 ? 21.652  -15.508 6.878   1.00 9.69   ? 212 ARG A C   1 
ATOM   1740  O  O   . ARG A  1 212 ? 20.488  -15.610 7.268   1.00 11.39  ? 212 ARG A O   1 
ATOM   1741  C  CB  . ARG A  1 212 ? 22.110  -16.022 4.517   1.00 10.64  ? 212 ARG A CB  1 
ATOM   1742  C  CG  . ARG A  1 212 ? 20.900  -16.898 4.363   1.00 13.45  ? 212 ARG A CG  1 
ATOM   1743  C  CD  . ARG A  1 212 ? 21.198  -18.138 3.528   1.00 16.50  ? 212 ARG A CD  1 
ATOM   1744  N  NE  . ARG A  1 212 ? 19.997  -18.871 3.205   1.00 23.57  ? 212 ARG A NE  1 
ATOM   1745  C  CZ  . ARG A  1 212 ? 19.875  -19.826 2.275   1.00 30.86  ? 212 ARG A CZ  1 
ATOM   1746  N  NH1 . ARG A  1 212 ? 20.925  -20.248 1.594   1.00 27.90  ? 212 ARG A NH1 1 
ATOM   1747  N  NH2 . ARG A  1 212 ? 18.687  -20.304 2.004   1.00 38.32  ? 212 ARG A NH2 1 
ATOM   1748  N  N   . ASN A  1 213 ? 22.698  -15.986 7.539   1.00 9.93   ? 213 ASN A N   1 
ATOM   1749  C  CA  . ASN A  1 213 ? 22.494  -16.784 8.749   1.00 11.34  ? 213 ASN A CA  1 
ATOM   1750  C  C   . ASN A  1 213 ? 22.671  -15.892 9.966   1.00 10.04  ? 213 ASN A C   1 
ATOM   1751  O  O   . ASN A  1 213 ? 23.555  -15.063 10.019  1.00 10.04  ? 213 ASN A O   1 
ATOM   1752  C  CB  . ASN A  1 213 ? 23.509  -17.888 8.773   1.00 12.23  ? 213 ASN A CB  1 
ATOM   1753  C  CG  . ASN A  1 213 ? 23.409  -18.746 7.551   1.00 14.71  ? 213 ASN A CG  1 
ATOM   1754  O  OD1 . ASN A  1 213 ? 24.433  -18.962 6.866   1.00 18.54  ? 213 ASN A OD1 1 
ATOM   1755  N  ND2 . ASN A  1 213 ? 22.217  -19.127 7.176   1.00 14.76  ? 213 ASN A ND2 1 
ATOM   1756  N  N   . PRO A  1 214 ? 21.789  -16.055 10.971  1.00 10.03  ? 214 PRO A N   1 
ATOM   1757  C  CA  . PRO A  1 214 ? 21.905  -15.264 12.169  1.00 10.09  ? 214 PRO A CA  1 
ATOM   1758  C  C   . PRO A  1 214 ? 22.996  -15.804 13.132  1.00 9.47   ? 214 PRO A C   1 
ATOM   1759  O  O   . PRO A  1 214 ? 23.407  -16.980 12.998  1.00 11.81  ? 214 PRO A O   1 
ATOM   1760  C  CB  . PRO A  1 214 ? 20.526  -15.426 12.847  1.00 11.49  ? 214 PRO A CB  1 
ATOM   1761  C  CG  . PRO A  1 214 ? 20.145  -16.798 12.433  1.00 13.25  ? 214 PRO A CG  1 
ATOM   1762  C  CD  . PRO A  1 214 ? 20.583  -16.900 10.972  1.00 13.43  ? 214 PRO A CD  1 
ATOM   1763  N  N   . VAL A  1 215 ? 23.389  -15.027 14.109  1.00 9.83   ? 215 VAL A N   1 
ATOM   1764  C  CA  . VAL A  1 215 ? 24.096  -15.496 15.263  1.00 10.11  ? 215 VAL A CA  1 
ATOM   1765  C  C   . VAL A  1 215 ? 23.135  -15.647 16.440  1.00 10.07  ? 215 VAL A C   1 
ATOM   1766  O  O   . VAL A  1 215 ? 22.065  -15.091 16.399  1.00 10.93  ? 215 VAL A O   1 
ATOM   1767  C  CB  . VAL A  1 215 ? 25.280  -14.567 15.645  1.00 10.62  ? 215 VAL A CB  1 
ATOM   1768  C  CG1 . VAL A  1 215 ? 26.344  -14.472 14.533  1.00 11.34  ? 215 VAL A CG1 1 
ATOM   1769  C  CG2 . VAL A  1 215 ? 24.809  -13.235 16.055  1.00 10.95  ? 215 VAL A CG2 1 
ATOM   1770  N  N   A GLN A  1 216 ? 23.679  -16.205 17.525  0.50 10.28  ? 216 GLN A N   1 
ATOM   1771  N  N   B GLN A  1 216 ? 23.439  -16.530 17.393  0.50 10.07  ? 216 GLN A N   1 
ATOM   1772  C  CA  A GLN A  1 216 ? 22.925  -16.379 18.747  0.50 10.42  ? 216 GLN A CA  1 
ATOM   1773  C  CA  B GLN A  1 216 ? 22.642  -16.662 18.615  0.50 10.37  ? 216 GLN A CA  1 
ATOM   1774  C  C   A GLN A  1 216 ? 23.607  -15.736 19.865  0.50 10.64  ? 216 GLN A C   1 
ATOM   1775  C  C   B GLN A  1 216 ? 23.407  -16.031 19.817  0.50 10.94  ? 216 GLN A C   1 
ATOM   1776  O  O   A GLN A  1 216 ? 24.842  -15.716 20.027  0.50 11.95  ? 216 GLN A O   1 
ATOM   1777  O  O   B GLN A  1 216 ? 24.610  -16.254 19.913  0.50 10.14  ? 216 GLN A O   1 
ATOM   1778  C  CB  A GLN A  1 216 ? 22.757  -17.864 19.104  0.50 14.30  ? 216 GLN A CB  1 
ATOM   1779  C  CB  B GLN A  1 216 ? 22.402  -18.184 18.831  0.50 11.29  ? 216 GLN A CB  1 
ATOM   1780  C  CG  A GLN A  1 216 ? 21.968  -18.543 18.010  0.50 15.36  ? 216 GLN A CG  1 
ATOM   1781  C  CG  B GLN A  1 216 ? 21.598  -18.936 17.772  0.50 12.64  ? 216 GLN A CG  1 
ATOM   1782  C  CD  A GLN A  1 216 ? 21.431  -19.872 18.385  0.50 15.29  ? 216 GLN A CD  1 
ATOM   1783  C  CD  B GLN A  1 216 ? 22.415  -19.142 16.473  0.50 13.01  ? 216 GLN A CD  1 
ATOM   1784  O  OE1 A GLN A  1 216 ? 21.882  -20.483 19.362  0.50 17.53  ? 216 GLN A OE1 1 
ATOM   1785  O  OE1 B GLN A  1 216 ? 23.644  -19.481 16.534  0.50 15.65  ? 216 GLN A OE1 1 
ATOM   1786  N  NE2 A GLN A  1 216 ? 20.397  -20.298 17.708  0.50 24.60  ? 216 GLN A NE2 1 
ATOM   1787  N  NE2 B GLN A  1 216 ? 21.800  -18.969 15.299  0.50 17.90  ? 216 GLN A NE2 1 
ATOM   1788  N  N   . ILE A  1 217 ? 22.720  -15.234 20.697  1.00 11.28  ? 217 ILE A N   1 
ATOM   1789  C  CA  . ILE A  1 217 ? 23.190  -14.797 22.016  1.00 11.81  ? 217 ILE A CA  1 
ATOM   1790  C  C   . ILE A  1 217 ? 22.211  -15.306 23.034  1.00 12.24  ? 217 ILE A C   1 
ATOM   1791  O  O   . ILE A  1 217 ? 21.065  -15.617 22.704  1.00 12.20  ? 217 ILE A O   1 
ATOM   1792  C  CB  . ILE A  1 217 ? 23.336  -13.253 22.110  1.00 11.51  ? 217 ILE A CB  1 
ATOM   1793  C  CG1 . ILE A  1 217 ? 21.994  -12.527 21.938  1.00 10.81  ? 217 ILE A CG1 1 
ATOM   1794  C  CG2 . ILE A  1 217 ? 24.359  -12.788 21.050  1.00 12.66  ? 217 ILE A CG2 1 
ATOM   1795  C  CD1 . ILE A  1 217 ? 22.067  -11.047 22.133  1.00 11.50  ? 217 ILE A CD1 1 
ATOM   1796  N  N   . SER A  1 218 ? 22.605  -15.400 24.313  1.00 11.68  ? 218 SER A N   1 
ATOM   1797  C  CA  . SER A  1 218 ? 21.680  -15.972 25.302  1.00 12.90  ? 218 SER A CA  1 
ATOM   1798  C  C   . SER A  1 218 ? 20.544  -15.023 25.630  1.00 12.37  ? 218 SER A C   1 
ATOM   1799  O  O   . SER A  1 218 ? 20.585  -13.795 25.427  1.00 11.71  ? 218 SER A O   1 
ATOM   1800  C  CB  . SER A  1 218 ? 22.393  -16.392 26.584  1.00 14.88  ? 218 SER A CB  1 
ATOM   1801  O  OG  . SER A  1 218 ? 22.853  -15.215 27.229  1.00 14.60  ? 218 SER A OG  1 
ATOM   1802  N  N   A GLN A  1 219 ? 19.551  -15.600 26.287  0.50 14.73  ? 219 GLN A N   1 
ATOM   1803  N  N   B GLN A  1 219 ? 19.535  -15.594 26.297  0.50 14.70  ? 219 GLN A N   1 
ATOM   1804  C  CA  A GLN A  1 219 ? 18.478  -14.810 26.790  0.50 13.65  ? 219 GLN A CA  1 
ATOM   1805  C  CA  B GLN A  1 219 ? 18.456  -14.823 26.896  0.50 14.41  ? 219 GLN A CA  1 
ATOM   1806  C  C   A GLN A  1 219 ? 18.970  -13.714 27.779  0.50 13.95  ? 219 GLN A C   1 
ATOM   1807  C  C   B GLN A  1 219 ? 18.991  -13.703 27.785  0.50 13.95  ? 219 GLN A C   1 
ATOM   1808  O  O   A GLN A  1 219 ? 18.493  -12.579 27.688  0.50 12.80  ? 219 GLN A O   1 
ATOM   1809  O  O   B GLN A  1 219 ? 18.525  -12.584 27.716  0.50 12.81  ? 219 GLN A O   1 
ATOM   1810  C  CB  A GLN A  1 219 ? 17.406  -15.758 27.372  0.50 17.79  ? 219 GLN A CB  1 
ATOM   1811  C  CB  B GLN A  1 219 ? 17.601  -15.727 27.823  0.50 19.32  ? 219 GLN A CB  1 
ATOM   1812  C  CG  A GLN A  1 219 ? 17.712  -16.488 28.667  0.50 24.40  ? 219 GLN A CG  1 
ATOM   1813  C  CG  B GLN A  1 219 ? 16.539  -14.877 28.534  0.50 25.32  ? 219 GLN A CG  1 
ATOM   1814  C  CD  A GLN A  1 219 ? 16.654  -17.540 29.051  0.50 27.77  ? 219 GLN A CD  1 
ATOM   1815  C  CD  B GLN A  1 219 ? 16.493  -14.851 30.078  0.50 30.69  ? 219 GLN A CD  1 
ATOM   1816  O  OE1 A GLN A  1 219 ? 15.592  -17.626 28.416  0.50 37.21  ? 219 GLN A OE1 1 
ATOM   1817  O  OE1 B GLN A  1 219 ? 16.002  -15.828 30.641  0.50 44.15  ? 219 GLN A OE1 1 
ATOM   1818  N  NE2 A GLN A  1 219 ? 16.942  -18.343 30.098  0.50 38.24  ? 219 GLN A NE2 1 
ATOM   1819  N  NE2 B GLN A  1 219 ? 16.767  -13.680 30.751  0.50 19.10  ? 219 GLN A NE2 1 
ATOM   1820  N  N   . GLU A  1 220 ? 19.956  -14.017 28.630  1.00 13.33  ? 220 GLU A N   1 
ATOM   1821  C  CA  . GLU A  1 220 ? 20.513  -13.004 29.519  1.00 14.26  ? 220 GLU A CA  1 
ATOM   1822  C  C   . GLU A  1 220 ? 21.302  -11.974 28.780  1.00 13.01  ? 220 GLU A C   1 
ATOM   1823  O  O   . GLU A  1 220 ? 21.238  -10.801 29.152  1.00 13.14  ? 220 GLU A O   1 
ATOM   1824  C  CB  . GLU A  1 220 ? 21.365  -13.684 30.561  1.00 19.38  ? 220 GLU A CB  1 
ATOM   1825  C  CG  . GLU A  1 220 ? 20.532  -14.637 31.423  1.00 20.44  ? 220 GLU A CG  1 
ATOM   1826  C  CD  . GLU A  1 220 ? 20.297  -16.017 30.846  1.00 28.06  ? 220 GLU A CD  1 
ATOM   1827  O  OE1 . GLU A  1 220 ? 20.898  -16.367 29.809  1.00 21.62  ? 220 GLU A OE1 1 
ATOM   1828  O  OE2 . GLU A  1 220 ? 19.498  -16.772 31.451  1.00 29.84  ? 220 GLU A OE2 1 
ATOM   1829  N  N   . GLN A  1 221 ? 22.041  -12.372 27.726  1.00 12.16  ? 221 GLN A N   1 
ATOM   1830  C  CA  . GLN A  1 221 ? 22.767  -11.358 26.949  1.00 11.56  ? 221 GLN A CA  1 
ATOM   1831  C  C   . GLN A  1 221 ? 21.806  -10.424 26.267  1.00 11.70  ? 221 GLN A C   1 
ATOM   1832  O  O   . GLN A  1 221 ? 22.056  -9.196  26.229  1.00 11.58  ? 221 GLN A O   1 
ATOM   1833  C  CB  . GLN A  1 221 ? 23.640  -12.019 25.903  1.00 11.80  ? 221 GLN A CB  1 
ATOM   1834  C  CG  . GLN A  1 221 ? 24.829  -12.766 26.522  1.00 13.95  ? 221 GLN A CG  1 
ATOM   1835  C  CD  . GLN A  1 221 ? 25.699  -13.403 25.461  1.00 12.82  ? 221 GLN A CD  1 
ATOM   1836  O  OE1 . GLN A  1 221 ? 25.257  -14.313 24.759  1.00 12.78  ? 221 GLN A OE1 1 
ATOM   1837  N  NE2 . GLN A  1 221 ? 26.937  -12.920 25.311  1.00 14.16  ? 221 GLN A NE2 1 
ATOM   1838  N  N   . LEU A  1 222 ? 20.742  -10.944 25.662  1.00 11.16  ? 222 LEU A N   1 
ATOM   1839  C  CA  . LEU A  1 222 ? 19.795  -10.083 24.975  1.00 11.41  ? 222 LEU A CA  1 
ATOM   1840  C  C   . LEU A  1 222 ? 19.132  -9.154  25.924  1.00 10.77  ? 222 LEU A C   1 
ATOM   1841  O  O   . LEU A  1 222 ? 18.945  -7.957  25.679  1.00 11.04  ? 222 LEU A O   1 
ATOM   1842  C  CB  . LEU A  1 222 ? 18.789  -10.959 24.241  1.00 10.88  ? 222 LEU A CB  1 
ATOM   1843  C  CG  . LEU A  1 222 ? 17.684  -10.172 23.550  1.00 10.68  ? 222 LEU A CG  1 
ATOM   1844  C  CD1 . LEU A  1 222 ? 18.228  -9.260  22.431  1.00 11.16  ? 222 LEU A CD1 1 
ATOM   1845  C  CD2 . LEU A  1 222 ? 16.667  -11.116 22.933  1.00 13.20  ? 222 LEU A CD2 1 
ATOM   1846  N  N   . LEU A  1 223 ? 18.759  -9.676  27.091  1.00 11.65  ? 223 LEU A N   1 
ATOM   1847  C  CA  . LEU A  1 223 ? 18.144  -8.810  28.134  1.00 11.70  ? 223 LEU A CA  1 
ATOM   1848  C  C   . LEU A  1 223 ? 19.118  -7.732  28.602  1.00 11.79  ? 223 LEU A C   1 
ATOM   1849  O  O   . LEU A  1 223 ? 18.709  -6.638  28.809  1.00 12.44  ? 223 LEU A O   1 
ATOM   1850  C  CB  . LEU A  1 223 ? 17.704  -9.664  29.290  1.00 13.01  ? 223 LEU A CB  1 
ATOM   1851  C  CG  . LEU A  1 223 ? 16.966  -8.924  30.389  1.00 14.97  ? 223 LEU A CG  1 
ATOM   1852  C  CD1 . LEU A  1 223 ? 15.616  -8.406  29.903  1.00 16.17  ? 223 LEU A CD1 1 
ATOM   1853  C  CD2 . LEU A  1 223 ? 16.677  -9.959  31.501  1.00 18.67  ? 223 LEU A CD2 1 
ATOM   1854  N  N   . ALA A  1 224 ? 20.397  -8.060  28.745  1.00 12.54  ? 224 ALA A N   1 
ATOM   1855  C  CA  . ALA A  1 224 ? 21.403  -7.061  29.114  1.00 13.80  ? 224 ALA A CA  1 
ATOM   1856  C  C   . ALA A  1 224 ? 21.446  -5.969  28.098  1.00 13.19  ? 224 ALA A C   1 
ATOM   1857  O  O   . ALA A  1 224 ? 21.429  -4.772  28.419  1.00 14.41  ? 224 ALA A O   1 
ATOM   1858  C  CB  . ALA A  1 224 ? 22.770  -7.692  29.287  1.00 15.06  ? 224 ALA A CB  1 
ATOM   1859  N  N   . LEU A  1 225 ? 21.486  -6.332  26.838  1.00 12.34  ? 225 LEU A N   1 
ATOM   1860  C  CA  . LEU A  1 225 ? 21.572  -5.322  25.771  1.00 12.12  ? 225 LEU A CA  1 
ATOM   1861  C  C   . LEU A  1 225 ? 20.362  -4.398  25.843  1.00 12.22  ? 225 LEU A C   1 
ATOM   1862  O  O   . LEU A  1 225 ? 20.465  -3.182  25.667  1.00 13.83  ? 225 LEU A O   1 
ATOM   1863  C  CB  . LEU A  1 225 ? 21.674  -6.009  24.411  1.00 11.31  ? 225 LEU A CB  1 
ATOM   1864  C  CG  . LEU A  1 225 ? 21.765  -5.059  23.235  1.00 11.92  ? 225 LEU A CG  1 
ATOM   1865  C  CD1 . LEU A  1 225 ? 23.014  -4.168  23.310  1.00 14.39  ? 225 LEU A CD1 1 
ATOM   1866  C  CD2 . LEU A  1 225 ? 21.701  -5.910  21.977  1.00 12.90  ? 225 LEU A CD2 1 
ATOM   1867  N  N   . GLU A  1 226 ? 19.183  -5.001  26.060  1.00 10.70  ? 226 GLU A N   1 
ATOM   1868  C  CA  . GLU A  1 226 ? 17.957  -4.248  26.078  1.00 11.55  ? 226 GLU A CA  1 
ATOM   1869  C  C   . GLU A  1 226 ? 17.724  -3.381  27.285  1.00 12.51  ? 226 GLU A C   1 
ATOM   1870  O  O   . GLU A  1 226 ? 16.890  -2.491  27.250  1.00 14.56  ? 226 GLU A O   1 
ATOM   1871  C  CB  . GLU A  1 226 ? 16.756  -5.203  26.030  1.00 10.75  ? 226 GLU A CB  1 
ATOM   1872  C  CG  . GLU A  1 226 ? 16.640  -5.975  24.676  1.00 11.50  ? 226 GLU A CG  1 
ATOM   1873  C  CD  . GLU A  1 226 ? 15.721  -7.179  24.753  1.00 10.94  ? 226 GLU A CD  1 
ATOM   1874  O  OE1 . GLU A  1 226 ? 15.451  -7.659  25.874  1.00 12.29  ? 226 GLU A OE1 1 
ATOM   1875  O  OE2 . GLU A  1 226 ? 15.271  -7.646  23.687  1.00 11.86  ? 226 GLU A OE2 1 
ATOM   1876  N  N   . THR A  1 227 ? 18.427  -3.652  28.385  1.00 12.29  ? 227 THR A N   1 
ATOM   1877  C  CA  . THR A  1 227 ? 18.154  -2.970  29.667  1.00 13.50  ? 227 THR A CA  1 
ATOM   1878  C  C   . THR A  1 227 ? 19.360  -2.215  30.176  1.00 14.21  ? 227 THR A C   1 
ATOM   1879  O  O   . THR A  1 227 ? 19.240  -1.551  31.191  1.00 18.82  ? 227 THR A O   1 
ATOM   1880  C  CB  . THR A  1 227 ? 17.686  -4.023  30.739  1.00 14.31  ? 227 THR A CB  1 
ATOM   1881  O  OG1 . THR A  1 227 ? 18.699  -4.970  30.957  1.00 14.93  ? 227 THR A OG1 1 
ATOM   1882  C  CG2 . THR A  1 227 ? 16.462  -4.709  30.316  1.00 17.31  ? 227 THR A CG2 1 
ATOM   1883  N  N   . ALA A  1 228 ? 20.527  -2.318  29.566  1.00 14.06  ? 228 ALA A N   1 
ATOM   1884  C  CA  . ALA A  1 228 ? 21.737  -1.727  30.180  1.00 14.89  ? 228 ALA A CA  1 
ATOM   1885  C  C   . ALA A  1 228 ? 21.842  -0.254  29.949  1.00 14.47  ? 228 ALA A C   1 
ATOM   1886  O  O   . ALA A  1 228 ? 22.504  0.372   30.737  1.00 16.12  ? 228 ALA A O   1 
ATOM   1887  C  CB  . ALA A  1 228 ? 23.008  -2.420  29.625  1.00 18.25  ? 228 ALA A CB  1 
ATOM   1888  N  N   . LEU A  1 229 ? 21.248  0.318   28.859  1.00 12.93  ? 229 LEU A N   1 
ATOM   1889  C  CA  . LEU A  1 229 ? 21.590  1.656   28.416  1.00 13.77  ? 229 LEU A CA  1 
ATOM   1890  C  C   . LEU A  1 229 ? 20.431  2.577   28.453  1.00 13.45  ? 229 LEU A C   1 
ATOM   1891  O  O   . LEU A  1 229 ? 19.279  2.196   28.272  1.00 13.49  ? 229 LEU A O   1 
ATOM   1892  C  CB  . LEU A  1 229 ? 22.132  1.601   26.953  1.00 14.34  ? 229 LEU A CB  1 
ATOM   1893  C  CG  . LEU A  1 229 ? 23.260  0.527   26.731  1.00 14.20  ? 229 LEU A CG  1 
ATOM   1894  C  CD1 . LEU A  1 229 ? 23.595  0.520   25.255  1.00 18.28  ? 229 LEU A CD1 1 
ATOM   1895  C  CD2 . LEU A  1 229 ? 24.446  0.742   27.656  1.00 17.95  ? 229 LEU A CD2 1 
ATOM   1896  N  N   . TYR A  1 230 ? 20.786  3.849   28.599  1.00 14.82  ? 230 TYR A N   1 
ATOM   1897  C  CA  . TYR A  1 230 ? 19.846  4.960   28.525  1.00 14.66  ? 230 TYR A CA  1 
ATOM   1898  C  C   . TYR A  1 230 ? 20.238  5.884   27.394  1.00 14.95  ? 230 TYR A C   1 
ATOM   1899  O  O   . TYR A  1 230 ? 21.415  6.040   27.075  1.00 15.84  ? 230 TYR A O   1 
ATOM   1900  C  CB  . TYR A  1 230 ? 19.858  5.761   29.824  1.00 15.41  ? 230 TYR A CB  1 
ATOM   1901  C  CG  . TYR A  1 230 ? 19.241  5.041   30.970  1.00 17.86  ? 230 TYR A CG  1 
ATOM   1902  C  CD1 . TYR A  1 230 ? 19.946  4.039   31.597  1.00 23.96  ? 230 TYR A CD1 1 
ATOM   1903  C  CD2 . TYR A  1 230 ? 18.046  5.454   31.491  1.00 24.68  ? 230 TYR A CD2 1 
ATOM   1904  C  CE1 . TYR A  1 230 ? 19.419  3.376   32.689  1.00 30.57  ? 230 TYR A CE1 1 
ATOM   1905  C  CE2 . TYR A  1 230 ? 17.460  4.831   32.601  1.00 27.50  ? 230 TYR A CE2 1 
ATOM   1906  C  CZ  . TYR A  1 230 ? 18.142  3.774   33.205  1.00 33.08  ? 230 TYR A CZ  1 
ATOM   1907  O  OH  . TYR A  1 230 ? 17.599  3.148   34.332  1.00 42.02  ? 230 TYR A OH  1 
ATOM   1908  N  N   A CYS A  1 231 ? 19.258  6.519   26.756  0.50 15.08  ? 231 CYS A N   1 
ATOM   1909  N  N   B CYS A  1 231 ? 19.256  6.512   26.796  0.50 18.40  ? 231 CYS A N   1 
ATOM   1910  C  CA  A CYS A  1 231 ? 19.505  7.551   25.738  0.50 16.29  ? 231 CYS A CA  1 
ATOM   1911  C  CA  B CYS A  1 231 ? 19.575  7.416   25.740  0.50 19.64  ? 231 CYS A CA  1 
ATOM   1912  C  C   A CYS A  1 231 ? 20.001  8.840   26.317  0.50 15.22  ? 231 CYS A C   1 
ATOM   1913  C  C   B CYS A  1 231 ? 19.721  8.864   26.245  0.50 17.34  ? 231 CYS A C   1 
ATOM   1914  O  O   A CYS A  1 231 ? 20.627  9.681   25.625  0.50 15.68  ? 231 CYS A O   1 
ATOM   1915  O  O   B CYS A  1 231 ? 19.988  9.801   25.458  0.50 19.30  ? 231 CYS A O   1 
ATOM   1916  C  CB  A CYS A  1 231 ? 18.208  7.896   24.971  0.50 14.45  ? 231 CYS A CB  1 
ATOM   1917  C  CB  B CYS A  1 231 ? 18.532  7.264   24.624  0.50 23.91  ? 231 CYS A CB  1 
ATOM   1918  S  SG  A CYS A  1 231 ? 17.548  6.550   24.008  0.50 15.76  ? 231 CYS A SG  1 
ATOM   1919  S  SG  B CYS A  1 231 ? 16.879  7.452   25.175  0.50 27.50  ? 231 CYS A SG  1 
ATOM   1920  N  N   . THR A  1 232 ? 19.607  9.045   27.571  1.00 17.06  ? 232 THR A N   1 
ATOM   1921  C  CA  . THR A  1 232 ? 19.768  10.334  28.231  1.00 17.69  ? 232 THR A CA  1 
ATOM   1922  C  C   . THR A  1 232 ? 21.079  10.406  29.010  1.00 16.72  ? 232 THR A C   1 
ATOM   1923  O  O   . THR A  1 232 ? 21.692  9.400   29.359  1.00 17.89  ? 232 THR A O   1 
ATOM   1924  C  CB  . THR A  1 232 ? 18.587  10.538  29.220  1.00 17.70  ? 232 THR A CB  1 
ATOM   1925  O  OG1 . THR A  1 232 ? 18.259  9.315   29.896  1.00 19.63  ? 232 THR A OG1 1 
ATOM   1926  C  CG2 . THR A  1 232 ? 17.359  11.026  28.527  1.00 21.35  ? 232 THR A CG2 1 
ATOM   1927  N  N   . HIS A  1 233 ? 21.556  11.652  29.215  1.00 18.15  ? 233 HIS A N   1 
ATOM   1928  C  CA  . HIS A  1 233 ? 22.688  11.923  30.093  1.00 18.70  ? 233 HIS A CA  1 
ATOM   1929  C  C   . HIS A  1 233 ? 22.366  11.507  31.521  1.00 17.95  ? 233 HIS A C   1 
ATOM   1930  O  O   . HIS A  1 233 ? 21.201  11.518  31.978  1.00 17.84  ? 233 HIS A O   1 
ATOM   1931  C  CB  . HIS A  1 233 ? 23.078  13.413  30.055  1.00 23.20  ? 233 HIS A CB  1 
ATOM   1932  C  CG  . HIS A  1 233 ? 23.680  13.824  28.719  1.00 29.70  ? 233 HIS A CG  1 
ATOM   1933  N  ND1 . HIS A  1 233 ? 22.996  14.577  27.803  1.00 37.73  ? 233 HIS A ND1 1 
ATOM   1934  C  CD2 . HIS A  1 233 ? 24.915  13.532  28.138  1.00 35.61  ? 233 HIS A CD2 1 
ATOM   1935  C  CE1 . HIS A  1 233 ? 23.762  14.774  26.704  1.00 47.61  ? 233 HIS A CE1 1 
ATOM   1936  N  NE2 . HIS A  1 233 ? 24.936  14.139  26.897  1.00 39.00  ? 233 HIS A NE2 1 
ATOM   1937  N  N   . MET A  1 234 ? 23.400  11.175  32.263  1.00 19.70  ? 234 MET A N   1 
ATOM   1938  C  CA  . MET A  1 234 ? 23.231  10.658  33.620  1.00 19.92  ? 234 MET A CA  1 
ATOM   1939  C  C   . MET A  1 234 ? 22.392  11.568  34.514  1.00 19.09  ? 234 MET A C   1 
ATOM   1940  O  O   . MET A  1 234 ? 21.646  11.074  35.373  1.00 22.99  ? 234 MET A O   1 
ATOM   1941  C  CB  . MET A  1 234 ? 24.600  10.500  34.265  1.00 21.10  ? 234 MET A CB  1 
ATOM   1942  C  CG  . MET A  1 234 ? 24.612  9.851   35.608  1.00 23.80  ? 234 MET A CG  1 
ATOM   1943  S  SD  . MET A  1 234 ? 26.352  9.539   36.053  1.00 34.24  ? 234 MET A SD  1 
ATOM   1944  C  CE  . MET A  1 234 ? 27.102  11.177  36.037  1.00 50.11  ? 234 MET A CE  1 
ATOM   1945  N  N   A ASP A  1 235 ? 22.595  12.872  34.326  0.50 20.21  ? 235 ASP A N   1 
ATOM   1946  N  N   B ASP A  1 235 ? 22.576  12.870  34.390  0.50 22.13  ? 235 ASP A N   1 
ATOM   1947  C  CA  A ASP A  1 235 ? 21.976  13.882  35.213  0.50 23.74  ? 235 ASP A CA  1 
ATOM   1948  C  CA  B ASP A  1 235 ? 21.899  13.767  35.322  0.50 25.07  ? 235 ASP A CA  1 
ATOM   1949  C  C   A ASP A  1 235 ? 20.593  14.335  34.791  0.50 22.25  ? 235 ASP A C   1 
ATOM   1950  C  C   B ASP A  1 235 ? 20.664  14.410  34.709  0.50 28.74  ? 235 ASP A C   1 
ATOM   1951  O  O   A ASP A  1 235 ? 19.977  15.165  35.454  0.50 22.54  ? 235 ASP A O   1 
ATOM   1952  O  O   B ASP A  1 235 ? 20.235  15.474  35.136  0.50 29.91  ? 235 ASP A O   1 
ATOM   1953  C  CB  A ASP A  1 235 ? 22.925  15.070  35.554  0.50 27.90  ? 235 ASP A CB  1 
ATOM   1954  C  CB  B ASP A  1 235 ? 22.884  14.799  35.884  0.50 35.05  ? 235 ASP A CB  1 
ATOM   1955  C  CG  A ASP A  1 235 ? 23.211  15.988  34.386  0.50 34.07  ? 235 ASP A CG  1 
ATOM   1956  C  CG  B ASP A  1 235 ? 24.143  14.146  36.503  0.50 29.92  ? 235 ASP A CG  1 
ATOM   1957  O  OD1 A ASP A  1 235 ? 22.677  15.774  33.289  0.50 33.85  ? 235 ASP A OD1 1 
ATOM   1958  O  OD1 B ASP A  1 235 ? 24.021  13.233  37.375  0.50 33.55  ? 235 ASP A OD1 1 
ATOM   1959  O  OD2 A ASP A  1 235 ? 23.988  16.955  34.581  0.50 38.72  ? 235 ASP A OD2 1 
ATOM   1960  O  OD2 B ASP A  1 235 ? 25.252  14.549  36.104  0.50 36.14  ? 235 ASP A OD2 1 
ATOM   1961  N  N   . ASP A  1 236 ? 20.067  13.747  33.728  1.00 23.74  ? 236 ASP A N   1 
ATOM   1962  C  CA  . ASP A  1 236 ? 18.769  14.146  33.147  1.00 23.38  ? 236 ASP A CA  1 
ATOM   1963  C  C   . ASP A  1 236 ? 17.691  13.820  34.164  1.00 23.27  ? 236 ASP A C   1 
ATOM   1964  O  O   . ASP A  1 236 ? 17.551  12.666  34.505  1.00 23.01  ? 236 ASP A O   1 
ATOM   1965  C  CB  . ASP A  1 236 ? 18.496  13.374  31.852  1.00 20.66  ? 236 ASP A CB  1 
ATOM   1966  C  CG  . ASP A  1 236 ? 17.374  14.007  31.029  1.00 25.43  ? 236 ASP A CG  1 
ATOM   1967  O  OD1 . ASP A  1 236 ? 16.318  14.358  31.611  1.00 28.05  ? 236 ASP A OD1 1 
ATOM   1968  O  OD2 . ASP A  1 236 ? 17.568  14.164  29.809  1.00 26.79  ? 236 ASP A OD2 1 
ATOM   1969  N  N   . PRO A  1 237 ? 16.873  14.802  34.601  1.00 26.34  ? 237 PRO A N   1 
ATOM   1970  C  CA  . PRO A  1 237 ? 15.824  14.399  35.531  1.00 27.68  ? 237 PRO A CA  1 
ATOM   1971  C  C   . PRO A  1 237 ? 14.657  13.552  34.958  1.00 34.20  ? 237 PRO A C   1 
ATOM   1972  O  O   . PRO A  1 237 ? 13.793  13.086  35.734  1.00 30.27  ? 237 PRO A O   1 
ATOM   1973  C  CB  . PRO A  1 237 ? 15.258  15.747  35.996  1.00 29.29  ? 237 PRO A CB  1 
ATOM   1974  C  CG  . PRO A  1 237 ? 15.502  16.673  34.864  1.00 36.79  ? 237 PRO A CG  1 
ATOM   1975  C  CD  . PRO A  1 237 ? 16.824  16.243  34.276  1.00 29.44  ? 237 PRO A CD  1 
ATOM   1976  N  N   . SER A  1 238 ? 14.652  13.351  33.635  1.00 26.02  ? 238 SER A N   1 
ATOM   1977  C  CA  . SER A  1 238 ? 13.673  12.509  32.957  1.00 29.78  ? 238 SER A CA  1 
ATOM   1978  C  C   . SER A  1 238 ? 14.372  11.410  32.099  1.00 23.19  ? 238 SER A C   1 
ATOM   1979  O  O   . SER A  1 238 ? 14.382  11.466  30.855  1.00 26.21  ? 238 SER A O   1 
ATOM   1980  C  CB  . SER A  1 238 ? 12.716  13.319  32.107  1.00 29.18  ? 238 SER A CB  1 
ATOM   1981  O  OG  . SER A  1 238 ? 11.986  14.188  32.951  1.00 46.81  ? 238 SER A OG  1 
ATOM   1982  N  N   . PRO A  1 239 ? 14.899  10.373  32.759  1.00 24.41  ? 239 PRO A N   1 
ATOM   1983  C  CA  . PRO A  1 239 ? 15.668  9.358   32.067  1.00 20.75  ? 239 PRO A CA  1 
ATOM   1984  C  C   . PRO A  1 239 ? 14.838  8.619   31.029  1.00 24.93  ? 239 PRO A C   1 
ATOM   1985  O  O   . PRO A  1 239 ? 13.625  8.418   31.282  1.00 27.14  ? 239 PRO A O   1 
ATOM   1986  C  CB  . PRO A  1 239 ? 16.136  8.427   33.171  1.00 24.17  ? 239 PRO A CB  1 
ATOM   1987  C  CG  . PRO A  1 239 ? 15.319  8.712   34.365  1.00 30.10  ? 239 PRO A CG  1 
ATOM   1988  C  CD  . PRO A  1 239 ? 14.872  10.157  34.217  1.00 24.43  ? 239 PRO A CD  1 
ATOM   1989  N  N   . ARG A  1 240 ? 15.471  8.196   29.921  1.00 20.42  ? 240 ARG A N   1 
ATOM   1990  C  CA  . ARG A  1 240 ? 14.775  7.415   28.916  1.00 22.74  ? 240 ARG A CA  1 
ATOM   1991  C  C   . ARG A  1 240 ? 15.663  6.196   28.622  1.00 20.28  ? 240 ARG A C   1 
ATOM   1992  O  O   . ARG A  1 240 ? 16.834  6.374   28.233  1.00 18.87  ? 240 ARG A O   1 
ATOM   1993  C  CB  . ARG A  1 240 ? 14.548  8.165   27.559  1.00 31.07  ? 240 ARG A CB  1 
ATOM   1994  C  CG  . ARG A  1 240 ? 13.732  9.450   27.502  1.00 38.74  ? 240 ARG A CG  1 
ATOM   1995  C  CD  . ARG A  1 240 ? 13.716  10.068  26.084  1.00 56.16  ? 240 ARG A CD  1 
ATOM   1996  N  NE  . ARG A  1 240 ? 14.734  11.113  25.790  1.00 44.04  ? 240 ARG A NE  1 
ATOM   1997  C  CZ  . ARG A  1 240 ? 15.709  11.050  24.870  1.00 40.15  ? 240 ARG A CZ  1 
ATOM   1998  N  NH1 . ARG A  1 240 ? 15.875  9.962   24.121  1.00 32.97  ? 240 ARG A NH1 1 
ATOM   1999  N  NH2 . ARG A  1 240 ? 16.553  12.079  24.684  1.00 49.95  ? 240 ARG A NH2 1 
ATOM   2000  N  N   . GLU A  1 241 ? 15.125  4.989   28.791  1.00 20.39  ? 241 GLU A N   1 
ATOM   2001  C  CA  . GLU A  1 241 ? 15.808  3.764   28.445  1.00 19.45  ? 241 GLU A CA  1 
ATOM   2002  C  C   . GLU A  1 241 ? 16.070  3.700   26.935  1.00 16.32  ? 241 GLU A C   1 
ATOM   2003  O  O   . GLU A  1 241 ? 15.201  4.073   26.145  1.00 20.35  ? 241 GLU A O   1 
ATOM   2004  C  CB  . GLU A  1 241 ? 14.921  2.563   28.737  1.00 25.73  ? 241 GLU A CB  1 
ATOM   2005  C  CG  . GLU A  1 241 ? 14.679  2.264   30.198  1.00 31.68  ? 241 GLU A CG  1 
ATOM   2006  C  CD  . GLU A  1 241 ? 13.618  1.145   30.398  1.00 41.38  ? 241 GLU A CD  1 
ATOM   2007  O  OE1 . GLU A  1 241 ? 13.102  0.531   29.408  1.00 48.47  ? 241 GLU A OE1 1 
ATOM   2008  O  OE2 . GLU A  1 241 ? 13.306  0.891   31.575  1.00 40.27  ? 241 GLU A OE2 1 
ATOM   2009  N  N   . MET A  1 242 ? 17.211  3.163   26.547  1.00 14.11  ? 242 MET A N   1 
ATOM   2010  C  CA  . MET A  1 242 ? 17.543  2.978   25.125  1.00 12.91  ? 242 MET A CA  1 
ATOM   2011  C  C   . MET A  1 242 ? 17.027  1.631   24.706  1.00 11.47  ? 242 MET A C   1 
ATOM   2012  O  O   . MET A  1 242 ? 17.633  0.575   24.933  1.00 12.17  ? 242 MET A O   1 
ATOM   2013  C  CB  . MET A  1 242 ? 19.055  3.070   24.911  1.00 13.06  ? 242 MET A CB  1 
ATOM   2014  C  CG  . MET A  1 242 ? 19.453  3.001   23.463  1.00 12.94  ? 242 MET A CG  1 
ATOM   2015  S  SD  . MET A  1 242 ? 21.201  2.995   23.196  1.00 13.94  ? 242 MET A SD  1 
ATOM   2016  C  CE  . MET A  1 242 ? 21.601  4.686   23.655  1.00 15.98  ? 242 MET A CE  1 
ATOM   2017  N  N   . ILE A  1 243 ? 15.850  1.685   24.091  1.00 11.24  ? 243 ILE A N   1 
ATOM   2018  C  CA  . ILE A  1 243 ? 15.110  0.533   23.588  1.00 10.52  ? 243 ILE A CA  1 
ATOM   2019  C  C   . ILE A  1 243 ? 14.524  0.879   22.234  1.00 10.21  ? 243 ILE A C   1 
ATOM   2020  O  O   . ILE A  1 243 ? 14.339  2.070   21.897  1.00 10.32  ? 243 ILE A O   1 
ATOM   2021  C  CB  . ILE A  1 243 ? 13.939  0.113   24.533  1.00 12.34  ? 243 ILE A CB  1 
ATOM   2022  C  CG1 . ILE A  1 243 ? 13.019  1.276   24.865  1.00 15.72  ? 243 ILE A CG1 1 
ATOM   2023  C  CG2 . ILE A  1 243 ? 14.517  -0.486  25.801  1.00 15.62  ? 243 ILE A CG2 1 
ATOM   2024  C  CD1 . ILE A  1 243 ? 11.775  0.831   25.665  1.00 16.65  ? 243 ILE A CD1 1 
ATOM   2025  N  N   . ASN A  1 244 ? 14.172  -0.137  21.466  1.00 9.17   ? 244 ASN A N   1 
ATOM   2026  C  CA  . ASN A  1 244 ? 13.450  0.031   20.221  1.00 8.99   ? 244 ASN A CA  1 
ATOM   2027  C  C   . ASN A  1 244 ? 14.154  1.000   19.286  1.00 9.46   ? 244 ASN A C   1 
ATOM   2028  O  O   . ASN A  1 244 ? 13.542  1.850   18.618  1.00 9.80   ? 244 ASN A O   1 
ATOM   2029  C  CB  . ASN A  1 244 ? 11.989  0.436   20.453  1.00 10.76  ? 244 ASN A CB  1 
ATOM   2030  C  CG  . ASN A  1 244 ? 11.288  -0.556  21.381  1.00 10.78  ? 244 ASN A CG  1 
ATOM   2031  O  OD1 . ASN A  1 244 ? 11.504  -1.728  21.323  1.00 12.59  ? 244 ASN A OD1 1 
ATOM   2032  N  ND2 . ASN A  1 244 ? 10.451  -0.008  22.278  1.00 14.02  ? 244 ASN A ND2 1 
ATOM   2033  N  N   . ASN A  1 245 ? 15.501  0.856   19.224  1.00 8.64   ? 245 ASN A N   1 
ATOM   2034  C  CA  . ASN A  1 245 ? 16.336  1.768   18.471  1.00 9.14   ? 245 ASN A CA  1 
ATOM   2035  C  C   . ASN A  1 245 ? 16.567  1.230   17.048  1.00 8.17   ? 245 ASN A C   1 
ATOM   2036  O  O   . ASN A  1 245 ? 17.719  1.086   16.633  1.00 9.09   ? 245 ASN A O   1 
ATOM   2037  C  CB  . ASN A  1 245 ? 17.609  2.159   19.189  1.00 9.47   ? 245 ASN A CB  1 
ATOM   2038  C  CG  . ASN A  1 245 ? 18.487  0.964   19.492  1.00 8.67   ? 245 ASN A CG  1 
ATOM   2039  O  OD1 . ASN A  1 245 ? 18.027  -0.186  19.491  1.00 9.77   ? 245 ASN A OD1 1 
ATOM   2040  N  ND2 . ASN A  1 245 ? 19.744  1.211   19.764  1.00 11.55  ? 245 ASN A ND2 1 
ATOM   2041  N  N   . PHE A  1 246 ? 15.480  0.959   16.357  1.00 8.34   ? 246 PHE A N   1 
ATOM   2042  C  CA  . PHE A  1 246 ? 15.506  0.431   14.970  1.00 8.92   ? 246 PHE A CA  1 
ATOM   2043  C  C   . PHE A  1 246 ? 14.545  1.275   14.176  1.00 7.90   ? 246 PHE A C   1 
ATOM   2044  O  O   . PHE A  1 246 ? 13.524  1.715   14.708  1.00 8.80   ? 246 PHE A O   1 
ATOM   2045  C  CB  . PHE A  1 246 ? 15.215  -1.088  14.924  1.00 9.20   ? 246 PHE A CB  1 
ATOM   2046  C  CG  . PHE A  1 246 ? 13.818  -1.436  15.426  1.00 8.71   ? 246 PHE A CG  1 
ATOM   2047  C  CD1 . PHE A  1 246 ? 13.592  -1.642  16.771  1.00 8.91   ? 246 PHE A CD1 1 
ATOM   2048  C  CD2 . PHE A  1 246 ? 12.730  -1.522  14.570  1.00 10.26  ? 246 PHE A CD2 1 
ATOM   2049  C  CE1 . PHE A  1 246 ? 12.286  -1.952  17.264  1.00 9.79   ? 246 PHE A CE1 1 
ATOM   2050  C  CE2 . PHE A  1 246 ? 11.466  -1.825  15.047  1.00 11.42  ? 246 PHE A CE2 1 
ATOM   2051  C  CZ  . PHE A  1 246 ? 11.268  -2.081  16.398  1.00 11.38  ? 246 PHE A CZ  1 
ATOM   2052  N  N   . ARG A  1 247 ? 14.821  1.403   12.879  1.00 7.78   ? 247 ARG A N   1 
ATOM   2053  C  CA  . ARG A  1 247 ? 13.905  2.092   11.956  1.00 7.79   ? 247 ARG A CA  1 
ATOM   2054  C  C   . ARG A  1 247 ? 12.926  1.054   11.406  1.00 7.60   ? 247 ARG A C   1 
ATOM   2055  O  O   . ARG A  1 247 ? 13.312  -0.093  11.155  1.00 8.17   ? 247 ARG A O   1 
ATOM   2056  C  CB  . ARG A  1 247 ? 14.673  2.737   10.850  1.00 8.05   ? 247 ARG A CB  1 
ATOM   2057  C  CG  . ARG A  1 247 ? 13.880  3.733   10.030  1.00 8.36   ? 247 ARG A CG  1 
ATOM   2058  C  CD  . ARG A  1 247 ? 14.722  4.214   8.844   1.00 8.18   ? 247 ARG A CD  1 
ATOM   2059  N  NE  . ARG A  1 247 ? 14.075  5.392   8.227   1.00 8.55   ? 247 ARG A NE  1 
ATOM   2060  C  CZ  . ARG A  1 247 ? 14.554  5.970   7.134   1.00 8.64   ? 247 ARG A CZ  1 
ATOM   2061  N  NH1 . ARG A  1 247 ? 15.568  5.418   6.471   1.00 8.91   ? 247 ARG A NH1 1 
ATOM   2062  N  NH2 . ARG A  1 247 ? 14.009  7.091   6.681   1.00 9.29   ? 247 ARG A NH2 1 
ATOM   2063  N  N   . GLN A  1 248 ? 11.652  1.453   11.180  1.00 7.83   ? 248 GLN A N   1 
ATOM   2064  C  CA  . GLN A  1 248 ? 10.714  0.629   10.455  1.00 7.84   ? 248 GLN A CA  1 
ATOM   2065  C  C   . GLN A  1 248 ? 11.235  0.351   9.049   1.00 7.44   ? 248 GLN A C   1 
ATOM   2066  O  O   . GLN A  1 248 ? 11.927  1.169   8.448   1.00 7.87   ? 248 GLN A O   1 
ATOM   2067  C  CB  . GLN A  1 248 ? 9.350   1.284   10.334  1.00 7.96   ? 248 GLN A CB  1 
ATOM   2068  C  CG  . GLN A  1 248 ? 8.631   1.589   11.658  1.00 8.35   ? 248 GLN A CG  1 
ATOM   2069  C  CD  . GLN A  1 248 ? 8.329   0.356   12.431  1.00 8.81   ? 248 GLN A CD  1 
ATOM   2070  O  OE1 . GLN A  1 248 ? 9.092   -0.122  13.292  1.00 9.89   ? 248 GLN A OE1 1 
ATOM   2071  N  NE2 . GLN A  1 248 ? 7.189   -0.224  12.129  1.00 10.05  ? 248 GLN A NE2 1 
ATOM   2072  N  N   . VAL A  1 249 ? 10.809  -0.773  8.463   1.00 7.45   ? 249 VAL A N   1 
ATOM   2073  C  CA  . VAL A  1 249 ? 11.169  -1.067  7.084   1.00 8.01   ? 249 VAL A CA  1 
ATOM   2074  C  C   . VAL A  1 249 ? 10.527  -0.070  6.140   1.00 7.65   ? 249 VAL A C   1 
ATOM   2075  O  O   . VAL A  1 249 ? 9.410   0.455   6.353   1.00 8.28   ? 249 VAL A O   1 
ATOM   2076  C  CB  . VAL A  1 249 ? 10.824  -2.509  6.680   1.00 9.25   ? 249 VAL A CB  1 
ATOM   2077  C  CG1 . VAL A  1 249 ? 11.667  -3.536  7.458   1.00 10.79  ? 249 VAL A CG1 1 
ATOM   2078  C  CG2 . VAL A  1 249 ? 9.367   -2.805  6.750   1.00 11.35  ? 249 VAL A CG2 1 
ATOM   2079  N  N   . GLN A  1 250 ? 11.255  0.176   5.062   1.00 8.06   ? 250 GLN A N   1 
ATOM   2080  C  CA  . GLN A  1 250 ? 10.891  1.135   4.018   1.00 8.29   ? 250 GLN A CA  1 
ATOM   2081  C  C   . GLN A  1 250 ? 10.264  0.460   2.832   1.00 9.02   ? 250 GLN A C   1 
ATOM   2082  O  O   . GLN A  1 250 ? 10.602  -0.676  2.527   1.00 11.17  ? 250 GLN A O   1 
ATOM   2083  C  CB  . GLN A  1 250 ? 12.180  1.886   3.586   1.00 8.77   ? 250 GLN A CB  1 
ATOM   2084  C  CG  . GLN A  1 250 ? 12.955  2.505   4.736   1.00 8.82   ? 250 GLN A CG  1 
ATOM   2085  C  CD  . GLN A  1 250 ? 12.233  3.596   5.433   1.00 7.94   ? 250 GLN A CD  1 
ATOM   2086  O  OE1 . GLN A  1 250 ? 11.971  4.649   4.824   1.00 9.26   ? 250 GLN A OE1 1 
ATOM   2087  N  NE2 . GLN A  1 250 ? 11.893  3.438   6.685   1.00 8.61   ? 250 GLN A NE2 1 
ATOM   2088  N  N   . LYS A  1 251 ? 9.425   1.194   2.079   1.00 9.99   ? 251 LYS A N   1 
ATOM   2089  C  CA  . LYS A  1 251 ? 8.949   0.650   0.830   1.00 10.75  ? 251 LYS A CA  1 
ATOM   2090  C  C   . LYS A  1 251 ? 10.133  0.350   -0.090  1.00 10.04  ? 251 LYS A C   1 
ATOM   2091  O  O   . LYS A  1 251 ? 11.119  1.101   -0.097  1.00 11.23  ? 251 LYS A O   1 
ATOM   2092  C  CB  . LYS A  1 251 ? 8.038   1.664   0.177   1.00 12.29  ? 251 LYS A CB  1 
ATOM   2093  C  CG  . LYS A  1 251 ? 6.673   1.553   0.870   1.00 14.44  ? 251 LYS A CG  1 
ATOM   2094  C  CD  . LYS A  1 251 ? 5.675   2.411   0.236   1.00 14.85  ? 251 LYS A CD  1 
ATOM   2095  C  CE  . LYS A  1 251 ? 4.211   2.154   0.590   1.00 9.16   ? 251 LYS A CE  1 
ATOM   2096  N  NZ  . LYS A  1 251 ? 3.978   2.164   2.094   1.00 8.55   ? 251 LYS A NZ  1 
ATOM   2097  N  N   . PHE A  1 252 ? 10.056  -0.689  -0.897  1.00 12.38  ? 252 PHE A N   1 
ATOM   2098  C  CA  . PHE A  1 252 ? 11.165  -1.098  -1.768  1.00 13.32  ? 252 PHE A CA  1 
ATOM   2099  C  C   . PHE A  1 252 ? 10.428  -1.762  -2.971  1.00 16.48  ? 252 PHE A C   1 
ATOM   2100  O  O   . PHE A  1 252 ? 9.953   -2.910  -2.871  1.00 22.25  ? 252 PHE A O   1 
ATOM   2101  C  CB  . PHE A  1 252 ? 11.975  -2.182  -1.039  1.00 14.77  ? 252 PHE A CB  1 
ATOM   2102  C  CG  . PHE A  1 252 ? 13.179  -2.621  -1.778  1.00 14.95  ? 252 PHE A CG  1 
ATOM   2103  C  CD1 . PHE A  1 252 ? 14.353  -1.827  -1.720  1.00 15.83  ? 252 PHE A CD1 1 
ATOM   2104  C  CD2 . PHE A  1 252 ? 13.218  -3.871  -2.418  1.00 17.58  ? 252 PHE A CD2 1 
ATOM   2105  C  CE1 . PHE A  1 252 ? 15.563  -2.355  -2.331  1.00 17.32  ? 252 PHE A CE1 1 
ATOM   2106  C  CE2 . PHE A  1 252 ? 14.393  -4.389  -2.970  1.00 17.06  ? 252 PHE A CE2 1 
ATOM   2107  C  CZ  . PHE A  1 252 ? 15.545  -3.579  -2.944  1.00 17.41  ? 252 PHE A CZ  1 
ATOM   2108  N  N   . ASP A  1 253 ? 10.308  -1.038  -4.063  1.00 22.87  ? 253 ASP A N   1 
ATOM   2109  C  CA  . ASP A  1 253 ? 9.395   -1.459  -5.152  1.00 23.71  ? 253 ASP A CA  1 
ATOM   2110  C  C   . ASP A  1 253 ? 10.175  -1.354  -6.427  1.00 21.46  ? 253 ASP A C   1 
ATOM   2111  O  O   . ASP A  1 253 ? 10.970  -0.419  -6.652  1.00 23.32  ? 253 ASP A O   1 
ATOM   2112  C  CB  . ASP A  1 253 ? 8.108   -0.599  -5.161  1.00 30.86  ? 253 ASP A CB  1 
ATOM   2113  C  CG  . ASP A  1 253 ? 7.043   -1.111  -6.166  1.00 47.41  ? 253 ASP A CG  1 
ATOM   2114  O  OD1 . ASP A  1 253 ? 6.758   -2.358  -6.168  1.00 41.20  ? 253 ASP A OD1 1 
ATOM   2115  O  OD2 . ASP A  1 253 ? 6.478   -0.277  -6.944  1.00 42.83  ? 253 ASP A OD2 1 
ATOM   2116  N  N   A GLU A  1 254 ? 9.958   -2.351  -7.280  0.50 20.96  ? 254 GLU A N   1 
ATOM   2117  N  N   B GLU A  1 254 ? 9.928   -2.327  -7.296  0.50 24.53  ? 254 GLU A N   1 
ATOM   2118  C  CA  A GLU A  1 254 ? 10.596  -2.413  -8.615  0.50 20.16  ? 254 GLU A CA  1 
ATOM   2119  C  CA  B GLU A  1 254 ? 10.592  -2.412  -8.613  0.50 21.66  ? 254 GLU A CA  1 
ATOM   2120  C  C   A GLU A  1 254 ? 12.107  -2.506  -8.477  0.50 22.40  ? 254 GLU A C   1 
ATOM   2121  C  C   B GLU A  1 254 ? 12.106  -2.454  -8.447  0.50 22.24  ? 254 GLU A C   1 
ATOM   2122  O  O   A GLU A  1 254 ? 12.865  -2.010  -9.314  0.50 21.56  ? 254 GLU A O   1 
ATOM   2123  O  O   B GLU A  1 254 ? 12.860  -1.872  -9.238  0.50 28.94  ? 254 GLU A O   1 
ATOM   2124  C  CB  A GLU A  1 254 ? 10.201  -1.207  -9.449  0.50 21.48  ? 254 GLU A CB  1 
ATOM   2125  C  CB  B GLU A  1 254 ? 10.145  -1.267  -9.506  0.50 23.40  ? 254 GLU A CB  1 
ATOM   2126  C  CG  A GLU A  1 254 ? 8.724   -1.273  -9.829  0.50 22.66  ? 254 GLU A CG  1 
ATOM   2127  C  CG  B GLU A  1 254 ? 8.643   -1.365  -9.774  0.50 30.77  ? 254 GLU A CG  1 
ATOM   2128  C  CD  A GLU A  1 254 ? 8.248   -0.103  -10.669 0.50 24.89  ? 254 GLU A CD  1 
ATOM   2129  C  CD  B GLU A  1 254 ? 8.236   -2.696  -10.404 0.50 32.61  ? 254 GLU A CD  1 
ATOM   2130  O  OE1 A GLU A  1 254 ? 8.976   0.910   -10.756 0.50 39.26  ? 254 GLU A OE1 1 
ATOM   2131  O  OE1 B GLU A  1 254 ? 8.878   -3.093  -11.409 0.50 41.87  ? 254 GLU A OE1 1 
ATOM   2132  O  OE2 A GLU A  1 254 ? 7.149   -0.212  -11.260 0.50 31.93  ? 254 GLU A OE2 1 
ATOM   2133  O  OE2 B GLU A  1 254 ? 7.283   -3.357  -9.899  0.50 36.65  ? 254 GLU A OE2 1 
ATOM   2134  N  N   . ARG A  1 255 ? 12.536  -3.185  -7.416  1.00 21.58  ? 255 ARG A N   1 
ATOM   2135  C  CA  . ARG A  1 255 ? 13.935  -3.365  -7.137  1.00 20.93  ? 255 ARG A CA  1 
ATOM   2136  C  C   . ARG A  1 255 ? 14.178  -4.799  -6.669  1.00 18.82  ? 255 ARG A C   1 
ATOM   2137  O  O   . ARG A  1 255 ? 13.256  -5.489  -6.148  1.00 20.54  ? 255 ARG A O   1 
ATOM   2138  C  CB  . ARG A  1 255 ? 14.390  -2.395  -6.054  1.00 19.00  ? 255 ARG A CB  1 
ATOM   2139  C  CG  . ARG A  1 255 ? 14.348  -0.953  -6.497  1.00 21.20  ? 255 ARG A CG  1 
ATOM   2140  C  CD  . ARG A  1 255 ? 14.891  -0.003  -5.417  1.00 22.32  ? 255 ARG A CD  1 
ATOM   2141  N  NE  . ARG A  1 255 ? 16.277  -0.280  -5.262  1.00 21.31  ? 255 ARG A NE  1 
ATOM   2142  C  CZ  . ARG A  1 255 ? 16.960  -0.073  -4.154  1.00 20.02  ? 255 ARG A CZ  1 
ATOM   2143  N  NH1 . ARG A  1 255 ? 16.370  0.581   -3.116  1.00 21.56  ? 255 ARG A NH1 1 
ATOM   2144  N  NH2 . ARG A  1 255 ? 18.258  -0.492  -4.107  1.00 17.70  ? 255 ARG A NH2 1 
ATOM   2145  N  N   . LEU A  1 256 ? 15.436  -5.203  -6.721  1.00 20.96  ? 256 LEU A N   1 
ATOM   2146  C  CA  . LEU A  1 256 ? 15.830  -6.541  -6.327  1.00 20.82  ? 256 LEU A CA  1 
ATOM   2147  C  C   . LEU A  1 256 ? 16.812  -6.473  -5.176  1.00 18.43  ? 256 LEU A C   1 
ATOM   2148  O  O   . LEU A  1 256 ? 17.579  -5.519  -5.037  1.00 19.80  ? 256 LEU A O   1 
ATOM   2149  C  CB  . LEU A  1 256 ? 16.501  -7.317  -7.480  1.00 21.05  ? 256 LEU A CB  1 
ATOM   2150  C  CG  . LEU A  1 256 ? 15.515  -7.640  -8.608  1.00 28.07  ? 256 LEU A CG  1 
ATOM   2151  C  CD1 . LEU A  1 256 ? 16.325  -8.191  -9.779  1.00 29.21  ? 256 LEU A CD1 1 
ATOM   2152  C  CD2 . LEU A  1 256 ? 14.391  -8.651  -8.260  1.00 33.10  ? 256 LEU A CD2 1 
ATOM   2153  N  N   . VAL A  1 257 ? 16.814  -7.513  -4.379  1.00 18.18  ? 257 VAL A N   1 
ATOM   2154  C  CA  . VAL A  1 257 ? 17.954  -7.805  -3.549  1.00 15.82  ? 257 VAL A CA  1 
ATOM   2155  C  C   . VAL A  1 257 ? 18.656  -9.001  -4.096  1.00 15.39  ? 257 VAL A C   1 
ATOM   2156  O  O   . VAL A  1 257 ? 18.048  -10.016 -4.413  1.00 17.09  ? 257 VAL A O   1 
ATOM   2157  C  CB  . VAL A  1 257 ? 17.451  -8.107  -2.131  1.00 15.58  ? 257 VAL A CB  1 
ATOM   2158  C  CG1 . VAL A  1 257 ? 18.554  -8.649  -1.253  1.00 15.90  ? 257 VAL A CG1 1 
ATOM   2159  C  CG2 . VAL A  1 257 ? 16.773  -6.893  -1.512  1.00 17.24  ? 257 VAL A CG2 1 
ATOM   2160  N  N   . TYR A  1 258 ? 19.952  -8.848  -4.249  1.00 14.36  ? 258 TYR A N   1 
ATOM   2161  C  CA  . TYR A  1 258 ? 20.691  -9.911  -4.868  1.00 15.41  ? 258 TYR A CA  1 
ATOM   2162  C  C   . TYR A  1 258 ? 21.217  -10.815 -3.793  1.00 13.95  ? 258 TYR A C   1 
ATOM   2163  O  O   . TYR A  1 258 ? 21.555  -10.359 -2.706  1.00 15.49  ? 258 TYR A O   1 
ATOM   2164  C  CB  . TYR A  1 258 ? 21.847  -9.298  -5.680  1.00 17.66  ? 258 TYR A CB  1 
ATOM   2165  C  CG  . TYR A  1 258 ? 21.274  -8.399  -6.705  1.00 18.07  ? 258 TYR A CG  1 
ATOM   2166  C  CD1 . TYR A  1 258 ? 20.749  -8.940  -7.843  1.00 20.72  ? 258 TYR A CD1 1 
ATOM   2167  C  CD2 . TYR A  1 258 ? 21.176  -7.039  -6.468  1.00 19.09  ? 258 TYR A CD2 1 
ATOM   2168  C  CE1 . TYR A  1 258 ? 20.164  -8.110  -8.859  1.00 25.72  ? 258 TYR A CE1 1 
ATOM   2169  C  CE2 . TYR A  1 258 ? 20.558  -6.202  -7.392  1.00 22.78  ? 258 TYR A CE2 1 
ATOM   2170  C  CZ  . TYR A  1 258 ? 20.064  -6.742  -8.608  1.00 22.55  ? 258 TYR A CZ  1 
ATOM   2171  O  OH  . TYR A  1 258 ? 19.486  -5.854  -9.492  1.00 30.59  ? 258 TYR A OH  1 
ATOM   2172  N  N   . THR A  1 259 ? 21.242  -12.097 -4.065  1.00 14.46  ? 259 THR A N   1 
ATOM   2173  C  CA  . THR A  1 259 ? 21.745  -13.068 -3.105  1.00 13.48  ? 259 THR A CA  1 
ATOM   2174  C  C   . THR A  1 259 ? 22.945  -13.796 -3.658  1.00 12.48  ? 259 THR A C   1 
ATOM   2175  O  O   . THR A  1 259 ? 23.042  -14.103 -4.853  1.00 14.96  ? 259 THR A O   1 
ATOM   2176  C  CB  . THR A  1 259 ? 20.659  -14.081 -2.668  1.00 14.42  ? 259 THR A CB  1 
ATOM   2177  O  OG1 . THR A  1 259 ? 20.196  -14.766 -3.821  1.00 18.28  ? 259 THR A OG1 1 
ATOM   2178  C  CG2 . THR A  1 259 ? 19.483  -13.333 -2.044  1.00 16.26  ? 259 THR A CG2 1 
ATOM   2179  N  N   . SER A  1 260 ? 23.852  -14.135 -2.752  1.00 12.69  ? 260 SER A N   1 
ATOM   2180  C  CA  . SER A  1 260 ? 25.001  -14.924 -3.116  1.00 14.81  ? 260 SER A CA  1 
ATOM   2181  C  C   . SER A  1 260 ? 24.739  -16.409 -3.054  1.00 15.34  ? 260 SER A C   1 
ATOM   2182  O  O   . SER A  1 260 ? 25.625  -17.196 -3.311  1.00 19.68  ? 260 SER A O   1 
ATOM   2183  C  CB  . SER A  1 260 ? 26.190  -14.589 -2.242  1.00 14.33  ? 260 SER A CB  1 
ATOM   2184  O  OG  . SER A  1 260 ? 25.895  -14.997 -0.955  1.00 13.75  ? 260 SER A OG  1 
ATOM   2185  N  N   . PHE A  1 261 ? 23.543  -16.781 -2.682  1.00 16.07  ? 261 PHE A N   1 
ATOM   2186  C  CA  . PHE A  1 261 ? 23.154  -18.161 -2.516  1.00 18.75  ? 261 PHE A CA  1 
ATOM   2187  C  C   . PHE A  1 261 ? 21.928  -18.381 -3.361  1.00 19.57  ? 261 PHE A C   1 
ATOM   2188  O  O   . PHE A  1 261 ? 21.094  -17.469 -3.572  1.00 22.28  ? 261 PHE A O   1 
ATOM   2189  C  CB  . PHE A  1 261 ? 22.869  -18.469 -1.030  1.00 18.01  ? 261 PHE A CB  1 
ATOM   2190  C  CG  . PHE A  1 261 ? 21.874  -17.566 -0.401  1.00 17.94  ? 261 PHE A CG  1 
ATOM   2191  C  CD1 . PHE A  1 261 ? 20.531  -17.894 -0.367  1.00 20.85  ? 261 PHE A CD1 1 
ATOM   2192  C  CD2 . PHE A  1 261 ? 22.275  -16.308 0.131   1.00 15.26  ? 261 PHE A CD2 1 
ATOM   2193  C  CE1 . PHE A  1 261 ? 19.599  -17.037 0.248   1.00 23.54  ? 261 PHE A CE1 1 
ATOM   2194  C  CE2 . PHE A  1 261 ? 21.329  -15.476 0.736   1.00 16.37  ? 261 PHE A CE2 1 
ATOM   2195  C  CZ  . PHE A  1 261 ? 20.005  -15.824 0.799   1.00 18.97  ? 261 PHE A CZ  1 
ATOM   2196  N  N   . SER A  1 262 ? 21.863  -19.553 -3.926  1.00 30.30  ? 262 SER A N   1 
ATOM   2197  C  CA  . SER A  1 262 ? 20.596  -19.893 -4.565  1.00 41.57  ? 262 SER A CA  1 
ATOM   2198  C  C   . SER A  1 262 ? 19.885  -20.905 -3.678  1.00 47.86  ? 262 SER A C   1 
ATOM   2199  O  O   . SER A  1 262 ? 18.679  -20.754 -3.386  1.00 59.80  ? 262 SER A O   1 
ATOM   2200  C  CB  . SER A  1 262 ? 20.787  -20.391 -5.998  1.00 54.70  ? 262 SER A CB  1 
ATOM   2201  O  OG  . SER A  1 262 ? 21.777  -21.406 -6.073  1.00 59.65  ? 262 SER A OG  1 
ATOM   2202  N  N   . GLN A  1 263 ? 20.651  -21.906 -3.223  1.00 46.16  ? 263 GLN A N   1 
ATOM   2203  C  CA  . GLN A  1 263 ? 20.169  -22.874 -2.269  1.00 53.72  ? 263 GLN A CA  1 
ATOM   2204  C  C   . GLN A  1 263 ? 19.835  -22.085 -1.004  1.00 62.96  ? 263 GLN A C   1 
ATOM   2205  O  O   . GLN A  1 263 ? 19.180  -22.634 -0.075  1.00 171.99 ? 263 GLN A O   1 
ATOM   2206  C  CB  . GLN A  1 263 ? 21.250  -23.897 -1.891  1.00 59.97  ? 263 GLN A CB  1 
ATOM   2207  C  CG  . GLN A  1 263 ? 21.927  -24.597 -3.024  1.00 65.35  ? 263 GLN A CG  1 
ATOM   2208  C  CD  . GLN A  1 263 ? 22.376  -26.045 -2.718  1.00 31.01  ? 263 GLN A CD  1 
ATOM   2209  O  OE1 . GLN A  1 263 ? 23.471  -26.283 -2.115  1.00 35.19  ? 263 GLN A OE1 1 
ATOM   2210  N  NE2 . GLN A  1 263 ? 21.640  -26.990 -3.264  1.00 20.36  ? 263 GLN A NE2 1 
ATOM   2211  N  N   . LYS B  1 3   ? -1.189  17.612  -1.939  1.00 302.94 ? 3   LYS B N   1 
ATOM   2212  C  CA  . LYS B  1 3   ? -0.331  16.895  -2.913  1.00 54.11  ? 3   LYS B CA  1 
ATOM   2213  C  C   . LYS B  1 3   ? 0.585   15.800  -2.224  1.00 30.03  ? 3   LYS B C   1 
ATOM   2214  O  O   . LYS B  1 3   ? 1.627   15.369  -2.874  1.00 27.39  ? 3   LYS B O   1 
ATOM   2215  C  CB  . LYS B  1 3   ? 0.541   17.868  -3.658  1.00 43.37  ? 3   LYS B CB  1 
ATOM   2216  C  CG  . LYS B  1 3   ? 1.623   18.373  -2.761  1.00 35.37  ? 3   LYS B CG  1 
ATOM   2217  C  CD  . LYS B  1 3   ? 1.955   19.807  -3.111  1.00 52.99  ? 3   LYS B CD  1 
ATOM   2218  C  CE  . LYS B  1 3   ? 3.125   19.846  -4.077  1.00 76.84  ? 3   LYS B CE  1 
ATOM   2219  N  NZ  . LYS B  1 3   ? 4.263   18.951  -3.641  1.00 85.23  ? 3   LYS B NZ  1 
ATOM   2220  N  N   . TRP B  1 4   ? 0.244   15.372  -0.998  1.00 16.80  ? 4   TRP B N   1 
ATOM   2221  C  CA  . TRP B  1 4   ? 0.902   14.207  -0.442  1.00 12.96  ? 4   TRP B CA  1 
ATOM   2222  C  C   . TRP B  1 4   ? 0.652   13.022  -1.362  1.00 12.44  ? 4   TRP B C   1 
ATOM   2223  O  O   . TRP B  1 4   ? -0.340  12.987  -2.080  1.00 12.90  ? 4   TRP B O   1 
ATOM   2224  C  CB  . TRP B  1 4   ? 0.396   14.022  0.978   1.00 12.99  ? 4   TRP B CB  1 
ATOM   2225  C  CG  . TRP B  1 4   ? -1.053  13.718  1.154   1.00 11.47  ? 4   TRP B CG  1 
ATOM   2226  C  CD1 . TRP B  1 4   ? -2.071  14.607  1.447   1.00 13.32  ? 4   TRP B CD1 1 
ATOM   2227  C  CD2 . TRP B  1 4   ? -1.688  12.425  1.102   1.00 10.66  ? 4   TRP B CD2 1 
ATOM   2228  N  NE1 . TRP B  1 4   ? -3.253  13.957  1.611   1.00 12.54  ? 4   TRP B NE1 1 
ATOM   2229  C  CE2 . TRP B  1 4   ? -3.088  12.619  1.394   1.00 11.22  ? 4   TRP B CE2 1 
ATOM   2230  C  CE3 . TRP B  1 4   ? -1.190  11.134  0.924   1.00 11.42  ? 4   TRP B CE3 1 
ATOM   2231  C  CZ2 . TRP B  1 4   ? -3.975  11.593  1.470   1.00 13.22  ? 4   TRP B CZ2 1 
ATOM   2232  C  CZ3 . TRP B  1 4   ? -2.075  10.112  0.980   1.00 11.88  ? 4   TRP B CZ3 1 
ATOM   2233  C  CH2 . TRP B  1 4   ? -3.441  10.324  1.255   1.00 12.31  ? 4   TRP B CH2 1 
ATOM   2234  N  N   . THR B  1 5   ? 1.554   12.074  -1.301  1.00 11.84  ? 5   THR B N   1 
ATOM   2235  C  CA  . THR B  1 5   ? 1.448   10.899  -2.120  1.00 11.90  ? 5   THR B CA  1 
ATOM   2236  C  C   . THR B  1 5   ? 1.907   9.693   -1.296  1.00 10.81  ? 5   THR B C   1 
ATOM   2237  O  O   . THR B  1 5   ? 2.301   9.796   -0.135  1.00 10.71  ? 5   THR B O   1 
ATOM   2238  C  CB  . THR B  1 5   ? 2.394   11.001  -3.400  1.00 13.05  ? 5   THR B CB  1 
ATOM   2239  O  OG1 . THR B  1 5   ? 3.718   10.908  -2.861  1.00 14.61  ? 5   THR B OG1 1 
ATOM   2240  C  CG2 . THR B  1 5   ? 2.123   12.262  -4.233  1.00 15.40  ? 5   THR B CG2 1 
ATOM   2241  N  N   . TYR B  1 6   ? 1.965   8.547   -1.961  1.00 11.09  ? 6   TYR B N   1 
ATOM   2242  C  CA  . TYR B  1 6   ? 2.523   7.334   -1.362  1.00 12.20  ? 6   TYR B CA  1 
ATOM   2243  C  C   . TYR B  1 6   ? 3.924   7.006   -1.939  1.00 12.32  ? 6   TYR B C   1 
ATOM   2244  O  O   . TYR B  1 6   ? 4.435   5.938   -1.600  1.00 12.37  ? 6   TYR B O   1 
ATOM   2245  C  CB  . TYR B  1 6   ? 1.580   6.149   -1.603  1.00 12.59  ? 6   TYR B CB  1 
ATOM   2246  C  CG  . TYR B  1 6   ? 0.358   6.208   -0.714  1.00 10.33  ? 6   TYR B CG  1 
ATOM   2247  C  CD1 . TYR B  1 6   ? -0.840  6.769   -1.162  1.00 9.95   ? 6   TYR B CD1 1 
ATOM   2248  C  CD2 . TYR B  1 6   ? 0.405   5.710   0.581   1.00 10.01  ? 6   TYR B CD2 1 
ATOM   2249  C  CE1 . TYR B  1 6   ? -1.991  6.765   -0.373  1.00 11.04  ? 6   TYR B CE1 1 
ATOM   2250  C  CE2 . TYR B  1 6   ? -0.738  5.650   1.375   1.00 9.60   ? 6   TYR B CE2 1 
ATOM   2251  C  CZ  . TYR B  1 6   ? -1.926  6.176   0.896   1.00 9.60   ? 6   TYR B CZ  1 
ATOM   2252  O  OH  . TYR B  1 6   ? -3.091  6.113   1.631   1.00 11.79  ? 6   TYR B OH  1 
ATOM   2253  N  N   . PHE B  1 7   ? 4.453   7.828   -2.813  1.00 13.04  ? 7   PHE B N   1 
ATOM   2254  C  CA  . PHE B  1 7   ? 5.670   7.454   -3.551  1.00 15.24  ? 7   PHE B CA  1 
ATOM   2255  C  C   . PHE B  1 7   ? 6.419   8.669   -3.932  1.00 17.40  ? 7   PHE B C   1 
ATOM   2256  O  O   . PHE B  1 7   ? 5.854   9.563   -4.573  1.00 17.13  ? 7   PHE B O   1 
ATOM   2257  C  CB  . PHE B  1 7   ? 5.351   6.627   -4.807  1.00 20.16  ? 7   PHE B CB  1 
ATOM   2258  C  CG  . PHE B  1 7   ? 6.589   6.231   -5.558  1.00 23.02  ? 7   PHE B CG  1 
ATOM   2259  C  CD1 . PHE B  1 7   ? 7.464   5.222   -5.094  1.00 28.27  ? 7   PHE B CD1 1 
ATOM   2260  C  CD2 . PHE B  1 7   ? 6.937   6.934   -6.713  1.00 32.75  ? 7   PHE B CD2 1 
ATOM   2261  C  CE1 . PHE B  1 7   ? 8.626   4.901   -5.808  1.00 30.38  ? 7   PHE B CE1 1 
ATOM   2262  C  CE2 . PHE B  1 7   ? 8.076   6.619   -7.438  1.00 43.76  ? 7   PHE B CE2 1 
ATOM   2263  C  CZ  . PHE B  1 7   ? 8.930   5.606   -6.989  1.00 50.39  ? 7   PHE B CZ  1 
ATOM   2264  N  N   . GLY B  1 8   ? 7.694   8.677   -3.576  1.00 18.25  ? 8   GLY B N   1 
ATOM   2265  C  CA  . GLY B  1 8   ? 8.560   9.736   -4.089  1.00 18.38  ? 8   GLY B CA  1 
ATOM   2266  C  C   . GLY B  1 8   ? 8.692   10.825  -3.033  1.00 16.12  ? 8   GLY B C   1 
ATOM   2267  O  O   . GLY B  1 8   ? 8.473   10.604  -1.802  1.00 15.74  ? 8   GLY B O   1 
ATOM   2268  N  N   A PRO B  1 9   ? 9.091   12.020  -3.474  0.50 17.10  ? 9   PRO B N   1 
ATOM   2269  N  N   B PRO B  1 9   ? 9.071   12.060  -3.434  0.50 17.44  ? 9   PRO B N   1 
ATOM   2270  C  CA  A PRO B  1 9   ? 9.429   13.121  -2.617  0.50 16.61  ? 9   PRO B CA  1 
ATOM   2271  C  CA  B PRO B  1 9   ? 9.468   12.999  -2.390  0.50 18.81  ? 9   PRO B CA  1 
ATOM   2272  C  C   A PRO B  1 9   ? 8.365   13.480  -1.588  0.50 15.76  ? 9   PRO B C   1 
ATOM   2273  C  C   B PRO B  1 9   ? 8.334   13.584  -1.555  0.50 18.45  ? 9   PRO B C   1 
ATOM   2274  O  O   A PRO B  1 9   ? 8.700   13.834  -0.447  0.50 13.98  ? 9   PRO B O   1 
ATOM   2275  O  O   B PRO B  1 9   ? 8.581   14.268  -0.555  0.50 20.01  ? 9   PRO B O   1 
ATOM   2276  C  CB  A PRO B  1 9   ? 9.663   14.265  -3.612  0.50 18.02  ? 9   PRO B CB  1 
ATOM   2277  C  CB  B PRO B  1 9   ? 10.084  14.164  -3.189  0.50 21.02  ? 9   PRO B CB  1 
ATOM   2278  C  CG  A PRO B  1 9   ? 10.263  13.562  -4.752  0.50 21.44  ? 9   PRO B CG  1 
ATOM   2279  C  CG  B PRO B  1 9   ? 9.268   14.136  -4.431  0.50 23.77  ? 9   PRO B CG  1 
ATOM   2280  C  CD  A PRO B  1 9   ? 9.501   12.266  -4.865  0.50 19.45  ? 9   PRO B CD  1 
ATOM   2281  C  CD  B PRO B  1 9   ? 9.148   12.680  -4.772  0.50 22.14  ? 9   PRO B CD  1 
ATOM   2282  N  N   . ASP B  1 10  ? 7.094   13.371  -1.967  1.00 16.29  ? 10  ASP B N   1 
ATOM   2283  C  CA  . ASP B  1 10  ? 5.991   13.731  -1.098  1.00 13.03  ? 10  ASP B CA  1 
ATOM   2284  C  C   . ASP B  1 10  ? 5.348   12.502  -0.404  1.00 11.43  ? 10  ASP B C   1 
ATOM   2285  O  O   . ASP B  1 10  ? 4.189   12.602  0.080   1.00 12.25  ? 10  ASP B O   1 
ATOM   2286  C  CB  . ASP B  1 10  ? 4.918   14.500  -1.907  1.00 16.00  ? 10  ASP B CB  1 
ATOM   2287  C  CG  . ASP B  1 10  ? 5.491   15.749  -2.514  1.00 19.31  ? 10  ASP B CG  1 
ATOM   2288  O  OD1 . ASP B  1 10  ? 6.142   16.507  -1.758  1.00 23.03  ? 10  ASP B OD1 1 
ATOM   2289  O  OD2 . ASP B  1 10  ? 5.273   16.009  -3.701  1.00 25.88  ? 10  ASP B OD2 1 
ATOM   2290  N  N   . GLY B  1 11  ? 6.045   11.391  -0.431  1.00 12.31  ? 11  GLY B N   1 
ATOM   2291  C  CA  . GLY B  1 11  ? 5.545   10.189  0.259   1.00 10.80  ? 11  GLY B CA  1 
ATOM   2292  C  C   . GLY B  1 11  ? 5.604   10.189  1.750   1.00 9.56   ? 11  GLY B C   1 
ATOM   2293  O  O   . GLY B  1 11  ? 5.824   11.212  2.408   1.00 9.74   ? 11  GLY B O   1 
ATOM   2294  N  N   . GLU B  1 12  ? 5.327   9.011   2.341   1.00 8.74   ? 12  GLU B N   1 
ATOM   2295  C  CA  . GLU B  1 12  ? 4.924   8.986   3.763   1.00 8.51   ? 12  GLU B CA  1 
ATOM   2296  C  C   . GLU B  1 12  ? 5.973   9.427   4.723   1.00 8.60   ? 12  GLU B C   1 
ATOM   2297  O  O   . GLU B  1 12  ? 5.601   9.904   5.818   1.00 9.13   ? 12  GLU B O   1 
ATOM   2298  C  CB  . GLU B  1 12  ? 4.426   7.577   4.139   1.00 8.64   ? 12  GLU B CB  1 
ATOM   2299  C  CG  . GLU B  1 12  ? 5.555   6.547   4.229   1.00 8.57   ? 12  GLU B CG  1 
ATOM   2300  C  CD  . GLU B  1 12  ? 4.977   5.171   4.143   1.00 8.19   ? 12  GLU B CD  1 
ATOM   2301  O  OE1 . GLU B  1 12  ? 4.591   4.638   5.222   1.00 8.43   ? 12  GLU B OE1 1 
ATOM   2302  O  OE2 . GLU B  1 12  ? 4.812   4.615   3.041   1.00 9.59   ? 12  GLU B OE2 1 
ATOM   2303  N  N   . ASN B  1 13  ? 7.269   9.347   4.411   1.00 8.43   ? 13  ASN B N   1 
ATOM   2304  C  CA  . ASN B  1 13  ? 8.261   9.830   5.383   1.00 8.80   ? 13  ASN B CA  1 
ATOM   2305  C  C   . ASN B  1 13  ? 8.253   11.371  5.423   1.00 9.00   ? 13  ASN B C   1 
ATOM   2306  O  O   . ASN B  1 13  ? 8.866   11.905  6.352   1.00 10.23  ? 13  ASN B O   1 
ATOM   2307  C  CB  . ASN B  1 13  ? 9.651   9.343   5.046   1.00 9.09   ? 13  ASN B CB  1 
ATOM   2308  C  CG  . ASN B  1 13  ? 9.841   7.860   5.272   1.00 8.82   ? 13  ASN B CG  1 
ATOM   2309  O  OD1 . ASN B  1 13  ? 8.917   7.183   5.792   1.00 9.05   ? 13  ASN B OD1 1 
ATOM   2310  N  ND2 . ASN B  1 13  ? 10.994  7.348   4.967   1.00 9.54   ? 13  ASN B ND2 1 
ATOM   2311  N  N   . SER B  1 14  ? 7.597   12.019  4.486   1.00 8.72   ? 14  SER B N   1 
ATOM   2312  C  CA  . SER B  1 14  ? 7.547   13.466  4.382   1.00 10.15  ? 14  SER B CA  1 
ATOM   2313  C  C   . SER B  1 14  ? 6.198   14.022  4.862   1.00 8.39   ? 14  SER B C   1 
ATOM   2314  O  O   . SER B  1 14  ? 6.060   15.246  4.967   1.00 9.82   ? 14  SER B O   1 
ATOM   2315  C  CB  . SER B  1 14  ? 7.833   13.937  2.968   1.00 11.00  ? 14  SER B CB  1 
ATOM   2316  O  OG  . SER B  1 14  ? 9.202   13.695  2.706   1.00 11.67  ? 14  SER B OG  1 
ATOM   2317  N  N   . TRP B  1 15  ? 5.181   13.189  5.098   1.00 8.53   ? 15  TRP B N   1 
ATOM   2318  C  CA  . TRP B  1 15  ? 3.875   13.697  5.492   1.00 9.09   ? 15  TRP B CA  1 
ATOM   2319  C  C   . TRP B  1 15  ? 3.940   14.616  6.668   1.00 9.19   ? 15  TRP B C   1 
ATOM   2320  O  O   . TRP B  1 15  ? 3.226   15.621  6.721   1.00 9.96   ? 15  TRP B O   1 
ATOM   2321  C  CB  . TRP B  1 15  ? 2.887   12.555  5.761   1.00 8.94   ? 15  TRP B CB  1 
ATOM   2322  C  CG  . TRP B  1 15  ? 2.555   11.707  4.637   1.00 8.44   ? 15  TRP B CG  1 
ATOM   2323  C  CD1 . TRP B  1 15  ? 2.785   11.895  3.272   1.00 9.36   ? 15  TRP B CD1 1 
ATOM   2324  C  CD2 . TRP B  1 15  ? 1.779   10.492  4.715   1.00 8.19   ? 15  TRP B CD2 1 
ATOM   2325  N  NE1 . TRP B  1 15  ? 2.254   10.886  2.518   1.00 8.84   ? 15  TRP B NE1 1 
ATOM   2326  C  CE2 . TRP B  1 15  ? 1.602   10.006  3.383   1.00 9.00   ? 15  TRP B CE2 1 
ATOM   2327  C  CE3 . TRP B  1 15  ? 1.233   9.773   5.784   1.00 8.37   ? 15  TRP B CE3 1 
ATOM   2328  C  CZ2 . TRP B  1 15  ? 0.929   8.838   3.105   1.00 9.40   ? 15  TRP B CZ2 1 
ATOM   2329  C  CZ3 . TRP B  1 15  ? 0.535   8.617   5.493   1.00 8.68   ? 15  TRP B CZ3 1 
ATOM   2330  C  CH2 . TRP B  1 15  ? 0.389   8.174   4.186   1.00 8.99   ? 15  TRP B CH2 1 
ATOM   2331  N  N   . SER B  1 16  ? 4.791   14.302  7.626   1.00 9.74   ? 16  SER B N   1 
ATOM   2332  C  CA  . SER B  1 16  ? 4.812   15.069  8.836   1.00 10.10  ? 16  SER B CA  1 
ATOM   2333  C  C   . SER B  1 16  ? 5.307   16.505  8.652   1.00 10.19  ? 16  SER B C   1 
ATOM   2334  O  O   . SER B  1 16  ? 5.096   17.347  9.549   1.00 11.94  ? 16  SER B O   1 
ATOM   2335  C  CB  . SER B  1 16  ? 5.762   14.425  9.888   1.00 12.90  ? 16  SER B CB  1 
ATOM   2336  O  OG  . SER B  1 16  ? 7.091   14.536  9.362   1.00 15.64  ? 16  SER B OG  1 
ATOM   2337  N  N   . LYS B  1 17  ? 5.947   16.807  7.533   1.00 10.43  ? 17  LYS B N   1 
ATOM   2338  C  CA  . LYS B  1 17  ? 6.364   18.192  7.233   1.00 10.53  ? 17  LYS B CA  1 
ATOM   2339  C  C   . LYS B  1 17  ? 5.190   19.130  7.153   1.00 11.57  ? 17  LYS B C   1 
ATOM   2340  O  O   . LYS B  1 17  ? 5.330   20.316  7.568   1.00 14.40  ? 17  LYS B O   1 
ATOM   2341  C  CB  . LYS B  1 17  ? 7.171   18.252  5.957   1.00 11.59  ? 17  LYS B CB  1 
ATOM   2342  C  CG  . LYS B  1 17  ? 8.438   17.410  5.913   1.00 11.77  ? 17  LYS B CG  1 
ATOM   2343  C  CD  . LYS B  1 17  ? 9.046   17.371  4.471   1.00 11.40  ? 17  LYS B CD  1 
ATOM   2344  C  CE  . LYS B  1 17  ? 10.228  16.480  4.322   1.00 11.16  ? 17  LYS B CE  1 
ATOM   2345  N  NZ  . LYS B  1 17  ? 10.824  16.601  3.015   1.00 12.18  ? 17  LYS B NZ  1 
ATOM   2346  N  N   . LYS B  1 18  ? 4.086   18.672  6.592   1.00 11.69  ? 18  LYS B N   1 
ATOM   2347  C  CA  . LYS B  1 18  ? 2.858   19.484  6.429   1.00 12.12  ? 18  LYS B CA  1 
ATOM   2348  C  C   . LYS B  1 18  ? 1.776   19.097  7.428   1.00 11.83  ? 18  LYS B C   1 
ATOM   2349  O  O   . LYS B  1 18  ? 0.886   19.899  7.640   1.00 15.01  ? 18  LYS B O   1 
ATOM   2350  C  CB  . LYS B  1 18  ? 2.321   19.381  4.998   1.00 15.34  ? 18  LYS B CB  1 
ATOM   2351  C  CG  . LYS B  1 18  ? 3.241   20.048  3.981   1.00 21.65  ? 18  LYS B CG  1 
ATOM   2352  C  CD  . LYS B  1 18  ? 2.600   19.980  2.578   1.00 27.78  ? 18  LYS B CD  1 
ATOM   2353  N  N   . TYR B  1 19  ? 1.838   17.875  7.944   1.00 10.88  ? 19  TYR B N   1 
ATOM   2354  C  CA  . TYR B  1 19  ? 0.753   17.297  8.723   1.00 10.63  ? 19  TYR B CA  1 
ATOM   2355  C  C   . TYR B  1 19  ? 1.320   16.795  10.022  1.00 10.51  ? 19  TYR B C   1 
ATOM   2356  O  O   . TYR B  1 19  ? 1.757   15.624  10.087  1.00 11.05  ? 19  TYR B O   1 
ATOM   2357  C  CB  . TYR B  1 19  ? 0.021   16.179  7.970   1.00 11.48  ? 19  TYR B CB  1 
ATOM   2358  C  CG  . TYR B  1 19  ? -0.564  16.596  6.651   1.00 11.14  ? 19  TYR B CG  1 
ATOM   2359  C  CD1 . TYR B  1 19  ? -1.803  17.258  6.614   1.00 13.98  ? 19  TYR B CD1 1 
ATOM   2360  C  CD2 . TYR B  1 19  ? 0.150   16.428  5.470   1.00 11.25  ? 19  TYR B CD2 1 
ATOM   2361  C  CE1 . TYR B  1 19  ? -2.345  17.656  5.403   1.00 16.44  ? 19  TYR B CE1 1 
ATOM   2362  C  CE2 . TYR B  1 19  ? -0.406  16.827  4.240   1.00 14.24  ? 19  TYR B CE2 1 
ATOM   2363  C  CZ  . TYR B  1 19  ? -1.637  17.454  4.228   1.00 17.26  ? 19  TYR B CZ  1 
ATOM   2364  O  OH  . TYR B  1 19  ? -2.156  17.812  3.030   1.00 20.85  ? 19  TYR B OH  1 
ATOM   2365  N  N   . PRO B  1 20  ? 1.473   17.637  11.026  1.00 11.97  ? 20  PRO B N   1 
ATOM   2366  C  CA  . PRO B  1 20  ? 2.217   17.264  12.188  1.00 13.65  ? 20  PRO B CA  1 
ATOM   2367  C  C   . PRO B  1 20  ? 1.718   16.009  12.884  1.00 11.53  ? 20  PRO B C   1 
ATOM   2368  O  O   . PRO B  1 20  ? 2.530   15.331  13.513  1.00 12.35  ? 20  PRO B O   1 
ATOM   2369  C  CB  . PRO B  1 20  ? 2.072   18.507  13.144  1.00 19.11  ? 20  PRO B CB  1 
ATOM   2370  C  CG  . PRO B  1 20  ? 1.720   19.624  12.254  1.00 20.69  ? 20  PRO B CG  1 
ATOM   2371  C  CD  . PRO B  1 20  ? 1.039   19.084  11.051  1.00 14.40  ? 20  PRO B CD  1 
ATOM   2372  N  N   . SER B  1 21  ? 0.426   15.725  12.840  1.00 10.74  ? 21  SER B N   1 
ATOM   2373  C  CA  . SER B  1 21  ? -0.011  14.517  13.533  1.00 10.83  ? 21  SER B CA  1 
ATOM   2374  C  C   . SER B  1 21  ? 0.576   13.266  12.926  1.00 8.76   ? 21  SER B C   1 
ATOM   2375  O  O   . SER B  1 21  ? 0.574   12.240  13.615  1.00 10.61  ? 21  SER B O   1 
ATOM   2376  C  CB  . SER B  1 21  ? -1.542  14.443  13.538  1.00 11.65  ? 21  SER B CB  1 
ATOM   2377  O  OG  . SER B  1 21  ? -2.091  15.451  14.337  1.00 14.64  ? 21  SER B OG  1 
ATOM   2378  N  N   . CYS B  1 22  ? 1.014   13.280  11.665  1.00 9.68   ? 22  CYS B N   1 
ATOM   2379  C  CA  . CYS B  1 22  ? 1.615   12.094  11.040  1.00 10.09  ? 22  CYS B CA  1 
ATOM   2380  C  C   . CYS B  1 22  ? 2.890   11.696  11.745  1.00 10.40  ? 22  CYS B C   1 
ATOM   2381  O  O   . CYS B  1 22  ? 3.341   10.570  11.561  1.00 10.72  ? 22  CYS B O   1 
ATOM   2382  C  CB  . CYS B  1 22  ? 1.835   12.309  9.554   1.00 9.96   ? 22  CYS B CB  1 
ATOM   2383  S  SG  . CYS B  1 22  ? 0.285   12.635  8.656   1.00 10.36  ? 22  CYS B SG  1 
ATOM   2384  N  N   . GLY B  1 23  ? 3.528   12.610  12.512  1.00 11.16  ? 23  GLY B N   1 
ATOM   2385  C  CA  . GLY B  1 23  ? 4.697   12.338  13.300  1.00 12.05  ? 23  GLY B CA  1 
ATOM   2386  C  C   . GLY B  1 23  ? 4.401   12.246  14.788  1.00 11.95  ? 23  GLY B C   1 
ATOM   2387  O  O   . GLY B  1 23  ? 5.322   12.225  15.604  1.00 13.88  ? 23  GLY B O   1 
ATOM   2388  N  N   . GLY B  1 24  ? 3.121   12.201  15.142  1.00 12.90  ? 24  GLY B N   1 
ATOM   2389  C  CA  . GLY B  1 24  ? 2.709   12.194  16.518  1.00 14.32  ? 24  GLY B CA  1 
ATOM   2390  C  C   . GLY B  1 24  ? 2.421   10.830  17.037  1.00 15.97  ? 24  GLY B C   1 
ATOM   2391  O  O   . GLY B  1 24  ? 2.871   9.831   16.484  1.00 17.04  ? 24  GLY B O   1 
ATOM   2392  N  N   . LEU B  1 25  ? 1.653   10.827  18.123  1.00 17.63  ? 25  LEU B N   1 
ATOM   2393  C  CA  . LEU B  1 25  ? 1.290   9.563   18.784  1.00 18.94  ? 25  LEU B CA  1 
ATOM   2394  C  C   . LEU B  1 25  ? 0.170   8.820   18.091  1.00 17.00  ? 25  LEU B C   1 
ATOM   2395  O  O   . LEU B  1 25  ? -0.548  9.411   17.263  1.00 14.85  ? 25  LEU B O   1 
ATOM   2396  C  CB  . LEU B  1 25  ? 0.944   9.888   20.246  1.00 31.79  ? 25  LEU B CB  1 
ATOM   2397  C  CG  . LEU B  1 25  ? 2.098   10.517  21.021  1.00 30.24  ? 25  LEU B CG  1 
ATOM   2398  C  CD1 . LEU B  1 25  ? 1.726   10.987  22.422  1.00 41.41  ? 25  LEU B CD1 1 
ATOM   2399  C  CD2 . LEU B  1 25  ? 3.303   9.547   20.946  1.00 32.63  ? 25  LEU B CD2 1 
ATOM   2400  N  N   . LEU B  1 26  ? 0.020   7.536   18.455  1.00 15.02  ? 26  LEU B N   1 
ATOM   2401  C  CA  . LEU B  1 26  ? -1.162  6.683   18.201  1.00 14.16  ? 26  LEU B CA  1 
ATOM   2402  C  C   . LEU B  1 26  ? -1.303  6.462   16.687  1.00 11.48  ? 26  LEU B C   1 
ATOM   2403  O  O   . LEU B  1 26  ? -2.434  6.326   16.218  1.00 12.28  ? 26  LEU B O   1 
ATOM   2404  C  CB  . LEU B  1 26  ? -2.434  7.303   18.805  1.00 16.72  ? 26  LEU B CB  1 
ATOM   2405  C  CG  . LEU B  1 26  ? -2.503  7.399   20.348  1.00 23.69  ? 26  LEU B CG  1 
ATOM   2406  C  CD1 . LEU B  1 26  ? -3.857  7.906   20.800  1.00 33.87  ? 26  LEU B CD1 1 
ATOM   2407  C  CD2 . LEU B  1 26  ? -2.126  6.130   21.029  1.00 25.09  ? 26  LEU B CD2 1 
ATOM   2408  N  N   . GLN B  1 27  ? -0.183  6.383   15.959  1.00 11.03  ? 27  GLN B N   1 
ATOM   2409  C  CA  . GLN B  1 27  ? -0.300  6.199   14.507  1.00 9.01   ? 27  GLN B CA  1 
ATOM   2410  C  C   . GLN B  1 27  ? -0.662  4.773   14.101  1.00 8.77   ? 27  GLN B C   1 
ATOM   2411  O  O   . GLN B  1 27  ? -0.197  3.792   14.656  1.00 10.53  ? 27  GLN B O   1 
ATOM   2412  C  CB  . GLN B  1 27  ? 0.942   6.677   13.784  1.00 10.12  ? 27  GLN B CB  1 
ATOM   2413  C  CG  . GLN B  1 27  ? 1.211   8.171   14.016  1.00 10.38  ? 27  GLN B CG  1 
ATOM   2414  C  CD  . GLN B  1 27  ? 0.154   8.998   13.324  1.00 9.30   ? 27  GLN B CD  1 
ATOM   2415  O  OE1 . GLN B  1 27  ? 0.157   9.135   12.109  1.00 9.85   ? 27  GLN B OE1 1 
ATOM   2416  N  NE2 . GLN B  1 27  ? -0.821  9.519   14.110  1.00 9.86   ? 27  GLN B NE2 1 
ATOM   2417  N  N   . SER B  1 28  ? -1.441  4.709   13.044  1.00 7.75   ? 28  SER B N   1 
ATOM   2418  C  CA  . SER B  1 28  ? -1.839  3.520   12.330  1.00 6.88   ? 28  SER B CA  1 
ATOM   2419  C  C   . SER B  1 28  ? -1.252  3.514   10.910  1.00 6.98   ? 28  SER B C   1 
ATOM   2420  O  O   . SER B  1 28  ? -0.979  4.580   10.381  1.00 7.63   ? 28  SER B O   1 
ATOM   2421  C  CB  . SER B  1 28  ? -3.324  3.450   12.270  1.00 7.35   ? 28  SER B CB  1 
ATOM   2422  O  OG  . SER B  1 28  ? -3.896  3.362   13.577  1.00 7.86   ? 28  SER B OG  1 
ATOM   2423  N  N   . PRO B  1 29  ? -1.163  2.351   10.266  1.00 6.83   ? 29  PRO B N   1 
ATOM   2424  C  CA  . PRO B  1 29  ? -1.509  0.996   10.732  1.00 6.68   ? 29  PRO B CA  1 
ATOM   2425  C  C   . PRO B  1 29  ? -0.353  0.423   11.516  1.00 6.32   ? 29  PRO B C   1 
ATOM   2426  O  O   . PRO B  1 29  ? 0.690   1.014   11.709  1.00 7.09   ? 29  PRO B O   1 
ATOM   2427  C  CB  . PRO B  1 29  ? -1.728  0.281   9.407   1.00 7.27   ? 29  PRO B CB  1 
ATOM   2428  C  CG  . PRO B  1 29  ? -0.615  0.864   8.517   1.00 7.64   ? 29  PRO B CG  1 
ATOM   2429  C  CD  . PRO B  1 29  ? -0.634  2.329   8.885   1.00 7.42   ? 29  PRO B CD  1 
ATOM   2430  N  N   . ILE B  1 30  ? -0.576  -0.825  12.001  1.00 7.32   ? 30  ILE B N   1 
ATOM   2431  C  CA  . ILE B  1 30  ? 0.366   -1.557  12.828  1.00 6.91   ? 30  ILE B CA  1 
ATOM   2432  C  C   . ILE B  1 30  ? 0.426   -2.990  12.399  1.00 7.34   ? 30  ILE B C   1 
ATOM   2433  O  O   . ILE B  1 30  ? -0.470  -3.488  11.728  1.00 7.95   ? 30  ILE B O   1 
ATOM   2434  C  CB  . ILE B  1 30  ? 0.032   -1.408  14.311  1.00 8.09   ? 30  ILE B CB  1 
ATOM   2435  C  CG1 . ILE B  1 30  ? -1.349  -2.016  14.639  1.00 9.00   ? 30  ILE B CG1 1 
ATOM   2436  C  CG2 . ILE B  1 30  ? 0.126   0.017   14.782  1.00 10.94  ? 30  ILE B CG2 1 
ATOM   2437  C  CD1 . ILE B  1 30  ? -1.664  -2.057  16.097  1.00 11.09  ? 30  ILE B CD1 1 
ATOM   2438  N  N   . ASP B  1 31  ? 1.503   -3.650  12.839  1.00 7.60   ? 31  ASP B N   1 
ATOM   2439  C  CA  . ASP B  1 31  ? 1.622   -5.086  12.683  1.00 8.12   ? 31  ASP B CA  1 
ATOM   2440  C  C   . ASP B  1 31  ? 0.987   -5.751  13.882  1.00 8.23   ? 31  ASP B C   1 
ATOM   2441  O  O   . ASP B  1 31  ? 1.387   -5.561  15.024  1.00 10.25  ? 31  ASP B O   1 
ATOM   2442  C  CB  . ASP B  1 31  ? 3.098   -5.467  12.604  1.00 9.43   ? 31  ASP B CB  1 
ATOM   2443  C  CG  . ASP B  1 31  ? 3.243   -6.986  12.465  1.00 10.42  ? 31  ASP B CG  1 
ATOM   2444  O  OD1 . ASP B  1 31  ? 2.682   -7.596  11.535  1.00 11.08  ? 31  ASP B OD1 1 
ATOM   2445  O  OD2 . ASP B  1 31  ? 3.910   -7.552  13.380  1.00 13.00  ? 31  ASP B OD2 1 
ATOM   2446  N  N   . LEU B  1 32  ? 0.032   -6.612  13.625  1.00 8.94   ? 32  LEU B N   1 
ATOM   2447  C  CA  . LEU B  1 32  ? -0.699  -7.341  14.696  1.00 9.91   ? 32  LEU B CA  1 
ATOM   2448  C  C   . LEU B  1 32  ? 0.085   -8.623  14.944  1.00 10.02  ? 32  LEU B C   1 
ATOM   2449  O  O   . LEU B  1 32  ? 0.090   -9.485  14.113  1.00 12.29  ? 32  LEU B O   1 
ATOM   2450  C  CB  . LEU B  1 32  ? -2.124  -7.598  14.193  1.00 10.57  ? 32  LEU B CB  1 
ATOM   2451  C  CG  . LEU B  1 32  ? -2.902  -6.325  13.832  1.00 10.23  ? 32  LEU B CG  1 
ATOM   2452  C  CD1 . LEU B  1 32  ? -4.143  -6.618  12.985  1.00 13.01  ? 32  LEU B CD1 1 
ATOM   2453  C  CD2 . LEU B  1 32  ? -3.239  -5.483  15.036  1.00 14.69  ? 32  LEU B CD2 1 
ATOM   2454  N  N   . HIS B  1 33  ? 0.755   -8.717  16.079  1.00 10.49  ? 33  HIS B N   1 
ATOM   2455  C  CA  . HIS B  1 33  ? 1.635   -9.871  16.387  1.00 11.30  ? 33  HIS B CA  1 
ATOM   2456  C  C   . HIS B  1 33  ? 1.532   -10.148 17.859  1.00 11.01  ? 33  HIS B C   1 
ATOM   2457  O  O   . HIS B  1 33  ? 1.177   -9.290  18.661  1.00 11.20  ? 33  HIS B O   1 
ATOM   2458  C  CB  . HIS B  1 33  ? 3.088   -9.551  15.950  1.00 12.26  ? 33  HIS B CB  1 
ATOM   2459  C  CG  . HIS B  1 33  ? 3.703   -8.401  16.699  1.00 11.53  ? 33  HIS B CG  1 
ATOM   2460  N  ND1 . HIS B  1 33  ? 3.410   -7.086  16.441  1.00 15.57  ? 33  HIS B ND1 1 
ATOM   2461  C  CD2 . HIS B  1 33  ? 4.668   -8.378  17.672  1.00 12.49  ? 33  HIS B CD2 1 
ATOM   2462  C  CE1 . HIS B  1 33  ? 4.126   -6.271  17.222  1.00 17.35  ? 33  HIS B CE1 1 
ATOM   2463  N  NE2 . HIS B  1 33  ? 4.920   -7.038  17.948  1.00 13.43  ? 33  HIS B NE2 1 
ATOM   2464  N  N   . SER B  1 34  ? 1.861   -11.374 18.246  1.00 11.61  ? 34  SER B N   1 
ATOM   2465  C  CA  . SER B  1 34  ? 1.515   -11.911 19.576  1.00 13.33  ? 34  SER B CA  1 
ATOM   2466  C  C   . SER B  1 34  ? 2.022   -11.081 20.666  1.00 12.40  ? 34  SER B C   1 
ATOM   2467  O  O   . SER B  1 34  ? 1.288   -10.939 21.676  1.00 14.09  ? 34  SER B O   1 
ATOM   2468  C  CB  . SER B  1 34  ? 2.008   -13.334 19.637  1.00 19.18  ? 34  SER B CB  1 
ATOM   2469  O  OG  . SER B  1 34  ? 3.449   -13.387 19.577  1.00 20.77  ? 34  SER B OG  1 
ATOM   2470  N  N   . ASP B  1 35  ? 3.200   -10.472 20.609  1.00 12.17  ? 35  ASP B N   1 
ATOM   2471  C  CA  . ASP B  1 35  ? 3.757   -9.749  21.767  1.00 12.41  ? 35  ASP B CA  1 
ATOM   2472  C  C   . ASP B  1 35  ? 2.944   -8.578  22.205  1.00 14.35  ? 35  ASP B C   1 
ATOM   2473  O  O   . ASP B  1 35  ? 3.086   -8.162  23.387  1.00 16.11  ? 35  ASP B O   1 
ATOM   2474  C  CB  . ASP B  1 35  ? 5.173   -9.227  21.444  1.00 13.79  ? 35  ASP B CB  1 
ATOM   2475  C  CG  . ASP B  1 35  ? 6.073   -10.256 20.830  1.00 14.04  ? 35  ASP B CG  1 
ATOM   2476  O  OD1 . ASP B  1 35  ? 5.740   -10.727 19.712  1.00 14.44  ? 35  ASP B OD1 1 
ATOM   2477  O  OD2 . ASP B  1 35  ? 7.089   -10.663 21.473  1.00 15.65  ? 35  ASP B OD2 1 
ATOM   2478  N  N   . ILE B  1 36  ? 2.097   -8.046  21.332  1.00 12.28  ? 36  ILE B N   1 
ATOM   2479  C  CA  . ILE B  1 36  ? 1.302   -6.874  21.664  1.00 12.61  ? 36  ILE B CA  1 
ATOM   2480  C  C   . ILE B  1 36  ? -0.174  -7.143  21.807  1.00 13.02  ? 36  ILE B C   1 
ATOM   2481  O  O   . ILE B  1 36  ? -0.954  -6.185  21.982  1.00 13.88  ? 36  ILE B O   1 
ATOM   2482  C  CB  . ILE B  1 36  ? 1.539   -5.653  20.717  1.00 15.06  ? 36  ILE B CB  1 
ATOM   2483  C  CG1 . ILE B  1 36  ? 1.294   -6.038  19.279  1.00 17.06  ? 36  ILE B CG1 1 
ATOM   2484  C  CG2 . ILE B  1 36  ? 2.966   -5.146  20.924  1.00 17.77  ? 36  ILE B CG2 1 
ATOM   2485  C  CD1 . ILE B  1 36  ? -0.006  -6.352  18.745  1.00 26.00  ? 36  ILE B CD1 1 
ATOM   2486  N  N   . LEU B  1 37  ? -0.592  -8.419  21.723  1.00 11.55  ? 37  LEU B N   1 
ATOM   2487  C  CA  . LEU B  1 37  ? -2.007  -8.804  21.803  1.00 11.80  ? 37  LEU B CA  1 
ATOM   2488  C  C   . LEU B  1 37  ? -2.402  -9.158  23.230  1.00 12.03  ? 37  LEU B C   1 
ATOM   2489  O  O   . LEU B  1 37  ? -1.624  -9.747  23.929  1.00 15.89  ? 37  LEU B O   1 
ATOM   2490  C  CB  . LEU B  1 37  ? -2.298  -9.982  20.859  1.00 12.26  ? 37  LEU B CB  1 
ATOM   2491  C  CG  . LEU B  1 37  ? -2.008  -9.797  19.411  1.00 13.28  ? 37  LEU B CG  1 
ATOM   2492  C  CD1 . LEU B  1 37  ? -2.281  -11.018 18.612  1.00 16.81  ? 37  LEU B CD1 1 
ATOM   2493  C  CD2 . LEU B  1 37  ? -2.747  -8.650  18.794  1.00 13.51  ? 37  LEU B CD2 1 
ATOM   2494  N  N   . GLN B  1 38  ? -3.657  -8.815  23.583  1.00 12.54  ? 38  GLN B N   1 
ATOM   2495  C  CA  . GLN B  1 38  ? -4.200  -9.358  24.828  1.00 13.41  ? 38  GLN B CA  1 
ATOM   2496  C  C   . GLN B  1 38  ? -5.667  -9.564  24.663  1.00 12.30  ? 38  GLN B C   1 
ATOM   2497  O  O   . GLN B  1 38  ? -6.408  -8.660  24.267  1.00 12.54  ? 38  GLN B O   1 
ATOM   2498  C  CB  . GLN B  1 38  ? -3.963  -8.363  25.910  1.00 16.88  ? 38  GLN B CB  1 
ATOM   2499  C  CG  . GLN B  1 38  ? -4.358  -8.845  27.305  1.00 23.22  ? 38  GLN B CG  1 
ATOM   2500  C  CD  . GLN B  1 38  ? -3.927  -7.875  28.310  1.00 27.77  ? 38  GLN B CD  1 
ATOM   2501  O  OE1 . GLN B  1 38  ? -2.745  -7.819  28.655  1.00 38.40  ? 38  GLN B OE1 1 
ATOM   2502  N  NE2 . GLN B  1 38  ? -4.829  -7.032  28.720  1.00 32.34  ? 38  GLN B NE2 1 
ATOM   2503  N  N   . TYR B  1 39  ? -6.111  -10.733 25.088  1.00 12.31  ? 39  TYR B N   1 
ATOM   2504  C  CA  . TYR B  1 39  ? -7.509  -11.020 25.070  1.00 10.96  ? 39  TYR B CA  1 
ATOM   2505  C  C   . TYR B  1 39  ? -8.264  -10.100 26.014  1.00 11.10  ? 39  TYR B C   1 
ATOM   2506  O  O   . TYR B  1 39  ? -7.836  -9.886  27.129  1.00 11.98  ? 39  TYR B O   1 
ATOM   2507  C  CB  . TYR B  1 39  ? -7.685  -12.504 25.472  1.00 13.77  ? 39  TYR B CB  1 
ATOM   2508  C  CG  . TYR B  1 39  ? -9.137  -12.899 25.644  1.00 12.49  ? 39  TYR B CG  1 
ATOM   2509  C  CD1 . TYR B  1 39  ? -10.039 -12.847 24.575  1.00 13.61  ? 39  TYR B CD1 1 
ATOM   2510  C  CD2 . TYR B  1 39  ? -9.634  -13.284 26.894  1.00 13.22  ? 39  TYR B CD2 1 
ATOM   2511  C  CE1 . TYR B  1 39  ? -11.365 -13.171 24.702  1.00 14.16  ? 39  TYR B CE1 1 
ATOM   2512  C  CE2 . TYR B  1 39  ? -10.968 -13.589 26.992  1.00 13.86  ? 39  TYR B CE2 1 
ATOM   2513  C  CZ  . TYR B  1 39  ? -11.814 -13.567 25.910  1.00 14.27  ? 39  TYR B CZ  1 
ATOM   2514  O  OH  . TYR B  1 39  ? -13.102 -13.909 26.076  1.00 16.99  ? 39  TYR B OH  1 
ATOM   2515  N  N   . ASP B  1 40  ? -9.413  -9.625  25.574  1.00 10.35  ? 40  ASP B N   1 
ATOM   2516  C  CA  . ASP B  1 40  ? -10.286 -8.796  26.405  1.00 11.91  ? 40  ASP B CA  1 
ATOM   2517  C  C   . ASP B  1 40  ? -11.680 -9.324  26.278  1.00 10.97  ? 40  ASP B C   1 
ATOM   2518  O  O   . ASP B  1 40  ? -12.341 -9.120  25.239  1.00 11.34  ? 40  ASP B O   1 
ATOM   2519  C  CB  . ASP B  1 40  ? -10.189 -7.345  26.019  1.00 12.41  ? 40  ASP B CB  1 
ATOM   2520  C  CG  . ASP B  1 40  ? -11.043 -6.422  26.845  1.00 14.50  ? 40  ASP B CG  1 
ATOM   2521  O  OD1 . ASP B  1 40  ? -11.872 -6.843  27.618  1.00 16.33  ? 40  ASP B OD1 1 
ATOM   2522  O  OD2 . ASP B  1 40  ? -10.877 -5.204  26.615  1.00 22.29  ? 40  ASP B OD2 1 
ATOM   2523  N  N   . ALA B  1 41  ? -12.197 -9.980  27.330  1.00 12.39  ? 41  ALA B N   1 
ATOM   2524  C  CA  . ALA B  1 41  ? -13.537 -10.558 27.252  1.00 13.77  ? 41  ALA B CA  1 
ATOM   2525  C  C   . ALA B  1 41  ? -14.655 -9.535  27.106  1.00 13.10  ? 41  ALA B C   1 
ATOM   2526  O  O   . ALA B  1 41  ? -15.810 -9.935  26.761  1.00 15.64  ? 41  ALA B O   1 
ATOM   2527  C  CB  . ALA B  1 41  ? -13.764 -11.434 28.504  1.00 14.97  ? 41  ALA B CB  1 
ATOM   2528  N  N   A SER B  1 42  ? -14.399 -8.243  27.447  0.50 13.80  ? 42  SER B N   1 
ATOM   2529  N  N   B SER B  1 42  ? -14.360 -8.251  27.400  0.50 13.76  ? 42  SER B N   1 
ATOM   2530  C  CA  A SER B  1 42  ? -15.413 -7.223  27.283  0.50 15.37  ? 42  SER B CA  1 
ATOM   2531  C  CA  B SER B  1 42  ? -15.353 -7.228  27.288  0.50 14.10  ? 42  SER B CA  1 
ATOM   2532  C  C   A SER B  1 42  ? -15.744 -6.933  25.804  0.50 13.35  ? 42  SER B C   1 
ATOM   2533  C  C   B SER B  1 42  ? -15.546 -6.728  25.852  0.50 12.86  ? 42  SER B C   1 
ATOM   2534  O  O   A SER B  1 42  ? -16.796 -6.334  25.485  0.50 15.71  ? 42  SER B O   1 
ATOM   2535  O  O   B SER B  1 42  ? -16.351 -5.833  25.621  0.50 12.31  ? 42  SER B O   1 
ATOM   2536  C  CB  A SER B  1 42  ? -15.032 -5.887  27.984  0.50 20.75  ? 42  SER B CB  1 
ATOM   2537  C  CB  B SER B  1 42  ? -15.020 -6.044  28.188  0.50 17.88  ? 42  SER B CB  1 
ATOM   2538  O  OG  A SER B  1 42  ? -13.971 -5.117  27.408  0.50 19.15  ? 42  SER B OG  1 
ATOM   2539  O  OG  B SER B  1 42  ? -14.962 -6.541  29.481  0.50 19.77  ? 42  SER B OG  1 
ATOM   2540  N  N   . LEU B  1 43  ? -14.839 -7.326  24.902  1.00 12.60  ? 43  LEU B N   1 
ATOM   2541  C  CA  . LEU B  1 43  ? -14.989 -7.001  23.472  1.00 12.77  ? 43  LEU B CA  1 
ATOM   2542  C  C   . LEU B  1 43  ? -16.084 -7.898  22.878  1.00 12.94  ? 43  LEU B C   1 
ATOM   2543  O  O   . LEU B  1 43  ? -15.831 -8.949  22.281  1.00 14.14  ? 43  LEU B O   1 
ATOM   2544  C  CB  . LEU B  1 43  ? -13.705 -7.163  22.765  1.00 11.38  ? 43  LEU B CB  1 
ATOM   2545  C  CG  . LEU B  1 43  ? -12.645 -6.175  23.127  1.00 10.54  ? 43  LEU B CG  1 
ATOM   2546  C  CD1 . LEU B  1 43  ? -11.375 -6.530  22.375  1.00 12.55  ? 43  LEU B CD1 1 
ATOM   2547  C  CD2 . LEU B  1 43  ? -13.043 -4.753  22.887  1.00 13.26  ? 43  LEU B CD2 1 
ATOM   2548  N  N   . THR B  1 44  ? -17.322 -7.482  23.060  1.00 14.36  ? 44  THR B N   1 
ATOM   2549  C  CA  . THR B  1 44  ? -18.486 -8.280  22.664  1.00 15.86  ? 44  THR B CA  1 
ATOM   2550  C  C   . THR B  1 44  ? -18.790 -8.003  21.179  1.00 15.43  ? 44  THR B C   1 
ATOM   2551  O  O   . THR B  1 44  ? -18.226 -7.101  20.545  1.00 14.28  ? 44  THR B O   1 
ATOM   2552  C  CB  . THR B  1 44  ? -19.647 -7.904  23.613  1.00 21.11  ? 44  THR B CB  1 
ATOM   2553  O  OG1 . THR B  1 44  ? -19.708 -6.471  23.663  1.00 24.89  ? 44  THR B OG1 1 
ATOM   2554  C  CG2 . THR B  1 44  ? -19.405 -8.462  25.029  1.00 25.41  ? 44  THR B CG2 1 
ATOM   2555  N  N   . PRO B  1 45  ? -19.695 -8.753  20.547  1.00 16.56  ? 45  PRO B N   1 
ATOM   2556  C  CA  . PRO B  1 45  ? -19.891 -8.622  19.093  1.00 15.05  ? 45  PRO B CA  1 
ATOM   2557  C  C   . PRO B  1 45  ? -20.501 -7.268  18.701  1.00 14.89  ? 45  PRO B C   1 
ATOM   2558  O  O   . PRO B  1 45  ? -21.422 -6.800  19.348  1.00 19.32  ? 45  PRO B O   1 
ATOM   2559  C  CB  . PRO B  1 45  ? -20.843 -9.773  18.738  1.00 19.00  ? 45  PRO B CB  1 
ATOM   2560  C  CG  . PRO B  1 45  ? -20.536 -10.800 19.841  1.00 20.10  ? 45  PRO B CG  1 
ATOM   2561  C  CD  . PRO B  1 45  ? -20.402 -9.920  21.070  1.00 20.98  ? 45  PRO B CD  1 
ATOM   2562  N  N   . LEU B  1 46  ? -20.049 -6.716  17.597  1.00 13.48  ? 46  LEU B N   1 
ATOM   2563  C  CA  . LEU B  1 46  ? -20.726 -5.569  16.997  1.00 13.79  ? 46  LEU B CA  1 
ATOM   2564  C  C   . LEU B  1 46  ? -21.943 -6.006  16.215  1.00 13.25  ? 46  LEU B C   1 
ATOM   2565  O  O   . LEU B  1 46  ? -21.986 -7.121  15.715  1.00 14.62  ? 46  LEU B O   1 
ATOM   2566  C  CB  . LEU B  1 46  ? -19.780 -4.845  16.033  1.00 14.16  ? 46  LEU B CB  1 
ATOM   2567  C  CG  . LEU B  1 46  ? -18.571 -4.207  16.686  1.00 15.95  ? 46  LEU B CG  1 
ATOM   2568  C  CD1 . LEU B  1 46  ? -17.653 -3.633  15.596  1.00 18.35  ? 46  LEU B CD1 1 
ATOM   2569  C  CD2 . LEU B  1 46  ? -18.914 -3.221  17.804  1.00 20.72  ? 46  LEU B CD2 1 
ATOM   2570  N  N   . GLU B  1 47  ? -22.920 -5.116  16.129  1.00 12.93  ? 47  GLU B N   1 
ATOM   2571  C  CA  . GLU B  1 47  ? -24.094 -5.344  15.283  1.00 14.83  ? 47  GLU B CA  1 
ATOM   2572  C  C   . GLU B  1 47  ? -24.105 -4.263  14.197  1.00 12.38  ? 47  GLU B C   1 
ATOM   2573  O  O   . GLU B  1 47  ? -23.830 -3.106  14.457  1.00 14.48  ? 47  GLU B O   1 
ATOM   2574  C  CB  . GLU B  1 47  ? -25.358 -5.244  16.126  1.00 17.47  ? 47  GLU B CB  1 
ATOM   2575  C  CG  . GLU B  1 47  ? -25.436 -6.422  17.154  1.00 20.59  ? 47  GLU B CG  1 
ATOM   2576  C  CD  . GLU B  1 47  ? -26.588 -6.261  18.104  1.00 25.83  ? 47  GLU B CD  1 
ATOM   2577  O  OE1 . GLU B  1 47  ? -26.343 -6.089  19.319  1.00 46.56  ? 47  GLU B OE1 1 
ATOM   2578  O  OE2 . GLU B  1 47  ? -27.729 -6.409  17.693  1.00 43.42  ? 47  GLU B OE2 1 
ATOM   2579  N  N   . PHE B  1 48  ? -24.338 -4.713  12.981  1.00 12.29  ? 48  PHE B N   1 
ATOM   2580  C  CA  . PHE B  1 48  ? -24.272 -3.888  11.758  1.00 11.69  ? 48  PHE B CA  1 
ATOM   2581  C  C   . PHE B  1 48  ? -25.693 -3.581  11.334  1.00 12.07  ? 48  PHE B C   1 
ATOM   2582  O  O   . PHE B  1 48  ? -26.393 -4.491  10.909  1.00 16.67  ? 48  PHE B O   1 
ATOM   2583  C  CB  . PHE B  1 48  ? -23.473 -4.635  10.711  1.00 13.99  ? 48  PHE B CB  1 
ATOM   2584  C  CG  . PHE B  1 48  ? -22.166 -5.106  11.243  1.00 13.45  ? 48  PHE B CG  1 
ATOM   2585  C  CD1 . PHE B  1 48  ? -21.117 -4.233  11.574  1.00 12.80  ? 48  PHE B CD1 1 
ATOM   2586  C  CD2 . PHE B  1 48  ? -21.998 -6.443  11.513  1.00 14.61  ? 48  PHE B CD2 1 
ATOM   2587  C  CE1 . PHE B  1 48  ? -19.914 -4.750  12.155  1.00 13.75  ? 48  PHE B CE1 1 
ATOM   2588  C  CE2 . PHE B  1 48  ? -20.813 -6.936  12.067  1.00 15.89  ? 48  PHE B CE2 1 
ATOM   2589  C  CZ  . PHE B  1 48  ? -19.806 -6.097  12.373  1.00 14.96  ? 48  PHE B CZ  1 
ATOM   2590  N  N   . GLN B  1 49  ? -26.106 -2.328  11.496  1.00 12.37  ? 49  GLN B N   1 
ATOM   2591  C  CA  . GLN B  1 49  ? -27.513 -1.977  11.320  1.00 12.56  ? 49  GLN B CA  1 
ATOM   2592  C  C   . GLN B  1 49  ? -27.643 -1.061  10.111  1.00 11.22  ? 49  GLN B C   1 
ATOM   2593  O  O   . GLN B  1 49  ? -26.821 -0.142  9.905   1.00 11.62  ? 49  GLN B O   1 
ATOM   2594  C  CB  . GLN B  1 49  ? -27.975 -1.164  12.537  1.00 15.02  ? 49  GLN B CB  1 
ATOM   2595  C  CG  . GLN B  1 49  ? -27.831 -1.951  13.843  1.00 16.93  ? 49  GLN B CG  1 
ATOM   2596  C  CD  . GLN B  1 49  ? -28.640 -3.258  13.864  1.00 15.22  ? 49  GLN B CD  1 
ATOM   2597  O  OE1 . GLN B  1 49  ? -28.108 -4.387  13.895  1.00 24.38  ? 49  GLN B OE1 1 
ATOM   2598  N  NE2 . GLN B  1 49  ? -29.919 -3.129  13.735  1.00 22.06  ? 49  GLN B NE2 1 
ATOM   2599  N  N   . GLY B  1 50  ? -28.611 -1.286  9.266   1.00 12.89  ? 50  GLY B N   1 
ATOM   2600  C  CA  . GLY B  1 50  ? -28.805 -0.459  8.100   1.00 13.05  ? 50  GLY B CA  1 
ATOM   2601  C  C   . GLY B  1 50  ? -27.703 -0.629  7.053   1.00 11.56  ? 50  GLY B C   1 
ATOM   2602  O  O   . GLY B  1 50  ? -27.559 0.196   6.207   1.00 12.89  ? 50  GLY B O   1 
ATOM   2603  N  N   . TYR B  1 51  ? -26.984 -1.747  7.102   1.00 10.78  ? 51  TYR B N   1 
ATOM   2604  C  CA  . TYR B  1 51  ? -25.970 -2.075  6.098   1.00 9.83   ? 51  TYR B CA  1 
ATOM   2605  C  C   . TYR B  1 51  ? -26.597 -2.576  4.788   1.00 9.97   ? 51  TYR B C   1 
ATOM   2606  O  O   . TYR B  1 51  ? -25.929 -2.535  3.770   1.00 10.44  ? 51  TYR B O   1 
ATOM   2607  C  CB  . TYR B  1 51  ? -24.964 -3.115  6.592   1.00 9.59   ? 51  TYR B CB  1 
ATOM   2608  C  CG  . TYR B  1 51  ? -23.800 -2.560  7.392   1.00 8.95   ? 51  TYR B CG  1 
ATOM   2609  C  CD1 . TYR B  1 51  ? -23.992 -1.601  8.384   1.00 9.45   ? 51  TYR B CD1 1 
ATOM   2610  C  CD2 . TYR B  1 51  ? -22.511 -3.014  7.163   1.00 8.93   ? 51  TYR B CD2 1 
ATOM   2611  C  CE1 . TYR B  1 51  ? -22.922 -1.108  9.117   1.00 9.63   ? 51  TYR B CE1 1 
ATOM   2612  C  CE2 . TYR B  1 51  ? -21.438 -2.529  7.889   1.00 9.14   ? 51  TYR B CE2 1 
ATOM   2613  C  CZ  . TYR B  1 51  ? -21.646 -1.579  8.862   1.00 9.65   ? 51  TYR B CZ  1 
ATOM   2614  O  OH  . TYR B  1 51  ? -20.564 -1.110  9.571   1.00 10.57  ? 51  TYR B OH  1 
ATOM   2615  N  N   . ASN B  1 52  ? -27.868 -3.065  4.843   1.00 11.19  ? 52  ASN B N   1 
ATOM   2616  C  CA  . ASN B  1 52  ? -28.486 -3.587  3.661   1.00 12.39  ? 52  ASN B CA  1 
ATOM   2617  C  C   . ASN B  1 52  ? -29.116 -2.425  2.887   1.00 12.02  ? 52  ASN B C   1 
ATOM   2618  O  O   . ASN B  1 52  ? -30.262 -2.072  3.044   1.00 16.82  ? 52  ASN B O   1 
ATOM   2619  C  CB  . ASN B  1 52  ? -29.534 -4.643  4.008   1.00 14.65  ? 52  ASN B CB  1 
ATOM   2620  C  CG  . ASN B  1 52  ? -30.050 -5.337  2.794   1.00 17.24  ? 52  ASN B CG  1 
ATOM   2621  O  OD1 . ASN B  1 52  ? -29.592 -5.178  1.676   1.00 26.93  ? 52  ASN B OD1 1 
ATOM   2622  N  ND2 . ASN B  1 52  ? -31.151 -6.070  2.979   1.00 20.26  ? 52  ASN B ND2 1 
ATOM   2623  N  N   . LEU B  1 53  ? -28.292 -1.771  2.071   1.00 11.11  ? 53  LEU B N   1 
ATOM   2624  C  CA  . LEU B  1 53  ? -28.726 -0.515  1.419   1.00 11.42  ? 53  LEU B CA  1 
ATOM   2625  C  C   . LEU B  1 53  ? -29.673 -0.883  0.277   1.00 11.59  ? 53  LEU B C   1 
ATOM   2626  O  O   . LEU B  1 53  ? -29.457 -1.860  -0.465  1.00 13.30  ? 53  LEU B O   1 
ATOM   2627  C  CB  . LEU B  1 53  ? -27.502 0.134   0.790   1.00 11.77  ? 53  LEU B CB  1 
ATOM   2628  C  CG  . LEU B  1 53  ? -26.377 0.505   1.749   1.00 13.07  ? 53  LEU B CG  1 
ATOM   2629  C  CD1 . LEU B  1 53  ? -25.308 1.243   0.972   1.00 15.76  ? 53  LEU B CD1 1 
ATOM   2630  C  CD2 . LEU B  1 53  ? -26.888 1.370   2.892   1.00 17.54  ? 53  LEU B CD2 1 
ATOM   2631  N  N   . SER B  1 54  ? -30.709 -0.083  0.078   1.00 12.43  ? 54  SER B N   1 
ATOM   2632  C  CA  . SER B  1 54  ? -31.705 -0.372  -0.920  1.00 14.84  ? 54  SER B CA  1 
ATOM   2633  C  C   . SER B  1 54  ? -31.080 -0.412  -2.353  1.00 13.47  ? 54  SER B C   1 
ATOM   2634  O  O   . SER B  1 54  ? -30.419 0.572   -2.731  1.00 12.48  ? 54  SER B O   1 
ATOM   2635  C  CB  . SER B  1 54  ? -32.802 0.659   -0.866  1.00 18.44  ? 54  SER B CB  1 
ATOM   2636  O  OG  . SER B  1 54  ? -33.687 0.365   -1.957  1.00 17.60  ? 54  SER B OG  1 
ATOM   2637  N  N   . ALA B  1 55  ? -31.350 -1.494  -3.122  1.00 15.40  ? 55  ALA B N   1 
ATOM   2638  C  CA  . ALA B  1 55  ? -30.836 -1.604  -4.505  1.00 16.50  ? 55  ALA B CA  1 
ATOM   2639  C  C   . ALA B  1 55  ? -31.535 -0.612  -5.392  1.00 13.67  ? 55  ALA B C   1 
ATOM   2640  O  O   . ALA B  1 55  ? -31.122 -0.445  -6.560  1.00 16.55  ? 55  ALA B O   1 
ATOM   2641  C  CB  . ALA B  1 55  ? -31.011 -3.000  -5.072  1.00 23.41  ? 55  ALA B CB  1 
ATOM   2642  N  N   . ASN B  1 56  ? -32.641 -0.014  -4.928  1.00 13.91  ? 56  ASN B N   1 
ATOM   2643  C  CA  . ASN B  1 56  ? -33.328 1.014   -5.717  1.00 14.29  ? 56  ASN B CA  1 
ATOM   2644  C  C   . ASN B  1 56  ? -32.777 2.385   -5.472  1.00 12.24  ? 56  ASN B C   1 
ATOM   2645  O  O   . ASN B  1 56  ? -33.185 3.330   -6.173  1.00 17.04  ? 56  ASN B O   1 
ATOM   2646  C  CB  . ASN B  1 56  ? -34.806 0.952   -5.458  1.00 16.19  ? 56  ASN B CB  1 
ATOM   2647  C  CG  . ASN B  1 56  ? -35.420 -0.388  -5.784  1.00 22.19  ? 56  ASN B CG  1 
ATOM   2648  O  OD1 . ASN B  1 56  ? -34.949 -1.129  -6.652  1.00 22.47  ? 56  ASN B OD1 1 
ATOM   2649  N  ND2 . ASN B  1 56  ? -36.344 -0.776  -4.950  1.00 26.11  ? 56  ASN B ND2 1 
ATOM   2650  N  N   . LYS B  1 57  ? -31.853 2.525   -4.522  1.00 12.59  ? 57  LYS B N   1 
ATOM   2651  C  CA  . LYS B  1 57  ? -31.153 3.793   -4.285  1.00 12.49  ? 57  LYS B CA  1 
ATOM   2652  C  C   . LYS B  1 57  ? -29.742 3.684   -4.859  1.00 11.78  ? 57  LYS B C   1 
ATOM   2653  O  O   . LYS B  1 57  ? -29.287 2.604   -5.185  1.00 12.26  ? 57  LYS B O   1 
ATOM   2654  C  CB  . LYS B  1 57  ? -31.116 4.068   -2.778  1.00 14.64  ? 57  LYS B CB  1 
ATOM   2655  C  CG  . LYS B  1 57  ? -32.495 4.330   -2.195  1.00 20.29  ? 57  LYS B CG  1 
ATOM   2656  C  CD  . LYS B  1 57  ? -32.417 4.709   -0.732  1.00 29.69  ? 57  LYS B CD  1 
ATOM   2657  C  CE  . LYS B  1 57  ? -32.972 6.085   -0.518  1.00 45.21  ? 57  LYS B CE  1 
ATOM   2658  N  NZ  . LYS B  1 57  ? -33.194 6.149   0.952   1.00 35.80  ? 57  LYS B NZ  1 
ATOM   2659  N  N   . GLN B  1 58  ? -29.097 4.834   -4.942  1.00 12.86  ? 58  GLN B N   1 
ATOM   2660  C  CA  . GLN B  1 58  ? -27.732 4.834   -5.457  1.00 13.12  ? 58  GLN B CA  1 
ATOM   2661  C  C   . GLN B  1 58  ? -26.858 5.646   -4.535  1.00 12.19  ? 58  GLN B C   1 
ATOM   2662  O  O   . GLN B  1 58  ? -27.334 6.549   -3.845  1.00 13.41  ? 58  GLN B O   1 
ATOM   2663  C  CB  . GLN B  1 58  ? -27.604 5.207   -6.909  1.00 17.20  ? 58  GLN B CB  1 
ATOM   2664  C  CG  . GLN B  1 58  ? -28.404 6.448   -7.254  1.00 21.72  ? 58  GLN B CG  1 
ATOM   2665  C  CD  . GLN B  1 58  ? -28.585 6.597   -8.741  1.00 26.09  ? 58  GLN B CD  1 
ATOM   2666  O  OE1 . GLN B  1 58  ? -28.246 5.697   -9.506  1.00 25.16  ? 58  GLN B OE1 1 
ATOM   2667  N  NE2 . GLN B  1 58  ? -29.123 7.738   -9.167  1.00 27.96  ? 58  GLN B NE2 1 
ATOM   2668  N  N   . PHE B  1 59  ? -25.582 5.332   -4.543  1.00 11.39  ? 59  PHE B N   1 
ATOM   2669  C  CA  . PHE B  1 59  ? -24.621 5.902   -3.568  1.00 10.13  ? 59  PHE B CA  1 
ATOM   2670  C  C   . PHE B  1 59  ? -23.408 6.361   -4.346  1.00 9.86   ? 59  PHE B C   1 
ATOM   2671  O  O   . PHE B  1 59  ? -22.976 5.752   -5.332  1.00 10.77  ? 59  PHE B O   1 
ATOM   2672  C  CB  . PHE B  1 59  ? -24.249 4.773   -2.572  1.00 10.94  ? 59  PHE B CB  1 
ATOM   2673  C  CG  . PHE B  1 59  ? -25.501 4.414   -1.788  1.00 10.31  ? 59  PHE B CG  1 
ATOM   2674  C  CD1 . PHE B  1 59  ? -26.380 3.431   -2.245  1.00 10.85  ? 59  PHE B CD1 1 
ATOM   2675  C  CD2 . PHE B  1 59  ? -25.815 5.155   -0.627  1.00 11.46  ? 59  PHE B CD2 1 
ATOM   2676  C  CE1 . PHE B  1 59  ? -27.590 3.238   -1.586  1.00 12.40  ? 59  PHE B CE1 1 
ATOM   2677  C  CE2 . PHE B  1 59  ? -27.048 4.930   0.044   1.00 12.46  ? 59  PHE B CE2 1 
ATOM   2678  C  CZ  . PHE B  1 59  ? -27.901 3.955   -0.453  1.00 13.72  ? 59  PHE B CZ  1 
ATOM   2679  N  N   . LEU B  1 60  ? -22.894 7.507   -3.958  1.00 10.61  ? 60  LEU B N   1 
ATOM   2680  C  CA  . LEU B  1 60  ? -21.876 8.147   -4.754  1.00 10.85  ? 60  LEU B CA  1 
ATOM   2681  C  C   . LEU B  1 60  ? -20.489 7.598   -4.531  1.00 9.69   ? 60  LEU B C   1 
ATOM   2682  O  O   . LEU B  1 60  ? -19.996 7.582   -3.393  1.00 11.57  ? 60  LEU B O   1 
ATOM   2683  C  CB  . LEU B  1 60  ? -21.858 9.640   -4.351  1.00 13.78  ? 60  LEU B CB  1 
ATOM   2684  C  CG  . LEU B  1 60  ? -21.073 10.524  -5.246  1.00 17.65  ? 60  LEU B CG  1 
ATOM   2685  C  CD1 . LEU B  1 60  ? -21.817 10.650  -6.592  1.00 21.68  ? 60  LEU B CD1 1 
ATOM   2686  C  CD2 . LEU B  1 60  ? -20.848 11.886  -4.554  1.00 23.53  ? 60  LEU B CD2 1 
ATOM   2687  N  N   . LEU B  1 61  ? -19.862 7.181   -5.613  1.00 10.88  ? 61  LEU B N   1 
ATOM   2688  C  CA  . LEU B  1 61  ? -18.528 6.695   -5.665  1.00 10.87  ? 61  LEU B CA  1 
ATOM   2689  C  C   . LEU B  1 61  ? -17.631 7.866   -6.175  1.00 11.73  ? 61  LEU B C   1 
ATOM   2690  O  O   . LEU B  1 61  ? -17.997 8.446   -7.201  1.00 14.33  ? 61  LEU B O   1 
ATOM   2691  C  CB  . LEU B  1 61  ? -18.457 5.456   -6.591  1.00 12.93  ? 61  LEU B CB  1 
ATOM   2692  C  CG  . LEU B  1 61  ? -17.144 4.730   -6.598  1.00 12.57  ? 61  LEU B CG  1 
ATOM   2693  C  CD1 . LEU B  1 61  ? -16.967 3.915   -5.329  1.00 15.03  ? 61  LEU B CD1 1 
ATOM   2694  C  CD2 . LEU B  1 61  ? -17.152 3.786   -7.760  1.00 15.58  ? 61  LEU B CD2 1 
ATOM   2695  N  N   . THR B  1 62  ? -16.514 8.170   -5.514  1.00 12.53  ? 62  THR B N   1 
ATOM   2696  C  CA  . THR B  1 62  ? -15.689 9.324   -5.909  1.00 15.22  ? 62  THR B CA  1 
ATOM   2697  C  C   . THR B  1 62  ? -14.229 8.949   -5.841  1.00 14.67  ? 62  THR B C   1 
ATOM   2698  O  O   . THR B  1 62  ? -13.810 8.298   -4.912  1.00 18.53  ? 62  THR B O   1 
ATOM   2699  C  CB  . THR B  1 62  ? -15.813 10.410  -4.905  1.00 25.07  ? 62  THR B CB  1 
ATOM   2700  O  OG1 . THR B  1 62  ? -17.165 10.796  -4.884  1.00 21.97  ? 62  THR B OG1 1 
ATOM   2701  C  CG2 . THR B  1 62  ? -15.001 11.571  -5.363  1.00 29.04  ? 62  THR B CG2 1 
ATOM   2702  N  N   . ASN B  1 63  ? -13.438 9.338   -6.832  1.00 17.53  ? 63  ASN B N   1 
ATOM   2703  C  CA  . ASN B  1 63  ? -12.017 9.105   -6.837  1.00 15.65  ? 63  ASN B CA  1 
ATOM   2704  C  C   . ASN B  1 63  ? -11.496 10.340  -6.195  1.00 15.65  ? 63  ASN B C   1 
ATOM   2705  O  O   . ASN B  1 63  ? -11.664 11.423  -6.711  1.00 15.29  ? 63  ASN B O   1 
ATOM   2706  C  CB  . ASN B  1 63  ? -11.490 9.048   -8.262  1.00 16.00  ? 63  ASN B CB  1 
ATOM   2707  C  CG  . ASN B  1 63  ? -9.974  9.052   -8.324  1.00 14.65  ? 63  ASN B CG  1 
ATOM   2708  O  OD1 . ASN B  1 63  ? -9.295  9.637   -7.476  1.00 16.08  ? 63  ASN B OD1 1 
ATOM   2709  N  ND2 . ASN B  1 63  ? -9.433  8.395   -9.340  1.00 17.59  ? 63  ASN B ND2 1 
ATOM   2710  N  N   . ASN B  1 64  ? -10.882 10.217  -5.046  1.00 16.27  ? 64  ASN B N   1 
ATOM   2711  C  CA  . ASN B  1 64  ? -10.458 11.477  -4.371  1.00 17.48  ? 64  ASN B CA  1 
ATOM   2712  C  C   . ASN B  1 64  ? -8.948  11.713  -4.492  1.00 13.20  ? 64  ASN B C   1 
ATOM   2713  O  O   . ASN B  1 64  ? -8.414  12.576  -3.770  1.00 14.88  ? 64  ASN B O   1 
ATOM   2714  C  CB  . ASN B  1 64  ? -10.765 11.403  -2.819  1.00 16.17  ? 64  ASN B CB  1 
ATOM   2715  C  CG  . ASN B  1 64  ? -9.982  10.296  -2.089  1.00 14.80  ? 64  ASN B CG  1 
ATOM   2716  O  OD1 . ASN B  1 64  ? -9.023  9.684   -2.598  1.00 13.71  ? 64  ASN B OD1 1 
ATOM   2717  N  ND2 . ASN B  1 64  ? -10.339 10.053  -0.853  1.00 21.51  ? 64  ASN B ND2 1 
ATOM   2718  N  N   . GLY B  1 65  ? -8.287  11.144  -5.477  1.00 16.39  ? 65  GLY B N   1 
ATOM   2719  C  CA  . GLY B  1 65  ? -6.858  11.354  -5.638  1.00 15.59  ? 65  GLY B CA  1 
ATOM   2720  C  C   . GLY B  1 65  ? -5.972  10.402  -4.855  1.00 14.30  ? 65  GLY B C   1 
ATOM   2721  O  O   . GLY B  1 65  ? -4.814  10.403  -5.157  1.00 16.00  ? 65  GLY B O   1 
ATOM   2722  N  N   . HIS B  1 66  ? -6.506  9.693   -3.843  1.00 14.54  ? 66  HIS B N   1 
ATOM   2723  C  CA  . HIS B  1 66  ? -5.752  8.812   -2.927  1.00 14.68  ? 66  HIS B CA  1 
ATOM   2724  C  C   . HIS B  1 66  ? -6.237  7.432   -2.794  1.00 12.63  ? 66  HIS B C   1 
ATOM   2725  O  O   . HIS B  1 66  ? -5.455  6.455   -2.511  1.00 13.00  ? 66  HIS B O   1 
ATOM   2726  C  CB  . HIS B  1 66  ? -5.672  9.450   -1.568  1.00 16.07  ? 66  HIS B CB  1 
ATOM   2727  C  CG  . HIS B  1 66  ? -5.142  10.861  -1.572  1.00 14.94  ? 66  HIS B CG  1 
ATOM   2728  N  ND1 . HIS B  1 66  ? -3.809  11.179  -1.862  1.00 17.90  ? 66  HIS B ND1 1 
ATOM   2729  C  CD2 . HIS B  1 66  ? -5.741  11.997  -1.409  1.00 15.99  ? 66  HIS B CD2 1 
ATOM   2730  C  CE1 . HIS B  1 66  ? -3.663  12.462  -1.817  1.00 13.74  ? 66  HIS B CE1 1 
ATOM   2731  N  NE2 . HIS B  1 66  ? -4.896  12.992  -1.538  1.00 18.57  ? 66  HIS B NE2 1 
ATOM   2732  N  N   A SER B  1 67  ? -7.550  7.241   -3.016  0.50 12.09  ? 67  SER B N   1 
ATOM   2733  N  N   B SER B  1 67  ? -7.558  7.247   -2.978  0.50 12.10  ? 67  SER B N   1 
ATOM   2734  C  CA  A SER B  1 67  ? -8.286  5.959   -2.975  0.50 12.73  ? 67  SER B CA  1 
ATOM   2735  C  CA  B SER B  1 67  ? -8.264  5.935   -2.865  0.50 12.81  ? 67  SER B CA  1 
ATOM   2736  C  C   A SER B  1 67  ? -9.565  6.148   -3.837  0.50 12.48  ? 67  SER B C   1 
ATOM   2737  C  C   B SER B  1 67  ? -9.545  6.150   -3.731  0.50 12.81  ? 67  SER B C   1 
ATOM   2738  O  O   A SER B  1 67  ? -9.768  7.179   -4.507  0.50 12.40  ? 67  SER B O   1 
ATOM   2739  O  O   B SER B  1 67  ? -9.785  7.201   -4.327  0.50 13.63  ? 67  SER B O   1 
ATOM   2740  C  CB  A SER B  1 67  ? -8.596  5.611   -1.582  0.50 12.15  ? 67  SER B CB  1 
ATOM   2741  C  CB  B SER B  1 67  ? -8.637  5.570   -1.408  0.50 13.91  ? 67  SER B CB  1 
ATOM   2742  O  OG  A SER B  1 67  ? -9.206  4.303   -1.468  0.50 6.38   ? 67  SER B OG  1 
ATOM   2743  O  OG  B SER B  1 67  ? -7.752  4.862   -0.422  0.50 12.48  ? 67  SER B OG  1 
ATOM   2744  N  N   A VAL B  1 68  ? -10.415 5.127   -3.793  0.50 12.29  ? 68  VAL B N   1 
ATOM   2745  N  N   B VAL B  1 68  ? -10.273 5.062   -3.821  0.50 12.48  ? 68  VAL B N   1 
ATOM   2746  C  CA  A VAL B  1 68  ? -11.764 5.308   -4.281  0.50 15.50  ? 68  VAL B CA  1 
ATOM   2747  C  CA  B VAL B  1 68  ? -11.644 5.141   -4.267  0.50 13.91  ? 68  VAL B CA  1 
ATOM   2748  C  C   A VAL B  1 68  ? -12.669 5.314   -3.096  0.50 16.01  ? 68  VAL B C   1 
ATOM   2749  C  C   B VAL B  1 68  ? -12.596 5.214   -3.092  0.50 14.94  ? 68  VAL B C   1 
ATOM   2750  O  O   A VAL B  1 68  ? -12.507 4.425   -2.383  0.50 15.02  ? 68  VAL B O   1 
ATOM   2751  O  O   B VAL B  1 68  ? -12.397 4.259   -2.369  0.50 14.51  ? 68  VAL B O   1 
ATOM   2752  C  CB  A VAL B  1 68  ? -12.048 4.276   -5.426  0.50 15.47  ? 68  VAL B CB  1 
ATOM   2753  C  CB  B VAL B  1 68  ? -11.908 4.106   -5.421  0.50 15.89  ? 68  VAL B CB  1 
ATOM   2754  C  CG1 A VAL B  1 68  ? -11.715 2.782   -5.032  0.50 16.31  ? 68  VAL B CG1 1 
ATOM   2755  C  CG1 B VAL B  1 68  ? -11.754 2.604   -4.981  0.50 15.04  ? 68  VAL B CG1 1 
ATOM   2756  C  CG2 A VAL B  1 68  ? -13.425 4.522   -5.963  0.50 19.23  ? 68  VAL B CG2 1 
ATOM   2757  C  CG2 B VAL B  1 68  ? -13.187 4.554   -6.099  0.50 19.23  ? 68  VAL B CG2 1 
ATOM   2758  N  N   . LYS B  1 69  ? -13.619 6.251   -2.903  1.00 14.45  ? 69  LYS B N   1 
ATOM   2759  C  CA  . LYS B  1 69  ? -14.535 6.064   -1.752  1.00 10.17  ? 69  LYS B CA  1 
ATOM   2760  C  C   . LYS B  1 69  ? -15.965 5.998   -2.197  1.00 9.53   ? 69  LYS B C   1 
ATOM   2761  O  O   . LYS B  1 69  ? -16.391 6.659   -3.131  1.00 12.74  ? 69  LYS B O   1 
ATOM   2762  C  CB  . LYS B  1 69  ? -14.339 7.133   -0.692  1.00 14.05  ? 69  LYS B CB  1 
ATOM   2763  C  CG  . LYS B  1 69  ? -14.777 8.507   -1.105  1.00 18.98  ? 69  LYS B CG  1 
ATOM   2764  C  CD  . LYS B  1 69  ? -14.713 9.454   0.077   1.00 21.81  ? 69  LYS B CD  1 
ATOM   2765  C  CE  . LYS B  1 69  ? -14.907 10.777  -0.625  1.00 26.12  ? 69  LYS B CE  1 
ATOM   2766  N  NZ  . LYS B  1 69  ? -14.827 11.832  0.383   1.00 27.61  ? 69  LYS B NZ  1 
ATOM   2767  N  N   . LEU B  1 70  ? -16.726 5.209   -1.453  1.00 8.06   ? 70  LEU B N   1 
ATOM   2768  C  CA  . LEU B  1 70  ? -18.174 5.100   -1.646  1.00 7.66   ? 70  LEU B CA  1 
ATOM   2769  C  C   . LEU B  1 70  ? -18.802 5.818   -0.465  1.00 8.01   ? 70  LEU B C   1 
ATOM   2770  O  O   . LEU B  1 70  ? -18.578 5.413   0.684   1.00 7.78   ? 70  LEU B O   1 
ATOM   2771  C  CB  . LEU B  1 70  ? -18.595 3.635   -1.669  1.00 8.74   ? 70  LEU B CB  1 
ATOM   2772  C  CG  . LEU B  1 70  ? -20.100 3.375   -1.867  1.00 8.77   ? 70  LEU B CG  1 
ATOM   2773  C  CD1 . LEU B  1 70  ? -20.536 3.873   -3.229  1.00 11.46  ? 70  LEU B CD1 1 
ATOM   2774  C  CD2 . LEU B  1 70  ? -20.415 1.916   -1.667  1.00 11.45  ? 70  LEU B CD2 1 
ATOM   2775  N  N   . ASN B  1 71  ? -19.647 6.800   -0.727  1.00 8.23   ? 71  ASN B N   1 
ATOM   2776  C  CA  . ASN B  1 71  ? -20.382 7.481   0.367   1.00 9.75   ? 71  ASN B CA  1 
ATOM   2777  C  C   . ASN B  1 71  ? -21.466 6.526   0.901   1.00 9.67   ? 71  ASN B C   1 
ATOM   2778  O  O   . ASN B  1 71  ? -22.102 5.809   0.150   1.00 12.06  ? 71  ASN B O   1 
ATOM   2779  C  CB  . ASN B  1 71  ? -21.028 8.742   -0.183  1.00 12.28  ? 71  ASN B CB  1 
ATOM   2780  C  CG  . ASN B  1 71  ? -20.041 9.853   -0.349  1.00 14.31  ? 71  ASN B CG  1 
ATOM   2781  O  OD1 . ASN B  1 71  ? -18.856 9.736   -0.061  1.00 18.22  ? 71  ASN B OD1 1 
ATOM   2782  N  ND2 . ASN B  1 71  ? -20.568 11.047  -0.764  1.00 22.67  ? 71  ASN B ND2 1 
ATOM   2783  N  N   . LEU B  1 72  ? -21.650 6.619   2.190   1.00 9.40   ? 72  LEU B N   1 
ATOM   2784  C  CA  . LEU B  1 72  ? -22.606 5.741   2.898   1.00 8.97   ? 72  LEU B CA  1 
ATOM   2785  C  C   . LEU B  1 72  ? -23.596 6.625   3.674   1.00 9.33   ? 72  LEU B C   1 
ATOM   2786  O  O   . LEU B  1 72  ? -23.235 7.739   4.096   1.00 11.18  ? 72  LEU B O   1 
ATOM   2787  C  CB  . LEU B  1 72  ? -21.878 4.818   3.864   1.00 9.25   ? 72  LEU B CB  1 
ATOM   2788  C  CG  . LEU B  1 72  ? -20.940 3.841   3.152   1.00 8.48   ? 72  LEU B CG  1 
ATOM   2789  C  CD1 . LEU B  1 72  ? -20.036 3.173   4.152   1.00 8.88   ? 72  LEU B CD1 1 
ATOM   2790  C  CD2 . LEU B  1 72  ? -21.682 2.844   2.270   1.00 9.72   ? 72  LEU B CD2 1 
ATOM   2791  N  N   . PRO B  1 73  ? -24.824 6.144   3.857   1.00 9.87   ? 73  PRO B N   1 
ATOM   2792  C  CA  . PRO B  1 73  ? -25.859 6.954   4.490   1.00 10.90  ? 73  PRO B CA  1 
ATOM   2793  C  C   . PRO B  1 73  ? -25.728 6.872   6.000   1.00 11.95  ? 73  PRO B C   1 
ATOM   2794  O  O   . PRO B  1 73  ? -25.299 5.878   6.596   1.00 13.05  ? 73  PRO B O   1 
ATOM   2795  C  CB  . PRO B  1 73  ? -27.164 6.324   3.961   1.00 12.39  ? 73  PRO B CB  1 
ATOM   2796  C  CG  . PRO B  1 73  ? -26.784 4.844   3.905   1.00 11.61  ? 73  PRO B CG  1 
ATOM   2797  C  CD  . PRO B  1 73  ? -25.359 4.859   3.396   1.00 10.96  ? 73  PRO B CD  1 
ATOM   2798  N  N   . SER B  1 74  ? -26.102 7.934   6.645   1.00 15.40  ? 74  SER B N   1 
ATOM   2799  C  CA  . SER B  1 74  ? -25.918 7.996   8.120   1.00 15.08  ? 74  SER B CA  1 
ATOM   2800  C  C   . SER B  1 74  ? -26.908 7.102   8.876   1.00 14.08  ? 74  SER B C   1 
ATOM   2801  O  O   . SER B  1 74  ? -26.658 6.874   10.080  1.00 16.56  ? 74  SER B O   1 
ATOM   2802  C  CB  . SER B  1 74  ? -26.006 9.413   8.619   1.00 19.58  ? 74  SER B CB  1 
ATOM   2803  O  OG  . SER B  1 74  ? -27.302 9.963   8.308   1.00 23.12  ? 74  SER B OG  1 
ATOM   2804  N  N   . ASP B  1 75  ? -27.937 6.563   8.234   1.00 14.73  ? 75  ASP B N   1 
ATOM   2805  C  CA  . ASP B  1 75  ? -28.811 5.626   8.945   1.00 15.83  ? 75  ASP B CA  1 
ATOM   2806  C  C   . ASP B  1 75  ? -28.038 4.272   9.108   1.00 14.13  ? 75  ASP B C   1 
ATOM   2807  O  O   . ASP B  1 75  ? -28.428 3.478   9.952   1.00 17.26  ? 75  ASP B O   1 
ATOM   2808  C  CB  . ASP B  1 75  ? -30.213 5.407   8.319   1.00 18.12  ? 75  ASP B CB  1 
ATOM   2809  C  CG  . ASP B  1 75  ? -30.215 5.305   6.787   1.00 32.37  ? 75  ASP B CG  1 
ATOM   2810  O  OD1 . ASP B  1 75  ? -29.209 4.899   6.169   1.00 34.48  ? 75  ASP B OD1 1 
ATOM   2811  O  OD2 . ASP B  1 75  ? -31.277 5.617   6.201   1.00 56.15  ? 75  ASP B OD2 1 
ATOM   2812  N  N   . MET B  1 76  ? -26.990 4.034   8.332   1.00 11.90  ? 76  MET B N   1 
ATOM   2813  C  CA  . MET B  1 76  ? -26.174 2.855   8.509   1.00 11.00  ? 76  MET B CA  1 
ATOM   2814  C  C   . MET B  1 76  ? -25.259 3.057   9.722   1.00 10.48  ? 76  MET B C   1 
ATOM   2815  O  O   . MET B  1 76  ? -24.623 4.106   9.870   1.00 11.58  ? 76  MET B O   1 
ATOM   2816  C  CB  . MET B  1 76  ? -25.425 2.646   7.212   1.00 11.33  ? 76  MET B CB  1 
ATOM   2817  C  CG  . MET B  1 76  ? -24.374 1.590   7.308   1.00 11.81  ? 76  MET B CG  1 
ATOM   2818  S  SD  . MET B  1 76  ? -23.613 1.467   5.628   1.00 11.67  ? 76  MET B SD  1 
ATOM   2819  C  CE  . MET B  1 76  ? -22.161 0.533   6.086   1.00 10.28  ? 76  MET B CE  1 
ATOM   2820  N  N   . HIS B  1 77  ? -25.239 2.105   10.663  1.00 10.90  ? 77  HIS B N   1 
ATOM   2821  C  CA  . HIS B  1 77  ? -24.473 2.324   11.888  1.00 11.40  ? 77  HIS B CA  1 
ATOM   2822  C  C   . HIS B  1 77  ? -24.031 1.049   12.535  1.00 10.12  ? 77  HIS B C   1 
ATOM   2823  O  O   . HIS B  1 77  ? -24.547 -0.020  12.220  1.00 11.80  ? 77  HIS B O   1 
ATOM   2824  C  CB  . HIS B  1 77  ? -25.235 3.263   12.864  1.00 14.03  ? 77  HIS B CB  1 
ATOM   2825  C  CG  . HIS B  1 77  ? -26.471 2.703   13.382  1.00 15.72  ? 77  HIS B CG  1 
ATOM   2826  N  ND1 . HIS B  1 77  ? -27.657 2.683   12.720  1.00 20.29  ? 77  HIS B ND1 1 
ATOM   2827  C  CD2 . HIS B  1 77  ? -26.700 2.067   14.582  1.00 16.43  ? 77  HIS B CD2 1 
ATOM   2828  C  CE1 . HIS B  1 77  ? -28.612 2.132   13.518  1.00 20.23  ? 77  HIS B CE1 1 
ATOM   2829  N  NE2 . HIS B  1 77  ? -28.025 1.735   14.636  1.00 21.20  ? 77  HIS B NE2 1 
ATOM   2830  N  N   . ILE B  1 78  ? -23.081 1.232   13.436  1.00 11.79  ? 78  ILE B N   1 
ATOM   2831  C  CA  . ILE B  1 78  ? -22.663 0.131   14.310  1.00 12.03  ? 78  ILE B CA  1 
ATOM   2832  C  C   . ILE B  1 78  ? -23.330 0.315   15.636  1.00 11.91  ? 78  ILE B C   1 
ATOM   2833  O  O   . ILE B  1 78  ? -23.314 1.429   16.178  1.00 14.05  ? 78  ILE B O   1 
ATOM   2834  C  CB  . ILE B  1 78  ? -21.080 0.206   14.496  1.00 14.39  ? 78  ILE B CB  1 
ATOM   2835  C  CG1 . ILE B  1 78  ? -20.255 -0.103  13.239  1.00 18.12  ? 78  ILE B CG1 1 
ATOM   2836  C  CG2 . ILE B  1 78  ? -20.693 -0.766  15.587  1.00 17.79  ? 78  ILE B CG2 1 
ATOM   2837  C  CD1 . ILE B  1 78  ? -18.851 0.533   13.463  1.00 16.03  ? 78  ILE B CD1 1 
ATOM   2838  N  N   . GLN B  1 79  ? -23.770 -0.830  16.166  1.00 12.81  ? 79  GLN B N   1 
ATOM   2839  C  CA  . GLN B  1 79  ? -24.324 -0.885  17.537  1.00 15.50  ? 79  GLN B CA  1 
ATOM   2840  C  C   . GLN B  1 79  ? -23.329 -1.746  18.291  1.00 16.01  ? 79  GLN B C   1 
ATOM   2841  O  O   . GLN B  1 79  ? -22.876 -2.808  17.808  1.00 16.98  ? 79  GLN B O   1 
ATOM   2842  C  CB  . GLN B  1 79  ? -25.756 -1.510  17.499  1.00 19.54  ? 79  GLN B CB  1 
ATOM   2843  C  CG  . GLN B  1 79  ? -26.336 -2.078  18.788  1.00 28.10  ? 79  GLN B CG  1 
ATOM   2844  C  CD  . GLN B  1 79  ? -27.180 -1.063  19.466  1.00 41.31  ? 79  GLN B CD  1 
ATOM   2845  O  OE1 . GLN B  1 79  ? -27.897 -0.301  18.818  1.00 51.48  ? 79  GLN B OE1 1 
ATOM   2846  N  NE2 . GLN B  1 79  ? -27.101 -1.025  20.805  1.00 58.19  ? 79  GLN B NE2 1 
ATOM   2847  N  N   . GLY B  1 80  ? -22.991 -1.353  19.529  1.00 16.42  ? 80  GLY B N   1 
ATOM   2848  C  CA  . GLY B  1 80  ? -22.132 -2.154  20.397  1.00 18.81  ? 80  GLY B CA  1 
ATOM   2849  C  C   . GLY B  1 80  ? -21.017 -1.358  20.974  1.00 17.40  ? 80  GLY B C   1 
ATOM   2850  O  O   . GLY B  1 80  ? -20.481 -1.800  22.001  1.00 21.22  ? 80  GLY B O   1 
ATOM   2851  N  N   . LEU B  1 81  ? -20.665 -0.198  20.413  1.00 15.46  ? 81  LEU B N   1 
ATOM   2852  C  CA  . LEU B  1 81  ? -19.608 0.669   20.950  1.00 16.51  ? 81  LEU B CA  1 
ATOM   2853  C  C   . LEU B  1 81  ? -20.208 1.593   22.006  1.00 18.60  ? 81  LEU B C   1 
ATOM   2854  O  O   . LEU B  1 81  ? -21.416 1.547   22.279  1.00 18.18  ? 81  LEU B O   1 
ATOM   2855  C  CB  . LEU B  1 81  ? -18.923 1.459   19.825  1.00 18.59  ? 81  LEU B CB  1 
ATOM   2856  C  CG  . LEU B  1 81  ? -18.176 0.560   18.845  1.00 17.87  ? 81  LEU B CG  1 
ATOM   2857  C  CD1 . LEU B  1 81  ? -17.662 1.429   17.696  1.00 18.25  ? 81  LEU B CD1 1 
ATOM   2858  C  CD2 . LEU B  1 81  ? -16.971 -0.101  19.527  1.00 21.23  ? 81  LEU B CD2 1 
ATOM   2859  N  N   . GLN B  1 82  ? -19.411 2.496   22.583  1.00 20.09  ? 82  GLN B N   1 
ATOM   2860  C  CA  . GLN B  1 82  ? -19.944 3.292   23.664  1.00 22.94  ? 82  GLN B CA  1 
ATOM   2861  C  C   . GLN B  1 82  ? -20.826 4.492   23.278  1.00 23.81  ? 82  GLN B C   1 
ATOM   2862  O  O   . GLN B  1 82  ? -21.440 5.089   24.132  1.00 27.53  ? 82  GLN B O   1 
ATOM   2863  C  CB  . GLN B  1 82  ? -18.816 3.692   24.596  1.00 31.35  ? 82  GLN B CB  1 
ATOM   2864  C  CG  . GLN B  1 82  ? -18.482 2.540   25.595  1.00 48.76  ? 82  GLN B CG  1 
ATOM   2865  C  CD  . GLN B  1 82  ? -17.534 2.936   26.712  1.00 54.15  ? 82  GLN B CD  1 
ATOM   2866  O  OE1 . GLN B  1 82  ? -17.883 2.793   27.924  1.00 118.72 ? 82  GLN B OE1 1 
ATOM   2867  N  NE2 . GLN B  1 82  ? -16.314 3.368   26.319  1.00 53.76  ? 82  GLN B NE2 1 
ATOM   2868  N  N   . SER B  1 83  ? -20.834 4.811   21.969  1.00 20.03  ? 83  SER B N   1 
ATOM   2869  C  CA  . SER B  1 83  ? -21.787 5.700   21.323  1.00 16.27  ? 83  SER B CA  1 
ATOM   2870  C  C   . SER B  1 83  ? -22.217 4.992   20.039  1.00 15.68  ? 83  SER B C   1 
ATOM   2871  O  O   . SER B  1 83  ? -21.545 4.009   19.597  1.00 15.46  ? 83  SER B O   1 
ATOM   2872  C  CB  . SER B  1 83  ? -21.131 7.032   21.020  1.00 20.92  ? 83  SER B CB  1 
ATOM   2873  O  OG  . SER B  1 83  ? -20.739 7.641   22.216  1.00 24.14  ? 83  SER B OG  1 
ATOM   2874  N  N   A ARG B  1 84  ? -23.310 5.476   19.444  0.50 14.69  ? 84  ARG B N   1 
ATOM   2875  N  N   B ARG B  1 84  ? -23.299 5.479   19.438  0.50 14.79  ? 84  ARG B N   1 
ATOM   2876  C  CA  A ARG B  1 84  ? -23.611 5.133   18.079  0.50 15.06  ? 84  ARG B CA  1 
ATOM   2877  C  CA  B ARG B  1 84  ? -23.600 5.095   18.092  0.50 15.25  ? 84  ARG B CA  1 
ATOM   2878  C  C   A ARG B  1 84  ? -22.578 5.738   17.117  0.50 11.90  ? 84  ARG B C   1 
ATOM   2879  C  C   B ARG B  1 84  ? -22.571 5.711   17.138  0.50 11.98  ? 84  ARG B C   1 
ATOM   2880  O  O   A ARG B  1 84  ? -22.280 6.964   17.153  0.50 13.75  ? 84  ARG B O   1 
ATOM   2881  O  O   B ARG B  1 84  ? -22.278 6.915   17.193  0.50 14.00  ? 84  ARG B O   1 
ATOM   2882  C  CB  A ARG B  1 84  ? -25.008 5.625   17.683  0.50 17.18  ? 84  ARG B CB  1 
ATOM   2883  C  CB  B ARG B  1 84  ? -24.993 5.582   17.688  0.50 17.45  ? 84  ARG B CB  1 
ATOM   2884  C  CG  A ARG B  1 84  ? -25.260 5.417   16.202  0.50 15.55  ? 84  ARG B CG  1 
ATOM   2885  C  CG  B ARG B  1 84  ? -25.199 5.406   16.198  0.50 15.78  ? 84  ARG B CG  1 
ATOM   2886  C  CD  A ARG B  1 84  ? -26.727 5.676   15.847  0.50 16.22  ? 84  ARG B CD  1 
ATOM   2887  C  CD  B ARG B  1 84  ? -26.596 5.815   15.780  0.50 19.83  ? 84  ARG B CD  1 
ATOM   2888  N  NE  A ARG B  1 84  ? -26.855 5.851   14.405  0.50 14.36  ? 84  ARG B NE  1 
ATOM   2889  N  NE  B ARG B  1 84  ? -27.593 5.037   16.476  0.50 25.98  ? 84  ARG B NE  1 
ATOM   2890  C  CZ  A ARG B  1 84  ? -27.981 5.779   13.721  0.50 19.07  ? 84  ARG B CZ  1 
ATOM   2891  C  CZ  B ARG B  1 84  ? -28.859 4.980   16.088  0.50 27.27  ? 84  ARG B CZ  1 
ATOM   2892  N  NH1 A ARG B  1 84  ? -29.103 5.441   14.334  0.50 23.31  ? 84  ARG B NH1 1 
ATOM   2893  N  NH1 B ARG B  1 84  ? -29.257 5.602   14.997  0.50 35.03  ? 84  ARG B NH1 1 
ATOM   2894  N  NH2 A ARG B  1 84  ? -27.969 5.945   12.402  0.50 22.06  ? 84  ARG B NH2 1 
ATOM   2895  N  NH2 B ARG B  1 84  ? -29.714 4.273   16.813  0.50 29.12  ? 84  ARG B NH2 1 
ATOM   2896  N  N   . TYR B  1 85  ? -22.059 4.877   16.235  1.00 11.90  ? 85  TYR B N   1 
ATOM   2897  C  CA  . TYR B  1 85  ? -21.160 5.347   15.178  1.00 11.35  ? 85  TYR B CA  1 
ATOM   2898  C  C   . TYR B  1 85  ? -21.858 5.125   13.876  1.00 10.41  ? 85  TYR B C   1 
ATOM   2899  O  O   . TYR B  1 85  ? -22.206 3.992   13.547  1.00 12.37  ? 85  TYR B O   1 
ATOM   2900  C  CB  . TYR B  1 85  ? -19.787 4.637   15.255  1.00 11.57  ? 85  TYR B CB  1 
ATOM   2901  C  CG  . TYR B  1 85  ? -18.901 5.162   16.321  1.00 11.11  ? 85  TYR B CG  1 
ATOM   2902  C  CD1 . TYR B  1 85  ? -19.055 4.726   17.640  1.00 13.54  ? 85  TYR B CD1 1 
ATOM   2903  C  CD2 . TYR B  1 85  ? -17.895 6.063   16.094  1.00 11.68  ? 85  TYR B CD2 1 
ATOM   2904  C  CE1 . TYR B  1 85  ? -18.234 5.175   18.649  1.00 14.21  ? 85  TYR B CE1 1 
ATOM   2905  C  CE2 . TYR B  1 85  ? -17.052 6.515   17.059  1.00 12.62  ? 85  TYR B CE2 1 
ATOM   2906  C  CZ  . TYR B  1 85  ? -17.247 6.067   18.377  1.00 13.59  ? 85  TYR B CZ  1 
ATOM   2907  O  OH  . TYR B  1 85  ? -16.425 6.477   19.367  1.00 16.78  ? 85  TYR B OH  1 
ATOM   2908  N  N   . SER B  1 86  ? -22.118 6.186   13.117  1.00 10.79  ? 86  SER B N   1 
ATOM   2909  C  CA  . SER B  1 86  ? -22.825 6.094   11.857  1.00 10.53  ? 86  SER B CA  1 
ATOM   2910  C  C   . SER B  1 86  ? -21.812 6.093   10.713  1.00 8.58   ? 86  SER B C   1 
ATOM   2911  O  O   . SER B  1 86  ? -20.769 6.772   10.801  1.00 9.34   ? 86  SER B O   1 
ATOM   2912  C  CB  . SER B  1 86  ? -23.753 7.299   11.691  1.00 12.30  ? 86  SER B CB  1 
ATOM   2913  O  OG  . SER B  1 86  ? -24.798 7.211   12.714  1.00 14.89  ? 86  SER B OG  1 
ATOM   2914  N  N   . ALA B  1 87  ? -22.159 5.374   9.651   1.00 9.49   ? 87  ALA B N   1 
ATOM   2915  C  CA  . ALA B  1 87  ? -21.230 5.299   8.525   1.00 8.89   ? 87  ALA B CA  1 
ATOM   2916  C  C   . ALA B  1 87  ? -21.138 6.595   7.781   1.00 9.17   ? 87  ALA B C   1 
ATOM   2917  O  O   . ALA B  1 87  ? -22.123 7.376   7.729   1.00 10.29  ? 87  ALA B O   1 
ATOM   2918  C  CB  . ALA B  1 87  ? -21.741 4.207   7.604   1.00 11.19  ? 87  ALA B CB  1 
ATOM   2919  N  N   . THR B  1 88  ? -20.005 6.822   7.165   1.00 8.22   ? 88  THR B N   1 
ATOM   2920  C  CA  . THR B  1 88  ? -19.810 7.940   6.259   1.00 8.88   ? 88  THR B CA  1 
ATOM   2921  C  C   . THR B  1 88  ? -19.287 7.520   4.922   1.00 7.62   ? 88  THR B C   1 
ATOM   2922  O  O   . THR B  1 88  ? -19.689 8.069   3.899   1.00 8.15   ? 88  THR B O   1 
ATOM   2923  C  CB  . THR B  1 88  ? -18.969 9.067   6.926   1.00 11.20  ? 88  THR B CB  1 
ATOM   2924  O  OG1 . THR B  1 88  ? -18.949 10.191  6.023   1.00 15.90  ? 88  THR B OG1 1 
ATOM   2925  C  CG2 . THR B  1 88  ? -17.623 8.648   7.320   1.00 11.99  ? 88  THR B CG2 1 
ATOM   2926  N  N   . GLN B  1 89  ? -18.331 6.568   4.850   1.00 7.24   ? 89  GLN B N   1 
ATOM   2927  C  CA  . GLN B  1 89  ? -17.779 6.173   3.563   1.00 7.01   ? 89  GLN B CA  1 
ATOM   2928  C  C   . GLN B  1 89  ? -17.019 4.880   3.780   1.00 6.24   ? 89  GLN B C   1 
ATOM   2929  O  O   . GLN B  1 89  ? -16.627 4.535   4.896   1.00 7.39   ? 89  GLN B O   1 
ATOM   2930  C  CB  . GLN B  1 89  ? -16.868 7.261   2.956   1.00 7.95   ? 89  GLN B CB  1 
ATOM   2931  C  CG  . GLN B  1 89  ? -15.764 7.728   3.866   1.00 9.02   ? 89  GLN B CG  1 
ATOM   2932  C  CD  . GLN B  1 89  ? -14.385 7.259   3.423   1.00 9.26   ? 89  GLN B CD  1 
ATOM   2933  O  OE1 . GLN B  1 89  ? -14.221 6.102   3.111   1.00 8.84   ? 89  GLN B OE1 1 
ATOM   2934  N  NE2 . GLN B  1 89  ? -13.414 8.050   3.461   1.00 13.63  ? 89  GLN B NE2 1 
ATOM   2935  N  N   . LEU B  1 90  ? -16.763 4.195   2.654   1.00 6.46   ? 90  LEU B N   1 
ATOM   2936  C  CA  . LEU B  1 90  ? -15.802 3.112   2.657   1.00 6.10   ? 90  LEU B CA  1 
ATOM   2937  C  C   . LEU B  1 90  ? -14.823 3.355   1.505   1.00 6.29   ? 90  LEU B C   1 
ATOM   2938  O  O   . LEU B  1 90  ? -15.129 4.038   0.536   1.00 6.99   ? 90  LEU B O   1 
ATOM   2939  C  CB  . LEU B  1 90  ? -16.465 1.720   2.624   1.00 6.74   ? 90  LEU B CB  1 
ATOM   2940  C  CG  . LEU B  1 90  ? -17.365 1.407   1.463   1.00 7.65   ? 90  LEU B CG  1 
ATOM   2941  C  CD1 . LEU B  1 90  ? -16.621 1.077   0.168   1.00 8.11   ? 90  LEU B CD1 1 
ATOM   2942  C  CD2 . LEU B  1 90  ? -18.269 0.194   1.842   1.00 9.21   ? 90  LEU B CD2 1 
ATOM   2943  N  N   . HIS B  1 91  ? -13.645 2.736   1.625   1.00 6.17   ? 91  HIS B N   1 
ATOM   2944  C  CA  . HIS B  1 91  ? -12.603 2.859   0.620   1.00 6.27   ? 91  HIS B CA  1 
ATOM   2945  C  C   . HIS B  1 91  ? -11.644 1.718   0.819   1.00 5.98   ? 91  HIS B C   1 
ATOM   2946  O  O   . HIS B  1 91  ? -11.708 0.958   1.795   1.00 6.26   ? 91  HIS B O   1 
ATOM   2947  C  CB  . HIS B  1 91  ? -11.906 4.245   0.718   1.00 6.99   ? 91  HIS B CB  1 
ATOM   2948  C  CG  . HIS B  1 91  ? -11.183 4.400   1.987   1.00 6.36   ? 91  HIS B CG  1 
ATOM   2949  N  ND1 . HIS B  1 91  ? -11.758 4.928   3.123   1.00 6.86   ? 91  HIS B ND1 1 
ATOM   2950  C  CD2 . HIS B  1 91  ? -9.945  3.963   2.417   1.00 6.08   ? 91  HIS B CD2 1 
ATOM   2951  C  CE1 . HIS B  1 91  ? -10.912 4.853   4.149   1.00 6.99   ? 91  HIS B CE1 1 
ATOM   2952  N  NE2 . HIS B  1 91  ? -9.790  4.240   3.723   1.00 5.97   ? 91  HIS B NE2 1 
ATOM   2953  N  N   . LEU B  1 92  ? -10.652 1.621   -0.100  1.00 6.57   ? 92  LEU B N   1 
ATOM   2954  C  CA  . LEU B  1 92  ? -9.708  0.503   -0.077  1.00 6.48   ? 92  LEU B CA  1 
ATOM   2955  C  C   . LEU B  1 92  ? -8.283  1.004   -0.171  1.00 6.02   ? 92  LEU B C   1 
ATOM   2956  O  O   . LEU B  1 92  ? -8.001  2.150   -0.552  1.00 6.93   ? 92  LEU B O   1 
ATOM   2957  C  CB  . LEU B  1 92  ? -9.958  -0.510  -1.197  1.00 8.68   ? 92  LEU B CB  1 
ATOM   2958  C  CG  . LEU B  1 92  ? -11.339 -1.198  -1.110  1.00 9.06   ? 92  LEU B CG  1 
ATOM   2959  C  CD1 . LEU B  1 92  ? -12.368 -0.546  -1.954  1.00 12.51  ? 92  LEU B CD1 1 
ATOM   2960  C  CD2 . LEU B  1 92  ? -11.200 -2.656  -1.448  1.00 12.27  ? 92  LEU B CD2 1 
ATOM   2961  N  N   . HIS B  1 93  ? -7.359  0.105   0.133   1.00 6.06   ? 93  HIS B N   1 
ATOM   2962  C  CA  . HIS B  1 93  ? -5.919  0.246   -0.039  1.00 6.11   ? 93  HIS B CA  1 
ATOM   2963  C  C   . HIS B  1 93  ? -5.402  -0.973  -0.702  1.00 6.28   ? 93  HIS B C   1 
ATOM   2964  O  O   . HIS B  1 93  ? -5.856  -2.083  -0.369  1.00 6.63   ? 93  HIS B O   1 
ATOM   2965  C  CB  . HIS B  1 93  ? -5.234  0.445   1.306   1.00 6.40   ? 93  HIS B CB  1 
ATOM   2966  C  CG  . HIS B  1 93  ? -5.755  1.626   2.096   1.00 6.20   ? 93  HIS B CG  1 
ATOM   2967  N  ND1 . HIS B  1 93  ? -5.176  2.873   2.056   1.00 6.92   ? 93  HIS B ND1 1 
ATOM   2968  C  CD2 . HIS B  1 93  ? -6.811  1.752   2.968   1.00 6.68   ? 93  HIS B CD2 1 
ATOM   2969  C  CE1 . HIS B  1 93  ? -5.898  3.708   2.830   1.00 6.64   ? 93  HIS B CE1 1 
ATOM   2970  N  NE2 . HIS B  1 93  ? -6.872  3.056   3.413   1.00 6.22   ? 93  HIS B NE2 1 
ATOM   2971  N  N   . TRP B  1 94  ? -4.435  -0.837  -1.616  1.00 6.54   ? 94  TRP B N   1 
ATOM   2972  C  CA  . TRP B  1 94  ? -3.963  -1.960  -2.424  1.00 6.81   ? 94  TRP B CA  1 
ATOM   2973  C  C   . TRP B  1 94  ? -2.568  -1.704  -2.900  1.00 7.42   ? 94  TRP B C   1 
ATOM   2974  O  O   . TRP B  1 94  ? -1.938  -0.662  -2.648  1.00 7.35   ? 94  TRP B O   1 
ATOM   2975  C  CB  . TRP B  1 94  ? -4.896  -2.234  -3.589  1.00 7.93   ? 94  TRP B CB  1 
ATOM   2976  C  CG  . TRP B  1 94  ? -5.052  -1.045  -4.505  1.00 7.18   ? 94  TRP B CG  1 
ATOM   2977  C  CD1 . TRP B  1 94  ? -4.230  -0.719  -5.552  1.00 8.88   ? 94  TRP B CD1 1 
ATOM   2978  C  CD2 . TRP B  1 94  ? -6.055  -0.042  -4.452  1.00 7.46   ? 94  TRP B CD2 1 
ATOM   2979  N  NE1 . TRP B  1 94  ? -4.683  0.422   -6.166  1.00 8.58   ? 94  TRP B NE1 1 
ATOM   2980  C  CE2 . TRP B  1 94  ? -5.778  0.898   -5.506  1.00 8.12   ? 94  TRP B CE2 1 
ATOM   2981  C  CE3 . TRP B  1 94  ? -7.131  0.217   -3.605  1.00 7.54   ? 94  TRP B CE3 1 
ATOM   2982  C  CZ2 . TRP B  1 94  ? -6.588  1.963   -5.748  1.00 8.76   ? 94  TRP B CZ2 1 
ATOM   2983  C  CZ3 . TRP B  1 94  ? -7.923  1.349   -3.826  1.00 8.69   ? 94  TRP B CZ3 1 
ATOM   2984  C  CH2 . TRP B  1 94  ? -7.654  2.204   -4.896  1.00 8.80   ? 94  TRP B CH2 1 
ATOM   2985  N  N   . GLY B  1 95  ? -2.013  -2.752  -3.560  1.00 7.75   ? 95  GLY B N   1 
ATOM   2986  C  CA  . GLY B  1 95  ? -0.625  -2.748  -4.054  1.00 9.21   ? 95  GLY B CA  1 
ATOM   2987  C  C   . GLY B  1 95  ? -0.563  -2.414  -5.512  1.00 8.41   ? 95  GLY B C   1 
ATOM   2988  O  O   . GLY B  1 95  ? -1.063  -1.379  -5.971  1.00 8.89   ? 95  GLY B O   1 
ATOM   2989  N  N   . ASN B  1 96  ? -0.010  -3.345  -6.327  1.00 9.18   ? 96  ASN B N   1 
ATOM   2990  C  CA  . ASN B  1 96  ? 0.126   -3.074  -7.754  1.00 11.05  ? 96  ASN B CA  1 
ATOM   2991  C  C   . ASN B  1 96  ? 0.121   -4.395  -8.479  1.00 11.35  ? 96  ASN B C   1 
ATOM   2992  O  O   . ASN B  1 96  ? 0.272   -5.435  -7.855  1.00 11.24  ? 96  ASN B O   1 
ATOM   2993  C  CB  . ASN B  1 96  ? 1.356   -2.202  -8.037  1.00 13.79  ? 96  ASN B CB  1 
ATOM   2994  C  CG  . ASN B  1 96  ? 2.624   -2.966  -7.882  1.00 15.90  ? 96  ASN B CG  1 
ATOM   2995  O  OD1 . ASN B  1 96  ? 3.012   -3.735  -8.790  1.00 22.67  ? 96  ASN B OD1 1 
ATOM   2996  N  ND2 . ASN B  1 96  ? 3.335   -2.737  -6.790  1.00 17.12  ? 96  ASN B ND2 1 
ATOM   2997  N  N   . PRO B  1 97  ? 0.000   -4.413  -9.832  1.00 12.83  ? 97  PRO B N   1 
ATOM   2998  C  CA  . PRO B  1 97  ? -0.189  -5.651  -10.583 1.00 14.92  ? 97  PRO B CA  1 
ATOM   2999  C  C   . PRO B  1 97  ? 0.933   -6.613  -10.398 1.00 12.81  ? 97  PRO B C   1 
ATOM   3000  O  O   . PRO B  1 97  ? 0.703   -7.829  -10.504 1.00 16.03  ? 97  PRO B O   1 
ATOM   3001  C  CB  . PRO B  1 97  ? -0.323  -5.231  -12.038 1.00 18.57  ? 97  PRO B CB  1 
ATOM   3002  C  CG  . PRO B  1 97  ? -0.965  -3.934  -11.906 1.00 17.81  ? 97  PRO B CG  1 
ATOM   3003  C  CD  . PRO B  1 97  ? -0.248  -3.267  -10.717 1.00 16.61  ? 97  PRO B CD  1 
ATOM   3004  N  N   . ASN B  1 98  ? 2.144   -6.099  -10.206 1.00 11.63  ? 98  ASN B N   1 
ATOM   3005  C  CA  . ASN B  1 98  ? 3.308   -6.978  -10.122 1.00 13.99  ? 98  ASN B CA  1 
ATOM   3006  C  C   . ASN B  1 98  ? 3.563   -7.321  -8.658  1.00 17.00  ? 98  ASN B C   1 
ATOM   3007  O  O   . ASN B  1 98  ? 4.447   -8.127  -8.411  1.00 23.58  ? 98  ASN B O   1 
ATOM   3008  C  CB  . ASN B  1 98  ? 4.461   -6.236  -10.775 1.00 14.49  ? 98  ASN B CB  1 
ATOM   3009  C  CG  . ASN B  1 98  ? 4.248   -6.081  -12.278 1.00 13.12  ? 98  ASN B CG  1 
ATOM   3010  O  OD1 . ASN B  1 98  ? 4.091   -7.088  -13.008 1.00 15.23  ? 98  ASN B OD1 1 
ATOM   3011  N  ND2 . ASN B  1 98  ? 4.124   -4.852  -12.701 1.00 16.55  ? 98  ASN B ND2 1 
ATOM   3012  N  N   . ASP B  1 99  ? 2.855   -6.729  -7.683  1.00 13.87  ? 99  ASP B N   1 
ATOM   3013  C  CA  . ASP B  1 99  ? 3.037   -7.010  -6.298  1.00 15.08  ? 99  ASP B CA  1 
ATOM   3014  C  C   . ASP B  1 99  ? 1.749   -6.778  -5.547  1.00 12.44  ? 99  ASP B C   1 
ATOM   3015  O  O   . ASP B  1 99  ? 1.506   -5.683  -5.014  1.00 11.89  ? 99  ASP B O   1 
ATOM   3016  C  CB  . ASP B  1 99  ? 4.140   -6.149  -5.663  1.00 18.19  ? 99  ASP B CB  1 
ATOM   3017  C  CG  . ASP B  1 99  ? 4.392   -6.529  -4.212  1.00 25.20  ? 99  ASP B CG  1 
ATOM   3018  O  OD1 . ASP B  1 99  ? 3.879   -7.600  -3.830  1.00 30.59  ? 99  ASP B OD1 1 
ATOM   3019  O  OD2 . ASP B  1 99  ? 5.042   -5.783  -3.500  1.00 45.58  ? 99  ASP B OD2 1 
ATOM   3020  N  N   . PRO B  1 100 ? 0.827   -7.752  -5.596  1.00 11.10  ? 100 PRO B N   1 
ATOM   3021  C  CA  . PRO B  1 100 ? -0.538  -7.559  -5.042  1.00 11.76  ? 100 PRO B CA  1 
ATOM   3022  C  C   . PRO B  1 100 ? -0.534  -7.817  -3.534  1.00 10.69  ? 100 PRO B C   1 
ATOM   3023  O  O   . PRO B  1 100 ? -1.112  -8.736  -3.039  1.00 12.97  ? 100 PRO B O   1 
ATOM   3024  C  CB  . PRO B  1 100 ? -1.369  -8.573  -5.840  1.00 14.09  ? 100 PRO B CB  1 
ATOM   3025  C  CG  . PRO B  1 100 ? -0.359  -9.659  -6.145  1.00 16.76  ? 100 PRO B CG  1 
ATOM   3026  C  CD  . PRO B  1 100 ? 0.910   -8.947  -6.444  1.00 14.77  ? 100 PRO B CD  1 
ATOM   3027  N  N   . HIS B  1 101 ? 0.181   -6.952  -2.803  1.00 11.54  ? 101 HIS B N   1 
ATOM   3028  C  CA  . HIS B  1 101 ? 0.391   -7.046  -1.333  1.00 12.06  ? 101 HIS B CA  1 
ATOM   3029  C  C   . HIS B  1 101 ? 0.294   -5.701  -0.645  1.00 12.09  ? 101 HIS B C   1 
ATOM   3030  O  O   . HIS B  1 101 ? 1.267   -5.338  0.115   1.00 17.21  ? 101 HIS B O   1 
ATOM   3031  C  CB  . HIS B  1 101 ? 1.666   -7.763  -0.960  1.00 13.58  ? 101 HIS B CB  1 
ATOM   3032  C  CG  . HIS B  1 101 ? 1.716   -9.155  -1.550  1.00 17.31  ? 101 HIS B CG  1 
ATOM   3033  N  ND1 . HIS B  1 101 ? 1.151   -10.285 -1.031  1.00 24.07  ? 101 HIS B ND1 1 
ATOM   3034  C  CD2 . HIS B  1 101 ? 2.340   -9.532  -2.695  1.00 18.56  ? 101 HIS B CD2 1 
ATOM   3035  C  CE1 . HIS B  1 101 ? 1.373   -11.315 -1.876  1.00 22.87  ? 101 HIS B CE1 1 
ATOM   3036  N  NE2 . HIS B  1 101 ? 2.129   -10.842 -2.899  1.00 22.28  ? 101 HIS B NE2 1 
ATOM   3037  N  N   . GLY B  1 102 ? -0.859  -5.098  -0.635  1.00 8.95   ? 102 GLY B N   1 
ATOM   3038  C  CA  . GLY B  1 102 ? -1.051  -3.716  -0.291  1.00 8.67   ? 102 GLY B CA  1 
ATOM   3039  C  C   . GLY B  1 102 ? -1.980  -3.503  0.884   1.00 8.46   ? 102 GLY B C   1 
ATOM   3040  O  O   . GLY B  1 102 ? -2.505  -2.377  0.992   1.00 8.97   ? 102 GLY B O   1 
ATOM   3041  N  N   . SER B  1 103 ? -2.189  -4.457  1.794   1.00 7.58   ? 103 SER B N   1 
ATOM   3042  C  CA  . SER B  1 103 ? -2.920  -4.110  2.998   1.00 7.79   ? 103 SER B CA  1 
ATOM   3043  C  C   . SER B  1 103 ? -2.119  -3.101  3.796   1.00 7.13   ? 103 SER B C   1 
ATOM   3044  O  O   . SER B  1 103 ? -0.922  -2.929  3.652   1.00 9.32   ? 103 SER B O   1 
ATOM   3045  C  CB  . SER B  1 103 ? -3.239  -5.335  3.838   1.00 7.65   ? 103 SER B CB  1 
ATOM   3046  O  OG  . SER B  1 103 ? -2.068  -5.920  4.402   1.00 7.90   ? 103 SER B OG  1 
ATOM   3047  N  N   . GLU B  1 104 ? -2.831  -2.409  4.709   1.00 6.84   ? 104 GLU B N   1 
ATOM   3048  C  CA  . GLU B  1 104 ? -2.189  -1.490  5.637   1.00 7.19   ? 104 GLU B CA  1 
ATOM   3049  C  C   . GLU B  1 104 ? -1.761  -2.211  6.891   1.00 6.43   ? 104 GLU B C   1 
ATOM   3050  O  O   . GLU B  1 104 ? -0.579  -2.234  7.250   1.00 7.23   ? 104 GLU B O   1 
ATOM   3051  C  CB  . GLU B  1 104 ? -3.114  -0.313  5.949   1.00 7.29   ? 104 GLU B CB  1 
ATOM   3052  C  CG  . GLU B  1 104 ? -3.583  0.410   4.689   1.00 7.31   ? 104 GLU B CG  1 
ATOM   3053  C  CD  . GLU B  1 104 ? -3.621  1.873   4.960   1.00 7.02   ? 104 GLU B CD  1 
ATOM   3054  O  OE1 . GLU B  1 104 ? -4.650  2.352   5.500   1.00 7.82   ? 104 GLU B OE1 1 
ATOM   3055  O  OE2 . GLU B  1 104 ? -2.627  2.582   4.657   1.00 8.29   ? 104 GLU B OE2 1 
ATOM   3056  N  N   . HIS B  1 105 ? -2.735  -2.825  7.587   1.00 6.89   ? 105 HIS B N   1 
ATOM   3057  C  CA  . HIS B  1 105 ? -2.364  -3.688  8.689   1.00 7.02   ? 105 HIS B CA  1 
ATOM   3058  C  C   . HIS B  1 105 ? -1.703  -4.959  8.179   1.00 6.48   ? 105 HIS B C   1 
ATOM   3059  O  O   . HIS B  1 105 ? -2.010  -5.429  7.097   1.00 7.80   ? 105 HIS B O   1 
ATOM   3060  C  CB  . HIS B  1 105 ? -3.608  -4.011  9.544   1.00 6.95   ? 105 HIS B CB  1 
ATOM   3061  C  CG  . HIS B  1 105 ? -4.165  -2.833  10.235  1.00 6.49   ? 105 HIS B CG  1 
ATOM   3062  N  ND1 . HIS B  1 105 ? -5.070  -2.005  9.703   1.00 7.27   ? 105 HIS B ND1 1 
ATOM   3063  C  CD2 . HIS B  1 105 ? -3.861  -2.296  11.446  1.00 6.80   ? 105 HIS B CD2 1 
ATOM   3064  C  CE1 . HIS B  1 105 ? -5.311  -0.966  10.569  1.00 7.72   ? 105 HIS B CE1 1 
ATOM   3065  N  NE2 . HIS B  1 105 ? -4.569  -1.140  11.652  1.00 7.28   ? 105 HIS B NE2 1 
ATOM   3066  N  N   . THR B  1 106 ? -0.787  -5.479  8.990   1.00 7.53   ? 106 THR B N   1 
ATOM   3067  C  CA  . THR B  1 106 ? -0.155  -6.755  8.708   1.00 8.46   ? 106 THR B CA  1 
ATOM   3068  C  C   . THR B  1 106 ? -0.461  -7.666  9.899   1.00 8.07   ? 106 THR B C   1 
ATOM   3069  O  O   . THR B  1 106 ? -0.763  -7.173  11.000  1.00 8.72   ? 106 THR B O   1 
ATOM   3070  C  CB  . THR B  1 106 ? 1.345   -6.588  8.439   1.00 9.18   ? 106 THR B CB  1 
ATOM   3071  O  OG1 . THR B  1 106 ? 1.997   -6.047  9.557   1.00 9.77   ? 106 THR B OG1 1 
ATOM   3072  C  CG2 . THR B  1 106 ? 1.565   -5.727  7.264   1.00 10.65  ? 106 THR B CG2 1 
ATOM   3073  N  N   . VAL B  1 107 ? -0.336  -8.973  9.668   1.00 9.29   ? 107 VAL B N   1 
ATOM   3074  C  CA  . VAL B  1 107 ? -0.571  -9.898  10.797  1.00 10.55  ? 107 VAL B CA  1 
ATOM   3075  C  C   . VAL B  1 107 ? 0.689   -10.801 10.835  1.00 10.69  ? 107 VAL B C   1 
ATOM   3076  O  O   . VAL B  1 107 ? 1.031   -11.456 9.835   1.00 12.55  ? 107 VAL B O   1 
ATOM   3077  C  CB  . VAL B  1 107 ? -1.827  -10.784 10.580  1.00 11.40  ? 107 VAL B CB  1 
ATOM   3078  C  CG1 . VAL B  1 107 ? -1.923  -11.812 11.719  1.00 13.70  ? 107 VAL B CG1 1 
ATOM   3079  C  CG2 . VAL B  1 107 ? -3.082  -9.926  10.573  1.00 12.82  ? 107 VAL B CG2 1 
ATOM   3080  N  N   . SER B  1 108 ? 1.371   -10.758 11.967  1.00 11.01  ? 108 SER B N   1 
ATOM   3081  C  CA  . SER B  1 108 ? 2.611   -11.515 12.136  1.00 11.71  ? 108 SER B CA  1 
ATOM   3082  C  C   . SER B  1 108 ? 3.568   -11.264 10.945  1.00 12.08  ? 108 SER B C   1 
ATOM   3083  O  O   . SER B  1 108 ? 4.177   -12.182 10.393  1.00 13.62  ? 108 SER B O   1 
ATOM   3084  C  CB  . SER B  1 108 ? 2.291   -13.012 12.322  1.00 15.38  ? 108 SER B CB  1 
ATOM   3085  O  OG  . SER B  1 108 ? 1.508   -13.149 13.474  1.00 17.84  ? 108 SER B OG  1 
ATOM   3086  N  N   . GLY B  1 109 ? 3.684   -9.994  10.578  1.00 11.43  ? 109 GLY B N   1 
ATOM   3087  C  CA  . GLY B  1 109 ? 4.624   -9.553  9.573   1.00 12.26  ? 109 GLY B CA  1 
ATOM   3088  C  C   . GLY B  1 109 ? 4.195   -9.759  8.133   1.00 16.22  ? 109 GLY B C   1 
ATOM   3089  O  O   . GLY B  1 109 ? 4.945   -9.398  7.200   1.00 21.33  ? 109 GLY B O   1 
ATOM   3090  N  N   . GLN B  1 110 ? 2.995   -10.286 7.886   1.00 14.51  ? 110 GLN B N   1 
ATOM   3091  C  CA  . GLN B  1 110 ? 2.579   -10.524 6.526   1.00 17.05  ? 110 GLN B CA  1 
ATOM   3092  C  C   . GLN B  1 110 ? 1.516   -9.544  6.093   1.00 12.88  ? 110 GLN B C   1 
ATOM   3093  O  O   . GLN B  1 110 ? 0.542   -9.268  6.824   1.00 10.11  ? 110 GLN B O   1 
ATOM   3094  C  CB  . GLN B  1 110 ? 2.005   -11.912 6.479   1.00 20.53  ? 110 GLN B CB  1 
ATOM   3095  C  CG  . GLN B  1 110 ? 2.950   -12.946 7.078   1.00 18.62  ? 110 GLN B CG  1 
ATOM   3096  C  CD  . GLN B  1 110 ? 4.351   -12.899 6.462   1.00 22.17  ? 110 GLN B CD  1 
ATOM   3097  O  OE1 . GLN B  1 110 ? 4.530   -13.152 5.252   1.00 36.09  ? 110 GLN B OE1 1 
ATOM   3098  N  NE2 . GLN B  1 110 ? 5.353   -12.699 7.327   1.00 31.79  ? 110 GLN B NE2 1 
ATOM   3099  N  N   . HIS B  1 111 ? 1.729   -8.990  4.885   1.00 13.10  ? 111 HIS B N   1 
ATOM   3100  C  CA  . HIS B  1 111 ? 0.709   -8.228  4.201   1.00 10.67  ? 111 HIS B CA  1 
ATOM   3101  C  C   . HIS B  1 111 ? -0.340  -9.089  3.584   1.00 10.74  ? 111 HIS B C   1 
ATOM   3102  O  O   . HIS B  1 111 ? -0.022  -10.188 3.115   1.00 19.81  ? 111 HIS B O   1 
ATOM   3103  C  CB  . HIS B  1 111 ? 1.163   -7.368  3.007   1.00 14.74  ? 111 HIS B CB  1 
ATOM   3104  C  CG  . HIS B  1 111 ? 1.860   -6.086  3.362   1.00 12.03  ? 111 HIS B CG  1 
ATOM   3105  N  ND1 . HIS B  1 111 ? 1.234   -4.916  3.580   1.00 14.98  ? 111 HIS B ND1 1 
ATOM   3106  C  CD2 . HIS B  1 111 ? 3.171   -5.893  3.756   1.00 15.22  ? 111 HIS B CD2 1 
ATOM   3107  C  CE1 . HIS B  1 111 ? 2.170   -3.964  3.998   1.00 15.16  ? 111 HIS B CE1 1 
ATOM   3108  N  NE2 . HIS B  1 111 ? 3.349   -4.569  4.004   1.00 18.50  ? 111 HIS B NE2 1 
ATOM   3109  N  N   . PHE B  1 112 ? -1.541  -8.617  3.526   1.00 8.46   ? 112 PHE B N   1 
ATOM   3110  C  CA  . PHE B  1 112 ? -2.579  -9.172  2.715   1.00 8.27   ? 112 PHE B CA  1 
ATOM   3111  C  C   . PHE B  1 112 ? -2.609  -8.420  1.392   1.00 7.73   ? 112 PHE B C   1 
ATOM   3112  O  O   . PHE B  1 112 ? -1.904  -7.408  1.216   1.00 9.29   ? 112 PHE B O   1 
ATOM   3113  C  CB  . PHE B  1 112 ? -3.897  -9.088  3.469   1.00 9.27   ? 112 PHE B CB  1 
ATOM   3114  C  CG  . PHE B  1 112 ? -3.905  -10.048 4.631   1.00 11.40  ? 112 PHE B CG  1 
ATOM   3115  C  CD1 . PHE B  1 112 ? -3.220  -9.759  5.861   1.00 14.83  ? 112 PHE B CD1 1 
ATOM   3116  C  CD2 . PHE B  1 112 ? -4.566  -11.243 4.495   1.00 15.24  ? 112 PHE B CD2 1 
ATOM   3117  C  CE1 . PHE B  1 112 ? -3.192  -10.697 6.844   1.00 21.17  ? 112 PHE B CE1 1 
ATOM   3118  C  CE2 . PHE B  1 112 ? -4.560  -12.187 5.509   1.00 19.25  ? 112 PHE B CE2 1 
ATOM   3119  C  CZ  . PHE B  1 112 ? -3.878  -11.887 6.672   1.00 24.48  ? 112 PHE B CZ  1 
ATOM   3120  N  N   . ALA B  1 113 ? -3.400  -8.901  0.442   1.00 7.89   ? 113 ALA B N   1 
ATOM   3121  C  CA  . ALA B  1 113 ? -3.454  -8.263  -0.889  1.00 8.47   ? 113 ALA B CA  1 
ATOM   3122  C  C   . ALA B  1 113 ? -3.977  -6.853  -0.829  1.00 6.91   ? 113 ALA B C   1 
ATOM   3123  O  O   . ALA B  1 113 ? -3.526  -5.989  -1.591  1.00 7.74   ? 113 ALA B O   1 
ATOM   3124  C  CB  . ALA B  1 113 ? -4.288  -9.102  -1.818  1.00 9.83   ? 113 ALA B CB  1 
ATOM   3125  N  N   . ALA B  1 114 ? -5.000  -6.596  0.003   1.00 6.84   ? 114 ALA B N   1 
ATOM   3126  C  CA  . ALA B  1 114 ? -5.644  -5.285  0.019   1.00 6.69   ? 114 ALA B CA  1 
ATOM   3127  C  C   . ALA B  1 114 ? -6.343  -5.150  1.376   1.00 6.12   ? 114 ALA B C   1 
ATOM   3128  O  O   . ALA B  1 114 ? -6.337  -6.090  2.194   1.00 6.25   ? 114 ALA B O   1 
ATOM   3129  C  CB  . ALA B  1 114 ? -6.575  -5.148  -1.184  1.00 7.57   ? 114 ALA B CB  1 
ATOM   3130  N  N   . GLU B  1 115 ? -6.982  -4.016  1.578   1.00 6.25   ? 115 GLU B N   1 
ATOM   3131  C  CA  . GLU B  1 115 ? -7.694  -3.769  2.834   1.00 6.31   ? 115 GLU B CA  1 
ATOM   3132  C  C   . GLU B  1 115 ? -8.852  -2.834  2.578   1.00 6.06   ? 115 GLU B C   1 
ATOM   3133  O  O   . GLU B  1 115 ? -8.696  -1.834  1.861   1.00 6.85   ? 115 GLU B O   1 
ATOM   3134  C  CB  . GLU B  1 115 ? -6.743  -3.238  3.885   1.00 6.65   ? 115 GLU B CB  1 
ATOM   3135  C  CG  . GLU B  1 115 ? -7.287  -3.070  5.301   1.00 6.43   ? 115 GLU B CG  1 
ATOM   3136  C  CD  . GLU B  1 115 ? -6.214  -2.831  6.291   1.00 6.50   ? 115 GLU B CD  1 
ATOM   3137  O  OE1 . GLU B  1 115 ? -5.073  -3.312  6.132   1.00 7.01   ? 115 GLU B OE1 1 
ATOM   3138  O  OE2 . GLU B  1 115 ? -6.518  -2.155  7.355   1.00 7.02   ? 115 GLU B OE2 1 
ATOM   3139  N  N   . LEU B  1 116 ? -10.012 -3.161  3.136   1.00 5.53   ? 116 LEU B N   1 
ATOM   3140  C  CA  . LEU B  1 116 ? -11.214 -2.335  3.087   1.00 5.75   ? 116 LEU B CA  1 
ATOM   3141  C  C   . LEU B  1 116 ? -11.365 -1.613  4.410   1.00 4.72   ? 116 LEU B C   1 
ATOM   3142  O  O   . LEU B  1 116 ? -11.233 -2.231  5.461   1.00 5.80   ? 116 LEU B O   1 
ATOM   3143  C  CB  . LEU B  1 116 ? -12.436 -3.185  2.862   1.00 6.85   ? 116 LEU B CB  1 
ATOM   3144  C  CG  . LEU B  1 116 ? -13.809 -2.489  2.960   1.00 7.52   ? 116 LEU B CG  1 
ATOM   3145  C  CD1 . LEU B  1 116 ? -14.055 -1.586  1.742   1.00 8.67   ? 116 LEU B CD1 1 
ATOM   3146  C  CD2 . LEU B  1 116 ? -14.921 -3.493  3.154   1.00 8.77   ? 116 LEU B CD2 1 
ATOM   3147  N  N   . HIS B  1 117 ? -11.646 -0.310  4.351   1.00 5.28   ? 117 HIS B N   1 
ATOM   3148  C  CA  . HIS B  1 117 ? -11.978 0.475   5.522   1.00 5.36   ? 117 HIS B CA  1 
ATOM   3149  C  C   . HIS B  1 117 ? -13.375 1.005   5.422   1.00 5.25   ? 117 HIS B C   1 
ATOM   3150  O  O   . HIS B  1 117 ? -13.703 1.675   4.426   1.00 6.30   ? 117 HIS B O   1 
ATOM   3151  C  CB  . HIS B  1 117 ? -10.971 1.653   5.653   1.00 5.96   ? 117 HIS B CB  1 
ATOM   3152  C  CG  . HIS B  1 117 ? -9.612  1.193   6.008   1.00 5.59   ? 117 HIS B CG  1 
ATOM   3153  N  ND1 . HIS B  1 117 ? -8.498  1.943   5.760   1.00 5.62   ? 117 HIS B ND1 1 
ATOM   3154  C  CD2 . HIS B  1 117 ? -9.205  0.033   6.603   1.00 5.88   ? 117 HIS B CD2 1 
ATOM   3155  C  CE1 . HIS B  1 117 ? -7.443  1.229   6.211   1.00 6.43   ? 117 HIS B CE1 1 
ATOM   3156  N  NE2 . HIS B  1 117 ? -7.881  0.074   6.710   1.00 6.26   ? 117 HIS B NE2 1 
ATOM   3157  N  N   . ILE B  1 118 ? -14.199 0.727   6.435   1.00 5.65   ? 118 ILE B N   1 
ATOM   3158  C  CA  . ILE B  1 118 ? -15.570 1.280   6.513   1.00 6.49   ? 118 ILE B CA  1 
ATOM   3159  C  C   . ILE B  1 118 ? -15.547 2.287   7.623   1.00 6.35   ? 118 ILE B C   1 
ATOM   3160  O  O   . ILE B  1 118 ? -15.396 1.933   8.820   1.00 7.22   ? 118 ILE B O   1 
ATOM   3161  C  CB  . ILE B  1 118 ? -16.651 0.193   6.697   1.00 6.83   ? 118 ILE B CB  1 
ATOM   3162  C  CG1 . ILE B  1 118 ? -16.486 -0.947  5.711   1.00 7.55   ? 118 ILE B CG1 1 
ATOM   3163  C  CG2 . ILE B  1 118 ? -18.017 0.863   6.599   1.00 8.71   ? 118 ILE B CG2 1 
ATOM   3164  C  CD1 . ILE B  1 118 ? -17.490 -2.067  5.919   1.00 10.41  ? 118 ILE B CD1 1 
ATOM   3165  N  N   . VAL B  1 119 ? -15.653 3.552   7.283   1.00 7.10   ? 119 VAL B N   1 
ATOM   3166  C  CA  . VAL B  1 119 ? -15.430 4.648   8.169   1.00 7.96   ? 119 VAL B CA  1 
ATOM   3167  C  C   . VAL B  1 119 ? -16.760 5.096   8.793   1.00 7.79   ? 119 VAL B C   1 
ATOM   3168  O  O   . VAL B  1 119 ? -17.729 5.341   8.094   1.00 8.64   ? 119 VAL B O   1 
ATOM   3169  C  CB  . VAL B  1 119 ? -14.778 5.831   7.458   1.00 8.39   ? 119 VAL B CB  1 
ATOM   3170  C  CG1 . VAL B  1 119 ? -14.483 6.973   8.422   1.00 9.77   ? 119 VAL B CG1 1 
ATOM   3171  C  CG2 . VAL B  1 119 ? -13.544 5.390   6.646   1.00 9.97   ? 119 VAL B CG2 1 
ATOM   3172  N  N   . HIS B  1 120 ? -16.773 5.211   10.121  1.00 7.49   ? 120 HIS B N   1 
ATOM   3173  C  CA  . HIS B  1 120 ? -17.929 5.666   10.876  1.00 8.37   ? 120 HIS B CA  1 
ATOM   3174  C  C   . HIS B  1 120 ? -17.508 6.809   11.767  1.00 8.89   ? 120 HIS B C   1 
ATOM   3175  O  O   . HIS B  1 120 ? -16.332 6.915   12.153  1.00 8.80   ? 120 HIS B O   1 
ATOM   3176  C  CB  . HIS B  1 120 ? -18.488 4.510   11.736  1.00 9.05   ? 120 HIS B CB  1 
ATOM   3177  C  CG  . HIS B  1 120 ? -18.896 3.275   11.033  1.00 8.02   ? 120 HIS B CG  1 
ATOM   3178  N  ND1 . HIS B  1 120 ? -17.943 2.406   10.461  1.00 8.41   ? 120 HIS B ND1 1 
ATOM   3179  C  CD2 . HIS B  1 120 ? -20.070 2.705   10.788  1.00 8.67   ? 120 HIS B CD2 1 
ATOM   3180  C  CE1 . HIS B  1 120 ? -18.618 1.351   9.929   1.00 8.49   ? 120 HIS B CE1 1 
ATOM   3181  N  NE2 . HIS B  1 120 ? -19.903 1.504   10.136  1.00 8.90   ? 120 HIS B NE2 1 
ATOM   3182  N  N   . TYR B  1 121 ? -18.489 7.593   12.208  1.00 9.76   ? 121 TYR B N   1 
ATOM   3183  C  CA  . TYR B  1 121 ? -18.211 8.686   13.097  1.00 10.71  ? 121 TYR B CA  1 
ATOM   3184  C  C   . TYR B  1 121 ? -19.240 8.704   14.215  1.00 10.40  ? 121 TYR B C   1 
ATOM   3185  O  O   . TYR B  1 121 ? -20.328 8.172   14.101  1.00 10.87  ? 121 TYR B O   1 
ATOM   3186  C  CB  . TYR B  1 121 ? -18.206 10.071  12.392  1.00 13.51  ? 121 TYR B CB  1 
ATOM   3187  C  CG  . TYR B  1 121 ? -19.582 10.521  11.868  1.00 12.60  ? 121 TYR B CG  1 
ATOM   3188  C  CD1 . TYR B  1 121 ? -20.136 9.995   10.710  1.00 13.18  ? 121 TYR B CD1 1 
ATOM   3189  C  CD2 . TYR B  1 121 ? -20.352 11.460  12.626  1.00 15.68  ? 121 TYR B CD2 1 
ATOM   3190  C  CE1 . TYR B  1 121 ? -21.402 10.310  10.267  1.00 15.62  ? 121 TYR B CE1 1 
ATOM   3191  C  CE2 . TYR B  1 121 ? -21.602 11.820  12.150  1.00 17.87  ? 121 TYR B CE2 1 
ATOM   3192  C  CZ  . TYR B  1 121 ? -22.101 11.272  10.962  1.00 18.07  ? 121 TYR B CZ  1 
ATOM   3193  O  OH  . TYR B  1 121 ? -23.351 11.603  10.548  1.00 27.45  ? 121 TYR B OH  1 
ATOM   3194  N  N   . ASN B  1 122 ? -18.838 9.310   15.347  1.00 12.62  ? 122 ASN B N   1 
ATOM   3195  C  CA  . ASN B  1 122 ? -19.724 9.345   16.521  1.00 12.31  ? 122 ASN B CA  1 
ATOM   3196  C  C   . ASN B  1 122 ? -20.833 10.399  16.249  1.00 11.78  ? 122 ASN B C   1 
ATOM   3197  O  O   . ASN B  1 122 ? -20.618 11.617  16.465  1.00 13.97  ? 122 ASN B O   1 
ATOM   3198  C  CB  . ASN B  1 122 ? -18.934 9.669   17.743  1.00 14.20  ? 122 ASN B CB  1 
ATOM   3199  C  CG  . ASN B  1 122 ? -19.791 9.589   18.991  1.00 15.33  ? 122 ASN B CG  1 
ATOM   3200  O  OD1 . ASN B  1 122 ? -20.999 9.786   18.927  1.00 15.26  ? 122 ASN B OD1 1 
ATOM   3201  N  ND2 . ASN B  1 122 ? -19.171 9.324   20.148  1.00 20.06  ? 122 ASN B ND2 1 
ATOM   3202  N  N   . SER B  1 123 ? -21.975 9.887   15.778  1.00 12.90  ? 123 SER B N   1 
ATOM   3203  C  CA  . SER B  1 123 ? -23.107 10.754  15.404  1.00 14.29  ? 123 SER B CA  1 
ATOM   3204  C  C   . SER B  1 123 ? -23.885 11.135  16.635  1.00 15.30  ? 123 SER B C   1 
ATOM   3205  O  O   . SER B  1 123 ? -24.739 12.014  16.550  1.00 17.24  ? 123 SER B O   1 
ATOM   3206  C  CB  . SER B  1 123 ? -23.979 10.090  14.368  1.00 14.97  ? 123 SER B CB  1 
ATOM   3207  O  OG  . SER B  1 123 ? -24.256 8.792   14.783  1.00 15.35  ? 123 SER B OG  1 
ATOM   3208  N  N   . ASP B  1 124 ? -23.696 10.490  17.789  1.00 16.33  ? 124 ASP B N   1 
ATOM   3209  C  CA  . ASP B  1 124 ? -24.284 11.013  19.002  1.00 17.30  ? 124 ASP B CA  1 
ATOM   3210  C  C   . ASP B  1 124 ? -23.713 12.348  19.396  1.00 16.87  ? 124 ASP B C   1 
ATOM   3211  O  O   . ASP B  1 124 ? -24.448 13.171  19.967  1.00 18.97  ? 124 ASP B O   1 
ATOM   3212  C  CB  . ASP B  1 124 ? -24.110 10.044  20.154  1.00 19.17  ? 124 ASP B CB  1 
ATOM   3213  C  CG  . ASP B  1 124 ? -24.960 8.798   19.990  1.00 20.41  ? 124 ASP B CG  1 
ATOM   3214  O  OD1 . ASP B  1 124 ? -25.958 8.768   19.211  1.00 22.21  ? 124 ASP B OD1 1 
ATOM   3215  O  OD2 . ASP B  1 124 ? -24.621 7.768   20.640  1.00 21.02  ? 124 ASP B OD2 1 
ATOM   3216  N  N   . LEU B  1 125 ? -22.415 12.539  19.149  1.00 16.52  ? 125 LEU B N   1 
ATOM   3217  C  CA  . LEU B  1 125 ? -21.702 13.707  19.628  1.00 15.78  ? 125 LEU B CA  1 
ATOM   3218  C  C   . LEU B  1 125 ? -21.506 14.752  18.539  1.00 17.22  ? 125 LEU B C   1 
ATOM   3219  O  O   . LEU B  1 125 ? -21.425 15.941  18.877  1.00 21.47  ? 125 LEU B O   1 
ATOM   3220  C  CB  . LEU B  1 125 ? -20.367 13.375  20.250  1.00 18.05  ? 125 LEU B CB  1 
ATOM   3221  C  CG  . LEU B  1 125 ? -20.413 12.427  21.479  1.00 21.06  ? 125 LEU B CG  1 
ATOM   3222  C  CD1 . LEU B  1 125 ? -19.028 12.138  22.067  1.00 22.00  ? 125 LEU B CD1 1 
ATOM   3223  C  CD2 . LEU B  1 125 ? -21.330 13.001  22.596  1.00 22.87  ? 125 LEU B CD2 1 
ATOM   3224  N  N   . TYR B  1 126 ? -21.342 14.356  17.252  1.00 14.92  ? 126 TYR B N   1 
ATOM   3225  C  CA  . TYR B  1 126 ? -20.960 15.275  16.224  1.00 16.17  ? 126 TYR B CA  1 
ATOM   3226  C  C   . TYR B  1 126 ? -21.865 15.246  15.054  1.00 17.02  ? 126 TYR B C   1 
ATOM   3227  O  O   . TYR B  1 126 ? -22.445 14.181  14.781  1.00 18.18  ? 126 TYR B O   1 
ATOM   3228  C  CB  . TYR B  1 126 ? -19.509 14.876  15.792  1.00 17.10  ? 126 TYR B CB  1 
ATOM   3229  C  CG  . TYR B  1 126 ? -18.569 14.794  16.948  1.00 17.54  ? 126 TYR B CG  1 
ATOM   3230  C  CD1 . TYR B  1 126 ? -18.299 15.916  17.692  1.00 22.51  ? 126 TYR B CD1 1 
ATOM   3231  C  CD2 . TYR B  1 126 ? -17.994 13.571  17.290  1.00 17.21  ? 126 TYR B CD2 1 
ATOM   3232  C  CE1 . TYR B  1 126 ? -17.495 15.821  18.800  1.00 26.06  ? 126 TYR B CE1 1 
ATOM   3233  C  CE2 . TYR B  1 126 ? -17.186 13.435  18.370  1.00 19.24  ? 126 TYR B CE2 1 
ATOM   3234  C  CZ  . TYR B  1 126 ? -16.963 14.581  19.150  1.00 22.57  ? 126 TYR B CZ  1 
ATOM   3235  O  OH  . TYR B  1 126 ? -16.129 14.484  20.234  1.00 26.03  ? 126 TYR B OH  1 
ATOM   3236  N  N   . PRO B  1 127 ? -21.927 16.357  14.307  1.00 21.38  ? 127 PRO B N   1 
ATOM   3237  C  CA  . PRO B  1 127 ? -22.922 16.396  13.230  1.00 23.18  ? 127 PRO B CA  1 
ATOM   3238  C  C   . PRO B  1 127 ? -22.441 15.816  11.929  1.00 20.57  ? 127 PRO B C   1 
ATOM   3239  O  O   . PRO B  1 127 ? -23.230 15.659  11.025  1.00 24.72  ? 127 PRO B O   1 
ATOM   3240  C  CB  . PRO B  1 127 ? -23.154 17.917  13.028  1.00 26.32  ? 127 PRO B CB  1 
ATOM   3241  C  CG  . PRO B  1 127 ? -21.969 18.587  13.593  1.00 31.38  ? 127 PRO B CG  1 
ATOM   3242  C  CD  . PRO B  1 127 ? -21.468 17.721  14.684  1.00 24.88  ? 127 PRO B CD  1 
ATOM   3243  N  N   . ASP B  1 128 ? -21.145 15.514  11.842  1.00 18.87  ? 128 ASP B N   1 
ATOM   3244  C  CA  . ASP B  1 128 ? -20.600 15.030  10.605  1.00 16.77  ? 128 ASP B CA  1 
ATOM   3245  C  C   . ASP B  1 128 ? -19.187 14.422  10.938  1.00 15.95  ? 128 ASP B C   1 
ATOM   3246  O  O   . ASP B  1 128 ? -18.616 14.666  11.990  1.00 17.43  ? 128 ASP B O   1 
ATOM   3247  C  CB  . ASP B  1 128 ? -20.406 16.215  9.634   1.00 20.35  ? 128 ASP B CB  1 
ATOM   3248  C  CG  . ASP B  1 128 ? -19.475 17.275  10.154  1.00 20.97  ? 128 ASP B CG  1 
ATOM   3249  O  OD1 . ASP B  1 128 ? -19.917 18.123  10.955  1.00 36.48  ? 128 ASP B OD1 1 
ATOM   3250  O  OD2 . ASP B  1 128 ? -18.310 17.292  9.713   1.00 30.13  ? 128 ASP B OD2 1 
ATOM   3251  N  N   . ALA B  1 129 ? -18.675 13.597  10.006  1.00 16.44  ? 129 ALA B N   1 
ATOM   3252  C  CA  . ALA B  1 129 ? -17.400 12.938  10.201  1.00 15.59  ? 129 ALA B CA  1 
ATOM   3253  C  C   . ALA B  1 129 ? -16.214 13.898  10.244  1.00 14.55  ? 129 ALA B C   1 
ATOM   3254  O  O   . ALA B  1 129 ? -15.254 13.654  10.970  1.00 16.38  ? 129 ALA B O   1 
ATOM   3255  C  CB  . ALA B  1 129 ? -17.192 11.932  9.090   1.00 16.78  ? 129 ALA B CB  1 
ATOM   3256  N  N   A SER B  1 130 ? -16.263 14.999  9.494   0.50 18.02  ? 130 SER B N   1 
ATOM   3257  N  N   B SER B  1 130 ? -16.253 15.002  9.486   0.50 18.38  ? 130 SER B N   1 
ATOM   3258  C  CA  A SER B  1 130 ? -15.103 15.927  9.489   0.50 18.29  ? 130 SER B CA  1 
ATOM   3259  C  CA  B SER B  1 130 ? -15.093 15.939  9.524   0.50 20.30  ? 130 SER B CA  1 
ATOM   3260  C  C   A SER B  1 130 ? -14.909 16.583  10.863  0.50 19.09  ? 130 SER B C   1 
ATOM   3261  C  C   B SER B  1 130 ? -14.911 16.471  10.930  0.50 19.70  ? 130 SER B C   1 
ATOM   3262  O  O   A SER B  1 130 ? -13.761 16.709  11.366  0.50 22.71  ? 130 SER B O   1 
ATOM   3263  O  O   B SER B  1 130 ? -13.785 16.432  11.514  0.50 18.86  ? 130 SER B O   1 
ATOM   3264  C  CB  A SER B  1 130 ? -15.293 17.014  8.423   0.50 19.73  ? 130 SER B CB  1 
ATOM   3265  C  CB  B SER B  1 130 ? -15.277 17.148  8.595   0.50 23.38  ? 130 SER B CB  1 
ATOM   3266  O  OG  A SER B  1 130 ? -14.207 17.928  8.371   0.50 26.32  ? 130 SER B OG  1 
ATOM   3267  O  OG  B SER B  1 130 ? -15.362 16.766  7.234   0.50 30.85  ? 130 SER B OG  1 
ATOM   3268  N  N   . THR B  1 131 ? -16.017 16.932  11.503  1.00 21.63  ? 131 THR B N   1 
ATOM   3269  C  CA  . THR B  1 131 ? -15.967 17.369  12.933  1.00 21.73  ? 131 THR B CA  1 
ATOM   3270  C  C   . THR B  1 131 ? -15.458 16.318  13.857  1.00 20.37  ? 131 THR B C   1 
ATOM   3271  O  O   . THR B  1 131 ? -14.615 16.606  14.718  1.00 23.27  ? 131 THR B O   1 
ATOM   3272  C  CB  . THR B  1 131 ? -17.355 17.816  13.448  1.00 23.53  ? 131 THR B CB  1 
ATOM   3273  O  OG1 . THR B  1 131 ? -17.794 18.892  12.631  1.00 26.66  ? 131 THR B OG1 1 
ATOM   3274  C  CG2 . THR B  1 131 ? -17.288 18.351  14.919  1.00 33.24  ? 131 THR B CG2 1 
ATOM   3275  N  N   . ALA B  1 132 ? -16.003 15.109  13.721  1.00 17.86  ? 132 ALA B N   1 
ATOM   3276  C  CA  . ALA B  1 132 ? -15.670 14.016  14.624  1.00 17.75  ? 132 ALA B CA  1 
ATOM   3277  C  C   . ALA B  1 132 ? -14.177 13.725  14.520  1.00 17.22  ? 132 ALA B C   1 
ATOM   3278  O  O   . ALA B  1 132 ? -13.553 13.254  15.487  1.00 18.14  ? 132 ALA B O   1 
ATOM   3279  C  CB  . ALA B  1 132 ? -16.500 12.815  14.219  1.00 16.12  ? 132 ALA B CB  1 
ATOM   3280  N  N   . SER B  1 133 ? -13.640 13.923  13.304  1.00 17.66  ? 133 SER B N   1 
ATOM   3281  C  CA  . SER B  1 133 ? -12.276 13.427  12.969  1.00 16.53  ? 133 SER B CA  1 
ATOM   3282  C  C   . SER B  1 133 ? -11.192 14.080  13.684  1.00 17.17  ? 133 SER B C   1 
ATOM   3283  O  O   . SER B  1 133 ? -10.084 13.561  13.771  1.00 19.10  ? 133 SER B O   1 
ATOM   3284  C  CB  . SER B  1 133 ? -11.977 13.536  11.501  1.00 19.84  ? 133 SER B CB  1 
ATOM   3285  O  OG  . SER B  1 133 ? -11.716 14.863  11.141  1.00 20.69  ? 133 SER B OG  1 
ATOM   3286  N  N   A ASN B  1 134 ? -11.466 15.254  14.222  0.50 21.42  ? 134 ASN B N   1 
ATOM   3287  N  N   B ASN B  1 134 ? -11.460 15.218  14.266  0.50 19.66  ? 134 ASN B N   1 
ATOM   3288  C  CA  A ASN B  1 134 ? -10.462 15.878  15.101  0.50 23.00  ? 134 ASN B CA  1 
ATOM   3289  C  CA  B ASN B  1 134 ? -10.403 15.770  15.097  0.50 26.61  ? 134 ASN B CA  1 
ATOM   3290  C  C   A ASN B  1 134 ? -10.766 15.826  16.598  0.50 24.25  ? 134 ASN B C   1 
ATOM   3291  C  C   B ASN B  1 134 ? -10.686 15.710  16.583  0.50 25.23  ? 134 ASN B C   1 
ATOM   3292  O  O   A ASN B  1 134 ? -10.202 16.561  17.368  0.50 33.73  ? 134 ASN B O   1 
ATOM   3293  O  O   B ASN B  1 134 ? -10.086 16.416  17.338  0.50 26.72  ? 134 ASN B O   1 
ATOM   3294  C  CB  A ASN B  1 134 ? -9.649  17.073  14.523  0.50 37.96  ? 134 ASN B CB  1 
ATOM   3295  C  CB  B ASN B  1 134 ? -9.822  17.082  14.573  0.50 41.82  ? 134 ASN B CB  1 
ATOM   3296  C  CG  A ASN B  1 134 ? -10.515 18.224  14.060  0.50 47.90  ? 134 ASN B CG  1 
ATOM   3297  C  CG  B ASN B  1 134 ? -10.886 18.117  14.318  0.50 59.75  ? 134 ASN B CG  1 
ATOM   3298  O  OD1 A ASN B  1 134 ? -11.680 18.070  13.628  0.50 80.05  ? 134 ASN B OD1 1 
ATOM   3299  O  OD1 B ASN B  1 134 ? -11.935 17.857  13.711  0.50 78.77  ? 134 ASN B OD1 1 
ATOM   3300  N  ND2 A ASN B  1 134 ? -9.933  19.418  14.176  0.50 33.94  ? 134 ASN B ND2 1 
ATOM   3301  N  ND2 B ASN B  1 134 ? -10.607 19.328  14.783  0.50 49.27  ? 134 ASN B ND2 1 
ATOM   3302  N  N   A LYS B  1 135 ? -11.569 14.817  16.996  0.50 22.37  ? 135 LYS B N   1 
ATOM   3303  N  N   B LYS B  1 135 ? -11.580 14.794  16.992  0.50 22.37  ? 135 LYS B N   1 
ATOM   3304  C  CA  A LYS B  1 135 ? -11.952 14.603  18.428  0.50 24.58  ? 135 LYS B CA  1 
ATOM   3305  C  CA  B LYS B  1 135 ? -11.884 14.590  18.436  0.50 25.09  ? 135 LYS B CA  1 
ATOM   3306  C  C   A LYS B  1 135 ? -11.553 13.218  18.931  0.50 26.32  ? 135 LYS B C   1 
ATOM   3307  C  C   B LYS B  1 135 ? -11.552 13.200  18.929  0.50 26.54  ? 135 LYS B C   1 
ATOM   3308  O  O   A LYS B  1 135 ? -11.682 12.288  18.174  0.50 20.52  ? 135 LYS B O   1 
ATOM   3309  O  O   B LYS B  1 135 ? -11.734 12.264  18.183  0.50 20.89  ? 135 LYS B O   1 
ATOM   3310  C  CB  A LYS B  1 135 ? -13.448 14.698  18.502  0.50 25.11  ? 135 LYS B CB  1 
ATOM   3311  C  CG  A LYS B  1 135 ? -13.958 16.016  17.866  0.50 29.95  ? 135 LYS B CG  1 
ATOM   3312  N  N   . SER B  1 136 ? -11.074 13.029  20.164  1.00 37.60  ? 136 SER B N   1 
ATOM   3313  C  CA  . SER B  1 136 ? -10.603 11.676  20.544  1.00 27.91  ? 136 SER B CA  1 
ATOM   3314  C  C   . SER B  1 136 ? -11.742 10.602  20.401  1.00 25.57  ? 136 SER B C   1 
ATOM   3315  O  O   . SER B  1 136 ? -12.891 10.847  20.743  1.00 20.34  ? 136 SER B O   1 
ATOM   3316  N  N   . GLU B  1 137 ? -11.461 9.438   19.839  1.00 21.87  ? 137 GLU B N   1 
ATOM   3317  C  CA  . GLU B  1 137 ? -12.495 8.383   19.632  1.00 22.59  ? 137 GLU B CA  1 
ATOM   3318  C  C   . GLU B  1 137 ? -13.679 8.901   18.779  1.00 19.07  ? 137 GLU B C   1 
ATOM   3319  O  O   . GLU B  1 137 ? -14.773 8.317   18.831  1.00 19.59  ? 137 GLU B O   1 
ATOM   3320  C  CB  . GLU B  1 137 ? -13.012 7.731   20.928  1.00 31.80  ? 137 GLU B CB  1 
ATOM   3321  C  CG  . GLU B  1 137 ? -11.934 7.037   21.748  1.00 43.65  ? 137 GLU B CG  1 
ATOM   3322  C  CD  . GLU B  1 137 ? -12.506 6.194   22.875  1.00 54.85  ? 137 GLU B CD  1 
ATOM   3323  O  OE1 . GLU B  1 137 ? -13.752 6.018   22.982  1.00 70.31  ? 137 GLU B OE1 1 
ATOM   3324  O  OE2 . GLU B  1 137 ? -11.697 5.703   23.652  1.00 48.30  ? 137 GLU B OE2 1 
ATOM   3325  N  N   . GLY B  1 138 ? -13.488 10.014  18.026  1.00 16.99  ? 138 GLY B N   1 
ATOM   3326  C  CA  . GLY B  1 138 ? -14.537 10.541  17.136  1.00 14.34  ? 138 GLY B CA  1 
ATOM   3327  C  C   . GLY B  1 138 ? -14.901 9.626   15.972  1.00 12.24  ? 138 GLY B C   1 
ATOM   3328  O  O   . GLY B  1 138 ? -15.992 9.726   15.454  1.00 13.92  ? 138 GLY B O   1 
ATOM   3329  N  N   . LEU B  1 139 ? -13.958 8.793   15.579  1.00 10.59  ? 139 LEU B N   1 
ATOM   3330  C  CA  . LEU B  1 139 ? -14.175 7.907   14.448  1.00 10.44  ? 139 LEU B CA  1 
ATOM   3331  C  C   . LEU B  1 139 ? -14.010 6.489   14.862  1.00 9.04   ? 139 LEU B C   1 
ATOM   3332  O  O   . LEU B  1 139 ? -13.264 6.157   15.790  1.00 10.35  ? 139 LEU B O   1 
ATOM   3333  C  CB  . LEU B  1 139 ? -13.094 8.191   13.375  1.00 10.61  ? 139 LEU B CB  1 
ATOM   3334  C  CG  . LEU B  1 139 ? -13.167 9.589   12.764  1.00 11.83  ? 139 LEU B CG  1 
ATOM   3335  C  CD1 . LEU B  1 139 ? -11.958 9.790   11.872  1.00 13.05  ? 139 LEU B CD1 1 
ATOM   3336  C  CD2 . LEU B  1 139 ? -14.458 9.907   12.048  1.00 11.94  ? 139 LEU B CD2 1 
ATOM   3337  N  N   . ALA B  1 140 ? -14.708 5.599   14.149  1.00 9.41   ? 140 ALA B N   1 
ATOM   3338  C  CA  . ALA B  1 140 ? -14.514 4.138   14.337  1.00 9.00   ? 140 ALA B CA  1 
ATOM   3339  C  C   . ALA B  1 140 ? -14.432 3.592   12.931  1.00 8.41   ? 140 ALA B C   1 
ATOM   3340  O  O   . ALA B  1 140 ? -15.340 3.786   12.097  1.00 9.05   ? 140 ALA B O   1 
ATOM   3341  C  CB  . ALA B  1 140 ? -15.733 3.494   15.066  1.00 10.09  ? 140 ALA B CB  1 
ATOM   3342  N  N   . VAL B  1 141 ? -13.340 2.881   12.640  1.00 7.28   ? 141 VAL B N   1 
ATOM   3343  C  CA  . VAL B  1 141 ? -13.117 2.303   11.328  1.00 6.83   ? 141 VAL B CA  1 
ATOM   3344  C  C   . VAL B  1 141 ? -13.128 0.812   11.470  1.00 6.17   ? 141 VAL B C   1 
ATOM   3345  O  O   . VAL B  1 141 ? -12.483 0.271   12.368  1.00 7.21   ? 141 VAL B O   1 
ATOM   3346  C  CB  . VAL B  1 141 ? -11.843 2.845   10.631  1.00 7.86   ? 141 VAL B CB  1 
ATOM   3347  C  CG1 . VAL B  1 141 ? -11.711 2.217   9.246   1.00 8.68   ? 141 VAL B CG1 1 
ATOM   3348  C  CG2 . VAL B  1 141 ? -11.872 4.349   10.543  1.00 9.07   ? 141 VAL B CG2 1 
ATOM   3349  N  N   . LEU B  1 142 ? -13.847 0.143   10.575  1.00 6.00   ? 142 LEU B N   1 
ATOM   3350  C  CA  . LEU B  1 142 ? -13.803 -1.287  10.449  1.00 6.52   ? 142 LEU B CA  1 
ATOM   3351  C  C   . LEU B  1 142 ? -12.821 -1.625  9.332   1.00 5.92   ? 142 LEU B C   1 
ATOM   3352  O  O   . LEU B  1 142 ? -12.960 -1.079  8.226   1.00 7.30   ? 142 LEU B O   1 
ATOM   3353  C  CB  . LEU B  1 142 ? -15.140 -1.870  10.109  1.00 7.60   ? 142 LEU B CB  1 
ATOM   3354  C  CG  . LEU B  1 142 ? -16.293 -1.548  11.029  1.00 8.57   ? 142 LEU B CG  1 
ATOM   3355  C  CD1 . LEU B  1 142 ? -17.571 -2.229  10.522  1.00 10.24  ? 142 LEU B CD1 1 
ATOM   3356  C  CD2 . LEU B  1 142 ? -16.026 -1.952  12.462  1.00 9.82   ? 142 LEU B CD2 1 
ATOM   3357  N  N   . ALA B  1 143 ? -11.895 -2.545  9.587   1.00 6.30   ? 143 ALA B N   1 
ATOM   3358  C  CA  . ALA B  1 143 ? -10.925 -2.967  8.586   1.00 6.08   ? 143 ALA B CA  1 
ATOM   3359  C  C   . ALA B  1 143 ? -11.148 -4.422  8.258   1.00 5.66   ? 143 ALA B C   1 
ATOM   3360  O  O   . ALA B  1 143 ? -11.195 -5.277  9.152   1.00 6.64   ? 143 ALA B O   1 
ATOM   3361  C  CB  . ALA B  1 143 ? -9.515  -2.760  9.083   1.00 6.82   ? 143 ALA B CB  1 
ATOM   3362  N  N   . VAL B  1 144 ? -11.222 -4.695  6.958   1.00 5.73   ? 144 VAL B N   1 
ATOM   3363  C  CA  . VAL B  1 144 ? -11.313 -6.048  6.460   1.00 6.15   ? 144 VAL B CA  1 
ATOM   3364  C  C   . VAL B  1 144 ? -10.058 -6.306  5.644   1.00 6.16   ? 144 VAL B C   1 
ATOM   3365  O  O   . VAL B  1 144 ? -9.780  -5.599  4.662   1.00 6.67   ? 144 VAL B O   1 
ATOM   3366  C  CB  . VAL B  1 144 ? -12.575 -6.278  5.575   1.00 7.23   ? 144 VAL B CB  1 
ATOM   3367  C  CG1 . VAL B  1 144 ? -12.634 -7.724  5.076   1.00 8.35   ? 144 VAL B CG1 1 
ATOM   3368  C  CG2 . VAL B  1 144 ? -13.864 -5.892  6.298   1.00 8.37   ? 144 VAL B CG2 1 
ATOM   3369  N  N   . LEU B  1 145 ? -9.325  -7.359  6.024   1.00 6.55   ? 145 LEU B N   1 
ATOM   3370  C  CA  . LEU B  1 145 ? -8.162  -7.816  5.318   1.00 6.83   ? 145 LEU B CA  1 
ATOM   3371  C  C   . LEU B  1 145 ? -8.629  -8.597  4.115   1.00 6.42   ? 145 LEU B C   1 
ATOM   3372  O  O   . LEU B  1 145 ? -9.575  -9.415  4.193   1.00 7.56   ? 145 LEU B O   1 
ATOM   3373  C  CB  . LEU B  1 145 ? -7.294  -8.671  6.219   1.00 7.59   ? 145 LEU B CB  1 
ATOM   3374  C  CG  . LEU B  1 145 ? -6.773  -7.922  7.445   1.00 9.17   ? 145 LEU B CG  1 
ATOM   3375  C  CD1 . LEU B  1 145 ? -6.263  -8.949  8.481   1.00 11.71  ? 145 LEU B CD1 1 
ATOM   3376  C  CD2 . LEU B  1 145 ? -5.732  -6.884  7.037   1.00 12.57  ? 145 LEU B CD2 1 
ATOM   3377  N  N   . ILE B  1 146 ? -7.994  -8.375  2.943   1.00 6.93   ? 146 ILE B N   1 
ATOM   3378  C  CA  . ILE B  1 146 ? -8.410  -9.016  1.665   1.00 7.21   ? 146 ILE B CA  1 
ATOM   3379  C  C   . ILE B  1 146 ? -7.256  -9.841  1.143   1.00 6.99   ? 146 ILE B C   1 
ATOM   3380  O  O   . ILE B  1 146 ? -6.156  -9.322  0.967   1.00 8.05   ? 146 ILE B O   1 
ATOM   3381  C  CB  . ILE B  1 146 ? -8.852  -7.933  0.656   1.00 7.44   ? 146 ILE B CB  1 
ATOM   3382  C  CG1 . ILE B  1 146 ? -10.027 -7.131  1.169   1.00 8.07   ? 146 ILE B CG1 1 
ATOM   3383  C  CG2 . ILE B  1 146 ? -9.128  -8.569  -0.692  1.00 8.45   ? 146 ILE B CG2 1 
ATOM   3384  C  CD1 . ILE B  1 146 ? -10.275 -5.869  0.379   1.00 8.57   ? 146 ILE B CD1 1 
ATOM   3385  N  N   . GLU B  1 147 ? -7.539  -11.099 0.859   1.00 8.15   ? 147 GLU B N   1 
ATOM   3386  C  CA  . GLU B  1 147 ? -6.526  -11.985 0.285   1.00 9.33   ? 147 GLU B CA  1 
ATOM   3387  C  C   . GLU B  1 147 ? -6.953  -12.368 -1.131  1.00 7.79   ? 147 GLU B C   1 
ATOM   3388  O  O   . GLU B  1 147 ? -8.133  -12.362 -1.492  1.00 9.13   ? 147 GLU B O   1 
ATOM   3389  C  CB  . GLU B  1 147 ? -6.306  -13.209 1.188   1.00 15.50  ? 147 GLU B CB  1 
ATOM   3390  C  CG  . GLU B  1 147 ? -7.381  -14.186 1.269   1.00 19.82  ? 147 GLU B CG  1 
ATOM   3391  C  CD  . GLU B  1 147 ? -7.096  -15.334 2.219   1.00 25.45  ? 147 GLU B CD  1 
ATOM   3392  O  OE1 . GLU B  1 147 ? -6.083  -15.284 2.946   1.00 25.36  ? 147 GLU B OE1 1 
ATOM   3393  O  OE2 . GLU B  1 147 ? -7.894  -16.294 2.233   1.00 36.07  ? 147 GLU B OE2 1 
ATOM   3394  N  N   . MET B  1 148 ? -5.963  -12.739 -1.961  1.00 8.16   ? 148 MET B N   1 
ATOM   3395  C  CA  . MET B  1 148 ? -6.266  -13.269 -3.283  1.00 8.26   ? 148 MET B CA  1 
ATOM   3396  C  C   . MET B  1 148 ? -6.868  -14.642 -3.159  1.00 8.37   ? 148 MET B C   1 
ATOM   3397  O  O   . MET B  1 148 ? -6.287  -15.531 -2.558  1.00 10.42  ? 148 MET B O   1 
ATOM   3398  C  CB  . MET B  1 148 ? -4.980  -13.283 -4.102  1.00 9.92   ? 148 MET B CB  1 
ATOM   3399  C  CG  . MET B  1 148 ? -5.176  -13.679 -5.533  1.00 11.41  ? 148 MET B CG  1 
ATOM   3400  S  SD  . MET B  1 148 ? -3.696  -13.780 -6.516  1.00 14.06  ? 148 MET B SD  1 
ATOM   3401  C  CE  . MET B  1 148 ? -3.232  -12.063 -6.494  1.00 15.15  ? 148 MET B CE  1 
ATOM   3402  N  N   . GLY B  1 149 ? -8.018  -14.841 -3.795  1.00 8.79   ? 149 GLY B N   1 
ATOM   3403  C  CA  . GLY B  1 149 ? -8.730  -16.129 -3.662  1.00 9.61   ? 149 GLY B CA  1 
ATOM   3404  C  C   . GLY B  1 149 ? -9.842  -16.168 -4.687  1.00 8.49   ? 149 GLY B C   1 
ATOM   3405  O  O   . GLY B  1 149 ? -9.655  -15.889 -5.872  1.00 9.10   ? 149 GLY B O   1 
ATOM   3406  N  N   . SER B  1 150 ? -11.017 -16.568 -4.256  1.00 9.35   ? 150 SER B N   1 
ATOM   3407  C  CA  . SER B  1 150 ? -12.143 -16.666 -5.129  1.00 9.14   ? 150 SER B CA  1 
ATOM   3408  C  C   . SER B  1 150 ? -12.709 -15.320 -5.525  1.00 9.52   ? 150 SER B C   1 
ATOM   3409  O  O   . SER B  1 150 ? -12.637 -14.338 -4.770  1.00 10.30  ? 150 SER B O   1 
ATOM   3410  C  CB  . SER B  1 150 ? -13.260 -17.459 -4.428  1.00 10.10  ? 150 SER B CB  1 
ATOM   3411  O  OG  . SER B  1 150 ? -12.890 -18.810 -4.258  1.00 10.25  ? 150 SER B OG  1 
ATOM   3412  N  N   . PHE B  1 151 ? -13.322 -15.288 -6.714  1.00 10.23  ? 151 PHE B N   1 
ATOM   3413  C  CA  . PHE B  1 151 ? -14.086 -14.125 -7.140  1.00 9.68   ? 151 PHE B CA  1 
ATOM   3414  C  C   . PHE B  1 151 ? -15.115 -13.776 -6.117  1.00 9.96   ? 151 PHE B C   1 
ATOM   3415  O  O   . PHE B  1 151 ? -15.806 -14.652 -5.575  1.00 11.67  ? 151 PHE B O   1 
ATOM   3416  C  CB  . PHE B  1 151 ? -14.698 -14.455 -8.493  1.00 11.09  ? 151 PHE B CB  1 
ATOM   3417  C  CG  . PHE B  1 151 ? -15.545 -13.310 -9.020  1.00 10.94  ? 151 PHE B CG  1 
ATOM   3418  C  CD1 . PHE B  1 151 ? -14.930 -12.221 -9.673  1.00 12.15  ? 151 PHE B CD1 1 
ATOM   3419  C  CD2 . PHE B  1 151 ? -16.937 -13.321 -8.925  1.00 12.58  ? 151 PHE B CD2 1 
ATOM   3420  C  CE1 . PHE B  1 151 ? -15.670 -11.157 -10.129 1.00 13.23  ? 151 PHE B CE1 1 
ATOM   3421  C  CE2 . PHE B  1 151 ? -17.702 -12.264 -9.412  1.00 13.85  ? 151 PHE B CE2 1 
ATOM   3422  C  CZ  . PHE B  1 151 ? -17.037 -11.183 -9.985  1.00 13.45  ? 151 PHE B CZ  1 
ATOM   3423  N  N   . ASN B  1 152 ? -15.286 -12.495 -5.863  1.00 9.01   ? 152 ASN B N   1 
ATOM   3424  C  CA  . ASN B  1 152 ? -16.201 -12.047 -4.859  1.00 8.98   ? 152 ASN B CA  1 
ATOM   3425  C  C   . ASN B  1 152 ? -17.289 -11.161 -5.475  1.00 9.17   ? 152 ASN B C   1 
ATOM   3426  O  O   . ASN B  1 152 ? -16.998 -9.982  -5.802  1.00 8.99   ? 152 ASN B O   1 
ATOM   3427  C  CB  . ASN B  1 152 ? -15.418 -11.293 -3.772  1.00 8.96   ? 152 ASN B CB  1 
ATOM   3428  C  CG  . ASN B  1 152 ? -16.246 -11.028 -2.567  1.00 9.09   ? 152 ASN B CG  1 
ATOM   3429  O  OD1 . ASN B  1 152 ? -17.350 -10.503 -2.665  1.00 10.14  ? 152 ASN B OD1 1 
ATOM   3430  N  ND2 . ASN B  1 152 ? -15.675 -11.322 -1.386  1.00 9.05   ? 152 ASN B ND2 1 
ATOM   3431  N  N   . PRO B  1 153 ? -18.478 -11.648 -5.701  1.00 9.88   ? 153 PRO B N   1 
ATOM   3432  C  CA  . PRO B  1 153 ? -19.515 -10.865 -6.366  1.00 11.91  ? 153 PRO B CA  1 
ATOM   3433  C  C   . PRO B  1 153 ? -19.820 -9.592  -5.607  1.00 10.11  ? 153 PRO B C   1 
ATOM   3434  O  O   . PRO B  1 153 ? -20.197 -8.581  -6.228  1.00 11.81  ? 153 PRO B O   1 
ATOM   3435  C  CB  . PRO B  1 153 ? -20.721 -11.836 -6.431  1.00 14.57  ? 153 PRO B CB  1 
ATOM   3436  C  CG  . PRO B  1 153 ? -20.136 -13.165 -6.354  1.00 18.84  ? 153 PRO B CG  1 
ATOM   3437  C  CD  . PRO B  1 153 ? -18.915 -13.059 -5.504  1.00 13.26  ? 153 PRO B CD  1 
ATOM   3438  N  N   . SER B  1 154 ? -19.753 -9.629  -4.301  1.00 10.23  ? 154 SER B N   1 
ATOM   3439  C  CA  . SER B  1 154 ? -20.138 -8.459  -3.516  1.00 10.50  ? 154 SER B CA  1 
ATOM   3440  C  C   . SER B  1 154 ? -19.139 -7.318  -3.698  1.00 9.26   ? 154 SER B C   1 
ATOM   3441  O  O   . SER B  1 154 ? -19.520 -6.169  -3.929  1.00 9.90   ? 154 SER B O   1 
ATOM   3442  C  CB  . SER B  1 154 ? -20.288 -8.809  -2.044  1.00 12.11  ? 154 SER B CB  1 
ATOM   3443  O  OG  . SER B  1 154 ? -21.258 -9.840  -1.893  1.00 17.56  ? 154 SER B OG  1 
ATOM   3444  N  N   . TYR B  1 155 ? -17.836 -7.585  -3.615  1.00 8.44   ? 155 TYR B N   1 
ATOM   3445  C  CA  . TYR B  1 155 ? -16.861 -6.554  -3.894  1.00 8.40   ? 155 TYR B CA  1 
ATOM   3446  C  C   . TYR B  1 155 ? -16.986 -6.109  -5.331  1.00 8.21   ? 155 TYR B C   1 
ATOM   3447  O  O   . TYR B  1 155 ? -16.689 -4.939  -5.638  1.00 8.86   ? 155 TYR B O   1 
ATOM   3448  C  CB  . TYR B  1 155 ? -15.425 -7.050  -3.566  1.00 8.45   ? 155 TYR B CB  1 
ATOM   3449  C  CG  . TYR B  1 155 ? -15.095 -6.951  -2.122  1.00 7.28   ? 155 TYR B CG  1 
ATOM   3450  C  CD1 . TYR B  1 155 ? -15.497 -7.933  -1.203  1.00 8.42   ? 155 TYR B CD1 1 
ATOM   3451  C  CD2 . TYR B  1 155 ? -14.349 -5.841  -1.643  1.00 8.56   ? 155 TYR B CD2 1 
ATOM   3452  C  CE1 . TYR B  1 155 ? -15.239 -7.799  0.150   1.00 8.12   ? 155 TYR B CE1 1 
ATOM   3453  C  CE2 . TYR B  1 155 ? -14.042 -5.728  -0.294  1.00 9.07   ? 155 TYR B CE2 1 
ATOM   3454  C  CZ  . TYR B  1 155 ? -14.532 -6.695  0.592   1.00 8.00   ? 155 TYR B CZ  1 
ATOM   3455  O  OH  . TYR B  1 155 ? -14.211 -6.549  1.918   1.00 8.57   ? 155 TYR B OH  1 
ATOM   3456  N  N   . ASP B  1 156 ? -17.392 -6.983  -6.244  1.00 8.56   ? 156 ASP B N   1 
ATOM   3457  C  CA  . ASP B  1 156 ? -17.512 -6.567  -7.593  1.00 9.43   ? 156 ASP B CA  1 
ATOM   3458  C  C   . ASP B  1 156 ? -18.607 -5.524  -7.811  1.00 10.07  ? 156 ASP B C   1 
ATOM   3459  O  O   . ASP B  1 156 ? -18.601 -4.792  -8.804  1.00 10.97  ? 156 ASP B O   1 
ATOM   3460  C  CB  . ASP B  1 156 ? -17.689 -7.753  -8.604  1.00 12.55  ? 156 ASP B CB  1 
ATOM   3461  C  CG  . ASP B  1 156 ? -16.733 -7.571  -9.786  1.00 11.99  ? 156 ASP B CG  1 
ATOM   3462  O  OD1 . ASP B  1 156 ? -15.488 -7.349  -9.539  1.00 11.35  ? 156 ASP B OD1 1 
ATOM   3463  O  OD2 . ASP B  1 156 ? -17.214 -7.637  -10.923 1.00 17.44  ? 156 ASP B OD2 1 
ATOM   3464  N  N   . LYS B  1 157 ? -19.578 -5.426  -6.879  1.00 9.75   ? 157 LYS B N   1 
ATOM   3465  C  CA  . LYS B  1 157 ? -20.576 -4.354  -6.964  1.00 11.16  ? 157 LYS B CA  1 
ATOM   3466  C  C   . LYS B  1 157 ? -19.920 -2.979  -6.866  1.00 9.99   ? 157 LYS B C   1 
ATOM   3467  O  O   . LYS B  1 157 ? -20.420 -2.025  -7.444  1.00 13.89  ? 157 LYS B O   1 
ATOM   3468  C  CB  . LYS B  1 157 ? -21.596 -4.527  -5.843  1.00 11.49  ? 157 LYS B CB  1 
ATOM   3469  C  CG  . LYS B  1 157 ? -22.421 -5.806  -6.041  1.00 14.29  ? 157 LYS B CG  1 
ATOM   3470  C  CD  . LYS B  1 157 ? -23.431 -6.174  -4.977  1.00 16.67  ? 157 LYS B CD  1 
ATOM   3471  C  CE  . LYS B  1 157 ? -24.048 -7.509  -5.282  1.00 19.55  ? 157 LYS B CE  1 
ATOM   3472  N  NZ  . LYS B  1 157 ? -24.939 -7.933  -4.119  1.00 20.39  ? 157 LYS B NZ  1 
ATOM   3473  N  N   . ILE B  1 158 ? -18.763 -2.895  -6.236  1.00 9.91   ? 158 ILE B N   1 
ATOM   3474  C  CA  . ILE B  1 158 ? -17.925 -1.655  -6.257  1.00 10.77  ? 158 ILE B CA  1 
ATOM   3475  C  C   . ILE B  1 158 ? -17.030 -1.685  -7.476  1.00 10.17  ? 158 ILE B C   1 
ATOM   3476  O  O   . ILE B  1 158 ? -16.974 -0.727  -8.235  1.00 11.18  ? 158 ILE B O   1 
ATOM   3477  C  CB  . ILE B  1 158 ? -17.122 -1.522  -4.957  1.00 11.88  ? 158 ILE B CB  1 
ATOM   3478  C  CG1 . ILE B  1 158 ? -18.041 -1.394  -3.752  1.00 14.42  ? 158 ILE B CG1 1 
ATOM   3479  C  CG2 . ILE B  1 158 ? -16.137 -0.371  -5.112  1.00 12.86  ? 158 ILE B CG2 1 
ATOM   3480  C  CD1 . ILE B  1 158 ? -17.308 -1.683  -2.421  1.00 16.85  ? 158 ILE B CD1 1 
ATOM   3481  N  N   . PHE B  1 159 ? -16.266 -2.773  -7.652  1.00 11.08  ? 159 PHE B N   1 
ATOM   3482  C  CA  . PHE B  1 159 ? -15.208 -2.776  -8.671  1.00 12.51  ? 159 PHE B CA  1 
ATOM   3483  C  C   . PHE B  1 159 ? -15.724 -2.578  -10.059 1.00 13.59  ? 159 PHE B C   1 
ATOM   3484  O  O   . PHE B  1 159 ? -15.008 -2.036  -10.881 1.00 18.06  ? 159 PHE B O   1 
ATOM   3485  C  CB  . PHE B  1 159 ? -14.360 -4.042  -8.571  1.00 12.65  ? 159 PHE B CB  1 
ATOM   3486  C  CG  . PHE B  1 159 ? -13.681 -4.302  -7.246  1.00 11.61  ? 159 PHE B CG  1 
ATOM   3487  C  CD1 . PHE B  1 159 ? -13.332 -3.283  -6.375  1.00 13.54  ? 159 PHE B CD1 1 
ATOM   3488  C  CD2 . PHE B  1 159 ? -13.341 -5.615  -6.912  1.00 13.75  ? 159 PHE B CD2 1 
ATOM   3489  C  CE1 . PHE B  1 159 ? -12.680 -3.573  -5.186  1.00 13.47  ? 159 PHE B CE1 1 
ATOM   3490  C  CE2 . PHE B  1 159 ? -12.689 -5.910  -5.734  1.00 13.66  ? 159 PHE B CE2 1 
ATOM   3491  C  CZ  . PHE B  1 159 ? -12.358 -4.886  -4.872  1.00 13.48  ? 159 PHE B CZ  1 
ATOM   3492  N  N   . SER B  1 160 ? -16.909 -3.028  -10.317 1.00 14.58  ? 160 SER B N   1 
ATOM   3493  C  CA  . SER B  1 160 ? -17.471 -2.862  -11.667 1.00 18.58  ? 160 SER B CA  1 
ATOM   3494  C  C   . SER B  1 160 ? -17.694 -1.421  -12.067 1.00 16.43  ? 160 SER B C   1 
ATOM   3495  O  O   . SER B  1 160 ? -17.913 -1.173  -13.263 1.00 20.23  ? 160 SER B O   1 
ATOM   3496  C  CB  . SER B  1 160 ? -18.755 -3.710  -11.785 1.00 19.40  ? 160 SER B CB  1 
ATOM   3497  O  OG  . SER B  1 160 ? -19.747 -3.157  -10.957 1.00 19.42  ? 160 SER B OG  1 
ATOM   3498  N  N   . HIS B  1 161 ? -17.616 -0.473  -11.139 1.00 15.91  ? 161 HIS B N   1 
ATOM   3499  C  CA  . HIS B  1 161 ? -17.772 0.931   -11.448 1.00 15.88  ? 161 HIS B CA  1 
ATOM   3500  C  C   . HIS B  1 161 ? -16.522 1.715   -11.515 1.00 20.08  ? 161 HIS B C   1 
ATOM   3501  O  O   . HIS B  1 161 ? -16.565 2.911   -11.827 1.00 20.27  ? 161 HIS B O   1 
ATOM   3502  C  CB  . HIS B  1 161 ? -18.694 1.587   -10.452 1.00 16.94  ? 161 HIS B CB  1 
ATOM   3503  C  CG  . HIS B  1 161 ? -20.043 1.043   -10.486 1.00 18.00  ? 161 HIS B CG  1 
ATOM   3504  N  ND1 . HIS B  1 161 ? -20.960 1.529   -11.332 1.00 17.69  ? 161 HIS B ND1 1 
ATOM   3505  C  CD2 . HIS B  1 161 ? -20.623 0.017   -9.833  1.00 18.32  ? 161 HIS B CD2 1 
ATOM   3506  C  CE1 . HIS B  1 161 ? -22.105 0.864   -11.192 1.00 18.22  ? 161 HIS B CE1 1 
ATOM   3507  N  NE2 . HIS B  1 161 ? -21.898 -0.062  -10.260 1.00 18.17  ? 161 HIS B NE2 1 
ATOM   3508  N  N   . LEU B  1 162 ? -15.399 1.106   -11.276 1.00 22.61  ? 162 LEU B N   1 
ATOM   3509  C  CA  . LEU B  1 162 ? -14.164 1.835   -11.385 1.00 27.05  ? 162 LEU B CA  1 
ATOM   3510  C  C   . LEU B  1 162 ? -13.713 2.486   -12.656 1.00 27.32  ? 162 LEU B C   1 
ATOM   3511  O  O   . LEU B  1 162 ? -13.037 3.536   -12.527 1.00 29.57  ? 162 LEU B O   1 
ATOM   3512  C  CB  . LEU B  1 162 ? -13.030 1.008   -10.944 1.00 30.61  ? 162 LEU B CB  1 
ATOM   3513  C  CG  . LEU B  1 162 ? -13.175 0.312   -9.597  1.00 27.16  ? 162 LEU B CG  1 
ATOM   3514  C  CD1 . LEU B  1 162 ? -11.973 -0.591  -9.390  1.00 37.58  ? 162 LEU B CD1 1 
ATOM   3515  C  CD2 . LEU B  1 162 ? -13.315 1.289   -8.443  1.00 25.90  ? 162 LEU B CD2 1 
ATOM   3516  N  N   . GLN B  1 163 ? -14.005 1.980   -13.877 1.00 29.62  ? 163 GLN B N   1 
ATOM   3517  C  CA  . GLN B  1 163 ? -13.519 2.607   -15.115 1.00 27.48  ? 163 GLN B CA  1 
ATOM   3518  C  C   . GLN B  1 163 ? -14.258 3.905   -15.213 1.00 33.61  ? 163 GLN B C   1 
ATOM   3519  O  O   . GLN B  1 163 ? -14.063 4.735   -16.133 1.00 41.31  ? 163 GLN B O   1 
ATOM   3520  C  CB  . GLN B  1 163 ? -13.643 1.668   -16.347 1.00 31.58  ? 163 GLN B CB  1 
ATOM   3521  C  CG  . GLN B  1 163 ? -12.732 0.424   -16.190 1.00 43.92  ? 163 GLN B CG  1 
ATOM   3522  C  CD  . GLN B  1 163 ? -11.197 0.684   -16.093 1.00 40.86  ? 163 GLN B CD  1 
ATOM   3523  O  OE1 . GLN B  1 163 ? -10.693 1.848   -16.117 1.00 45.47  ? 163 GLN B OE1 1 
ATOM   3524  N  NE2 . GLN B  1 163 ? -10.445 -0.433  -16.005 1.00 32.15  ? 163 GLN B NE2 1 
ATOM   3525  N  N   . HIS B  1 164 ? -15.115 4.148   -14.233 1.00 34.90  ? 164 HIS B N   1 
ATOM   3526  C  CA  . HIS B  1 164 ? -15.971 5.316   -14.276 1.00 27.60  ? 164 HIS B CA  1 
ATOM   3527  C  C   . HIS B  1 164 ? -15.595 6.412   -13.317 1.00 21.18  ? 164 HIS B C   1 
ATOM   3528  O  O   . HIS B  1 164 ? -16.082 7.547   -13.352 1.00 23.67  ? 164 HIS B O   1 
ATOM   3529  C  CB  . HIS B  1 164 ? -17.417 4.896   -14.361 1.00 30.78  ? 164 HIS B CB  1 
ATOM   3530  C  CG  . HIS B  1 164 ? -17.599 3.738   -15.342 1.00 37.41  ? 164 HIS B CG  1 
ATOM   3531  N  ND1 . HIS B  1 164 ? -17.121 3.794   -16.630 1.00 26.72  ? 164 HIS B ND1 1 
ATOM   3532  C  CD2 . HIS B  1 164 ? -18.102 2.428   -15.162 1.00 26.03  ? 164 HIS B CD2 1 
ATOM   3533  C  CE1 . HIS B  1 164 ? -17.417 2.599   -17.287 1.00 33.09  ? 164 HIS B CE1 1 
ATOM   3534  N  NE2 . HIS B  1 164 ? -18.006 1.762   -16.378 1.00 33.96  ? 164 HIS B NE2 1 
ATOM   3535  N  N   . VAL B  1 165 ? -14.622 6.081   -12.524 1.00 15.99  ? 165 VAL B N   1 
ATOM   3536  C  CA  . VAL B  1 165 ? -14.072 7.043   -11.583 1.00 13.28  ? 165 VAL B CA  1 
ATOM   3537  C  C   . VAL B  1 165 ? -12.533 6.983   -11.688 1.00 11.10  ? 165 VAL B C   1 
ATOM   3538  O  O   . VAL B  1 165 ? -11.777 7.122   -10.731 1.00 13.08  ? 165 VAL B O   1 
ATOM   3539  C  CB  . VAL B  1 165 ? -14.537 6.865   -10.133 1.00 15.83  ? 165 VAL B CB  1 
ATOM   3540  C  CG1 . VAL B  1 165 ? -15.979 7.237   -10.019 1.00 17.99  ? 165 VAL B CG1 1 
ATOM   3541  C  CG2 . VAL B  1 165 ? -14.279 5.490   -9.604  1.00 17.70  ? 165 VAL B CG2 1 
ATOM   3542  N  N   A LYS B  1 166 ? -12.000 6.710   -12.893 0.50 13.76  ? 166 LYS B N   1 
ATOM   3543  N  N   B LYS B  1 166 ? -12.183 6.902   -12.956 0.50 11.01  ? 166 LYS B N   1 
ATOM   3544  C  CA  A LYS B  1 166 ? -10.526 6.594   -13.073 0.50 12.79  ? 166 LYS B CA  1 
ATOM   3545  C  CA  B LYS B  1 166 ? -10.855 6.661   -13.275 0.50 9.35   ? 166 LYS B CA  1 
ATOM   3546  C  C   A LYS B  1 166 ? -9.735  7.812   -12.613 0.50 12.00  ? 166 LYS B C   1 
ATOM   3547  C  C   B LYS B  1 166 ? -9.892  7.744   -12.812 0.50 10.13  ? 166 LYS B C   1 
ATOM   3548  O  O   A LYS B  1 166 ? -8.599  7.656   -12.091 0.50 11.64  ? 166 LYS B O   1 
ATOM   3549  O  O   B LYS B  1 166 ? -8.780  7.426   -12.463 0.50 9.95   ? 166 LYS B O   1 
ATOM   3550  C  CB  A LYS B  1 166 ? -10.162 6.393   -14.562 0.50 14.53  ? 166 LYS B CB  1 
ATOM   3551  C  CB  B LYS B  1 166 ? -10.737 6.457   -14.751 0.50 11.15  ? 166 LYS B CB  1 
ATOM   3552  C  CG  A LYS B  1 166 ? -10.707 5.148   -15.258 0.50 15.40  ? 166 LYS B CG  1 
ATOM   3553  C  CG  B LYS B  1 166 ? -9.305  6.168   -15.123 0.50 10.91  ? 166 LYS B CG  1 
ATOM   3554  C  CD  A LYS B  1 166 ? -10.189 5.074   -16.707 0.50 17.73  ? 166 LYS B CD  1 
ATOM   3555  C  CD  B LYS B  1 166 ? -9.216  5.777   -16.595 0.50 14.00  ? 166 LYS B CD  1 
ATOM   3556  C  CE  A LYS B  1 166 ? -8.684  4.665   -16.798 0.50 22.50  ? 166 LYS B CE  1 
ATOM   3557  C  CE  B LYS B  1 166 ? -9.700  4.356   -16.909 0.50 24.33  ? 166 LYS B CE  1 
ATOM   3558  N  NZ  A LYS B  1 166 ? -8.375  3.346   -16.106 0.50 21.51  ? 166 LYS B NZ  1 
ATOM   3559  N  NZ  B LYS B  1 166 ? -8.770  3.280   -16.459 0.50 21.98  ? 166 LYS B NZ  1 
ATOM   3560  N  N   . TYR B  1 167 ? -10.311 9.012   -12.776 1.00 10.69  ? 167 TYR B N   1 
ATOM   3561  C  CA  . TYR B  1 167 ? -9.493  10.141  -12.492 1.00 10.58  ? 167 TYR B CA  1 
ATOM   3562  C  C   . TYR B  1 167 ? -9.991  10.938  -11.329 1.00 10.06  ? 167 TYR B C   1 
ATOM   3563  O  O   . TYR B  1 167 ? -11.184 10.902  -10.981 1.00 11.00  ? 167 TYR B O   1 
ATOM   3564  C  CB  . TYR B  1 167 ? -9.471  11.038  -13.766 1.00 11.74  ? 167 TYR B CB  1 
ATOM   3565  C  CG  . TYR B  1 167 ? -9.074  10.294  -15.036 1.00 12.41  ? 167 TYR B CG  1 
ATOM   3566  C  CD1 . TYR B  1 167 ? -7.753  9.961   -15.265 1.00 16.83  ? 167 TYR B CD1 1 
ATOM   3567  C  CD2 . TYR B  1 167 ? -10.022 9.907   -15.986 1.00 14.23  ? 167 TYR B CD2 1 
ATOM   3568  C  CE1 . TYR B  1 167 ? -7.377  9.263   -16.397 1.00 14.89  ? 167 TYR B CE1 1 
ATOM   3569  C  CE2 . TYR B  1 167 ? -9.654  9.214   -17.120 1.00 14.28  ? 167 TYR B CE2 1 
ATOM   3570  C  CZ  . TYR B  1 167 ? -8.326  8.891   -17.323 1.00 13.79  ? 167 TYR B CZ  1 
ATOM   3571  O  OH  . TYR B  1 167 ? -7.953  8.207   -18.451 1.00 18.16  ? 167 TYR B OH  1 
ATOM   3572  N  N   . LYS B  1 168 ? -9.062  11.723  -10.758 1.00 11.38  ? 168 LYS B N   1 
ATOM   3573  C  CA  . LYS B  1 168 ? -9.364  12.553  -9.622  1.00 14.35  ? 168 LYS B CA  1 
ATOM   3574  C  C   . LYS B  1 168 ? -10.522 13.444  -9.927  1.00 14.88  ? 168 LYS B C   1 
ATOM   3575  O  O   . LYS B  1 168 ? -10.582 14.078  -10.975 1.00 15.48  ? 168 LYS B O   1 
ATOM   3576  C  CB  . LYS B  1 168 ? -8.141  13.414  -9.249  1.00 14.53  ? 168 LYS B CB  1 
ATOM   3577  C  CG  . LYS B  1 168 ? -8.398  14.279  -8.056  1.00 19.74  ? 168 LYS B CG  1 
ATOM   3578  C  CD  . LYS B  1 168 ? -7.133  15.079  -7.728  1.00 25.19  ? 168 LYS B CD  1 
ATOM   3579  C  CE  . LYS B  1 168 ? -7.496  16.019  -6.530  1.00 37.49  ? 168 LYS B CE  1 
ATOM   3580  N  NZ  . LYS B  1 168 ? -6.299  16.479  -5.759  1.00 44.69  ? 168 LYS B NZ  1 
ATOM   3581  N  N   . GLY B  1 169 ? -11.489 13.502  -9.011  1.00 17.55  ? 169 GLY B N   1 
ATOM   3582  C  CA  . GLY B  1 169 ? -12.673 14.362  -9.187  1.00 21.88  ? 169 GLY B CA  1 
ATOM   3583  C  C   . GLY B  1 169 ? -13.875 13.710  -9.836  1.00 20.07  ? 169 GLY B C   1 
ATOM   3584  O  O   . GLY B  1 169 ? -14.960 14.237  -9.836  1.00 27.59  ? 169 GLY B O   1 
ATOM   3585  N  N   . GLN B  1 170 ? -13.674 12.568  -10.425 1.00 13.91  ? 170 GLN B N   1 
ATOM   3586  C  CA  . GLN B  1 170 ? -14.805 11.888  -11.108 1.00 13.04  ? 170 GLN B CA  1 
ATOM   3587  C  C   . GLN B  1 170 ? -15.694 11.198  -10.027 1.00 12.94  ? 170 GLN B C   1 
ATOM   3588  O  O   . GLN B  1 170 ? -15.211 10.722  -8.998  1.00 14.63  ? 170 GLN B O   1 
ATOM   3589  C  CB  . GLN B  1 170 ? -14.265 10.915  -12.125 1.00 12.11  ? 170 GLN B CB  1 
ATOM   3590  C  CG  . GLN B  1 170 ? -13.569 11.715  -13.272 1.00 14.83  ? 170 GLN B CG  1 
ATOM   3591  C  CD  . GLN B  1 170 ? -13.259 10.844  -14.405 1.00 18.06  ? 170 GLN B CD  1 
ATOM   3592  O  OE1 . GLN B  1 170 ? -12.828 9.690   -14.242 1.00 16.66  ? 170 GLN B OE1 1 
ATOM   3593  N  NE2 . GLN B  1 170 ? -13.319 11.428  -15.624 1.00 23.86  ? 170 GLN B NE2 1 
ATOM   3594  N  N   . GLU B  1 171 ? -16.963 11.114  -10.384 1.00 13.31  ? 171 GLU B N   1 
ATOM   3595  C  CA  . GLU B  1 171 ? -18.007 10.578  -9.497  1.00 13.38  ? 171 GLU B CA  1 
ATOM   3596  C  C   . GLU B  1 171 ? -18.900 9.624   -10.318 1.00 14.95  ? 171 GLU B C   1 
ATOM   3597  O  O   . GLU B  1 171 ? -19.068 9.804   -11.571 1.00 17.98  ? 171 GLU B O   1 
ATOM   3598  C  CB  . GLU B  1 171 ? -18.882 11.699  -8.949  1.00 17.90  ? 171 GLU B CB  1 
ATOM   3599  C  CG  . GLU B  1 171 ? -18.119 12.630  -8.049  1.00 23.30  ? 171 GLU B CG  1 
ATOM   3600  C  CD  . GLU B  1 171 ? -18.952 13.800  -7.587  1.00 35.75  ? 171 GLU B CD  1 
ATOM   3601  O  OE1 . GLU B  1 171 ? -20.122 13.907  -8.064  1.00 55.75  ? 171 GLU B OE1 1 
ATOM   3602  O  OE2 . GLU B  1 171 ? -18.511 14.546  -6.680  1.00 44.54  ? 171 GLU B OE2 1 
ATOM   3603  N  N   . ALA B  1 172 ? -19.384 8.562   -9.692  1.00 15.20  ? 172 ALA B N   1 
ATOM   3604  C  CA  . ALA B  1 172 ? -20.270 7.612   -10.306 1.00 15.13  ? 172 ALA B CA  1 
ATOM   3605  C  C   . ALA B  1 172 ? -21.306 7.238   -9.246  1.00 12.69  ? 172 ALA B C   1 
ATOM   3606  O  O   . ALA B  1 172 ? -21.056 7.435   -8.071  1.00 16.18  ? 172 ALA B O   1 
ATOM   3607  C  CB  . ALA B  1 172 ? -19.480 6.445   -10.854 1.00 17.25  ? 172 ALA B CB  1 
ATOM   3608  N  N   . PHE B  1 173 ? -22.333 6.592   -9.659  1.00 14.08  ? 173 PHE B N   1 
ATOM   3609  C  CA  . PHE B  1 173 ? -23.351 6.062   -8.749  1.00 13.15  ? 173 PHE B CA  1 
ATOM   3610  C  C   . PHE B  1 173 ? -23.319 4.579   -8.754  1.00 13.10  ? 173 PHE B C   1 
ATOM   3611  O  O   . PHE B  1 173 ? -23.283 3.957   -9.786  1.00 18.42  ? 173 PHE B O   1 
ATOM   3612  C  CB  . PHE B  1 173 ? -24.727 6.571   -9.158  1.00 18.34  ? 173 PHE B CB  1 
ATOM   3613  C  CG  . PHE B  1 173 ? -24.998 7.980   -8.636  1.00 18.12  ? 173 PHE B CG  1 
ATOM   3614  C  CD1 . PHE B  1 173 ? -25.085 8.238   -7.228  1.00 18.99  ? 173 PHE B CD1 1 
ATOM   3615  C  CD2 . PHE B  1 173 ? -25.197 9.020   -9.501  1.00 25.31  ? 173 PHE B CD2 1 
ATOM   3616  C  CE1 . PHE B  1 173 ? -25.303 9.483   -6.707  1.00 25.32  ? 173 PHE B CE1 1 
ATOM   3617  C  CE2 . PHE B  1 173 ? -25.436 10.303  -8.991  1.00 35.70  ? 173 PHE B CE2 1 
ATOM   3618  C  CZ  . PHE B  1 173 ? -25.508 10.521  -7.607  1.00 30.83  ? 173 PHE B CZ  1 
ATOM   3619  N  N   . VAL B  1 174 ? -23.421 4.037   -7.551  1.00 12.11  ? 174 VAL B N   1 
ATOM   3620  C  CA  . VAL B  1 174 ? -23.397 2.600   -7.348  1.00 11.42  ? 174 VAL B CA  1 
ATOM   3621  C  C   . VAL B  1 174 ? -24.756 2.239   -6.724  1.00 11.46  ? 174 VAL B C   1 
ATOM   3622  O  O   . VAL B  1 174 ? -25.133 2.776   -5.695  1.00 11.52  ? 174 VAL B O   1 
ATOM   3623  C  CB  . VAL B  1 174 ? -22.282 2.166   -6.372  1.00 12.27  ? 174 VAL B CB  1 
ATOM   3624  C  CG1 . VAL B  1 174 ? -22.348 0.652   -6.057  1.00 13.53  ? 174 VAL B CG1 1 
ATOM   3625  C  CG2 . VAL B  1 174 ? -20.882 2.537   -6.981  1.00 14.44  ? 174 VAL B CG2 1 
ATOM   3626  N  N   . PRO B  1 175 ? -25.539 1.303   -7.307  1.00 10.59  ? 175 PRO B N   1 
ATOM   3627  C  CA  . PRO B  1 175 ? -26.771 0.885   -6.669  1.00 11.18  ? 175 PRO B CA  1 
ATOM   3628  C  C   . PRO B  1 175 ? -26.502 0.341   -5.277  1.00 10.84  ? 175 PRO B C   1 
ATOM   3629  O  O   . PRO B  1 175 ? -25.493 -0.335  -5.056  1.00 11.84  ? 175 PRO B O   1 
ATOM   3630  C  CB  . PRO B  1 175 ? -27.269 -0.189  -7.606  1.00 13.19  ? 175 PRO B CB  1 
ATOM   3631  C  CG  . PRO B  1 175 ? -26.718 0.117   -8.975  1.00 15.94  ? 175 PRO B CG  1 
ATOM   3632  C  CD  . PRO B  1 175 ? -25.315 0.687   -8.616  1.00 12.40  ? 175 PRO B CD  1 
ATOM   3633  N  N   . GLY B  1 176 ? -27.440 0.544   -4.350  1.00 11.37  ? 176 GLY B N   1 
ATOM   3634  C  CA  . GLY B  1 176 ? -27.297 -0.030  -3.027  1.00 11.88  ? 176 GLY B CA  1 
ATOM   3635  C  C   . GLY B  1 176 ? -27.162 -1.535  -3.070  1.00 11.35  ? 176 GLY B C   1 
ATOM   3636  O  O   . GLY B  1 176 ? -27.780 -2.232  -3.885  1.00 12.35  ? 176 GLY B O   1 
ATOM   3637  N  N   . PHE B  1 177 ? -26.384 -2.053  -2.119  1.00 10.69  ? 177 PHE B N   1 
ATOM   3638  C  CA  . PHE B  1 177 ? -26.274 -3.494  -1.887  1.00 11.45  ? 177 PHE B CA  1 
ATOM   3639  C  C   . PHE B  1 177 ? -26.003 -3.672  -0.411  1.00 10.62  ? 177 PHE B C   1 
ATOM   3640  O  O   . PHE B  1 177 ? -25.829 -2.704  0.342   1.00 11.13  ? 177 PHE B O   1 
ATOM   3641  C  CB  . PHE B  1 177 ? -25.204 -4.148  -2.781  1.00 11.91  ? 177 PHE B CB  1 
ATOM   3642  C  CG  . PHE B  1 177 ? -23.806 -3.716  -2.490  1.00 11.19  ? 177 PHE B CG  1 
ATOM   3643  C  CD1 . PHE B  1 177 ? -23.297 -2.486  -3.021  1.00 11.85  ? 177 PHE B CD1 1 
ATOM   3644  C  CD2 . PHE B  1 177 ? -22.996 -4.520  -1.685  1.00 13.42  ? 177 PHE B CD2 1 
ATOM   3645  C  CE1 . PHE B  1 177 ? -21.948 -2.135  -2.757  1.00 12.14  ? 177 PHE B CE1 1 
ATOM   3646  C  CE2 . PHE B  1 177 ? -21.673 -4.143  -1.445  1.00 12.80  ? 177 PHE B CE2 1 
ATOM   3647  C  CZ  . PHE B  1 177 ? -21.156 -2.989  -1.999  1.00 14.13  ? 177 PHE B CZ  1 
ATOM   3648  N  N   . ASN B  1 178 ? -25.966 -4.936  -0.002  1.00 12.75  ? 178 ASN B N   1 
ATOM   3649  C  CA  . ASN B  1 178 ? -25.781 -5.182  1.403   1.00 12.18  ? 178 ASN B CA  1 
ATOM   3650  C  C   . ASN B  1 178 ? -24.291 -5.107  1.769   1.00 10.17  ? 178 ASN B C   1 
ATOM   3651  O  O   . ASN B  1 178 ? -23.529 -6.033  1.447   1.00 11.01  ? 178 ASN B O   1 
ATOM   3652  C  CB  . ASN B  1 178 ? -26.360 -6.580  1.761   1.00 14.23  ? 178 ASN B CB  1 
ATOM   3653  C  CG  . ASN B  1 178 ? -26.262 -6.863  3.213   1.00 13.52  ? 178 ASN B CG  1 
ATOM   3654  O  OD1 . ASN B  1 178 ? -25.847 -6.037  4.053   1.00 13.16  ? 178 ASN B OD1 1 
ATOM   3655  N  ND2 . ASN B  1 178 ? -26.565 -8.122  3.568   1.00 16.41  ? 178 ASN B ND2 1 
ATOM   3656  N  N   . ILE B  1 179 ? -23.893 -4.066  2.410   1.00 9.93   ? 179 ILE B N   1 
ATOM   3657  C  CA  . ILE B  1 179 ? -22.495 -3.864  2.778   1.00 9.14   ? 179 ILE B CA  1 
ATOM   3658  C  C   . ILE B  1 179 ? -21.974 -4.946  3.676   1.00 9.05   ? 179 ILE B C   1 
ATOM   3659  O  O   . ILE B  1 179 ? -20.756 -5.182  3.722   1.00 9.28   ? 179 ILE B O   1 
ATOM   3660  C  CB  . ILE B  1 179 ? -22.296 -2.447  3.362   1.00 9.23   ? 179 ILE B CB  1 
ATOM   3661  C  CG1 . ILE B  1 179 ? -22.871 -1.356  2.449   1.00 10.52  ? 179 ILE B CG1 1 
ATOM   3662  C  CG2 . ILE B  1 179 ? -20.877 -2.208  3.752   1.00 9.71   ? 179 ILE B CG2 1 
ATOM   3663  C  CD1 . ILE B  1 179 ? -22.243 -1.328  1.005   1.00 10.89  ? 179 ILE B CD1 1 
ATOM   3664  N  N   . GLU B  1 180 ? -22.867 -5.584  4.461   1.00 9.41   ? 180 GLU B N   1 
ATOM   3665  C  CA  . GLU B  1 180 ? -22.401 -6.667  5.296   1.00 10.55  ? 180 GLU B CA  1 
ATOM   3666  C  C   . GLU B  1 180 ? -21.771 -7.777  4.490   1.00 10.44  ? 180 GLU B C   1 
ATOM   3667  O  O   . GLU B  1 180 ? -20.973 -8.538  5.041   1.00 11.07  ? 180 GLU B O   1 
ATOM   3668  C  CB  . GLU B  1 180 ? -23.569 -7.172  6.165   1.00 13.24  ? 180 GLU B CB  1 
ATOM   3669  C  CG  . GLU B  1 180 ? -23.026 -7.908  7.392   1.00 18.82  ? 180 GLU B CG  1 
ATOM   3670  C  CD  . GLU B  1 180 ? -24.104 -8.141  8.422   1.00 19.76  ? 180 GLU B CD  1 
ATOM   3671  O  OE1 . GLU B  1 180 ? -25.259 -7.718  8.238   1.00 22.96  ? 180 GLU B OE1 1 
ATOM   3672  O  OE2 . GLU B  1 180 ? -23.761 -8.740  9.445   1.00 24.40  ? 180 GLU B OE2 1 
ATOM   3673  N  N   . GLU B  1 181 ? -22.131 -7.916  3.206   1.00 10.02  ? 181 GLU B N   1 
ATOM   3674  C  CA  . GLU B  1 181 ? -21.522 -8.900  2.356   1.00 10.58  ? 181 GLU B CA  1 
ATOM   3675  C  C   . GLU B  1 181 ? -20.032 -8.682  2.135   1.00 9.52   ? 181 GLU B C   1 
ATOM   3676  O  O   . GLU B  1 181 ? -19.368 -9.578  1.646   1.00 11.65  ? 181 GLU B O   1 
ATOM   3677  C  CB  . GLU B  1 181 ? -22.218 -8.900  0.981   1.00 13.31  ? 181 GLU B CB  1 
ATOM   3678  C  CG  . GLU B  1 181 ? -23.656 -9.298  0.936   1.00 17.26  ? 181 GLU B CG  1 
ATOM   3679  C  CD  . GLU B  1 181 ? -24.349 -8.983  -0.399  1.00 18.91  ? 181 GLU B CD  1 
ATOM   3680  O  OE1 . GLU B  1 181 ? -23.665 -8.576  -1.393  1.00 22.92  ? 181 GLU B OE1 1 
ATOM   3681  O  OE2 . GLU B  1 181 ? -25.568 -9.170  -0.480  1.00 19.46  ? 181 GLU B OE2 1 
ATOM   3682  N  N   . LEU B  1 182 ? -19.519 -7.495  2.472   1.00 8.32   ? 182 LEU B N   1 
ATOM   3683  C  CA  . LEU B  1 182 ? -18.088 -7.204  2.354   1.00 8.52   ? 182 LEU B CA  1 
ATOM   3684  C  C   . LEU B  1 182 ? -17.324 -7.680  3.575   1.00 8.29   ? 182 LEU B C   1 
ATOM   3685  O  O   . LEU B  1 182 ? -16.097 -7.665  3.583   1.00 9.01   ? 182 LEU B O   1 
ATOM   3686  C  CB  . LEU B  1 182 ? -17.876 -5.688  2.156   1.00 8.43   ? 182 LEU B CB  1 
ATOM   3687  C  CG  . LEU B  1 182 ? -18.581 -5.079  0.964   1.00 8.21   ? 182 LEU B CG  1 
ATOM   3688  C  CD1 . LEU B  1 182 ? -18.261 -3.563  0.914   1.00 9.19   ? 182 LEU B CD1 1 
ATOM   3689  C  CD2 . LEU B  1 182 ? -18.209 -5.727  -0.348  1.00 9.05   ? 182 LEU B CD2 1 
ATOM   3690  N  N   . LEU B  1 183 ? -18.016 -8.022  4.667   1.00 9.66   ? 183 LEU B N   1 
ATOM   3691  C  CA  . LEU B  1 183 ? -17.376 -8.432  5.914   1.00 9.16   ? 183 LEU B CA  1 
ATOM   3692  C  C   . LEU B  1 183 ? -17.068 -9.910  5.865   1.00 9.21   ? 183 LEU B C   1 
ATOM   3693  O  O   . LEU B  1 183 ? -17.765 -10.676 5.178   1.00 11.23  ? 183 LEU B O   1 
ATOM   3694  C  CB  . LEU B  1 183 ? -18.306 -8.100  7.109   1.00 10.30  ? 183 LEU B CB  1 
ATOM   3695  C  CG  . LEU B  1 183 ? -18.742 -6.645  7.213   1.00 11.43  ? 183 LEU B CG  1 
ATOM   3696  C  CD1 . LEU B  1 183 ? -19.542 -6.466  8.499   1.00 15.31  ? 183 LEU B CD1 1 
ATOM   3697  C  CD2 . LEU B  1 183 ? -17.524 -5.749  7.218   1.00 13.30  ? 183 LEU B CD2 1 
ATOM   3698  N  N   . PRO B  1 184 ? -16.062 -10.325 6.629   1.00 8.83   ? 184 PRO B N   1 
ATOM   3699  C  CA  . PRO B  1 184 ? -15.726 -11.745 6.685   1.00 10.38  ? 184 PRO B CA  1 
ATOM   3700  C  C   . PRO B  1 184 ? -16.547 -12.521 7.601   1.00 12.58  ? 184 PRO B C   1 
ATOM   3701  O  O   . PRO B  1 184 ? -17.522 -12.047 8.235   1.00 14.76  ? 184 PRO B O   1 
ATOM   3702  C  CB  . PRO B  1 184 ? -14.268 -11.654 7.271   1.00 12.94  ? 184 PRO B CB  1 
ATOM   3703  C  CG  . PRO B  1 184 ? -14.330 -10.457 8.195   1.00 11.83  ? 184 PRO B CG  1 
ATOM   3704  C  CD  . PRO B  1 184 ? -15.188 -9.508  7.494   1.00 9.23   ? 184 PRO B CD  1 
ATOM   3705  N  N   A GLU B  1 185 ? -16.143 -13.802 7.648   0.50 13.38  ? 185 GLU B N   1 
ATOM   3706  N  N   B GLU B  1 185 ? -16.155 -13.803 7.648   0.50 13.49  ? 185 GLU B N   1 
ATOM   3707  C  CA  A GLU B  1 185 ? -16.692 -14.776 8.588   0.50 14.68  ? 185 GLU B CA  1 
ATOM   3708  C  CA  B GLU B  1 185 ? -16.744 -14.766 8.573   0.50 14.93  ? 185 GLU B CA  1 
ATOM   3709  C  C   A GLU B  1 185 ? -16.341 -14.385 10.039  0.50 13.24  ? 185 GLU B C   1 
ATOM   3710  C  C   B GLU B  1 185 ? -16.355 -14.410 10.026  0.50 13.53  ? 185 GLU B C   1 
ATOM   3711  O  O   A GLU B  1 185 ? -15.263 -13.802 10.304  0.50 14.59  ? 185 GLU B O   1 
ATOM   3712  O  O   B GLU B  1 185 ? -15.268 -13.863 10.278  0.50 14.96  ? 185 GLU B O   1 
ATOM   3713  C  CB  A GLU B  1 185 ? -16.099 -16.133 8.284   0.50 17.52  ? 185 GLU B CB  1 
ATOM   3714  C  CB  B GLU B  1 185 ? -16.291 -16.171 8.187   0.50 17.88  ? 185 GLU B CB  1 
ATOM   3715  C  CG  A GLU B  1 185 ? -16.527 -16.670 6.920   0.50 25.11  ? 185 GLU B CG  1 
ATOM   3716  C  CG  B GLU B  1 185 ? -17.001 -16.652 6.888   0.50 24.25  ? 185 GLU B CG  1 
ATOM   3717  C  CD  A GLU B  1 185 ? -16.275 -18.138 6.833   0.50 30.74  ? 185 GLU B CD  1 
ATOM   3718  C  CD  B GLU B  1 185 ? -18.484 -16.246 6.864   0.50 37.59  ? 185 GLU B CD  1 
ATOM   3719  O  OE1 A GLU B  1 185 ? -15.321 -18.594 7.499   0.50 40.26  ? 185 GLU B OE1 1 
ATOM   3720  O  OE1 B GLU B  1 185 ? -19.344 -17.037 7.322   0.50 39.33  ? 185 GLU B OE1 1 
ATOM   3721  O  OE2 A GLU B  1 185 ? -17.055 -18.794 6.126   0.50 179.57 ? 185 GLU B OE2 1 
ATOM   3722  O  OE2 B GLU B  1 185 ? -18.781 -15.109 6.439   0.50 68.06  ? 185 GLU B OE2 1 
ATOM   3723  N  N   . ARG B  1 186 ? -17.292 -14.694 10.942  1.00 13.12  ? 186 ARG B N   1 
ATOM   3724  C  CA  . ARG B  1 186 ? -17.040 -14.580 12.407  1.00 13.89  ? 186 ARG B CA  1 
ATOM   3725  C  C   . ARG B  1 186 ? -16.592 -13.185 12.719  1.00 13.39  ? 186 ARG B C   1 
ATOM   3726  O  O   . ARG B  1 186 ? -15.501 -12.956 13.283  1.00 13.69  ? 186 ARG B O   1 
ATOM   3727  C  CB  . ARG B  1 186 ? -16.088 -15.653 12.919  1.00 16.15  ? 186 ARG B CB  1 
ATOM   3728  C  CG  . ARG B  1 186 ? -16.643 -17.047 12.667  1.00 24.83  ? 186 ARG B CG  1 
ATOM   3729  C  CD  . ARG B  1 186 ? -15.728 -18.156 13.185  1.00 22.99  ? 186 ARG B CD  1 
ATOM   3730  N  NE  . ARG B  1 186 ? -14.445 -18.136 12.464  1.00 28.70  ? 186 ARG B NE  1 
ATOM   3731  C  CZ  . ARG B  1 186 ? -14.216 -18.677 11.274  1.00 30.55  ? 186 ARG B CZ  1 
ATOM   3732  N  NH1 . ARG B  1 186 ? -15.195 -19.250 10.612  1.00 39.11  ? 186 ARG B NH1 1 
ATOM   3733  N  NH2 . ARG B  1 186 ? -13.008 -18.567 10.706  1.00 38.83  ? 186 ARG B NH2 1 
ATOM   3734  N  N   . THR B  1 187 ? -17.428 -12.235 12.319  1.00 11.46  ? 187 THR B N   1 
ATOM   3735  C  CA  . THR B  1 187 ? -17.119 -10.871 12.713  1.00 10.29  ? 187 THR B CA  1 
ATOM   3736  C  C   . THR B  1 187 ? -16.973 -10.665 14.197  1.00 10.85  ? 187 THR B C   1 
ATOM   3737  O  O   . THR B  1 187 ? -16.426 -9.670  14.606  1.00 11.23  ? 187 THR B O   1 
ATOM   3738  C  CB  . THR B  1 187 ? -18.070 -9.902  12.139  1.00 10.99  ? 187 THR B CB  1 
ATOM   3739  O  OG1 . THR B  1 187 ? -19.410 -10.266 12.482  1.00 14.56  ? 187 THR B OG1 1 
ATOM   3740  C  CG2 . THR B  1 187 ? -17.935 -9.794  10.618  1.00 14.58  ? 187 THR B CG2 1 
ATOM   3741  N  N   . ALA B  1 188 ? -17.463 -11.629 15.042  1.00 12.75  ? 188 ALA B N   1 
ATOM   3742  C  CA  . ALA B  1 188 ? -17.223 -11.543 16.456  1.00 12.62  ? 188 ALA B CA  1 
ATOM   3743  C  C   . ALA B  1 188 ? -15.779 -11.556 16.833  1.00 10.33  ? 188 ALA B C   1 
ATOM   3744  O  O   . ALA B  1 188 ? -15.434 -11.116 17.923  1.00 11.20  ? 188 ALA B O   1 
ATOM   3745  C  CB  . ALA B  1 188 ? -17.932 -12.699 17.144  1.00 16.10  ? 188 ALA B CB  1 
ATOM   3746  N  N   A GLU B  1 189 ? -14.909 -12.107 15.941  0.50 10.76  ? 189 GLU B N   1 
ATOM   3747  N  N   B GLU B  1 189 ? -14.861 -12.058 15.981  0.50 10.70  ? 189 GLU B N   1 
ATOM   3748  C  CA  A GLU B  1 189 ? -13.462 -12.214 16.148  0.50 9.53   ? 189 GLU B CA  1 
ATOM   3749  C  CA  B GLU B  1 189 ? -13.440 -12.156 16.358  0.50 9.58   ? 189 GLU B CA  1 
ATOM   3750  C  C   A GLU B  1 189 ? -12.772 -10.940 15.555  0.50 8.03   ? 189 GLU B C   1 
ATOM   3751  C  C   B GLU B  1 189 ? -12.721 -11.022 15.621  0.50 8.67   ? 189 GLU B C   1 
ATOM   3752  O  O   A GLU B  1 189 ? -12.818 -10.710 14.321  0.50 7.97   ? 189 GLU B O   1 
ATOM   3753  O  O   B GLU B  1 189 ? -12.638 -11.027 14.344  0.50 8.84   ? 189 GLU B O   1 
ATOM   3754  C  CB  A GLU B  1 189 ? -13.017 -13.534 15.527  0.50 10.11  ? 189 GLU B CB  1 
ATOM   3755  C  CB  B GLU B  1 189 ? -12.807 -13.462 15.884  0.50 13.60  ? 189 GLU B CB  1 
ATOM   3756  C  CG  A GLU B  1 189 ? -13.620 -14.672 16.404  0.50 12.25  ? 189 GLU B CG  1 
ATOM   3757  C  CG  B GLU B  1 189 ? -13.646 -14.727 16.010  0.50 16.33  ? 189 GLU B CG  1 
ATOM   3758  C  CD  A GLU B  1 189 ? -13.175 -16.022 15.978  0.50 18.11  ? 189 GLU B CD  1 
ATOM   3759  C  CD  B GLU B  1 189 ? -12.814 -15.814 15.422  0.50 15.47  ? 189 GLU B CD  1 
ATOM   3760  O  OE1 A GLU B  1 189 ? -11.973 -16.138 15.555  0.50 18.32  ? 189 GLU B OE1 1 
ATOM   3761  O  OE1 B GLU B  1 189 ? -12.875 -16.054 14.176  0.50 16.76  ? 189 GLU B OE1 1 
ATOM   3762  O  OE2 A GLU B  1 189 ? -14.006 -16.977 16.059  0.50 23.15  ? 189 GLU B OE2 1 
ATOM   3763  O  OE2 B GLU B  1 189 ? -12.047 -16.410 16.242  0.50 20.64  ? 189 GLU B OE2 1 
ATOM   3764  N  N   . TYR B  1 190 ? -12.149 -10.126 16.401  1.00 8.42   ? 190 TYR B N   1 
ATOM   3765  C  CA  . TYR B  1 190 ? -11.520 -8.919  15.897  1.00 8.07   ? 190 TYR B CA  1 
ATOM   3766  C  C   . TYR B  1 190 ? -10.463 -8.463  16.864  1.00 7.92   ? 190 TYR B C   1 
ATOM   3767  O  O   . TYR B  1 190 ? -10.397 -8.839  18.040  1.00 8.54   ? 190 TYR B O   1 
ATOM   3768  C  CB  . TYR B  1 190 ? -12.566 -7.816  15.645  1.00 8.43   ? 190 TYR B CB  1 
ATOM   3769  C  CG  . TYR B  1 190 ? -13.387 -7.418  16.901  1.00 8.21   ? 190 TYR B CG  1 
ATOM   3770  C  CD1 . TYR B  1 190 ? -12.896 -6.524  17.855  1.00 8.44   ? 190 TYR B CD1 1 
ATOM   3771  C  CD2 . TYR B  1 190 ? -14.683 -7.942  17.068  1.00 9.36   ? 190 TYR B CD2 1 
ATOM   3772  C  CE1 . TYR B  1 190 ? -13.703 -6.145  18.940  1.00 8.89   ? 190 TYR B CE1 1 
ATOM   3773  C  CE2 . TYR B  1 190 ? -15.446 -7.585  18.188  1.00 9.84   ? 190 TYR B CE2 1 
ATOM   3774  C  CZ  . TYR B  1 190 ? -14.970 -6.669  19.074  1.00 9.37   ? 190 TYR B CZ  1 
ATOM   3775  O  OH  . TYR B  1 190 ? -15.721 -6.266  20.159  1.00 11.17  ? 190 TYR B OH  1 
ATOM   3776  N  N   . TYR B  1 191 ? -9.583  -7.609  16.302  1.00 7.35   ? 191 TYR B N   1 
ATOM   3777  C  CA  . TYR B  1 191 ? -8.606  -6.849  17.007  1.00 7.51   ? 191 TYR B CA  1 
ATOM   3778  C  C   . TYR B  1 191 ? -9.110  -5.439  17.214  1.00 7.45   ? 191 TYR B C   1 
ATOM   3779  O  O   . TYR B  1 191 ? -9.741  -4.882  16.325  1.00 9.10   ? 191 TYR B O   1 
ATOM   3780  C  CB  . TYR B  1 191 ? -7.298  -6.731  16.173  1.00 7.95   ? 191 TYR B CB  1 
ATOM   3781  C  CG  . TYR B  1 191 ? -6.712  -8.011  15.652  1.00 8.15   ? 191 TYR B CG  1 
ATOM   3782  C  CD1 . TYR B  1 191 ? -5.695  -8.654  16.375  1.00 8.99   ? 191 TYR B CD1 1 
ATOM   3783  C  CD2 . TYR B  1 191 ? -7.065  -8.537  14.425  1.00 8.16   ? 191 TYR B CD2 1 
ATOM   3784  C  CE1 . TYR B  1 191 ? -5.071  -9.787  15.825  1.00 9.77   ? 191 TYR B CE1 1 
ATOM   3785  C  CE2 . TYR B  1 191 ? -6.462  -9.652  13.883  1.00 9.73   ? 191 TYR B CE2 1 
ATOM   3786  C  CZ  . TYR B  1 191 ? -5.482  -10.286 14.623  1.00 9.72   ? 191 TYR B CZ  1 
ATOM   3787  O  OH  . TYR B  1 191 ? -4.866  -11.389 14.057  1.00 12.86  ? 191 TYR B OH  1 
ATOM   3788  N  N   . ARG B  1 192 ? -8.866  -4.877  18.391  1.00 7.87   ? 192 ARG B N   1 
ATOM   3789  C  CA  . ARG B  1 192 ? -9.294  -3.535  18.732  1.00 8.08   ? 192 ARG B CA  1 
ATOM   3790  C  C   . ARG B  1 192 ? -8.159  -2.716  19.256  1.00 8.35   ? 192 ARG B C   1 
ATOM   3791  O  O   . ARG B  1 192 ? -7.490  -3.174  20.183  1.00 9.30   ? 192 ARG B O   1 
ATOM   3792  C  CB  . ARG B  1 192 ? -10.425 -3.602  19.794  1.00 9.58   ? 192 ARG B CB  1 
ATOM   3793  C  CG  . ARG B  1 192 ? -10.772 -2.311  20.499  1.00 10.71  ? 192 ARG B CG  1 
ATOM   3794  C  CD  . ARG B  1 192 ? -11.441 -1.276  19.592  1.00 11.98  ? 192 ARG B CD  1 
ATOM   3795  N  NE  . ARG B  1 192 ? -12.560 -1.799  18.799  1.00 11.44  ? 192 ARG B NE  1 
ATOM   3796  C  CZ  . ARG B  1 192 ? -13.739 -2.207  19.262  1.00 10.41  ? 192 ARG B CZ  1 
ATOM   3797  N  NH1 . ARG B  1 192 ? -14.024 -2.062  20.573  1.00 11.90  ? 192 ARG B NH1 1 
ATOM   3798  N  NH2 . ARG B  1 192 ? -14.657 -2.716  18.478  1.00 12.65  ? 192 ARG B NH2 1 
ATOM   3799  N  N   . TYR B  1 193 ? -7.935  -1.489  18.761  1.00 8.92   ? 193 TYR B N   1 
ATOM   3800  C  CA  . TYR B  1 193 ? -6.921  -0.630  19.345  1.00 9.26   ? 193 TYR B CA  1 
ATOM   3801  C  C   . TYR B  1 193 ? -7.220  0.801   19.005  1.00 9.19   ? 193 TYR B C   1 
ATOM   3802  O  O   . TYR B  1 193 ? -8.002  1.096   18.067  1.00 8.95   ? 193 TYR B O   1 
ATOM   3803  C  CB  . TYR B  1 193 ? -5.497  -1.036  18.933  1.00 10.09  ? 193 TYR B CB  1 
ATOM   3804  C  CG  . TYR B  1 193 ? -5.098  -0.680  17.495  1.00 8.71   ? 193 TYR B CG  1 
ATOM   3805  C  CD1 . TYR B  1 193 ? -5.539  -1.434  16.378  1.00 8.44   ? 193 TYR B CD1 1 
ATOM   3806  C  CD2 . TYR B  1 193 ? -4.350  0.493   17.262  1.00 8.64   ? 193 TYR B CD2 1 
ATOM   3807  C  CE1 . TYR B  1 193 ? -5.202  -1.034  15.075  1.00 7.58   ? 193 TYR B CE1 1 
ATOM   3808  C  CE2 . TYR B  1 193 ? -4.019  0.885   15.997  1.00 7.78   ? 193 TYR B CE2 1 
ATOM   3809  C  CZ  . TYR B  1 193 ? -4.438  0.143   14.913  1.00 7.41   ? 193 TYR B CZ  1 
ATOM   3810  O  OH  . TYR B  1 193 ? -4.092  0.549   13.659  1.00 8.32   ? 193 TYR B OH  1 
ATOM   3811  N  N   . ARG B  1 194 ? -6.652  1.705   19.771  1.00 11.14  ? 194 ARG B N   1 
ATOM   3812  C  CA  . ARG B  1 194 ? -6.783  3.155   19.512  1.00 10.74  ? 194 ARG B CA  1 
ATOM   3813  C  C   . ARG B  1 194 ? -5.662  3.578   18.615  1.00 10.26  ? 194 ARG B C   1 
ATOM   3814  O  O   . ARG B  1 194 ? -4.485  3.384   18.902  1.00 11.75  ? 194 ARG B O   1 
ATOM   3815  C  CB  . ARG B  1 194 ? -6.727  3.891   20.889  1.00 15.90  ? 194 ARG B CB  1 
ATOM   3816  C  CG  . ARG B  1 194 ? -8.007  3.630   21.702  1.00 22.67  ? 194 ARG B CG  1 
ATOM   3817  C  CD  . ARG B  1 194 ? -8.070  4.478   22.973  1.00 30.70  ? 194 ARG B CD  1 
ATOM   3818  N  NE  . ARG B  1 194 ? -9.438  4.385   23.501  1.00 49.06  ? 194 ARG B NE  1 
ATOM   3819  C  CZ  . ARG B  1 194 ? -9.962  3.275   24.027  1.00 44.76  ? 194 ARG B CZ  1 
ATOM   3820  N  NH1 . ARG B  1 194 ? -9.231  2.156   24.145  1.00 62.74  ? 194 ARG B NH1 1 
ATOM   3821  N  NH2 . ARG B  1 194 ? -11.217 3.279   24.463  1.00 53.25  ? 194 ARG B NH2 1 
ATOM   3822  N  N   . GLY B  1 195 ? -6.008  4.221   17.497  1.00 9.43   ? 195 GLY B N   1 
ATOM   3823  C  CA  . GLY B  1 195 ? -5.011  4.628   16.517  1.00 9.82   ? 195 GLY B CA  1 
ATOM   3824  C  C   . GLY B  1 195 ? -5.466  5.857   15.795  1.00 8.53   ? 195 GLY B C   1 
ATOM   3825  O  O   . GLY B  1 195 ? -6.088  6.765   16.366  1.00 9.89   ? 195 GLY B O   1 
ATOM   3826  N  N   . SER B  1 196 ? -5.057  5.922   14.527  1.00 8.19   ? 196 SER B N   1 
ATOM   3827  C  CA  . SER B  1 196 ? -5.156  7.155   13.779  1.00 9.12   ? 196 SER B CA  1 
ATOM   3828  C  C   . SER B  1 196 ? -5.712  6.941   12.400  1.00 7.82   ? 196 SER B C   1 
ATOM   3829  O  O   . SER B  1 196 ? -5.785  5.790   11.910  1.00 8.01   ? 196 SER B O   1 
ATOM   3830  C  CB  . SER B  1 196 ? -3.769  7.828   13.634  1.00 9.10   ? 196 SER B CB  1 
ATOM   3831  O  OG  . SER B  1 196 ? -2.951  7.159   12.656  1.00 8.62   ? 196 SER B OG  1 
ATOM   3832  N  N   . LEU B  1 197 ? -6.019  8.041   11.726  1.00 8.06   ? 197 LEU B N   1 
ATOM   3833  C  CA  . LEU B  1 197 ? -6.153  7.974   10.279  1.00 7.77   ? 197 LEU B CA  1 
ATOM   3834  C  C   . LEU B  1 197 ? -4.790  7.491   9.701   1.00 7.61   ? 197 LEU B C   1 
ATOM   3835  O  O   . LEU B  1 197 ? -3.733  7.906   10.162  1.00 8.57   ? 197 LEU B O   1 
ATOM   3836  C  CB  . LEU B  1 197 ? -6.413  9.383   9.733   1.00 8.65   ? 197 LEU B CB  1 
ATOM   3837  C  CG  . LEU B  1 197 ? -7.721  10.009  10.148  1.00 11.86  ? 197 LEU B CG  1 
ATOM   3838  C  CD1 . LEU B  1 197 ? -7.843  11.392  9.568   1.00 17.45  ? 197 LEU B CD1 1 
ATOM   3839  C  CD2 . LEU B  1 197 ? -8.962  9.218   9.951   1.00 14.80  ? 197 LEU B CD2 1 
ATOM   3840  N  N   . THR B  1 198 ? -4.847  6.677   8.654   1.00 7.65   ? 198 THR B N   1 
ATOM   3841  C  CA  . THR B  1 198 ? -3.636  6.162   8.050   1.00 7.47   ? 198 THR B CA  1 
ATOM   3842  C  C   . THR B  1 198 ? -3.136  7.068   6.927   1.00 7.81   ? 198 THR B C   1 
ATOM   3843  O  O   . THR B  1 198 ? -2.132  6.710   6.283   1.00 8.21   ? 198 THR B O   1 
ATOM   3844  C  CB  . THR B  1 198 ? -3.811  4.769   7.568   1.00 7.77   ? 198 THR B CB  1 
ATOM   3845  O  OG1 . THR B  1 198 ? -4.741  4.809   6.473   1.00 7.06   ? 198 THR B OG1 1 
ATOM   3846  C  CG2 . THR B  1 198 ? -4.222  3.781   8.621   1.00 8.07   ? 198 THR B CG2 1 
ATOM   3847  N  N   . THR B  1 199 ? -3.800  8.183   6.682   1.00 8.87   ? 199 THR B N   1 
ATOM   3848  C  CA  . THR B  1 199 ? -3.322  9.110   5.665   1.00 9.46   ? 199 THR B CA  1 
ATOM   3849  C  C   . THR B  1 199 ? -3.345  10.479  6.336   1.00 8.99   ? 199 THR B C   1 
ATOM   3850  O  O   . THR B  1 199 ? -4.026  10.669  7.345   1.00 9.29   ? 199 THR B O   1 
ATOM   3851  C  CB  . THR B  1 199 ? -4.167  9.188   4.378   1.00 13.97  ? 199 THR B CB  1 
ATOM   3852  O  OG1 . THR B  1 199 ? -5.345  9.961   4.627   1.00 15.63  ? 199 THR B OG1 1 
ATOM   3853  C  CG2 . THR B  1 199 ? -4.559  7.812   3.878   1.00 14.73  ? 199 THR B CG2 1 
ATOM   3854  N  N   . PRO B  1 200 ? -2.669  11.468  5.757   1.00 9.10   ? 200 PRO B N   1 
ATOM   3855  C  CA  . PRO B  1 200 ? -2.837  12.834  6.262   1.00 9.00   ? 200 PRO B CA  1 
ATOM   3856  C  C   . PRO B  1 200 ? -4.305  13.180  6.332   1.00 9.74   ? 200 PRO B C   1 
ATOM   3857  O  O   . PRO B  1 200 ? -5.064  12.816  5.456   1.00 10.75  ? 200 PRO B O   1 
ATOM   3858  C  CB  . PRO B  1 200 ? -2.104  13.654  5.187   1.00 10.76  ? 200 PRO B CB  1 
ATOM   3859  C  CG  . PRO B  1 200 ? -1.002  12.726  4.675   1.00 10.55  ? 200 PRO B CG  1 
ATOM   3860  C  CD  . PRO B  1 200 ? -1.729  11.399  4.623   1.00 9.62   ? 200 PRO B CD  1 
ATOM   3861  N  N   A PRO B  1 201 ? -4.700  13.917  7.444   0.50 10.67  ? 201 PRO B N   1 
ATOM   3862  N  N   B PRO B  1 201 ? -4.758  13.877  7.383   0.50 9.16   ? 201 PRO B N   1 
ATOM   3863  C  CA  A PRO B  1 201 ? -3.769  14.524  8.434   0.50 11.04  ? 201 PRO B CA  1 
ATOM   3864  C  CA  B PRO B  1 201 ? -3.932  14.544  8.369   0.50 9.31   ? 201 PRO B CA  1 
ATOM   3865  C  C   A PRO B  1 201 ? -3.485  13.645  9.661   0.50 9.92   ? 201 PRO B C   1 
ATOM   3866  C  C   B PRO B  1 201 ? -3.391  13.649  9.499   0.50 9.25   ? 201 PRO B C   1 
ATOM   3867  O  O   A PRO B  1 201 ? -3.020  14.146  10.707  0.50 9.71   ? 201 PRO B O   1 
ATOM   3868  O  O   B PRO B  1 201 ? -2.644  14.168  10.326  0.50 8.25   ? 201 PRO B O   1 
ATOM   3869  C  CB  A PRO B  1 201 ? -4.491  15.805  8.874   0.50 13.78  ? 201 PRO B CB  1 
ATOM   3870  C  CB  B PRO B  1 201 ? -4.880  15.606  8.935   0.50 10.07  ? 201 PRO B CB  1 
ATOM   3871  C  CG  A PRO B  1 201 ? -5.861  15.726  8.312   0.50 17.90  ? 201 PRO B CG  1 
ATOM   3872  C  CG  B PRO B  1 201 ? -6.190  15.014  8.731   0.50 9.35   ? 201 PRO B CG  1 
ATOM   3873  C  CD  A PRO B  1 201 ? -6.082  14.373  7.676   0.50 14.22  ? 201 PRO B CD  1 
ATOM   3874  C  CD  B PRO B  1 201 ? -6.148  14.360  7.386   0.50 9.71   ? 201 PRO B CD  1 
ATOM   3875  N  N   . CYS B  1 202 ? -3.737  12.347  9.525   1.00 9.52   ? 202 CYS B N   1 
ATOM   3876  C  CA  . CYS B  1 202 ? -3.179  11.364  10.501  1.00 9.67   ? 202 CYS B CA  1 
ATOM   3877  C  C   . CYS B  1 202 ? -3.697  11.573  11.920  1.00 8.84   ? 202 CYS B C   1 
ATOM   3878  O  O   . CYS B  1 202 ? -3.086  11.192  12.886  1.00 9.82   ? 202 CYS B O   1 
ATOM   3879  C  CB  . CYS B  1 202 ? -1.636  11.374  10.553  1.00 10.67  ? 202 CYS B CB  1 
ATOM   3880  S  SG  . CYS B  1 202 ? -0.847  10.978  8.986   1.00 9.47   ? 202 CYS B SG  1 
ATOM   3881  N  N   . ASN B  1 203 ? -4.907  12.146  12.019  1.00 9.86   ? 203 ASN B N   1 
ATOM   3882  C  CA  . ASN B  1 203 ? -5.416  12.465  13.362  1.00 11.14  ? 203 ASN B CA  1 
ATOM   3883  C  C   . ASN B  1 203 ? -5.487  11.224  14.211  1.00 10.02  ? 203 ASN B C   1 
ATOM   3884  O  O   . ASN B  1 203 ? -6.001  10.213  13.749  1.00 9.83   ? 203 ASN B O   1 
ATOM   3885  C  CB  . ASN B  1 203 ? -6.816  13.093  13.296  1.00 12.46  ? 203 ASN B CB  1 
ATOM   3886  C  CG  . ASN B  1 203 ? -6.897  14.296  12.363  1.00 15.86  ? 203 ASN B CG  1 
ATOM   3887  O  OD1 . ASN B  1 203 ? -5.910  14.814  11.888  1.00 22.68  ? 203 ASN B OD1 1 
ATOM   3888  N  ND2 . ASN B  1 203 ? -8.084  14.813  12.215  1.00 22.08  ? 203 ASN B ND2 1 
ATOM   3889  N  N   . PRO B  1 204 ? -5.080  11.289  15.511  1.00 11.11  ? 204 PRO B N   1 
ATOM   3890  C  CA  . PRO B  1 204 ? -5.066  10.089  16.386  1.00 10.42  ? 204 PRO B CA  1 
ATOM   3891  C  C   . PRO B  1 204 ? -6.444  9.875   17.021  1.00 11.23  ? 204 PRO B C   1 
ATOM   3892  O  O   . PRO B  1 204 ? -6.559  9.841   18.264  1.00 14.05  ? 204 PRO B O   1 
ATOM   3893  C  CB  . PRO B  1 204 ? -3.957  10.429  17.341  1.00 13.35  ? 204 PRO B CB  1 
ATOM   3894  C  CG  . PRO B  1 204 ? -4.058  11.945  17.473  1.00 13.96  ? 204 PRO B CG  1 
ATOM   3895  C  CD  . PRO B  1 204 ? -4.318  12.412  16.074  1.00 12.65  ? 204 PRO B CD  1 
ATOM   3896  N  N   . THR B  1 205 ? -7.484  9.746   16.223  1.00 10.55  ? 205 THR B N   1 
ATOM   3897  C  CA  . THR B  1 205 ? -8.871  9.871   16.688  1.00 11.70  ? 205 THR B CA  1 
ATOM   3898  C  C   . THR B  1 205 ? -9.714  8.668   16.273  1.00 10.59  ? 205 THR B C   1 
ATOM   3899  O  O   . THR B  1 205 ? -10.944 8.722   16.320  1.00 12.58  ? 205 THR B O   1 
ATOM   3900  C  CB  . THR B  1 205 ? -9.470  11.177  16.109  1.00 13.04  ? 205 THR B CB  1 
ATOM   3901  O  OG1 . THR B  1 205 ? -9.292  11.099  14.720  1.00 13.54  ? 205 THR B OG1 1 
ATOM   3902  C  CG2 . THR B  1 205 ? -8.781  12.409  16.725  1.00 15.65  ? 205 THR B CG2 1 
ATOM   3903  N  N   . VAL B  1 206 ? -9.034  7.550   15.920  1.00 9.26   ? 206 VAL B N   1 
ATOM   3904  C  CA  . VAL B  1 206 ? -9.748  6.395   15.448  1.00 9.59   ? 206 VAL B CA  1 
ATOM   3905  C  C   . VAL B  1 206 ? -9.753  5.231   16.408  1.00 9.41   ? 206 VAL B C   1 
ATOM   3906  O  O   . VAL B  1 206 ? -8.679  4.795   16.832  1.00 10.81  ? 206 VAL B O   1 
ATOM   3907  C  CB  . VAL B  1 206 ? -9.165  5.909   14.089  1.00 9.76   ? 206 VAL B CB  1 
ATOM   3908  C  CG1 . VAL B  1 206 ? -9.889  4.653   13.583  1.00 9.27   ? 206 VAL B CG1 1 
ATOM   3909  C  CG2 . VAL B  1 206 ? -9.220  7.026   13.051  1.00 10.36  ? 206 VAL B CG2 1 
ATOM   3910  N  N   . LEU B  1 207 ? -10.937 4.697   16.680  1.00 8.85   ? 207 LEU B N   1 
ATOM   3911  C  CA  . LEU B  1 207 ? -11.069 3.404   17.296  1.00 9.02   ? 207 LEU B CA  1 
ATOM   3912  C  C   . LEU B  1 207 ? -11.092 2.352   16.185  1.00 7.61   ? 207 LEU B C   1 
ATOM   3913  O  O   . LEU B  1 207 ? -12.023 2.304   15.401  1.00 8.20   ? 207 LEU B O   1 
ATOM   3914  C  CB  . LEU B  1 207 ? -12.396 3.330   18.054  1.00 11.79  ? 207 LEU B CB  1 
ATOM   3915  C  CG  . LEU B  1 207 ? -12.533 2.259   19.069  1.00 17.35  ? 207 LEU B CG  1 
ATOM   3916  C  CD1 . LEU B  1 207 ? -11.357 2.313   20.077  1.00 24.45  ? 207 LEU B CD1 1 
ATOM   3917  C  CD2 . LEU B  1 207 ? -13.824 2.565   19.816  1.00 30.40  ? 207 LEU B CD2 1 
ATOM   3918  N  N   . TRP B  1 208 ? -10.003 1.586   16.077  1.00 7.98   ? 208 TRP B N   1 
ATOM   3919  C  CA  . TRP B  1 208 ? -9.871  0.563   15.033  1.00 7.44   ? 208 TRP B CA  1 
ATOM   3920  C  C   . TRP B  1 208 ? -10.455 -0.743  15.464  1.00 7.58   ? 208 TRP B C   1 
ATOM   3921  O  O   . TRP B  1 208 ? -10.221 -1.216  16.588  1.00 8.45   ? 208 TRP B O   1 
ATOM   3922  C  CB  . TRP B  1 208 ? -8.386  0.360   14.688  1.00 8.00   ? 208 TRP B CB  1 
ATOM   3923  C  CG  . TRP B  1 208 ? -7.876  1.423   13.795  1.00 7.40   ? 208 TRP B CG  1 
ATOM   3924  C  CD1 . TRP B  1 208 ? -7.165  2.543   14.139  1.00 8.06   ? 208 TRP B CD1 1 
ATOM   3925  C  CD2 . TRP B  1 208 ? -8.045  1.478   12.373  1.00 6.98   ? 208 TRP B CD2 1 
ATOM   3926  N  NE1 . TRP B  1 208 ? -6.943  3.310   13.023  1.00 7.85   ? 208 TRP B NE1 1 
ATOM   3927  C  CE2 . TRP B  1 208 ? -7.446  2.686   11.928  1.00 6.70   ? 208 TRP B CE2 1 
ATOM   3928  C  CE3 . TRP B  1 208 ? -8.637  0.633   11.440  1.00 7.46   ? 208 TRP B CE3 1 
ATOM   3929  C  CZ2 . TRP B  1 208 ? -7.487  3.076   10.585  1.00 7.44   ? 208 TRP B CZ2 1 
ATOM   3930  C  CZ3 . TRP B  1 208 ? -8.636  1.026   10.093  1.00 7.54   ? 208 TRP B CZ3 1 
ATOM   3931  C  CH2 . TRP B  1 208 ? -8.075  2.232   9.699   1.00 7.85   ? 208 TRP B CH2 1 
ATOM   3932  N  N   . THR B  1 209 ? -11.138 -1.404  14.541  1.00 7.05   ? 209 THR B N   1 
ATOM   3933  C  CA  . THR B  1 209 ? -11.568 -2.773  14.640  1.00 7.25   ? 209 THR B CA  1 
ATOM   3934  C  C   . THR B  1 209 ? -11.081 -3.483  13.371  1.00 6.77   ? 209 THR B C   1 
ATOM   3935  O  O   . THR B  1 209 ? -11.569 -3.141  12.297  1.00 8.11   ? 209 THR B O   1 
ATOM   3936  C  CB  . THR B  1 209 ? -13.106 -2.868  14.772  1.00 8.03   ? 209 THR B CB  1 
ATOM   3937  O  OG1 . THR B  1 209 ? -13.531 -2.152  15.896  1.00 8.59   ? 209 THR B OG1 1 
ATOM   3938  C  CG2 . THR B  1 209 ? -13.551 -4.312  14.867  1.00 8.92   ? 209 THR B CG2 1 
ATOM   3939  N  N   . VAL B  1 210 ? -10.170 -4.423  13.528  1.00 6.68   ? 210 VAL B N   1 
ATOM   3940  C  CA  . VAL B  1 210 ? -9.675  -5.168  12.357  1.00 6.52   ? 210 VAL B CA  1 
ATOM   3941  C  C   . VAL B  1 210 ? -10.208 -6.588  12.505  1.00 6.51   ? 210 VAL B C   1 
ATOM   3942  O  O   . VAL B  1 210 ? -9.931  -7.262  13.529  1.00 7.26   ? 210 VAL B O   1 
ATOM   3943  C  CB  . VAL B  1 210 ? -8.126  -5.169  12.313  1.00 7.62   ? 210 VAL B CB  1 
ATOM   3944  C  CG1 . VAL B  1 210 ? -7.666  -5.954  11.115  1.00 8.12   ? 210 VAL B CG1 1 
ATOM   3945  C  CG2 . VAL B  1 210 ? -7.540  -3.773  12.356  1.00 8.52   ? 210 VAL B CG2 1 
ATOM   3946  N  N   . PHE B  1 211 ? -11.023 -7.028  11.593  1.00 6.75   ? 211 PHE B N   1 
ATOM   3947  C  CA  . PHE B  1 211 ? -11.546 -8.370  11.750  1.00 7.17   ? 211 PHE B CA  1 
ATOM   3948  C  C   . PHE B  1 211 ? -10.435 -9.394  11.630  1.00 7.20   ? 211 PHE B C   1 
ATOM   3949  O  O   . PHE B  1 211 ? -9.507  -9.255  10.833  1.00 8.20   ? 211 PHE B O   1 
ATOM   3950  C  CB  . PHE B  1 211 ? -12.670 -8.595  10.740  1.00 8.11   ? 211 PHE B CB  1 
ATOM   3951  C  CG  . PHE B  1 211 ? -13.865 -7.756  11.019  1.00 7.28   ? 211 PHE B CG  1 
ATOM   3952  C  CD1 . PHE B  1 211 ? -14.658 -7.965  12.183  1.00 9.09   ? 211 PHE B CD1 1 
ATOM   3953  C  CD2 . PHE B  1 211 ? -14.199 -6.679  10.191  1.00 8.91   ? 211 PHE B CD2 1 
ATOM   3954  C  CE1 . PHE B  1 211 ? -15.724 -7.146  12.470  1.00 10.17  ? 211 PHE B CE1 1 
ATOM   3955  C  CE2 . PHE B  1 211 ? -15.277 -5.876  10.460  1.00 9.56   ? 211 PHE B CE2 1 
ATOM   3956  C  CZ  . PHE B  1 211 ? -16.054 -6.103  11.606  1.00 10.88  ? 211 PHE B CZ  1 
ATOM   3957  N  N   . ARG B  1 212 ? -10.554 -10.475 12.402  1.00 7.87   ? 212 ARG B N   1 
ATOM   3958  C  CA  . ARG B  1 212 ? -9.540  -11.505 12.405  1.00 8.56   ? 212 ARG B CA  1 
ATOM   3959  C  C   . ARG B  1 212 ? -9.446  -12.186 11.053  1.00 8.80   ? 212 ARG B C   1 
ATOM   3960  O  O   . ARG B  1 212 ? -8.333  -12.542 10.647  1.00 10.16  ? 212 ARG B O   1 
ATOM   3961  C  CB  . ARG B  1 212 ? -9.864  -12.527 13.469  1.00 9.41   ? 212 ARG B CB  1 
ATOM   3962  C  CG  . ARG B  1 212 ? -8.791  -13.553 13.623  1.00 11.01  ? 212 ARG B CG  1 
ATOM   3963  C  CD  . ARG B  1 212 ? -9.243  -14.649 14.607  1.00 12.36  ? 212 ARG B CD  1 
ATOM   3964  N  NE  . ARG B  1 212 ? -8.105  -15.545 14.867  1.00 14.69  ? 212 ARG B NE  1 
ATOM   3965  C  CZ  . ARG B  1 212 ? -8.113  -16.482 15.773  1.00 16.48  ? 212 ARG B CZ  1 
ATOM   3966  N  NH1 . ARG B  1 212 ? -9.236  -16.826 16.414  1.00 18.55  ? 212 ARG B NH1 1 
ATOM   3967  N  NH2 . ARG B  1 212 ? -6.974  -17.123 16.054  1.00 22.14  ? 212 ARG B NH2 1 
ATOM   3968  N  N   . ASN B  1 213 ? -10.569 -12.482 10.424  1.00 8.47   ? 213 ASN B N   1 
ATOM   3969  C  CA  . ASN B  1 213 ? -10.576 -13.345 9.255   1.00 9.22   ? 213 ASN B CA  1 
ATOM   3970  C  C   . ASN B  1 213 ? -10.606 -12.491 8.006   1.00 8.36   ? 213 ASN B C   1 
ATOM   3971  O  O   . ASN B  1 213 ? -11.388 -11.522 7.941   1.00 9.58   ? 213 ASN B O   1 
ATOM   3972  C  CB  . ASN B  1 213 ? -11.822 -14.211 9.261   1.00 11.02  ? 213 ASN B CB  1 
ATOM   3973  C  CG  . ASN B  1 213 ? -11.804 -15.119 10.498  1.00 14.21  ? 213 ASN B CG  1 
ATOM   3974  O  OD1 . ASN B  1 213 ? -10.773 -15.697 10.777  1.00 20.91  ? 213 ASN B OD1 1 
ATOM   3975  N  ND2 . ASN B  1 213 ? -12.820 -15.145 11.265  1.00 21.34  ? 213 ASN B ND2 1 
ATOM   3976  N  N   . PRO B  1 214 ? -9.821  -12.813 6.986   1.00 8.80   ? 214 PRO B N   1 
ATOM   3977  C  CA  . PRO B  1 214 ? -9.861  -12.096 5.717   1.00 8.45   ? 214 PRO B CA  1 
ATOM   3978  C  C   . PRO B  1 214 ? -11.029 -12.527 4.878   1.00 8.23   ? 214 PRO B C   1 
ATOM   3979  O  O   . PRO B  1 214 ? -11.621 -13.586 5.087   1.00 9.83   ? 214 PRO B O   1 
ATOM   3980  C  CB  . PRO B  1 214 ? -8.554  -12.465 5.054   1.00 10.24  ? 214 PRO B CB  1 
ATOM   3981  C  CG  . PRO B  1 214 ? -8.337  -13.908 5.509   1.00 13.84  ? 214 PRO B CG  1 
ATOM   3982  C  CD  . PRO B  1 214 ? -8.732  -13.819 7.010   1.00 11.63  ? 214 PRO B CD  1 
ATOM   3983  N  N   . VAL B  1 215 ? -11.321 -11.729 3.865   1.00 8.13   ? 215 VAL B N   1 
ATOM   3984  C  CA  . VAL B  1 215 ? -12.162 -12.120 2.725   1.00 7.65   ? 215 VAL B CA  1 
ATOM   3985  C  C   . VAL B  1 215 ? -11.261 -12.384 1.538   1.00 7.62   ? 215 VAL B C   1 
ATOM   3986  O  O   . VAL B  1 215 ? -10.090 -12.037 1.569   1.00 8.77   ? 215 VAL B O   1 
ATOM   3987  C  CB  . VAL B  1 215 ? -13.218 -11.042 2.405   1.00 8.40   ? 215 VAL B CB  1 
ATOM   3988  C  CG1 . VAL B  1 215 ? -14.136 -10.792 3.601   1.00 10.69  ? 215 VAL B CG1 1 
ATOM   3989  C  CG2 . VAL B  1 215 ? -12.581 -9.765  1.904   1.00 8.78   ? 215 VAL B CG2 1 
ATOM   3990  N  N   . GLN B  1 216 ? -11.840 -12.961 0.495   1.00 7.69   ? 216 GLN B N   1 
ATOM   3991  C  CA  . GLN B  1 216 ? -11.103 -13.218 -0.759  1.00 8.10   ? 216 GLN B CA  1 
ATOM   3992  C  C   . GLN B  1 216 ? -11.723 -12.415 -1.874  1.00 7.89   ? 216 GLN B C   1 
ATOM   3993  O  O   . GLN B  1 216 ? -12.948 -12.293 -1.996  1.00 9.17   ? 216 GLN B O   1 
ATOM   3994  C  CB  . GLN B  1 216 ? -11.187 -14.667 -1.168  1.00 9.97   ? 216 GLN B CB  1 
ATOM   3995  C  CG  . GLN B  1 216 ? -10.447 -15.587 -0.126  1.00 10.95  ? 216 GLN B CG  1 
ATOM   3996  C  CD  . GLN B  1 216 ? -10.429 -17.040 -0.554  1.00 11.88  ? 216 GLN B CD  1 
ATOM   3997  O  OE1 . GLN B  1 216 ? -11.009 -17.470 -1.560  1.00 12.22  ? 216 GLN B OE1 1 
ATOM   3998  N  NE2 . GLN B  1 216 ? -9.588  -17.773 0.117   1.00 18.88  ? 216 GLN B NE2 1 
ATOM   3999  N  N   . ILE B  1 217 ? -10.853 -11.928 -2.782  1.00 7.73   ? 217 ILE B N   1 
ATOM   4000  C  CA  . ILE B  1 217 ? -11.270 -11.433 -4.081  1.00 7.88   ? 217 ILE B CA  1 
ATOM   4001  C  C   . ILE B  1 217 ? -10.323 -12.099 -5.084  1.00 7.54   ? 217 ILE B C   1 
ATOM   4002  O  O   . ILE B  1 217 ? -9.231  -12.535 -4.702  1.00 8.43   ? 217 ILE B O   1 
ATOM   4003  C  CB  . ILE B  1 217 ? -11.261 -9.892  -4.222  1.00 8.01   ? 217 ILE B CB  1 
ATOM   4004  C  CG1 . ILE B  1 217 ? -9.862  -9.318  -4.144  1.00 8.38   ? 217 ILE B CG1 1 
ATOM   4005  C  CG2 . ILE B  1 217 ? -12.197 -9.303  -3.122  1.00 8.87   ? 217 ILE B CG2 1 
ATOM   4006  C  CD1 . ILE B  1 217 ? -9.810  -7.796  -4.358  1.00 10.11  ? 217 ILE B CD1 1 
ATOM   4007  N  N   . SER B  1 218 ? -10.678 -12.141 -6.353  1.00 7.83   ? 218 SER B N   1 
ATOM   4008  C  CA  . SER B  1 218 ? -9.824  -12.865 -7.306  1.00 8.28   ? 218 SER B CA  1 
ATOM   4009  C  C   . SER B  1 218 ? -8.647  -12.077 -7.776  1.00 8.66   ? 218 SER B C   1 
ATOM   4010  O  O   . SER B  1 218 ? -8.602  -10.850 -7.711  1.00 9.46   ? 218 SER B O   1 
ATOM   4011  C  CB  . SER B  1 218 ? -10.601 -13.380 -8.476  1.00 9.36   ? 218 SER B CB  1 
ATOM   4012  O  OG  . SER B  1 218 ? -10.997 -12.253 -9.256  1.00 10.42  ? 218 SER B OG  1 
ATOM   4013  N  N   . GLN B  1 219 ? -7.704  -12.787 -8.371  1.00 10.18  ? 219 GLN B N   1 
ATOM   4014  C  CA  . GLN B  1 219 ? -6.563  -12.161 -9.072  1.00 10.83  ? 219 GLN B CA  1 
ATOM   4015  C  C   . GLN B  1 219 ? -7.073  -11.164 -10.082 1.00 10.57  ? 219 GLN B C   1 
ATOM   4016  O  O   . GLN B  1 219 ? -6.501  -10.052 -10.225 1.00 10.86  ? 219 GLN B O   1 
ATOM   4017  C  CB  . GLN B  1 219 ? -5.786  -13.248 -9.763  1.00 16.57  ? 219 GLN B CB  1 
ATOM   4018  C  CG  . GLN B  1 219 ? -4.480  -12.615 -10.325 1.00 23.26  ? 219 GLN B CG  1 
ATOM   4019  C  CD  . GLN B  1 219 ? -4.462  -11.928 -11.637 1.00 28.78  ? 219 GLN B CD  1 
ATOM   4020  O  OE1 . GLN B  1 219 ? -3.555  -11.089 -11.870 1.00 33.76  ? 219 GLN B OE1 1 
ATOM   4021  N  NE2 . GLN B  1 219 ? -5.400  -12.272 -12.530 1.00 35.35  ? 219 GLN B NE2 1 
ATOM   4022  N  N   . GLU B  1 220 ? -8.127  -11.503 -10.836 1.00 10.98  ? 220 GLU B N   1 
ATOM   4023  C  CA  . GLU B  1 220 ? -8.650  -10.580 -11.866 1.00 12.77  ? 220 GLU B CA  1 
ATOM   4024  C  C   . GLU B  1 220 ? -9.246  -9.345  -11.237 1.00 10.59  ? 220 GLU B C   1 
ATOM   4025  O  O   . GLU B  1 220 ? -9.114  -8.236  -11.751 1.00 11.24  ? 220 GLU B O   1 
ATOM   4026  C  CB  . GLU B  1 220 ? -9.644  -11.304 -12.778 1.00 14.81  ? 220 GLU B CB  1 
ATOM   4027  C  CG  . GLU B  1 220 ? -8.936  -12.451 -13.580 1.00 15.71  ? 220 GLU B CG  1 
ATOM   4028  C  CD  . GLU B  1 220 ? -8.726  -13.717 -12.841 1.00 17.86  ? 220 GLU B CD  1 
ATOM   4029  O  OE1 . GLU B  1 220 ? -9.198  -13.970 -11.723 1.00 16.30  ? 220 GLU B OE1 1 
ATOM   4030  O  OE2 . GLU B  1 220 ? -8.188  -14.634 -13.499 1.00 25.92  ? 220 GLU B OE2 1 
ATOM   4031  N  N   . GLN B  1 221 ? -9.914  -9.499  -10.090 1.00 9.98   ? 221 GLN B N   1 
ATOM   4032  C  CA  . GLN B  1 221 ? -10.472 -8.324  -9.403  1.00 9.59   ? 221 GLN B CA  1 
ATOM   4033  C  C   . GLN B  1 221 ? -9.371  -7.436  -8.871  1.00 9.13   ? 221 GLN B C   1 
ATOM   4034  O  O   . GLN B  1 221 ? -9.398  -6.218  -8.979  1.00 9.93   ? 221 GLN B O   1 
ATOM   4035  C  CB  . GLN B  1 221 ? -11.368 -8.800  -8.253  1.00 9.23   ? 221 GLN B CB  1 
ATOM   4036  C  CG  . GLN B  1 221 ? -12.656 -9.418  -8.763  1.00 9.03   ? 221 GLN B CG  1 
ATOM   4037  C  CD  . GLN B  1 221 ? -13.546 -9.814  -7.622  1.00 8.10   ? 221 GLN B CD  1 
ATOM   4038  O  OE1 . GLN B  1 221 ? -13.238 -10.756 -6.868  1.00 8.73   ? 221 GLN B OE1 1 
ATOM   4039  N  NE2 . GLN B  1 221 ? -14.681 -9.137  -7.432  1.00 9.39   ? 221 GLN B NE2 1 
ATOM   4040  N  N   . LEU B  1 222 ? -8.336  -8.054  -8.297  1.00 9.01   ? 222 LEU B N   1 
ATOM   4041  C  CA  . LEU B  1 222 ? -7.189  -7.256  -7.864  1.00 9.30   ? 222 LEU B CA  1 
ATOM   4042  C  C   . LEU B  1 222 ? -6.537  -6.531  -9.014  1.00 9.56   ? 222 LEU B C   1 
ATOM   4043  O  O   . LEU B  1 222 ? -6.204  -5.372  -8.873  1.00 9.72   ? 222 LEU B O   1 
ATOM   4044  C  CB  . LEU B  1 222 ? -6.190  -8.179  -7.120  1.00 10.69  ? 222 LEU B CB  1 
ATOM   4045  C  CG  . LEU B  1 222 ? -6.570  -8.521  -5.723  1.00 10.23  ? 222 LEU B CG  1 
ATOM   4046  C  CD1 . LEU B  1 222 ? -5.855  -9.797  -5.231  1.00 10.86  ? 222 LEU B CD1 1 
ATOM   4047  C  CD2 . LEU B  1 222 ? -6.210  -7.347  -4.772  1.00 11.03  ? 222 LEU B CD2 1 
ATOM   4048  N  N   . LEU B  1 223 ? -6.330  -7.208  -10.129 1.00 10.12  ? 223 LEU B N   1 
ATOM   4049  C  CA  . LEU B  1 223 ? -5.674  -6.553  -11.259 1.00 11.88  ? 223 LEU B CA  1 
ATOM   4050  C  C   . LEU B  1 223 ? -6.523  -5.392  -11.743 1.00 11.21  ? 223 LEU B C   1 
ATOM   4051  O  O   . LEU B  1 223 ? -6.005  -4.331  -12.082 1.00 12.41  ? 223 LEU B O   1 
ATOM   4052  C  CB  . LEU B  1 223 ? -5.486  -7.598  -12.448 1.00 13.10  ? 223 LEU B CB  1 
ATOM   4053  C  CG  . LEU B  1 223 ? -4.802  -7.079  -13.667 1.00 14.70  ? 223 LEU B CG  1 
ATOM   4054  C  CD1 . LEU B  1 223 ? -3.401  -6.592  -13.288 1.00 17.99  ? 223 LEU B CD1 1 
ATOM   4055  C  CD2 . LEU B  1 223 ? -4.839  -8.137  -14.757 1.00 18.79  ? 223 LEU B CD2 1 
ATOM   4056  N  N   . ALA B  1 224 ? -7.850  -5.586  -11.794 1.00 12.12  ? 224 ALA B N   1 
ATOM   4057  C  CA  . ALA B  1 224 ? -8.750  -4.474  -12.209 1.00 11.94  ? 224 ALA B CA  1 
ATOM   4058  C  C   . ALA B  1 224 ? -8.582  -3.289  -11.281 1.00 12.00  ? 224 ALA B C   1 
ATOM   4059  O  O   . ALA B  1 224 ? -8.400  -2.153  -11.683 1.00 13.57  ? 224 ALA B O   1 
ATOM   4060  C  CB  . ALA B  1 224 ? -10.173 -4.896  -12.303 1.00 14.76  ? 224 ALA B CB  1 
ATOM   4061  N  N   . LEU B  1 225 ? -8.662  -3.586  -9.985  1.00 11.70  ? 225 LEU B N   1 
ATOM   4062  C  CA  . LEU B  1 225 ? -8.491  -2.503  -8.973  1.00 11.05  ? 225 LEU B CA  1 
ATOM   4063  C  C   . LEU B  1 225 ? -7.172  -1.763  -9.102  1.00 11.21  ? 225 LEU B C   1 
ATOM   4064  O  O   . LEU B  1 225 ? -7.117  -0.544  -8.996  1.00 12.44  ? 225 LEU B O   1 
ATOM   4065  C  CB  . LEU B  1 225 ? -8.652  -3.152  -7.583  1.00 10.14  ? 225 LEU B CB  1 
ATOM   4066  C  CG  . LEU B  1 225 ? -8.473  -2.190  -6.384  1.00 11.19  ? 225 LEU B CG  1 
ATOM   4067  C  CD1 . LEU B  1 225 ? -9.486  -1.065  -6.367  1.00 11.63  ? 225 LEU B CD1 1 
ATOM   4068  C  CD2 . LEU B  1 225 ? -8.510  -2.981  -5.098  1.00 11.25  ? 225 LEU B CD2 1 
ATOM   4069  N  N   . GLU B  1 226 ? -6.104  -2.545  -9.340  1.00 9.76   ? 226 GLU B N   1 
ATOM   4070  C  CA  . GLU B  1 226 ? -4.762  -2.027  -9.379  1.00 10.49  ? 226 GLU B CA  1 
ATOM   4071  C  C   . GLU B  1 226 ? -4.432  -1.327  -10.744 1.00 9.42   ? 226 GLU B C   1 
ATOM   4072  O  O   . GLU B  1 226 ? -3.404  -0.696  -10.771 1.00 13.62  ? 226 GLU B O   1 
ATOM   4073  C  CB  . GLU B  1 226 ? -3.749  -3.186  -9.216  1.00 10.42  ? 226 GLU B CB  1 
ATOM   4074  C  CG  . GLU B  1 226 ? -3.758  -3.810  -7.807  1.00 10.98  ? 226 GLU B CG  1 
ATOM   4075  C  CD  . GLU B  1 226 ? -3.365  -5.277  -7.817  1.00 11.12  ? 226 GLU B CD  1 
ATOM   4076  O  OE1 . GLU B  1 226 ? -3.033  -5.800  -8.936  1.00 12.72  ? 226 GLU B OE1 1 
ATOM   4077  O  OE2 . GLU B  1 226 ? -3.420  -5.956  -6.789  1.00 12.54  ? 226 GLU B OE2 1 
ATOM   4078  N  N   . THR B  1 227 ? -5.321  -1.432  -11.712 1.00 10.78  ? 227 THR B N   1 
ATOM   4079  C  CA  . THR B  1 227 ? -5.019  -0.790  -13.036 1.00 12.71  ? 227 THR B CA  1 
ATOM   4080  C  C   . THR B  1 227 ? -6.119  0.197   -13.387 1.00 12.86  ? 227 THR B C   1 
ATOM   4081  O  O   . THR B  1 227 ? -5.986  0.839   -14.413 1.00 18.29  ? 227 THR B O   1 
ATOM   4082  C  CB  . THR B  1 227 ? -4.910  -1.826  -14.189 1.00 13.47  ? 227 THR B CB  1 
ATOM   4083  O  OG1 . THR B  1 227 ? -6.127  -2.596  -14.233 1.00 13.08  ? 227 THR B OG1 1 
ATOM   4084  C  CG2 . THR B  1 227 ? -3.725  -2.757  -13.926 1.00 13.72  ? 227 THR B CG2 1 
ATOM   4085  N  N   . ALA B  1 228 ? -7.145  0.376   -12.609 1.00 12.61  ? 228 ALA B N   1 
ATOM   4086  C  CA  . ALA B  1 228 ? -8.294  1.148   -13.013 1.00 17.07  ? 228 ALA B CA  1 
ATOM   4087  C  C   . ALA B  1 228 ? -8.070  2.662   -12.786 1.00 15.97  ? 228 ALA B C   1 
ATOM   4088  O  O   . ALA B  1 228 ? -8.734  3.463   -13.384 1.00 23.64  ? 228 ALA B O   1 
ATOM   4089  C  CB  . ALA B  1 228 ? -9.543  0.710   -12.203 1.00 23.77  ? 228 ALA B CB  1 
ATOM   4090  N  N   . LEU B  1 229 ? -7.293  3.028   -11.768 1.00 11.88  ? 229 LEU B N   1 
ATOM   4091  C  CA  . LEU B  1 229 ? -7.402  4.314   -11.162 1.00 10.62  ? 229 LEU B CA  1 
ATOM   4092  C  C   . LEU B  1 229 ? -6.143  5.122   -11.198 1.00 10.55  ? 229 LEU B C   1 
ATOM   4093  O  O   . LEU B  1 229 ? -5.038  4.600   -11.141 1.00 11.11  ? 229 LEU B O   1 
ATOM   4094  C  CB  . LEU B  1 229 ? -7.855  4.219   -9.652  1.00 11.82  ? 229 LEU B CB  1 
ATOM   4095  C  CG  . LEU B  1 229 ? -9.203  3.471   -9.488  1.00 11.79  ? 229 LEU B CG  1 
ATOM   4096  C  CD1 . LEU B  1 229 ? -9.418  3.195   -8.010  1.00 13.94  ? 229 LEU B CD1 1 
ATOM   4097  C  CD2 . LEU B  1 229 ? -10.344 4.330   -9.958  1.00 19.45  ? 229 LEU B CD2 1 
ATOM   4098  N  N   . TYR B  1 230 ? -6.342  6.431   -11.252 1.00 11.64  ? 230 TYR B N   1 
ATOM   4099  C  CA  . TYR B  1 230 ? -5.278  7.406   -11.256 1.00 12.48  ? 230 TYR B CA  1 
ATOM   4100  C  C   . TYR B  1 230 ? -5.515  8.438   -10.107 1.00 12.12  ? 230 TYR B C   1 
ATOM   4101  O  O   . TYR B  1 230 ? -6.631  8.776   -9.769  1.00 12.91  ? 230 TYR B O   1 
ATOM   4102  C  CB  . TYR B  1 230 ? -5.228  8.161   -12.624 1.00 12.41  ? 230 TYR B CB  1 
ATOM   4103  C  CG  . TYR B  1 230 ? -4.658  7.281   -13.685 1.00 11.58  ? 230 TYR B CG  1 
ATOM   4104  C  CD1 . TYR B  1 230 ? -5.433  6.305   -14.257 1.00 15.33  ? 230 TYR B CD1 1 
ATOM   4105  C  CD2 . TYR B  1 230 ? -3.327  7.370   -14.031 1.00 15.36  ? 230 TYR B CD2 1 
ATOM   4106  C  CE1 . TYR B  1 230 ? -4.923  5.383   -15.140 1.00 18.23  ? 230 TYR B CE1 1 
ATOM   4107  C  CE2 . TYR B  1 230 ? -2.798  6.412   -14.927 1.00 20.07  ? 230 TYR B CE2 1 
ATOM   4108  C  CZ  . TYR B  1 230 ? -3.639  5.449   -15.446 1.00 19.85  ? 230 TYR B CZ  1 
ATOM   4109  O  OH  . TYR B  1 230 ? -3.207  4.488   -16.328 1.00 26.89  ? 230 TYR B OH  1 
ATOM   4110  N  N   . CYS B  1 231 ? -4.406  8.892   -9.576  1.00 12.77  ? 231 CYS B N   1 
ATOM   4111  C  CA  . CYS B  1 231 ? -4.415  9.943   -8.569  1.00 11.89  ? 231 CYS B CA  1 
ATOM   4112  C  C   . CYS B  1 231 ? -4.688  11.321  -9.149  1.00 12.79  ? 231 CYS B C   1 
ATOM   4113  O  O   . CYS B  1 231 ? -5.004  12.255  -8.436  1.00 13.86  ? 231 CYS B O   1 
ATOM   4114  C  CB  . CYS B  1 231 ? -3.051  10.020  -7.913  1.00 15.84  ? 231 CYS B CB  1 
ATOM   4115  S  SG  . CYS B  1 231 ? -2.556  8.487   -7.031  1.00 16.95  ? 231 CYS B SG  1 
ATOM   4116  N  N   . THR B  1 232 ? -4.474  11.440  -10.437 1.00 12.90  ? 232 THR B N   1 
ATOM   4117  C  CA  . THR B  1 232 ? -4.469  12.715  -11.155 1.00 11.37  ? 232 THR B CA  1 
ATOM   4118  C  C   . THR B  1 232 ? -5.770  12.936  -11.918 1.00 11.59  ? 232 THR B C   1 
ATOM   4119  O  O   . THR B  1 232 ? -6.510  12.030  -12.214 1.00 12.78  ? 232 THR B O   1 
ATOM   4120  C  CB  . THR B  1 232 ? -3.215  12.712  -12.058 1.00 11.27  ? 232 THR B CB  1 
ATOM   4121  O  OG1 . THR B  1 232 ? -3.062  11.444  -12.696 1.00 11.77  ? 232 THR B OG1 1 
ATOM   4122  C  CG2 . THR B  1 232 ? -1.985  12.989  -11.273 1.00 14.44  ? 232 THR B CG2 1 
ATOM   4123  N  N   . HIS B  1 233 ? -5.972  14.220  -12.256 1.00 12.91  ? 233 HIS B N   1 
ATOM   4124  C  CA  . HIS B  1 233 ? -7.094  14.573  -13.136 1.00 12.81  ? 233 HIS B CA  1 
ATOM   4125  C  C   . HIS B  1 233 ? -6.987  14.034  -14.530 1.00 11.04  ? 233 HIS B C   1 
ATOM   4126  O  O   . HIS B  1 233 ? -5.862  13.759  -15.017 1.00 12.70  ? 233 HIS B O   1 
ATOM   4127  C  CB  . HIS B  1 233 ? -7.207  16.102  -13.205 1.00 16.20  ? 233 HIS B CB  1 
ATOM   4128  C  CG  . HIS B  1 233 ? -7.673  16.698  -11.924 1.00 19.56  ? 233 HIS B CG  1 
ATOM   4129  N  ND1 . HIS B  1 233 ? -6.913  17.490  -11.160 1.00 31.40  ? 233 HIS B ND1 1 
ATOM   4130  C  CD2 . HIS B  1 233 ? -8.856  16.584  -11.272 1.00 22.63  ? 233 HIS B CD2 1 
ATOM   4131  C  CE1 . HIS B  1 233 ? -7.582  17.884  -10.072 1.00 35.62  ? 233 HIS B CE1 1 
ATOM   4132  N  NE2 . HIS B  1 233 ? -8.767  17.332  -10.132 1.00 26.95  ? 233 HIS B NE2 1 
ATOM   4133  N  N   A MET B  1 234 ? -8.102  13.950  -15.244 0.50 11.73  ? 234 MET B N   1 
ATOM   4134  N  N   B MET B  1 234 ? -8.123  13.882  -15.178 0.50 12.56  ? 234 MET B N   1 
ATOM   4135  C  CA  A MET B  1 234 ? -8.148  13.343  -16.603 0.50 12.89  ? 234 MET B CA  1 
ATOM   4136  C  CA  B MET B  1 234 ? -8.115  13.358  -16.524 0.50 12.11  ? 234 MET B CA  1 
ATOM   4137  C  C   A MET B  1 234 ? -7.309  14.120  -17.665 0.50 11.74  ? 234 MET B C   1 
ATOM   4138  C  C   B MET B  1 234 ? -7.069  14.158  -17.351 0.50 10.52  ? 234 MET B C   1 
ATOM   4139  O  O   A MET B  1 234 ? -6.821  13.536  -18.653 0.50 9.50   ? 234 MET B O   1 
ATOM   4140  O  O   B MET B  1 234 ? -6.364  13.545  -18.133 0.50 10.95  ? 234 MET B O   1 
ATOM   4141  C  CB  A MET B  1 234 ? -9.618  13.306  -17.028 0.50 12.46  ? 234 MET B CB  1 
ATOM   4142  C  CB  B MET B  1 234 ? -9.542  13.466  -17.104 0.50 14.71  ? 234 MET B CB  1 
ATOM   4143  C  CG  A MET B  1 234 ? -9.839  12.837  -18.491 0.50 17.74  ? 234 MET B CG  1 
ATOM   4144  C  CG  B MET B  1 234 ? -9.776  12.645  -18.446 0.50 15.69  ? 234 MET B CG  1 
ATOM   4145  S  SD  A MET B  1 234 ? -11.576 12.925  -18.931 0.50 17.40  ? 234 MET B SD  1 
ATOM   4146  S  SD  B MET B  1 234 ? -11.554 12.342  -18.675 0.50 20.02  ? 234 MET B SD  1 
ATOM   4147  C  CE  A MET B  1 234 ? -11.492 11.965  -20.421 0.50 18.05  ? 234 MET B CE  1 
ATOM   4148  C  CE  B MET B  1 234 ? -12.231 13.962  -18.497 0.50 23.76  ? 234 MET B CE  1 
ATOM   4149  N  N   A ASP B  1 235 ? -7.108  15.413  -17.451 0.50 10.50  ? 235 ASP B N   1 
ATOM   4150  N  N   B ASP B  1 235 ? -6.956  15.480  -17.138 0.50 12.70  ? 235 ASP B N   1 
ATOM   4151  C  CA  A ASP B  1 235 ? -6.258  16.182  -18.360 0.50 12.81  ? 235 ASP B CA  1 
ATOM   4152  C  CA  B ASP B  1 235 ? -6.164  16.343  -18.011 0.50 13.95  ? 235 ASP B CA  1 
ATOM   4153  C  C   A ASP B  1 235 ? -4.798  16.360  -17.811 0.50 11.78  ? 235 ASP B C   1 
ATOM   4154  C  C   B ASP B  1 235 ? -4.844  16.570  -17.606 0.50 12.56  ? 235 ASP B C   1 
ATOM   4155  O  O   A ASP B  1 235 ? -4.002  17.054  -18.461 0.50 13.38  ? 235 ASP B O   1 
ATOM   4156  O  O   B ASP B  1 235 ? -4.188  17.517  -18.097 0.50 13.48  ? 235 ASP B O   1 
ATOM   4157  C  CB  A ASP B  1 235 ? -6.887  17.544  -18.680 0.50 14.25  ? 235 ASP B CB  1 
ATOM   4158  C  CB  B ASP B  1 235 ? -6.764  17.724  -18.003 0.50 18.32  ? 235 ASP B CB  1 
ATOM   4159  C  CG  A ASP B  1 235 ? -6.977  18.473  -17.465 0.50 16.26  ? 235 ASP B CG  1 
ATOM   4160  C  CG  B ASP B  1 235 ? -7.997  17.802  -18.780 0.50 27.30  ? 235 ASP B CG  1 
ATOM   4161  O  OD1 A ASP B  1 235 ? -6.597  18.078  -16.338 0.50 19.09  ? 235 ASP B OD1 1 
ATOM   4162  O  OD1 B ASP B  1 235 ? -8.334  16.786  -19.422 0.50 30.88  ? 235 ASP B OD1 1 
ATOM   4163  O  OD2 A ASP B  1 235 ? -7.436  19.621  -17.655 0.50 26.96  ? 235 ASP B OD2 1 
ATOM   4164  O  OD2 B ASP B  1 235 ? -8.625  18.874  -18.734 0.50 34.55  ? 235 ASP B OD2 1 
ATOM   4165  N  N   . ASP B  1 236 ? -4.384  15.755  -16.701 1.00 12.58  ? 236 ASP B N   1 
ATOM   4166  C  CA  . ASP B  1 236 ? -3.090  16.078  -16.117 1.00 11.61  ? 236 ASP B CA  1 
ATOM   4167  C  C   . ASP B  1 236 ? -1.994  15.607  -17.094 1.00 10.94  ? 236 ASP B C   1 
ATOM   4168  O  O   . ASP B  1 236 ? -1.970  14.409  -17.485 1.00 11.45  ? 236 ASP B O   1 
ATOM   4169  C  CB  . ASP B  1 236 ? -2.917  15.372  -14.774 1.00 13.85  ? 236 ASP B CB  1 
ATOM   4170  C  CG  . ASP B  1 236 ? -1.737  15.931  -13.937 1.00 14.39  ? 236 ASP B CG  1 
ATOM   4171  O  OD1 . ASP B  1 236 ? -0.621  16.103  -14.432 1.00 15.08  ? 236 ASP B OD1 1 
ATOM   4172  O  OD2 . ASP B  1 236 ? -1.921  16.268  -12.775 1.00 18.55  ? 236 ASP B OD2 1 
ATOM   4173  N  N   . PRO B  1 237 ? -1.034  16.422  -17.452 1.00 12.40  ? 237 PRO B N   1 
ATOM   4174  C  CA  . PRO B  1 237 ? 0.052   15.951  -18.340 1.00 12.55  ? 237 PRO B CA  1 
ATOM   4175  C  C   . PRO B  1 237 ? 1.104   15.062  -17.653 1.00 11.83  ? 237 PRO B C   1 
ATOM   4176  O  O   . PRO B  1 237 ? 2.004   14.555  -18.336 1.00 12.69  ? 237 PRO B O   1 
ATOM   4177  C  CB  . PRO B  1 237 ? 0.711   17.305  -18.856 1.00 14.55  ? 237 PRO B CB  1 
ATOM   4178  C  CG  . PRO B  1 237 ? 0.464   18.215  -17.650 1.00 17.60  ? 237 PRO B CG  1 
ATOM   4179  C  CD  . PRO B  1 237 ? -0.955  17.878  -17.195 1.00 13.02  ? 237 PRO B CD  1 
ATOM   4180  N  N   A SER B  1 238 ? 0.968   14.827  -16.356 0.50 11.60  ? 238 SER B N   1 
ATOM   4181  N  N   B SER B  1 238 ? 1.059   14.914  -16.335 0.50 10.82  ? 238 SER B N   1 
ATOM   4182  C  CA  A SER B  1 238 ? 1.941   14.021  -15.615 0.50 12.49  ? 238 SER B CA  1 
ATOM   4183  C  CA  B SER B  1 238 ? 1.913   13.945  -15.607 0.50 10.73  ? 238 SER B CA  1 
ATOM   4184  C  C   A SER B  1 238 ? 1.169   12.966  -14.787 0.50 10.61  ? 238 SER B C   1 
ATOM   4185  C  C   B SER B  1 238 ? 0.987   13.043  -14.804 0.50 9.59   ? 238 SER B C   1 
ATOM   4186  O  O   A SER B  1 238 ? 1.211   12.982  -13.526 0.50 11.34  ? 238 SER B O   1 
ATOM   4187  O  O   B SER B  1 238 ? 0.730   13.233  -13.601 0.50 9.69   ? 238 SER B O   1 
ATOM   4188  C  CB  A SER B  1 238 ? 2.737   14.938  -14.682 0.50 17.05  ? 238 SER B CB  1 
ATOM   4189  C  CB  B SER B  1 238 ? 2.802   14.684  -14.647 0.50 14.76  ? 238 SER B CB  1 
ATOM   4190  O  OG  A SER B  1 238 ? 3.780   14.144  -14.116 0.50 25.15  ? 238 SER B OG  1 
ATOM   4191  O  OG  B SER B  1 238 ? 3.569   15.650  -15.353 0.50 17.18  ? 238 SER B OG  1 
ATOM   4192  N  N   . PRO B  1 239 ? 0.418   12.047  -15.495 1.00 10.55  ? 239 PRO B N   1 
ATOM   4193  C  CA  . PRO B  1 239 ? -0.467  11.136  -14.787 1.00 11.53  ? 239 PRO B CA  1 
ATOM   4194  C  C   . PRO B  1 239 ? 0.264   10.305  -13.767 1.00 10.61  ? 239 PRO B C   1 
ATOM   4195  O  O   . PRO B  1 239 ? 1.434   9.929   -13.941 1.00 12.17  ? 239 PRO B O   1 
ATOM   4196  C  CB  . PRO B  1 239 ? -0.965  10.222  -15.894 1.00 13.36  ? 239 PRO B CB  1 
ATOM   4197  C  CG  . PRO B  1 239 ? -0.582  10.814  -17.153 1.00 16.44  ? 239 PRO B CG  1 
ATOM   4198  C  CD  . PRO B  1 239 ? 0.452   11.834  -16.959 1.00 11.43  ? 239 PRO B CD  1 
ATOM   4199  N  N   . ARG B  1 240 ? -0.417  9.945   -12.678 1.00 11.38  ? 240 ARG B N   1 
ATOM   4200  C  CA  . ARG B  1 240 ? 0.102   9.022   -11.694 1.00 12.67  ? 240 ARG B CA  1 
ATOM   4201  C  C   . ARG B  1 240 ? -0.906  7.965   -11.369 1.00 11.54  ? 240 ARG B C   1 
ATOM   4202  O  O   . ARG B  1 240 ? -2.046  8.295   -11.028 1.00 12.42  ? 240 ARG B O   1 
ATOM   4203  C  CB  . ARG B  1 240 ? 0.435   9.800   -10.429 1.00 13.11  ? 240 ARG B CB  1 
ATOM   4204  C  CG  . ARG B  1 240 ? 1.658   10.757  -10.605 1.00 17.11  ? 240 ARG B CG  1 
ATOM   4205  C  CD  . ARG B  1 240 ? 1.935   11.516  -9.346  1.00 16.28  ? 240 ARG B CD  1 
ATOM   4206  N  NE  . ARG B  1 240 ? 0.895   12.507  -8.987  1.00 20.14  ? 240 ARG B NE  1 
ATOM   4207  C  CZ  . ARG B  1 240 ? -0.033  12.336  -8.026  1.00 17.70  ? 240 ARG B CZ  1 
ATOM   4208  N  NH1 . ARG B  1 240 ? -0.058  11.250  -7.253  1.00 17.72  ? 240 ARG B NH1 1 
ATOM   4209  N  NH2 . ARG B  1 240 ? -0.913  13.312  -7.813  1.00 22.84  ? 240 ARG B NH2 1 
ATOM   4210  N  N   . GLU B  1 241 ? -0.515  6.715   -11.547 1.00 12.33  ? 241 GLU B N   1 
ATOM   4211  C  CA  . GLU B  1 241 ? -1.392  5.573   -11.251 1.00 12.85  ? 241 GLU B CA  1 
ATOM   4212  C  C   . GLU B  1 241 ? -1.666  5.491   -9.748  1.00 11.70  ? 241 GLU B C   1 
ATOM   4213  O  O   . GLU B  1 241 ? -0.766  5.708   -8.927  1.00 12.65  ? 241 GLU B O   1 
ATOM   4214  C  CB  . GLU B  1 241 ? -0.702  4.259   -11.674 1.00 14.84  ? 241 GLU B CB  1 
ATOM   4215  C  CG  . GLU B  1 241 ? -0.614  4.144   -13.190 1.00 15.77  ? 241 GLU B CG  1 
ATOM   4216  C  CD  . GLU B  1 241 ? 0.345   3.086   -13.567 1.00 22.10  ? 241 GLU B CD  1 
ATOM   4217  O  OE1 . GLU B  1 241 ? 1.469   3.082   -13.084 1.00 31.73  ? 241 GLU B OE1 1 
ATOM   4218  O  OE2 . GLU B  1 241 ? -0.036  2.238   -14.340 1.00 30.30  ? 241 GLU B OE2 1 
ATOM   4219  N  N   . MET B  1 242 ? -2.903  5.183   -9.376  1.00 11.08  ? 242 MET B N   1 
ATOM   4220  C  CA  . MET B  1 242 ? -3.253  4.985   -7.951  1.00 12.09  ? 242 MET B CA  1 
ATOM   4221  C  C   . MET B  1 242 ? -2.942  3.496   -7.620  1.00 9.95   ? 242 MET B C   1 
ATOM   4222  O  O   . MET B  1 242 ? -3.776  2.606   -7.822  1.00 10.63  ? 242 MET B O   1 
ATOM   4223  C  CB  . MET B  1 242 ? -4.725  5.265   -7.752  1.00 10.89  ? 242 MET B CB  1 
ATOM   4224  C  CG  . MET B  1 242 ? -5.102  5.307   -6.227  1.00 11.74  ? 242 MET B CG  1 
ATOM   4225  S  SD  . MET B  1 242 ? -6.784  5.648   -5.956  1.00 11.59  ? 242 MET B SD  1 
ATOM   4226  C  CE  . MET B  1 242 ? -6.885  7.387   -6.416  1.00 14.27  ? 242 MET B CE  1 
ATOM   4227  N  N   . ILE B  1 243 ? -1.715  3.321   -7.149  1.00 9.82   ? 243 ILE B N   1 
ATOM   4228  C  CA  . ILE B  1 243 ? -1.171  2.033   -6.782  1.00 9.26   ? 243 ILE B CA  1 
ATOM   4229  C  C   . ILE B  1 243 ? -0.393  2.182   -5.500  1.00 8.79   ? 243 ILE B C   1 
ATOM   4230  O  O   . ILE B  1 243 ? 0.059   3.313   -5.119  1.00 9.70   ? 243 ILE B O   1 
ATOM   4231  C  CB  . ILE B  1 243 ? -0.276  1.468   -7.935  1.00 10.99  ? 243 ILE B CB  1 
ATOM   4232  C  CG1 . ILE B  1 243 ? 0.873   2.401   -8.244  1.00 14.14  ? 243 ILE B CG1 1 
ATOM   4233  C  CG2 . ILE B  1 243 ? -1.119  0.954   -9.108  1.00 13.50  ? 243 ILE B CG2 1 
ATOM   4234  C  CD1 . ILE B  1 243 ? 1.840   1.865   -9.296  1.00 15.67  ? 243 ILE B CD1 1 
ATOM   4235  N  N   . ASN B  1 244 ? -0.227  1.084   -4.780  1.00 8.40   ? 244 ASN B N   1 
ATOM   4236  C  CA  . ASN B  1 244 ? 0.607   1.117   -3.606  1.00 7.97   ? 244 ASN B CA  1 
ATOM   4237  C  C   . ASN B  1 244 ? 0.173   2.151   -2.581  1.00 7.75   ? 244 ASN B C   1 
ATOM   4238  O  O   . ASN B  1 244 ? 1.006   2.825   -1.939  1.00 8.88   ? 244 ASN B O   1 
ATOM   4239  C  CB  . ASN B  1 244 ? 2.095   1.228   -3.918  1.00 10.52  ? 244 ASN B CB  1 
ATOM   4240  C  CG  . ASN B  1 244 ? 2.502   0.183   -4.951  1.00 12.39  ? 244 ASN B CG  1 
ATOM   4241  O  OD1 . ASN B  1 244 ? 2.176   -0.995  -4.858  1.00 13.04  ? 244 ASN B OD1 1 
ATOM   4242  N  ND2 . ASN B  1 244 ? 3.255   0.627   -5.939  1.00 16.95  ? 244 ASN B ND2 1 
ATOM   4243  N  N   . ASN B  1 245 ? -1.134  2.298   -2.413  1.00 7.27   ? 245 ASN B N   1 
ATOM   4244  C  CA  . ASN B  1 245 ? -1.694  3.325   -1.585  1.00 7.03   ? 245 ASN B CA  1 
ATOM   4245  C  C   . ASN B  1 245 ? -1.944  2.850   -0.150  1.00 6.46   ? 245 ASN B C   1 
ATOM   4246  O  O   . ASN B  1 245 ? -3.070  2.909   0.330   1.00 8.90   ? 245 ASN B O   1 
ATOM   4247  C  CB  . ASN B  1 245 ? -2.927  3.941   -2.213  1.00 7.73   ? 245 ASN B CB  1 
ATOM   4248  C  CG  . ASN B  1 245 ? -4.037  2.951   -2.455  1.00 7.07   ? 245 ASN B CG  1 
ATOM   4249  O  OD1 . ASN B  1 245 ? -3.825  1.758   -2.564  1.00 8.92   ? 245 ASN B OD1 1 
ATOM   4250  N  ND2 . ASN B  1 245 ? -5.244  3.437   -2.583  1.00 9.72   ? 245 ASN B ND2 1 
ATOM   4251  N  N   . PHE B  1 246 ? -0.898  2.388   0.472   1.00 7.05   ? 246 PHE B N   1 
ATOM   4252  C  CA  . PHE B  1 246 ? -0.928  1.901   1.833   1.00 7.30   ? 246 PHE B CA  1 
ATOM   4253  C  C   . PHE B  1 246 ? 0.235   2.498   2.568   1.00 7.41   ? 246 PHE B C   1 
ATOM   4254  O  O   . PHE B  1 246 ? 1.332   2.706   1.969   1.00 7.74   ? 246 PHE B O   1 
ATOM   4255  C  CB  . PHE B  1 246 ? -0.876  0.339   1.915   1.00 7.73   ? 246 PHE B CB  1 
ATOM   4256  C  CG  . PHE B  1 246 ? 0.358   -0.269  1.327   1.00 7.83   ? 246 PHE B CG  1 
ATOM   4257  C  CD1 . PHE B  1 246 ? 0.455   -0.507  -0.058  1.00 8.89   ? 246 PHE B CD1 1 
ATOM   4258  C  CD2 . PHE B  1 246 ? 1.472   -0.589  2.138   1.00 9.31   ? 246 PHE B CD2 1 
ATOM   4259  C  CE1 . PHE B  1 246 ? 1.616   -1.072  -0.606  1.00 8.95   ? 246 PHE B CE1 1 
ATOM   4260  C  CE2 . PHE B  1 246 ? 2.640   -1.136  1.522   1.00 10.16  ? 246 PHE B CE2 1 
ATOM   4261  C  CZ  . PHE B  1 246 ? 2.684   -1.361  0.195   1.00 10.81  ? 246 PHE B CZ  1 
ATOM   4262  N  N   . ARG B  1 247 ? 0.093   2.770   3.851   1.00 6.81   ? 247 ARG B N   1 
ATOM   4263  C  CA  . ARG B  1 247 ? 1.145   3.288   4.701   1.00 7.11   ? 247 ARG B CA  1 
ATOM   4264  C  C   . ARG B  1 247 ? 1.920   2.093   5.280   1.00 6.66   ? 247 ARG B C   1 
ATOM   4265  O  O   . ARG B  1 247 ? 1.309   1.082   5.599   1.00 7.48   ? 247 ARG B O   1 
ATOM   4266  C  CB  . ARG B  1 247 ? 0.548   4.163   5.794   1.00 7.71   ? 247 ARG B CB  1 
ATOM   4267  C  CG  . ARG B  1 247 ? 1.542   5.022   6.553   1.00 7.40   ? 247 ARG B CG  1 
ATOM   4268  C  CD  . ARG B  1 247 ? 0.885   5.686   7.718   1.00 7.59   ? 247 ARG B CD  1 
ATOM   4269  N  NE  . ARG B  1 247 ? 1.672   6.801   8.234   1.00 7.88   ? 247 ARG B NE  1 
ATOM   4270  C  CZ  . ARG B  1 247 ? 1.364   7.499   9.322   1.00 6.78   ? 247 ARG B CZ  1 
ATOM   4271  N  NH1 . ARG B  1 247 ? 0.277   7.206   10.026  1.00 9.29   ? 247 ARG B NH1 1 
ATOM   4272  N  NH2 . ARG B  1 247 ? 2.148   8.494   9.708   1.00 8.68   ? 247 ARG B NH2 1 
ATOM   4273  N  N   . GLN B  1 248 ? 3.237   2.242   5.474   1.00 7.08   ? 248 GLN B N   1 
ATOM   4274  C  CA  . GLN B  1 248 ? 3.972   1.252   6.254   1.00 7.21   ? 248 GLN B CA  1 
ATOM   4275  C  C   . GLN B  1 248 ? 3.462   1.184   7.663   1.00 6.98   ? 248 GLN B C   1 
ATOM   4276  O  O   . GLN B  1 248 ? 2.918   2.167   8.231   1.00 7.54   ? 248 GLN B O   1 
ATOM   4277  C  CB  . GLN B  1 248 ? 5.467   1.676   6.287   1.00 7.41   ? 248 GLN B CB  1 
ATOM   4278  C  CG  . GLN B  1 248 ? 6.175   1.667   4.948   1.00 7.81   ? 248 GLN B CG  1 
ATOM   4279  C  CD  . GLN B  1 248 ? 6.199   0.305   4.278   1.00 7.57   ? 248 GLN B CD  1 
ATOM   4280  O  OE1 . GLN B  1 248 ? 5.304   -0.017  3.485   1.00 8.27   ? 248 GLN B OE1 1 
ATOM   4281  N  NE2 . GLN B  1 248 ? 7.210   -0.490  4.584   1.00 9.19   ? 248 GLN B NE2 1 
ATOM   4282  N  N   . VAL B  1 249 ? 3.652   0.031   8.313   1.00 6.95   ? 249 VAL B N   1 
ATOM   4283  C  CA  . VAL B  1 249 ? 3.273   -0.093  9.718   1.00 7.39   ? 249 VAL B CA  1 
ATOM   4284  C  C   . VAL B  1 249 ? 4.129   0.814   10.600  1.00 7.21   ? 249 VAL B C   1 
ATOM   4285  O  O   . VAL B  1 249 ? 5.294   1.109   10.315  1.00 8.24   ? 249 VAL B O   1 
ATOM   4286  C  CB  . VAL B  1 249 ? 3.322   -1.562  10.192  1.00 8.44   ? 249 VAL B CB  1 
ATOM   4287  C  CG1 . VAL B  1 249 ? 2.277   -2.384  9.430   1.00 9.39   ? 249 VAL B CG1 1 
ATOM   4288  C  CG2 . VAL B  1 249 ? 4.716   -2.183  10.057  1.00 10.07  ? 249 VAL B CG2 1 
ATOM   4289  N  N   . GLN B  1 250 ? 3.514   1.246   11.707  1.00 7.65   ? 250 GLN B N   1 
ATOM   4290  C  CA  . GLN B  1 250 ? 4.062   2.201   12.626  1.00 7.89   ? 250 GLN B CA  1 
ATOM   4291  C  C   . GLN B  1 250 ? 4.552   1.514   13.908  1.00 8.13   ? 250 GLN B C   1 
ATOM   4292  O  O   . GLN B  1 250 ? 4.078   0.475   14.264  1.00 10.19  ? 250 GLN B O   1 
ATOM   4293  C  CB  . GLN B  1 250 ? 2.940   3.179   13.010  1.00 8.33   ? 250 GLN B CB  1 
ATOM   4294  C  CG  . GLN B  1 250 ? 2.279   3.827   11.825  1.00 8.59   ? 250 GLN B CG  1 
ATOM   4295  C  CD  . GLN B  1 250 ? 3.186   4.789   11.063  1.00 8.26   ? 250 GLN B CD  1 
ATOM   4296  O  OE1 . GLN B  1 250 ? 3.635   5.796   11.627  1.00 9.35   ? 250 GLN B OE1 1 
ATOM   4297  N  NE2 . GLN B  1 250 ? 3.521   4.442   9.831   1.00 8.77   ? 250 GLN B NE2 1 
ATOM   4298  N  N   . LYS B  1 251 ? 5.491   2.186   14.594  1.00 9.15   ? 251 LYS B N   1 
ATOM   4299  C  CA  . LYS B  1 251 ? 5.867   1.696   15.900  1.00 9.73   ? 251 LYS B CA  1 
ATOM   4300  C  C   . LYS B  1 251 ? 4.657   1.617   16.858  1.00 10.09  ? 251 LYS B C   1 
ATOM   4301  O  O   . LYS B  1 251 ? 3.790   2.485   16.774  1.00 10.58  ? 251 LYS B O   1 
ATOM   4302  C  CB  . LYS B  1 251 ? 6.911   2.602   16.498  1.00 11.31  ? 251 LYS B CB  1 
ATOM   4303  C  CG  . LYS B  1 251 ? 8.276   2.662   15.880  1.00 14.93  ? 251 LYS B CG  1 
ATOM   4304  C  CD  . LYS B  1 251 ? 9.166   1.688   16.421  1.00 17.54  ? 251 LYS B CD  1 
ATOM   4305  C  CE  . LYS B  1 251 ? 10.636  1.781   15.978  1.00 12.61  ? 251 LYS B CE  1 
ATOM   4306  N  NZ  . LYS B  1 251 ? 10.863  1.768   14.528  1.00 9.81   ? 251 LYS B NZ  1 
ATOM   4307  N  N   . PHE B  1 252 ? 4.633   0.641   17.727  1.00 11.01  ? 252 PHE B N   1 
ATOM   4308  C  CA  . PHE B  1 252 ? 3.508   0.509   18.667  1.00 12.21  ? 252 PHE B CA  1 
ATOM   4309  C  C   . PHE B  1 252 ? 4.071   -0.195  19.872  1.00 22.19  ? 252 PHE B C   1 
ATOM   4310  O  O   . PHE B  1 252 ? 4.264   -1.419  19.861  1.00 25.73  ? 252 PHE B O   1 
ATOM   4311  C  CB  . PHE B  1 252 ? 2.455   -0.449  18.056  1.00 16.39  ? 252 PHE B CB  1 
ATOM   4312  C  CG  . PHE B  1 252 ? 1.194   -0.470  18.777  1.00 15.74  ? 252 PHE B CG  1 
ATOM   4313  C  CD1 . PHE B  1 252 ? 0.205   0.491   18.537  1.00 17.42  ? 252 PHE B CD1 1 
ATOM   4314  C  CD2 . PHE B  1 252 ? 0.912   -1.528  19.686  1.00 18.70  ? 252 PHE B CD2 1 
ATOM   4315  C  CE1 . PHE B  1 252 ? -1.031  0.458   19.206  1.00 21.91  ? 252 PHE B CE1 1 
ATOM   4316  C  CE2 . PHE B  1 252 ? -0.351  -1.583  20.263  1.00 21.11  ? 252 PHE B CE2 1 
ATOM   4317  C  CZ  . PHE B  1 252 ? -1.325  -0.590  20.025  1.00 23.20  ? 252 PHE B CZ  1 
ATOM   4318  N  N   . ASP B  1 253 ? 4.534   0.604   20.783  1.00 35.48  ? 253 ASP B N   1 
ATOM   4319  C  CA  . ASP B  1 253 ? 5.188   0.120   22.006  1.00 39.32  ? 253 ASP B CA  1 
ATOM   4320  C  C   . ASP B  1 253 ? 4.532   0.939   23.047  1.00 49.39  ? 253 ASP B C   1 
ATOM   4321  O  O   . ASP B  1 253 ? 4.135   2.094   22.807  1.00 49.82  ? 253 ASP B O   1 
ATOM   4322  C  CB  . ASP B  1 253 ? 6.655   0.479   22.011  1.00 44.85  ? 253 ASP B CB  1 
ATOM   4323  C  CG  . ASP B  1 253 ? 6.881   1.987   21.908  1.00 88.17  ? 253 ASP B CG  1 
ATOM   4324  O  OD1 . ASP B  1 253 ? 7.599   2.530   22.782  1.00 87.67  ? 253 ASP B OD1 1 
ATOM   4325  O  OD2 . ASP B  1 253 ? 6.323   2.626   20.967  1.00 117.41 ? 253 ASP B OD2 1 
ATOM   4326  N  N   . GLU B  1 254 ? 4.449   0.365   24.230  1.00 55.01  ? 254 GLU B N   1 
ATOM   4327  C  CA  . GLU B  1 254 ? 3.479   0.879   25.137  1.00 64.79  ? 254 GLU B CA  1 
ATOM   4328  C  C   . GLU B  1 254 ? 2.041   0.655   24.611  1.00 62.64  ? 254 GLU B C   1 
ATOM   4329  O  O   . GLU B  1 254 ? 1.243   0.382   25.442  1.00 68.46  ? 254 GLU B O   1 
ATOM   4330  N  N   . ARG B  1 255 ? 1.692   0.722   23.302  1.00 47.43  ? 255 ARG B N   1 
ATOM   4331  C  CA  . ARG B  1 255 ? 0.286   0.426   22.979  1.00 24.62  ? 255 ARG B CA  1 
ATOM   4332  C  C   . ARG B  1 255 ? 0.071   -1.194  23.057  1.00 30.44  ? 255 ARG B C   1 
ATOM   4333  O  O   . ARG B  1 255 ? 0.996   -1.917  22.674  1.00 26.30  ? 255 ARG B O   1 
ATOM   4334  C  CB  . ARG B  1 255 ? -0.333  1.059   21.663  1.00 27.63  ? 255 ARG B CB  1 
ATOM   4335  C  CG  . ARG B  1 255 ? -0.616  2.656   21.493  1.00 23.32  ? 255 ARG B CG  1 
ATOM   4336  C  CD  . ARG B  1 255 ? -1.101  3.019   20.098  1.00 24.38  ? 255 ARG B CD  1 
ATOM   4337  N  NE  . ARG B  1 255 ? -0.008  3.177   19.147  1.00 46.16  ? 255 ARG B NE  1 
ATOM   4338  C  CZ  . ARG B  1 255 ? -0.179  3.297   17.829  1.00 27.97  ? 255 ARG B CZ  1 
ATOM   4339  N  NH1 . ARG B  1 255 ? -1.399  3.277   17.313  1.00 17.71  ? 255 ARG B NH1 1 
ATOM   4340  N  NH2 . ARG B  1 255 ? 0.872   3.434   17.030  1.00 16.95  ? 255 ARG B NH2 1 
ATOM   4341  N  N   . LEU B  1 256 ? -1.102  -1.718  23.393  1.00 29.04  ? 256 LEU B N   1 
ATOM   4342  C  CA  . LEU B  1 256 ? -1.555  -3.068  23.289  1.00 22.01  ? 256 LEU B CA  1 
ATOM   4343  C  C   . LEU B  1 256 ? -2.819  -3.083  22.421  1.00 19.66  ? 256 LEU B C   1 
ATOM   4344  O  O   . LEU B  1 256 ? -3.677  -2.143  22.351  1.00 21.59  ? 256 LEU B O   1 
ATOM   4345  C  CB  . LEU B  1 256 ? -1.883  -3.647  24.667  1.00 30.59  ? 256 LEU B CB  1 
ATOM   4346  C  CG  . LEU B  1 256 ? -0.743  -3.904  25.647  1.00 27.75  ? 256 LEU B CG  1 
ATOM   4347  C  CD1 . LEU B  1 256 ? -1.191  -4.862  26.739  1.00 36.35  ? 256 LEU B CD1 1 
ATOM   4348  C  CD2 . LEU B  1 256 ? 0.480   -4.443  24.930  1.00 29.85  ? 256 LEU B CD2 1 
ATOM   4349  N  N   . VAL B  1 257 ? -2.939  -4.155  21.749  1.00 14.56  ? 257 VAL B N   1 
ATOM   4350  C  CA  . VAL B  1 257 ? -4.073  -4.447  20.899  1.00 11.17  ? 257 VAL B CA  1 
ATOM   4351  C  C   . VAL B  1 257 ? -4.899  -5.517  21.608  1.00 10.00  ? 257 VAL B C   1 
ATOM   4352  O  O   . VAL B  1 257 ? -4.368  -6.549  22.005  1.00 12.51  ? 257 VAL B O   1 
ATOM   4353  C  CB  . VAL B  1 257 ? -3.550  -4.994  19.551  1.00 11.46  ? 257 VAL B CB  1 
ATOM   4354  C  CG1 . VAL B  1 257 ? -4.726  -5.453  18.697  1.00 12.51  ? 257 VAL B CG1 1 
ATOM   4355  C  CG2 . VAL B  1 257 ? -2.739  -3.940  18.809  1.00 13.30  ? 257 VAL B CG2 1 
ATOM   4356  N  N   . TYR B  1 258 ? -6.168  -5.270  21.722  1.00 10.02  ? 258 TYR B N   1 
ATOM   4357  C  CA  . TYR B  1 258 ? -7.056  -6.154  22.463  1.00 10.81  ? 258 TYR B CA  1 
ATOM   4358  C  C   . TYR B  1 258 ? -7.824  -7.032  21.510  1.00 9.85   ? 258 TYR B C   1 
ATOM   4359  O  O   . TYR B  1 258 ? -8.221  -6.588  20.431  1.00 11.47  ? 258 TYR B O   1 
ATOM   4360  C  CB  . TYR B  1 258 ? -7.999  -5.307  23.305  1.00 13.41  ? 258 TYR B CB  1 
ATOM   4361  C  CG  . TYR B  1 258 ? -7.246  -4.428  24.275  1.00 15.35  ? 258 TYR B CG  1 
ATOM   4362  C  CD1 . TYR B  1 258 ? -6.700  -4.992  25.422  1.00 18.46  ? 258 TYR B CD1 1 
ATOM   4363  C  CD2 . TYR B  1 258 ? -6.926  -3.078  23.949  1.00 17.31  ? 258 TYR B CD2 1 
ATOM   4364  C  CE1 . TYR B  1 258 ? -5.924  -4.211  26.309  1.00 21.63  ? 258 TYR B CE1 1 
ATOM   4365  C  CE2 . TYR B  1 258 ? -6.154  -2.292  24.767  1.00 20.68  ? 258 TYR B CE2 1 
ATOM   4366  C  CZ  . TYR B  1 258 ? -5.648  -2.865  25.923  1.00 21.77  ? 258 TYR B CZ  1 
ATOM   4367  O  OH  . TYR B  1 258 ? -4.892  -2.081  26.750  1.00 29.06  ? 258 TYR B OH  1 
ATOM   4368  N  N   . THR B  1 259 ? -7.953  -8.297  21.823  1.00 9.49   ? 259 THR B N   1 
ATOM   4369  C  CA  . THR B  1 259 ? -8.576  -9.246  20.941  1.00 9.40   ? 259 THR B CA  1 
ATOM   4370  C  C   . THR B  1 259 ? -9.830  -9.789  21.569  1.00 9.10   ? 259 THR B C   1 
ATOM   4371  O  O   . THR B  1 259 ? -9.918  -10.021 22.759  1.00 10.71  ? 259 THR B O   1 
ATOM   4372  C  CB  . THR B  1 259 ? -7.679  -10.414 20.521  1.00 10.28  ? 259 THR B CB  1 
ATOM   4373  O  OG1 . THR B  1 259 ? -7.244  -11.114 21.697  1.00 12.16  ? 259 THR B OG1 1 
ATOM   4374  C  CG2 . THR B  1 259 ? -6.445  -9.872  19.774  1.00 12.14  ? 259 THR B CG2 1 
ATOM   4375  N  N   . SER B  1 260 ? -10.824 -10.008 20.730  1.00 9.05   ? 260 SER B N   1 
ATOM   4376  C  CA  . SER B  1 260 ? -12.122 -10.566 21.214  1.00 10.38  ? 260 SER B CA  1 
ATOM   4377  C  C   . SER B  1 260 ? -12.078 -12.053 21.174  1.00 10.30  ? 260 SER B C   1 
ATOM   4378  O  O   . SER B  1 260 ? -13.078 -12.703 21.546  1.00 14.39  ? 260 SER B O   1 
ATOM   4379  C  CB  . SER B  1 260 ? -13.260 -10.118 20.353  1.00 10.21  ? 260 SER B CB  1 
ATOM   4380  O  OG  . SER B  1 260 ? -13.094 -10.646 19.054  1.00 10.06  ? 260 SER B OG  1 
ATOM   4381  N  N   . PHE B  1 261 ? -10.949 -12.667 20.810  1.00 10.06  ? 261 PHE B N   1 
ATOM   4382  C  CA  . PHE B  1 261 ? -10.707 -14.082 20.695  1.00 10.99  ? 261 PHE B CA  1 
ATOM   4383  C  C   . PHE B  1 261 ? -9.510  -14.403 21.542  1.00 11.65  ? 261 PHE B C   1 
ATOM   4384  O  O   . PHE B  1 261 ? -8.548  -13.626 21.619  1.00 12.11  ? 261 PHE B O   1 
ATOM   4385  C  CB  . PHE B  1 261 ? -10.589 -14.554 19.258  1.00 11.76  ? 261 PHE B CB  1 
ATOM   4386  C  CG  . PHE B  1 261 ? -9.535  -13.790 18.494  1.00 11.26  ? 261 PHE B CG  1 
ATOM   4387  C  CD1 . PHE B  1 261 ? -9.833  -12.571 17.904  1.00 10.92  ? 261 PHE B CD1 1 
ATOM   4388  C  CD2 . PHE B  1 261 ? -8.250  -14.274 18.387  1.00 13.54  ? 261 PHE B CD2 1 
ATOM   4389  C  CE1 . PHE B  1 261 ? -8.884  -11.893 17.189  1.00 12.03  ? 261 PHE B CE1 1 
ATOM   4390  C  CE2 . PHE B  1 261 ? -7.286  -13.552 17.686  1.00 13.72  ? 261 PHE B CE2 1 
ATOM   4391  C  CZ  . PHE B  1 261 ? -7.610  -12.390 17.062  1.00 13.19  ? 261 PHE B CZ  1 
ATOM   4392  N  N   . SER B  1 262 ? -9.473  -15.541 22.247  1.00 14.89  ? 262 SER B N   1 
ATOM   4393  C  CA  . SER B  1 262 ? -8.306  -15.830 23.130  1.00 16.97  ? 262 SER B CA  1 
ATOM   4394  C  C   . SER B  1 262 ? -7.042  -16.203 22.366  1.00 27.83  ? 262 SER B C   1 
ATOM   4395  O  O   . SER B  1 262 ? -5.854  -15.897 22.838  1.00 34.19  ? 262 SER B O   1 
ATOM   4396  C  CB  . SER B  1 262 ? -8.689  -16.890 24.178  1.00 34.80  ? 262 SER B CB  1 
ATOM   4397  O  OG  . SER B  1 262 ? -9.985  -17.444 23.943  1.00 42.65  ? 262 SER B OG  1 
ATOM   4398  N  N   . GLN B  1 263 ? -7.319  -16.692 21.185  1.00 32.35  ? 263 GLN B N   1 
ATOM   4399  C  CA  . GLN B  1 263 ? -6.757  -17.987 20.638  1.00 38.19  ? 263 GLN B CA  1 
ATOM   4400  C  C   . GLN B  1 263 ? -7.488  -18.355 19.326  1.00 52.91  ? 263 GLN B C   1 
ATOM   4401  O  O   . GLN B  1 263 ? -6.897  -18.969 18.378  1.00 53.15  ? 263 GLN B O   1 
ATOM   4402  C  CB  . GLN B  1 263 ? -6.666  -19.260 21.589  1.00 50.40  ? 263 GLN B CB  1 
ATOM   4403  C  CG  . GLN B  1 263 ? -7.718  -19.425 22.692  1.00 76.48  ? 263 GLN B CG  1 
ATOM   4404  C  CD  . GLN B  1 263 ? -8.071  -20.938 22.994  1.00 97.66  ? 263 GLN B CD  1 
ATOM   4405  O  OE1 . GLN B  1 263 ? -7.166  -21.825 23.104  1.00 47.82  ? 263 GLN B OE1 1 
ATOM   4406  N  NE2 . GLN B  1 263 ? -9.428  -21.215 23.159  1.00 152.79 ? 263 GLN B NE2 1 
ATOM   4407  O  OXT . GLN B  1 263 ? -8.685  -17.978 19.199  1.00 23.09  ? 263 GLN B OXT 1 
ATOM   4408  N  N   . SER C  1 2   ? 35.194  20.574  -26.775 1.00 65.50  ? 2   SER C N   1 
ATOM   4409  C  CA  . SER C  1 2   ? 35.377  19.172  -27.245 1.00 68.90  ? 2   SER C CA  1 
ATOM   4410  C  C   . SER C  1 2   ? 34.128  18.330  -27.001 1.00 57.86  ? 2   SER C C   1 
ATOM   4411  O  O   . SER C  1 2   ? 33.533  17.857  -27.993 1.00 40.38  ? 2   SER C O   1 
ATOM   4412  C  CB  . SER C  1 2   ? 36.626  18.534  -26.606 1.00 96.46  ? 2   SER C CB  1 
ATOM   4413  O  OG  . SER C  1 2   ? 36.391  18.048  -25.281 1.00 88.91  ? 2   SER C OG  1 
ATOM   4414  N  N   . LYS C  1 3   ? 33.767  18.243  -25.725 1.00 60.81  ? 3   LYS C N   1 
ATOM   4415  C  CA  . LYS C  1 3   ? 32.430  18.011  -25.215 1.00 56.35  ? 3   LYS C CA  1 
ATOM   4416  C  C   . LYS C  1 3   ? 31.545  17.088  -26.022 1.00 45.62  ? 3   LYS C C   1 
ATOM   4417  O  O   . LYS C  1 3   ? 30.379  17.397  -26.268 1.00 53.06  ? 3   LYS C O   1 
ATOM   4418  C  CB  . LYS C  1 3   ? 31.711  19.349  -25.005 1.00 53.93  ? 3   LYS C CB  1 
ATOM   4419  N  N   . TRP C  1 4   ? 32.080  15.941  -26.410 1.00 23.60  ? 4   TRP C N   1 
ATOM   4420  C  CA  . TRP C  1 4   ? 31.189  14.857  -26.885 1.00 19.71  ? 4   TRP C CA  1 
ATOM   4421  C  C   . TRP C  1 4   ? 31.107  13.718  -25.892 1.00 18.23  ? 4   TRP C C   1 
ATOM   4422  O  O   . TRP C  1 4   ? 32.023  13.475  -25.119 1.00 21.90  ? 4   TRP C O   1 
ATOM   4423  C  CB  . TRP C  1 4   ? 31.629  14.401  -28.251 1.00 16.90  ? 4   TRP C CB  1 
ATOM   4424  C  CG  . TRP C  1 4   ? 32.959  13.742  -28.294 1.00 15.87  ? 4   TRP C CG  1 
ATOM   4425  C  CD1 . TRP C  1 4   ? 34.207  14.304  -28.502 1.00 17.33  ? 4   TRP C CD1 1 
ATOM   4426  C  CD2 . TRP C  1 4   ? 33.203  12.314  -28.116 1.00 15.33  ? 4   TRP C CD2 1 
ATOM   4427  N  NE1 . TRP C  1 4   ? 35.194  13.346  -28.498 1.00 18.01  ? 4   TRP C NE1 1 
ATOM   4428  C  CE2 . TRP C  1 4   ? 34.640  12.111  -28.287 1.00 17.76  ? 4   TRP C CE2 1 
ATOM   4429  C  CE3 . TRP C  1 4   ? 32.367  11.189  -27.925 1.00 14.64  ? 4   TRP C CE3 1 
ATOM   4430  C  CZ2 . TRP C  1 4   ? 35.227  10.847  -28.234 1.00 18.06  ? 4   TRP C CZ2 1 
ATOM   4431  C  CZ3 . TRP C  1 4   ? 32.934  9.913   -27.907 1.00 15.61  ? 4   TRP C CZ3 1 
ATOM   4432  C  CH2 . TRP C  1 4   ? 34.335  9.725   -28.052 1.00 17.33  ? 4   TRP C CH2 1 
ATOM   4433  N  N   . THR C  1 5   ? 29.976  13.019  -25.953 1.00 17.60  ? 5   THR C N   1 
ATOM   4434  C  CA  . THR C  1 5   ? 29.719  11.903  -25.051 1.00 16.99  ? 5   THR C CA  1 
ATOM   4435  C  C   . THR C  1 5   ? 29.036  10.765  -25.856 1.00 15.51  ? 5   THR C C   1 
ATOM   4436  O  O   . THR C  1 5   ? 28.775  10.860  -27.037 1.00 16.68  ? 5   THR C O   1 
ATOM   4437  C  CB  . THR C  1 5   ? 28.800  12.247  -23.874 1.00 25.35  ? 5   THR C CB  1 
ATOM   4438  O  OG1 . THR C  1 5   ? 27.506  12.545  -24.448 1.00 22.72  ? 5   THR C OG1 1 
ATOM   4439  C  CG2 . THR C  1 5   ? 29.338  13.477  -23.174 1.00 24.47  ? 5   THR C CG2 1 
ATOM   4440  N  N   . TYR C  1 6   ? 28.705  9.703   -25.129 1.00 19.28  ? 6   TYR C N   1 
ATOM   4441  C  CA  . TYR C  1 6   ? 27.834  8.605   -25.652 1.00 20.75  ? 6   TYR C CA  1 
ATOM   4442  C  C   . TYR C  1 6   ? 26.451  8.640   -25.088 1.00 21.34  ? 6   TYR C C   1 
ATOM   4443  O  O   . TYR C  1 6   ? 25.667  7.671   -25.277 1.00 23.06  ? 6   TYR C O   1 
ATOM   4444  C  CB  . TYR C  1 6   ? 28.354  7.226   -25.390 1.00 20.47  ? 6   TYR C CB  1 
ATOM   4445  C  CG  . TYR C  1 6   ? 29.645  6.972   -26.208 1.00 18.71  ? 6   TYR C CG  1 
ATOM   4446  C  CD1 . TYR C  1 6   ? 30.921  7.105   -25.633 1.00 17.32  ? 6   TYR C CD1 1 
ATOM   4447  C  CD2 . TYR C  1 6   ? 29.625  6.523   -27.535 1.00 15.49  ? 6   TYR C CD2 1 
ATOM   4448  C  CE1 . TYR C  1 6   ? 32.097  6.783   -26.255 1.00 17.79  ? 6   TYR C CE1 1 
ATOM   4449  C  CE2 . TYR C  1 6   ? 30.814  6.184   -28.186 1.00 14.87  ? 6   TYR C CE2 1 
ATOM   4450  C  CZ  . TYR C  1 6   ? 32.013  6.322   -27.580 1.00 16.02  ? 6   TYR C CZ  1 
ATOM   4451  O  OH  . TYR C  1 6   ? 33.141  6.006   -28.232 1.00 17.92  ? 6   TYR C OH  1 
ATOM   4452  N  N   . PHE C  1 7   ? 26.120  9.716   -24.429 1.00 31.96  ? 7   PHE C N   1 
ATOM   4453  C  CA  . PHE C  1 7   ? 24.830  9.783   -23.749 1.00 41.49  ? 7   PHE C CA  1 
ATOM   4454  C  C   . PHE C  1 7   ? 24.162  11.156  -23.871 1.00 55.97  ? 7   PHE C C   1 
ATOM   4455  O  O   . PHE C  1 7   ? 24.747  12.100  -24.435 1.00 47.55  ? 7   PHE C O   1 
ATOM   4456  C  CB  . PHE C  1 7   ? 25.010  9.516   -22.231 1.00 67.47  ? 7   PHE C CB  1 
ATOM   4457  N  N   . GLY C  1 8   ? 22.968  11.281  -23.293 1.00 49.39  ? 8   GLY C N   1 
ATOM   4458  C  CA  . GLY C  1 8   ? 22.380  12.611  -23.001 1.00 41.65  ? 8   GLY C CA  1 
ATOM   4459  C  C   . GLY C  1 8   ? 22.495  13.477  -24.254 1.00 46.46  ? 8   GLY C C   1 
ATOM   4460  O  O   . GLY C  1 8   ? 22.479  12.935  -25.411 1.00 76.84  ? 8   GLY C O   1 
ATOM   4461  N  N   . PRO C  1 9   ? 22.640  14.797  -24.048 1.00 45.34  ? 9   PRO C N   1 
ATOM   4462  C  CA  . PRO C  1 9   ? 22.525  15.777  -25.129 1.00 36.19  ? 9   PRO C CA  1 
ATOM   4463  C  C   . PRO C  1 9   ? 23.745  15.894  -26.074 1.00 30.16  ? 9   PRO C C   1 
ATOM   4464  O  O   . PRO C  1 9   ? 23.598  16.436  -27.179 1.00 31.50  ? 9   PRO C O   1 
ATOM   4465  C  CB  . PRO C  1 9   ? 22.294  17.118  -24.369 1.00 55.99  ? 9   PRO C CB  1 
ATOM   4466  C  CG  . PRO C  1 9   ? 21.866  16.723  -23.010 1.00 56.35  ? 9   PRO C CG  1 
ATOM   4467  C  CD  . PRO C  1 9   ? 22.605  15.476  -22.718 1.00 40.26  ? 9   PRO C CD  1 
ATOM   4468  N  N   . ASP C  1 10  ? 24.922  15.427  -25.640 1.00 26.54  ? 10  ASP C N   1 
ATOM   4469  C  CA  . ASP C  1 10  ? 26.173  15.514  -26.421 1.00 25.82  ? 10  ASP C CA  1 
ATOM   4470  C  C   . ASP C  1 10  ? 26.581  14.186  -26.988 1.00 21.95  ? 10  ASP C C   1 
ATOM   4471  O  O   . ASP C  1 10  ? 27.765  14.007  -27.399 1.00 23.11  ? 10  ASP C O   1 
ATOM   4472  C  CB  . ASP C  1 10  ? 27.305  16.060  -25.535 1.00 32.30  ? 10  ASP C CB  1 
ATOM   4473  C  CG  . ASP C  1 10  ? 27.108  17.532  -25.149 1.00 54.48  ? 10  ASP C CG  1 
ATOM   4474  O  OD1 . ASP C  1 10  ? 26.569  18.316  -25.966 1.00 36.16  ? 10  ASP C OD1 1 
ATOM   4475  O  OD2 . ASP C  1 10  ? 27.527  17.909  -24.037 1.00 139.45 ? 10  ASP C OD2 1 
ATOM   4476  N  N   . GLY C  1 11  ? 25.613  13.279  -27.051 1.00 20.37  ? 11  GLY C N   1 
ATOM   4477  C  CA  . GLY C  1 11  ? 25.740  11.947  -27.590 1.00 17.40  ? 11  GLY C CA  1 
ATOM   4478  C  C   . GLY C  1 11  ? 25.737  11.903  -29.093 1.00 13.99  ? 11  GLY C C   1 
ATOM   4479  O  O   . GLY C  1 11  ? 25.786  12.887  -29.813 1.00 14.07  ? 11  GLY C O   1 
ATOM   4480  N  N   . GLU C  1 12  ? 25.753  10.647  -29.609 1.00 13.20  ? 12  GLU C N   1 
ATOM   4481  C  CA  . GLU C  1 12  ? 26.215  10.439  -30.979 1.00 10.96  ? 12  GLU C CA  1 
ATOM   4482  C  C   . GLU C  1 12  ? 25.329  11.052  -32.025 1.00 10.91  ? 12  GLU C C   1 
ATOM   4483  O  O   . GLU C  1 12  ? 25.865  11.400  -33.093 1.00 10.92  ? 12  GLU C O   1 
ATOM   4484  C  CB  . GLU C  1 12  ? 26.405  8.930   -31.221 1.00 11.24  ? 12  GLU C CB  1 
ATOM   4485  C  CG  . GLU C  1 12  ? 25.055  8.171   -31.330 1.00 10.74  ? 12  GLU C CG  1 
ATOM   4486  C  CD  . GLU C  1 12  ? 25.311  6.692   -31.130 1.00 10.50  ? 12  GLU C CD  1 
ATOM   4487  O  OE1 . GLU C  1 12  ? 25.591  5.973   -32.106 1.00 10.24  ? 12  GLU C OE1 1 
ATOM   4488  O  OE2 . GLU C  1 12  ? 25.344  6.209   -29.927 1.00 13.00  ? 12  GLU C OE2 1 
ATOM   4489  N  N   . ASN C  1 13  ? 24.022  11.246  -31.781 1.00 10.34  ? 13  ASN C N   1 
ATOM   4490  C  CA  . ASN C  1 13  ? 23.189  11.911  -32.793 1.00 9.41   ? 13  ASN C CA  1 
ATOM   4491  C  C   . ASN C  1 13  ? 23.543  13.377  -32.963 1.00 10.26  ? 13  ASN C C   1 
ATOM   4492  O  O   . ASN C  1 13  ? 23.164  13.945  -33.968 1.00 10.92  ? 13  ASN C O   1 
ATOM   4493  C  CB  . ASN C  1 13  ? 21.737  11.745  -32.541 1.00 10.05  ? 13  ASN C CB  1 
ATOM   4494  C  CG  . ASN C  1 13  ? 21.240  10.314  -32.597 1.00 9.06   ? 13  ASN C CG  1 
ATOM   4495  O  OD1 . ASN C  1 13  ? 21.919  9.448   -33.140 1.00 10.59  ? 13  ASN C OD1 1 
ATOM   4496  N  ND2 . ASN C  1 13  ? 20.031  10.095  -32.139 1.00 9.82   ? 13  ASN C ND2 1 
ATOM   4497  N  N   A SER C  1 14  ? 24.217  13.892  -31.942 0.50 11.05  ? 14  SER C N   1 
ATOM   4498  N  N   B SER C  1 14  ? 24.230  13.979  -32.006 0.50 10.56  ? 14  SER C N   1 
ATOM   4499  C  CA  A SER C  1 14  ? 24.597  15.302  -31.929 0.50 11.41  ? 14  SER C CA  1 
ATOM   4500  C  CA  B SER C  1 14  ? 24.602  15.406  -32.182 0.50 11.64  ? 14  SER C CA  1 
ATOM   4501  C  C   A SER C  1 14  ? 25.992  15.591  -32.480 0.50 10.95  ? 14  SER C C   1 
ATOM   4502  C  C   B SER C  1 14  ? 26.092  15.620  -32.435 0.50 10.63  ? 14  SER C C   1 
ATOM   4503  O  O   A SER C  1 14  ? 26.269  16.765  -32.829 0.50 10.30  ? 14  SER C O   1 
ATOM   4504  O  O   B SER C  1 14  ? 26.585  16.746  -32.477 0.50 11.21  ? 14  SER C O   1 
ATOM   4505  C  CB  A SER C  1 14  ? 24.404  15.888  -30.524 0.50 12.30  ? 14  SER C CB  1 
ATOM   4506  C  CB  B SER C  1 14  ? 24.269  16.150  -30.917 0.50 14.03  ? 14  SER C CB  1 
ATOM   4507  O  OG  A SER C  1 14  ? 23.007  16.069  -30.371 0.50 14.02  ? 14  SER C OG  1 
ATOM   4508  O  OG  B SER C  1 14  ? 25.132  15.658  -29.918 0.50 19.61  ? 14  SER C OG  1 
ATOM   4509  N  N   . TRP C  1 15  ? 26.849  14.550  -32.593 1.00 10.74  ? 15  TRP C N   1 
ATOM   4510  C  CA  . TRP C  1 15  ? 28.230  14.740  -32.990 1.00 10.68  ? 15  TRP C CA  1 
ATOM   4511  C  C   . TRP C  1 15  ? 28.430  15.564  -34.220 1.00 10.56  ? 15  TRP C C   1 
ATOM   4512  O  O   . TRP C  1 15  ? 29.364  16.353  -34.309 1.00 11.12  ? 15  TRP C O   1 
ATOM   4513  C  CB  . TRP C  1 15  ? 28.959  13.432  -33.163 1.00 11.48  ? 15  TRP C CB  1 
ATOM   4514  C  CG  . TRP C  1 15  ? 29.106  12.590  -31.941 1.00 10.90  ? 15  TRP C CG  1 
ATOM   4515  C  CD1 . TRP C  1 15  ? 28.878  12.928  -30.609 1.00 11.37  ? 15  TRP C CD1 1 
ATOM   4516  C  CD2 . TRP C  1 15  ? 29.551  11.211  -31.925 1.00 10.42  ? 15  TRP C CD2 1 
ATOM   4517  N  NE1 . TRP C  1 15  ? 29.145  11.857  -29.791 1.00 11.35  ? 15  TRP C NE1 1 
ATOM   4518  C  CE2 . TRP C  1 15  ? 29.556  10.792  -30.526 1.00 10.55  ? 15  TRP C CE2 1 
ATOM   4519  C  CE3 . TRP C  1 15  ? 29.931  10.310  -32.902 1.00 11.26  ? 15  TRP C CE3 1 
ATOM   4520  C  CZ2 . TRP C  1 15  ? 29.932  9.514   -30.151 1.00 11.58  ? 15  TRP C CZ2 1 
ATOM   4521  C  CZ3 . TRP C  1 15  ? 30.307  9.029   -32.517 1.00 10.39  ? 15  TRP C CZ3 1 
ATOM   4522  C  CH2 . TRP C  1 15  ? 30.308  8.640   -31.175 1.00 11.50  ? 15  TRP C CH2 1 
ATOM   4523  N  N   . SER C  1 16  ? 27.556  15.390  -35.211 1.00 10.07  ? 16  SER C N   1 
ATOM   4524  C  CA  . SER C  1 16  ? 27.738  16.041  -36.492 1.00 9.97   ? 16  SER C CA  1 
ATOM   4525  C  C   . SER C  1 16  ? 27.667  17.567  -36.414 1.00 10.32  ? 16  SER C C   1 
ATOM   4526  O  O   . SER C  1 16  ? 28.106  18.219  -37.314 1.00 11.48  ? 16  SER C O   1 
ATOM   4527  C  CB  . SER C  1 16  ? 26.700  15.537  -37.469 1.00 10.97  ? 16  SER C CB  1 
ATOM   4528  O  OG  . SER C  1 16  ? 25.391  15.930  -37.025 1.00 12.06  ? 16  SER C OG  1 
ATOM   4529  N  N   A LYS C  1 17  ? 27.151  18.113  -35.294 0.50 11.83  ? 17  LYS C N   1 
ATOM   4530  N  N   B LYS C  1 17  ? 27.087  18.147  -35.352 0.50 10.63  ? 17  LYS C N   1 
ATOM   4531  C  CA  A LYS C  1 17  ? 27.097  19.577  -35.197 0.50 12.30  ? 17  LYS C CA  1 
ATOM   4532  C  CA  B LYS C  1 17  ? 27.044  19.616  -35.267 0.50 11.28  ? 17  LYS C CA  1 
ATOM   4533  C  C   A LYS C  1 17  ? 28.506  20.150  -35.216 0.50 11.13  ? 17  LYS C C   1 
ATOM   4534  C  C   B LYS C  1 17  ? 28.460  20.201  -35.172 0.50 11.61  ? 17  LYS C C   1 
ATOM   4535  O  O   A LYS C  1 17  ? 28.833  21.039  -35.986 0.50 13.50  ? 17  LYS C O   1 
ATOM   4536  O  O   B LYS C  1 17  ? 28.794  21.131  -35.882 0.50 14.79  ? 17  LYS C O   1 
ATOM   4537  C  CB  A LYS C  1 17  ? 26.393  19.998  -33.903 0.50 14.29  ? 17  LYS C CB  1 
ATOM   4538  C  CB  B LYS C  1 17  ? 26.147  20.004  -34.071 0.50 12.53  ? 17  LYS C CB  1 
ATOM   4539  C  CG  A LYS C  1 17  ? 25.004  19.443  -33.714 0.50 19.65  ? 17  LYS C CG  1 
ATOM   4540  C  CG  B LYS C  1 17  ? 24.657  19.769  -34.265 0.50 17.49  ? 17  LYS C CG  1 
ATOM   4541  C  CD  A LYS C  1 17  ? 24.485  19.632  -32.292 0.50 18.52  ? 17  LYS C CD  1 
ATOM   4542  C  CD  B LYS C  1 17  ? 23.846  20.087  -33.017 0.50 16.62  ? 17  LYS C CD  1 
ATOM   4543  C  CE  A LYS C  1 17  ? 23.049  19.194  -32.147 0.50 18.55  ? 17  LYS C CE  1 
ATOM   4544  C  CE  B LYS C  1 17  ? 23.923  21.587  -32.763 0.50 15.28  ? 17  LYS C CE  1 
ATOM   4545  N  NZ  A LYS C  1 17  ? 22.414  19.371  -30.837 0.50 15.71  ? 17  LYS C NZ  1 
ATOM   4546  N  NZ  B LYS C  1 17  ? 23.172  21.820  -31.514 0.50 16.24  ? 17  LYS C NZ  1 
ATOM   4547  N  N   A LYS C  1 18  ? 29.334  19.647  -34.330 0.50 11.39  ? 18  LYS C N   1 
ATOM   4548  N  N   B LYS C  1 18  ? 29.302  19.643  -34.326 0.50 11.51  ? 18  LYS C N   1 
ATOM   4549  C  CA  A LYS C  1 18  ? 30.708  20.128  -34.206 0.50 12.43  ? 18  LYS C CA  1 
ATOM   4550  C  CA  B LYS C  1 18  ? 30.688  20.117  -34.204 0.50 12.48  ? 18  LYS C CA  1 
ATOM   4551  C  C   A LYS C  1 18  ? 31.683  19.353  -35.058 0.50 13.02  ? 18  LYS C C   1 
ATOM   4552  C  C   B LYS C  1 18  ? 31.689  19.336  -35.030 0.50 13.13  ? 18  LYS C C   1 
ATOM   4553  O  O   A LYS C  1 18  ? 32.785  19.833  -35.285 0.50 16.96  ? 18  LYS C O   1 
ATOM   4554  O  O   B LYS C  1 18  ? 32.788  19.813  -35.262 0.50 17.06  ? 18  LYS C O   1 
ATOM   4555  C  CB  A LYS C  1 18  ? 31.217  19.988  -32.772 0.50 15.48  ? 18  LYS C CB  1 
ATOM   4556  C  CB  B LYS C  1 18  ? 31.127  20.100  -32.746 0.50 15.19  ? 18  LYS C CB  1 
ATOM   4557  C  CG  A LYS C  1 18  ? 30.668  20.945  -31.754 0.50 20.82  ? 18  LYS C CG  1 
ATOM   4558  C  CG  B LYS C  1 18  ? 32.615  20.341  -32.498 0.50 20.92  ? 18  LYS C CG  1 
ATOM   4559  C  CD  A LYS C  1 18  ? 30.475  22.283  -32.367 0.50 28.08  ? 18  LYS C CD  1 
ATOM   4560  C  CD  B LYS C  1 18  ? 32.833  20.592  -31.007 0.50 26.31  ? 18  LYS C CD  1 
ATOM   4561  C  CE  A LYS C  1 18  ? 31.474  23.327  -31.908 0.50 31.37  ? 18  LYS C CE  1 
ATOM   4562  C  CE  B LYS C  1 18  ? 34.297  20.463  -30.607 0.50 27.59  ? 18  LYS C CE  1 
ATOM   4563  N  NZ  A LYS C  1 18  ? 30.995  24.118  -30.751 0.50 35.46  ? 18  LYS C NZ  1 
ATOM   4564  N  NZ  B LYS C  1 18  ? 34.578  21.431  -29.512 0.50 37.54  ? 18  LYS C NZ  1 
ATOM   4565  N  N   . TYR C  1 19  ? 31.305  18.140  -35.450 1.00 11.26  ? 19  TYR C N   1 
ATOM   4566  C  CA  . TYR C  1 19  ? 32.213  17.244  -36.192 1.00 10.99  ? 19  TYR C CA  1 
ATOM   4567  C  C   . TYR C  1 19  ? 31.497  16.787  -37.444 1.00 9.87   ? 19  TYR C C   1 
ATOM   4568  O  O   . TYR C  1 19  ? 30.851  15.694  -37.453 1.00 11.06  ? 19  TYR C O   1 
ATOM   4569  C  CB  . TYR C  1 19  ? 32.525  16.045  -35.298 1.00 11.57  ? 19  TYR C CB  1 
ATOM   4570  C  CG  . TYR C  1 19  ? 33.215  16.451  -34.007 1.00 12.56  ? 19  TYR C CG  1 
ATOM   4571  C  CD1 . TYR C  1 19  ? 34.572  16.765  -33.998 1.00 13.56  ? 19  TYR C CD1 1 
ATOM   4572  C  CD2 . TYR C  1 19  ? 32.484  16.463  -32.791 1.00 12.56  ? 19  TYR C CD2 1 
ATOM   4573  C  CE1 . TYR C  1 19  ? 35.218  17.047  -32.755 1.00 15.84  ? 19  TYR C CE1 1 
ATOM   4574  C  CE2 . TYR C  1 19  ? 33.099  16.794  -31.600 1.00 15.29  ? 19  TYR C CE2 1 
ATOM   4575  C  CZ  . TYR C  1 19  ? 34.420  17.104  -31.583 1.00 16.48  ? 19  TYR C CZ  1 
ATOM   4576  O  OH  . TYR C  1 19  ? 34.986  17.372  -30.348 1.00 21.31  ? 19  TYR C OH  1 
ATOM   4577  N  N   A PRO C  1 20  ? 31.487  17.616  -38.498 0.50 10.77  ? 20  PRO C N   1 
ATOM   4578  N  N   B PRO C  1 20  ? 31.586  17.554  -38.526 0.50 11.06  ? 20  PRO C N   1 
ATOM   4579  C  CA  A PRO C  1 20  ? 30.671  17.384  -39.666 0.50 10.89  ? 20  PRO C CA  1 
ATOM   4580  C  CA  B PRO C  1 20  ? 30.624  17.318  -39.582 0.50 12.24  ? 20  PRO C CA  1 
ATOM   4581  C  C   A PRO C  1 20  ? 30.899  15.984  -40.261 0.50 10.17  ? 20  PRO C C   1 
ATOM   4582  C  C   B PRO C  1 20  ? 30.904  15.999  -40.320 0.50 10.89  ? 20  PRO C C   1 
ATOM   4583  O  O   A PRO C  1 20  ? 29.971  15.401  -40.782 0.50 11.52  ? 20  PRO C O   1 
ATOM   4584  O  O   B PRO C  1 20  ? 30.016  15.503  -41.011 0.50 9.54   ? 20  PRO C O   1 
ATOM   4585  C  CB  A PRO C  1 20  ? 31.115  18.475  -40.641 0.50 12.26  ? 20  PRO C CB  1 
ATOM   4586  C  CB  B PRO C  1 20  ? 30.818  18.513  -40.521 0.50 13.05  ? 20  PRO C CB  1 
ATOM   4587  C  CG  A PRO C  1 20  ? 31.572  19.594  -39.759 0.50 12.25  ? 20  PRO C CG  1 
ATOM   4588  C  CG  B PRO C  1 20  ? 32.246  18.922  -40.242 0.50 14.35  ? 20  PRO C CG  1 
ATOM   4589  C  CD  A PRO C  1 20  ? 32.168  18.932  -38.522 0.50 10.11  ? 20  PRO C CD  1 
ATOM   4590  C  CD  B PRO C  1 20  ? 32.435  18.739  -38.764 0.50 12.21  ? 20  PRO C CD  1 
ATOM   4591  N  N   . SER C  1 21  ? 32.087  15.413  -40.194 1.00 10.09  ? 21  SER C N   1 
ATOM   4592  C  CA  . SER C  1 21  ? 32.281  14.119  -40.833 1.00 10.30  ? 21  SER C CA  1 
ATOM   4593  C  C   . SER C  1 21  ? 31.434  13.014  -40.192 1.00 8.83   ? 21  SER C C   1 
ATOM   4594  O  O   . SER C  1 21  ? 31.210  11.988  -40.832 1.00 9.55   ? 21  SER C O   1 
ATOM   4595  C  CB  . SER C  1 21  ? 33.781  13.673  -40.802 1.00 10.78  ? 21  SER C CB  1 
ATOM   4596  O  OG  . SER C  1 21  ? 34.565  14.484  -41.622 1.00 12.08  ? 21  SER C OG  1 
ATOM   4597  N  N   . CYS C  1 22  ? 30.952  13.226  -38.961 1.00 9.75   ? 22  CYS C N   1 
ATOM   4598  C  CA  . CYS C  1 22  ? 30.096  12.218  -38.316 1.00 9.66   ? 22  CYS C CA  1 
ATOM   4599  C  C   . CYS C  1 22  ? 28.764  12.056  -39.034 1.00 9.96   ? 22  CYS C C   1 
ATOM   4600  O  O   . CYS C  1 22  ? 28.092  11.035  -38.792 1.00 9.93   ? 22  CYS C O   1 
ATOM   4601  C  CB  . CYS C  1 22  ? 29.887  12.559  -36.843 1.00 10.34  ? 22  CYS C CB  1 
ATOM   4602  S  SG  . CYS C  1 22  ? 31.423  12.628  -35.874 1.00 10.52  ? 22  CYS C SG  1 
ATOM   4603  N  N   . GLY C  1 23  ? 28.388  13.023  -39.889 1.00 9.97   ? 23  GLY C N   1 
ATOM   4604  C  CA  . GLY C  1 23  ? 27.219  12.895  -40.719 1.00 10.66  ? 23  GLY C CA  1 
ATOM   4605  C  C   . GLY C  1 23  ? 27.529  12.665  -42.201 1.00 9.81   ? 23  GLY C C   1 
ATOM   4606  O  O   . GLY C  1 23  ? 26.624  12.769  -43.029 1.00 10.64  ? 23  GLY C O   1 
ATOM   4607  N  N   . GLY C  1 24  ? 28.800  12.343  -42.506 1.00 10.71  ? 24  GLY C N   1 
ATOM   4608  C  CA  . GLY C  1 24  ? 29.213  12.143  -43.880 1.00 11.37  ? 24  GLY C CA  1 
ATOM   4609  C  C   . GLY C  1 24  ? 29.337  10.717  -44.306 1.00 10.47  ? 24  GLY C C   1 
ATOM   4610  O  O   . GLY C  1 24  ? 28.646  9.828   -43.786 1.00 11.84  ? 24  GLY C O   1 
ATOM   4611  N  N   . LEU C  1 25  ? 30.146  10.521  -45.324 1.00 11.60  ? 25  LEU C N   1 
ATOM   4612  C  CA  . LEU C  1 25  ? 30.307  9.202   -45.962 1.00 12.65  ? 25  LEU C CA  1 
ATOM   4613  C  C   . LEU C  1 25  ? 31.182  8.282   -45.100 1.00 9.95   ? 25  LEU C C   1 
ATOM   4614  O  O   . LEU C  1 25  ? 31.936  8.719   -44.223 1.00 10.67  ? 25  LEU C O   1 
ATOM   4615  C  CB  . LEU C  1 25  ? 31.001  9.400   -47.341 1.00 15.13  ? 25  LEU C CB  1 
ATOM   4616  C  CG  . LEU C  1 25  ? 30.250  10.278  -48.331 1.00 17.84  ? 25  LEU C CG  1 
ATOM   4617  C  CD1 . LEU C  1 25  ? 30.984  10.480  -49.634 1.00 23.50  ? 25  LEU C CD1 1 
ATOM   4618  C  CD2 . LEU C  1 25  ? 28.892  9.660   -48.549 1.00 26.12  ? 25  LEU C CD2 1 
ATOM   4619  N  N   . LEU C  1 26  ? 31.084  7.007   -45.411 1.00 11.33  ? 26  LEU C N   1 
ATOM   4620  C  CA  . LEU C  1 26  ? 32.004  5.946   -44.978 1.00 10.46  ? 26  LEU C CA  1 
ATOM   4621  C  C   . LEU C  1 26  ? 31.979  5.751   -43.482 1.00 8.86   ? 26  LEU C C   1 
ATOM   4622  O  O   . LEU C  1 26  ? 32.986  5.364   -42.912 1.00 10.96  ? 26  LEU C O   1 
ATOM   4623  C  CB  . LEU C  1 26  ? 33.446  6.145   -45.503 1.00 12.28  ? 26  LEU C CB  1 
ATOM   4624  C  CG  . LEU C  1 26  ? 33.726  6.082   -46.982 1.00 20.84  ? 26  LEU C CG  1 
ATOM   4625  C  CD1 . LEU C  1 26  ? 35.258  6.015   -47.218 1.00 24.21  ? 26  LEU C CD1 1 
ATOM   4626  C  CD2 . LEU C  1 26  ? 32.859  5.216   -47.841 1.00 20.02  ? 26  LEU C CD2 1 
ATOM   4627  N  N   . GLN C  1 27  ? 30.837  5.955   -42.835 1.00 8.97   ? 27  GLN C N   1 
ATOM   4628  C  CA  . GLN C  1 27  ? 30.856  5.872   -41.352 1.00 7.97   ? 27  GLN C CA  1 
ATOM   4629  C  C   . GLN C  1 27  ? 30.862  4.436   -40.845 1.00 8.49   ? 27  GLN C C   1 
ATOM   4630  O  O   . GLN C  1 27  ? 30.230  3.530   -41.378 1.00 10.69  ? 27  GLN C O   1 
ATOM   4631  C  CB  . GLN C  1 27  ? 29.648  6.632   -40.771 1.00 8.44   ? 27  GLN C CB  1 
ATOM   4632  C  CG  . GLN C  1 27  ? 29.721  8.123   -41.079 1.00 8.93   ? 27  GLN C CG  1 
ATOM   4633  C  CD  . GLN C  1 27  ? 30.882  8.754   -40.376 1.00 8.12   ? 27  GLN C CD  1 
ATOM   4634  O  OE1 . GLN C  1 27  ? 30.841  8.945   -39.171 1.00 9.08   ? 27  GLN C OE1 1 
ATOM   4635  N  NE2 . GLN C  1 27  ? 31.983  9.042   -41.109 1.00 8.64   ? 27  GLN C NE2 1 
ATOM   4636  N  N   . SER C  1 28  ? 31.590  4.276   -39.762 1.00 7.25   ? 28  SER C N   1 
ATOM   4637  C  CA  . SER C  1 28  ? 31.708  3.050   -38.981 1.00 7.59   ? 28  SER C CA  1 
ATOM   4638  C  C   . SER C  1 28  ? 31.124  3.232   -37.605 1.00 7.46   ? 28  SER C C   1 
ATOM   4639  O  O   . SER C  1 28  ? 31.001  4.378   -37.125 1.00 8.28   ? 28  SER C O   1 
ATOM   4640  C  CB  . SER C  1 28  ? 33.189  2.712   -38.842 1.00 7.89   ? 28  SER C CB  1 
ATOM   4641  O  OG  . SER C  1 28  ? 33.768  2.447   -40.112 1.00 7.96   ? 28  SER C OG  1 
ATOM   4642  N  N   . PRO C  1 29  ? 30.773  2.146   -36.878 1.00 6.90   ? 29  PRO C N   1 
ATOM   4643  C  CA  . PRO C  1 29  ? 30.862  0.752   -37.259 1.00 7.26   ? 29  PRO C CA  1 
ATOM   4644  C  C   . PRO C  1 29  ? 29.671  0.327   -38.069 1.00 6.93   ? 29  PRO C C   1 
ATOM   4645  O  O   . PRO C  1 29  ? 28.740  1.094   -38.319 1.00 7.48   ? 29  PRO C O   1 
ATOM   4646  C  CB  . PRO C  1 29  ? 30.876  0.061   -35.882 1.00 8.38   ? 29  PRO C CB  1 
ATOM   4647  C  CG  . PRO C  1 29  ? 29.876  0.921   -35.094 1.00 8.53   ? 29  PRO C CG  1 
ATOM   4648  C  CD  . PRO C  1 29  ? 30.189  2.319   -35.549 1.00 7.65   ? 29  PRO C CD  1 
ATOM   4649  N  N   . ILE C  1 30  ? 29.695  -0.951  -38.482 1.00 7.55   ? 30  ILE C N   1 
ATOM   4650  C  CA  . ILE C  1 30  ? 28.662  -1.525  -39.355 1.00 7.61   ? 30  ILE C CA  1 
ATOM   4651  C  C   . ILE C  1 30  ? 28.366  -2.935  -38.903 1.00 7.58   ? 30  ILE C C   1 
ATOM   4652  O  O   . ILE C  1 30  ? 29.156  -3.565  -38.133 1.00 8.21   ? 30  ILE C O   1 
ATOM   4653  C  CB  . ILE C  1 30  ? 29.122  -1.538  -40.826 1.00 7.49   ? 30  ILE C CB  1 
ATOM   4654  C  CG1 . ILE C  1 30  ? 30.372  -2.426  -41.042 1.00 8.46   ? 30  ILE C CG1 1 
ATOM   4655  C  CG2 . ILE C  1 30  ? 29.339  -0.117  -41.305 1.00 10.04  ? 30  ILE C CG2 1 
ATOM   4656  C  CD1 . ILE C  1 30  ? 30.729  -2.661  -42.504 1.00 9.61   ? 30  ILE C CD1 1 
ATOM   4657  N  N   . ASP C  1 31  ? 27.257  -3.445  -39.402 1.00 7.92   ? 31  ASP C N   1 
ATOM   4658  C  CA  . ASP C  1 31  ? 26.896  -4.856  -39.248 1.00 8.43   ? 31  ASP C CA  1 
ATOM   4659  C  C   . ASP C  1 31  ? 27.549  -5.687  -40.361 1.00 8.09   ? 31  ASP C C   1 
ATOM   4660  O  O   . ASP C  1 31  ? 27.426  -5.395  -41.545 1.00 10.94  ? 31  ASP C O   1 
ATOM   4661  C  CB  . ASP C  1 31  ? 25.402  -5.022  -39.347 1.00 9.51   ? 31  ASP C CB  1 
ATOM   4662  C  CG  . ASP C  1 31  ? 24.939  -6.449  -39.101 1.00 10.16  ? 31  ASP C CG  1 
ATOM   4663  O  OD1 . ASP C  1 31  ? 25.458  -7.092  -38.148 1.00 10.38  ? 31  ASP C OD1 1 
ATOM   4664  O  OD2 . ASP C  1 31  ? 24.121  -6.936  -39.893 1.00 14.54  ? 31  ASP C OD2 1 
ATOM   4665  N  N   . LEU C  1 32  ? 28.222  -6.756  -39.965 1.00 9.04   ? 32  LEU C N   1 
ATOM   4666  C  CA  . LEU C  1 32  ? 28.936  -7.668  -40.843 1.00 9.92   ? 32  LEU C CA  1 
ATOM   4667  C  C   . LEU C  1 32  ? 28.035  -8.873  -41.055 1.00 11.28  ? 32  LEU C C   1 
ATOM   4668  O  O   . LEU C  1 32  ? 27.787  -9.626  -40.122 1.00 12.04  ? 32  LEU C O   1 
ATOM   4669  C  CB  . LEU C  1 32  ? 30.238  -8.041  -40.181 1.00 10.25  ? 32  LEU C CB  1 
ATOM   4670  C  CG  . LEU C  1 32  ? 31.154  -6.917  -39.780 1.00 9.65   ? 32  LEU C CG  1 
ATOM   4671  C  CD1 . LEU C  1 32  ? 32.306  -7.365  -38.966 1.00 12.34  ? 32  LEU C CD1 1 
ATOM   4672  C  CD2 . LEU C  1 32  ? 31.665  -6.113  -41.000 1.00 12.70  ? 32  LEU C CD2 1 
ATOM   4673  N  N   . HIS C  1 33  ? 27.482  -9.075  -42.239 1.00 13.94  ? 33  HIS C N   1 
ATOM   4674  C  CA  . HIS C  1 33  ? 26.499  -10.168 -42.466 1.00 16.60  ? 33  HIS C CA  1 
ATOM   4675  C  C   . HIS C  1 33  ? 26.686  -10.721 -43.818 1.00 15.35  ? 33  HIS C C   1 
ATOM   4676  O  O   . HIS C  1 33  ? 27.200  -10.040 -44.663 1.00 14.06  ? 33  HIS C O   1 
ATOM   4677  C  CB  . HIS C  1 33  ? 25.075  -9.679  -42.207 1.00 17.44  ? 33  HIS C CB  1 
ATOM   4678  C  CG  . HIS C  1 33  ? 24.629  -8.591  -43.115 1.00 17.43  ? 33  HIS C CG  1 
ATOM   4679  N  ND1 . HIS C  1 33  ? 23.865  -8.859  -44.222 1.00 22.88  ? 33  HIS C ND1 1 
ATOM   4680  C  CD2 . HIS C  1 33  ? 24.798  -7.227  -43.073 1.00 20.10  ? 33  HIS C CD2 1 
ATOM   4681  C  CE1 . HIS C  1 33  ? 23.589  -7.728  -44.850 1.00 22.60  ? 33  HIS C CE1 1 
ATOM   4682  N  NE2 . HIS C  1 33  ? 24.201  -6.722  -44.220 1.00 20.73  ? 33  HIS C NE2 1 
ATOM   4683  N  N   . SER C  1 34  ? 26.199  -11.961 -44.043 1.00 18.05  ? 34  SER C N   1 
ATOM   4684  C  CA  . SER C  1 34  ? 26.611  -12.777 -45.198 1.00 17.88  ? 34  SER C CA  1 
ATOM   4685  C  C   . SER C  1 34  ? 26.382  -12.128 -46.517 1.00 16.12  ? 34  SER C C   1 
ATOM   4686  O  O   . SER C  1 34  ? 27.225  -12.230 -47.434 1.00 18.96  ? 34  SER C O   1 
ATOM   4687  C  CB  . SER C  1 34  ? 25.880  -14.111 -45.132 1.00 29.84  ? 34  SER C CB  1 
ATOM   4688  O  OG  . SER C  1 34  ? 26.463  -14.782 -44.039 1.00 40.20  ? 34  SER C OG  1 
ATOM   4689  N  N   . ASP C  1 35  ? 25.213  -11.487 -46.673 1.00 16.89  ? 35  ASP C N   1 
ATOM   4690  C  CA  . ASP C  1 35  ? 24.833  -10.997 -47.993 1.00 19.88  ? 35  ASP C CA  1 
ATOM   4691  C  C   . ASP C  1 35  ? 25.708  -9.906  -48.512 1.00 16.38  ? 35  ASP C C   1 
ATOM   4692  O  O   . ASP C  1 35  ? 25.623  -9.588  -49.703 1.00 22.34  ? 35  ASP C O   1 
ATOM   4693  C  CB  . ASP C  1 35  ? 23.343  -10.633 -47.962 1.00 29.65  ? 35  ASP C CB  1 
ATOM   4694  C  CG  . ASP C  1 35  ? 22.424  -11.869 -47.606 1.00 42.49  ? 35  ASP C CG  1 
ATOM   4695  O  OD1 . ASP C  1 35  ? 22.919  -13.030 -47.605 1.00 53.50  ? 35  ASP C OD1 1 
ATOM   4696  O  OD2 . ASP C  1 35  ? 21.205  -11.681 -47.308 1.00 63.42  ? 35  ASP C OD2 1 
ATOM   4697  N  N   . ILE C  1 36  ? 26.525  -9.278  -47.654 1.00 13.63  ? 36  ILE C N   1 
ATOM   4698  C  CA  . ILE C  1 36  ? 27.391  -8.233  -48.123 1.00 13.06  ? 36  ILE C CA  1 
ATOM   4699  C  C   . ILE C  1 36  ? 28.853  -8.664  -48.076 1.00 12.07  ? 36  ILE C C   1 
ATOM   4700  O  O   . ILE C  1 36  ? 29.736  -7.850  -48.327 1.00 13.27  ? 36  ILE C O   1 
ATOM   4701  C  CB  . ILE C  1 36  ? 27.196  -6.934  -47.325 1.00 13.58  ? 36  ILE C CB  1 
ATOM   4702  C  CG1 . ILE C  1 36  ? 27.524  -7.126  -45.820 1.00 15.87  ? 36  ILE C CG1 1 
ATOM   4703  C  CG2 . ILE C  1 36  ? 25.796  -6.333  -47.628 1.00 19.53  ? 36  ILE C CG2 1 
ATOM   4704  C  CD1 . ILE C  1 36  ? 27.647  -5.817  -45.097 1.00 16.59  ? 36  ILE C CD1 1 
ATOM   4705  N  N   . LEU C  1 37  ? 29.158  -9.959  -47.795 1.00 12.55  ? 37  LEU C N   1 
ATOM   4706  C  CA  . LEU C  1 37  ? 30.572  -10.382 -47.773 1.00 12.35  ? 37  LEU C CA  1 
ATOM   4707  C  C   . LEU C  1 37  ? 31.043  -10.849 -49.116 1.00 12.13  ? 37  LEU C C   1 
ATOM   4708  O  O   . LEU C  1 37  ? 30.264  -11.487 -49.902 1.00 16.33  ? 37  LEU C O   1 
ATOM   4709  C  CB  . LEU C  1 37  ? 30.781  -11.573 -46.823 1.00 14.54  ? 37  LEU C CB  1 
ATOM   4710  C  CG  . LEU C  1 37  ? 30.242  -11.302 -45.411 1.00 15.28  ? 37  LEU C CG  1 
ATOM   4711  C  CD1 . LEU C  1 37  ? 30.568  -12.503 -44.510 1.00 16.93  ? 37  LEU C CD1 1 
ATOM   4712  C  CD2 . LEU C  1 37  ? 30.882  -10.070 -44.771 1.00 14.24  ? 37  LEU C CD2 1 
ATOM   4713  N  N   . GLN C  1 38  ? 32.295  -10.602 -49.437 1.00 11.45  ? 38  GLN C N   1 
ATOM   4714  C  CA  . GLN C  1 38  ? 32.873  -11.105 -50.705 1.00 10.97  ? 38  GLN C CA  1 
ATOM   4715  C  C   . GLN C  1 38  ? 34.305  -11.473 -50.433 1.00 11.30  ? 38  GLN C C   1 
ATOM   4716  O  O   . GLN C  1 38  ? 35.097  -10.658 -49.963 1.00 11.51  ? 38  GLN C O   1 
ATOM   4717  C  CB  . GLN C  1 38  ? 32.764  -10.046 -51.782 1.00 13.28  ? 38  GLN C CB  1 
ATOM   4718  C  CG  . GLN C  1 38  ? 33.312  -10.611 -53.133 1.00 15.98  ? 38  GLN C CG  1 
ATOM   4719  C  CD  . GLN C  1 38  ? 33.019  -9.587  -54.230 1.00 18.57  ? 38  GLN C CD  1 
ATOM   4720  O  OE1 . GLN C  1 38  ? 31.825  -9.395  -54.685 1.00 26.33  ? 38  GLN C OE1 1 
ATOM   4721  N  NE2 . GLN C  1 38  ? 33.970  -8.812  -54.508 1.00 21.30  ? 38  GLN C NE2 1 
ATOM   4722  N  N   . TYR C  1 39  ? 34.665  -12.730 -50.745 1.00 12.18  ? 39  TYR C N   1 
ATOM   4723  C  CA  . TYR C  1 39  ? 36.082  -13.151 -50.616 1.00 12.82  ? 39  TYR C CA  1 
ATOM   4724  C  C   . TYR C  1 39  ? 36.961  -12.298 -51.513 1.00 10.99  ? 39  TYR C C   1 
ATOM   4725  O  O   . TYR C  1 39  ? 36.597  -12.012 -52.690 1.00 13.31  ? 39  TYR C O   1 
ATOM   4726  C  CB  . TYR C  1 39  ? 36.130  -14.641 -50.965 1.00 14.32  ? 39  TYR C CB  1 
ATOM   4727  C  CG  . TYR C  1 39  ? 37.561  -15.114 -51.139 1.00 13.92  ? 39  TYR C CG  1 
ATOM   4728  C  CD1 . TYR C  1 39  ? 38.396  -15.209 -50.025 1.00 15.16  ? 39  TYR C CD1 1 
ATOM   4729  C  CD2 . TYR C  1 39  ? 38.050  -15.548 -52.365 1.00 16.77  ? 39  TYR C CD2 1 
ATOM   4730  C  CE1 . TYR C  1 39  ? 39.694  -15.638 -50.139 1.00 17.24  ? 39  TYR C CE1 1 
ATOM   4731  C  CE2 . TYR C  1 39  ? 39.381  -15.993 -52.483 1.00 19.85  ? 39  TYR C CE2 1 
ATOM   4732  C  CZ  . TYR C  1 39  ? 40.204  -16.049 -51.375 1.00 21.03  ? 39  TYR C CZ  1 
ATOM   4733  O  OH  . TYR C  1 39  ? 41.528  -16.456 -51.384 1.00 23.39  ? 39  TYR C OH  1 
ATOM   4734  N  N   . ASP C  1 40  ? 38.139  -11.937 -51.027 1.00 12.38  ? 40  ASP C N   1 
ATOM   4735  C  CA  . ASP C  1 40  ? 39.090  -11.144 -51.804 1.00 12.98  ? 40  ASP C CA  1 
ATOM   4736  C  C   . ASP C  1 40  ? 40.466  -11.760 -51.591 1.00 13.32  ? 40  ASP C C   1 
ATOM   4737  O  O   . ASP C  1 40  ? 40.993  -11.753 -50.503 1.00 13.80  ? 40  ASP C O   1 
ATOM   4738  C  CB  . ASP C  1 40  ? 39.008  -9.710  -51.313 1.00 14.36  ? 40  ASP C CB  1 
ATOM   4739  C  CG  . ASP C  1 40  ? 39.987  -8.749  -51.902 1.00 16.55  ? 40  ASP C CG  1 
ATOM   4740  O  OD1 . ASP C  1 40  ? 40.899  -9.122  -52.613 1.00 15.91  ? 40  ASP C OD1 1 
ATOM   4741  O  OD2 . ASP C  1 40  ? 39.849  -7.504  -51.566 1.00 19.74  ? 40  ASP C OD2 1 
ATOM   4742  N  N   . ALA C  1 41  ? 41.019  -12.329 -52.670 1.00 15.13  ? 41  ALA C N   1 
ATOM   4743  C  CA  . ALA C  1 41  ? 42.362  -12.981 -52.607 1.00 15.11  ? 41  ALA C CA  1 
ATOM   4744  C  C   . ALA C  1 41  ? 43.460  -12.089 -52.248 1.00 15.14  ? 41  ALA C C   1 
ATOM   4745  O  O   . ALA C  1 41  ? 44.575  -12.563 -51.914 1.00 17.11  ? 41  ALA C O   1 
ATOM   4746  C  CB  . ALA C  1 41  ? 42.658  -13.650 -53.923 1.00 19.15  ? 41  ALA C CB  1 
ATOM   4747  N  N   . SER C  1 42  ? 43.304  -10.779 -52.333 1.00 13.93  ? 42  SER C N   1 
ATOM   4748  C  CA  . SER C  1 42  ? 44.376  -9.869  -51.951 1.00 14.48  ? 42  SER C CA  1 
ATOM   4749  C  C   . SER C  1 42  ? 44.584  -9.831  -50.450 1.00 14.36  ? 42  SER C C   1 
ATOM   4750  O  O   . SER C  1 42  ? 45.574  -9.242  -49.985 1.00 15.82  ? 42  SER C O   1 
ATOM   4751  C  CB  . SER C  1 42  ? 44.159  -8.448  -52.428 1.00 17.01  ? 42  SER C CB  1 
ATOM   4752  O  OG  . SER C  1 42  ? 43.096  -7.799  -51.672 1.00 17.69  ? 42  SER C OG  1 
ATOM   4753  N  N   . LEU C  1 43  ? 43.626  -10.356 -49.681 1.00 13.74  ? 43  LEU C N   1 
ATOM   4754  C  CA  . LEU C  1 43  ? 43.648  -10.130 -48.235 1.00 13.21  ? 43  LEU C CA  1 
ATOM   4755  C  C   . LEU C  1 43  ? 44.503  -11.187 -47.597 1.00 14.23  ? 43  LEU C C   1 
ATOM   4756  O  O   . LEU C  1 43  ? 44.016  -12.182 -47.001 1.00 15.78  ? 43  LEU C O   1 
ATOM   4757  C  CB  . LEU C  1 43  ? 42.215  -10.109 -47.706 1.00 12.82  ? 43  LEU C CB  1 
ATOM   4758  C  CG  . LEU C  1 43  ? 41.409  -8.975  -48.251 1.00 11.81  ? 43  LEU C CG  1 
ATOM   4759  C  CD1 . LEU C  1 43  ? 40.003  -9.056  -47.619 1.00 12.94  ? 43  LEU C CD1 1 
ATOM   4760  C  CD2 . LEU C  1 43  ? 42.032  -7.635  -48.037 1.00 14.14  ? 43  LEU C CD2 1 
ATOM   4761  N  N   . THR C  1 44  ? 45.802  -11.031 -47.765 1.00 15.06  ? 44  THR C N   1 
ATOM   4762  C  CA  . THR C  1 44  ? 46.806  -12.011 -47.254 1.00 16.37  ? 44  THR C CA  1 
ATOM   4763  C  C   . THR C  1 44  ? 47.067  -11.710 -45.772 1.00 16.25  ? 44  THR C C   1 
ATOM   4764  O  O   . THR C  1 44  ? 46.615  -10.665 -45.209 1.00 16.49  ? 44  THR C O   1 
ATOM   4765  C  CB  . THR C  1 44  ? 48.086  -11.864 -48.082 1.00 19.73  ? 44  THR C CB  1 
ATOM   4766  O  OG1 . THR C  1 44  ? 48.411  -10.476 -48.090 1.00 22.50  ? 44  THR C OG1 1 
ATOM   4767  C  CG2 . THR C  1 44  ? 47.868  -12.437 -49.529 1.00 24.45  ? 44  THR C CG2 1 
ATOM   4768  N  N   . PRO C  1 45  ? 47.785  -12.567 -45.096 1.00 17.97  ? 45  PRO C N   1 
ATOM   4769  C  CA  . PRO C  1 45  ? 47.983  -12.361 -43.665 1.00 17.60  ? 45  PRO C CA  1 
ATOM   4770  C  C   . PRO C  1 45  ? 48.803  -11.101 -43.327 1.00 19.02  ? 45  PRO C C   1 
ATOM   4771  O  O   . PRO C  1 45  ? 49.817  -10.900 -43.947 1.00 22.85  ? 45  PRO C O   1 
ATOM   4772  C  CB  . PRO C  1 45  ? 48.713  -13.658 -43.233 1.00 22.95  ? 45  PRO C CB  1 
ATOM   4773  C  CG  . PRO C  1 45  ? 48.164  -14.687 -44.235 1.00 25.09  ? 45  PRO C CG  1 
ATOM   4774  C  CD  . PRO C  1 45  ? 48.211  -13.917 -45.526 1.00 21.91  ? 45  PRO C CD  1 
ATOM   4775  N  N   . LEU C  1 46  ? 48.384  -10.297 -42.343 1.00 17.64  ? 46  LEU C N   1 
ATOM   4776  C  CA  . LEU C  1 46  ? 49.154  -9.167  -41.868 1.00 18.33  ? 46  LEU C CA  1 
ATOM   4777  C  C   . LEU C  1 46  ? 50.300  -9.662  -41.009 1.00 20.33  ? 46  LEU C C   1 
ATOM   4778  O  O   . LEU C  1 46  ? 50.208  -10.723 -40.392 1.00 22.64  ? 46  LEU C O   1 
ATOM   4779  C  CB  . LEU C  1 46  ? 48.201  -8.317  -41.022 1.00 18.90  ? 46  LEU C CB  1 
ATOM   4780  C  CG  . LEU C  1 46  ? 47.071  -7.616  -41.833 1.00 20.60  ? 46  LEU C CG  1 
ATOM   4781  C  CD1 . LEU C  1 46  ? 46.182  -6.820  -40.905 1.00 21.62  ? 46  LEU C CD1 1 
ATOM   4782  C  CD2 . LEU C  1 46  ? 47.645  -6.780  -42.965 1.00 22.86  ? 46  LEU C CD2 1 
ATOM   4783  N  N   . GLU C  1 47  ? 51.361  -8.850  -40.892 1.00 21.35  ? 47  GLU C N   1 
ATOM   4784  C  CA  . GLU C  1 47  ? 52.483  -9.095  -39.958 1.00 23.31  ? 47  GLU C CA  1 
ATOM   4785  C  C   . GLU C  1 47  ? 52.477  -7.972  -38.871 1.00 23.45  ? 47  GLU C C   1 
ATOM   4786  O  O   . GLU C  1 47  ? 52.329  -6.777  -39.195 1.00 22.39  ? 47  GLU C O   1 
ATOM   4787  C  CB  . GLU C  1 47  ? 53.779  -9.136  -40.800 1.00 33.13  ? 47  GLU C CB  1 
ATOM   4788  C  CG  . GLU C  1 47  ? 53.681  -10.114 -41.962 1.00 40.59  ? 47  GLU C CG  1 
ATOM   4789  C  CD  . GLU C  1 47  ? 54.673  -9.853  -43.142 1.00 57.85  ? 47  GLU C CD  1 
ATOM   4790  O  OE1 . GLU C  1 47  ? 54.972  -10.798 -43.897 1.00 67.02  ? 47  GLU C OE1 1 
ATOM   4791  O  OE2 . GLU C  1 47  ? 55.155  -8.718  -43.361 1.00 67.48  ? 47  GLU C OE2 1 
ATOM   4792  N  N   . PHE C  1 48  ? 52.614  -8.355  -37.571 1.00 17.54  ? 48  PHE C N   1 
ATOM   4793  C  CA  . PHE C  1 48  ? 52.546  -7.400  -36.486 1.00 20.80  ? 48  PHE C CA  1 
ATOM   4794  C  C   . PHE C  1 48  ? 54.004  -7.279  -36.040 1.00 19.79  ? 48  PHE C C   1 
ATOM   4795  O  O   . PHE C  1 48  ? 54.576  -8.223  -35.448 1.00 27.30  ? 48  PHE C O   1 
ATOM   4796  C  CB  . PHE C  1 48  ? 51.560  -7.943  -35.437 1.00 21.57  ? 48  PHE C CB  1 
ATOM   4797  C  CG  . PHE C  1 48  ? 50.265  -8.376  -36.056 1.00 21.62  ? 48  PHE C CG  1 
ATOM   4798  C  CD1 . PHE C  1 48  ? 49.364  -7.450  -36.566 1.00 20.15  ? 48  PHE C CD1 1 
ATOM   4799  C  CD2 . PHE C  1 48  ? 49.970  -9.730  -36.246 1.00 19.90  ? 48  PHE C CD2 1 
ATOM   4800  C  CE1 . PHE C  1 48  ? 48.210  -7.851  -37.221 1.00 22.49  ? 48  PHE C CE1 1 
ATOM   4801  C  CE2 . PHE C  1 48  ? 48.764  -10.158 -36.851 1.00 22.75  ? 48  PHE C CE2 1 
ATOM   4802  C  CZ  . PHE C  1 48  ? 47.872  -9.191  -37.328 1.00 21.19  ? 48  PHE C CZ  1 
ATOM   4803  N  N   . GLN C  1 49  ? 54.590  -6.126  -36.309 1.00 19.23  ? 49  GLN C N   1 
ATOM   4804  C  CA  . GLN C  1 49  ? 56.025  -5.947  -36.055 1.00 24.81  ? 49  GLN C CA  1 
ATOM   4805  C  C   . GLN C  1 49  ? 56.205  -5.039  -34.863 1.00 24.87  ? 49  GLN C C   1 
ATOM   4806  O  O   . GLN C  1 49  ? 55.520  -3.993  -34.752 1.00 21.77  ? 49  GLN C O   1 
ATOM   4807  C  CB  . GLN C  1 49  ? 56.591  -5.261  -37.324 1.00 25.90  ? 49  GLN C CB  1 
ATOM   4808  C  CG  . GLN C  1 49  ? 56.438  -6.114  -38.561 1.00 28.90  ? 49  GLN C CG  1 
ATOM   4809  C  CD  . GLN C  1 49  ? 57.667  -6.958  -38.781 1.00 48.46  ? 49  GLN C CD  1 
ATOM   4810  O  OE1 . GLN C  1 49  ? 58.744  -6.624  -38.262 1.00 61.82  ? 49  GLN C OE1 1 
ATOM   4811  N  NE2 . GLN C  1 49  ? 57.539  -8.042  -39.553 1.00 49.53  ? 49  GLN C NE2 1 
ATOM   4812  N  N   . GLY C  1 50  ? 57.146  -5.413  -33.953 1.00 23.43  ? 50  GLY C N   1 
ATOM   4813  C  CA  . GLY C  1 50  ? 57.401  -4.512  -32.859 1.00 28.14  ? 50  GLY C CA  1 
ATOM   4814  C  C   . GLY C  1 50  ? 56.338  -4.511  -31.767 1.00 17.25  ? 50  GLY C C   1 
ATOM   4815  O  O   . GLY C  1 50  ? 56.183  -3.516  -31.011 1.00 25.89  ? 50  GLY C O   1 
ATOM   4816  N  N   . TYR C  1 51  ? 55.483  -5.536  -31.854 1.00 25.89  ? 51  TYR C N   1 
ATOM   4817  C  CA  . TYR C  1 51  ? 54.374  -5.616  -30.881 1.00 21.42  ? 51  TYR C CA  1 
ATOM   4818  C  C   . TYR C  1 51  ? 54.792  -6.149  -29.490 1.00 26.58  ? 51  TYR C C   1 
ATOM   4819  O  O   . TYR C  1 51  ? 54.114  -5.880  -28.508 1.00 21.18  ? 51  TYR C O   1 
ATOM   4820  C  CB  . TYR C  1 51  ? 53.236  -6.466  -31.364 1.00 20.11  ? 51  TYR C CB  1 
ATOM   4821  C  CG  . TYR C  1 51  ? 52.233  -5.824  -32.288 1.00 21.68  ? 51  TYR C CG  1 
ATOM   4822  C  CD1 . TYR C  1 51  ? 52.582  -4.939  -33.322 1.00 17.34  ? 51  TYR C CD1 1 
ATOM   4823  C  CD2 . TYR C  1 51  ? 50.867  -6.042  -32.091 1.00 16.30  ? 51  TYR C CD2 1 
ATOM   4824  C  CE1 . TYR C  1 51  ? 51.619  -4.375  -34.161 1.00 18.47  ? 51  TYR C CE1 1 
ATOM   4825  C  CE2 . TYR C  1 51  ? 49.920  -5.542  -32.944 1.00 20.43  ? 51  TYR C CE2 1 
ATOM   4826  C  CZ  . TYR C  1 51  ? 50.283  -4.657  -33.941 1.00 17.38  ? 51  TYR C CZ  1 
ATOM   4827  O  OH  . TYR C  1 51  ? 49.262  -4.148  -34.695 1.00 18.73  ? 51  TYR C OH  1 
ATOM   4828  N  N   . ASN C  1 52  ? 55.996  -6.638  -29.362 1.00 24.11  ? 52  ASN C N   1 
ATOM   4829  C  CA  . ASN C  1 52  ? 56.433  -7.153  -28.082 1.00 26.11  ? 52  ASN C CA  1 
ATOM   4830  C  C   . ASN C  1 52  ? 57.125  -6.054  -27.338 1.00 26.06  ? 52  ASN C C   1 
ATOM   4831  O  O   . ASN C  1 52  ? 58.362  -5.891  -27.470 1.00 38.16  ? 52  ASN C O   1 
ATOM   4832  C  CB  . ASN C  1 52  ? 57.378  -8.302  -28.381 1.00 35.09  ? 52  ASN C CB  1 
ATOM   4833  C  CG  . ASN C  1 52  ? 57.520  -9.223  -27.232 1.00 39.67  ? 52  ASN C CG  1 
ATOM   4834  O  OD1 . ASN C  1 52  ? 57.030  -8.919  -26.143 1.00 32.99  ? 52  ASN C OD1 1 
ATOM   4835  N  ND2 . ASN C  1 52  ? 58.161  -10.336 -27.456 1.00 51.70  ? 52  ASN C ND2 1 
ATOM   4836  N  N   . LEU C  1 53  ? 56.391  -5.305  -26.532 1.00 27.92  ? 53  LEU C N   1 
ATOM   4837  C  CA  . LEU C  1 53  ? 56.883  -4.169  -25.790 1.00 26.52  ? 53  LEU C CA  1 
ATOM   4838  C  C   . LEU C  1 53  ? 57.644  -4.717  -24.547 1.00 35.55  ? 53  LEU C C   1 
ATOM   4839  O  O   . LEU C  1 53  ? 57.318  -5.837  -24.058 1.00 52.20  ? 53  LEU C O   1 
ATOM   4840  C  CB  . LEU C  1 53  ? 55.718  -3.254  -25.439 1.00 24.67  ? 53  LEU C CB  1 
ATOM   4841  C  CG  . LEU C  1 53  ? 54.798  -2.754  -26.608 1.00 19.86  ? 53  LEU C CG  1 
ATOM   4842  C  CD1 . LEU C  1 53  ? 53.757  -1.774  -26.096 1.00 18.94  ? 53  LEU C CD1 1 
ATOM   4843  C  CD2 . LEU C  1 53  ? 55.636  -2.150  -27.785 1.00 27.32  ? 53  LEU C CD2 1 
ATOM   4844  N  N   . SER C  1 54  ? 58.719  -4.016  -24.144 1.00 33.15  ? 54  SER C N   1 
ATOM   4845  C  CA  . SER C  1 54  ? 59.562  -4.428  -22.999 1.00 37.85  ? 54  SER C CA  1 
ATOM   4846  C  C   . SER C  1 54  ? 58.877  -4.222  -21.681 1.00 52.92  ? 54  SER C C   1 
ATOM   4847  O  O   . SER C  1 54  ? 58.257  -3.137  -21.445 1.00 88.64  ? 54  SER C O   1 
ATOM   4848  C  CB  . SER C  1 54  ? 60.901  -3.670  -22.943 1.00 48.78  ? 54  SER C CB  1 
ATOM   4849  O  OG  . SER C  1 54  ? 61.553  -3.645  -24.193 1.00 55.90  ? 54  SER C OG  1 
ATOM   4850  N  N   . ALA C  1 55  ? 59.083  -5.225  -20.794 1.00 64.07  ? 55  ALA C N   1 
ATOM   4851  C  CA  . ALA C  1 55  ? 58.433  -5.206  -19.506 1.00 57.97  ? 55  ALA C CA  1 
ATOM   4852  C  C   . ALA C  1 55  ? 58.971  -3.964  -18.793 1.00 83.80  ? 55  ALA C C   1 
ATOM   4853  O  O   . ALA C  1 55  ? 58.201  -3.246  -18.026 1.00 141.01 ? 55  ALA C O   1 
ATOM   4854  C  CB  . ALA C  1 55  ? 58.740  -6.482  -18.753 1.00 51.34  ? 55  ALA C CB  1 
ATOM   4855  N  N   . ASN C  1 56  ? 60.237  -3.634  -19.149 1.00 45.01  ? 56  ASN C N   1 
ATOM   4856  C  CA  . ASN C  1 56  ? 60.943  -2.559  -18.404 1.00 66.60  ? 56  ASN C CA  1 
ATOM   4857  C  C   . ASN C  1 56  ? 60.664  -1.133  -18.978 1.00 70.65  ? 56  ASN C C   1 
ATOM   4858  O  O   . ASN C  1 56  ? 61.019  -0.095  -18.349 1.00 193.41 ? 56  ASN C O   1 
ATOM   4859  N  N   . LYS C  1 57  ? 59.954  -1.117  -20.140 1.00 46.84  ? 57  LYS C N   1 
ATOM   4860  C  CA  . LYS C  1 57  ? 59.502  0.105   -20.775 1.00 57.25  ? 57  LYS C CA  1 
ATOM   4861  C  C   . LYS C  1 57  ? 58.066  0.225   -20.165 1.00 24.18  ? 57  LYS C C   1 
ATOM   4862  O  O   . LYS C  1 57  ? 57.444  -0.801  -19.733 1.00 36.08  ? 57  LYS C O   1 
ATOM   4863  C  CB  . LYS C  1 57  ? 59.433  -0.088  -22.293 1.00 46.01  ? 57  LYS C CB  1 
ATOM   4864  C  CG  . LYS C  1 57  ? 59.787  1.133   -23.212 1.00 62.31  ? 57  LYS C CG  1 
ATOM   4865  N  N   . GLN C  1 58  ? 57.521  1.472   -20.125 1.00 30.70  ? 58  GLN C N   1 
ATOM   4866  C  CA  . GLN C  1 58  ? 56.146  1.732   -19.704 1.00 30.42  ? 58  GLN C CA  1 
ATOM   4867  C  C   . GLN C  1 58  ? 55.419  2.685   -20.666 1.00 33.18  ? 58  GLN C C   1 
ATOM   4868  O  O   . GLN C  1 58  ? 56.027  3.470   -21.388 1.00 28.55  ? 58  GLN C O   1 
ATOM   4869  C  CB  . GLN C  1 58  ? 56.111  2.255   -18.250 1.00 43.91  ? 58  GLN C CB  1 
ATOM   4870  C  CG  . GLN C  1 58  ? 56.615  3.675   -18.115 1.00 27.84  ? 58  GLN C CG  1 
ATOM   4871  C  CD  . GLN C  1 58  ? 56.550  4.193   -16.691 1.00 31.44  ? 58  GLN C CD  1 
ATOM   4872  O  OE1 . GLN C  1 58  ? 56.275  3.444   -15.749 1.00 48.65  ? 58  GLN C OE1 1 
ATOM   4873  N  NE2 . GLN C  1 58  ? 56.712  5.463   -16.556 1.00 27.30  ? 58  GLN C NE2 1 
ATOM   4874  N  N   . PHE C  1 59  ? 54.079  2.583   -20.588 1.00 26.10  ? 59  PHE C N   1 
ATOM   4875  C  CA  . PHE C  1 59  ? 53.083  3.082   -21.570 1.00 26.35  ? 59  PHE C CA  1 
ATOM   4876  C  C   . PHE C  1 59  ? 51.966  3.817   -20.914 1.00 22.14  ? 59  PHE C C   1 
ATOM   4877  O  O   . PHE C  1 59  ? 51.407  3.323   -19.934 1.00 24.18  ? 59  PHE C O   1 
ATOM   4878  C  CB  . PHE C  1 59  ? 52.655  1.938   -22.549 1.00 23.99  ? 59  PHE C CB  1 
ATOM   4879  C  CG  . PHE C  1 59  ? 53.844  1.357   -23.253 1.00 28.99  ? 59  PHE C CG  1 
ATOM   4880  C  CD1 . PHE C  1 59  ? 54.375  2.003   -24.373 1.00 28.33  ? 59  PHE C CD1 1 
ATOM   4881  C  CD2 . PHE C  1 59  ? 54.579  0.291   -22.715 1.00 31.04  ? 59  PHE C CD2 1 
ATOM   4882  C  CE1 . PHE C  1 59  ? 55.525  1.524   -24.971 1.00 25.78  ? 59  PHE C CE1 1 
ATOM   4883  C  CE2 . PHE C  1 59  ? 55.770  -0.103  -23.247 1.00 27.01  ? 59  PHE C CE2 1 
ATOM   4884  C  CZ  . PHE C  1 59  ? 56.268  0.487   -24.405 1.00 29.35  ? 59  PHE C CZ  1 
ATOM   4885  N  N   A LEU C  1 60  ? 51.550  5.000   -21.418 0.50 17.53  ? 60  LEU C N   1 
ATOM   4886  N  N   B LEU C  1 60  ? 51.869  5.075   -21.289 0.50 25.29  ? 60  LEU C N   1 
ATOM   4887  C  CA  A LEU C  1 60  ? 50.665  5.898   -20.670 0.50 17.15  ? 60  LEU C CA  1 
ATOM   4888  C  CA  B LEU C  1 60  ? 50.838  5.913   -20.807 0.50 22.56  ? 60  LEU C CA  1 
ATOM   4889  C  C   A LEU C  1 60  ? 49.210  5.435   -20.863 0.50 15.30  ? 60  LEU C C   1 
ATOM   4890  C  C   B LEU C  1 60  ? 49.526  5.144   -21.118 0.50 32.40  ? 60  LEU C C   1 
ATOM   4891  O  O   A LEU C  1 60  ? 48.706  5.314   -21.988 0.50 12.65  ? 60  LEU C O   1 
ATOM   4892  O  O   B LEU C  1 60  ? 49.329  4.518   -22.188 0.50 26.14  ? 60  LEU C O   1 
ATOM   4893  C  CB  A LEU C  1 60  ? 50.846  7.363   -21.092 0.50 15.41  ? 60  LEU C CB  1 
ATOM   4894  C  CB  B LEU C  1 60  ? 50.899  7.282   -21.503 0.50 26.61  ? 60  LEU C CB  1 
ATOM   4895  C  CG  A LEU C  1 60  ? 49.873  8.353   -20.486 0.50 15.55  ? 60  LEU C CG  1 
ATOM   4896  C  CG  B LEU C  1 60  ? 50.495  8.561   -20.749 0.50 20.59  ? 60  LEU C CG  1 
ATOM   4897  C  CD1 A LEU C  1 60  ? 50.164  8.501   -18.975 0.50 18.95  ? 60  LEU C CD1 1 
ATOM   4898  C  CD1 B LEU C  1 60  ? 50.978  8.624   -19.283 0.50 22.74  ? 60  LEU C CD1 1 
ATOM   4899  C  CD2 A LEU C  1 60  ? 49.976  9.703   -21.199 0.50 16.58  ? 60  LEU C CD2 1 
ATOM   4900  C  CD2 B LEU C  1 60  ? 50.877  9.847   -21.488 0.50 27.40  ? 60  LEU C CD2 1 
ATOM   4901  N  N   A LEU C  1 61  ? 48.564  5.159   -19.736 0.50 15.73  ? 61  LEU C N   1 
ATOM   4902  N  N   B LEU C  1 61  ? 48.672  5.168   -20.099 0.50 39.22  ? 61  LEU C N   1 
ATOM   4903  C  CA  A LEU C  1 61  ? 47.127  4.863   -19.694 0.50 13.72  ? 61  LEU C CA  1 
ATOM   4904  C  CA  B LEU C  1 61  ? 47.305  4.653   -20.105 0.50 32.64  ? 61  LEU C CA  1 
ATOM   4905  C  C   A LEU C  1 61  ? 46.394  6.137   -19.284 0.50 18.25  ? 61  LEU C C   1 
ATOM   4906  C  C   B LEU C  1 61  ? 46.505  5.884   -19.472 0.50 25.31  ? 61  LEU C C   1 
ATOM   4907  O  O   A LEU C  1 61  ? 46.693  6.746   -18.295 0.50 15.21  ? 61  LEU C O   1 
ATOM   4908  O  O   B LEU C  1 61  ? 46.995  6.312   -18.449 0.50 34.23  ? 61  LEU C O   1 
ATOM   4909  C  CB  A LEU C  1 61  ? 46.842  3.895   -18.593 0.50 16.43  ? 61  LEU C CB  1 
ATOM   4910  C  CB  B LEU C  1 61  ? 47.396  3.348   -19.236 0.50 26.29  ? 61  LEU C CB  1 
ATOM   4911  C  CG  A LEU C  1 61  ? 45.626  3.023   -18.745 0.50 16.03  ? 61  LEU C CG  1 
ATOM   4912  C  CG  B LEU C  1 61  ? 46.281  2.250   -19.165 0.50 28.29  ? 61  LEU C CG  1 
ATOM   4913  C  CD1 A LEU C  1 61  ? 45.639  2.184   -20.055 0.50 15.97  ? 61  LEU C CD1 1 
ATOM   4914  C  CD1 B LEU C  1 61  ? 46.064  1.300   -20.382 0.50 22.93  ? 61  LEU C CD1 1 
ATOM   4915  C  CD2 A LEU C  1 61  ? 45.507  2.143   -17.508 0.50 21.13  ? 61  LEU C CD2 1 
ATOM   4916  C  CD2 B LEU C  1 61  ? 46.312  1.475   -17.830 0.50 29.39  ? 61  LEU C CD2 1 
ATOM   4917  N  N   . THR C  1 62  ? 45.358  6.416   -20.033 1.00 16.43  ? 62  THR C N   1 
ATOM   4918  C  CA  . THR C  1 62  ? 44.574  7.671   -19.796 1.00 18.24  ? 62  THR C CA  1 
ATOM   4919  C  C   . THR C  1 62  ? 43.093  7.366   -19.875 1.00 18.83  ? 62  THR C C   1 
ATOM   4920  O  O   . THR C  1 62  ? 42.603  6.766   -20.858 1.00 19.91  ? 62  THR C O   1 
ATOM   4921  C  CB  . THR C  1 62  ? 44.836  8.752   -20.892 1.00 19.29  ? 62  THR C CB  1 
ATOM   4922  O  OG1 . THR C  1 62  ? 46.218  9.057   -21.026 1.00 21.51  ? 62  THR C OG1 1 
ATOM   4923  C  CG2 . THR C  1 62  ? 44.098  10.026  -20.660 1.00 27.93  ? 62  THR C CG2 1 
ATOM   4924  N  N   . ASN C  1 63  ? 42.388  7.819   -18.866 1.00 21.29  ? 63  ASN C N   1 
ATOM   4925  C  CA  . ASN C  1 63  ? 40.998  7.962   -18.977 1.00 17.72  ? 63  ASN C CA  1 
ATOM   4926  C  C   . ASN C  1 63  ? 40.641  9.332   -19.626 1.00 18.71  ? 63  ASN C C   1 
ATOM   4927  O  O   . ASN C  1 63  ? 40.913  10.368  -19.028 1.00 18.95  ? 63  ASN C O   1 
ATOM   4928  C  CB  . ASN C  1 63  ? 40.389  7.757   -17.622 1.00 18.79  ? 63  ASN C CB  1 
ATOM   4929  C  CG  . ASN C  1 63  ? 38.914  7.983   -17.603 1.00 21.16  ? 63  ASN C CG  1 
ATOM   4930  O  OD1 . ASN C  1 63  ? 38.322  8.676   -18.407 1.00 21.17  ? 63  ASN C OD1 1 
ATOM   4931  N  ND2 . ASN C  1 63  ? 38.294  7.479   -16.504 1.00 22.06  ? 63  ASN C ND2 1 
ATOM   4932  N  N   . ASN C  1 64  ? 40.189  9.330   -20.878 1.00 20.43  ? 64  ASN C N   1 
ATOM   4933  C  CA  . ASN C  1 64  ? 39.955  10.589  -21.512 1.00 19.86  ? 64  ASN C CA  1 
ATOM   4934  C  C   . ASN C  1 64  ? 38.530  10.928  -21.434 1.00 18.49  ? 64  ASN C C   1 
ATOM   4935  O  O   . ASN C  1 64  ? 38.099  11.878  -22.109 1.00 22.72  ? 64  ASN C O   1 
ATOM   4936  C  CB  . ASN C  1 64  ? 40.500  10.540  -22.943 1.00 21.77  ? 64  ASN C CB  1 
ATOM   4937  C  CG  . ASN C  1 64  ? 39.834  9.464   -23.767 1.00 23.66  ? 64  ASN C CG  1 
ATOM   4938  O  OD1 . ASN C  1 64  ? 38.869  8.770   -23.375 1.00 27.62  ? 64  ASN C OD1 1 
ATOM   4939  N  ND2 . ASN C  1 64  ? 40.301  9.360   -24.966 1.00 29.47  ? 64  ASN C ND2 1 
ATOM   4940  N  N   . GLY C  1 65  ? 37.803  10.232  -20.532 1.00 24.87  ? 65  GLY C N   1 
ATOM   4941  C  CA  . GLY C  1 65  ? 36.385  10.508  -20.381 1.00 25.56  ? 65  GLY C CA  1 
ATOM   4942  C  C   . GLY C  1 65  ? 35.541  9.824   -21.390 1.00 21.68  ? 65  GLY C C   1 
ATOM   4943  O  O   . GLY C  1 65  ? 34.341  9.801   -21.231 1.00 31.56  ? 65  GLY C O   1 
ATOM   4944  N  N   . HIS C  1 66  ? 36.164  9.200   -22.398 1.00 22.47  ? 66  HIS C N   1 
ATOM   4945  C  CA  . HIS C  1 66  ? 35.418  8.533   -23.455 1.00 21.73  ? 66  HIS C CA  1 
ATOM   4946  C  C   . HIS C  1 66  ? 35.671  7.064   -23.402 1.00 18.28  ? 66  HIS C C   1 
ATOM   4947  O  O   . HIS C  1 66  ? 34.841  6.197   -23.671 1.00 24.22  ? 66  HIS C O   1 
ATOM   4948  C  CB  . HIS C  1 66  ? 35.874  9.062   -24.835 1.00 17.85  ? 66  HIS C CB  1 
ATOM   4949  C  CG  . HIS C  1 66  ? 35.645  10.524  -24.996 1.00 20.69  ? 66  HIS C CG  1 
ATOM   4950  N  ND1 . HIS C  1 66  ? 36.666  11.394  -25.220 1.00 23.06  ? 66  HIS C ND1 1 
ATOM   4951  C  CD2 . HIS C  1 66  ? 34.474  11.310  -24.855 1.00 19.75  ? 66  HIS C CD2 1 
ATOM   4952  C  CE1 . HIS C  1 66  ? 36.174  12.657  -25.322 1.00 21.61  ? 66  HIS C CE1 1 
ATOM   4953  N  NE2 . HIS C  1 66  ? 34.821  12.591  -25.131 1.00 23.48  ? 66  HIS C NE2 1 
ATOM   4954  N  N   . SER C  1 67  ? 36.911  6.744   -23.166 1.00 20.26  ? 67  SER C N   1 
ATOM   4955  C  CA  . SER C  1 67  ? 37.351  5.416   -23.015 1.00 16.93  ? 67  SER C CA  1 
ATOM   4956  C  C   . SER C  1 67  ? 38.561  5.421   -22.145 1.00 19.58  ? 67  SER C C   1 
ATOM   4957  O  O   . SER C  1 67  ? 38.903  6.433   -21.567 1.00 20.50  ? 67  SER C O   1 
ATOM   4958  C  CB  . SER C  1 67  ? 37.590  4.827   -24.430 1.00 23.43  ? 67  SER C CB  1 
ATOM   4959  O  OG  . SER C  1 67  ? 38.118  3.458   -24.410 1.00 23.68  ? 67  SER C OG  1 
ATOM   4960  N  N   . VAL C  1 68  ? 39.217  4.250   -22.089 1.00 16.26  ? 68  VAL C N   1 
ATOM   4961  C  CA  . VAL C  1 68  ? 40.613  4.149   -21.591 1.00 21.26  ? 68  VAL C CA  1 
ATOM   4962  C  C   . VAL C  1 68  ? 41.543  3.730   -22.702 1.00 24.13  ? 68  VAL C C   1 
ATOM   4963  O  O   . VAL C  1 68  ? 41.233  2.822   -23.464 1.00 20.24  ? 68  VAL C O   1 
ATOM   4964  C  CB  . VAL C  1 68  ? 40.672  3.208   -20.382 1.00 22.09  ? 68  VAL C CB  1 
ATOM   4965  C  CG1 . VAL C  1 68  ? 40.361  1.786   -20.724 1.00 20.75  ? 68  VAL C CG1 1 
ATOM   4966  C  CG2 . VAL C  1 68  ? 42.069  3.170   -19.798 1.00 28.89  ? 68  VAL C CG2 1 
ATOM   4967  N  N   . LYS C  1 69  ? 42.554  4.567   -22.874 1.00 21.40  ? 69  LYS C N   1 
ATOM   4968  C  CA  . LYS C  1 69  ? 43.482  4.439   -23.998 1.00 17.14  ? 69  LYS C CA  1 
ATOM   4969  C  C   . LYS C  1 69  ? 44.850  4.219   -23.420 1.00 19.19  ? 69  LYS C C   1 
ATOM   4970  O  O   . LYS C  1 69  ? 45.193  4.660   -22.356 1.00 20.75  ? 69  LYS C O   1 
ATOM   4971  C  CB  . LYS C  1 69  ? 43.411  5.578   -25.010 1.00 20.94  ? 69  LYS C CB  1 
ATOM   4972  C  CG  . LYS C  1 69  ? 43.912  6.903   -24.458 1.00 22.32  ? 69  LYS C CG  1 
ATOM   4973  C  CD  . LYS C  1 69  ? 43.978  8.002   -25.529 1.00 23.48  ? 69  LYS C CD  1 
ATOM   4974  C  CE  . LYS C  1 69  ? 44.625  9.207   -24.932 1.00 27.97  ? 69  LYS C CE  1 
ATOM   4975  N  NZ  . LYS C  1 69  ? 44.831  10.331  -25.883 1.00 24.96  ? 69  LYS C NZ  1 
ATOM   4976  N  N   . LEU C  1 70  ? 45.600  3.330   -24.067 1.00 15.47  ? 70  LEU C N   1 
ATOM   4977  C  CA  . LEU C  1 70  ? 46.967  3.132   -23.943 1.00 15.90  ? 70  LEU C CA  1 
ATOM   4978  C  C   . LEU C  1 70  ? 47.796  3.562   -25.088 1.00 18.45  ? 70  LEU C C   1 
ATOM   4979  O  O   . LEU C  1 70  ? 47.598  3.095   -26.226 1.00 18.07  ? 70  LEU C O   1 
ATOM   4980  C  CB  . LEU C  1 70  ? 47.266  1.633   -23.760 1.00 15.65  ? 70  LEU C CB  1 
ATOM   4981  C  CG  . LEU C  1 70  ? 48.688  1.173   -23.408 1.00 20.01  ? 70  LEU C CG  1 
ATOM   4982  C  CD1 . LEU C  1 70  ? 49.091  1.566   -21.977 1.00 25.68  ? 70  LEU C CD1 1 
ATOM   4983  C  CD2 . LEU C  1 70  ? 48.864  -0.334  -23.515 1.00 17.36  ? 70  LEU C CD2 1 
ATOM   4984  N  N   . ASN C  1 71  ? 48.722  4.474   -24.842 1.00 16.96  ? 71  ASN C N   1 
ATOM   4985  C  CA  . ASN C  1 71  ? 49.586  4.998   -25.898 1.00 18.95  ? 71  ASN C CA  1 
ATOM   4986  C  C   . ASN C  1 71  ? 50.488  3.887   -26.275 1.00 15.45  ? 71  ASN C C   1 
ATOM   4987  O  O   . ASN C  1 71  ? 51.021  3.102   -25.451 1.00 24.32  ? 71  ASN C O   1 
ATOM   4988  C  CB  . ASN C  1 71  ? 50.321  6.211   -25.418 1.00 16.73  ? 71  ASN C CB  1 
ATOM   4989  C  CG  . ASN C  1 71  ? 49.440  7.474   -25.289 1.00 22.37  ? 71  ASN C CG  1 
ATOM   4990  O  OD1 . ASN C  1 71  ? 48.226  7.466   -25.566 1.00 19.91  ? 71  ASN C OD1 1 
ATOM   4991  N  ND2 . ASN C  1 71  ? 50.064  8.565   -24.862 1.00 21.87  ? 71  ASN C ND2 1 
ATOM   4992  N  N   . LEU C  1 72  ? 50.784  3.842   -27.580 1.00 17.19  ? 72  LEU C N   1 
ATOM   4993  C  CA  . LEU C  1 72  ? 51.649  2.820   -28.081 1.00 16.62  ? 72  LEU C CA  1 
ATOM   4994  C  C   . LEU C  1 72  ? 52.807  3.447   -28.944 1.00 18.86  ? 72  LEU C C   1 
ATOM   4995  O  O   . LEU C  1 72  ? 52.625  4.501   -29.487 1.00 19.44  ? 72  LEU C O   1 
ATOM   4996  C  CB  . LEU C  1 72  ? 50.910  1.882   -29.078 1.00 19.20  ? 72  LEU C CB  1 
ATOM   4997  C  CG  . LEU C  1 72  ? 49.845  0.968   -28.444 1.00 21.14  ? 72  LEU C CG  1 
ATOM   4998  C  CD1 . LEU C  1 72  ? 49.009  0.271   -29.551 1.00 21.09  ? 72  LEU C CD1 1 
ATOM   4999  C  CD2 . LEU C  1 72  ? 50.429  -0.075  -27.489 1.00 23.27  ? 72  LEU C CD2 1 
ATOM   5000  N  N   . PRO C  1 73  ? 53.999  2.829   -29.032 1.00 20.11  ? 73  PRO C N   1 
ATOM   5001  C  CA  . PRO C  1 73  ? 55.201  3.436   -29.678 1.00 22.31  ? 73  PRO C CA  1 
ATOM   5002  C  C   . PRO C  1 73  ? 55.223  3.328   -31.201 1.00 23.97  ? 73  PRO C C   1 
ATOM   5003  O  O   . PRO C  1 73  ? 54.715  2.350   -31.744 1.00 22.87  ? 73  PRO C O   1 
ATOM   5004  C  CB  . PRO C  1 73  ? 56.356  2.631   -29.104 1.00 23.58  ? 73  PRO C CB  1 
ATOM   5005  C  CG  . PRO C  1 73  ? 55.835  1.265   -28.900 1.00 22.01  ? 73  PRO C CG  1 
ATOM   5006  C  CD  . PRO C  1 73  ? 54.345  1.462   -28.607 1.00 20.93  ? 73  PRO C CD  1 
ATOM   5007  N  N   . SER C  1 74  ? 55.706  4.337   -31.894 1.00 32.27  ? 74  SER C N   1 
ATOM   5008  C  CA  . SER C  1 74  ? 55.543  4.374   -33.363 1.00 26.80  ? 74  SER C CA  1 
ATOM   5009  C  C   . SER C  1 74  ? 56.404  3.326   -34.126 1.00 27.68  ? 74  SER C C   1 
ATOM   5010  O  O   . SER C  1 74  ? 56.169  3.065   -35.283 1.00 32.84  ? 74  SER C O   1 
ATOM   5011  C  CB  . SER C  1 74  ? 55.760  5.789   -33.878 1.00 33.03  ? 74  SER C CB  1 
ATOM   5012  O  OG  . SER C  1 74  ? 57.112  6.227   -33.610 1.00 40.34  ? 74  SER C OG  1 
ATOM   5013  N  N   . ASP C  1 75  ? 57.411  2.721   -33.470 1.00 27.97  ? 75  ASP C N   1 
ATOM   5014  C  CA  . ASP C  1 75  ? 58.171  1.648   -34.119 1.00 28.95  ? 75  ASP C CA  1 
ATOM   5015  C  C   . ASP C  1 75  ? 57.376  0.292   -34.143 1.00 32.54  ? 75  ASP C C   1 
ATOM   5016  O  O   . ASP C  1 75  ? 57.661  -0.646  -34.909 1.00 31.57  ? 75  ASP C O   1 
ATOM   5017  C  CB  . ASP C  1 75  ? 59.510  1.518   -33.462 1.00 25.77  ? 75  ASP C CB  1 
ATOM   5018  C  CG  . ASP C  1 75  ? 59.341  1.017   -32.107 1.00 23.26  ? 75  ASP C CG  1 
ATOM   5019  O  OD1 . ASP C  1 75  ? 59.058  1.904   -31.196 1.00 36.13  ? 75  ASP C OD1 1 
ATOM   5020  O  OD2 . ASP C  1 75  ? 59.374  -0.203  -31.985 1.00 41.64  ? 75  ASP C OD2 1 
ATOM   5021  N  N   . MET C  1 76  ? 56.234  0.259   -33.437 1.00 20.06  ? 76  MET C N   1 
ATOM   5022  C  CA  . MET C  1 76  ? 55.344  -0.871  -33.593 1.00 20.00  ? 76  MET C CA  1 
ATOM   5023  C  C   . MET C  1 76  ? 54.442  -0.624  -34.838 1.00 19.02  ? 76  MET C C   1 
ATOM   5024  O  O   . MET C  1 76  ? 53.946  0.502   -35.031 1.00 19.98  ? 76  MET C O   1 
ATOM   5025  C  CB  . MET C  1 76  ? 54.454  -0.803  -32.400 1.00 20.07  ? 76  MET C CB  1 
ATOM   5026  C  CG  . MET C  1 76  ? 53.353  -1.762  -32.409 1.00 20.44  ? 76  MET C CG  1 
ATOM   5027  S  SD  . MET C  1 76  ? 52.467  -1.702  -30.783 1.00 21.98  ? 76  MET C SD  1 
ATOM   5028  C  CE  . MET C  1 76  ? 50.916  -2.353  -31.292 1.00 20.83  ? 76  MET C CE  1 
ATOM   5029  N  N   . HIS C  1 77  ? 54.303  -1.655  -35.709 1.00 18.17  ? 77  HIS C N   1 
ATOM   5030  C  CA  . HIS C  1 77  ? 53.671  -1.422  -37.024 1.00 19.51  ? 77  HIS C CA  1 
ATOM   5031  C  C   . HIS C  1 77  ? 53.118  -2.659  -37.651 1.00 18.44  ? 77  HIS C C   1 
ATOM   5032  O  O   . HIS C  1 77  ? 53.399  -3.786  -37.256 1.00 19.24  ? 77  HIS C O   1 
ATOM   5033  C  CB  . HIS C  1 77  ? 54.578  -0.627  -37.952 1.00 20.77  ? 77  HIS C CB  1 
ATOM   5034  C  CG  . HIS C  1 77  ? 55.750  -1.371  -38.420 1.00 19.21  ? 77  HIS C CG  1 
ATOM   5035  N  ND1 . HIS C  1 77  ? 56.917  -1.276  -37.847 1.00 22.32  ? 77  HIS C ND1 1 
ATOM   5036  C  CD2 . HIS C  1 77  ? 55.904  -2.178  -39.516 1.00 18.61  ? 77  HIS C CD2 1 
ATOM   5037  C  CE1 . HIS C  1 77  ? 57.807  -2.002  -38.534 1.00 22.36  ? 77  HIS C CE1 1 
ATOM   5038  N  NE2 . HIS C  1 77  ? 57.186  -2.600  -39.526 1.00 26.12  ? 77  HIS C NE2 1 
ATOM   5039  N  N   . ILE C  1 78  ? 52.152  -2.437  -38.516 1.00 17.69  ? 78  ILE C N   1 
ATOM   5040  C  CA  . ILE C  1 78  ? 51.621  -3.465  -39.374 1.00 15.73  ? 78  ILE C CA  1 
ATOM   5041  C  C   . ILE C  1 78  ? 52.368  -3.487  -40.701 1.00 18.35  ? 78  ILE C C   1 
ATOM   5042  O  O   . ILE C  1 78  ? 52.561  -2.435  -41.294 1.00 18.54  ? 78  ILE C O   1 
ATOM   5043  C  CB  . ILE C  1 78  ? 50.127  -3.220  -39.757 1.00 17.22  ? 78  ILE C CB  1 
ATOM   5044  C  CG1 . ILE C  1 78  ? 49.223  -3.163  -38.525 1.00 19.71  ? 78  ILE C CG1 1 
ATOM   5045  C  CG2 . ILE C  1 78  ? 49.678  -4.176  -40.823 1.00 19.79  ? 78  ILE C CG2 1 
ATOM   5046  C  CD1 . ILE C  1 78  ? 47.840  -2.485  -38.745 1.00 17.74  ? 78  ILE C CD1 1 
ATOM   5047  N  N   . GLN C  1 79  ? 52.753  -4.675  -41.145 1.00 20.22  ? 79  GLN C N   1 
ATOM   5048  C  CA  . GLN C  1 79  ? 53.396  -4.844  -42.443 1.00 22.93  ? 79  GLN C CA  1 
ATOM   5049  C  C   . GLN C  1 79  ? 52.402  -5.707  -43.275 1.00 21.04  ? 79  GLN C C   1 
ATOM   5050  O  O   . GLN C  1 79  ? 51.709  -6.613  -42.716 1.00 24.22  ? 79  GLN C O   1 
ATOM   5051  C  CB  . GLN C  1 79  ? 54.752  -5.501  -42.297 1.00 30.42  ? 79  GLN C CB  1 
ATOM   5052  N  N   . GLY C  1 80  ? 52.239  -5.391  -44.541 1.00 23.95  ? 80  GLY C N   1 
ATOM   5053  C  CA  . GLY C  1 80  ? 51.331  -6.111  -45.358 1.00 26.16  ? 80  GLY C CA  1 
ATOM   5054  C  C   . GLY C  1 80  ? 50.294  -5.248  -46.060 1.00 24.28  ? 80  GLY C C   1 
ATOM   5055  O  O   . GLY C  1 80  ? 49.645  -5.733  -46.994 1.00 25.76  ? 80  GLY C O   1 
ATOM   5056  N  N   . LEU C  1 81  ? 50.061  -4.028  -45.577 1.00 19.94  ? 81  LEU C N   1 
ATOM   5057  C  CA  . LEU C  1 81  ? 49.092  -3.118  -46.222 1.00 19.32  ? 81  LEU C CA  1 
ATOM   5058  C  C   . LEU C  1 81  ? 49.832  -2.313  -47.314 1.00 18.45  ? 81  LEU C C   1 
ATOM   5059  O  O   . LEU C  1 81  ? 51.067  -2.484  -47.500 1.00 23.27  ? 81  LEU C O   1 
ATOM   5060  C  CB  . LEU C  1 81  ? 48.470  -2.195  -45.220 1.00 17.22  ? 81  LEU C CB  1 
ATOM   5061  C  CG  . LEU C  1 81  ? 47.596  -2.939  -44.148 1.00 17.66  ? 81  LEU C CG  1 
ATOM   5062  C  CD1 . LEU C  1 81  ? 47.126  -2.009  -43.074 1.00 20.49  ? 81  LEU C CD1 1 
ATOM   5063  C  CD2 . LEU C  1 81  ? 46.384  -3.549  -44.810 1.00 19.68  ? 81  LEU C CD2 1 
ATOM   5064  N  N   . GLN C  1 82  ? 49.119  -1.429  -48.024 1.00 19.82  ? 82  GLN C N   1 
ATOM   5065  C  CA  . GLN C  1 82  ? 49.711  -0.727  -49.181 1.00 23.92  ? 82  GLN C CA  1 
ATOM   5066  C  C   . GLN C  1 82  ? 50.768  0.312   -48.711 1.00 21.26  ? 82  GLN C C   1 
ATOM   5067  O  O   . GLN C  1 82  ? 51.578  0.776   -49.492 1.00 28.26  ? 82  GLN C O   1 
ATOM   5068  C  CB  . GLN C  1 82  ? 48.629  0.010   -50.021 1.00 30.19  ? 82  GLN C CB  1 
ATOM   5069  N  N   . SER C  1 83  ? 50.705  0.721   -47.445 1.00 17.52  ? 83  SER C N   1 
ATOM   5070  C  CA  . SER C  1 83  ? 51.651  1.605   -46.739 1.00 16.72  ? 83  SER C CA  1 
ATOM   5071  C  C   . SER C  1 83  ? 51.984  0.988   -45.430 1.00 15.35  ? 83  SER C C   1 
ATOM   5072  O  O   . SER C  1 83  ? 51.221  0.165   -44.929 1.00 14.01  ? 83  SER C O   1 
ATOM   5073  C  CB  . SER C  1 83  ? 51.058  2.969   -46.437 1.00 19.88  ? 83  SER C CB  1 
ATOM   5074  O  OG  . SER C  1 83  ? 50.799  3.778   -47.550 1.00 24.23  ? 83  SER C OG  1 
ATOM   5075  N  N   . ARG C  1 84  ? 53.076  1.462   -44.795 1.00 14.61  ? 84  ARG C N   1 
ATOM   5076  C  CA  . ARG C  1 84  ? 53.321  1.083   -43.444 1.00 14.53  ? 84  ARG C CA  1 
ATOM   5077  C  C   . ARG C  1 84  ? 52.392  1.825   -42.524 1.00 13.43  ? 84  ARG C C   1 
ATOM   5078  O  O   . ARG C  1 84  ? 52.247  3.011   -42.653 1.00 14.63  ? 84  ARG C O   1 
ATOM   5079  C  CB  . ARG C  1 84  ? 54.771  1.374   -43.030 1.00 17.80  ? 84  ARG C CB  1 
ATOM   5080  C  CG  . ARG C  1 84  ? 54.961  1.039   -41.545 1.00 16.90  ? 84  ARG C CG  1 
ATOM   5081  C  CD  . ARG C  1 84  ? 56.373  1.241   -41.059 1.00 19.13  ? 84  ARG C CD  1 
ATOM   5082  N  NE  . ARG C  1 84  ? 57.247  0.215   -41.598 1.00 18.23  ? 84  ARG C NE  1 
ATOM   5083  C  CZ  . ARG C  1 84  ? 58.546  0.118   -41.274 1.00 19.15  ? 84  ARG C CZ  1 
ATOM   5084  N  NH1 . ARG C  1 84  ? 59.082  1.023   -40.506 1.00 23.18  ? 84  ARG C NH1 1 
ATOM   5085  N  NH2 . ARG C  1 84  ? 59.294  -0.838  -41.779 1.00 21.62  ? 84  ARG C NH2 1 
ATOM   5086  N  N   . TYR C  1 85  ? 51.721  1.125   -41.588 1.00 14.46  ? 85  TYR C N   1 
ATOM   5087  C  CA  . TYR C  1 85  ? 50.858  1.787   -40.560 1.00 13.94  ? 85  TYR C CA  1 
ATOM   5088  C  C   . TYR C  1 85  ? 51.461  1.534   -39.208 1.00 14.52  ? 85  TYR C C   1 
ATOM   5089  O  O   . TYR C  1 85  ? 51.665  0.409   -38.816 1.00 16.99  ? 85  TYR C O   1 
ATOM   5090  C  CB  . TYR C  1 85  ? 49.428  1.230   -40.604 1.00 14.99  ? 85  TYR C CB  1 
ATOM   5091  C  CG  . TYR C  1 85  ? 48.686  1.797   -41.802 1.00 12.02  ? 85  TYR C CG  1 
ATOM   5092  C  CD1 . TYR C  1 85  ? 47.869  2.893   -41.670 1.00 13.00  ? 85  TYR C CD1 1 
ATOM   5093  C  CD2 . TYR C  1 85  ? 48.776  1.157   -43.063 1.00 12.57  ? 85  TYR C CD2 1 
ATOM   5094  C  CE1 . TYR C  1 85  ? 47.180  3.424   -42.784 1.00 12.84  ? 85  TYR C CE1 1 
ATOM   5095  C  CE2 . TYR C  1 85  ? 48.038  1.642   -44.151 1.00 12.91  ? 85  TYR C CE2 1 
ATOM   5096  C  CZ  . TYR C  1 85  ? 47.270  2.775   -44.000 1.00 12.68  ? 85  TYR C CZ  1 
ATOM   5097  O  OH  . TYR C  1 85  ? 46.558  3.309   -45.036 1.00 15.60  ? 85  TYR C OH  1 
ATOM   5098  N  N   . SER C  1 86  ? 51.862  2.595   -38.513 1.00 14.88  ? 86  SER C N   1 
ATOM   5099  C  CA  . SER C  1 86  ? 52.539  2.497   -37.237 1.00 15.88  ? 86  SER C CA  1 
ATOM   5100  C  C   . SER C  1 86  ? 51.539  2.741   -36.121 1.00 14.25  ? 86  SER C C   1 
ATOM   5101  O  O   . SER C  1 86  ? 50.628  3.549   -36.218 1.00 14.99  ? 86  SER C O   1 
ATOM   5102  C  CB  . SER C  1 86  ? 53.657  3.547   -37.205 1.00 19.99  ? 86  SER C CB  1 
ATOM   5103  O  OG  . SER C  1 86  ? 54.642  3.235   -38.190 1.00 20.48  ? 86  SER C OG  1 
ATOM   5104  N  N   . ALA C  1 87  ? 51.784  2.050   -35.013 1.00 17.18  ? 87  ALA C N   1 
ATOM   5105  C  CA  . ALA C  1 87  ? 50.845  2.234   -33.843 1.00 14.35  ? 87  ALA C CA  1 
ATOM   5106  C  C   . ALA C  1 87  ? 50.791  3.614   -33.192 1.00 16.76  ? 87  ALA C C   1 
ATOM   5107  O  O   . ALA C  1 87  ? 51.847  4.306   -33.164 1.00 17.35  ? 87  ALA C O   1 
ATOM   5108  C  CB  . ALA C  1 87  ? 51.112  1.133   -32.792 1.00 20.03  ? 87  ALA C CB  1 
ATOM   5109  N  N   . THR C  1 88  ? 49.609  3.975   -32.680 1.00 14.45  ? 88  THR C N   1 
ATOM   5110  C  CA  . THR C  1 88  ? 49.471  5.196   -31.883 1.00 16.25  ? 88  THR C CA  1 
ATOM   5111  C  C   . THR C  1 88  ? 48.822  4.957   -30.537 1.00 14.11  ? 88  THR C C   1 
ATOM   5112  O  O   . THR C  1 88  ? 49.282  5.489   -29.528 1.00 16.35  ? 88  THR C O   1 
ATOM   5113  C  CB  . THR C  1 88  ? 48.879  6.370   -32.635 1.00 15.18  ? 88  THR C CB  1 
ATOM   5114  O  OG1 . THR C  1 88  ? 48.756  7.503   -31.764 1.00 18.27  ? 88  THR C OG1 1 
ATOM   5115  C  CG2 . THR C  1 88  ? 47.485  6.055   -33.182 1.00 15.65  ? 88  THR C CG2 1 
ATOM   5116  N  N   . GLN C  1 89  ? 47.795  4.126   -30.507 1.00 16.02  ? 89  GLN C N   1 
ATOM   5117  C  CA  . GLN C  1 89  ? 47.168  3.787   -29.218 1.00 15.10  ? 89  GLN C CA  1 
ATOM   5118  C  C   . GLN C  1 89  ? 46.169  2.658   -29.379 1.00 16.19  ? 89  GLN C C   1 
ATOM   5119  O  O   . GLN C  1 89  ? 45.752  2.420   -30.512 1.00 14.72  ? 89  GLN C O   1 
ATOM   5120  C  CB  . GLN C  1 89  ? 46.444  5.009   -28.645 1.00 18.18  ? 89  GLN C CB  1 
ATOM   5121  C  CG  . GLN C  1 89  ? 45.423  5.627   -29.592 1.00 18.65  ? 89  GLN C CG  1 
ATOM   5122  C  CD  . GLN C  1 89  ? 43.986  5.411   -29.147 1.00 15.73  ? 89  GLN C CD  1 
ATOM   5123  O  OE1 . GLN C  1 89  ? 43.545  4.278   -28.955 1.00 20.12  ? 89  GLN C OE1 1 
ATOM   5124  N  NE2 . GLN C  1 89  ? 43.245  6.503   -28.991 1.00 28.57  ? 89  GLN C NE2 1 
ATOM   5125  N  N   . LEU C  1 90  ? 45.790  2.002   -28.264 1.00 16.67  ? 90  LEU C N   1 
ATOM   5126  C  CA  . LEU C  1 90  ? 44.664  1.172   -28.282 1.00 14.58  ? 90  LEU C CA  1 
ATOM   5127  C  C   . LEU C  1 90  ? 43.660  1.589   -27.249 1.00 14.75  ? 90  LEU C C   1 
ATOM   5128  O  O   . LEU C  1 90  ? 44.011  2.310   -26.272 1.00 16.98  ? 90  LEU C O   1 
ATOM   5129  C  CB  . LEU C  1 90  ? 45.102  -0.250  -28.159 1.00 13.39  ? 90  LEU C CB  1 
ATOM   5130  C  CG  . LEU C  1 90  ? 45.848  -0.614  -26.828 1.00 16.02  ? 90  LEU C CG  1 
ATOM   5131  C  CD1 . LEU C  1 90  ? 44.980  -0.785  -25.603 1.00 19.99  ? 90  LEU C CD1 1 
ATOM   5132  C  CD2 . LEU C  1 90  ? 46.416  -1.933  -27.056 1.00 16.67  ? 90  LEU C CD2 1 
ATOM   5133  N  N   . HIS C  1 91  ? 42.486  1.062   -27.375 1.00 16.26  ? 91  HIS C N   1 
ATOM   5134  C  CA  . HIS C  1 91  ? 41.395  1.476   -26.438 1.00 13.44  ? 91  HIS C CA  1 
ATOM   5135  C  C   . HIS C  1 91  ? 40.319  0.365   -26.625 1.00 15.98  ? 91  HIS C C   1 
ATOM   5136  O  O   . HIS C  1 91  ? 40.381  -0.514  -27.507 1.00 16.32  ? 91  HIS C O   1 
ATOM   5137  C  CB  . HIS C  1 91  ? 40.952  2.884   -26.662 1.00 15.19  ? 91  HIS C CB  1 
ATOM   5138  C  CG  . HIS C  1 91  ? 40.352  3.012   -28.007 1.00 15.15  ? 91  HIS C CG  1 
ATOM   5139  N  ND1 . HIS C  1 91  ? 41.073  3.456   -29.076 1.00 14.85  ? 91  HIS C ND1 1 
ATOM   5140  C  CD2 . HIS C  1 91  ? 39.135  2.629   -28.484 1.00 13.24  ? 91  HIS C CD2 1 
ATOM   5141  C  CE1 . HIS C  1 91  ? 40.276  3.361   -30.148 1.00 13.70  ? 91  HIS C CE1 1 
ATOM   5142  N  NE2 . HIS C  1 91  ? 39.134  2.841   -29.807 1.00 12.99  ? 91  HIS C NE2 1 
ATOM   5143  N  N   . LEU C  1 92  ? 39.320  0.431   -25.762 1.00 14.99  ? 92  LEU C N   1 
ATOM   5144  C  CA  . LEU C  1 92  ? 38.215  -0.523  -25.819 1.00 16.01  ? 92  LEU C CA  1 
ATOM   5145  C  C   . LEU C  1 92  ? 36.867  0.160   -25.782 1.00 13.53  ? 92  LEU C C   1 
ATOM   5146  O  O   . LEU C  1 92  ? 36.748  1.377   -25.495 1.00 16.54  ? 92  LEU C O   1 
ATOM   5147  C  CB  . LEU C  1 92  ? 38.271  -1.465  -24.550 1.00 20.34  ? 92  LEU C CB  1 
ATOM   5148  C  CG  . LEU C  1 92  ? 39.502  -2.347  -24.542 1.00 19.12  ? 92  LEU C CG  1 
ATOM   5149  C  CD1 . LEU C  1 92  ? 40.674  -1.867  -23.732 1.00 26.80  ? 92  LEU C CD1 1 
ATOM   5150  C  CD2 . LEU C  1 92  ? 39.215  -3.784  -24.277 1.00 20.84  ? 92  LEU C CD2 1 
ATOM   5151  N  N   . HIS C  1 93  ? 35.890  -0.660  -26.171 1.00 14.51  ? 93  HIS C N   1 
ATOM   5152  C  CA  . HIS C  1 93  ? 34.486  -0.214  -26.120 1.00 14.43  ? 93  HIS C CA  1 
ATOM   5153  C  C   . HIS C  1 93  ? 33.735  -1.342  -25.467 1.00 13.13  ? 93  HIS C C   1 
ATOM   5154  O  O   . HIS C  1 93  ? 33.923  -2.544  -25.735 1.00 14.91  ? 93  HIS C O   1 
ATOM   5155  C  CB  . HIS C  1 93  ? 33.896  -0.003  -27.539 1.00 13.24  ? 93  HIS C CB  1 
ATOM   5156  C  CG  . HIS C  1 93  ? 34.666  1.044   -28.333 1.00 11.76  ? 93  HIS C CG  1 
ATOM   5157  N  ND1 . HIS C  1 93  ? 34.364  2.377   -28.329 1.00 13.74  ? 93  HIS C ND1 1 
ATOM   5158  C  CD2 . HIS C  1 93  ? 35.776  0.879   -29.164 1.00 11.65  ? 93  HIS C CD2 1 
ATOM   5159  C  CE1 . HIS C  1 93  ? 35.239  3.004   -29.148 1.00 12.52  ? 93  HIS C CE1 1 
ATOM   5160  N  NE2 . HIS C  1 93  ? 36.091  2.097   -29.666 1.00 12.05  ? 93  HIS C NE2 1 
ATOM   5161  N  N   . TRP C  1 94  ? 32.778  -0.992  -24.621 1.00 13.01  ? 94  TRP C N   1 
ATOM   5162  C  CA  . TRP C  1 94  ? 32.013  -2.064  -23.899 1.00 14.49  ? 94  TRP C CA  1 
ATOM   5163  C  C   . TRP C  1 94  ? 30.615  -1.575  -23.546 1.00 15.93  ? 94  TRP C C   1 
ATOM   5164  O  O   . TRP C  1 94  ? 30.246  -0.439  -23.785 1.00 13.72  ? 94  TRP C O   1 
ATOM   5165  C  CB  . TRP C  1 94  ? 32.787  -2.469  -22.647 1.00 17.66  ? 94  TRP C CB  1 
ATOM   5166  C  CG  . TRP C  1 94  ? 33.051  -1.375  -21.686 1.00 17.70  ? 94  TRP C CG  1 
ATOM   5167  C  CD1 . TRP C  1 94  ? 32.208  -0.914  -20.705 1.00 17.94  ? 94  TRP C CD1 1 
ATOM   5168  C  CD2 . TRP C  1 94  ? 34.246  -0.550  -21.622 1.00 19.55  ? 94  TRP C CD2 1 
ATOM   5169  N  NE1 . TRP C  1 94  ? 32.813  0.143   -20.046 1.00 19.30  ? 94  TRP C NE1 1 
ATOM   5170  C  CE2 . TRP C  1 94  ? 34.026  0.419   -20.573 1.00 19.73  ? 94  TRP C CE2 1 
ATOM   5171  C  CE3 . TRP C  1 94  ? 35.392  -0.446  -22.398 1.00 17.97  ? 94  TRP C CE3 1 
ATOM   5172  C  CZ2 . TRP C  1 94  ? 34.984  1.373   -20.223 1.00 20.79  ? 94  TRP C CZ2 1 
ATOM   5173  C  CZ3 . TRP C  1 94  ? 36.341  0.496   -22.073 1.00 19.87  ? 94  TRP C CZ3 1 
ATOM   5174  C  CH2 . TRP C  1 94  ? 36.142  1.393   -21.018 1.00 20.95  ? 94  TRP C CH2 1 
ATOM   5175  N  N   . GLY C  1 95  ? 29.852  -2.502  -22.988 1.00 13.58  ? 95  GLY C N   1 
ATOM   5176  C  CA  . GLY C  1 95  ? 28.473  -2.244  -22.638 1.00 14.74  ? 95  GLY C CA  1 
ATOM   5177  C  C   . GLY C  1 95  ? 28.277  -1.917  -21.163 1.00 15.00  ? 95  GLY C C   1 
ATOM   5178  O  O   . GLY C  1 95  ? 28.888  -1.000  -20.619 1.00 16.99  ? 95  GLY C O   1 
ATOM   5179  N  N   . ASN C  1 96  ? 27.422  -2.666  -20.490 1.00 17.38  ? 96  ASN C N   1 
ATOM   5180  C  CA  . ASN C  1 96  ? 27.245  -2.474  -19.062 1.00 18.42  ? 96  ASN C CA  1 
ATOM   5181  C  C   . ASN C  1 96  ? 26.781  -3.783  -18.470 1.00 17.74  ? 96  ASN C C   1 
ATOM   5182  O  O   . ASN C  1 96  ? 26.404  -4.704  -19.172 1.00 17.50  ? 96  ASN C O   1 
ATOM   5183  C  CB  . ASN C  1 96  ? 26.223  -1.322  -18.824 1.00 20.69  ? 96  ASN C CB  1 
ATOM   5184  C  CG  . ASN C  1 96  ? 24.793  -1.744  -19.152 1.00 22.88  ? 96  ASN C CG  1 
ATOM   5185  O  OD1 . ASN C  1 96  ? 24.154  -2.298  -18.328 1.00 27.20  ? 96  ASN C OD1 1 
ATOM   5186  N  ND2 . ASN C  1 96  ? 24.329  -1.498  -20.386 1.00 23.51  ? 96  ASN C ND2 1 
ATOM   5187  N  N   . PRO C  1 97  ? 26.785  -3.917  -17.125 1.00 22.02  ? 97  PRO C N   1 
ATOM   5188  C  CA  . PRO C  1 97  ? 26.481  -5.230  -16.541 1.00 23.74  ? 97  PRO C CA  1 
ATOM   5189  C  C   . PRO C  1 97  ? 25.082  -5.761  -16.828 1.00 19.92  ? 97  PRO C C   1 
ATOM   5190  O  O   . PRO C  1 97  ? 24.866  -6.993  -16.916 1.00 22.01  ? 97  PRO C O   1 
ATOM   5191  C  CB  . PRO C  1 97  ? 26.704  -4.984  -15.031 1.00 28.13  ? 97  PRO C CB  1 
ATOM   5192  C  CG  . PRO C  1 97  ? 27.793  -3.973  -15.057 1.00 25.30  ? 97  PRO C CG  1 
ATOM   5193  C  CD  . PRO C  1 97  ? 27.438  -3.025  -16.172 1.00 23.22  ? 97  PRO C CD  1 
ATOM   5194  N  N   . ASN C  1 98  ? 24.127  -4.864  -16.960 1.00 20.48  ? 98  ASN C N   1 
ATOM   5195  C  CA  . ASN C  1 98  ? 22.755  -5.275  -17.307 1.00 23.31  ? 98  ASN C CA  1 
ATOM   5196  C  C   . ASN C  1 98  ? 22.530  -5.590  -18.753 1.00 19.78  ? 98  ASN C C   1 
ATOM   5197  O  O   . ASN C  1 98  ? 21.519  -6.164  -19.092 1.00 23.72  ? 98  ASN C O   1 
ATOM   5198  C  CB  . ASN C  1 98  ? 21.756  -4.188  -16.922 1.00 24.23  ? 98  ASN C CB  1 
ATOM   5199  C  CG  . ASN C  1 98  ? 21.680  -3.979  -15.437 1.00 42.26  ? 98  ASN C CG  1 
ATOM   5200  O  OD1 . ASN C  1 98  ? 21.641  -4.932  -14.679 1.00 44.08  ? 98  ASN C OD1 1 
ATOM   5201  N  ND2 . ASN C  1 98  ? 21.706  -2.719  -15.003 1.00 61.07  ? 98  ASN C ND2 1 
ATOM   5202  N  N   . ASP C  1 99  ? 23.464  -5.228  -19.622 1.00 20.33  ? 99  ASP C N   1 
ATOM   5203  C  CA  . ASP C  1 99  ? 23.356  -5.493  -21.062 1.00 17.70  ? 99  ASP C CA  1 
ATOM   5204  C  C   . ASP C  1 99  ? 24.786  -5.542  -21.583 1.00 15.80  ? 99  ASP C C   1 
ATOM   5205  O  O   . ASP C  1 99  ? 25.280  -4.558  -22.169 1.00 18.76  ? 99  ASP C O   1 
ATOM   5206  C  CB  . ASP C  1 99  ? 22.516  -4.384  -21.661 1.00 17.85  ? 99  ASP C CB  1 
ATOM   5207  C  CG  . ASP C  1 99  ? 21.942  -4.738  -23.026 1.00 19.93  ? 99  ASP C CG  1 
ATOM   5208  O  OD1 . ASP C  1 99  ? 22.348  -5.714  -23.597 1.00 23.59  ? 99  ASP C OD1 1 
ATOM   5209  O  OD2 . ASP C  1 99  ? 21.106  -4.022  -23.529 1.00 23.94  ? 99  ASP C OD2 1 
ATOM   5210  N  N   . PRO C  1 100 ? 25.446  -6.675  -21.369 1.00 17.07  ? 100 PRO C N   1 
ATOM   5211  C  CA  . PRO C  1 100 ? 26.894  -6.733  -21.592 1.00 20.62  ? 100 PRO C CA  1 
ATOM   5212  C  C   . PRO C  1 100 ? 27.162  -7.089  -23.031 1.00 16.82  ? 100 PRO C C   1 
ATOM   5213  O  O   . PRO C  1 100 ? 27.753  -8.096  -23.343 1.00 18.37  ? 100 PRO C O   1 
ATOM   5214  C  CB  . PRO C  1 100 ? 27.340  -7.873  -20.623 1.00 19.12  ? 100 PRO C CB  1 
ATOM   5215  C  CG  . PRO C  1 100 ? 26.196  -8.787  -20.604 1.00 21.28  ? 100 PRO C CG  1 
ATOM   5216  C  CD  . PRO C  1 100 ? 24.983  -7.887  -20.668 1.00 17.15  ? 100 PRO C CD  1 
ATOM   5217  N  N   . HIS C  1 101 ? 26.776  -6.110  -23.924 1.00 14.69  ? 101 HIS C N   1 
ATOM   5218  C  CA  . HIS C  1 101 ? 26.860  -6.321  -25.369 1.00 15.36  ? 101 HIS C CA  1 
ATOM   5219  C  C   . HIS C  1 101 ? 27.289  -5.079  -26.065 1.00 17.03  ? 101 HIS C C   1 
ATOM   5220  O  O   . HIS C  1 101 ? 26.524  -4.511  -26.840 1.00 18.51  ? 101 HIS C O   1 
ATOM   5221  C  CB  . HIS C  1 101 ? 25.520  -6.849  -25.893 1.00 18.48  ? 101 HIS C CB  1 
ATOM   5222  C  CG  . HIS C  1 101 ? 24.996  -7.977  -25.171 1.00 18.41  ? 101 HIS C CG  1 
ATOM   5223  N  ND1 . HIS C  1 101 ? 25.463  -9.251  -25.271 1.00 19.72  ? 101 HIS C ND1 1 
ATOM   5224  C  CD2 . HIS C  1 101 ? 24.010  -8.001  -24.233 1.00 19.24  ? 101 HIS C CD2 1 
ATOM   5225  C  CE1 . HIS C  1 101 ? 24.781  -10.031 -24.451 1.00 20.58  ? 101 HIS C CE1 1 
ATOM   5226  N  NE2 . HIS C  1 101 ? 23.894  -9.260  -23.828 1.00 18.20  ? 101 HIS C NE2 1 
ATOM   5227  N  N   . GLY C  1 102 ? 28.514  -4.642  -25.853 1.00 13.85  ? 102 GLY C N   1 
ATOM   5228  C  CA  . GLY C  1 102 ? 28.936  -3.340  -26.237 1.00 13.38  ? 102 GLY C CA  1 
ATOM   5229  C  C   . GLY C  1 102 ? 30.053  -3.278  -27.235 1.00 11.34  ? 102 GLY C C   1 
ATOM   5230  O  O   . GLY C  1 102 ? 30.759  -2.268  -27.313 1.00 13.54  ? 102 GLY C O   1 
ATOM   5231  N  N   . SER C  1 103 ? 30.152  -4.294  -28.100 1.00 11.81  ? 103 SER C N   1 
ATOM   5232  C  CA  . SER C  1 103 ? 31.022  -4.123  -29.254 1.00 12.27  ? 103 SER C CA  1 
ATOM   5233  C  C   . SER C  1 103 ? 30.496  -3.049  -30.166 1.00 10.70  ? 103 SER C C   1 
ATOM   5234  O  O   . SER C  1 103 ? 29.291  -2.668  -30.059 1.00 11.74  ? 103 SER C O   1 
ATOM   5235  C  CB  . SER C  1 103 ? 31.157  -5.403  -30.044 1.00 11.78  ? 103 SER C CB  1 
ATOM   5236  O  OG  . SER C  1 103 ? 29.963  -5.865  -30.633 1.00 11.05  ? 103 SER C OG  1 
ATOM   5237  N  N   . GLU C  1 104 ? 31.347  -2.531  -31.032 1.00 9.44   ? 104 GLU C N   1 
ATOM   5238  C  CA  . GLU C  1 104 ? 30.905  -1.562  -32.039 1.00 9.41   ? 104 GLU C CA  1 
ATOM   5239  C  C   . GLU C  1 104 ? 30.392  -2.273  -33.290 1.00 8.47   ? 104 GLU C C   1 
ATOM   5240  O  O   . GLU C  1 104 ? 29.264  -2.050  -33.712 1.00 8.60   ? 104 GLU C O   1 
ATOM   5241  C  CB  . GLU C  1 104 ? 32.040  -0.619  -32.336 1.00 10.71  ? 104 GLU C CB  1 
ATOM   5242  C  CG  . GLU C  1 104 ? 32.601  0.118   -31.108 1.00 11.76  ? 104 GLU C CG  1 
ATOM   5243  C  CD  . GLU C  1 104 ? 32.947  1.546   -31.389 1.00 10.31  ? 104 GLU C CD  1 
ATOM   5244  O  OE1 . GLU C  1 104 ? 33.999  1.719   -32.020 1.00 10.30  ? 104 GLU C OE1 1 
ATOM   5245  O  OE2 . GLU C  1 104 ? 32.155  2.466   -31.101 1.00 11.85  ? 104 GLU C OE2 1 
ATOM   5246  N  N   . HIS C  1 105 ? 31.259  -3.082  -33.900 1.00 8.40   ? 105 HIS C N   1 
ATOM   5247  C  CA  . HIS C  1 105 ? 30.785  -3.937  -35.020 1.00 7.79   ? 105 HIS C CA  1 
ATOM   5248  C  C   . HIS C  1 105 ? 29.869  -5.016  -34.477 1.00 8.06   ? 105 HIS C C   1 
ATOM   5249  O  O   . HIS C  1 105 ? 30.028  -5.494  -33.353 1.00 10.20  ? 105 HIS C O   1 
ATOM   5250  C  CB  . HIS C  1 105 ? 31.976  -4.515  -35.740 1.00 8.82   ? 105 HIS C CB  1 
ATOM   5251  C  CG  . HIS C  1 105 ? 32.803  -3.479  -36.438 1.00 7.94   ? 105 HIS C CG  1 
ATOM   5252  N  ND1 . HIS C  1 105 ? 33.832  -2.805  -35.860 1.00 8.92   ? 105 HIS C ND1 1 
ATOM   5253  C  CD2 . HIS C  1 105 ? 32.639  -2.962  -37.700 1.00 8.04   ? 105 HIS C CD2 1 
ATOM   5254  C  CE1 . HIS C  1 105 ? 34.281  -1.861  -36.778 1.00 9.20   ? 105 HIS C CE1 1 
ATOM   5255  N  NE2 . HIS C  1 105 ? 33.552  -1.983  -37.898 1.00 8.49   ? 105 HIS C NE2 1 
ATOM   5256  N  N   . THR C  1 106 ? 28.933  -5.416  -35.320 1.00 7.92   ? 106 THR C N   1 
ATOM   5257  C  CA  . THR C  1 106 ? 28.053  -6.552  -35.057 1.00 8.80   ? 106 THR C CA  1 
ATOM   5258  C  C   . THR C  1 106 ? 28.248  -7.570  -36.153 1.00 8.33   ? 106 THR C C   1 
ATOM   5259  O  O   . THR C  1 106 ? 28.760  -7.259  -37.234 1.00 8.70   ? 106 THR C O   1 
ATOM   5260  C  CB  . THR C  1 106 ? 26.592  -6.109  -34.926 1.00 9.57   ? 106 THR C CB  1 
ATOM   5261  O  OG1 . THR C  1 106 ? 26.161  -5.501  -36.151 1.00 9.00   ? 106 THR C OG1 1 
ATOM   5262  C  CG2 . THR C  1 106 ? 26.405  -5.122  -33.816 1.00 11.39  ? 106 THR C CG2 1 
ATOM   5263  N  N   . VAL C  1 107 ? 27.891  -8.819  -35.842 1.00 9.35   ? 107 VAL C N   1 
ATOM   5264  C  CA  . VAL C  1 107 ? 27.988  -9.884  -36.832 1.00 9.25   ? 107 VAL C CA  1 
ATOM   5265  C  C   . VAL C  1 107 ? 26.604  -10.512 -36.923 1.00 9.06   ? 107 VAL C C   1 
ATOM   5266  O  O   . VAL C  1 107 ? 26.067  -10.953 -35.897 1.00 10.79  ? 107 VAL C O   1 
ATOM   5267  C  CB  . VAL C  1 107 ? 29.065  -10.940 -36.475 1.00 11.08  ? 107 VAL C CB  1 
ATOM   5268  C  CG1 . VAL C  1 107 ? 29.028  -12.081 -37.473 1.00 13.18  ? 107 VAL C CG1 1 
ATOM   5269  C  CG2 . VAL C  1 107 ? 30.424  -10.337 -36.369 1.00 12.98  ? 107 VAL C CG2 1 
ATOM   5270  N  N   . SER C  1 108 ? 25.979  -10.442 -38.086 1.00 10.21  ? 108 SER C N   1 
ATOM   5271  C  CA  . SER C  1 108 ? 24.631  -10.926 -38.243 1.00 11.52  ? 108 SER C CA  1 
ATOM   5272  C  C   . SER C  1 108 ? 23.679  -10.321 -37.213 1.00 10.40  ? 108 SER C C   1 
ATOM   5273  O  O   . SER C  1 108 ? 22.815  -11.022 -36.664 1.00 12.60  ? 108 SER C O   1 
ATOM   5274  C  CB  . SER C  1 108 ? 24.595  -12.476 -38.229 1.00 14.31  ? 108 SER C CB  1 
ATOM   5275  O  OG  . SER C  1 108 ? 25.496  -12.976 -39.215 1.00 19.82  ? 108 SER C OG  1 
ATOM   5276  N  N   . GLY C  1 109 ? 23.891  -9.029  -36.993 1.00 10.11  ? 109 GLY C N   1 
ATOM   5277  C  CA  . GLY C  1 109 ? 23.056  -8.280  -36.122 1.00 10.95  ? 109 GLY C CA  1 
ATOM   5278  C  C   . GLY C  1 109 ? 23.384  -8.382  -34.667 1.00 11.58  ? 109 GLY C C   1 
ATOM   5279  O  O   . GLY C  1 109 ? 22.752  -7.679  -33.860 1.00 13.31  ? 109 GLY C O   1 
ATOM   5280  N  N   . GLN C  1 110 ? 24.356  -9.204  -34.266 1.00 10.47  ? 110 GLN C N   1 
ATOM   5281  C  CA  . GLN C  1 110 ? 24.649  -9.451  -32.891 1.00 12.01  ? 110 GLN C CA  1 
ATOM   5282  C  C   . GLN C  1 110 ? 25.888  -8.735  -32.405 1.00 10.32  ? 110 GLN C C   1 
ATOM   5283  O  O   . GLN C  1 110 ? 26.927  -8.778  -33.070 1.00 10.36  ? 110 GLN C O   1 
ATOM   5284  C  CB  . GLN C  1 110 ? 24.885  -10.963 -32.661 1.00 13.20  ? 110 GLN C CB  1 
ATOM   5285  C  CG  . GLN C  1 110 ? 23.808  -11.820 -33.252 1.00 14.73  ? 110 GLN C CG  1 
ATOM   5286  C  CD  . GLN C  1 110 ? 22.384  -11.413 -32.913 1.00 14.96  ? 110 GLN C CD  1 
ATOM   5287  O  OE1 . GLN C  1 110 ? 21.568  -11.013 -33.841 1.00 19.37  ? 110 GLN C OE1 1 
ATOM   5288  N  NE2 . GLN C  1 110 ? 22.095  -11.376 -31.672 1.00 14.26  ? 110 GLN C NE2 1 
ATOM   5289  N  N   . HIS C  1 111 ? 25.759  -8.040  -31.263 1.00 11.48  ? 111 HIS C N   1 
ATOM   5290  C  CA  . HIS C  1 111 ? 26.905  -7.478  -30.626 1.00 12.36  ? 111 HIS C CA  1 
ATOM   5291  C  C   . HIS C  1 111 ? 27.687  -8.576  -29.940 1.00 14.13  ? 111 HIS C C   1 
ATOM   5292  O  O   . HIS C  1 111 ? 27.148  -9.603  -29.527 1.00 19.77  ? 111 HIS C O   1 
ATOM   5293  C  CB  . HIS C  1 111 ? 26.540  -6.480  -29.559 1.00 15.11  ? 111 HIS C CB  1 
ATOM   5294  C  CG  . HIS C  1 111 ? 26.008  -5.195  -30.052 1.00 13.06  ? 111 HIS C CG  1 
ATOM   5295  N  ND1 . HIS C  1 111 ? 26.814  -4.085  -30.237 1.00 13.72  ? 111 HIS C ND1 1 
ATOM   5296  C  CD2 . HIS C  1 111 ? 24.746  -4.836  -30.561 1.00 14.86  ? 111 HIS C CD2 1 
ATOM   5297  C  CE1 . HIS C  1 111 ? 26.046  -3.093  -30.811 1.00 15.04  ? 111 HIS C CE1 1 
ATOM   5298  N  NE2 . HIS C  1 111 ? 24.792  -3.535  -30.921 1.00 18.12  ? 111 HIS C NE2 1 
ATOM   5299  N  N   . PHE C  1 112 ? 28.949  -8.345  -29.787 1.00 12.16  ? 112 PHE C N   1 
ATOM   5300  C  CA  . PHE C  1 112 ? 29.843  -9.051  -28.877 1.00 14.04  ? 112 PHE C CA  1 
ATOM   5301  C  C   . PHE C  1 112 ? 29.875  -8.277  -27.562 1.00 13.52  ? 112 PHE C C   1 
ATOM   5302  O  O   . PHE C  1 112 ? 29.372  -7.105  -27.478 1.00 13.20  ? 112 PHE C O   1 
ATOM   5303  C  CB  . PHE C  1 112 ? 31.225  -9.368  -29.500 1.00 14.65  ? 112 PHE C CB  1 
ATOM   5304  C  CG  . PHE C  1 112 ? 31.158  -10.375 -30.546 1.00 15.13  ? 112 PHE C CG  1 
ATOM   5305  C  CD1 . PHE C  1 112 ? 30.625  -10.109 -31.814 1.00 17.65  ? 112 PHE C CD1 1 
ATOM   5306  C  CD2 . PHE C  1 112 ? 31.587  -11.698 -30.261 1.00 18.85  ? 112 PHE C CD2 1 
ATOM   5307  C  CE1 . PHE C  1 112 ? 30.512  -11.142 -32.755 1.00 23.03  ? 112 PHE C CE1 1 
ATOM   5308  C  CE2 . PHE C  1 112 ? 31.495  -12.693 -31.226 1.00 23.02  ? 112 PHE C CE2 1 
ATOM   5309  C  CZ  . PHE C  1 112 ? 30.976  -12.410 -32.470 1.00 26.07  ? 112 PHE C CZ  1 
ATOM   5310  N  N   . ALA C  1 113 ? 30.473  -8.863  -26.542 1.00 14.30  ? 113 ALA C N   1 
ATOM   5311  C  CA  . ALA C  1 113 ? 30.572  -8.171  -25.272 1.00 12.89  ? 113 ALA C CA  1 
ATOM   5312  C  C   . ALA C  1 113 ? 31.328  -6.872  -25.319 1.00 14.75  ? 113 ALA C C   1 
ATOM   5313  O  O   . ALA C  1 113 ? 30.900  -5.932  -24.665 1.00 15.05  ? 113 ALA C O   1 
ATOM   5314  C  CB  . ALA C  1 113 ? 31.144  -9.126  -24.235 1.00 16.85  ? 113 ALA C CB  1 
ATOM   5315  N  N   . ALA C  1 114 ? 32.450  -6.832  -26.049 1.00 13.83  ? 114 ALA C N   1 
ATOM   5316  C  CA  . ALA C  1 114 ? 33.281  -5.616  -26.057 1.00 13.90  ? 114 ALA C CA  1 
ATOM   5317  C  C   . ALA C  1 114 ? 34.159  -5.752  -27.318 1.00 12.45  ? 114 ALA C C   1 
ATOM   5318  O  O   . ALA C  1 114 ? 33.976  -6.687  -28.074 1.00 13.40  ? 114 ALA C O   1 
ATOM   5319  C  CB  . ALA C  1 114 ? 34.189  -5.626  -24.817 1.00 16.60  ? 114 ALA C CB  1 
ATOM   5320  N  N   . GLU C  1 115 ? 34.901  -4.705  -27.572 1.00 13.53  ? 115 GLU C N   1 
ATOM   5321  C  CA  . GLU C  1 115 ? 35.724  -4.681  -28.757 1.00 12.68  ? 115 GLU C CA  1 
ATOM   5322  C  C   . GLU C  1 115 ? 36.993  -3.891  -28.388 1.00 12.90  ? 115 GLU C C   1 
ATOM   5323  O  O   . GLU C  1 115 ? 36.908  -2.758  -27.781 1.00 14.10  ? 115 GLU C O   1 
ATOM   5324  C  CB  . GLU C  1 115 ? 34.940  -4.030  -29.898 1.00 12.36  ? 115 GLU C CB  1 
ATOM   5325  C  CG  . GLU C  1 115 ? 35.603  -4.098  -31.281 1.00 11.20  ? 115 GLU C CG  1 
ATOM   5326  C  CD  . GLU C  1 115 ? 34.651  -3.695  -32.367 1.00 10.21  ? 115 GLU C CD  1 
ATOM   5327  O  OE1 . GLU C  1 115 ? 35.126  -3.183  -33.428 1.00 10.12  ? 115 GLU C OE1 1 
ATOM   5328  O  OE2 . GLU C  1 115 ? 33.416  -3.946  -32.268 1.00 10.49  ? 115 GLU C OE2 1 
ATOM   5329  N  N   . LEU C  1 116 ? 38.139  -4.427  -28.846 1.00 13.42  ? 116 LEU C N   1 
ATOM   5330  C  CA  . LEU C  1 116 ? 39.416  -3.748  -28.697 1.00 14.35  ? 116 LEU C CA  1 
ATOM   5331  C  C   . LEU C  1 116 ? 39.851  -3.153  -30.076 1.00 11.44  ? 116 LEU C C   1 
ATOM   5332  O  O   . LEU C  1 116 ? 39.670  -3.838  -31.091 1.00 13.37  ? 116 LEU C O   1 
ATOM   5333  C  CB  . LEU C  1 116 ? 40.501  -4.760  -28.355 1.00 15.96  ? 116 LEU C CB  1 
ATOM   5334  C  CG  . LEU C  1 116 ? 41.953  -4.223  -28.357 1.00 17.15  ? 116 LEU C CG  1 
ATOM   5335  C  CD1 . LEU C  1 116 ? 42.255  -3.245  -27.266 1.00 22.90  ? 116 LEU C CD1 1 
ATOM   5336  C  CD2 . LEU C  1 116 ? 42.966  -5.324  -28.509 1.00 18.25  ? 116 LEU C CD2 1 
ATOM   5337  N  N   . HIS C  1 117 ? 40.284  -1.914  -30.075 1.00 12.95  ? 117 HIS C N   1 
ATOM   5338  C  CA  . HIS C  1 117 ? 40.811  -1.233  -31.272 1.00 11.94  ? 117 HIS C CA  1 
ATOM   5339  C  C   . HIS C  1 117 ? 42.255  -0.915  -31.079 1.00 12.68  ? 117 HIS C C   1 
ATOM   5340  O  O   . HIS C  1 117 ? 42.637  -0.258  -30.086 1.00 14.03  ? 117 HIS C O   1 
ATOM   5341  C  CB  . HIS C  1 117 ? 40.027  -0.036  -31.541 1.00 12.36  ? 117 HIS C CB  1 
ATOM   5342  C  CG  . HIS C  1 117 ? 38.669  -0.316  -32.017 1.00 11.20  ? 117 HIS C CG  1 
ATOM   5343  N  ND1 . HIS C  1 117 ? 37.619  0.556   -31.892 1.00 11.00  ? 117 HIS C ND1 1 
ATOM   5344  C  CD2 . HIS C  1 117 ? 38.153  -1.471  -32.558 1.00 10.96  ? 117 HIS C CD2 1 
ATOM   5345  C  CE1 . HIS C  1 117 ? 36.510  0.031   -32.366 1.00 10.89  ? 117 HIS C CE1 1 
ATOM   5346  N  NE2 . HIS C  1 117 ? 36.820  -1.207  -32.791 1.00 10.06  ? 117 HIS C NE2 1 
ATOM   5347  N  N   . ILE C  1 118 ? 43.083  -1.340  -32.039 1.00 12.51  ? 118 ILE C N   1 
ATOM   5348  C  CA  . ILE C  1 118 ? 44.500  -0.955  -32.043 1.00 14.13  ? 118 ILE C CA  1 
ATOM   5349  C  C   . ILE C  1 118 ? 44.707  -0.018  -33.217 1.00 11.10  ? 118 ILE C C   1 
ATOM   5350  O  O   . ILE C  1 118 ? 44.569  -0.466  -34.407 1.00 12.71  ? 118 ILE C O   1 
ATOM   5351  C  CB  . ILE C  1 118 ? 45.413  -2.174  -32.137 1.00 14.06  ? 118 ILE C CB  1 
ATOM   5352  C  CG1 . ILE C  1 118 ? 45.087  -3.186  -31.104 1.00 15.88  ? 118 ILE C CG1 1 
ATOM   5353  C  CG2 . ILE C  1 118 ? 46.922  -1.765  -31.999 1.00 17.11  ? 118 ILE C CG2 1 
ATOM   5354  C  CD1 . ILE C  1 118 ? 45.926  -4.391  -31.217 1.00 17.68  ? 118 ILE C CD1 1 
ATOM   5355  N  N   . VAL C  1 119 ? 44.882  1.261   -32.927 1.00 13.20  ? 119 VAL C N   1 
ATOM   5356  C  CA  . VAL C  1 119 ? 44.889  2.335   -33.873 1.00 12.28  ? 119 VAL C CA  1 
ATOM   5357  C  C   . VAL C  1 119 ? 46.272  2.530   -34.409 1.00 13.06  ? 119 VAL C C   1 
ATOM   5358  O  O   . VAL C  1 119 ? 47.215  2.691   -33.633 1.00 14.24  ? 119 VAL C O   1 
ATOM   5359  C  CB  . VAL C  1 119 ? 44.344  3.665   -33.297 1.00 12.82  ? 119 VAL C CB  1 
ATOM   5360  C  CG1 . VAL C  1 119 ? 44.285  4.759   -34.324 1.00 14.16  ? 119 VAL C CG1 1 
ATOM   5361  C  CG2 . VAL C  1 119 ? 43.017  3.472   -32.610 1.00 14.24  ? 119 VAL C CG2 1 
ATOM   5362  N  N   . HIS C  1 120 ? 46.393  2.550   -35.731 1.00 12.79  ? 120 HIS C N   1 
ATOM   5363  C  CA  . HIS C  1 120 ? 47.688  2.820   -36.411 1.00 12.15  ? 120 HIS C CA  1 
ATOM   5364  C  C   . HIS C  1 120 ? 47.498  3.964   -37.410 1.00 12.87  ? 120 HIS C C   1 
ATOM   5365  O  O   . HIS C  1 120 ? 46.395  4.193   -37.873 1.00 11.95  ? 120 HIS C O   1 
ATOM   5366  C  CB  . HIS C  1 120 ? 48.142  1.587   -37.214 1.00 12.78  ? 120 HIS C CB  1 
ATOM   5367  C  CG  . HIS C  1 120 ? 48.298  0.338   -36.452 1.00 13.79  ? 120 HIS C CG  1 
ATOM   5368  N  ND1 . HIS C  1 120 ? 47.246  -0.343  -35.897 1.00 13.62  ? 120 HIS C ND1 1 
ATOM   5369  C  CD2 . HIS C  1 120 ? 49.433  -0.409  -36.133 1.00 16.00  ? 120 HIS C CD2 1 
ATOM   5370  C  CE1 . HIS C  1 120 ? 47.685  -1.442  -35.320 1.00 15.11  ? 120 HIS C CE1 1 
ATOM   5371  N  NE2 . HIS C  1 120 ? 49.021  -1.528  -35.466 1.00 15.38  ? 120 HIS C NE2 1 
ATOM   5372  N  N   . TYR C  1 121 ? 48.613  4.668   -37.735 1.00 12.71  ? 121 TYR C N   1 
ATOM   5373  C  CA  . TYR C  1 121 ? 48.525  5.772   -38.695 1.00 13.08  ? 121 TYR C CA  1 
ATOM   5374  C  C   . TYR C  1 121 ? 49.506  5.470   -39.798 1.00 12.80  ? 121 TYR C C   1 
ATOM   5375  O  O   . TYR C  1 121 ? 50.495  4.770   -39.626 1.00 13.76  ? 121 TYR C O   1 
ATOM   5376  C  CB  . TYR C  1 121 ? 48.828  7.115   -38.055 1.00 14.14  ? 121 TYR C CB  1 
ATOM   5377  C  CG  . TYR C  1 121 ? 50.254  7.312   -37.569 1.00 15.13  ? 121 TYR C CG  1 
ATOM   5378  C  CD1 . TYR C  1 121 ? 50.641  6.769   -36.350 1.00 16.57  ? 121 TYR C CD1 1 
ATOM   5379  C  CD2 . TYR C  1 121 ? 51.182  8.004   -38.353 1.00 15.52  ? 121 TYR C CD2 1 
ATOM   5380  C  CE1 . TYR C  1 121 ? 51.931  6.957   -35.847 1.00 21.88  ? 121 TYR C CE1 1 
ATOM   5381  C  CE2 . TYR C  1 121 ? 52.471  8.184   -37.901 1.00 16.36  ? 121 TYR C CE2 1 
ATOM   5382  C  CZ  . TYR C  1 121 ? 52.839  7.668   -36.648 1.00 18.40  ? 121 TYR C CZ  1 
ATOM   5383  O  OH  . TYR C  1 121 ? 54.131  7.816   -36.200 1.00 22.66  ? 121 TYR C OH  1 
ATOM   5384  N  N   . ASN C  1 122 ? 49.286  6.098   -40.929 1.00 13.77  ? 122 ASN C N   1 
ATOM   5385  C  CA  . ASN C  1 122 ? 50.106  5.860   -42.121 1.00 13.37  ? 122 ASN C CA  1 
ATOM   5386  C  C   . ASN C  1 122 ? 51.350  6.718   -42.029 1.00 13.56  ? 122 ASN C C   1 
ATOM   5387  O  O   . ASN C  1 122 ? 51.379  7.955   -42.292 1.00 15.26  ? 122 ASN C O   1 
ATOM   5388  C  CB  . ASN C  1 122 ? 49.293  6.288   -43.316 1.00 13.87  ? 122 ASN C CB  1 
ATOM   5389  C  CG  . ASN C  1 122 ? 49.976  5.932   -44.600 1.00 14.01  ? 122 ASN C CG  1 
ATOM   5390  O  OD1 . ASN C  1 122 ? 51.209  5.924   -44.687 1.00 15.28  ? 122 ASN C OD1 1 
ATOM   5391  N  ND2 . ASN C  1 122 ? 49.208  5.676   -45.615 1.00 15.44  ? 122 ASN C ND2 1 
ATOM   5392  N  N   . SER C  1 123 ? 52.391  6.079   -41.548 1.00 13.86  ? 123 SER C N   1 
ATOM   5393  C  CA  . SER C  1 123 ? 53.646  6.815   -41.248 1.00 14.94  ? 123 SER C CA  1 
ATOM   5394  C  C   . SER C  1 123 ? 54.480  6.983   -42.514 1.00 14.30  ? 123 SER C C   1 
ATOM   5395  O  O   . SER C  1 123 ? 55.454  7.728   -42.491 1.00 17.14  ? 123 SER C O   1 
ATOM   5396  C  CB  . SER C  1 123 ? 54.422  6.085   -40.166 1.00 16.14  ? 123 SER C CB  1 
ATOM   5397  O  OG  . SER C  1 123 ? 54.565  4.670   -40.471 1.00 16.04  ? 123 SER C OG  1 
ATOM   5398  N  N   . ASP C  1 124 ? 54.153  6.278   -43.594 1.00 14.13  ? 124 ASP C N   1 
ATOM   5399  C  CA  . ASP C  1 124 ? 54.800  6.569   -44.845 1.00 14.45  ? 124 ASP C CA  1 
ATOM   5400  C  C   . ASP C  1 124 ? 54.347  7.943   -45.375 1.00 16.02  ? 124 ASP C C   1 
ATOM   5401  O  O   . ASP C  1 124 ? 55.155  8.667   -45.972 1.00 20.43  ? 124 ASP C O   1 
ATOM   5402  C  CB  . ASP C  1 124 ? 54.531  5.496   -45.897 1.00 14.84  ? 124 ASP C CB  1 
ATOM   5403  C  CG  . ASP C  1 124 ? 55.269  4.189   -45.655 1.00 15.82  ? 124 ASP C CG  1 
ATOM   5404  O  OD1 . ASP C  1 124 ? 56.298  4.206   -44.905 1.00 15.81  ? 124 ASP C OD1 1 
ATOM   5405  O  OD2 . ASP C  1 124 ? 54.824  3.139   -46.204 1.00 16.95  ? 124 ASP C OD2 1 
ATOM   5406  N  N   . LEU C  1 125 ? 53.093  8.275   -45.184 1.00 14.61  ? 125 LEU C N   1 
ATOM   5407  C  CA  . LEU C  1 125 ? 52.566  9.540   -45.699 1.00 15.16  ? 125 LEU C CA  1 
ATOM   5408  C  C   . LEU C  1 125 ? 52.623  10.686  -44.696 1.00 15.95  ? 125 LEU C C   1 
ATOM   5409  O  O   . LEU C  1 125 ? 52.660  11.846  -45.166 1.00 18.25  ? 125 LEU C O   1 
ATOM   5410  C  CB  . LEU C  1 125 ? 51.127  9.351   -46.222 1.00 15.81  ? 125 LEU C CB  1 
ATOM   5411  C  CG  . LEU C  1 125 ? 50.908  8.393   -47.396 1.00 16.42  ? 125 LEU C CG  1 
ATOM   5412  C  CD1 . LEU C  1 125 ? 49.459  8.389   -47.779 1.00 17.58  ? 125 LEU C CD1 1 
ATOM   5413  C  CD2 . LEU C  1 125 ? 51.752  8.865   -48.536 1.00 20.56  ? 125 LEU C CD2 1 
ATOM   5414  N  N   . TYR C  1 126 ? 52.490  10.394  -43.384 1.00 15.28  ? 126 TYR C N   1 
ATOM   5415  C  CA  . TYR C  1 126 ? 52.252  11.373  -42.370 1.00 15.62  ? 126 TYR C CA  1 
ATOM   5416  C  C   . TYR C  1 126 ? 53.206  11.268  -41.236 1.00 17.63  ? 126 TYR C C   1 
ATOM   5417  O  O   . TYR C  1 126 ? 53.606  10.170  -40.882 1.00 16.94  ? 126 TYR C O   1 
ATOM   5418  C  CB  . TYR C  1 126 ? 50.785  11.383  -41.898 1.00 17.02  ? 126 TYR C CB  1 
ATOM   5419  C  CG  . TYR C  1 126 ? 49.818  11.405  -43.088 1.00 15.54  ? 126 TYR C CG  1 
ATOM   5420  C  CD1 . TYR C  1 126 ? 49.752  12.518  -43.983 1.00 17.23  ? 126 TYR C CD1 1 
ATOM   5421  C  CD2 . TYR C  1 126 ? 48.967  10.301  -43.353 1.00 14.73  ? 126 TYR C CD2 1 
ATOM   5422  C  CE1 . TYR C  1 126 ? 48.917  12.482  -45.065 1.00 17.76  ? 126 TYR C CE1 1 
ATOM   5423  C  CE2 . TYR C  1 126 ? 48.141  10.289  -44.467 1.00 15.14  ? 126 TYR C CE2 1 
ATOM   5424  C  CZ  . TYR C  1 126 ? 48.112  11.362  -45.317 1.00 15.76  ? 126 TYR C CZ  1 
ATOM   5425  O  OH  . TYR C  1 126 ? 47.313  11.425  -46.426 1.00 17.35  ? 126 TYR C OH  1 
ATOM   5426  N  N   . PRO C  1 127 ? 53.478  12.399  -40.513 1.00 17.63  ? 127 PRO C N   1 
ATOM   5427  C  CA  . PRO C  1 127 ? 54.478  12.373  -39.478 1.00 19.81  ? 127 PRO C CA  1 
ATOM   5428  C  C   . PRO C  1 127 ? 53.987  11.850  -38.158 1.00 18.93  ? 127 PRO C C   1 
ATOM   5429  O  O   . PRO C  1 127 ? 54.791  11.440  -37.304 1.00 22.54  ? 127 PRO C O   1 
ATOM   5430  C  CB  . PRO C  1 127 ? 54.819  13.879  -39.284 1.00 27.37  ? 127 PRO C CB  1 
ATOM   5431  C  CG  . PRO C  1 127 ? 53.609  14.624  -39.788 1.00 24.37  ? 127 PRO C CG  1 
ATOM   5432  C  CD  . PRO C  1 127 ? 53.168  13.780  -40.964 1.00 20.28  ? 127 PRO C CD  1 
ATOM   5433  N  N   . ASP C  1 128 ? 52.680  11.888  -37.946 1.00 17.43  ? 128 ASP C N   1 
ATOM   5434  C  CA  . ASP C  1 128 ? 52.127  11.463  -36.649 1.00 20.40  ? 128 ASP C CA  1 
ATOM   5435  C  C   . ASP C  1 128 ? 50.646  11.167  -36.829 1.00 17.47  ? 128 ASP C C   1 
ATOM   5436  O  O   . ASP C  1 128 ? 50.050  11.516  -37.852 1.00 17.65  ? 128 ASP C O   1 
ATOM   5437  C  CB  . ASP C  1 128 ? 52.407  12.493  -35.525 1.00 22.42  ? 128 ASP C CB  1 
ATOM   5438  C  CG  . ASP C  1 128 ? 52.050  13.886  -35.919 1.00 23.35  ? 128 ASP C CG  1 
ATOM   5439  O  OD1 . ASP C  1 128 ? 52.946  14.755  -35.802 1.00 32.37  ? 128 ASP C OD1 1 
ATOM   5440  O  OD2 . ASP C  1 128 ? 50.885  14.117  -36.329 1.00 28.82  ? 128 ASP C OD2 1 
ATOM   5441  N  N   . ALA C  1 129 ? 50.022  10.628  -35.790 1.00 17.18  ? 129 ALA C N   1 
ATOM   5442  C  CA  . ALA C  1 129 ? 48.654  10.163  -35.907 1.00 16.78  ? 129 ALA C CA  1 
ATOM   5443  C  C   . ALA C  1 129 ? 47.659  11.329  -35.979 1.00 20.21  ? 129 ALA C C   1 
ATOM   5444  O  O   . ALA C  1 129 ? 46.702  11.263  -36.729 1.00 18.84  ? 129 ALA C O   1 
ATOM   5445  C  CB  . ALA C  1 129 ? 48.337  9.223   -34.752 1.00 19.77  ? 129 ALA C CB  1 
ATOM   5446  N  N   . SER C  1 130 ? 47.919  12.429  -35.255 1.00 20.72  ? 130 SER C N   1 
ATOM   5447  C  CA  . SER C  1 130 ? 47.021  13.528  -35.328 1.00 23.21  ? 130 SER C CA  1 
ATOM   5448  C  C   . SER C  1 130 ? 46.976  14.138  -36.704 1.00 21.85  ? 130 SER C C   1 
ATOM   5449  O  O   . SER C  1 130 ? 45.916  14.496  -37.164 1.00 26.44  ? 130 SER C O   1 
ATOM   5450  C  CB  . SER C  1 130 ? 47.244  14.550  -34.191 1.00 29.69  ? 130 SER C CB  1 
ATOM   5451  O  OG  . SER C  1 130 ? 48.589  14.896  -34.010 1.00 44.52  ? 130 SER C OG  1 
ATOM   5452  N  N   . THR C  1 131 ? 48.156  14.275  -37.356 1.00 19.08  ? 131 THR C N   1 
ATOM   5453  C  CA  . THR C  1 131 ? 48.161  14.857  -38.676 1.00 18.88  ? 131 THR C CA  1 
ATOM   5454  C  C   . THR C  1 131 ? 47.470  13.874  -39.619 1.00 17.36  ? 131 THR C C   1 
ATOM   5455  O  O   . THR C  1 131 ? 46.792  14.296  -40.550 1.00 17.77  ? 131 THR C O   1 
ATOM   5456  C  CB  . THR C  1 131 ? 49.647  15.052  -39.091 1.00 18.45  ? 131 THR C CB  1 
ATOM   5457  O  OG1 . THR C  1 131 ? 50.258  15.945  -38.144 1.00 23.58  ? 131 THR C OG1 1 
ATOM   5458  C  CG2 . THR C  1 131 ? 49.717  15.648  -40.456 1.00 19.67  ? 131 THR C CG2 1 
ATOM   5459  N  N   . ALA C  1 132 ? 47.756  12.571  -39.454 1.00 16.29  ? 132 ALA C N   1 
ATOM   5460  C  CA  . ALA C  1 132 ? 47.173  11.572  -40.397 1.00 14.46  ? 132 ALA C CA  1 
ATOM   5461  C  C   . ALA C  1 132 ? 45.665  11.469  -40.318 1.00 15.00  ? 132 ALA C C   1 
ATOM   5462  O  O   . ALA C  1 132 ? 45.048  11.046  -41.288 1.00 14.54  ? 132 ALA C O   1 
ATOM   5463  C  CB  . ALA C  1 132 ? 47.737  10.228  -39.989 1.00 14.59  ? 132 ALA C CB  1 
ATOM   5464  N  N   . SER C  1 133 ? 45.077  11.777  -39.168 1.00 15.19  ? 133 SER C N   1 
ATOM   5465  C  CA  . SER C  1 133 ? 43.740  11.225  -38.874 1.00 15.54  ? 133 SER C CA  1 
ATOM   5466  C  C   . SER C  1 133 ? 42.688  11.824  -39.772 1.00 14.50  ? 133 SER C C   1 
ATOM   5467  O  O   . SER C  1 133 ? 41.639  11.200  -39.930 1.00 14.99  ? 133 SER C O   1 
ATOM   5468  C  CB  . SER C  1 133 ? 43.433  11.459  -37.393 1.00 17.71  ? 133 SER C CB  1 
ATOM   5469  O  OG  . SER C  1 133 ? 43.312  12.909  -37.119 1.00 18.85  ? 133 SER C OG  1 
ATOM   5470  N  N   . ASN C  1 134 ? 42.889  13.031  -40.302 1.00 15.11  ? 134 ASN C N   1 
ATOM   5471  C  CA  . ASN C  1 134 ? 41.908  13.666  -41.186 1.00 16.72  ? 134 ASN C CA  1 
ATOM   5472  C  C   . ASN C  1 134 ? 42.345  13.633  -42.636 1.00 16.93  ? 134 ASN C C   1 
ATOM   5473  O  O   . ASN C  1 134 ? 41.787  14.430  -43.432 1.00 21.22  ? 134 ASN C O   1 
ATOM   5474  C  CB  . ASN C  1 134 ? 41.506  15.095  -40.722 1.00 17.87  ? 134 ASN C CB  1 
ATOM   5475  C  CG  . ASN C  1 134 ? 42.639  16.086  -40.910 1.00 21.42  ? 134 ASN C CG  1 
ATOM   5476  O  OD1 . ASN C  1 134 ? 43.798  15.699  -41.011 1.00 22.94  ? 134 ASN C OD1 1 
ATOM   5477  N  ND2 . ASN C  1 134 ? 42.316  17.346  -40.939 1.00 24.17  ? 134 ASN C ND2 1 
ATOM   5478  N  N   . LYS C  1 135 ? 43.295  12.755  -42.995 1.00 16.50  ? 135 LYS C N   1 
ATOM   5479  C  CA  . LYS C  1 135 ? 43.907  12.817  -44.327 1.00 16.66  ? 135 LYS C CA  1 
ATOM   5480  C  C   . LYS C  1 135 ? 43.700  11.459  -45.003 1.00 15.67  ? 135 LYS C C   1 
ATOM   5481  O  O   . LYS C  1 135 ? 43.519  10.412  -44.322 1.00 15.25  ? 135 LYS C O   1 
ATOM   5482  C  CB  . LYS C  1 135 ? 45.364  13.212  -44.224 1.00 19.30  ? 135 LYS C CB  1 
ATOM   5483  C  CG  . LYS C  1 135 ? 45.552  14.685  -43.838 1.00 23.37  ? 135 LYS C CG  1 
ATOM   5484  C  CD  . LYS C  1 135 ? 47.000  15.078  -43.644 1.00 21.75  ? 135 LYS C CD  1 
ATOM   5485  C  CE  . LYS C  1 135 ? 47.119  16.503  -43.178 1.00 24.23  ? 135 LYS C CE  1 
ATOM   5486  N  NZ  . LYS C  1 135 ? 46.429  16.744  -41.875 1.00 24.41  ? 135 LYS C NZ  1 
ATOM   5487  N  N   . SER C  1 136 ? 43.785  11.505  -46.345 1.00 18.18  ? 136 SER C N   1 
ATOM   5488  C  CA  . SER C  1 136 ? 43.623  10.344  -47.150 1.00 16.68  ? 136 SER C CA  1 
ATOM   5489  C  C   . SER C  1 136 ? 44.502  9.178   -46.689 1.00 13.16  ? 136 SER C C   1 
ATOM   5490  O  O   . SER C  1 136 ? 45.711  9.329   -46.495 1.00 14.73  ? 136 SER C O   1 
ATOM   5491  C  CB  . SER C  1 136 ? 44.046  10.788  -48.538 1.00 22.89  ? 136 SER C CB  1 
ATOM   5492  O  OG  . SER C  1 136 ? 44.034  9.679   -49.345 1.00 27.36  ? 136 SER C OG  1 
ATOM   5493  N  N   . GLU C  1 137 ? 43.895  8.006   -46.549 1.00 14.00  ? 137 GLU C N   1 
ATOM   5494  C  CA  . GLU C  1 137 ? 44.637  6.771   -46.193 1.00 13.87  ? 137 GLU C CA  1 
ATOM   5495  C  C   . GLU C  1 137 ? 45.375  6.944   -44.865 1.00 13.41  ? 137 GLU C C   1 
ATOM   5496  O  O   . GLU C  1 137 ? 46.408  6.284   -44.584 1.00 14.38  ? 137 GLU C O   1 
ATOM   5497  C  CB  . GLU C  1 137 ? 45.594  6.316   -47.295 1.00 14.41  ? 137 GLU C CB  1 
ATOM   5498  C  CG  . GLU C  1 137 ? 44.939  6.027   -48.604 1.00 19.02  ? 137 GLU C CG  1 
ATOM   5499  C  CD  . GLU C  1 137 ? 45.887  5.523   -49.687 1.00 27.51  ? 137 GLU C CD  1 
ATOM   5500  O  OE1 . GLU C  1 137 ? 47.111  5.570   -49.477 1.00 38.81  ? 137 GLU C OE1 1 
ATOM   5501  O  OE2 . GLU C  1 137 ? 45.351  5.103   -50.700 1.00 40.92  ? 137 GLU C OE2 1 
ATOM   5502  N  N   . GLY C  1 138 ? 44.787  7.731   -43.955 1.00 12.68  ? 138 GLY C N   1 
ATOM   5503  C  CA  . GLY C  1 138 ? 45.552  8.132   -42.761 1.00 14.38  ? 138 GLY C CA  1 
ATOM   5504  C  C   . GLY C  1 138 ? 45.681  7.069   -41.708 1.00 11.17  ? 138 GLY C C   1 
ATOM   5505  O  O   . GLY C  1 138 ? 46.652  7.089   -40.996 1.00 12.47  ? 138 GLY C O   1 
ATOM   5506  N  N   . LEU C  1 139 ? 44.660  6.206   -41.559 1.00 10.97  ? 139 LEU C N   1 
ATOM   5507  C  CA  . LEU C  1 139 ? 44.605  5.306   -40.424 1.00 11.05  ? 139 LEU C CA  1 
ATOM   5508  C  C   . LEU C  1 139 ? 44.267  3.876   -40.803 1.00 10.43  ? 139 LEU C C   1 
ATOM   5509  O  O   . LEU C  1 139 ? 43.606  3.595   -41.794 1.00 10.55  ? 139 LEU C O   1 
ATOM   5510  C  CB  . LEU C  1 139 ? 43.514  5.799   -39.402 1.00 11.49  ? 139 LEU C CB  1 
ATOM   5511  C  CG  . LEU C  1 139 ? 43.705  7.195   -38.818 1.00 12.72  ? 139 LEU C CG  1 
ATOM   5512  C  CD1 . LEU C  1 139 ? 42.474  7.599   -38.094 1.00 13.81  ? 139 LEU C CD1 1 
ATOM   5513  C  CD2 . LEU C  1 139 ? 44.967  7.284   -37.966 1.00 14.37  ? 139 LEU C CD2 1 
ATOM   5514  N  N   . ALA C  1 140 ? 44.682  2.945   -39.924 1.00 10.92  ? 140 ALA C N   1 
ATOM   5515  C  CA  . ALA C  1 140 ? 44.301  1.547   -40.034 1.00 10.80  ? 140 ALA C CA  1 
ATOM   5516  C  C   . ALA C  1 140 ? 44.036  1.106   -38.610 1.00 10.10  ? 140 ALA C C   1 
ATOM   5517  O  O   . ALA C  1 140 ? 44.882  1.242   -37.748 1.00 12.45  ? 140 ALA C O   1 
ATOM   5518  C  CB  . ALA C  1 140 ? 45.396  0.709   -40.690 1.00 11.51  ? 140 ALA C CB  1 
ATOM   5519  N  N   . VAL C  1 141 ? 42.879  0.458   -38.387 1.00 9.76   ? 141 VAL C N   1 
ATOM   5520  C  CA  . VAL C  1 141 ? 42.538  -0.003  -37.080 1.00 9.74   ? 141 VAL C CA  1 
ATOM   5521  C  C   . VAL C  1 141 ? 42.338  -1.500  -37.142 1.00 9.79   ? 141 VAL C C   1 
ATOM   5522  O  O   . VAL C  1 141 ? 41.694  -2.020  -38.085 1.00 10.71  ? 141 VAL C O   1 
ATOM   5523  C  CB  . VAL C  1 141 ? 41.312  0.711   -36.500 1.00 10.22  ? 141 VAL C CB  1 
ATOM   5524  C  CG1 . VAL C  1 141 ? 40.979  0.212   -35.081 1.00 11.27  ? 141 VAL C CG1 1 
ATOM   5525  C  CG2 . VAL C  1 141 ? 41.479  2.221   -36.423 1.00 11.47  ? 141 VAL C CG2 1 
ATOM   5526  N  N   . LEU C  1 142 ? 42.929  -2.174  -36.184 1.00 10.52  ? 142 LEU C N   1 
ATOM   5527  C  CA  . LEU C  1 142 ? 42.655  -3.550  -35.963 1.00 11.42  ? 142 LEU C CA  1 
ATOM   5528  C  C   . LEU C  1 142 ? 41.569  -3.716  -34.936 1.00 10.80  ? 142 LEU C C   1 
ATOM   5529  O  O   . LEU C  1 142 ? 41.716  -3.145  -33.835 1.00 12.56  ? 142 LEU C O   1 
ATOM   5530  C  CB  . LEU C  1 142 ? 43.907  -4.367  -35.483 1.00 13.02  ? 142 LEU C CB  1 
ATOM   5531  C  CG  . LEU C  1 142 ? 45.152  -4.224  -36.362 1.00 15.12  ? 142 LEU C CG  1 
ATOM   5532  C  CD1 . LEU C  1 142 ? 46.260  -5.019  -35.751 1.00 17.61  ? 142 LEU C CD1 1 
ATOM   5533  C  CD2 . LEU C  1 142 ? 44.853  -4.729  -37.777 1.00 14.42  ? 142 LEU C CD2 1 
ATOM   5534  N  N   . ALA C  1 143 ? 40.540  -4.499  -35.177 1.00 10.56  ? 143 ALA C N   1 
ATOM   5535  C  CA  . ALA C  1 143 ? 39.454  -4.705  -34.249 1.00 10.53  ? 143 ALA C CA  1 
ATOM   5536  C  C   . ALA C  1 143 ? 39.361  -6.133  -33.797 1.00 10.74  ? 143 ALA C C   1 
ATOM   5537  O  O   . ALA C  1 143 ? 39.326  -7.047  -34.663 1.00 11.21  ? 143 ALA C O   1 
ATOM   5538  C  CB  . ALA C  1 143 ? 38.127  -4.240  -34.868 1.00 11.14  ? 143 ALA C CB  1 
ATOM   5539  N  N   . VAL C  1 144 ? 39.309  -6.318  -32.521 1.00 11.99  ? 144 VAL C N   1 
ATOM   5540  C  CA  . VAL C  1 144 ? 39.180  -7.654  -31.952 1.00 12.42  ? 144 VAL C CA  1 
ATOM   5541  C  C   . VAL C  1 144 ? 37.858  -7.687  -31.175 1.00 13.66  ? 144 VAL C C   1 
ATOM   5542  O  O   . VAL C  1 144 ? 37.595  -6.880  -30.289 1.00 13.97  ? 144 VAL C O   1 
ATOM   5543  C  CB  . VAL C  1 144 ? 40.282  -7.974  -30.945 1.00 14.58  ? 144 VAL C CB  1 
ATOM   5544  C  CG1 . VAL C  1 144 ? 40.033  -9.423  -30.419 1.00 18.52  ? 144 VAL C CG1 1 
ATOM   5545  C  CG2 . VAL C  1 144 ? 41.653  -7.922  -31.659 1.00 16.46  ? 144 VAL C CG2 1 
ATOM   5546  N  N   . LEU C  1 145 ? 36.980  -8.635  -31.584 1.00 13.04  ? 145 LEU C N   1 
ATOM   5547  C  CA  . LEU C  1 145 ? 35.710  -8.853  -30.922 1.00 12.96  ? 145 LEU C CA  1 
ATOM   5548  C  C   . LEU C  1 145 ? 35.955  -9.681  -29.659 1.00 14.88  ? 145 LEU C C   1 
ATOM   5549  O  O   . LEU C  1 145 ? 36.739  -10.673 -29.680 1.00 16.33  ? 145 LEU C O   1 
ATOM   5550  C  CB  . LEU C  1 145 ? 34.731  -9.562  -31.822 1.00 13.95  ? 145 LEU C CB  1 
ATOM   5551  C  CG  . LEU C  1 145 ? 34.452  -8.795  -33.132 1.00 13.74  ? 145 LEU C CG  1 
ATOM   5552  C  CD1 . LEU C  1 145 ? 33.782  -9.767  -34.154 1.00 16.33  ? 145 LEU C CD1 1 
ATOM   5553  C  CD2 . LEU C  1 145 ? 33.549  -7.612  -32.843 1.00 16.08  ? 145 LEU C CD2 1 
ATOM   5554  N  N   . ILE C  1 146 ? 35.287  -9.318  -28.568 1.00 13.21  ? 146 ILE C N   1 
ATOM   5555  C  CA  . ILE C  1 146 ? 35.539  -9.931  -27.225 1.00 15.87  ? 146 ILE C CA  1 
ATOM   5556  C  C   . ILE C  1 146 ? 34.241  -10.526 -26.772 1.00 17.82  ? 146 ILE C C   1 
ATOM   5557  O  O   . ILE C  1 146 ? 33.181  -9.830  -26.727 1.00 15.50  ? 146 ILE C O   1 
ATOM   5558  C  CB  . ILE C  1 146 ? 35.997  -8.862  -26.207 1.00 19.03  ? 146 ILE C CB  1 
ATOM   5559  C  CG1 . ILE C  1 146 ? 37.317  -8.216  -26.668 1.00 16.98  ? 146 ILE C CG1 1 
ATOM   5560  C  CG2 . ILE C  1 146 ? 36.147  -9.543  -24.815 1.00 19.47  ? 146 ILE C CG2 1 
ATOM   5561  C  CD1 . ILE C  1 146 ? 37.741  -6.930  -25.993 1.00 20.19  ? 146 ILE C CD1 1 
ATOM   5562  N  N   . GLU C  1 147 ? 34.265  -11.797 -26.351 1.00 16.59  ? 147 GLU C N   1 
ATOM   5563  C  CA  . GLU C  1 147 ? 33.119  -12.454 -25.726 1.00 18.18  ? 147 GLU C CA  1 
ATOM   5564  C  C   . GLU C  1 147 ? 33.520  -13.012 -24.358 1.00 19.45  ? 147 GLU C C   1 
ATOM   5565  O  O   . GLU C  1 147 ? 34.689  -13.235 -24.041 1.00 21.99  ? 147 GLU C O   1 
ATOM   5566  C  CB  . GLU C  1 147 ? 32.518  -13.567 -26.587 1.00 17.75  ? 147 GLU C CB  1 
ATOM   5567  C  CG  . GLU C  1 147 ? 33.461  -14.715 -26.847 1.00 20.37  ? 147 GLU C CG  1 
ATOM   5568  C  CD  . GLU C  1 147 ? 32.990  -15.680 -27.913 1.00 25.27  ? 147 GLU C CD  1 
ATOM   5569  O  OE1 . GLU C  1 147 ? 32.024  -15.405 -28.665 1.00 27.08  ? 147 GLU C OE1 1 
ATOM   5570  O  OE2 . GLU C  1 147 ? 33.683  -16.696 -28.052 1.00 29.89  ? 147 GLU C OE2 1 
ATOM   5571  N  N   A MET C  1 148 ? 32.498  -13.285 -23.525 0.50 23.48  ? 148 MET C N   1 
ATOM   5572  N  N   B MET C  1 148 ? 32.526  -13.304 -23.549 0.50 20.77  ? 148 MET C N   1 
ATOM   5573  C  CA  A MET C  1 148 ? 32.641  -14.017 -22.254 0.50 25.67  ? 148 MET C CA  1 
ATOM   5574  C  CA  B MET C  1 148 ? 32.789  -13.973 -22.302 0.50 21.14  ? 148 MET C CA  1 
ATOM   5575  C  C   A MET C  1 148 ? 33.179  -15.432 -22.550 0.50 29.85  ? 148 MET C C   1 
ATOM   5576  C  C   B MET C  1 148 ? 33.163  -15.438 -22.493 0.50 24.81  ? 148 MET C C   1 
ATOM   5577  O  O   A MET C  1 148 ? 32.703  -16.119 -23.459 0.50 26.27  ? 148 MET C O   1 
ATOM   5578  O  O   B MET C  1 148 ? 32.580  -16.146 -23.305 0.50 23.73  ? 148 MET C O   1 
ATOM   5579  C  CB  A MET C  1 148 ? 31.247  -14.125 -21.523 0.50 36.14  ? 148 MET C CB  1 
ATOM   5580  C  CB  B MET C  1 148 ? 31.535  -13.846 -21.475 0.50 21.14  ? 148 MET C CB  1 
ATOM   5581  C  CG  A MET C  1 148 ? 30.537  -12.855 -20.975 0.50 36.12  ? 148 MET C CG  1 
ATOM   5582  C  CG  B MET C  1 148 ? 31.715  -14.540 -20.185 0.50 25.86  ? 148 MET C CG  1 
ATOM   5583  S  SD  A MET C  1 148 ? 28.860  -13.125 -20.243 0.50 54.49  ? 148 MET C SD  1 
ATOM   5584  S  SD  B MET C  1 148 ? 31.441  -16.348 -20.175 0.50 41.01  ? 148 MET C SD  1 
ATOM   5585  C  CE  A MET C  1 148 ? 29.399  -14.620 -19.326 0.50 58.70  ? 148 MET C CE  1 
ATOM   5586  C  CE  B MET C  1 148 ? 30.998  -16.806 -18.510 0.50 34.74  ? 148 MET C CE  1 
ATOM   5587  N  N   . GLY C  1 149 ? 34.166  -15.887 -21.738 1.00 31.18  ? 149 GLY C N   1 
ATOM   5588  C  CA  . GLY C  1 149 ? 34.622  -17.293 -21.789 1.00 26.40  ? 149 GLY C CA  1 
ATOM   5589  C  C   . GLY C  1 149 ? 35.733  -17.483 -20.767 1.00 26.10  ? 149 GLY C C   1 
ATOM   5590  O  O   . GLY C  1 149 ? 35.555  -17.099 -19.623 1.00 29.00  ? 149 GLY C O   1 
ATOM   5591  N  N   . SER C  1 150 ? 36.826  -18.162 -21.111 1.00 29.41  ? 150 SER C N   1 
ATOM   5592  C  CA  . SER C  1 150 ? 37.865  -18.460 -20.111 1.00 27.60  ? 150 SER C CA  1 
ATOM   5593  C  C   . SER C  1 150 ? 38.597  -17.174 -19.753 1.00 32.67  ? 150 SER C C   1 
ATOM   5594  O  O   . SER C  1 150 ? 38.615  -16.255 -20.572 1.00 30.39  ? 150 SER C O   1 
ATOM   5595  C  CB  . SER C  1 150 ? 38.849  -19.499 -20.648 1.00 41.63  ? 150 SER C CB  1 
ATOM   5596  O  OG  . SER C  1 150 ? 38.230  -20.340 -21.606 1.00 51.76  ? 150 SER C OG  1 
ATOM   5597  N  N   . PHE C  1 151 ? 39.195  -17.055 -18.563 1.00 32.93  ? 151 PHE C N   1 
ATOM   5598  C  CA  . PHE C  1 151 ? 39.783  -15.758 -18.321 1.00 50.73  ? 151 PHE C CA  1 
ATOM   5599  C  C   . PHE C  1 151 ? 41.090  -15.660 -19.192 1.00 33.16  ? 151 PHE C C   1 
ATOM   5600  O  O   . PHE C  1 151 ? 41.617  -16.678 -19.636 1.00 40.86  ? 151 PHE C O   1 
ATOM   5601  C  CB  . PHE C  1 151 ? 40.004  -15.619 -16.804 1.00 181.15 ? 151 PHE C CB  1 
ATOM   5602  C  CG  . PHE C  1 151 ? 41.286  -14.958 -16.398 1.00 107.44 ? 151 PHE C CG  1 
ATOM   5603  C  CD1 . PHE C  1 151 ? 41.261  -13.717 -15.785 1.00 114.07 ? 151 PHE C CD1 1 
ATOM   5604  C  CD2 . PHE C  1 151 ? 42.505  -15.602 -16.549 1.00 169.04 ? 151 PHE C CD2 1 
ATOM   5605  C  CE1 . PHE C  1 151 ? 42.431  -13.102 -15.373 1.00 129.60 ? 151 PHE C CE1 1 
ATOM   5606  C  CE2 . PHE C  1 151 ? 43.679  -14.992 -16.140 1.00 160.97 ? 151 PHE C CE2 1 
ATOM   5607  C  CZ  . PHE C  1 151 ? 43.642  -13.742 -15.552 1.00 149.56 ? 151 PHE C CZ  1 
ATOM   5608  N  N   . ASN C  1 152 ? 41.561  -14.437 -19.440 1.00 33.89  ? 152 ASN C N   1 
ATOM   5609  C  CA  . ASN C  1 152 ? 42.596  -14.006 -20.323 1.00 33.14  ? 152 ASN C CA  1 
ATOM   5610  C  C   . ASN C  1 152 ? 43.613  -13.092 -19.599 1.00 23.77  ? 152 ASN C C   1 
ATOM   5611  O  O   . ASN C  1 152 ? 43.410  -11.882 -19.303 1.00 37.61  ? 152 ASN C O   1 
ATOM   5612  C  CB  . ASN C  1 152 ? 41.891  -13.234 -21.519 1.00 30.27  ? 152 ASN C CB  1 
ATOM   5613  C  CG  . ASN C  1 152 ? 42.953  -12.787 -22.616 1.00 133.46 ? 152 ASN C CG  1 
ATOM   5614  O  OD1 . ASN C  1 152 ? 44.183  -12.441 -22.241 1.00 120.79 ? 152 ASN C OD1 1 
ATOM   5615  N  ND2 . ASN C  1 152 ? 42.517  -12.904 -23.945 1.00 100.67 ? 152 ASN C ND2 1 
ATOM   5616  N  N   . PRO C  1 153 ? 44.783  -13.664 -19.231 1.00 30.19  ? 153 PRO C N   1 
ATOM   5617  C  CA  . PRO C  1 153 ? 45.912  -13.015 -18.544 1.00 33.66  ? 153 PRO C CA  1 
ATOM   5618  C  C   . PRO C  1 153 ? 46.522  -11.921 -19.368 1.00 33.30  ? 153 PRO C C   1 
ATOM   5619  O  O   . PRO C  1 153 ? 46.955  -10.960 -18.803 1.00 33.10  ? 153 PRO C O   1 
ATOM   5620  C  CB  . PRO C  1 153 ? 46.963  -14.139 -18.340 1.00 32.99  ? 153 PRO C CB  1 
ATOM   5621  C  CG  . PRO C  1 153 ? 46.375  -15.377 -18.877 1.00 38.82  ? 153 PRO C CG  1 
ATOM   5622  C  CD  . PRO C  1 153 ? 45.027  -15.077 -19.479 1.00 25.67  ? 153 PRO C CD  1 
ATOM   5623  N  N   . SER C  1 154 ? 46.421  -11.953 -20.727 1.00 35.95  ? 154 SER C N   1 
ATOM   5624  C  CA  . SER C  1 154 ? 46.919  -10.801 -21.552 1.00 35.14  ? 154 SER C CA  1 
ATOM   5625  C  C   . SER C  1 154 ? 46.078  -9.576  -21.346 1.00 28.74  ? 154 SER C C   1 
ATOM   5626  O  O   . SER C  1 154 ? 46.604  -8.531  -21.092 1.00 29.59  ? 154 SER C O   1 
ATOM   5627  C  CB  . SER C  1 154 ? 47.053  -11.176 -22.979 1.00 31.57  ? 154 SER C CB  1 
ATOM   5628  O  OG  . SER C  1 154 ? 47.875  -12.307 -23.030 1.00 42.86  ? 154 SER C OG  1 
ATOM   5629  N  N   . TYR C  1 155 ? 44.732  -9.700  -21.444 1.00 23.43  ? 155 TYR C N   1 
ATOM   5630  C  CA  . TYR C  1 155 ? 43.866  -8.558  -21.308 1.00 24.00  ? 155 TYR C CA  1 
ATOM   5631  C  C   . TYR C  1 155 ? 44.039  -8.050  -19.841 1.00 16.22  ? 155 TYR C C   1 
ATOM   5632  O  O   . TYR C  1 155 ? 43.914  -6.772  -19.541 1.00 24.02  ? 155 TYR C O   1 
ATOM   5633  C  CB  . TYR C  1 155 ? 42.447  -9.014  -21.580 1.00 28.99  ? 155 TYR C CB  1 
ATOM   5634  C  CG  . TYR C  1 155 ? 42.211  -8.832  -23.068 1.00 22.64  ? 155 TYR C CG  1 
ATOM   5635  C  CD1 . TYR C  1 155 ? 42.642  -9.824  -23.997 1.00 21.57  ? 155 TYR C CD1 1 
ATOM   5636  C  CD2 . TYR C  1 155 ? 41.621  -7.650  -23.578 1.00 22.80  ? 155 TYR C CD2 1 
ATOM   5637  C  CE1 . TYR C  1 155 ? 42.458  -9.653  -25.405 1.00 21.03  ? 155 TYR C CE1 1 
ATOM   5638  C  CE2 . TYR C  1 155 ? 41.463  -7.472  -24.975 1.00 23.36  ? 155 TYR C CE2 1 
ATOM   5639  C  CZ  . TYR C  1 155 ? 41.847  -8.486  -25.857 1.00 19.88  ? 155 TYR C CZ  1 
ATOM   5640  O  OH  . TYR C  1 155 ? 41.721  -8.342  -27.222 1.00 19.16  ? 155 TYR C OH  1 
ATOM   5641  N  N   . ASP C  1 156 ? 44.351  -8.959  -18.860 1.00 31.51  ? 156 ASP C N   1 
ATOM   5642  C  CA  . ASP C  1 156 ? 44.531  -8.518  -17.461 1.00 35.89  ? 156 ASP C CA  1 
ATOM   5643  C  C   . ASP C  1 156 ? 45.757  -7.563  -17.235 1.00 26.70  ? 156 ASP C C   1 
ATOM   5644  O  O   . ASP C  1 156 ? 45.776  -6.687  -16.291 1.00 30.83  ? 156 ASP C O   1 
ATOM   5645  C  CB  . ASP C  1 156 ? 44.556  -9.683  -16.443 1.00 37.90  ? 156 ASP C CB  1 
ATOM   5646  C  CG  . ASP C  1 156 ? 43.318  -9.643  -15.465 1.00 59.42  ? 156 ASP C CG  1 
ATOM   5647  O  OD1 . ASP C  1 156 ? 42.125  -9.425  -15.951 1.00 74.03  ? 156 ASP C OD1 1 
ATOM   5648  O  OD2 . ASP C  1 156 ? 43.547  -9.871  -14.196 1.00 76.27  ? 156 ASP C OD2 1 
ATOM   5649  N  N   . LYS C  1 157 ? 46.668  -7.585  -18.219 1.00 31.97  ? 157 LYS C N   1 
ATOM   5650  C  CA  . LYS C  1 157 ? 47.781  -6.621  -18.247 1.00 26.57  ? 157 LYS C CA  1 
ATOM   5651  C  C   . LYS C  1 157 ? 47.356  -5.171  -18.404 1.00 32.53  ? 157 LYS C C   1 
ATOM   5652  O  O   . LYS C  1 157 ? 48.133  -4.313  -17.942 1.00 49.07  ? 157 LYS C O   1 
ATOM   5653  C  CB  . LYS C  1 157 ? 48.880  -7.079  -19.234 1.00 28.88  ? 157 LYS C CB  1 
ATOM   5654  C  CG  . LYS C  1 157 ? 49.236  -8.552  -19.115 1.00 31.96  ? 157 LYS C CG  1 
ATOM   5655  C  CD  . LYS C  1 157 ? 50.397  -9.013  -19.986 1.00 35.45  ? 157 LYS C CD  1 
ATOM   5656  C  CE  . LYS C  1 157 ? 50.526  -10.531 -19.933 1.00 40.75  ? 157 LYS C CE  1 
ATOM   5657  N  NZ  . LYS C  1 157 ? 51.666  -11.154 -20.678 1.00 44.07  ? 157 LYS C NZ  1 
ATOM   5658  N  N   . ILE C  1 158 ? 46.164  -4.889  -19.009 1.00 23.34  ? 158 ILE C N   1 
ATOM   5659  C  CA  . ILE C  1 158 ? 45.595  -3.584  -19.019 1.00 22.07  ? 158 ILE C CA  1 
ATOM   5660  C  C   . ILE C  1 158 ? 44.666  -3.514  -17.824 1.00 23.49  ? 158 ILE C C   1 
ATOM   5661  O  O   . ILE C  1 158 ? 44.667  -2.501  -17.115 1.00 27.22  ? 158 ILE C O   1 
ATOM   5662  C  CB  . ILE C  1 158 ? 44.847  -3.361  -20.352 1.00 22.64  ? 158 ILE C CB  1 
ATOM   5663  C  CG1 . ILE C  1 158 ? 45.900  -3.500  -21.506 1.00 36.25  ? 158 ILE C CG1 1 
ATOM   5664  C  CG2 . ILE C  1 158 ? 44.041  -2.057  -20.254 1.00 24.82  ? 158 ILE C CG2 1 
ATOM   5665  C  CD1 . ILE C  1 158 ? 45.332  -3.585  -22.913 1.00 33.39  ? 158 ILE C CD1 1 
ATOM   5666  N  N   . PHE C  1 159 ? 43.794  -4.518  -17.693 1.00 29.34  ? 159 PHE C N   1 
ATOM   5667  C  CA  . PHE C  1 159 ? 42.675  -4.353  -16.748 1.00 23.23  ? 159 PHE C CA  1 
ATOM   5668  C  C   . PHE C  1 159 ? 43.037  -4.163  -15.274 1.00 29.12  ? 159 PHE C C   1 
ATOM   5669  O  O   . PHE C  1 159 ? 42.302  -3.531  -14.493 1.00 29.52  ? 159 PHE C O   1 
ATOM   5670  C  CB  . PHE C  1 159 ? 41.753  -5.537  -16.839 1.00 27.23  ? 159 PHE C CB  1 
ATOM   5671  C  CG  . PHE C  1 159 ? 41.046  -5.782  -18.176 1.00 26.33  ? 159 PHE C CG  1 
ATOM   5672  C  CD1 . PHE C  1 159 ? 40.971  -4.840  -19.191 1.00 32.91  ? 159 PHE C CD1 1 
ATOM   5673  C  CD2 . PHE C  1 159 ? 40.404  -7.007  -18.375 1.00 25.05  ? 159 PHE C CD2 1 
ATOM   5674  C  CE1 . PHE C  1 159 ? 40.291  -5.127  -20.378 1.00 28.52  ? 159 PHE C CE1 1 
ATOM   5675  C  CE2 . PHE C  1 159 ? 39.729  -7.298  -19.550 1.00 28.58  ? 159 PHE C CE2 1 
ATOM   5676  C  CZ  . PHE C  1 159 ? 39.670  -6.355  -20.556 1.00 25.20  ? 159 PHE C CZ  1 
ATOM   5677  N  N   . SER C  1 160 ? 44.232  -4.604  -14.975 1.00 23.50  ? 160 SER C N   1 
ATOM   5678  C  CA  . SER C  1 160 ? 44.740  -4.592  -13.604 1.00 27.12  ? 160 SER C CA  1 
ATOM   5679  C  C   . SER C  1 160 ? 45.225  -3.221  -13.210 1.00 26.88  ? 160 SER C C   1 
ATOM   5680  O  O   . SER C  1 160 ? 45.622  -3.041  -12.096 1.00 35.41  ? 160 SER C O   1 
ATOM   5681  C  CB  . SER C  1 160 ? 45.822  -5.657  -13.507 1.00 31.08  ? 160 SER C CB  1 
ATOM   5682  O  OG  . SER C  1 160 ? 46.992  -5.214  -14.192 1.00 27.72  ? 160 SER C OG  1 
ATOM   5683  N  N   . HIS C  1 161 ? 45.236  -2.259  -14.138 1.00 28.00  ? 161 HIS C N   1 
ATOM   5684  C  CA  . HIS C  1 161 ? 45.609  -0.900  -13.910 1.00 31.56  ? 161 HIS C CA  1 
ATOM   5685  C  C   . HIS C  1 161 ? 44.423  0.051   -13.847 1.00 22.96  ? 161 HIS C C   1 
ATOM   5686  O  O   . HIS C  1 161 ? 44.608  1.279   -13.576 1.00 24.48  ? 161 HIS C O   1 
ATOM   5687  C  CB  . HIS C  1 161 ? 46.698  -0.550  -14.963 1.00 35.67  ? 161 HIS C CB  1 
ATOM   5688  C  CG  . HIS C  1 161 ? 48.019  -1.374  -14.786 1.00 41.25  ? 161 HIS C CG  1 
ATOM   5689  N  ND1 . HIS C  1 161 ? 49.021  -1.035  -13.904 1.00 51.52  ? 161 HIS C ND1 1 
ATOM   5690  C  CD2 . HIS C  1 161 ? 48.438  -2.571  -15.403 1.00 33.78  ? 161 HIS C CD2 1 
ATOM   5691  C  CE1 . HIS C  1 161 ? 50.016  -1.954  -13.991 1.00 51.10  ? 161 HIS C CE1 1 
ATOM   5692  N  NE2 . HIS C  1 161 ? 49.651  -2.892  -14.895 1.00 53.17  ? 161 HIS C NE2 1 
ATOM   5693  N  N   . LEU C  1 162 ? 43.175  -0.412  -14.154 1.00 29.96  ? 162 LEU C N   1 
ATOM   5694  C  CA  . LEU C  1 162 ? 42.033  0.538   -14.350 1.00 24.67  ? 162 LEU C CA  1 
ATOM   5695  C  C   . LEU C  1 162 ? 41.634  1.332   -13.120 1.00 18.04  ? 162 LEU C C   1 
ATOM   5696  O  O   . LEU C  1 162 ? 41.194  2.506   -13.224 1.00 22.22  ? 162 LEU C O   1 
ATOM   5697  C  CB  . LEU C  1 162 ? 40.813  -0.212  -14.807 1.00 28.62  ? 162 LEU C CB  1 
ATOM   5698  C  CG  . LEU C  1 162 ? 41.064  -0.891  -16.160 1.00 26.54  ? 162 LEU C CG  1 
ATOM   5699  C  CD1 . LEU C  1 162 ? 39.871  -1.719  -16.631 1.00 32.87  ? 162 LEU C CD1 1 
ATOM   5700  C  CD2 . LEU C  1 162 ? 41.472  -0.013  -17.345 1.00 35.79  ? 162 LEU C CD2 1 
ATOM   5701  N  N   . GLN C  1 163 ? 41.890  0.842   -11.867 1.00 25.96  ? 163 GLN C N   1 
ATOM   5702  C  CA  . GLN C  1 163 ? 41.528  1.626   -10.652 1.00 29.06  ? 163 GLN C CA  1 
ATOM   5703  C  C   . GLN C  1 163 ? 42.448  2.902   -10.510 1.00 21.87  ? 163 GLN C C   1 
ATOM   5704  O  O   . GLN C  1 163 ? 42.184  3.846   -9.694  1.00 31.06  ? 163 GLN C O   1 
ATOM   5705  C  CB  . GLN C  1 163 ? 41.456  0.747   -9.368  1.00 29.91  ? 163 GLN C CB  1 
ATOM   5706  C  CG  . GLN C  1 163 ? 40.350  -0.320  -9.318  1.00 47.11  ? 163 GLN C CG  1 
ATOM   5707  C  CD  . GLN C  1 163 ? 38.932  0.189   -9.613  1.00 39.19  ? 163 GLN C CD  1 
ATOM   5708  O  OE1 . GLN C  1 163 ? 38.351  0.965   -8.822  1.00 38.32  ? 163 GLN C OE1 1 
ATOM   5709  N  NE2 . GLN C  1 163 ? 38.356  -0.259  -10.734 1.00 51.04  ? 163 GLN C NE2 1 
ATOM   5710  N  N   . HIS C  1 164 ? 43.562  2.909   -11.274 1.00 22.99  ? 164 HIS C N   1 
ATOM   5711  C  CA  . HIS C  1 164 ? 44.484  4.072   -11.296 1.00 26.53  ? 164 HIS C CA  1 
ATOM   5712  C  C   . HIS C  1 164 ? 44.069  5.198   -12.177 1.00 29.72  ? 164 HIS C C   1 
ATOM   5713  O  O   . HIS C  1 164 ? 44.595  6.316   -12.086 1.00 29.19  ? 164 HIS C O   1 
ATOM   5714  C  CB  . HIS C  1 164 ? 45.959  3.683   -11.416 1.00 24.01  ? 164 HIS C CB  1 
ATOM   5715  C  CG  . HIS C  1 164 ? 46.361  2.636   -10.426 1.00 21.37  ? 164 HIS C CG  1 
ATOM   5716  N  ND1 . HIS C  1 164 ? 46.393  2.867   -9.090  1.00 19.23  ? 164 HIS C ND1 1 
ATOM   5717  C  CD2 . HIS C  1 164 ? 46.669  1.264   -10.624 1.00 22.19  ? 164 HIS C CD2 1 
ATOM   5718  C  CE1 . HIS C  1 164 ? 46.717  1.723   -8.453  1.00 20.62  ? 164 HIS C CE1 1 
ATOM   5719  N  NE2 . HIS C  1 164 ? 46.878  0.724   -9.403  1.00 24.36  ? 164 HIS C NE2 1 
ATOM   5720  N  N   . VAL C  1 165 ? 43.116  4.904   -13.071 1.00 25.58  ? 165 VAL C N   1 
ATOM   5721  C  CA  . VAL C  1 165 ? 42.605  5.998   -13.948 1.00 26.20  ? 165 VAL C CA  1 
ATOM   5722  C  C   . VAL C  1 165 ? 41.091  5.976   -13.905 1.00 24.55  ? 165 VAL C C   1 
ATOM   5723  O  O   . VAL C  1 165 ? 40.400  6.104   -14.911 1.00 25.90  ? 165 VAL C O   1 
ATOM   5724  C  CB  . VAL C  1 165 ? 43.121  5.836   -15.359 1.00 21.73  ? 165 VAL C CB  1 
ATOM   5725  C  CG1 . VAL C  1 165 ? 44.650  6.017   -15.399 1.00 25.99  ? 165 VAL C CG1 1 
ATOM   5726  C  CG2 . VAL C  1 165 ? 42.800  4.445   -15.863 1.00 25.28  ? 165 VAL C CG2 1 
ATOM   5727  N  N   . LYS C  1 166 ? 40.548  5.803   -12.706 1.00 36.73  ? 166 LYS C N   1 
ATOM   5728  C  CA  . LYS C  1 166 ? 39.116  5.698   -12.620 1.00 31.10  ? 166 LYS C CA  1 
ATOM   5729  C  C   . LYS C  1 166 ? 38.362  6.893   -13.130 1.00 32.95  ? 166 LYS C C   1 
ATOM   5730  O  O   . LYS C  1 166 ? 37.226  6.742   -13.575 1.00 34.36  ? 166 LYS C O   1 
ATOM   5731  C  CB  . LYS C  1 166 ? 38.691  5.489   -11.149 1.00 34.73  ? 166 LYS C CB  1 
ATOM   5732  C  CG  . LYS C  1 166 ? 38.759  4.082   -10.704 1.00 33.97  ? 166 LYS C CG  1 
ATOM   5733  C  CD  . LYS C  1 166 ? 38.393  4.106   -9.228  1.00 43.38  ? 166 LYS C CD  1 
ATOM   5734  C  CE  . LYS C  1 166 ? 36.888  4.130   -8.989  1.00 41.01  ? 166 LYS C CE  1 
ATOM   5735  N  NZ  . LYS C  1 166 ? 36.189  2.903   -9.514  1.00 36.34  ? 166 LYS C NZ  1 
ATOM   5736  N  N   . TYR C  1 167 ? 38.985  8.072   -13.059 1.00 22.02  ? 167 TYR C N   1 
ATOM   5737  C  CA  . TYR C  1 167 ? 38.324  9.361   -13.393 1.00 28.44  ? 167 TYR C CA  1 
ATOM   5738  C  C   . TYR C  1 167 ? 38.851  10.063  -14.608 1.00 25.44  ? 167 TYR C C   1 
ATOM   5739  O  O   . TYR C  1 167 ? 40.003  9.847   -14.898 1.00 28.07  ? 167 TYR C O   1 
ATOM   5740  C  CB  . TYR C  1 167 ? 38.446  10.244  -12.147 1.00 41.50  ? 167 TYR C CB  1 
ATOM   5741  C  CG  . TYR C  1 167 ? 37.753  9.573   -11.015 1.00 46.20  ? 167 TYR C CG  1 
ATOM   5742  C  CD1 . TYR C  1 167 ? 36.354  9.564   -10.960 1.00 43.40  ? 167 TYR C CD1 1 
ATOM   5743  C  CD2 . TYR C  1 167 ? 38.476  8.888   -10.000 1.00 44.43  ? 167 TYR C CD2 1 
ATOM   5744  C  CE1 . TYR C  1 167 ? 35.686  8.938   -9.929  1.00 57.54  ? 167 TYR C CE1 1 
ATOM   5745  C  CE2 . TYR C  1 167 ? 37.796  8.266   -8.939  1.00 52.89  ? 167 TYR C CE2 1 
ATOM   5746  C  CZ  . TYR C  1 167 ? 36.405  8.302   -8.947  1.00 84.64  ? 167 TYR C CZ  1 
ATOM   5747  O  OH  . TYR C  1 167 ? 35.660  7.714   -7.937  1.00 182.09 ? 167 TYR C OH  1 
ATOM   5748  N  N   . LYS C  1 168 ? 37.996  10.926  -15.211 1.00 23.70  ? 168 LYS C N   1 
ATOM   5749  C  CA  . LYS C  1 168 ? 38.339  11.654  -16.422 1.00 19.63  ? 168 LYS C CA  1 
ATOM   5750  C  C   . LYS C  1 168 ? 39.600  12.442  -16.208 1.00 21.28  ? 168 LYS C C   1 
ATOM   5751  O  O   . LYS C  1 168 ? 39.769  13.195  -15.230 1.00 29.99  ? 168 LYS C O   1 
ATOM   5752  C  CB  . LYS C  1 168 ? 37.199  12.593  -16.909 1.00 22.86  ? 168 LYS C CB  1 
ATOM   5753  C  CG  . LYS C  1 168 ? 37.606  13.351  -18.152 1.00 23.17  ? 168 LYS C CG  1 
ATOM   5754  C  CD  . LYS C  1 168 ? 36.457  14.180  -18.727 1.00 27.55  ? 168 LYS C CD  1 
ATOM   5755  C  CE  . LYS C  1 168 ? 36.826  14.857  -20.064 1.00 30.24  ? 168 LYS C CE  1 
ATOM   5756  N  NZ  . LYS C  1 168 ? 35.695  15.676  -20.565 1.00 40.04  ? 168 LYS C NZ  1 
ATOM   5757  N  N   . GLY C  1 169 ? 40.499  12.316  -17.163 1.00 21.01  ? 169 GLY C N   1 
ATOM   5758  C  CA  . GLY C  1 169 ? 41.787  12.968  -17.167 1.00 25.69  ? 169 GLY C CA  1 
ATOM   5759  C  C   . GLY C  1 169 ? 42.924  12.283  -16.448 1.00 29.29  ? 169 GLY C C   1 
ATOM   5760  O  O   . GLY C  1 169 ? 44.089  12.729  -16.548 1.00 27.21  ? 169 GLY C O   1 
ATOM   5761  N  N   . GLN C  1 170 ? 42.619  11.278  -15.641 1.00 22.93  ? 170 GLN C N   1 
ATOM   5762  C  CA  . GLN C  1 170 ? 43.670  10.598  -14.885 1.00 23.99  ? 170 GLN C CA  1 
ATOM   5763  C  C   . GLN C  1 170 ? 44.477  9.680   -15.772 1.00 22.78  ? 170 GLN C C   1 
ATOM   5764  O  O   . GLN C  1 170 ? 44.009  9.078   -16.732 1.00 21.29  ? 170 GLN C O   1 
ATOM   5765  C  CB  . GLN C  1 170 ? 43.090  9.840   -13.707 1.00 21.64  ? 170 GLN C CB  1 
ATOM   5766  C  CG  . GLN C  1 170 ? 42.490  10.707  -12.628 1.00 25.36  ? 170 GLN C CG  1 
ATOM   5767  C  CD  . GLN C  1 170 ? 42.094  9.891   -11.389 1.00 43.78  ? 170 GLN C CD  1 
ATOM   5768  O  OE1 . GLN C  1 170 ? 41.641  8.739   -11.517 1.00 31.21  ? 170 GLN C OE1 1 
ATOM   5769  N  NE2 . GLN C  1 170 ? 42.146  10.511  -10.216 1.00 193.19 ? 170 GLN C NE2 1 
ATOM   5770  N  N   . GLU C  1 171 ? 45.753  9.594   -15.393 1.00 21.17  ? 171 GLU C N   1 
ATOM   5771  C  CA  . GLU C  1 171 ? 46.737  8.842   -16.123 1.00 21.20  ? 171 GLU C CA  1 
ATOM   5772  C  C   . GLU C  1 171 ? 47.497  7.951   -15.189 1.00 21.99  ? 171 GLU C C   1 
ATOM   5773  O  O   . GLU C  1 171 ? 47.723  8.257   -13.997 1.00 25.18  ? 171 GLU C O   1 
ATOM   5774  C  CB  . GLU C  1 171 ? 47.716  9.865   -16.761 1.00 28.99  ? 171 GLU C CB  1 
ATOM   5775  C  CG  . GLU C  1 171 ? 47.078  10.759  -17.805 1.00 27.02  ? 171 GLU C CG  1 
ATOM   5776  C  CD  . GLU C  1 171 ? 48.024  11.775  -18.370 1.00 39.08  ? 171 GLU C CD  1 
ATOM   5777  O  OE1 . GLU C  1 171 ? 49.210  11.838  -17.922 1.00 38.38  ? 171 GLU C OE1 1 
ATOM   5778  O  OE2 . GLU C  1 171 ? 47.544  12.539  -19.249 1.00 34.75  ? 171 GLU C OE2 1 
ATOM   5779  N  N   . ALA C  1 172 ? 48.006  6.907   -15.756 1.00 21.10  ? 172 ALA C N   1 
ATOM   5780  C  CA  . ALA C  1 172 ? 48.914  5.958   -15.097 1.00 26.46  ? 172 ALA C CA  1 
ATOM   5781  C  C   . ALA C  1 172 ? 49.756  5.306   -16.141 1.00 28.27  ? 172 ALA C C   1 
ATOM   5782  O  O   . ALA C  1 172 ? 49.583  5.503   -17.304 1.00 33.05  ? 172 ALA C O   1 
ATOM   5783  C  CB  . ALA C  1 172 ? 48.164  4.873   -14.353 1.00 31.27  ? 172 ALA C CB  1 
ATOM   5784  N  N   . PHE C  1 173 ? 50.640  4.441   -15.763 1.00 32.33  ? 173 PHE C N   1 
ATOM   5785  C  CA  . PHE C  1 173 ? 51.534  3.788   -16.692 1.00 42.38  ? 173 PHE C CA  1 
ATOM   5786  C  C   . PHE C  1 173 ? 51.274  2.352   -16.512 1.00 41.15  ? 173 PHE C C   1 
ATOM   5787  O  O   . PHE C  1 173 ? 50.986  1.882   -15.397 1.00 29.36  ? 173 PHE C O   1 
ATOM   5788  C  CB  . PHE C  1 173 ? 53.031  4.107   -16.434 1.00 41.87  ? 173 PHE C CB  1 
ATOM   5789  C  CG  . PHE C  1 173 ? 53.468  5.482   -16.894 1.00 30.11  ? 173 PHE C CG  1 
ATOM   5790  C  CD1 . PHE C  1 173 ? 53.552  6.583   -16.029 1.00 42.53  ? 173 PHE C CD1 1 
ATOM   5791  C  CD2 . PHE C  1 173 ? 53.771  5.685   -18.237 1.00 36.17  ? 173 PHE C CD2 1 
ATOM   5792  C  CE1 . PHE C  1 173 ? 53.956  7.844   -16.516 1.00 37.74  ? 173 PHE C CE1 1 
ATOM   5793  C  CE2 . PHE C  1 173 ? 54.130  6.931   -18.750 1.00 30.93  ? 173 PHE C CE2 1 
ATOM   5794  C  CZ  . PHE C  1 173 ? 54.262  8.016   -17.895 1.00 33.63  ? 173 PHE C CZ  1 
ATOM   5795  N  N   . VAL C  1 174 ? 51.330  1.679   -17.654 1.00 36.75  ? 174 VAL C N   1 
ATOM   5796  C  CA  . VAL C  1 174 ? 51.315  0.226   -17.728 1.00 36.78  ? 174 VAL C CA  1 
ATOM   5797  C  C   . VAL C  1 174 ? 52.679  -0.266  -18.192 1.00 44.07  ? 174 VAL C C   1 
ATOM   5798  O  O   . VAL C  1 174 ? 53.203  0.294   -19.174 1.00 39.08  ? 174 VAL C O   1 
ATOM   5799  C  CB  . VAL C  1 174 ? 50.341  -0.234  -18.828 1.00 31.78  ? 174 VAL C CB  1 
ATOM   5800  C  CG1 . VAL C  1 174 ? 50.400  -1.736  -18.993 1.00 31.50  ? 174 VAL C CG1 1 
ATOM   5801  C  CG2 . VAL C  1 174 ? 48.938  0.175   -18.492 1.00 33.47  ? 174 VAL C CG2 1 
ATOM   5802  N  N   . PRO C  1 175 ? 53.246  -1.323  -17.539 1.00 33.96  ? 175 PRO C N   1 
ATOM   5803  C  CA  . PRO C  1 175 ? 54.478  -1.939  -18.088 1.00 35.91  ? 175 PRO C CA  1 
ATOM   5804  C  C   . PRO C  1 175 ? 54.225  -2.534  -19.441 1.00 42.64  ? 175 PRO C C   1 
ATOM   5805  O  O   . PRO C  1 175 ? 53.161  -3.128  -19.648 1.00 28.62  ? 175 PRO C O   1 
ATOM   5806  C  CB  . PRO C  1 175 ? 54.859  -3.058  -17.052 1.00 37.99  ? 175 PRO C CB  1 
ATOM   5807  C  CG  . PRO C  1 175 ? 53.795  -3.077  -16.024 1.00 42.59  ? 175 PRO C CG  1 
ATOM   5808  C  CD  . PRO C  1 175 ? 52.903  -1.858  -16.198 1.00 35.38  ? 175 PRO C CD  1 
ATOM   5809  N  N   . GLY C  1 176 ? 55.262  -2.467  -20.278 1.00 33.00  ? 176 GLY C N   1 
ATOM   5810  C  CA  . GLY C  1 176 ? 55.248  -3.131  -21.602 1.00 34.71  ? 176 GLY C CA  1 
ATOM   5811  C  C   . GLY C  1 176 ? 54.939  -4.599  -21.505 1.00 43.00  ? 176 GLY C C   1 
ATOM   5812  O  O   . GLY C  1 176 ? 55.456  -5.335  -20.612 1.00 197.15 ? 176 GLY C O   1 
ATOM   5813  N  N   . PHE C  1 177 ? 54.100  -5.040  -22.457 1.00 27.99  ? 177 PHE C N   1 
ATOM   5814  C  CA  . PHE C  1 177 ? 53.913  -6.473  -22.758 1.00 28.24  ? 177 PHE C CA  1 
ATOM   5815  C  C   . PHE C  1 177 ? 53.698  -6.715  -24.242 1.00 32.31  ? 177 PHE C C   1 
ATOM   5816  O  O   . PHE C  1 177 ? 53.706  -5.736  -25.007 1.00 25.52  ? 177 PHE C O   1 
ATOM   5817  C  CB  . PHE C  1 177 ? 52.753  -7.075  -21.942 1.00 30.34  ? 177 PHE C CB  1 
ATOM   5818  C  CG  . PHE C  1 177 ? 51.396  -6.555  -22.366 1.00 24.37  ? 177 PHE C CG  1 
ATOM   5819  C  CD1 . PHE C  1 177 ? 50.935  -5.333  -21.893 1.00 29.81  ? 177 PHE C CD1 1 
ATOM   5820  C  CD2 . PHE C  1 177 ? 50.563  -7.317  -23.191 1.00 36.15  ? 177 PHE C CD2 1 
ATOM   5821  C  CE1 . PHE C  1 177 ? 49.703  -4.857  -22.249 1.00 40.89  ? 177 PHE C CE1 1 
ATOM   5822  C  CE2 . PHE C  1 177 ? 49.328  -6.864  -23.553 1.00 30.80  ? 177 PHE C CE2 1 
ATOM   5823  C  CZ  . PHE C  1 177 ? 48.907  -5.617  -23.104 1.00 32.14  ? 177 PHE C CZ  1 
ATOM   5824  N  N   . ASN C  1 178 ? 53.506  -7.990  -24.659 1.00 25.88  ? 178 ASN C N   1 
ATOM   5825  C  CA  . ASN C  1 178 ? 53.323  -8.300  -26.014 1.00 27.91  ? 178 ASN C CA  1 
ATOM   5826  C  C   . ASN C  1 178 ? 51.907  -8.173  -26.496 1.00 22.71  ? 178 ASN C C   1 
ATOM   5827  O  O   . ASN C  1 178 ? 51.081  -9.101  -26.353 1.00 32.38  ? 178 ASN C O   1 
ATOM   5828  C  CB  . ASN C  1 178 ? 53.726  -9.732  -26.205 1.00 25.78  ? 178 ASN C CB  1 
ATOM   5829  C  CG  . ASN C  1 178 ? 53.739  -10.115 -27.675 1.00 29.89  ? 178 ASN C CG  1 
ATOM   5830  O  OD1 . ASN C  1 178 ? 53.488  -9.292  -28.607 1.00 25.31  ? 178 ASN C OD1 1 
ATOM   5831  N  ND2 . ASN C  1 178 ? 53.884  -11.379 -27.900 1.00 26.94  ? 178 ASN C ND2 1 
ATOM   5832  N  N   . ILE C  1 179 ? 51.732  -7.000  -27.184 1.00 21.57  ? 179 ILE C N   1 
ATOM   5833  C  CA  . ILE C  1 179 ? 50.427  -6.577  -27.648 1.00 20.62  ? 179 ILE C CA  1 
ATOM   5834  C  C   . ILE C  1 179 ? 49.770  -7.677  -28.557 1.00 18.37  ? 179 ILE C C   1 
ATOM   5835  O  O   . ILE C  1 179 ? 48.531  -7.880  -28.681 1.00 21.91  ? 179 ILE C O   1 
ATOM   5836  C  CB  . ILE C  1 179 ? 50.509  -5.185  -28.284 1.00 20.46  ? 179 ILE C CB  1 
ATOM   5837  C  CG1 . ILE C  1 179 ? 51.125  -4.145  -27.331 1.00 21.94  ? 179 ILE C CG1 1 
ATOM   5838  C  CG2 . ILE C  1 179 ? 49.106  -4.846  -28.824 1.00 22.81  ? 179 ILE C CG2 1 
ATOM   5839  C  CD1 . ILE C  1 179 ? 50.405  -3.872  -25.969 1.00 20.97  ? 179 ILE C CD1 1 
ATOM   5840  N  N   . GLU C  1 180 ? 50.583  -8.413  -29.259 1.00 18.44  ? 180 GLU C N   1 
ATOM   5841  C  CA  . GLU C  1 180 ? 50.134  -9.553  -30.032 1.00 17.82  ? 180 GLU C CA  1 
ATOM   5842  C  C   . GLU C  1 180 ? 49.218  -10.579 -29.329 1.00 24.12  ? 180 GLU C C   1 
ATOM   5843  O  O   . GLU C  1 180 ? 48.401  -11.297 -29.977 1.00 26.95  ? 180 GLU C O   1 
ATOM   5844  C  CB  . GLU C  1 180 ? 51.201  -10.199 -30.912 1.00 24.88  ? 180 GLU C CB  1 
ATOM   5845  C  CG  . GLU C  1 180 ? 50.628  -11.110 -31.974 1.00 25.78  ? 180 GLU C CG  1 
ATOM   5846  C  CD  . GLU C  1 180 ? 51.630  -11.510 -33.060 1.00 32.69  ? 180 GLU C CD  1 
ATOM   5847  O  OE1 . GLU C  1 180 ? 52.795  -11.096 -32.889 1.00 31.65  ? 180 GLU C OE1 1 
ATOM   5848  O  OE2 . GLU C  1 180 ? 51.314  -12.277 -34.034 1.00 37.04  ? 180 GLU C OE2 1 
ATOM   5849  N  N   . GLU C  1 181 ? 49.456  -10.738 -28.038 1.00 25.47  ? 181 GLU C N   1 
ATOM   5850  C  CA  . GLU C  1 181 ? 48.641  -11.641 -27.284 1.00 25.76  ? 181 GLU C CA  1 
ATOM   5851  C  C   . GLU C  1 181 ? 47.167  -11.176 -27.141 1.00 23.01  ? 181 GLU C C   1 
ATOM   5852  O  O   . GLU C  1 181 ? 46.356  -12.041 -26.706 1.00 27.61  ? 181 GLU C O   1 
ATOM   5853  C  CB  . GLU C  1 181 ? 49.248  -11.813 -25.900 1.00 37.19  ? 181 GLU C CB  1 
ATOM   5854  C  CG  . GLU C  1 181 ? 50.691  -12.402 -25.859 1.00 47.56  ? 181 GLU C CG  1 
ATOM   5855  C  CD  . GLU C  1 181 ? 51.363  -12.247 -24.475 1.00 57.47  ? 181 GLU C CD  1 
ATOM   5856  O  OE1 . GLU C  1 181 ? 50.643  -11.839 -23.553 1.00 39.18  ? 181 GLU C OE1 1 
ATOM   5857  O  OE2 . GLU C  1 181 ? 52.600  -12.501 -24.320 1.00 58.93  ? 181 GLU C OE2 1 
ATOM   5858  N  N   . LEU C  1 182 ? 46.885  -9.874  -27.399 1.00 20.64  ? 182 LEU C N   1 
ATOM   5859  C  CA  . LEU C  1 182 ? 45.482  -9.323  -27.429 1.00 17.58  ? 182 LEU C CA  1 
ATOM   5860  C  C   . LEU C  1 182 ? 44.709  -9.897  -28.659 1.00 20.18  ? 182 LEU C C   1 
ATOM   5861  O  O   . LEU C  1 182 ? 43.476  -9.827  -28.728 1.00 19.23  ? 182 LEU C O   1 
ATOM   5862  C  CB  . LEU C  1 182 ? 45.496  -7.783  -27.342 1.00 20.25  ? 182 LEU C CB  1 
ATOM   5863  C  CG  . LEU C  1 182 ? 46.181  -7.135  -26.086 1.00 17.43  ? 182 LEU C CG  1 
ATOM   5864  C  CD1 . LEU C  1 182 ? 46.046  -5.655  -26.000 1.00 19.23  ? 182 LEU C CD1 1 
ATOM   5865  C  CD2 . LEU C  1 182 ? 45.680  -7.758  -24.720 1.00 22.86  ? 182 LEU C CD2 1 
ATOM   5866  N  N   . LEU C  1 183 ? 45.424  -10.411 -29.653 1.00 20.68  ? 183 LEU C N   1 
ATOM   5867  C  CA  . LEU C  1 183 ? 44.790  -10.720 -30.913 1.00 19.57  ? 183 LEU C CA  1 
ATOM   5868  C  C   . LEU C  1 183 ? 44.246  -12.097 -30.853 1.00 16.91  ? 183 LEU C C   1 
ATOM   5869  O  O   . LEU C  1 183 ? 44.737  -12.979 -30.053 1.00 25.87  ? 183 LEU C O   1 
ATOM   5870  C  CB  . LEU C  1 183 ? 45.754  -10.578 -32.115 1.00 18.35  ? 183 LEU C CB  1 
ATOM   5871  C  CG  . LEU C  1 183 ? 46.406  -9.258  -32.298 1.00 21.31  ? 183 LEU C CG  1 
ATOM   5872  C  CD1 . LEU C  1 183 ? 47.183  -9.226  -33.594 1.00 23.22  ? 183 LEU C CD1 1 
ATOM   5873  C  CD2 . LEU C  1 183 ? 45.369  -8.182  -32.420 1.00 25.27  ? 183 LEU C CD2 1 
ATOM   5874  N  N   . PRO C  1 184 ? 43.220  -12.397 -31.604 1.00 18.01  ? 184 PRO C N   1 
ATOM   5875  C  CA  . PRO C  1 184 ? 42.635  -13.692 -31.550 1.00 18.68  ? 184 PRO C CA  1 
ATOM   5876  C  C   . PRO C  1 184 ? 43.388  -14.752 -32.269 1.00 19.99  ? 184 PRO C C   1 
ATOM   5877  O  O   . PRO C  1 184 ? 44.462  -14.550 -32.931 1.00 25.82  ? 184 PRO C O   1 
ATOM   5878  C  CB  . PRO C  1 184 ? 41.188  -13.494 -32.091 1.00 22.40  ? 184 PRO C CB  1 
ATOM   5879  C  CG  . PRO C  1 184 ? 41.561  -12.560 -33.147 1.00 21.87  ? 184 PRO C CG  1 
ATOM   5880  C  CD  . PRO C  1 184 ? 42.486  -11.556 -32.509 1.00 17.23  ? 184 PRO C CD  1 
ATOM   5881  N  N   . GLU C  1 185 ? 42.829  -15.943 -32.221 1.00 26.82  ? 185 GLU C N   1 
ATOM   5882  C  CA  . GLU C  1 185 ? 43.251  -17.051 -33.056 1.00 28.06  ? 185 GLU C CA  1 
ATOM   5883  C  C   . GLU C  1 185 ? 42.950  -16.822 -34.563 1.00 22.35  ? 185 GLU C C   1 
ATOM   5884  O  O   . GLU C  1 185 ? 41.921  -16.159 -34.912 1.00 23.45  ? 185 GLU C O   1 
ATOM   5885  C  CB  . GLU C  1 185 ? 42.545  -18.344 -32.679 1.00 32.85  ? 185 GLU C CB  1 
ATOM   5886  C  CG  . GLU C  1 185 ? 42.779  -18.827 -31.249 1.00 42.01  ? 185 GLU C CG  1 
ATOM   5887  C  CD  . GLU C  1 185 ? 44.042  -19.671 -31.046 1.00 51.31  ? 185 GLU C CD  1 
ATOM   5888  O  OE1 . GLU C  1 185 ? 44.976  -19.584 -31.878 1.00 47.37  ? 185 GLU C OE1 1 
ATOM   5889  O  OE2 . GLU C  1 185 ? 44.112  -20.451 -30.038 1.00 66.82  ? 185 GLU C OE2 1 
ATOM   5890  N  N   . ARG C  1 186 ? 43.871  -17.381 -35.380 1.00 24.97  ? 186 ARG C N   1 
ATOM   5891  C  CA  . ARG C  1 186 ? 43.742  -17.300 -36.830 1.00 25.65  ? 186 ARG C CA  1 
ATOM   5892  C  C   . ARG C  1 186 ? 43.620  -15.893 -37.339 1.00 17.59  ? 186 ARG C C   1 
ATOM   5893  O  O   . ARG C  1 186 ? 42.564  -15.537 -38.026 1.00 21.08  ? 186 ARG C O   1 
ATOM   5894  C  CB  . ARG C  1 186 ? 42.625  -18.233 -37.321 1.00 26.47  ? 186 ARG C CB  1 
ATOM   5895  C  CG  . ARG C  1 186 ? 42.911  -19.616 -36.921 1.00 27.33  ? 186 ARG C CG  1 
ATOM   5896  C  CD  . ARG C  1 186 ? 41.769  -20.547 -37.245 1.00 31.64  ? 186 ARG C CD  1 
ATOM   5897  N  NE  . ARG C  1 186 ? 40.737  -20.463 -36.182 1.00 50.90  ? 186 ARG C NE  1 
ATOM   5898  C  CZ  . ARG C  1 186 ? 39.435  -20.706 -36.348 1.00 51.23  ? 186 ARG C CZ  1 
ATOM   5899  N  NH1 . ARG C  1 186 ? 38.959  -21.061 -37.535 1.00 69.16  ? 186 ARG C NH1 1 
ATOM   5900  N  NH2 . ARG C  1 186 ? 38.599  -20.576 -35.320 1.00 59.40  ? 186 ARG C NH2 1 
ATOM   5901  N  N   . THR C  1 187 ? 44.571  -15.032 -36.992 1.00 18.25  ? 187 THR C N   1 
ATOM   5902  C  CA  . THR C  1 187 ? 44.546  -13.680 -37.487 1.00 16.78  ? 187 THR C CA  1 
ATOM   5903  C  C   . THR C  1 187 ? 44.454  -13.600 -39.012 1.00 20.52  ? 187 THR C C   1 
ATOM   5904  O  O   . THR C  1 187 ? 44.139  -12.543 -39.500 1.00 19.31  ? 187 THR C O   1 
ATOM   5905  C  CB  . THR C  1 187 ? 45.660  -12.805 -36.889 1.00 19.53  ? 187 THR C CB  1 
ATOM   5906  O  OG1 . THR C  1 187 ? 46.892  -13.445 -37.078 1.00 24.28  ? 187 THR C OG1 1 
ATOM   5907  C  CG2 . THR C  1 187 ? 45.430  -12.521 -35.417 1.00 19.43  ? 187 THR C CG2 1 
ATOM   5908  N  N   . ALA C  1 188 ? 44.747  -14.703 -39.733 1.00 18.01  ? 188 ALA C N   1 
ATOM   5909  C  CA  . ALA C  1 188 ? 44.615  -14.692 -41.181 1.00 19.27  ? 188 ALA C CA  1 
ATOM   5910  C  C   . ALA C  1 188 ? 43.190  -14.474 -41.635 1.00 14.62  ? 188 ALA C C   1 
ATOM   5911  O  O   . ALA C  1 188 ? 42.980  -14.063 -42.775 1.00 15.01  ? 188 ALA C O   1 
ATOM   5912  C  CB  . ALA C  1 188 ? 45.200  -15.974 -41.802 1.00 24.55  ? 188 ALA C CB  1 
ATOM   5913  N  N   . GLU C  1 189 ? 42.209  -14.771 -40.778 1.00 16.14  ? 189 GLU C N   1 
ATOM   5914  C  CA  . GLU C  1 189 ? 40.804  -14.664 -41.144 1.00 15.62  ? 189 GLU C CA  1 
ATOM   5915  C  C   . GLU C  1 189 ? 40.257  -13.316 -40.648 1.00 14.94  ? 189 GLU C C   1 
ATOM   5916  O  O   . GLU C  1 189 ? 40.229  -13.105 -39.407 1.00 13.41  ? 189 GLU C O   1 
ATOM   5917  C  CB  . GLU C  1 189 ? 39.959  -15.757 -40.476 1.00 19.41  ? 189 GLU C CB  1 
ATOM   5918  C  CG  . GLU C  1 189 ? 40.500  -17.162 -40.828 1.00 24.52  ? 189 GLU C CG  1 
ATOM   5919  C  CD  . GLU C  1 189 ? 39.577  -18.214 -40.234 1.00 34.00  ? 189 GLU C CD  1 
ATOM   5920  O  OE1 . GLU C  1 189 ? 39.013  -18.132 -39.100 1.00 31.99  ? 189 GLU C OE1 1 
ATOM   5921  O  OE2 . GLU C  1 189 ? 39.528  -19.306 -40.854 1.00 55.61  ? 189 GLU C OE2 1 
ATOM   5922  N  N   . TYR C  1 190 ? 39.831  -12.461 -41.557 1.00 11.82  ? 190 TYR C N   1 
ATOM   5923  C  CA  . TYR C  1 190 ? 39.392  -11.129 -41.169 1.00 10.98  ? 190 TYR C CA  1 
ATOM   5924  C  C   . TYR C  1 190 ? 38.423  -10.595 -42.209 1.00 9.93   ? 190 TYR C C   1 
ATOM   5925  O  O   . TYR C  1 190 ? 38.449  -10.975 -43.383 1.00 11.70  ? 190 TYR C O   1 
ATOM   5926  C  CB  . TYR C  1 190 ? 40.578  -10.190 -40.881 1.00 11.36  ? 190 TYR C CB  1 
ATOM   5927  C  CG  . TYR C  1 190 ? 41.545  -9.987  -42.020 1.00 11.23  ? 190 TYR C CG  1 
ATOM   5928  C  CD1 . TYR C  1 190 ? 41.304  -9.121  -43.055 1.00 10.95  ? 190 TYR C CD1 1 
ATOM   5929  C  CD2 . TYR C  1 190 ? 42.749  -10.720 -42.029 1.00 13.50  ? 190 TYR C CD2 1 
ATOM   5930  C  CE1 . TYR C  1 190 ? 42.221  -8.930  -44.071 1.00 11.40  ? 190 TYR C CE1 1 
ATOM   5931  C  CE2 . TYR C  1 190 ? 43.657  -10.554 -43.073 1.00 12.83  ? 190 TYR C CE2 1 
ATOM   5932  C  CZ  . TYR C  1 190 ? 43.403  -9.640  -44.064 1.00 12.58  ? 190 TYR C CZ  1 
ATOM   5933  O  OH  . TYR C  1 190 ? 44.285  -9.418  -45.113 1.00 13.64  ? 190 TYR C OH  1 
ATOM   5934  N  N   . TYR C  1 191 ? 37.653  -9.583  -41.767 1.00 9.98   ? 191 TYR C N   1 
ATOM   5935  C  CA  . TYR C  1 191 ? 36.849  -8.725  -42.589 1.00 9.50   ? 191 TYR C CA  1 
ATOM   5936  C  C   . TYR C  1 191 ? 37.614  -7.417  -42.831 1.00 8.63   ? 191 TYR C C   1 
ATOM   5937  O  O   . TYR C  1 191 ? 38.313  -6.942  -41.943 1.00 9.95   ? 191 TYR C O   1 
ATOM   5938  C  CB  . TYR C  1 191 ? 35.590  -8.312  -41.819 1.00 9.50   ? 191 TYR C CB  1 
ATOM   5939  C  CG  . TYR C  1 191 ? 34.748  -9.456  -41.270 1.00 10.28  ? 191 TYR C CG  1 
ATOM   5940  C  CD1 . TYR C  1 191 ? 33.705  -10.019 -42.012 1.00 10.47  ? 191 TYR C CD1 1 
ATOM   5941  C  CD2 . TYR C  1 191 ? 34.922  -9.914  -39.959 1.00 10.62  ? 191 TYR C CD2 1 
ATOM   5942  C  CE1 . TYR C  1 191 ? 32.864  -11.006 -41.528 1.00 11.52  ? 191 TYR C CE1 1 
ATOM   5943  C  CE2 . TYR C  1 191 ? 34.053  -10.878 -39.427 1.00 11.87  ? 191 TYR C CE2 1 
ATOM   5944  C  CZ  . TYR C  1 191 ? 33.072  -11.413 -40.190 1.00 11.13  ? 191 TYR C CZ  1 
ATOM   5945  O  OH  . TYR C  1 191 ? 32.225  -12.367 -39.648 1.00 14.70  ? 191 TYR C OH  1 
ATOM   5946  N  N   . ARG C  1 192 ? 37.416  -6.864  -44.026 1.00 9.27   ? 192 ARG C N   1 
ATOM   5947  C  CA  . ARG C  1 192 ? 38.114  -5.615  -44.395 1.00 8.60   ? 192 ARG C CA  1 
ATOM   5948  C  C   . ARG C  1 192 ? 37.136  -4.681  -45.065 1.00 8.04   ? 192 ARG C C   1 
ATOM   5949  O  O   . ARG C  1 192 ? 36.417  -5.083  -46.000 1.00 9.00   ? 192 ARG C O   1 
ATOM   5950  C  CB  . ARG C  1 192 ? 39.228  -5.981  -45.362 1.00 10.04  ? 192 ARG C CB  1 
ATOM   5951  C  CG  . ARG C  1 192 ? 39.872  -4.840  -46.169 1.00 11.12  ? 192 ARG C CG  1 
ATOM   5952  C  CD  . ARG C  1 192 ? 40.652  -3.843  -45.307 1.00 10.95  ? 192 ARG C CD  1 
ATOM   5953  N  NE  . ARG C  1 192 ? 41.599  -4.453  -44.416 1.00 11.59  ? 192 ARG C NE  1 
ATOM   5954  C  CZ  . ARG C  1 192 ? 42.756  -4.968  -44.802 1.00 11.11  ? 192 ARG C CZ  1 
ATOM   5955  N  NH1 . ARG C  1 192 ? 43.128  -4.903  -46.093 1.00 13.01  ? 192 ARG C NH1 1 
ATOM   5956  N  NH2 . ARG C  1 192 ? 43.560  -5.556  -43.936 1.00 13.13  ? 192 ARG C NH2 1 
ATOM   5957  N  N   . TYR C  1 193 ? 37.146  -3.413  -44.673 1.00 7.77   ? 193 TYR C N   1 
ATOM   5958  C  CA  . TYR C  1 193 ? 36.389  -2.408  -45.439 1.00 8.15   ? 193 TYR C CA  1 
ATOM   5959  C  C   . TYR C  1 193 ? 36.983  -1.057  -45.124 1.00 7.86   ? 193 TYR C C   1 
ATOM   5960  O  O   . TYR C  1 193 ? 37.660  -0.852  -44.093 1.00 8.74   ? 193 TYR C O   1 
ATOM   5961  C  CB  . TYR C  1 193 ? 34.881  -2.454  -45.117 1.00 8.47   ? 193 TYR C CB  1 
ATOM   5962  C  CG  . TYR C  1 193 ? 34.494  -1.943  -43.744 1.00 7.46   ? 193 TYR C CG  1 
ATOM   5963  C  CD1 . TYR C  1 193 ? 34.696  -2.723  -42.588 1.00 8.15   ? 193 TYR C CD1 1 
ATOM   5964  C  CD2 . TYR C  1 193 ? 33.953  -0.681  -43.619 1.00 8.01   ? 193 TYR C CD2 1 
ATOM   5965  C  CE1 . TYR C  1 193 ? 34.353  -2.188  -41.332 1.00 8.10   ? 193 TYR C CE1 1 
ATOM   5966  C  CE2 . TYR C  1 193 ? 33.580  -0.186  -42.393 1.00 8.34   ? 193 TYR C CE2 1 
ATOM   5967  C  CZ  . TYR C  1 193 ? 33.822  -0.933  -41.254 1.00 7.63   ? 193 TYR C CZ  1 
ATOM   5968  O  OH  . TYR C  1 193 ? 33.507  -0.379  -40.021 1.00 7.65   ? 193 TYR C OH  1 
ATOM   5969  N  N   . ARG C  1 194 ? 36.668  -0.078  -45.979 1.00 7.92   ? 194 ARG C N   1 
ATOM   5970  C  CA  . ARG C  1 194 ? 37.063  1.304   -45.754 1.00 8.56   ? 194 ARG C CA  1 
ATOM   5971  C  C   . ARG C  1 194 ? 35.924  2.010   -44.964 1.00 7.59   ? 194 ARG C C   1 
ATOM   5972  O  O   . ARG C  1 194 ? 34.767  1.995   -45.357 1.00 9.05   ? 194 ARG C O   1 
ATOM   5973  C  CB  . ARG C  1 194 ? 37.261  2.048   -47.068 1.00 11.34  ? 194 ARG C CB  1 
ATOM   5974  C  CG  . ARG C  1 194 ? 38.435  1.523   -47.872 1.00 15.72  ? 194 ARG C CG  1 
ATOM   5975  C  CD  . ARG C  1 194 ? 38.988  2.460   -48.922 1.00 33.76  ? 194 ARG C CD  1 
ATOM   5976  N  NE  . ARG C  1 194 ? 40.176  1.796   -49.425 1.00 54.27  ? 194 ARG C NE  1 
ATOM   5977  C  CZ  . ARG C  1 194 ? 41.408  2.080   -49.030 1.00 61.10  ? 194 ARG C CZ  1 
ATOM   5978  N  NH1 . ARG C  1 194 ? 41.625  3.068   -48.169 1.00 30.95  ? 194 ARG C NH1 1 
ATOM   5979  N  NH2 . ARG C  1 194 ? 42.425  1.388   -49.520 1.00 60.90  ? 194 ARG C NH2 1 
ATOM   5980  N  N   . GLY C  1 195 ? 36.321  2.615   -43.866 1.00 7.87   ? 195 GLY C N   1 
ATOM   5981  C  CA  . GLY C  1 195 ? 35.345  3.303   -43.019 1.00 8.29   ? 195 GLY C CA  1 
ATOM   5982  C  C   . GLY C  1 195 ? 35.944  4.468   -42.315 1.00 8.01   ? 195 GLY C C   1 
ATOM   5983  O  O   . GLY C  1 195 ? 36.797  5.205   -42.873 1.00 9.02   ? 195 GLY C O   1 
ATOM   5984  N  N   . SER C  1 196 ? 35.493  4.702   -41.084 1.00 7.90   ? 196 SER C N   1 
ATOM   5985  C  CA  . SER C  1 196 ? 35.771  5.954   -40.417 1.00 8.83   ? 196 SER C CA  1 
ATOM   5986  C  C   . SER C  1 196 ? 36.218  5.680   -38.977 1.00 8.51   ? 196 SER C C   1 
ATOM   5987  O  O   . SER C  1 196 ? 36.052  4.579   -38.449 1.00 8.90   ? 196 SER C O   1 
ATOM   5988  C  CB  . SER C  1 196 ? 34.526  6.859   -40.338 1.00 8.86   ? 196 SER C CB  1 
ATOM   5989  O  OG  . SER C  1 196 ? 33.557  6.373   -39.431 1.00 8.52   ? 196 SER C OG  1 
ATOM   5990  N  N   . LEU C  1 197 ? 36.707  6.747   -38.322 1.00 9.03   ? 197 LEU C N   1 
ATOM   5991  C  CA  . LEU C  1 197 ? 36.749  6.704   -36.869 1.00 9.62   ? 197 LEU C CA  1 
ATOM   5992  C  C   . LEU C  1 197 ? 35.319  6.477   -36.378 1.00 9.01   ? 197 LEU C C   1 
ATOM   5993  O  O   . LEU C  1 197 ? 34.381  7.082   -36.914 1.00 9.04   ? 197 LEU C O   1 
ATOM   5994  C  CB  . LEU C  1 197 ? 37.261  8.021   -36.263 1.00 10.86  ? 197 LEU C CB  1 
ATOM   5995  C  CG  . LEU C  1 197 ? 38.802  8.288   -36.397 1.00 12.44  ? 197 LEU C CG  1 
ATOM   5996  C  CD1 . LEU C  1 197 ? 39.118  8.818   -37.787 1.00 13.96  ? 197 LEU C CD1 1 
ATOM   5997  C  CD2 . LEU C  1 197 ? 39.065  9.409   -35.390 1.00 18.59  ? 197 LEU C CD2 1 
ATOM   5998  N  N   . THR C  1 198 ? 35.158  5.716   -35.294 1.00 9.80   ? 198 THR C N   1 
ATOM   5999  C  CA  . THR C  1 198 ? 33.833  5.562   -34.674 1.00 9.45   ? 198 THR C CA  1 
ATOM   6000  C  C   . THR C  1 198 ? 33.592  6.560   -33.603 1.00 10.12  ? 198 THR C C   1 
ATOM   6001  O  O   . THR C  1 198 ? 32.514  6.566   -32.981 1.00 10.63  ? 198 THR C O   1 
ATOM   6002  C  CB  . THR C  1 198 ? 33.660  4.184   -34.083 1.00 8.87   ? 198 THR C CB  1 
ATOM   6003  O  OG1 . THR C  1 198 ? 34.558  4.076   -33.009 1.00 9.58   ? 198 THR C OG1 1 
ATOM   6004  C  CG2 . THR C  1 198 ? 33.893  3.055   -35.108 1.00 9.78   ? 198 THR C CG2 1 
ATOM   6005  N  N   . THR C  1 199 ? 34.525  7.455   -33.400 1.00 10.01  ? 199 THR C N   1 
ATOM   6006  C  CA  . THR C  1 199 ? 34.409  8.605   -32.446 1.00 10.98  ? 199 THR C CA  1 
ATOM   6007  C  C   . THR C  1 199 ? 34.613  9.880   -33.212 1.00 10.21  ? 199 THR C C   1 
ATOM   6008  O  O   . THR C  1 199 ? 35.338  9.868   -34.221 1.00 11.06  ? 199 THR C O   1 
ATOM   6009  C  CB  . THR C  1 199 ? 35.563  8.535   -31.402 1.00 13.31  ? 199 THR C CB  1 
ATOM   6010  O  OG1 . THR C  1 199 ? 36.840  8.430   -32.085 1.00 15.96  ? 199 THR C OG1 1 
ATOM   6011  C  CG2 . THR C  1 199 ? 35.398  7.308   -30.555 1.00 14.06  ? 199 THR C CG2 1 
ATOM   6012  N  N   . PRO C  1 200 ? 34.133  11.007  -32.676 1.00 10.48  ? 200 PRO C N   1 
ATOM   6013  C  CA  . PRO C  1 200 ? 34.504  12.302  -33.308 1.00 11.38  ? 200 PRO C CA  1 
ATOM   6014  C  C   . PRO C  1 200 ? 36.011  12.381  -33.441 1.00 11.65  ? 200 PRO C C   1 
ATOM   6015  O  O   . PRO C  1 200 ? 36.728  11.983  -32.506 1.00 14.36  ? 200 PRO C O   1 
ATOM   6016  C  CB  . PRO C  1 200 ? 33.958  13.284  -32.243 1.00 12.19  ? 200 PRO C CB  1 
ATOM   6017  C  CG  . PRO C  1 200 ? 32.696  12.609  -31.749 1.00 13.41  ? 200 PRO C CG  1 
ATOM   6018  C  CD  . PRO C  1 200 ? 33.191  11.155  -31.552 1.00 12.10  ? 200 PRO C CD  1 
ATOM   6019  N  N   . PRO C  1 201 ? 36.508  12.941  -34.523 1.00 12.03  ? 201 PRO C N   1 
ATOM   6020  C  CA  . PRO C  1 201 ? 35.744  13.674  -35.570 1.00 11.44  ? 201 PRO C CA  1 
ATOM   6021  C  C   . PRO C  1 201 ? 35.172  12.745  -36.661 1.00 10.10  ? 201 PRO C C   1 
ATOM   6022  O  O   . PRO C  1 201 ? 34.684  13.328  -37.653 1.00 10.85  ? 201 PRO C O   1 
ATOM   6023  C  CB  . PRO C  1 201 ? 36.767  14.660  -36.150 1.00 12.09  ? 201 PRO C CB  1 
ATOM   6024  C  CG  . PRO C  1 201 ? 37.883  14.698  -35.188 1.00 13.87  ? 201 PRO C CG  1 
ATOM   6025  C  CD  . PRO C  1 201 ? 37.945  13.299  -34.616 1.00 13.58  ? 201 PRO C CD  1 
ATOM   6026  N  N   . CYS C  1 202 ? 35.233  11.413  -36.512 1.00 9.67   ? 202 CYS C N   1 
ATOM   6027  C  CA  . CYS C  1 202 ? 34.555  10.545  -37.473 1.00 8.94   ? 202 CYS C CA  1 
ATOM   6028  C  C   . CYS C  1 202 ? 35.115  10.607  -38.889 1.00 9.32   ? 202 CYS C C   1 
ATOM   6029  O  O   . CYS C  1 202 ? 34.411  10.294  -39.834 1.00 9.51   ? 202 CYS C O   1 
ATOM   6030  C  CB  . CYS C  1 202 ? 33.065  10.744  -37.507 1.00 9.36   ? 202 CYS C CB  1 
ATOM   6031  S  SG  . CYS C  1 202 ? 32.159  10.719  -35.969 1.00 10.15  ? 202 CYS C SG  1 
ATOM   6032  N  N   . ASN C  1 203 ? 36.393  10.959  -39.022 1.00 9.64   ? 203 ASN C N   1 
ATOM   6033  C  CA  . ASN C  1 203 ? 36.907  11.138  -40.357 1.00 10.54  ? 203 ASN C CA  1 
ATOM   6034  C  C   . ASN C  1 203 ? 36.871  9.803   -41.117 1.00 9.49   ? 203 ASN C C   1 
ATOM   6035  O  O   . ASN C  1 203 ? 37.161  8.747   -40.531 1.00 9.05   ? 203 ASN C O   1 
ATOM   6036  C  CB  . ASN C  1 203 ? 38.396  11.582  -40.281 1.00 12.61  ? 203 ASN C CB  1 
ATOM   6037  C  CG  . ASN C  1 203 ? 38.515  12.797  -39.396 1.00 12.90  ? 203 ASN C CG  1 
ATOM   6038  O  OD1 . ASN C  1 203 ? 38.592  12.649  -38.215 1.00 13.61  ? 203 ASN C OD1 1 
ATOM   6039  N  ND2 . ASN C  1 203 ? 38.484  13.989  -39.962 1.00 14.93  ? 203 ASN C ND2 1 
ATOM   6040  N  N   . PRO C  1 204 ? 36.568  9.876   -42.412 1.00 9.44   ? 204 PRO C N   1 
ATOM   6041  C  CA  . PRO C  1 204 ? 36.407  8.610   -43.216 1.00 10.14  ? 204 PRO C CA  1 
ATOM   6042  C  C   . PRO C  1 204 ? 37.752  8.161   -43.751 1.00 9.52   ? 204 PRO C C   1 
ATOM   6043  O  O   . PRO C  1 204 ? 37.939  7.994   -44.970 1.00 11.54  ? 204 PRO C O   1 
ATOM   6044  C  CB  . PRO C  1 204 ? 35.468  9.072   -44.331 1.00 11.65  ? 204 PRO C CB  1 
ATOM   6045  C  CG  . PRO C  1 204 ? 35.833  10.521  -44.532 1.00 12.37  ? 204 PRO C CG  1 
ATOM   6046  C  CD  . PRO C  1 204 ? 36.109  11.094  -43.144 1.00 11.66  ? 204 PRO C CD  1 
ATOM   6047  N  N   . THR C  1 205 ? 38.688  7.921   -42.817 1.00 9.69   ? 205 THR C N   1 
ATOM   6048  C  CA  . THR C  1 205 ? 40.088  7.755   -43.162 1.00 10.54  ? 205 THR C CA  1 
ATOM   6049  C  C   . THR C  1 205 ? 40.663  6.434   -42.622 1.00 10.37  ? 205 THR C C   1 
ATOM   6050  O  O   . THR C  1 205 ? 41.867  6.247   -42.612 1.00 11.27  ? 205 THR C O   1 
ATOM   6051  C  CB  . THR C  1 205 ? 40.892  8.930   -42.612 1.00 10.95  ? 205 THR C CB  1 
ATOM   6052  O  OG1 . THR C  1 205 ? 40.625  8.904   -41.211 1.00 11.94  ? 205 THR C OG1 1 
ATOM   6053  C  CG2 . THR C  1 205 ? 40.500  10.262  -43.235 1.00 12.55  ? 205 THR C CG2 1 
ATOM   6054  N  N   . VAL C  1 206 ? 39.760  5.501   -42.182 1.00 9.34   ? 206 VAL C N   1 
ATOM   6055  C  CA  . VAL C  1 206 ? 40.196  4.264   -41.554 1.00 9.77   ? 206 VAL C CA  1 
ATOM   6056  C  C   . VAL C  1 206 ? 40.045  3.046   -42.454 1.00 8.96   ? 206 VAL C C   1 
ATOM   6057  O  O   . VAL C  1 206 ? 38.957  2.751   -42.956 1.00 9.99   ? 206 VAL C O   1 
ATOM   6058  C  CB  . VAL C  1 206 ? 39.434  4.000   -40.255 1.00 9.33   ? 206 VAL C CB  1 
ATOM   6059  C  CG1 . VAL C  1 206 ? 39.896  2.658   -39.668 1.00 9.41   ? 206 VAL C CG1 1 
ATOM   6060  C  CG2 . VAL C  1 206 ? 39.680  5.129   -39.242 1.00 11.30  ? 206 VAL C CG2 1 
ATOM   6061  N  N   . LEU C  1 207 ? 41.157  2.325   -42.613 1.00 9.12   ? 207 LEU C N   1 
ATOM   6062  C  CA  . LEU C  1 207 ? 41.126  0.982   -43.233 1.00 9.67   ? 207 LEU C CA  1 
ATOM   6063  C  C   . LEU C  1 207 ? 40.826  0.046   -42.043 1.00 8.44   ? 207 LEU C C   1 
ATOM   6064  O  O   . LEU C  1 207 ? 41.708  -0.115  -41.181 1.00 9.14   ? 207 LEU C O   1 
ATOM   6065  C  CB  . LEU C  1 207 ? 42.469  0.695   -43.904 1.00 11.34  ? 207 LEU C CB  1 
ATOM   6066  C  CG  . LEU C  1 207 ? 42.459  -0.534  -44.795 1.00 15.30  ? 207 LEU C CG  1 
ATOM   6067  C  CD1 . LEU C  1 207 ? 41.408  -0.349  -45.948 1.00 20.20  ? 207 LEU C CD1 1 
ATOM   6068  C  CD2 . LEU C  1 207 ? 43.921  -0.674  -45.307 1.00 27.92  ? 207 LEU C CD2 1 
ATOM   6069  N  N   . TRP C  1 208 ? 39.656  -0.581  -42.024 1.00 8.28   ? 208 TRP C N   1 
ATOM   6070  C  CA  . TRP C  1 208 ? 39.264  -1.472  -40.941 1.00 8.72   ? 208 TRP C CA  1 
ATOM   6071  C  C   . TRP C  1 208 ? 39.649  -2.900  -41.227 1.00 7.92   ? 208 TRP C C   1 
ATOM   6072  O  O   . TRP C  1 208 ? 39.423  -3.412  -42.348 1.00 9.22   ? 208 TRP C O   1 
ATOM   6073  C  CB  . TRP C  1 208 ? 37.751  -1.432  -40.709 1.00 8.68   ? 208 TRP C CB  1 
ATOM   6074  C  CG  . TRP C  1 208 ? 37.348  -0.225  -39.911 1.00 7.80   ? 208 TRP C CG  1 
ATOM   6075  C  CD1 . TRP C  1 208 ? 36.875  0.958   -40.376 1.00 8.58   ? 208 TRP C CD1 1 
ATOM   6076  C  CD2 . TRP C  1 208 ? 37.448  -0.112  -38.495 1.00 7.46   ? 208 TRP C CD2 1 
ATOM   6077  N  NE1 . TRP C  1 208 ? 36.716  1.833   -39.342 1.00 8.28   ? 208 TRP C NE1 1 
ATOM   6078  C  CE2 . TRP C  1 208 ? 37.025  1.200   -38.167 1.00 8.66   ? 208 TRP C CE2 1 
ATOM   6079  C  CE3 . TRP C  1 208 ? 37.849  -0.969  -37.488 1.00 9.15   ? 208 TRP C CE3 1 
ATOM   6080  C  CZ2 . TRP C  1 208 ? 37.039  1.686   -36.853 1.00 9.79   ? 208 TRP C CZ2 1 
ATOM   6081  C  CZ3 . TRP C  1 208 ? 37.791  -0.486  -36.153 1.00 10.16  ? 208 TRP C CZ3 1 
ATOM   6082  C  CH2 . TRP C  1 208 ? 37.418  0.818   -35.869 1.00 10.52  ? 208 TRP C CH2 1 
ATOM   6083  N  N   . THR C  1 209 ? 40.182  -3.564  -40.230 1.00 8.86   ? 209 THR C N   1 
ATOM   6084  C  CA  . THR C  1 209 ? 40.398  -4.968  -40.265 1.00 9.03   ? 209 THR C CA  1 
ATOM   6085  C  C   . THR C  1 209 ? 39.755  -5.529  -38.983 1.00 9.86   ? 209 THR C C   1 
ATOM   6086  O  O   . THR C  1 209 ? 40.175  -5.177  -37.906 1.00 11.03  ? 209 THR C O   1 
ATOM   6087  C  CB  . THR C  1 209 ? 41.889  -5.327  -40.241 1.00 10.32  ? 209 THR C CB  1 
ATOM   6088  O  OG1 . THR C  1 209 ? 42.501  -4.769  -41.409 1.00 10.84  ? 209 THR C OG1 1 
ATOM   6089  C  CG2 . THR C  1 209 ? 42.104  -6.814  -40.262 1.00 12.25  ? 209 THR C CG2 1 
ATOM   6090  N  N   . VAL C  1 210 ? 38.687  -6.321  -39.147 1.00 9.29   ? 210 VAL C N   1 
ATOM   6091  C  CA  . VAL C  1 210 ? 37.980  -6.876  -38.006 1.00 10.01  ? 210 VAL C CA  1 
ATOM   6092  C  C   . VAL C  1 210 ? 38.255  -8.361  -38.013 1.00 10.27  ? 210 VAL C C   1 
ATOM   6093  O  O   . VAL C  1 210 ? 37.942  -9.056  -38.987 1.00 10.06  ? 210 VAL C O   1 
ATOM   6094  C  CB  . VAL C  1 210 ? 36.448  -6.639  -38.071 1.00 9.60   ? 210 VAL C CB  1 
ATOM   6095  C  CG1 . VAL C  1 210 ? 35.781  -7.216  -36.810 1.00 11.60  ? 210 VAL C CG1 1 
ATOM   6096  C  CG2 . VAL C  1 210 ? 36.137  -5.120  -38.222 1.00 10.19  ? 210 VAL C CG2 1 
ATOM   6097  N  N   . PHE C  1 211 ? 38.954  -8.897  -37.029 1.00 10.54  ? 211 PHE C N   1 
ATOM   6098  C  CA  . PHE C  1 211 ? 39.245  -10.293 -37.087 1.00 12.03  ? 211 PHE C CA  1 
ATOM   6099  C  C   . PHE C  1 211 ? 37.980  -11.157 -37.020 1.00 11.52  ? 211 PHE C C   1 
ATOM   6100  O  O   . PHE C  1 211 ? 37.027  -10.839 -36.268 1.00 12.48  ? 211 PHE C O   1 
ATOM   6101  C  CB  . PHE C  1 211 ? 40.283  -10.664 -35.997 1.00 12.90  ? 211 PHE C CB  1 
ATOM   6102  C  CG  . PHE C  1 211 ? 41.631  -9.994  -36.219 1.00 12.96  ? 211 PHE C CG  1 
ATOM   6103  C  CD1 . PHE C  1 211 ? 42.428  -10.432 -37.304 1.00 15.32  ? 211 PHE C CD1 1 
ATOM   6104  C  CD2 . PHE C  1 211 ? 42.059  -8.948  -35.468 1.00 15.17  ? 211 PHE C CD2 1 
ATOM   6105  C  CE1 . PHE C  1 211 ? 43.670  -9.780  -37.550 1.00 15.53  ? 211 PHE C CE1 1 
ATOM   6106  C  CE2 . PHE C  1 211 ? 43.283  -8.349  -35.708 1.00 14.71  ? 211 PHE C CE2 1 
ATOM   6107  C  CZ  . PHE C  1 211 ? 44.099  -8.737  -36.769 1.00 17.79  ? 211 PHE C CZ  1 
ATOM   6108  N  N   . ARG C  1 212 ? 37.936  -12.283 -37.737 1.00 12.85  ? 212 ARG C N   1 
ATOM   6109  C  CA  . ARG C  1 212 ? 36.752  -13.090 -37.771 1.00 12.62  ? 212 ARG C CA  1 
ATOM   6110  C  C   . ARG C  1 212 ? 36.438  -13.728 -36.422 1.00 13.77  ? 212 ARG C C   1 
ATOM   6111  O  O   . ARG C  1 212 ? 35.286  -13.844 -36.033 1.00 15.23  ? 212 ARG C O   1 
ATOM   6112  C  CB  . ARG C  1 212 ? 36.902  -14.173 -38.804 1.00 13.53  ? 212 ARG C CB  1 
ATOM   6113  C  CG  . ARG C  1 212 ? 35.664  -15.007 -39.050 1.00 16.28  ? 212 ARG C CG  1 
ATOM   6114  C  CD  . ARG C  1 212 ? 36.035  -16.267 -39.820 1.00 20.67  ? 212 ARG C CD  1 
ATOM   6115  N  NE  . ARG C  1 212 ? 34.814  -16.901 -40.271 1.00 25.50  ? 212 ARG C NE  1 
ATOM   6116  C  CZ  . ARG C  1 212 ? 34.728  -17.834 -41.231 1.00 29.99  ? 212 ARG C CZ  1 
ATOM   6117  N  NH1 . ARG C  1 212 ? 35.833  -18.347 -41.779 1.00 36.03  ? 212 ARG C NH1 1 
ATOM   6118  N  NH2 . ARG C  1 212 ? 33.566  -18.215 -41.716 1.00 35.01  ? 212 ARG C NH2 1 
ATOM   6119  N  N   . ASN C  1 213 ? 37.490  -14.168 -35.724 1.00 15.23  ? 213 ASN C N   1 
ATOM   6120  C  CA  . ASN C  1 213 ? 37.292  -14.932 -34.510 1.00 15.78  ? 213 ASN C CA  1 
ATOM   6121  C  C   . ASN C  1 213 ? 37.490  -14.049 -33.292 1.00 15.96  ? 213 ASN C C   1 
ATOM   6122  O  O   . ASN C  1 213 ? 38.365  -13.191 -33.245 1.00 16.35  ? 213 ASN C O   1 
ATOM   6123  C  CB  . ASN C  1 213 ? 38.356  -16.008 -34.468 1.00 19.54  ? 213 ASN C CB  1 
ATOM   6124  C  CG  . ASN C  1 213 ? 38.306  -16.875 -35.672 1.00 21.32  ? 213 ASN C CG  1 
ATOM   6125  O  OD1 . ASN C  1 213 ? 39.348  -17.099 -36.311 1.00 25.97  ? 213 ASN C OD1 1 
ATOM   6126  N  ND2 . ASN C  1 213 ? 37.123  -17.401 -36.025 1.00 23.56  ? 213 ASN C ND2 1 
ATOM   6127  N  N   . PRO C  1 214 ? 36.555  -14.151 -32.319 1.00 16.15  ? 214 PRO C N   1 
ATOM   6128  C  CA  . PRO C  1 214 ? 36.646  -13.373 -31.113 1.00 16.59  ? 214 PRO C CA  1 
ATOM   6129  C  C   . PRO C  1 214 ? 37.643  -13.933 -30.154 1.00 16.85  ? 214 PRO C C   1 
ATOM   6130  O  O   . PRO C  1 214 ? 38.043  -15.122 -30.338 1.00 20.93  ? 214 PRO C O   1 
ATOM   6131  C  CB  . PRO C  1 214 ? 35.253  -13.521 -30.503 1.00 17.75  ? 214 PRO C CB  1 
ATOM   6132  C  CG  . PRO C  1 214 ? 34.855  -14.903 -30.886 1.00 18.04  ? 214 PRO C CG  1 
ATOM   6133  C  CD  . PRO C  1 214 ? 35.354  -15.019 -32.355 1.00 17.46  ? 214 PRO C CD  1 
ATOM   6134  N  N   . VAL C  1 215 ? 38.103  -13.090 -29.208 1.00 18.26  ? 215 VAL C N   1 
ATOM   6135  C  CA  . VAL C  1 215 ? 38.854  -13.602 -28.035 1.00 21.31  ? 215 VAL C CA  1 
ATOM   6136  C  C   . VAL C  1 215 ? 37.848  -13.732 -26.890 1.00 22.99  ? 215 VAL C C   1 
ATOM   6137  O  O   . VAL C  1 215 ? 36.736  -13.204 -26.929 1.00 21.96  ? 215 VAL C O   1 
ATOM   6138  C  CB  . VAL C  1 215 ? 39.992  -12.602 -27.614 1.00 21.57  ? 215 VAL C CB  1 
ATOM   6139  C  CG1 . VAL C  1 215 ? 41.062  -12.474 -28.691 1.00 22.41  ? 215 VAL C CG1 1 
ATOM   6140  C  CG2 . VAL C  1 215 ? 39.467  -11.225 -27.123 1.00 22.12  ? 215 VAL C CG2 1 
ATOM   6141  N  N   . GLN C  1 216 ? 38.224  -14.488 -25.870 1.00 23.11  ? 216 GLN C N   1 
ATOM   6142  C  CA  . GLN C  1 216 ? 37.447  -14.622 -24.670 1.00 23.90  ? 216 GLN C CA  1 
ATOM   6143  C  C   . GLN C  1 216 ? 38.149  -13.985 -23.472 1.00 28.09  ? 216 GLN C C   1 
ATOM   6144  O  O   . GLN C  1 216 ? 39.375  -14.058 -23.328 1.00 28.68  ? 216 GLN C O   1 
ATOM   6145  C  CB  . GLN C  1 216 ? 37.244  -16.090 -24.395 1.00 25.20  ? 216 GLN C CB  1 
ATOM   6146  C  CG  . GLN C  1 216 ? 36.505  -16.774 -25.514 1.00 29.38  ? 216 GLN C CG  1 
ATOM   6147  C  CD  . GLN C  1 216 ? 35.894  -18.022 -25.034 1.00 41.53  ? 216 GLN C CD  1 
ATOM   6148  O  OE1 . GLN C  1 216 ? 36.268  -18.576 -23.955 1.00 49.40  ? 216 GLN C OE1 1 
ATOM   6149  N  NE2 . GLN C  1 216 ? 34.941  -18.529 -25.796 1.00 50.30  ? 216 GLN C NE2 1 
ATOM   6150  N  N   . ILE C  1 217 ? 37.343  -13.320 -22.666 1.00 22.18  ? 217 ILE C N   1 
ATOM   6151  C  CA  . ILE C  1 217 ? 37.726  -12.862 -21.327 1.00 22.36  ? 217 ILE C CA  1 
ATOM   6152  C  C   . ILE C  1 217 ? 36.742  -13.467 -20.341 1.00 27.30  ? 217 ILE C C   1 
ATOM   6153  O  O   . ILE C  1 217 ? 35.660  -13.927 -20.728 1.00 25.64  ? 217 ILE C O   1 
ATOM   6154  C  CB  . ILE C  1 217 ? 37.858  -11.293 -21.218 1.00 25.52  ? 217 ILE C CB  1 
ATOM   6155  C  CG1 . ILE C  1 217 ? 36.500  -10.533 -21.337 1.00 20.24  ? 217 ILE C CG1 1 
ATOM   6156  C  CG2 . ILE C  1 217 ? 38.910  -10.820 -22.190 1.00 24.01  ? 217 ILE C CG2 1 
ATOM   6157  C  CD1 . ILE C  1 217 ? 36.579  -9.045  -21.082 1.00 23.51  ? 217 ILE C CD1 1 
ATOM   6158  N  N   . SER C  1 218 ? 37.151  -13.671 -19.098 1.00 26.24  ? 218 SER C N   1 
ATOM   6159  C  CA  . SER C  1 218 ? 36.243  -14.320 -18.224 1.00 24.17  ? 218 SER C CA  1 
ATOM   6160  C  C   . SER C  1 218 ? 35.088  -13.403 -17.920 1.00 24.01  ? 218 SER C C   1 
ATOM   6161  O  O   . SER C  1 218 ? 35.166  -12.150 -18.011 1.00 26.41  ? 218 SER C O   1 
ATOM   6162  C  CB  . SER C  1 218 ? 36.894  -14.735 -16.901 1.00 30.90  ? 218 SER C CB  1 
ATOM   6163  O  OG  . SER C  1 218 ? 37.359  -13.593 -16.150 1.00 31.79  ? 218 SER C OG  1 
ATOM   6164  N  N   . GLN C  1 219 ? 34.038  -14.005 -17.348 1.00 27.33  ? 219 GLN C N   1 
ATOM   6165  C  CA  . GLN C  1 219 ? 32.939  -13.173 -16.892 1.00 24.63  ? 219 GLN C CA  1 
ATOM   6166  C  C   . GLN C  1 219 ? 33.415  -12.198 -15.802 1.00 27.07  ? 219 GLN C C   1 
ATOM   6167  O  O   . GLN C  1 219 ? 32.990  -11.040 -15.760 1.00 25.69  ? 219 GLN C O   1 
ATOM   6168  C  CB  . GLN C  1 219 ? 31.741  -13.966 -16.332 1.00 30.42  ? 219 GLN C CB  1 
ATOM   6169  N  N   . GLU C  1 220 ? 34.346  -12.645 -14.955 1.00 27.58  ? 220 GLU C N   1 
ATOM   6170  C  CA  . GLU C  1 220 ? 34.957  -11.694 -14.025 1.00 29.34  ? 220 GLU C CA  1 
ATOM   6171  C  C   . GLU C  1 220 ? 35.726  -10.539 -14.685 1.00 23.55  ? 220 GLU C C   1 
ATOM   6172  O  O   . GLU C  1 220 ? 35.576  -9.390  -14.233 1.00 23.36  ? 220 GLU C O   1 
ATOM   6173  C  CB  . GLU C  1 220 ? 35.822  -12.467 -12.991 1.00 33.33  ? 220 GLU C CB  1 
ATOM   6174  C  CG  . GLU C  1 220 ? 35.038  -13.518 -12.169 1.00 34.63  ? 220 GLU C CG  1 
ATOM   6175  C  CD  . GLU C  1 220 ? 34.931  -14.922 -12.820 1.00 35.01  ? 220 GLU C CD  1 
ATOM   6176  O  OE1 . GLU C  1 220 ? 34.376  -15.819 -12.156 1.00 40.58  ? 220 GLU C OE1 1 
ATOM   6177  O  OE2 . GLU C  1 220 ? 35.350  -15.209 -13.959 1.00 34.11  ? 220 GLU C OE2 1 
ATOM   6178  N  N   . GLN C  1 221 ? 36.532  -10.821 -15.704 1.00 22.66  ? 221 GLN C N   1 
ATOM   6179  C  CA  . GLN C  1 221 ? 37.274  -9.741  -16.411 1.00 23.10  ? 221 GLN C CA  1 
ATOM   6180  C  C   . GLN C  1 221 ? 36.250  -8.739  -17.023 1.00 23.97  ? 221 GLN C C   1 
ATOM   6181  O  O   . GLN C  1 221 ? 36.433  -7.520  -16.930 1.00 26.31  ? 221 GLN C O   1 
ATOM   6182  C  CB  . GLN C  1 221 ? 38.203  -10.323 -17.444 1.00 24.52  ? 221 GLN C CB  1 
ATOM   6183  C  CG  . GLN C  1 221 ? 39.416  -10.932 -16.849 1.00 27.44  ? 221 GLN C CG  1 
ATOM   6184  C  CD  . GLN C  1 221 ? 40.352  -11.474 -17.918 1.00 51.15  ? 221 GLN C CD  1 
ATOM   6185  O  OE1 . GLN C  1 221 ? 40.029  -12.447 -18.602 1.00 29.99  ? 221 GLN C OE1 1 
ATOM   6186  N  NE2 . GLN C  1 221 ? 41.511  -10.838 -18.077 1.00 70.38  ? 221 GLN C NE2 1 
ATOM   6187  N  N   . LEU C  1 222 ? 35.180  -9.269  -17.620 1.00 24.66  ? 222 LEU C N   1 
ATOM   6188  C  CA  . LEU C  1 222 ? 34.235  -8.425  -18.355 1.00 22.12  ? 222 LEU C CA  1 
ATOM   6189  C  C   . LEU C  1 222 ? 33.516  -7.505  -17.378 1.00 26.96  ? 222 LEU C C   1 
ATOM   6190  O  O   . LEU C  1 222 ? 33.373  -6.284  -17.595 1.00 25.51  ? 222 LEU C O   1 
ATOM   6191  C  CB  . LEU C  1 222 ? 33.236  -9.321  -19.105 1.00 25.08  ? 222 LEU C CB  1 
ATOM   6192  C  CG  . LEU C  1 222 ? 32.168  -8.489  -19.804 1.00 22.58  ? 222 LEU C CG  1 
ATOM   6193  C  CD1 . LEU C  1 222 ? 32.753  -7.559  -20.874 1.00 20.30  ? 222 LEU C CD1 1 
ATOM   6194  C  CD2 . LEU C  1 222 ? 31.226  -9.434  -20.503 1.00 21.81  ? 222 LEU C CD2 1 
ATOM   6195  N  N   . LEU C  1 223 ? 33.096  -8.103  -16.255 1.00 26.85  ? 223 LEU C N   1 
ATOM   6196  C  CA  . LEU C  1 223 ? 32.396  -7.368  -15.233 1.00 23.50  ? 223 LEU C CA  1 
ATOM   6197  C  C   . LEU C  1 223 ? 33.371  -6.309  -14.640 1.00 23.31  ? 223 LEU C C   1 
ATOM   6198  O  O   . LEU C  1 223 ? 32.974  -5.185  -14.473 1.00 23.00  ? 223 LEU C O   1 
ATOM   6199  C  CB  . LEU C  1 223 ? 31.937  -8.372  -14.154 1.00 24.38  ? 223 LEU C CB  1 
ATOM   6200  C  CG  . LEU C  1 223 ? 31.274  -7.674  -12.986 1.00 25.74  ? 223 LEU C CG  1 
ATOM   6201  C  CD1 . LEU C  1 223 ? 30.021  -6.936  -13.390 1.00 31.62  ? 223 LEU C CD1 1 
ATOM   6202  C  CD2 . LEU C  1 223 ? 30.918  -8.628  -11.835 1.00 30.57  ? 223 LEU C CD2 1 
ATOM   6203  N  N   . ALA C  1 224 ? 34.647  -6.657  -14.420 1.00 21.91  ? 224 ALA C N   1 
ATOM   6204  C  CA  . ALA C  1 224 ? 35.670  -5.696  -13.989 1.00 26.67  ? 224 ALA C CA  1 
ATOM   6205  C  C   . ALA C  1 224 ? 35.779  -4.502  -14.923 1.00 25.41  ? 224 ALA C C   1 
ATOM   6206  O  O   . ALA C  1 224 ? 35.749  -3.365  -14.513 1.00 26.44  ? 224 ALA C O   1 
ATOM   6207  C  CB  . ALA C  1 224 ? 37.041  -6.399  -13.786 1.00 23.52  ? 224 ALA C CB  1 
ATOM   6208  N  N   . LEU C  1 225 ? 35.888  -4.747  -16.219 1.00 24.54  ? 225 LEU C N   1 
ATOM   6209  C  CA  . LEU C  1 225 ? 35.989  -3.659  -17.183 1.00 24.33  ? 225 LEU C CA  1 
ATOM   6210  C  C   . LEU C  1 225 ? 34.748  -2.757  -17.178 1.00 20.99  ? 225 LEU C C   1 
ATOM   6211  O  O   . LEU C  1 225 ? 34.851  -1.542  -17.271 1.00 23.51  ? 225 LEU C O   1 
ATOM   6212  C  CB  . LEU C  1 225 ? 36.148  -4.281  -18.572 1.00 21.83  ? 225 LEU C CB  1 
ATOM   6213  C  CG  . LEU C  1 225 ? 36.223  -3.313  -19.743 1.00 22.62  ? 225 LEU C CG  1 
ATOM   6214  C  CD1 . LEU C  1 225 ? 37.407  -2.402  -19.648 1.00 23.68  ? 225 LEU C CD1 1 
ATOM   6215  C  CD2 . LEU C  1 225 ? 36.237  -4.116  -21.051 1.00 22.66  ? 225 LEU C CD2 1 
ATOM   6216  N  N   . GLU C  1 226 ? 33.579  -3.365  -17.098 1.00 21.77  ? 226 GLU C N   1 
ATOM   6217  C  CA  . GLU C  1 226 ? 32.312  -2.582  -17.134 1.00 21.77  ? 226 GLU C CA  1 
ATOM   6218  C  C   . GLU C  1 226 ? 32.078  -1.748  -15.928 1.00 22.08  ? 226 GLU C C   1 
ATOM   6219  O  O   . GLU C  1 226 ? 31.305  -0.796  -16.014 1.00 23.01  ? 226 GLU C O   1 
ATOM   6220  C  CB  . GLU C  1 226 ? 31.116  -3.518  -17.285 1.00 22.83  ? 226 GLU C CB  1 
ATOM   6221  C  CG  . GLU C  1 226 ? 31.162  -4.244  -18.646 1.00 23.09  ? 226 GLU C CG  1 
ATOM   6222  C  CD  . GLU C  1 226 ? 30.259  -5.458  -18.649 1.00 18.26  ? 226 GLU C CD  1 
ATOM   6223  O  OE1 . GLU C  1 226 ? 29.930  -5.940  -17.544 1.00 22.66  ? 226 GLU C OE1 1 
ATOM   6224  O  OE2 . GLU C  1 226 ? 29.875  -5.924  -19.742 1.00 21.52  ? 226 GLU C OE2 1 
ATOM   6225  N  N   . THR C  1 227 ? 32.747  -2.114  -14.817 1.00 23.86  ? 227 THR C N   1 
ATOM   6226  C  CA  . THR C  1 227 ? 32.577  -1.447  -13.550 1.00 26.08  ? 227 THR C CA  1 
ATOM   6227  C  C   . THR C  1 227 ? 33.772  -0.597  -13.140 1.00 29.85  ? 227 THR C C   1 
ATOM   6228  O  O   . THR C  1 227 ? 33.725  -0.002  -12.088 1.00 31.38  ? 227 THR C O   1 
ATOM   6229  C  CB  . THR C  1 227 ? 32.212  -2.503  -12.438 1.00 20.14  ? 227 THR C CB  1 
ATOM   6230  O  OG1 . THR C  1 227 ? 33.243  -3.516  -12.332 1.00 25.08  ? 227 THR C OG1 1 
ATOM   6231  C  CG2 . THR C  1 227 ? 30.927  -3.208  -12.764 1.00 26.47  ? 227 THR C CG2 1 
ATOM   6232  N  N   . ALA C  1 228 ? 34.861  -0.551  -13.898 1.00 30.57  ? 228 ALA C N   1 
ATOM   6233  C  CA  . ALA C  1 228 ? 36.073  0.081   -13.338 1.00 32.46  ? 228 ALA C CA  1 
ATOM   6234  C  C   . ALA C  1 228 ? 36.093  1.585   -13.409 1.00 36.79  ? 228 ALA C C   1 
ATOM   6235  O  O   . ALA C  1 228 ? 36.736  2.228   -12.562 1.00 39.73  ? 228 ALA C O   1 
ATOM   6236  C  CB  . ALA C  1 228 ? 37.355  -0.455  -14.021 1.00 34.85  ? 228 ALA C CB  1 
ATOM   6237  N  N   . LEU C  1 229 ? 35.469  2.168   -14.428 1.00 29.51  ? 229 LEU C N   1 
ATOM   6238  C  CA  . LEU C  1 229 ? 35.852  3.517   -14.826 1.00 31.20  ? 229 LEU C CA  1 
ATOM   6239  C  C   . LEU C  1 229 ? 34.695  4.455   -14.795 1.00 27.66  ? 229 LEU C C   1 
ATOM   6240  O  O   . LEU C  1 229 ? 33.512  4.049   -14.975 1.00 29.79  ? 229 LEU C O   1 
ATOM   6241  C  CB  . LEU C  1 229 ? 36.454  3.534   -16.234 1.00 31.11  ? 229 LEU C CB  1 
ATOM   6242  C  CG  . LEU C  1 229 ? 37.640  2.632   -16.459 1.00 29.70  ? 229 LEU C CG  1 
ATOM   6243  C  CD1 . LEU C  1 229 ? 38.038  2.628   -17.929 1.00 35.12  ? 229 LEU C CD1 1 
ATOM   6244  C  CD2 . LEU C  1 229 ? 38.722  3.176   -15.537 1.00 25.85  ? 229 LEU C CD2 1 
ATOM   6245  N  N   . TYR C  1 230 ? 35.057  5.730   -14.711 1.00 34.44  ? 230 TYR C N   1 
ATOM   6246  C  CA  . TYR C  1 230 ? 34.068  6.801   -14.685 1.00 33.36  ? 230 TYR C CA  1 
ATOM   6247  C  C   . TYR C  1 230 ? 34.410  7.760   -15.768 1.00 30.92  ? 230 TYR C C   1 
ATOM   6248  O  O   . TYR C  1 230 ? 35.583  7.871   -16.096 1.00 29.81  ? 230 TYR C O   1 
ATOM   6249  C  CB  . TYR C  1 230 ? 34.095  7.466   -13.331 1.00 34.48  ? 230 TYR C CB  1 
ATOM   6250  C  CG  . TYR C  1 230 ? 33.550  6.558   -12.309 1.00 31.96  ? 230 TYR C CG  1 
ATOM   6251  C  CD1 . TYR C  1 230 ? 34.310  5.496   -11.771 1.00 34.06  ? 230 TYR C CD1 1 
ATOM   6252  C  CD2 . TYR C  1 230 ? 32.272  6.769   -11.801 1.00 41.18  ? 230 TYR C CD2 1 
ATOM   6253  C  CE1 . TYR C  1 230 ? 33.766  4.611   -10.811 1.00 38.84  ? 230 TYR C CE1 1 
ATOM   6254  C  CE2 . TYR C  1 230 ? 31.747  5.926   -10.829 1.00 50.10  ? 230 TYR C CE2 1 
ATOM   6255  C  CZ  . TYR C  1 230 ? 32.493  4.867   -10.336 1.00 52.10  ? 230 TYR C CZ  1 
ATOM   6256  O  OH  . TYR C  1 230 ? 31.907  4.073   -9.362  1.00 60.87  ? 230 TYR C OH  1 
ATOM   6257  N  N   A CYS C  1 231 ? 33.376  8.386   -16.310 0.50 30.60  ? 231 CYS C N   1 
ATOM   6258  N  N   B CYS C  1 231 ? 33.424  8.467   -16.357 0.50 32.27  ? 231 CYS C N   1 
ATOM   6259  C  CA  A CYS C  1 231 ? 33.589  9.377   -17.335 0.50 27.39  ? 231 CYS C CA  1 
ATOM   6260  C  CA  B CYS C  1 231 ? 33.664  9.511   -17.416 0.50 31.02  ? 231 CYS C CA  1 
ATOM   6261  C  C   A CYS C  1 231 ? 34.135  10.676  -16.777 0.50 30.24  ? 231 CYS C C   1 
ATOM   6262  C  C   B CYS C  1 231 ? 33.729  10.962  -16.885 0.50 27.14  ? 231 CYS C C   1 
ATOM   6263  O  O   A CYS C  1 231 ? 35.015  11.254  -17.416 0.50 25.14  ? 231 CYS C O   1 
ATOM   6264  O  O   B CYS C  1 231 ? 33.899  11.973  -17.591 0.50 17.58  ? 231 CYS C O   1 
ATOM   6265  C  CB  A CYS C  1 231 ? 32.320  9.626   -18.155 0.50 28.96  ? 231 CYS C CB  1 
ATOM   6266  C  CB  B CYS C  1 231 ? 32.643  9.396   -18.564 0.50 25.05  ? 231 CYS C CB  1 
ATOM   6267  S  SG  A CYS C  1 231 ? 31.922  8.263   -19.280 0.50 31.21  ? 231 CYS C SG  1 
ATOM   6268  S  SG  B CYS C  1 231 ? 30.902  9.506   -18.153 0.50 32.71  ? 231 CYS C SG  1 
ATOM   6269  N  N   . THR C  1 232 ? 33.620  11.066  -15.593 1.00 29.35  ? 232 THR C N   1 
ATOM   6270  C  CA  . THR C  1 232 ? 33.732  12.386  -14.962 1.00 33.77  ? 232 THR C CA  1 
ATOM   6271  C  C   . THR C  1 232 ? 35.003  12.532  -14.131 1.00 34.85  ? 232 THR C C   1 
ATOM   6272  O  O   . THR C  1 232 ? 35.639  11.516  -13.826 1.00 32.50  ? 232 THR C O   1 
ATOM   6273  C  CB  . THR C  1 232 ? 32.532  12.516  -14.055 1.00 40.29  ? 232 THR C CB  1 
ATOM   6274  O  OG1 . THR C  1 232 ? 32.340  11.278  -13.339 1.00 37.72  ? 232 THR C OG1 1 
ATOM   6275  C  CG2 . THR C  1 232 ? 31.299  12.816  -14.879 1.00 40.46  ? 232 THR C CG2 1 
ATOM   6276  N  N   . HIS C  1 233 ? 35.384  13.788  -13.784 1.00 45.47  ? 233 HIS C N   1 
ATOM   6277  C  CA  . HIS C  1 233 ? 36.583  14.033  -12.980 1.00 53.94  ? 233 HIS C CA  1 
ATOM   6278  C  C   . HIS C  1 233 ? 36.400  13.599  -11.528 1.00 80.40  ? 233 HIS C C   1 
ATOM   6279  O  O   . HIS C  1 233 ? 35.240  13.617  -11.031 1.00 87.28  ? 233 HIS C O   1 
ATOM   6280  C  CB  . HIS C  1 233 ? 36.976  15.497  -13.110 1.00 56.59  ? 233 HIS C CB  1 
ATOM   6281  C  CG  . HIS C  1 233 ? 37.570  15.851  -14.458 1.00 62.43  ? 233 HIS C CG  1 
ATOM   6282  N  ND1 . HIS C  1 233 ? 36.839  16.414  -15.447 1.00 85.20  ? 233 HIS C ND1 1 
ATOM   6283  C  CD2 . HIS C  1 233 ? 38.889  15.777  -14.927 1.00 64.22  ? 233 HIS C CD2 1 
ATOM   6284  C  CE1 . HIS C  1 233 ? 37.645  16.662  -16.506 1.00 68.50  ? 233 HIS C CE1 1 
ATOM   6285  N  NE2 . HIS C  1 233 ? 38.900  16.275  -16.183 1.00 77.85  ? 233 HIS C NE2 1 
ATOM   6286  N  N   . MET C  1 234 ? 37.523  13.145  -10.898 1.00 66.70  ? 234 MET C N   1 
ATOM   6287  C  CA  . MET C  1 234 ? 37.523  12.558  -9.522  1.00 55.61  ? 234 MET C CA  1 
ATOM   6288  C  C   . MET C  1 234 ? 36.624  13.192  -8.550  1.00 74.84  ? 234 MET C C   1 
ATOM   6289  O  O   . MET C  1 234 ? 36.022  12.528  -7.650  1.00 93.66  ? 234 MET C O   1 
ATOM   6290  C  CB  . MET C  1 234 ? 38.922  12.452  -8.863  1.00 84.14  ? 234 MET C CB  1 
ATOM   6291  C  CG  . MET C  1 234 ? 39.049  11.236  -7.930  1.00 81.76  ? 234 MET C CG  1 
ATOM   6292  S  SD  . MET C  1 234 ? 40.674  10.827  -7.230  1.00 119.50 ? 234 MET C SD  1 
ATOM   6293  C  CE  . MET C  1 234 ? 40.801  9.067   -7.542  1.00 99.71  ? 234 MET C CE  1 
ATOM   6294  N  N   . ASP C  1 235 ? 36.546  14.524  -8.679  1.00 123.32 ? 235 ASP C N   1 
ATOM   6295  C  CA  . ASP C  1 235 ? 35.852  15.204  -7.588  1.00 63.84  ? 235 ASP C CA  1 
ATOM   6296  C  C   . ASP C  1 235 ? 34.545  15.797  -8.058  1.00 61.18  ? 235 ASP C C   1 
ATOM   6297  O  O   . ASP C  1 235 ? 33.963  16.629  -7.378  1.00 53.32  ? 235 ASP C O   1 
ATOM   6298  N  N   . ASP C  1 236 ? 34.057  15.330  -9.205  1.00 50.22  ? 236 ASP C N   1 
ATOM   6299  C  CA  . ASP C  1 236 ? 32.726  15.710  -9.615  1.00 50.26  ? 236 ASP C CA  1 
ATOM   6300  C  C   . ASP C  1 236 ? 31.744  15.122  -8.589  1.00 52.46  ? 236 ASP C C   1 
ATOM   6301  O  O   . ASP C  1 236 ? 31.792  13.900  -8.323  1.00 44.68  ? 236 ASP C O   1 
ATOM   6302  C  CB  . ASP C  1 236 ? 32.403  15.123  -11.000 1.00 40.55  ? 236 ASP C CB  1 
ATOM   6303  C  CG  . ASP C  1 236 ? 31.221  15.820  -11.687 1.00 52.84  ? 236 ASP C CG  1 
ATOM   6304  O  OD1 . ASP C  1 236 ? 30.305  16.423  -11.026 1.00 55.84  ? 236 ASP C OD1 1 
ATOM   6305  O  OD2 . ASP C  1 236 ? 31.230  15.752  -12.939 1.00 59.45  ? 236 ASP C OD2 1 
ATOM   6306  N  N   . PRO C  1 237 ? 30.846  15.979  -8.027  1.00 51.59  ? 237 PRO C N   1 
ATOM   6307  C  CA  . PRO C  1 237 ? 29.850  15.483  -7.072  1.00 53.15  ? 237 PRO C CA  1 
ATOM   6308  C  C   . PRO C  1 237 ? 28.712  14.706  -7.713  1.00 42.21  ? 237 PRO C C   1 
ATOM   6309  O  O   . PRO C  1 237 ? 27.803  14.264  -7.011  1.00 50.41  ? 237 PRO C O   1 
ATOM   6310  C  CB  . PRO C  1 237 ? 29.280  16.773  -6.422  1.00 49.85  ? 237 PRO C CB  1 
ATOM   6311  C  CG  . PRO C  1 237 ? 29.967  17.943  -7.067  1.00 53.37  ? 237 PRO C CG  1 
ATOM   6312  C  CD  . PRO C  1 237 ? 30.696  17.431  -8.283  1.00 49.94  ? 237 PRO C CD  1 
ATOM   6313  N  N   . SER C  1 238 ? 28.744  14.612  -9.042  1.00 45.20  ? 238 SER C N   1 
ATOM   6314  C  CA  . SER C  1 238 ? 27.820  13.787  -9.826  1.00 45.36  ? 238 SER C CA  1 
ATOM   6315  C  C   . SER C  1 238 ? 28.628  12.832  -10.732 1.00 50.25  ? 238 SER C C   1 
ATOM   6316  O  O   . SER C  1 238 ? 28.747  13.084  -11.957 1.00 46.42  ? 238 SER C O   1 
ATOM   6317  C  CB  . SER C  1 238 ? 26.902  14.651  -10.711 1.00 60.82  ? 238 SER C CB  1 
ATOM   6318  O  OG  . SER C  1 238 ? 26.297  15.722  -9.999  1.00 74.65  ? 238 SER C OG  1 
ATOM   6319  N  N   . PRO C  1 239 ? 29.203  11.744  -10.148 1.00 35.49  ? 239 PRO C N   1 
ATOM   6320  C  CA  . PRO C  1 239 ? 29.985  10.812  -10.997 1.00 37.15  ? 239 PRO C CA  1 
ATOM   6321  C  C   . PRO C  1 239 ? 29.141  10.063  -11.997 1.00 26.69  ? 239 PRO C C   1 
ATOM   6322  O  O   . PRO C  1 239 ? 27.981  9.704   -11.745 1.00 37.11  ? 239 PRO C O   1 
ATOM   6323  C  CB  . PRO C  1 239 ? 30.620  9.857   -9.976  1.00 34.56  ? 239 PRO C CB  1 
ATOM   6324  C  CG  . PRO C  1 239 ? 29.690  9.905   -8.800  1.00 43.26  ? 239 PRO C CG  1 
ATOM   6325  C  CD  . PRO C  1 239 ? 29.193  11.324  -8.735  1.00 40.32  ? 239 PRO C CD  1 
ATOM   6326  N  N   . ARG C  1 240 ? 29.753  9.839   -13.141 1.00 29.75  ? 240 ARG C N   1 
ATOM   6327  C  CA  . ARG C  1 240 ? 29.080  9.033   -14.167 1.00 38.37  ? 240 ARG C CA  1 
ATOM   6328  C  C   . ARG C  1 240 ? 29.938  7.826   -14.564 1.00 34.94  ? 240 ARG C C   1 
ATOM   6329  O  O   . ARG C  1 240 ? 31.119  8.023   -14.893 1.00 30.02  ? 240 ARG C O   1 
ATOM   6330  C  CB  . ARG C  1 240 ? 28.813  9.902   -15.380 1.00 41.99  ? 240 ARG C CB  1 
ATOM   6331  N  N   . GLU C  1 241 ? 29.389  6.610   -14.511 1.00 29.65  ? 241 GLU C N   1 
ATOM   6332  C  CA  . GLU C  1 241 ? 30.151  5.439   -14.879 1.00 30.51  ? 241 GLU C CA  1 
ATOM   6333  C  C   . GLU C  1 241 ? 30.386  5.461   -16.355 1.00 25.20  ? 241 GLU C C   1 
ATOM   6334  O  O   . GLU C  1 241 ? 29.542  5.882   -17.137 1.00 26.89  ? 241 GLU C O   1 
ATOM   6335  C  CB  . GLU C  1 241 ? 29.360  4.161   -14.634 1.00 27.11  ? 241 GLU C CB  1 
ATOM   6336  C  CG  . GLU C  1 241 ? 29.129  3.917   -13.167 1.00 32.93  ? 241 GLU C CG  1 
ATOM   6337  C  CD  . GLU C  1 241 ? 27.921  3.032   -12.889 1.00 45.57  ? 241 GLU C CD  1 
ATOM   6338  O  OE1 . GLU C  1 241 ? 27.107  2.701   -13.795 1.00 52.52  ? 241 GLU C OE1 1 
ATOM   6339  O  OE2 . GLU C  1 241 ? 27.763  2.675   -11.706 1.00 64.51  ? 241 GLU C OE2 1 
ATOM   6340  N  N   . MET C  1 242 ? 31.579  5.027   -16.730 1.00 25.40  ? 242 MET C N   1 
ATOM   6341  C  CA  . MET C  1 242 ? 31.914  4.804   -18.134 1.00 24.29  ? 242 MET C CA  1 
ATOM   6342  C  C   . MET C  1 242 ? 31.412  3.450   -18.603 1.00 20.22  ? 242 MET C C   1 
ATOM   6343  O  O   . MET C  1 242 ? 32.045  2.391   -18.371 1.00 23.30  ? 242 MET C O   1 
ATOM   6344  C  CB  . MET C  1 242 ? 33.417  4.885   -18.260 1.00 24.88  ? 242 MET C CB  1 
ATOM   6345  C  CG  . MET C  1 242 ? 33.791  4.890   -19.762 1.00 23.69  ? 242 MET C CG  1 
ATOM   6346  S  SD  . MET C  1 242 ? 35.575  4.917   -20.019 1.00 25.48  ? 242 MET C SD  1 
ATOM   6347  C  CE  . MET C  1 242 ? 36.036  6.605   -19.530 1.00 26.40  ? 242 MET C CE  1 
ATOM   6348  N  N   . ILE C  1 243 ? 30.265  3.505   -19.254 1.00 19.69  ? 243 ILE C N   1 
ATOM   6349  C  CA  . ILE C  1 243 ? 29.594  2.317   -19.775 1.00 18.38  ? 243 ILE C CA  1 
ATOM   6350  C  C   . ILE C  1 243 ? 28.985  2.666   -21.140 1.00 16.89  ? 243 ILE C C   1 
ATOM   6351  O  O   . ILE C  1 243 ? 28.843  3.848   -21.484 1.00 17.15  ? 243 ILE C O   1 
ATOM   6352  C  CB  . ILE C  1 243 ? 28.417  1.844   -18.818 1.00 20.84  ? 243 ILE C CB  1 
ATOM   6353  C  CG1 . ILE C  1 243 ? 27.502  3.007   -18.474 1.00 21.66  ? 243 ILE C CG1 1 
ATOM   6354  C  CG2 . ILE C  1 243 ? 28.971  1.250   -17.510 1.00 21.56  ? 243 ILE C CG2 1 
ATOM   6355  C  CD1 . ILE C  1 243 ? 26.282  2.605   -17.620 1.00 21.41  ? 243 ILE C CD1 1 
ATOM   6356  N  N   . ASN C  1 244 ? 28.706  1.636   -21.908 1.00 15.90  ? 244 ASN C N   1 
ATOM   6357  C  CA  . ASN C  1 244 ? 28.026  1.830   -23.192 1.00 15.90  ? 244 ASN C CA  1 
ATOM   6358  C  C   . ASN C  1 244 ? 28.753  2.827   -24.077 1.00 14.31  ? 244 ASN C C   1 
ATOM   6359  O  O   . ASN C  1 244 ? 28.169  3.653   -24.761 1.00 14.55  ? 244 ASN C O   1 
ATOM   6360  C  CB  . ASN C  1 244 ? 26.567  2.241   -22.936 1.00 15.17  ? 244 ASN C CB  1 
ATOM   6361  C  CG  . ASN C  1 244 ? 25.859  1.282   -22.042 1.00 16.03  ? 244 ASN C CG  1 
ATOM   6362  O  OD1 . ASN C  1 244 ? 26.019  0.072   -22.152 1.00 20.09  ? 244 ASN C OD1 1 
ATOM   6363  N  ND2 . ASN C  1 244 ? 25.098  1.864   -21.074 1.00 22.68  ? 244 ASN C ND2 1 
ATOM   6364  N  N   . ASN C  1 245 ? 30.085  2.723   -24.119 1.00 13.89  ? 245 ASN C N   1 
ATOM   6365  C  CA  . ASN C  1 245 ? 30.915  3.689   -24.876 1.00 13.77  ? 245 ASN C CA  1 
ATOM   6366  C  C   . ASN C  1 245 ? 31.232  3.169   -26.271 1.00 12.95  ? 245 ASN C C   1 
ATOM   6367  O  O   . ASN C  1 245 ? 32.362  2.960   -26.617 1.00 14.58  ? 245 ASN C O   1 
ATOM   6368  C  CB  . ASN C  1 245 ? 32.146  4.063   -24.075 1.00 16.67  ? 245 ASN C CB  1 
ATOM   6369  C  CG  . ASN C  1 245 ? 33.066  2.862   -23.753 1.00 18.00  ? 245 ASN C CG  1 
ATOM   6370  O  OD1 . ASN C  1 245 ? 32.627  1.698   -23.764 1.00 16.29  ? 245 ASN C OD1 1 
ATOM   6371  N  ND2 . ASN C  1 245 ? 34.317  3.143   -23.427 1.00 21.39  ? 245 ASN C ND2 1 
ATOM   6372  N  N   . PHE C  1 246 ? 30.143  2.871   -26.984 1.00 12.24  ? 246 PHE C N   1 
ATOM   6373  C  CA  . PHE C  1 246 ? 30.235  2.372   -28.383 1.00 11.80  ? 246 PHE C CA  1 
ATOM   6374  C  C   . PHE C  1 246 ? 29.276  3.162   -29.204 1.00 11.18  ? 246 PHE C C   1 
ATOM   6375  O  O   . PHE C  1 246 ? 28.246  3.654   -28.691 1.00 11.76  ? 246 PHE C O   1 
ATOM   6376  C  CB  . PHE C  1 246 ? 29.898  0.845   -28.409 1.00 12.00  ? 246 PHE C CB  1 
ATOM   6377  C  CG  . PHE C  1 246 ? 28.506  0.488   -27.950 1.00 11.46  ? 246 PHE C CG  1 
ATOM   6378  C  CD1 . PHE C  1 246 ? 28.258  0.261   -26.614 1.00 12.70  ? 246 PHE C CD1 1 
ATOM   6379  C  CD2 . PHE C  1 246 ? 27.463  0.366   -28.832 1.00 11.96  ? 246 PHE C CD2 1 
ATOM   6380  C  CE1 . PHE C  1 246 ? 26.988  -0.057  -26.198 1.00 13.96  ? 246 PHE C CE1 1 
ATOM   6381  C  CE2 . PHE C  1 246 ? 26.177  0.058   -28.446 1.00 12.80  ? 246 PHE C CE2 1 
ATOM   6382  C  CZ  . PHE C  1 246 ? 25.940  -0.154  -27.097 1.00 14.78  ? 246 PHE C CZ  1 
ATOM   6383  N  N   . ARG C  1 247 ? 29.578  3.298   -30.481 1.00 9.54   ? 247 ARG C N   1 
ATOM   6384  C  CA  . ARG C  1 247 ? 28.655  3.960   -31.408 1.00 8.62   ? 247 ARG C CA  1 
ATOM   6385  C  C   . ARG C  1 247 ? 27.657  2.947   -31.967 1.00 9.34   ? 247 ARG C C   1 
ATOM   6386  O  O   . ARG C  1 247 ? 28.061  1.768   -32.191 1.00 9.32   ? 247 ARG C O   1 
ATOM   6387  C  CB  . ARG C  1 247 ? 29.467  4.551   -32.564 1.00 8.76   ? 247 ARG C CB  1 
ATOM   6388  C  CG  . ARG C  1 247 ? 28.671  5.567   -33.404 1.00 9.48   ? 247 ARG C CG  1 
ATOM   6389  C  CD  . ARG C  1 247 ? 29.503  6.084   -34.566 1.00 8.97   ? 247 ARG C CD  1 
ATOM   6390  N  NE  . ARG C  1 247 ? 28.894  7.193   -35.225 1.00 8.57   ? 247 ARG C NE  1 
ATOM   6391  C  CZ  . ARG C  1 247 ? 29.358  7.767   -36.321 1.00 8.45   ? 247 ARG C CZ  1 
ATOM   6392  N  NH1 . ARG C  1 247 ? 30.368  7.214   -36.975 1.00 9.58   ? 247 ARG C NH1 1 
ATOM   6393  N  NH2 . ARG C  1 247 ? 28.816  8.901   -36.768 1.00 9.47   ? 247 ARG C NH2 1 
ATOM   6394  N  N   . GLN C  1 248 ? 26.407  3.329   -32.210 1.00 8.66   ? 248 GLN C N   1 
ATOM   6395  C  CA  . GLN C  1 248 ? 25.484  2.447   -32.906 1.00 8.60   ? 248 GLN C CA  1 
ATOM   6396  C  C   . GLN C  1 248 ? 25.987  2.149   -34.308 1.00 8.44   ? 248 GLN C C   1 
ATOM   6397  O  O   . GLN C  1 248 ? 26.729  2.970   -34.916 1.00 8.71   ? 248 GLN C O   1 
ATOM   6398  C  CB  . GLN C  1 248 ? 24.124  3.134   -33.036 1.00 9.14   ? 248 GLN C CB  1 
ATOM   6399  C  CG  . GLN C  1 248 ? 23.437  3.476   -31.703 1.00 9.37   ? 248 GLN C CG  1 
ATOM   6400  C  CD  . GLN C  1 248 ? 23.091  2.242   -30.899 1.00 9.37   ? 248 GLN C CD  1 
ATOM   6401  O  OE1 . GLN C  1 248 ? 23.833  1.813   -30.009 1.00 12.34  ? 248 GLN C OE1 1 
ATOM   6402  N  NE2 . GLN C  1 248 ? 21.957  1.637   -31.224 1.00 11.74  ? 248 GLN C NE2 1 
ATOM   6403  N  N   . VAL C  1 249 ? 25.541  1.046   -34.875 1.00 8.22   ? 249 VAL C N   1 
ATOM   6404  C  CA  . VAL C  1 249 ? 25.925  0.722   -36.233 1.00 8.39   ? 249 VAL C CA  1 
ATOM   6405  C  C   . VAL C  1 249 ? 25.312  1.710   -37.204 1.00 7.70   ? 249 VAL C C   1 
ATOM   6406  O  O   . VAL C  1 249 ? 24.188  2.254   -37.025 1.00 8.18   ? 249 VAL C O   1 
ATOM   6407  C  CB  . VAL C  1 249 ? 25.574  -0.713  -36.612 1.00 10.55  ? 249 VAL C CB  1 
ATOM   6408  C  CG1 . VAL C  1 249 ? 26.425  -1.716  -35.918 1.00 11.80  ? 249 VAL C CG1 1 
ATOM   6409  C  CG2 . VAL C  1 249 ? 24.125  -0.973  -36.564 1.00 13.15  ? 249 VAL C CG2 1 
ATOM   6410  N  N   . GLN C  1 250 ? 26.036  1.957   -38.282 1.00 7.72   ? 250 GLN C N   1 
ATOM   6411  C  CA  . GLN C  1 250 ? 25.703  2.925   -39.333 1.00 8.06   ? 250 GLN C CA  1 
ATOM   6412  C  C   . GLN C  1 250 ? 25.089  2.180   -40.519 1.00 8.02   ? 250 GLN C C   1 
ATOM   6413  O  O   . GLN C  1 250 ? 25.433  1.039   -40.776 1.00 9.62   ? 250 GLN C O   1 
ATOM   6414  C  CB  . GLN C  1 250 ? 26.998  3.599   -39.782 1.00 8.17   ? 250 GLN C CB  1 
ATOM   6415  C  CG  . GLN C  1 250 ? 27.794  4.224   -38.599 1.00 8.72   ? 250 GLN C CG  1 
ATOM   6416  C  CD  . GLN C  1 250 ? 27.045  5.373   -37.978 1.00 7.60   ? 250 GLN C CD  1 
ATOM   6417  O  OE1 . GLN C  1 250 ? 26.781  6.419   -38.610 1.00 8.76   ? 250 GLN C OE1 1 
ATOM   6418  N  NE2 . GLN C  1 250 ? 26.719  5.208   -36.713 1.00 8.23   ? 250 GLN C NE2 1 
ATOM   6419  N  N   . LYS C  1 251 ? 24.255  2.878   -41.259 1.00 8.39   ? 251 LYS C N   1 
ATOM   6420  C  CA  . LYS C  1 251 ? 23.792  2.350   -42.529 1.00 8.89   ? 251 LYS C CA  1 
ATOM   6421  C  C   . LYS C  1 251 ? 24.967  2.041   -43.412 1.00 8.22   ? 251 LYS C C   1 
ATOM   6422  O  O   . LYS C  1 251 ? 25.946  2.813   -43.450 1.00 9.44   ? 251 LYS C O   1 
ATOM   6423  C  CB  . LYS C  1 251 ? 22.844  3.291   -43.192 1.00 10.96  ? 251 LYS C CB  1 
ATOM   6424  C  CG  . LYS C  1 251 ? 21.500  3.260   -42.489 1.00 10.55  ? 251 LYS C CG  1 
ATOM   6425  C  CD  . LYS C  1 251 ? 20.491  4.125   -43.110 1.00 11.18  ? 251 LYS C CD  1 
ATOM   6426  C  CE  . LYS C  1 251 ? 19.024  3.868   -42.753 1.00 9.47   ? 251 LYS C CE  1 
ATOM   6427  N  NZ  . LYS C  1 251 ? 18.788  3.943   -41.266 1.00 8.18   ? 251 LYS C NZ  1 
ATOM   6428  N  N   . PHE C  1 252 ? 24.882  0.987   -44.223 1.00 8.99   ? 252 PHE C N   1 
ATOM   6429  C  CA  . PHE C  1 252 ? 26.003  0.534   -45.110 1.00 9.66   ? 252 PHE C CA  1 
ATOM   6430  C  C   . PHE C  1 252 ? 25.268  -0.077  -46.291 1.00 11.53  ? 252 PHE C C   1 
ATOM   6431  O  O   . PHE C  1 252 ? 24.870  -1.245  -46.234 1.00 14.81  ? 252 PHE C O   1 
ATOM   6432  C  CB  . PHE C  1 252 ? 26.832  -0.449  -44.362 1.00 10.48  ? 252 PHE C CB  1 
ATOM   6433  C  CG  . PHE C  1 252 ? 28.034  -0.939  -45.071 1.00 9.85   ? 252 PHE C CG  1 
ATOM   6434  C  CD1 . PHE C  1 252 ? 29.198  -0.186  -45.061 1.00 10.05  ? 252 PHE C CD1 1 
ATOM   6435  C  CD2 . PHE C  1 252 ? 28.057  -2.218  -45.691 1.00 11.22  ? 252 PHE C CD2 1 
ATOM   6436  C  CE1 . PHE C  1 252 ? 30.388  -0.700  -45.657 1.00 11.55  ? 252 PHE C CE1 1 
ATOM   6437  C  CE2 . PHE C  1 252 ? 29.222  -2.715  -46.257 1.00 12.44  ? 252 PHE C CE2 1 
ATOM   6438  C  CZ  . PHE C  1 252 ? 30.360  -1.940  -46.219 1.00 11.38  ? 252 PHE C CZ  1 
ATOM   6439  N  N   . ASP C  1 253 ? 25.074  0.680   -47.325 1.00 14.22  ? 253 ASP C N   1 
ATOM   6440  C  CA  . ASP C  1 253 ? 24.201  0.253   -48.425 1.00 16.07  ? 253 ASP C CA  1 
ATOM   6441  C  C   . ASP C  1 253 ? 24.924  0.265   -49.722 1.00 13.32  ? 253 ASP C C   1 
ATOM   6442  O  O   . ASP C  1 253 ? 25.737  1.154   -50.020 1.00 14.59  ? 253 ASP C O   1 
ATOM   6443  C  CB  . ASP C  1 253 ? 22.949  1.098   -48.366 1.00 21.33  ? 253 ASP C CB  1 
ATOM   6444  C  CG  . ASP C  1 253 ? 21.818  0.592   -49.232 1.00 26.89  ? 253 ASP C CG  1 
ATOM   6445  O  OD1 . ASP C  1 253 ? 21.254  -0.501  -48.943 1.00 37.59  ? 253 ASP C OD1 1 
ATOM   6446  O  OD2 . ASP C  1 253 ? 21.539  1.340   -50.189 1.00 30.35  ? 253 ASP C OD2 1 
ATOM   6447  N  N   . GLU C  1 254 ? 24.665  -0.747  -50.534 1.00 13.46  ? 254 GLU C N   1 
ATOM   6448  C  CA  . GLU C  1 254 ? 25.302  -0.852  -51.851 1.00 14.18  ? 254 GLU C CA  1 
ATOM   6449  C  C   . GLU C  1 254 ? 26.821  -0.932  -51.715 1.00 13.78  ? 254 GLU C C   1 
ATOM   6450  O  O   . GLU C  1 254 ? 27.582  -0.371  -52.568 1.00 17.15  ? 254 GLU C O   1 
ATOM   6451  C  CB  . GLU C  1 254 ? 24.900  0.263   -52.800 1.00 16.80  ? 254 GLU C CB  1 
ATOM   6452  C  CG  . GLU C  1 254 ? 23.367  0.351   -53.064 1.00 21.88  ? 254 GLU C CG  1 
ATOM   6453  C  CD  . GLU C  1 254 ? 22.688  -0.877  -53.691 1.00 24.13  ? 254 GLU C CD  1 
ATOM   6454  O  OE1 . GLU C  1 254 ? 23.333  -1.596  -54.493 1.00 39.72  ? 254 GLU C OE1 1 
ATOM   6455  O  OE2 . GLU C  1 254 ? 21.461  -1.118  -53.402 1.00 41.40  ? 254 GLU C OE2 1 
ATOM   6456  N  N   . ARG C  1 255 ? 27.283  -1.597  -50.661 1.00 12.30  ? 255 ARG C N   1 
ATOM   6457  C  CA  . ARG C  1 255 ? 28.701  -1.736  -50.383 1.00 11.71  ? 255 ARG C CA  1 
ATOM   6458  C  C   . ARG C  1 255 ? 28.986  -3.157  -49.932 1.00 11.24  ? 255 ARG C C   1 
ATOM   6459  O  O   . ARG C  1 255 ? 28.090  -3.882  -49.460 1.00 12.99  ? 255 ARG C O   1 
ATOM   6460  C  CB  . ARG C  1 255 ? 29.205  -0.735  -49.322 1.00 11.56  ? 255 ARG C CB  1 
ATOM   6461  C  CG  . ARG C  1 255 ? 29.108  0.709   -49.783 1.00 13.13  ? 255 ARG C CG  1 
ATOM   6462  C  CD  . ARG C  1 255 ? 29.735  1.635   -48.745 1.00 12.73  ? 255 ARG C CD  1 
ATOM   6463  N  NE  . ARG C  1 255 ? 31.137  1.278   -48.540 1.00 13.15  ? 255 ARG C NE  1 
ATOM   6464  C  CZ  . ARG C  1 255 ? 31.857  1.620   -47.476 1.00 12.83  ? 255 ARG C CZ  1 
ATOM   6465  N  NH1 . ARG C  1 255 ? 31.313  2.340   -46.505 1.00 12.45  ? 255 ARG C NH1 1 
ATOM   6466  N  NH2 . ARG C  1 255 ? 33.124  1.240   -47.386 1.00 12.56  ? 255 ARG C NH2 1 
ATOM   6467  N  N   . LEU C  1 256 ? 30.241  -3.579  -50.075 1.00 12.10  ? 256 LEU C N   1 
ATOM   6468  C  CA  . LEU C  1 256 ? 30.686  -4.897  -49.698 1.00 12.45  ? 256 LEU C CA  1 
ATOM   6469  C  C   . LEU C  1 256 ? 31.676  -4.816  -48.533 1.00 10.56  ? 256 LEU C C   1 
ATOM   6470  O  O   . LEU C  1 256 ? 32.355  -3.814  -48.324 1.00 12.09  ? 256 LEU C O   1 
ATOM   6471  C  CB  . LEU C  1 256 ? 31.416  -5.571  -50.894 1.00 14.20  ? 256 LEU C CB  1 
ATOM   6472  C  CG  . LEU C  1 256 ? 30.495  -5.860  -52.089 1.00 16.08  ? 256 LEU C CG  1 
ATOM   6473  C  CD1 . LEU C  1 256 ? 31.404  -6.183  -53.246 1.00 20.79  ? 256 LEU C CD1 1 
ATOM   6474  C  CD2 . LEU C  1 256 ? 29.533  -7.008  -51.791 1.00 20.94  ? 256 LEU C CD2 1 
ATOM   6475  N  N   . VAL C  1 257 ? 31.732  -5.892  -47.769 1.00 11.43  ? 257 VAL C N   1 
ATOM   6476  C  CA  . VAL C  1 257 ? 32.796  -6.106  -46.844 1.00 10.54  ? 257 VAL C CA  1 
ATOM   6477  C  C   . VAL C  1 257 ? 33.592  -7.274  -47.419 1.00 10.10  ? 257 VAL C C   1 
ATOM   6478  O  O   . VAL C  1 257 ? 33.044  -8.333  -47.764 1.00 11.77  ? 257 VAL C O   1 
ATOM   6479  C  CB  . VAL C  1 257 ? 32.243  -6.490  -45.460 1.00 11.54  ? 257 VAL C CB  1 
ATOM   6480  C  CG1 . VAL C  1 257 ? 33.410  -6.892  -44.576 1.00 12.74  ? 257 VAL C CG1 1 
ATOM   6481  C  CG2 . VAL C  1 257 ? 31.551  -5.253  -44.887 1.00 13.23  ? 257 VAL C CG2 1 
ATOM   6482  N  N   . TYR C  1 258 ? 34.880  -7.074  -47.542 1.00 9.72   ? 258 TYR C N   1 
ATOM   6483  C  CA  . TYR C  1 258 ? 35.734  -8.078  -48.153 1.00 10.11  ? 258 TYR C CA  1 
ATOM   6484  C  C   . TYR C  1 258 ? 36.267  -9.008  -47.092 1.00 10.64  ? 258 TYR C C   1 
ATOM   6485  O  O   . TYR C  1 258 ? 36.536  -8.589  -45.946 1.00 12.75  ? 258 TYR C O   1 
ATOM   6486  C  CB  . TYR C  1 258 ? 36.865  -7.349  -48.924 1.00 11.35  ? 258 TYR C CB  1 
ATOM   6487  C  CG  . TYR C  1 258 ? 36.241  -6.459  -49.978 1.00 11.27  ? 258 TYR C CG  1 
ATOM   6488  C  CD1 . TYR C  1 258 ? 35.785  -6.985  -51.181 1.00 13.04  ? 258 TYR C CD1 1 
ATOM   6489  C  CD2 . TYR C  1 258 ? 36.028  -5.111  -49.736 1.00 12.51  ? 258 TYR C CD2 1 
ATOM   6490  C  CE1 . TYR C  1 258 ? 35.179  -6.182  -52.132 1.00 17.50  ? 258 TYR C CE1 1 
ATOM   6491  C  CE2 . TYR C  1 258 ? 35.424  -4.301  -50.679 1.00 14.65  ? 258 TYR C CE2 1 
ATOM   6492  C  CZ  . TYR C  1 258 ? 35.001  -4.838  -51.872 1.00 15.56  ? 258 TYR C CZ  1 
ATOM   6493  O  OH  . TYR C  1 258 ? 34.404  -4.015  -52.800 1.00 20.42  ? 258 TYR C OH  1 
ATOM   6494  N  N   . THR C  1 259 ? 36.419  -10.300 -47.434 1.00 10.64  ? 259 THR C N   1 
ATOM   6495  C  CA  . THR C  1 259 ? 36.824  -11.237 -46.430 1.00 10.42  ? 259 THR C CA  1 
ATOM   6496  C  C   . THR C  1 259 ? 38.024  -11.993 -46.931 1.00 11.69  ? 259 THR C C   1 
ATOM   6497  O  O   . THR C  1 259 ? 38.206  -12.259 -48.131 1.00 12.21  ? 259 THR C O   1 
ATOM   6498  C  CB  . THR C  1 259 ? 35.711  -12.226 -46.080 1.00 11.91  ? 259 THR C CB  1 
ATOM   6499  O  OG1 . THR C  1 259 ? 35.330  -12.983 -47.265 1.00 13.67  ? 259 THR C OG1 1 
ATOM   6500  C  CG2 . THR C  1 259 ? 34.521  -11.547 -45.521 1.00 12.45  ? 259 THR C CG2 1 
ATOM   6501  N  N   . SER C  1 260 ? 38.917  -12.337 -45.990 1.00 12.07  ? 260 SER C N   1 
ATOM   6502  C  CA  . SER C  1 260 ? 40.150  -13.052 -46.336 1.00 13.63  ? 260 SER C CA  1 
ATOM   6503  C  C   . SER C  1 260 ? 39.878  -14.522 -46.336 1.00 14.88  ? 260 SER C C   1 
ATOM   6504  O  O   . SER C  1 260 ? 40.781  -15.292 -46.678 1.00 17.92  ? 260 SER C O   1 
ATOM   6505  C  CB  . SER C  1 260 ? 41.239  -12.746 -45.334 1.00 13.63  ? 260 SER C CB  1 
ATOM   6506  O  OG  . SER C  1 260 ? 40.854  -13.278 -44.090 1.00 13.15  ? 260 SER C OG  1 
ATOM   6507  N  N   . PHE C  1 261 ? 38.680  -14.945 -45.991 1.00 14.70  ? 261 PHE C N   1 
ATOM   6508  C  CA  . PHE C  1 261 ? 38.322  -16.320 -45.809 1.00 16.22  ? 261 PHE C CA  1 
ATOM   6509  C  C   . PHE C  1 261 ? 37.194  -16.536 -46.739 1.00 18.86  ? 261 PHE C C   1 
ATOM   6510  O  O   . PHE C  1 261 ? 36.458  -15.627 -47.114 1.00 17.53  ? 261 PHE C O   1 
ATOM   6511  C  CB  . PHE C  1 261 ? 37.871  -16.633 -44.389 1.00 17.44  ? 261 PHE C CB  1 
ATOM   6512  C  CG  . PHE C  1 261 ? 36.844  -15.687 -43.827 1.00 14.92  ? 261 PHE C CG  1 
ATOM   6513  C  CD1 . PHE C  1 261 ? 37.235  -14.529 -43.209 1.00 14.53  ? 261 PHE C CD1 1 
ATOM   6514  C  CD2 . PHE C  1 261 ? 35.500  -15.980 -43.892 1.00 16.44  ? 261 PHE C CD2 1 
ATOM   6515  C  CE1 . PHE C  1 261 ? 36.295  -13.671 -42.652 1.00 15.37  ? 261 PHE C CE1 1 
ATOM   6516  C  CE2 . PHE C  1 261 ? 34.531  -15.141 -43.340 1.00 20.94  ? 261 PHE C CE2 1 
ATOM   6517  C  CZ  . PHE C  1 261 ? 34.946  -13.947 -42.697 1.00 17.96  ? 261 PHE C CZ  1 
ATOM   6518  N  N   . SER C  1 262 ? 37.039  -17.756 -47.185 1.00 23.83  ? 262 SER C N   1 
ATOM   6519  C  CA  . SER C  1 262 ? 35.811  -17.978 -47.968 1.00 34.65  ? 262 SER C CA  1 
ATOM   6520  C  C   . SER C  1 262 ? 34.804  -18.709 -47.152 1.00 54.27  ? 262 SER C C   1 
ATOM   6521  O  O   . SER C  1 262 ? 33.591  -18.354 -47.092 1.00 94.84  ? 262 SER C O   1 
ATOM   6522  C  CB  . SER C  1 262 ? 36.031  -18.834 -49.160 1.00 46.15  ? 262 SER C CB  1 
ATOM   6523  O  OG  . SER C  1 262 ? 34.955  -19.731 -49.088 1.00 38.05  ? 262 SER C OG  1 
ATOM   6524  N  N   . GLN C  1 263 ? 35.336  -19.722 -46.530 1.00 32.33  ? 263 GLN C N   1 
ATOM   6525  C  CA  . GLN C  1 263 ? 34.479  -20.718 -45.932 1.00 41.41  ? 263 GLN C CA  1 
ATOM   6526  C  C   . GLN C  1 263 ? 34.449  -20.382 -44.444 1.00 71.60  ? 263 GLN C C   1 
ATOM   6527  O  O   . GLN C  1 263 ? 35.430  -19.800 -43.972 1.00 49.21  ? 263 GLN C O   1 
ATOM   6528  C  CB  . GLN C  1 263 ? 34.995  -22.129 -46.201 1.00 30.78  ? 263 GLN C CB  1 
ATOM   6529  C  CG  . GLN C  1 263 ? 36.353  -22.510 -45.552 1.00 31.08  ? 263 GLN C CG  1 
ATOM   6530  C  CD  . GLN C  1 263 ? 36.885  -23.906 -45.906 1.00 21.16  ? 263 GLN C CD  1 
ATOM   6531  O  OE1 . GLN C  1 263 ? 38.062  -24.232 -45.536 1.00 28.75  ? 263 GLN C OE1 1 
ATOM   6532  N  NE2 . GLN C  1 263 ? 36.085  -24.720 -46.596 1.00 19.23  ? 263 GLN C NE2 1 
ATOM   6533  N  N   . LYS D  1 3   ? 14.045  19.725  -45.225 1.00 45.28  ? 3   LYS D N   1 
ATOM   6534  C  CA  . LYS D  1 3   ? 14.739  18.912  -46.263 1.00 34.77  ? 3   LYS D CA  1 
ATOM   6535  C  C   . LYS D  1 3   ? 15.488  17.711  -45.671 1.00 23.47  ? 3   LYS D C   1 
ATOM   6536  O  O   . LYS D  1 3   ? 16.446  17.189  -46.275 1.00 23.41  ? 3   LYS D O   1 
ATOM   6537  C  CB  . LYS D  1 3   ? 15.722  19.716  -47.088 1.00 43.53  ? 3   LYS D CB  1 
ATOM   6538  C  CG  . LYS D  1 3   ? 16.899  20.311  -46.329 1.00 61.73  ? 3   LYS D CG  1 
ATOM   6539  C  CD  . LYS D  1 3   ? 17.826  21.075  -47.259 1.00 118.50 ? 3   LYS D CD  1 
ATOM   6540  C  CE  . LYS D  1 3   ? 19.114  20.307  -47.510 1.00 159.32 ? 3   LYS D CE  1 
ATOM   6541  N  NZ  . LYS D  1 3   ? 20.151  20.612  -46.487 1.00 280.96 ? 3   LYS D NZ  1 
ATOM   6542  N  N   . TRP D  1 4   ? 15.075  17.243  -44.488 1.00 15.83  ? 4   TRP D N   1 
ATOM   6543  C  CA  . TRP D  1 4   ? 15.710  16.080  -43.875 1.00 12.43  ? 4   TRP D CA  1 
ATOM   6544  C  C   . TRP D  1 4   ? 15.459  14.857  -44.755 1.00 11.33  ? 4   TRP D C   1 
ATOM   6545  O  O   . TRP D  1 4   ? 14.441  14.787  -45.449 1.00 12.88  ? 4   TRP D O   1 
ATOM   6546  C  CB  . TRP D  1 4   ? 15.246  15.845  -42.460 1.00 12.39  ? 4   TRP D CB  1 
ATOM   6547  C  CG  . TRP D  1 4   ? 13.824  15.542  -42.273 1.00 10.25  ? 4   TRP D CG  1 
ATOM   6548  C  CD1 . TRP D  1 4   ? 12.804  16.430  -41.982 1.00 12.47  ? 4   TRP D CD1 1 
ATOM   6549  C  CD2 . TRP D  1 4   ? 13.186  14.248  -42.305 1.00 10.18  ? 4   TRP D CD2 1 
ATOM   6550  N  NE1 . TRP D  1 4   ? 11.611  15.800  -41.835 1.00 12.63  ? 4   TRP D NE1 1 
ATOM   6551  C  CE2 . TRP D  1 4   ? 11.792  14.458  -42.002 1.00 10.84  ? 4   TRP D CE2 1 
ATOM   6552  C  CE3 . TRP D  1 4   ? 13.676  12.934  -42.430 1.00 10.74  ? 4   TRP D CE3 1 
ATOM   6553  C  CZ2 . TRP D  1 4   ? 10.887  13.416  -41.953 1.00 13.45  ? 4   TRP D CZ2 1 
ATOM   6554  C  CZ3 . TRP D  1 4   ? 12.725  11.913  -42.378 1.00 12.47  ? 4   TRP D CZ3 1 
ATOM   6555  C  CH2 . TRP D  1 4   ? 11.375  12.124  -42.098 1.00 12.29  ? 4   TRP D CH2 1 
ATOM   6556  N  N   . THR D  1 5   ? 16.375  13.900  -44.696 1.00 11.16  ? 5   THR D N   1 
ATOM   6557  C  CA  . THR D  1 5   ? 16.282  12.684  -45.532 1.00 11.15  ? 5   THR D CA  1 
ATOM   6558  C  C   . THR D  1 5   ? 16.727  11.486  -44.686 1.00 10.40  ? 5   THR D C   1 
ATOM   6559  O  O   . THR D  1 5   ? 17.128  11.631  -43.530 1.00 10.01  ? 5   THR D O   1 
ATOM   6560  C  CB  . THR D  1 5   ? 17.188  12.820  -46.783 1.00 12.04  ? 5   THR D CB  1 
ATOM   6561  O  OG1 . THR D  1 5   ? 18.503  12.711  -46.312 1.00 13.43  ? 5   THR D OG1 1 
ATOM   6562  C  CG2 . THR D  1 5   ? 16.917  14.054  -47.620 1.00 14.25  ? 5   THR D CG2 1 
ATOM   6563  N  N   . TYR D  1 6   ? 16.759  10.330  -45.360 1.00 10.82  ? 6   TYR D N   1 
ATOM   6564  C  CA  . TYR D  1 6   ? 17.354  9.141   -44.745 1.00 10.56  ? 6   TYR D CA  1 
ATOM   6565  C  C   . TYR D  1 6   ? 18.708  8.792   -45.344 1.00 10.98  ? 6   TYR D C   1 
ATOM   6566  O  O   . TYR D  1 6   ? 19.244  7.721   -45.006 1.00 11.91  ? 6   TYR D O   1 
ATOM   6567  C  CB  . TYR D  1 6   ? 16.414  7.943   -44.921 1.00 10.90  ? 6   TYR D CB  1 
ATOM   6568  C  CG  . TYR D  1 6   ? 15.198  8.040   -44.073 1.00 9.37   ? 6   TYR D CG  1 
ATOM   6569  C  CD1 . TYR D  1 6   ? 15.232  7.528   -42.771 1.00 9.11   ? 6   TYR D CD1 1 
ATOM   6570  C  CD2 . TYR D  1 6   ? 14.003  8.576   -44.517 1.00 9.58   ? 6   TYR D CD2 1 
ATOM   6571  C  CE1 . TYR D  1 6   ? 14.075  7.540   -41.982 1.00 8.38   ? 6   TYR D CE1 1 
ATOM   6572  C  CE2 . TYR D  1 6   ? 12.846  8.577   -43.738 1.00 9.37   ? 6   TYR D CE2 1 
ATOM   6573  C  CZ  . TYR D  1 6   ? 12.895  8.020   -42.465 1.00 8.45   ? 6   TYR D CZ  1 
ATOM   6574  O  OH  . TYR D  1 6   ? 11.737  8.007   -41.726 1.00 10.24  ? 6   TYR D OH  1 
ATOM   6575  N  N   . PHE D  1 7   ? 19.274  9.629   -46.197 1.00 11.78  ? 7   PHE D N   1 
ATOM   6576  C  CA  . PHE D  1 7   ? 20.506  9.210   -46.910 1.00 14.25  ? 7   PHE D CA  1 
ATOM   6577  C  C   . PHE D  1 7   ? 21.266  10.436  -47.320 1.00 15.97  ? 7   PHE D C   1 
ATOM   6578  O  O   . PHE D  1 7   ? 20.677  11.297  -47.967 1.00 15.46  ? 7   PHE D O   1 
ATOM   6579  C  CB  . PHE D  1 7   ? 20.146  8.398   -48.175 1.00 18.63  ? 7   PHE D CB  1 
ATOM   6580  C  CG  . PHE D  1 7   ? 21.357  7.988   -48.955 1.00 20.92  ? 7   PHE D CG  1 
ATOM   6581  C  CD1 . PHE D  1 7   ? 22.172  6.892   -48.527 1.00 24.98  ? 7   PHE D CD1 1 
ATOM   6582  C  CD2 . PHE D  1 7   ? 21.809  8.741   -50.039 1.00 28.20  ? 7   PHE D CD2 1 
ATOM   6583  C  CE1 . PHE D  1 7   ? 23.301  6.482   -49.208 1.00 27.19  ? 7   PHE D CE1 1 
ATOM   6584  C  CE2 . PHE D  1 7   ? 22.949  8.363   -50.676 1.00 39.05  ? 7   PHE D CE2 1 
ATOM   6585  C  CZ  . PHE D  1 7   ? 23.692  7.244   -50.293 1.00 39.28  ? 7   PHE D CZ  1 
ATOM   6586  N  N   . GLY D  1 8   ? 22.554  10.474  -47.029 1.00 15.43  ? 8   GLY D N   1 
ATOM   6587  C  CA  . GLY D  1 8   ? 23.376  11.556  -47.527 1.00 16.12  ? 8   GLY D CA  1 
ATOM   6588  C  C   . GLY D  1 8   ? 23.517  12.617  -46.481 1.00 15.41  ? 8   GLY D C   1 
ATOM   6589  O  O   . GLY D  1 8   ? 23.296  12.410  -45.251 1.00 15.38  ? 8   GLY D O   1 
ATOM   6590  N  N   . PRO D  1 9   ? 23.925  13.831  -46.894 1.00 17.32  ? 9   PRO D N   1 
ATOM   6591  C  CA  . PRO D  1 9   ? 24.283  14.883  -45.949 1.00 19.57  ? 9   PRO D CA  1 
ATOM   6592  C  C   . PRO D  1 9   ? 23.211  15.301  -44.993 1.00 15.54  ? 9   PRO D C   1 
ATOM   6593  O  O   . PRO D  1 9   ? 23.517  15.805  -43.927 1.00 18.29  ? 9   PRO D O   1 
ATOM   6594  C  CB  . PRO D  1 9   ? 24.676  16.091  -46.888 1.00 21.17  ? 9   PRO D CB  1 
ATOM   6595  C  CG  . PRO D  1 9   ? 24.878  15.519  -48.244 1.00 27.20  ? 9   PRO D CG  1 
ATOM   6596  C  CD  . PRO D  1 9   ? 24.164  14.211  -48.342 1.00 19.39  ? 9   PRO D CD  1 
ATOM   6597  N  N   . ASP D  1 10  ? 21.947  15.140  -45.411 1.00 14.94  ? 10  ASP D N   1 
ATOM   6598  C  CA  . ASP D  1 10  ? 20.809  15.513  -44.530 1.00 14.33  ? 10  ASP D CA  1 
ATOM   6599  C  C   . ASP D  1 10  ? 20.161  14.324  -43.856 1.00 11.70  ? 10  ASP D C   1 
ATOM   6600  O  O   . ASP D  1 10  ? 19.025  14.426  -43.351 1.00 12.00  ? 10  ASP D O   1 
ATOM   6601  C  CB  . ASP D  1 10  ? 19.761  16.334  -45.297 1.00 16.38  ? 10  ASP D CB  1 
ATOM   6602  C  CG  . ASP D  1 10  ? 20.377  17.594  -45.918 1.00 23.21  ? 10  ASP D CG  1 
ATOM   6603  O  OD1 . ASP D  1 10  ? 21.072  18.308  -45.163 1.00 23.12  ? 10  ASP D OD1 1 
ATOM   6604  O  OD2 . ASP D  1 10  ? 20.256  17.781  -47.142 1.00 27.51  ? 10  ASP D OD2 1 
ATOM   6605  N  N   . GLY D  1 11  ? 20.848  13.208  -43.833 1.00 11.92  ? 11  GLY D N   1 
ATOM   6606  C  CA  . GLY D  1 11  ? 20.356  12.000  -43.197 1.00 9.97   ? 11  GLY D CA  1 
ATOM   6607  C  C   . GLY D  1 11  ? 20.442  12.005  -41.691 1.00 9.29   ? 11  GLY D C   1 
ATOM   6608  O  O   . GLY D  1 11  ? 20.660  13.057  -41.046 1.00 9.47   ? 11  GLY D O   1 
ATOM   6609  N  N   . GLU D  1 12  ? 20.178  10.843  -41.092 1.00 8.71   ? 12  GLU D N   1 
ATOM   6610  C  CA  . GLU D  1 12  ? 19.768  10.801  -39.693 1.00 8.34   ? 12  GLU D CA  1 
ATOM   6611  C  C   . GLU D  1 12  ? 20.821  11.257  -38.706 1.00 7.76   ? 12  GLU D C   1 
ATOM   6612  O  O   . GLU D  1 12  ? 20.469  11.756  -37.648 1.00 8.96   ? 12  GLU D O   1 
ATOM   6613  C  CB  . GLU D  1 12  ? 19.294  9.385   -39.306 1.00 8.52   ? 12  GLU D CB  1 
ATOM   6614  C  CG  . GLU D  1 12  ? 20.422  8.365   -39.219 1.00 8.22   ? 12  GLU D CG  1 
ATOM   6615  C  CD  . GLU D  1 12  ? 19.812  6.979   -39.258 1.00 8.11   ? 12  GLU D CD  1 
ATOM   6616  O  OE1 . GLU D  1 12  ? 19.429  6.474   -38.167 1.00 8.54   ? 12  GLU D OE1 1 
ATOM   6617  O  OE2 . GLU D  1 12  ? 19.624  6.417   -40.357 1.00 9.62   ? 12  GLU D OE2 1 
ATOM   6618  N  N   . ASN D  1 13  ? 22.108  11.165  -39.028 1.00 8.55   ? 13  ASN D N   1 
ATOM   6619  C  CA  . ASN D  1 13  ? 23.108  11.668  -38.124 1.00 8.33   ? 13  ASN D CA  1 
ATOM   6620  C  C   . ASN D  1 13  ? 23.156  13.208  -38.123 1.00 9.06   ? 13  ASN D C   1 
ATOM   6621  O  O   . ASN D  1 13  ? 23.786  13.746  -37.210 1.00 10.41  ? 13  ASN D O   1 
ATOM   6622  C  CB  . ASN D  1 13  ? 24.492  11.163  -38.496 1.00 9.11   ? 13  ASN D CB  1 
ATOM   6623  C  CG  . ASN D  1 13  ? 24.644  9.667   -38.192 1.00 9.08   ? 13  ASN D CG  1 
ATOM   6624  O  OD1 . ASN D  1 13  ? 23.746  8.991   -37.695 1.00 9.05   ? 13  ASN D OD1 1 
ATOM   6625  N  ND2 . ASN D  1 13  ? 25.826  9.123   -38.467 1.00 8.84   ? 13  ASN D ND2 1 
ATOM   6626  N  N   . SER D  1 14  ? 22.482  13.846  -39.048 1.00 9.08   ? 14  SER D N   1 
ATOM   6627  C  CA  . SER D  1 14  ? 22.418  15.316  -39.136 1.00 9.47   ? 14  SER D CA  1 
ATOM   6628  C  C   . SER D  1 14  ? 21.112  15.893  -38.653 1.00 8.44   ? 14  SER D C   1 
ATOM   6629  O  O   . SER D  1 14  ? 21.000  17.090  -38.525 1.00 9.30   ? 14  SER D O   1 
ATOM   6630  C  CB  . SER D  1 14  ? 22.710  15.729  -40.581 1.00 10.34  ? 14  SER D CB  1 
ATOM   6631  O  OG  . SER D  1 14  ? 24.088  15.462  -40.835 1.00 11.98  ? 14  SER D OG  1 
ATOM   6632  N  N   . TRP D  1 15  ? 20.087  15.073  -38.382 1.00 8.41   ? 15  TRP D N   1 
ATOM   6633  C  CA  . TRP D  1 15  ? 18.796  15.586  -38.003 1.00 7.94   ? 15  TRP D CA  1 
ATOM   6634  C  C   . TRP D  1 15  ? 18.849  16.536  -36.810 1.00 7.90   ? 15  TRP D C   1 
ATOM   6635  O  O   . TRP D  1 15  ? 18.160  17.559  -36.792 1.00 9.34   ? 15  TRP D O   1 
ATOM   6636  C  CB  . TRP D  1 15  ? 17.815  14.451  -37.654 1.00 8.75   ? 15  TRP D CB  1 
ATOM   6637  C  CG  . TRP D  1 15  ? 17.426  13.592  -38.811 1.00 7.82   ? 15  TRP D CG  1 
ATOM   6638  C  CD1 . TRP D  1 15  ? 17.632  13.764  -40.164 1.00 8.46   ? 15  TRP D CD1 1 
ATOM   6639  C  CD2 . TRP D  1 15  ? 16.678  12.390  -38.690 1.00 7.79   ? 15  TRP D CD2 1 
ATOM   6640  N  NE1 . TRP D  1 15  ? 17.095  12.765  -40.898 1.00 8.07   ? 15  TRP D NE1 1 
ATOM   6641  C  CE2 . TRP D  1 15  ? 16.464  11.908  -40.037 1.00 7.83   ? 15  TRP D CE2 1 
ATOM   6642  C  CE3 . TRP D  1 15  ? 16.112  11.662  -37.615 1.00 8.32   ? 15  TRP D CE3 1 
ATOM   6643  C  CZ2 . TRP D  1 15  ? 15.785  10.717  -40.290 1.00 8.47   ? 15  TRP D CZ2 1 
ATOM   6644  C  CZ3 . TRP D  1 15  ? 15.427  10.494  -37.887 1.00 8.46   ? 15  TRP D CZ3 1 
ATOM   6645  C  CH2 . TRP D  1 15  ? 15.266  10.052  -39.200 1.00 8.26   ? 15  TRP D CH2 1 
ATOM   6646  N  N   . SER D  1 16  ? 19.719  16.224  -35.878 1.00 8.66   ? 16  SER D N   1 
ATOM   6647  C  CA  . SER D  1 16  ? 19.819  17.020  -34.645 1.00 9.44   ? 16  SER D CA  1 
ATOM   6648  C  C   . SER D  1 16  ? 20.331  18.428  -34.932 1.00 9.21   ? 16  SER D C   1 
ATOM   6649  O  O   . SER D  1 16  ? 20.151  19.282  -34.038 1.00 10.90  ? 16  SER D O   1 
ATOM   6650  C  CB  . SER D  1 16  ? 20.749  16.332  -33.667 1.00 10.90  ? 16  SER D CB  1 
ATOM   6651  O  OG  . SER D  1 16  ? 22.102  16.461  -34.184 1.00 15.46  ? 16  SER D OG  1 
ATOM   6652  N  N   . LYS D  1 17  ? 20.871  18.722  -36.091 1.00 9.95   ? 17  LYS D N   1 
ATOM   6653  C  CA  . LYS D  1 17  ? 21.350  20.089  -36.354 1.00 9.53   ? 17  LYS D CA  1 
ATOM   6654  C  C   . LYS D  1 17  ? 20.159  21.003  -36.410 1.00 9.85   ? 17  LYS D C   1 
ATOM   6655  O  O   . LYS D  1 17  ? 20.315  22.211  -36.100 1.00 12.06  ? 17  LYS D O   1 
ATOM   6656  C  CB  . LYS D  1 17  ? 22.128  20.104  -37.660 1.00 10.61  ? 17  LYS D CB  1 
ATOM   6657  C  CG  . LYS D  1 17  ? 23.366  19.251  -37.669 1.00 11.13  ? 17  LYS D CG  1 
ATOM   6658  C  CD  . LYS D  1 17  ? 23.987  19.250  -39.058 1.00 11.80  ? 17  LYS D CD  1 
ATOM   6659  C  CE  . LYS D  1 17  ? 25.142  18.278  -39.218 1.00 12.01  ? 17  LYS D CE  1 
ATOM   6660  N  NZ  . LYS D  1 17  ? 25.785  18.449  -40.579 1.00 12.98  ? 17  LYS D NZ  1 
ATOM   6661  N  N   . LYS D  1 18  ? 19.038  20.554  -36.874 1.00 10.18  ? 18  LYS D N   1 
ATOM   6662  C  CA  . LYS D  1 18  ? 17.821  21.352  -37.037 1.00 10.87  ? 18  LYS D CA  1 
ATOM   6663  C  C   . LYS D  1 18  ? 16.735  20.972  -36.039 1.00 11.58  ? 18  LYS D C   1 
ATOM   6664  O  O   . LYS D  1 18  ? 15.870  21.772  -35.769 1.00 13.55  ? 18  LYS D O   1 
ATOM   6665  C  CB  . LYS D  1 18  ? 17.266  21.259  -38.468 1.00 13.40  ? 18  LYS D CB  1 
ATOM   6666  C  CG  . LYS D  1 18  ? 18.121  21.967  -39.547 1.00 19.42  ? 18  LYS D CG  1 
ATOM   6667  C  CD  . LYS D  1 18  ? 17.507  21.792  -40.972 1.00 24.74  ? 18  LYS D CD  1 
ATOM   6668  C  CE  . LYS D  1 18  ? 18.094  22.746  -42.027 1.00 46.79  ? 18  LYS D CE  1 
ATOM   6669  N  NZ  . LYS D  1 18  ? 17.878  22.198  -43.469 1.00 199.33 ? 18  LYS D NZ  1 
ATOM   6670  N  N   . TYR D  1 19  ? 16.790  19.756  -35.516 1.00 9.07   ? 19  TYR D N   1 
ATOM   6671  C  CA  . TYR D  1 19  ? 15.732  19.212  -34.699 1.00 9.30   ? 19  TYR D CA  1 
ATOM   6672  C  C   . TYR D  1 19  ? 16.334  18.703  -33.420 1.00 9.37   ? 19  TYR D C   1 
ATOM   6673  O  O   . TYR D  1 19  ? 16.752  17.558  -33.359 1.00 10.12  ? 19  TYR D O   1 
ATOM   6674  C  CB  . TYR D  1 19  ? 15.047  18.052  -35.456 1.00 10.97  ? 19  TYR D CB  1 
ATOM   6675  C  CG  . TYR D  1 19  ? 14.438  18.485  -36.740 1.00 10.36  ? 19  TYR D CG  1 
ATOM   6676  C  CD1 . TYR D  1 19  ? 13.216  19.145  -36.773 1.00 11.51  ? 19  TYR D CD1 1 
ATOM   6677  C  CD2 . TYR D  1 19  ? 15.116  18.260  -37.962 1.00 10.37  ? 19  TYR D CD2 1 
ATOM   6678  C  CE1 . TYR D  1 19  ? 12.619  19.518  -37.957 1.00 14.05  ? 19  TYR D CE1 1 
ATOM   6679  C  CE2 . TYR D  1 19  ? 14.512  18.686  -39.147 1.00 12.06  ? 19  TYR D CE2 1 
ATOM   6680  C  CZ  . TYR D  1 19  ? 13.316  19.318  -39.148 1.00 13.78  ? 19  TYR D CZ  1 
ATOM   6681  O  OH  . TYR D  1 19  ? 12.758  19.652  -40.361 1.00 17.56  ? 19  TYR D OH  1 
ATOM   6682  N  N   . PRO D  1 20  ? 16.429  19.566  -32.417 1.00 10.31  ? 20  PRO D N   1 
ATOM   6683  C  CA  . PRO D  1 20  ? 17.229  19.213  -31.261 1.00 11.82  ? 20  PRO D CA  1 
ATOM   6684  C  C   . PRO D  1 20  ? 16.747  17.945  -30.527 1.00 10.13  ? 20  PRO D C   1 
ATOM   6685  O  O   . PRO D  1 20  ? 17.603  17.239  -29.924 1.00 11.36  ? 20  PRO D O   1 
ATOM   6686  C  CB  . PRO D  1 20  ? 17.079  20.427  -30.315 1.00 14.26  ? 20  PRO D CB  1 
ATOM   6687  C  CG  . PRO D  1 20  ? 16.376  21.365  -31.060 1.00 18.95  ? 20  PRO D CG  1 
ATOM   6688  C  CD  . PRO D  1 20  ? 15.926  20.965  -32.371 1.00 11.38  ? 20  PRO D CD  1 
ATOM   6689  N  N   . SER D  1 21  ? 15.441  17.645  -30.584 1.00 10.26  ? 21  SER D N   1 
ATOM   6690  C  CA  . SER D  1 21  ? 15.016  16.444  -29.879 1.00 9.96   ? 21  SER D CA  1 
ATOM   6691  C  C   . SER D  1 21  ? 15.574  15.160  -30.512 1.00 9.59   ? 21  SER D C   1 
ATOM   6692  O  O   . SER D  1 21  ? 15.603  14.138  -29.829 1.00 10.99  ? 21  SER D O   1 
ATOM   6693  C  CB  . SER D  1 21  ? 13.530  16.365  -29.829 1.00 10.83  ? 21  SER D CB  1 
ATOM   6694  O  OG  . SER D  1 21  ? 12.979  17.346  -28.980 1.00 13.98  ? 21  SER D OG  1 
ATOM   6695  N  N   . CYS D  1 22  ? 16.018  15.198  -31.755 1.00 9.33   ? 22  CYS D N   1 
ATOM   6696  C  CA  . CYS D  1 22  ? 16.607  14.043  -32.371 1.00 9.59   ? 22  CYS D CA  1 
ATOM   6697  C  C   . CYS D  1 22  ? 17.941  13.646  -31.746 1.00 10.15  ? 22  CYS D C   1 
ATOM   6698  O  O   . CYS D  1 22  ? 18.384  12.526  -31.927 1.00 11.80  ? 22  CYS D O   1 
ATOM   6699  C  CB  . CYS D  1 22  ? 16.785  14.245  -33.868 1.00 10.02  ? 22  CYS D CB  1 
ATOM   6700  S  SG  . CYS D  1 22  ? 15.263  14.539  -34.778 1.00 9.53   ? 22  CYS D SG  1 
ATOM   6701  N  N   . GLY D  1 23  ? 18.564  14.607  -30.977 1.00 11.34  ? 23  GLY D N   1 
ATOM   6702  C  CA  . GLY D  1 23  ? 19.731  14.345  -30.184 1.00 12.73  ? 23  GLY D CA  1 
ATOM   6703  C  C   . GLY D  1 23  ? 19.467  14.281  -28.691 1.00 14.50  ? 23  GLY D C   1 
ATOM   6704  O  O   . GLY D  1 23  ? 20.374  14.243  -27.898 1.00 15.63  ? 23  GLY D O   1 
ATOM   6705  N  N   . GLY D  1 24  ? 18.193  14.197  -28.340 1.00 13.82  ? 24  GLY D N   1 
ATOM   6706  C  CA  . GLY D  1 24  ? 17.767  14.194  -26.935 1.00 15.33  ? 24  GLY D CA  1 
ATOM   6707  C  C   . GLY D  1 24  ? 17.527  12.818  -26.396 1.00 15.70  ? 24  GLY D C   1 
ATOM   6708  O  O   . GLY D  1 24  ? 17.993  11.797  -26.949 1.00 18.93  ? 24  GLY D O   1 
ATOM   6709  N  N   . LEU D  1 25  ? 16.871  12.733  -25.284 1.00 20.16  ? 25  LEU D N   1 
ATOM   6710  C  CA  . LEU D  1 25  ? 16.610  11.466  -24.676 1.00 23.30  ? 25  LEU D CA  1 
ATOM   6711  C  C   . LEU D  1 25  ? 15.449  10.704  -25.306 1.00 16.61  ? 25  LEU D C   1 
ATOM   6712  O  O   . LEU D  1 25  ? 14.629  11.269  -26.082 1.00 15.71  ? 25  LEU D O   1 
ATOM   6713  C  CB  . LEU D  1 25  ? 16.292  11.658  -23.206 1.00 36.78  ? 25  LEU D CB  1 
ATOM   6714  C  CG  . LEU D  1 25  ? 17.381  12.379  -22.383 1.00 63.99  ? 25  LEU D CG  1 
ATOM   6715  C  CD1 . LEU D  1 25  ? 16.937  12.557  -20.903 1.00 81.77  ? 25  LEU D CD1 1 
ATOM   6716  C  CD2 . LEU D  1 25  ? 18.729  11.592  -22.521 1.00 65.66  ? 25  LEU D CD2 1 
ATOM   6717  N  N   . LEU D  1 26  ? 15.296  9.445   -24.899 1.00 18.38  ? 26  LEU D N   1 
ATOM   6718  C  CA  . LEU D  1 26  ? 14.105  8.619   -25.168 1.00 16.15  ? 26  LEU D CA  1 
ATOM   6719  C  C   . LEU D  1 26  ? 13.815  8.436   -26.638 1.00 12.09  ? 26  LEU D C   1 
ATOM   6720  O  O   . LEU D  1 26  ? 12.658  8.392   -27.071 1.00 13.07  ? 26  LEU D O   1 
ATOM   6721  C  CB  . LEU D  1 26  ? 12.820  9.174   -24.478 1.00 20.63  ? 26  LEU D CB  1 
ATOM   6722  C  CG  . LEU D  1 26  ? 12.883  9.232   -23.011 1.00 36.49  ? 26  LEU D CG  1 
ATOM   6723  C  CD1 . LEU D  1 26  ? 11.507  9.670   -22.491 1.00 35.65  ? 26  LEU D CD1 1 
ATOM   6724  C  CD2 . LEU D  1 26  ? 13.360  7.982   -22.281 1.00 35.14  ? 26  LEU D CD2 1 
ATOM   6725  N  N   . GLN D  1 27  ? 14.859  8.265   -27.430 1.00 11.24  ? 27  GLN D N   1 
ATOM   6726  C  CA  . GLN D  1 27  ? 14.650  8.121   -28.889 1.00 9.00   ? 27  GLN D CA  1 
ATOM   6727  C  C   . GLN D  1 27  ? 14.249  6.724   -29.282 1.00 8.76   ? 27  GLN D C   1 
ATOM   6728  O  O   . GLN D  1 27  ? 14.668  5.705   -28.695 1.00 10.58  ? 27  GLN D O   1 
ATOM   6729  C  CB  . GLN D  1 27  ? 15.933  8.559   -29.641 1.00 10.17  ? 27  GLN D CB  1 
ATOM   6730  C  CG  . GLN D  1 27  ? 16.240  10.049  -29.433 1.00 11.13  ? 27  GLN D CG  1 
ATOM   6731  C  CD  . GLN D  1 27  ? 15.192  10.911  -30.065 1.00 9.20   ? 27  GLN D CD  1 
ATOM   6732  O  OE1 . GLN D  1 27  ? 15.184  11.032  -31.289 1.00 9.94   ? 27  GLN D OE1 1 
ATOM   6733  N  NE2 . GLN D  1 27  ? 14.234  11.462  -29.279 1.00 9.72   ? 27  GLN D NE2 1 
ATOM   6734  N  N   . SER D  1 28  ? 13.502  6.669   -30.367 1.00 9.02   ? 28  SER D N   1 
ATOM   6735  C  CA  . SER D  1 28  ? 13.070  5.425   -31.010 1.00 8.31   ? 28  SER D CA  1 
ATOM   6736  C  C   . SER D  1 28  ? 13.650  5.424   -32.456 1.00 7.60   ? 28  SER D C   1 
ATOM   6737  O  O   . SER D  1 28  ? 13.945  6.468   -33.026 1.00 8.60   ? 28  SER D O   1 
ATOM   6738  C  CB  . SER D  1 28  ? 11.572  5.427   -31.058 1.00 8.10   ? 28  SER D CB  1 
ATOM   6739  O  OG  . SER D  1 28  ? 11.034  5.346   -29.779 1.00 8.94   ? 28  SER D OG  1 
ATOM   6740  N  N   . PRO D  1 29  ? 13.748  4.241   -33.091 1.00 6.96   ? 29  PRO D N   1 
ATOM   6741  C  CA  . PRO D  1 29  ? 13.370  2.914   -32.596 1.00 7.53   ? 29  PRO D CA  1 
ATOM   6742  C  C   . PRO D  1 29  ? 14.500  2.311   -31.800 1.00 7.62   ? 29  PRO D C   1 
ATOM   6743  O  O   . PRO D  1 29  ? 15.532  2.911   -31.605 1.00 8.03   ? 29  PRO D O   1 
ATOM   6744  C  CB  . PRO D  1 29  ? 13.092  2.199   -33.932 1.00 8.34   ? 29  PRO D CB  1 
ATOM   6745  C  CG  . PRO D  1 29  ? 14.239  2.729   -34.803 1.00 8.15   ? 29  PRO D CG  1 
ATOM   6746  C  CD  . PRO D  1 29  ? 14.261  4.192   -34.473 1.00 7.79   ? 29  PRO D CD  1 
ATOM   6747  N  N   . ILE D  1 30  ? 14.247  1.091   -31.340 1.00 7.88   ? 30  ILE D N   1 
ATOM   6748  C  CA  . ILE D  1 30  ? 15.202  0.347   -30.501 1.00 8.35   ? 30  ILE D CA  1 
ATOM   6749  C  C   . ILE D  1 30  ? 15.191  -1.085  -30.917 1.00 8.23   ? 30  ILE D C   1 
ATOM   6750  O  O   . ILE D  1 30  ? 14.277  -1.592  -31.588 1.00 8.82   ? 30  ILE D O   1 
ATOM   6751  C  CB  . ILE D  1 30  ? 14.885  0.509   -29.006 1.00 9.82   ? 30  ILE D CB  1 
ATOM   6752  C  CG1 . ILE D  1 30  ? 13.475  -0.041  -28.657 1.00 11.38  ? 30  ILE D CG1 1 
ATOM   6753  C  CG2 . ILE D  1 30  ? 15.105  1.991   -28.565 1.00 13.37  ? 30  ILE D CG2 1 
ATOM   6754  C  CD1 . ILE D  1 30  ? 13.146  -0.159  -27.185 1.00 13.24  ? 30  ILE D CD1 1 
ATOM   6755  N  N   . ASP D  1 31  ? 16.266  -1.771  -30.475 1.00 8.13   ? 31  ASP D N   1 
ATOM   6756  C  CA  . ASP D  1 31  ? 16.376  -3.225  -30.633 1.00 8.57   ? 31  ASP D CA  1 
ATOM   6757  C  C   . ASP D  1 31  ? 15.739  -3.914  -29.428 1.00 8.88   ? 31  ASP D C   1 
ATOM   6758  O  O   . ASP D  1 31  ? 16.160  -3.703  -28.301 1.00 12.48  ? 31  ASP D O   1 
ATOM   6759  C  CB  . ASP D  1 31  ? 17.835  -3.645  -30.719 1.00 10.36  ? 31  ASP D CB  1 
ATOM   6760  C  CG  . ASP D  1 31  ? 17.931  -5.153  -30.835 1.00 10.70  ? 31  ASP D CG  1 
ATOM   6761  O  OD1 . ASP D  1 31  ? 17.392  -5.760  -31.796 1.00 11.46  ? 31  ASP D OD1 1 
ATOM   6762  O  OD2 . ASP D  1 31  ? 18.586  -5.782  -29.973 1.00 14.73  ? 31  ASP D OD2 1 
ATOM   6763  N  N   . LEU D  1 32  ? 14.775  -4.755  -29.681 1.00 9.30   ? 32  LEU D N   1 
ATOM   6764  C  CA  . LEU D  1 32  ? 14.051  -5.470  -28.620 1.00 10.59  ? 32  LEU D CA  1 
ATOM   6765  C  C   . LEU D  1 32  ? 14.793  -6.787  -28.389 1.00 11.12  ? 32  LEU D C   1 
ATOM   6766  O  O   . LEU D  1 32  ? 14.817  -7.664  -29.252 1.00 12.64  ? 32  LEU D O   1 
ATOM   6767  C  CB  . LEU D  1 32  ? 12.655  -5.720  -29.122 1.00 12.01  ? 32  LEU D CB  1 
ATOM   6768  C  CG  . LEU D  1 32  ? 11.851  -4.479  -29.507 1.00 11.12  ? 32  LEU D CG  1 
ATOM   6769  C  CD1 . LEU D  1 32  ? 10.585  -4.774  -30.269 1.00 13.30  ? 32  LEU D CD1 1 
ATOM   6770  C  CD2 . LEU D  1 32  ? 11.568  -3.573  -28.276 1.00 15.88  ? 32  LEU D CD2 1 
ATOM   6771  N  N   . HIS D  1 33  ? 15.502  -6.907  -27.258 1.00 11.74  ? 33  HIS D N   1 
ATOM   6772  C  CA  . HIS D  1 33  ? 16.341  -8.087  -26.964 1.00 11.61  ? 33  HIS D CA  1 
ATOM   6773  C  C   . HIS D  1 33  ? 16.204  -8.423  -25.505 1.00 11.98  ? 33  HIS D C   1 
ATOM   6774  O  O   . HIS D  1 33  ? 15.859  -7.538  -24.686 1.00 12.71  ? 33  HIS D O   1 
ATOM   6775  C  CB  . HIS D  1 33  ? 17.804  -7.851  -27.384 1.00 13.43  ? 33  HIS D CB  1 
ATOM   6776  C  CG  . HIS D  1 33  ? 18.470  -6.720  -26.687 1.00 13.12  ? 33  HIS D CG  1 
ATOM   6777  N  ND1 . HIS D  1 33  ? 18.298  -5.439  -27.016 1.00 17.81  ? 33  HIS D ND1 1 
ATOM   6778  C  CD2 . HIS D  1 33  ? 19.366  -6.703  -25.638 1.00 16.08  ? 33  HIS D CD2 1 
ATOM   6779  C  CE1 . HIS D  1 33  ? 19.041  -4.637  -26.203 1.00 18.34  ? 33  HIS D CE1 1 
ATOM   6780  N  NE2 . HIS D  1 33  ? 19.689  -5.406  -25.383 1.00 17.68  ? 33  HIS D NE2 1 
ATOM   6781  N  N   . SER D  1 34  ? 16.557  -9.668  -25.187 1.00 13.16  ? 34  SER D N   1 
ATOM   6782  C  CA  . SER D  1 34  ? 16.165  -10.246 -23.905 1.00 14.89  ? 34  SER D CA  1 
ATOM   6783  C  C   . SER D  1 34  ? 16.706  -9.432  -22.738 1.00 13.85  ? 34  SER D C   1 
ATOM   6784  O  O   . SER D  1 34  ? 15.935  -9.279  -21.712 1.00 14.86  ? 34  SER D O   1 
ATOM   6785  C  CB  . SER D  1 34  ? 16.737  -11.653 -23.874 1.00 18.37  ? 34  SER D CB  1 
ATOM   6786  O  OG  . SER D  1 34  ? 18.168  -11.659 -23.889 1.00 21.71  ? 34  SER D OG  1 
ATOM   6787  N  N   . ASP D  1 35  ? 17.899  -8.850  -22.767 1.00 13.53  ? 35  ASP D N   1 
ATOM   6788  C  CA  . ASP D  1 35  ? 18.466  -8.202  -21.586 1.00 15.24  ? 35  ASP D CA  1 
ATOM   6789  C  C   . ASP D  1 35  ? 17.619  -7.071  -21.070 1.00 14.08  ? 35  ASP D C   1 
ATOM   6790  O  O   . ASP D  1 35  ? 17.737  -6.706  -19.930 1.00 18.24  ? 35  ASP D O   1 
ATOM   6791  C  CB  . ASP D  1 35  ? 19.905  -7.700  -21.830 1.00 17.23  ? 35  ASP D CB  1 
ATOM   6792  C  CG  . ASP D  1 35  ? 20.768  -8.703  -22.482 1.00 17.27  ? 35  ASP D CG  1 
ATOM   6793  O  OD1 . ASP D  1 35  ? 21.805  -9.088  -21.896 1.00 18.37  ? 35  ASP D OD1 1 
ATOM   6794  O  OD2 . ASP D  1 35  ? 20.506  -9.057  -23.665 1.00 18.40  ? 35  ASP D OD2 1 
ATOM   6795  N  N   . ILE D  1 36  ? 16.843  -6.431  -21.962 1.00 13.78  ? 36  ILE D N   1 
ATOM   6796  C  CA  . ILE D  1 36  ? 16.098  -5.245  -21.565 1.00 14.99  ? 36  ILE D CA  1 
ATOM   6797  C  C   . ILE D  1 36  ? 14.621  -5.435  -21.502 1.00 13.64  ? 36  ILE D C   1 
ATOM   6798  O  O   . ILE D  1 36  ? 13.870  -4.476  -21.260 1.00 16.24  ? 36  ILE D O   1 
ATOM   6799  C  CB  . ILE D  1 36  ? 16.523  -4.003  -22.431 1.00 17.67  ? 36  ILE D CB  1 
ATOM   6800  C  CG1 . ILE D  1 36  ? 16.326  -4.264  -23.861 1.00 18.91  ? 36  ILE D CG1 1 
ATOM   6801  C  CG2 . ILE D  1 36  ? 17.993  -3.678  -22.232 1.00 23.08  ? 36  ILE D CG2 1 
ATOM   6802  C  CD1 . ILE D  1 36  ? 14.962  -4.476  -24.344 1.00 19.14  ? 36  ILE D CD1 1 
ATOM   6803  N  N   . LEU D  1 37  ? 14.167  -6.685  -21.605 1.00 13.05  ? 37  LEU D N   1 
ATOM   6804  C  CA  . LEU D  1 37  ? 12.741  -6.967  -21.480 1.00 12.86  ? 37  LEU D CA  1 
ATOM   6805  C  C   . LEU D  1 37  ? 12.303  -7.318  -20.054 1.00 14.83  ? 37  LEU D C   1 
ATOM   6806  O  O   . LEU D  1 37  ? 13.067  -8.014  -19.368 1.00 17.81  ? 37  LEU D O   1 
ATOM   6807  C  CB  . LEU D  1 37  ? 12.408  -8.151  -22.350 1.00 12.79  ? 37  LEU D CB  1 
ATOM   6808  C  CG  . LEU D  1 37  ? 12.705  -8.031  -23.826 1.00 15.05  ? 37  LEU D CG  1 
ATOM   6809  C  CD1 . LEU D  1 37  ? 12.249  -9.300  -24.524 1.00 18.69  ? 37  LEU D CD1 1 
ATOM   6810  C  CD2 . LEU D  1 37  ? 12.014  -6.792  -24.431 1.00 15.68  ? 37  LEU D CD2 1 
ATOM   6811  N  N   . GLN D  1 38  ? 11.117  -6.885  -19.687 1.00 12.94  ? 38  GLN D N   1 
ATOM   6812  C  CA  . GLN D  1 38  ? 10.641  -7.215  -18.365 1.00 14.34  ? 38  GLN D CA  1 
ATOM   6813  C  C   . GLN D  1 38  ? 9.172   -7.395  -18.437 1.00 13.12  ? 38  GLN D C   1 
ATOM   6814  O  O   . GLN D  1 38  ? 8.425   -6.466  -18.856 1.00 13.84  ? 38  GLN D O   1 
ATOM   6815  C  CB  . GLN D  1 38  ? 11.025  -6.150  -17.340 1.00 18.17  ? 38  GLN D CB  1 
ATOM   6816  C  CG  . GLN D  1 38  ? 10.578  -6.489  -15.941 1.00 22.43  ? 38  GLN D CG  1 
ATOM   6817  C  CD  . GLN D  1 38  ? 11.157  -5.525  -15.001 1.00 30.79  ? 38  GLN D CD  1 
ATOM   6818  O  OE1 . GLN D  1 38  ? 12.366  -5.550  -14.751 1.00 32.72  ? 38  GLN D OE1 1 
ATOM   6819  N  NE2 . GLN D  1 38  ? 10.309  -4.592  -14.519 1.00 29.01  ? 38  GLN D NE2 1 
ATOM   6820  N  N   . TYR D  1 39  ? 8.670   -8.531  -18.007 1.00 14.62  ? 39  TYR D N   1 
ATOM   6821  C  CA  . TYR D  1 39  ? 7.261   -8.734  -17.978 1.00 12.38  ? 39  TYR D CA  1 
ATOM   6822  C  C   . TYR D  1 39  ? 6.577   -7.763  -17.017 1.00 12.04  ? 39  TYR D C   1 
ATOM   6823  O  O   . TYR D  1 39  ? 7.090   -7.511  -15.921 1.00 13.96  ? 39  TYR D O   1 
ATOM   6824  C  CB  . TYR D  1 39  ? 7.014   -10.194 -17.496 1.00 14.98  ? 39  TYR D CB  1 
ATOM   6825  C  CG  . TYR D  1 39  ? 5.534   -10.491 -17.288 1.00 13.20  ? 39  TYR D CG  1 
ATOM   6826  C  CD1 . TYR D  1 39  ? 4.639   -10.490 -18.318 1.00 15.77  ? 39  TYR D CD1 1 
ATOM   6827  C  CD2 . TYR D  1 39  ? 5.036   -10.664 -16.000 1.00 16.90  ? 39  TYR D CD2 1 
ATOM   6828  C  CE1 . TYR D  1 39  ? 3.257   -10.673 -18.125 1.00 16.02  ? 39  TYR D CE1 1 
ATOM   6829  C  CE2 . TYR D  1 39  ? 3.702   -10.897 -15.776 1.00 16.58  ? 39  TYR D CE2 1 
ATOM   6830  C  CZ  . TYR D  1 39  ? 2.811   -10.936 -16.793 1.00 15.84  ? 39  TYR D CZ  1 
ATOM   6831  O  OH  . TYR D  1 39  ? 1.473   -11.109 -16.588 1.00 20.04  ? 39  TYR D OH  1 
ATOM   6832  N  N   . ASP D  1 40  ? 5.424   -7.243  -17.422 1.00 11.83  ? 40  ASP D N   1 
ATOM   6833  C  CA  . ASP D  1 40  ? 4.681   -6.330  -16.559 1.00 13.10  ? 40  ASP D CA  1 
ATOM   6834  C  C   . ASP D  1 40  ? 3.225   -6.701  -16.643 1.00 11.47  ? 40  ASP D C   1 
ATOM   6835  O  O   . ASP D  1 40  ? 2.550   -6.626  -17.687 1.00 13.68  ? 40  ASP D O   1 
ATOM   6836  C  CB  . ASP D  1 40  ? 4.910   -4.902  -17.076 1.00 14.00  ? 40  ASP D CB  1 
ATOM   6837  C  CG  . ASP D  1 40  ? 4.179   -3.861  -16.316 1.00 19.45  ? 40  ASP D CG  1 
ATOM   6838  O  OD1 . ASP D  1 40  ? 3.390   -4.147  -15.412 1.00 14.16  ? 40  ASP D OD1 1 
ATOM   6839  O  OD2 . ASP D  1 40  ? 4.378   -2.659  -16.650 1.00 25.46  ? 40  ASP D OD2 1 
ATOM   6840  N  N   . ALA D  1 41  ? 2.686   -7.167  -15.484 1.00 11.61  ? 41  ALA D N   1 
ATOM   6841  C  CA  . ALA D  1 41  ? 1.286   -7.638  -15.465 1.00 13.50  ? 41  ALA D CA  1 
ATOM   6842  C  C   . ALA D  1 41  ? 0.288   -6.507  -15.616 1.00 13.57  ? 41  ALA D C   1 
ATOM   6843  O  O   . ALA D  1 41  ? -0.900  -6.777  -15.830 1.00 15.46  ? 41  ALA D O   1 
ATOM   6844  C  CB  . ALA D  1 41  ? 1.023   -8.316  -14.130 1.00 15.88  ? 41  ALA D CB  1 
ATOM   6845  N  N   . SER D  1 42  ? 0.753   -5.251  -15.542 1.00 13.10  ? 42  SER D N   1 
ATOM   6846  C  CA  . SER D  1 42  ? -0.177  -4.135  -15.748 1.00 16.31  ? 42  SER D CA  1 
ATOM   6847  C  C   . SER D  1 42  ? -0.538  -3.973  -17.254 1.00 18.66  ? 42  SER D C   1 
ATOM   6848  O  O   . SER D  1 42  ? -1.414  -3.122  -17.580 1.00 24.38  ? 42  SER D O   1 
ATOM   6849  C  CB  . SER D  1 42  ? 0.393   -2.854  -15.123 1.00 23.01  ? 42  SER D CB  1 
ATOM   6850  O  OG  . SER D  1 42  ? 1.319   -2.323  -15.963 1.00 25.06  ? 42  SER D OG  1 
ATOM   6851  N  N   . LEU D  1 43  ? 0.179   -4.678  -18.160 1.00 17.61  ? 43  LEU D N   1 
ATOM   6852  C  CA  . LEU D  1 43  ? -0.010  -4.483  -19.614 1.00 18.37  ? 43  LEU D CA  1 
ATOM   6853  C  C   . LEU D  1 43  ? -1.138  -5.360  -20.112 1.00 17.76  ? 43  LEU D C   1 
ATOM   6854  O  O   . LEU D  1 43  ? -0.969  -6.461  -20.619 1.00 21.52  ? 43  LEU D O   1 
ATOM   6855  C  CB  . LEU D  1 43  ? 1.300   -4.769  -20.376 1.00 15.95  ? 43  LEU D CB  1 
ATOM   6856  C  CG  . LEU D  1 43  ? 2.379   -3.846  -19.978 1.00 18.68  ? 43  LEU D CG  1 
ATOM   6857  C  CD1 . LEU D  1 43  ? 3.549   -4.221  -20.837 1.00 18.30  ? 43  LEU D CD1 1 
ATOM   6858  C  CD2 . LEU D  1 43  ? 1.904   -2.451  -20.254 1.00 21.16  ? 43  LEU D CD2 1 
ATOM   6859  N  N   . THR D  1 44  ? -2.350  -4.869  -19.987 1.00 19.88  ? 44  THR D N   1 
ATOM   6860  C  CA  . THR D  1 44  ? -3.566  -5.585  -20.321 1.00 21.50  ? 44  THR D CA  1 
ATOM   6861  C  C   . THR D  1 44  ? -3.875  -5.307  -21.763 1.00 18.84  ? 44  THR D C   1 
ATOM   6862  O  O   . THR D  1 44  ? -3.255  -4.483  -22.463 1.00 17.15  ? 44  THR D O   1 
ATOM   6863  C  CB  . THR D  1 44  ? -4.674  -5.066  -19.350 1.00 24.01  ? 44  THR D CB  1 
ATOM   6864  O  OG1 . THR D  1 44  ? -4.737  -3.653  -19.544 1.00 27.62  ? 44  THR D OG1 1 
ATOM   6865  C  CG2 . THR D  1 44  ? -4.296  -5.320  -17.849 1.00 33.46  ? 44  THR D CG2 1 
ATOM   6866  N  N   . PRO D  1 45  ? -4.768  -6.093  -22.367 1.00 17.49  ? 45  PRO D N   1 
ATOM   6867  C  CA  . PRO D  1 45  ? -4.998  -5.977  -23.785 1.00 19.06  ? 45  PRO D CA  1 
ATOM   6868  C  C   . PRO D  1 45  ? -5.564  -4.652  -24.240 1.00 15.76  ? 45  PRO D C   1 
ATOM   6869  O  O   . PRO D  1 45  ? -6.511  -4.153  -23.637 1.00 21.11  ? 45  PRO D O   1 
ATOM   6870  C  CB  . PRO D  1 45  ? -5.981  -7.067  -24.044 1.00 22.40  ? 45  PRO D CB  1 
ATOM   6871  C  CG  . PRO D  1 45  ? -5.802  -8.086  -22.918 1.00 19.37  ? 45  PRO D CG  1 
ATOM   6872  C  CD  . PRO D  1 45  ? -5.549  -7.175  -21.737 1.00 20.16  ? 45  PRO D CD  1 
ATOM   6873  N  N   . LEU D  1 46  ? -5.069  -4.123  -25.331 1.00 17.67  ? 46  LEU D N   1 
ATOM   6874  C  CA  . LEU D  1 46  ? -5.653  -2.945  -25.907 1.00 15.99  ? 46  LEU D CA  1 
ATOM   6875  C  C   . LEU D  1 46  ? -6.926  -3.269  -26.626 1.00 16.48  ? 46  LEU D C   1 
ATOM   6876  O  O   . LEU D  1 46  ? -7.179  -4.432  -27.156 1.00 17.95  ? 46  LEU D O   1 
ATOM   6877  C  CB  . LEU D  1 46  ? -4.742  -2.373  -27.012 1.00 17.11  ? 46  LEU D CB  1 
ATOM   6878  C  CG  . LEU D  1 46  ? -3.454  -1.764  -26.506 1.00 21.49  ? 46  LEU D CG  1 
ATOM   6879  C  CD1 . LEU D  1 46  ? -2.605  -1.406  -27.696 1.00 23.92  ? 46  LEU D CD1 1 
ATOM   6880  C  CD2 . LEU D  1 46  ? -3.766  -0.557  -25.676 1.00 31.41  ? 46  LEU D CD2 1 
ATOM   6881  N  N   . GLU D  1 47  ? -7.828  -2.281  -26.659 1.00 16.45  ? 47  GLU D N   1 
ATOM   6882  C  CA  . GLU D  1 47  ? -9.053  -2.476  -27.466 1.00 18.63  ? 47  GLU D CA  1 
ATOM   6883  C  C   . GLU D  1 47  ? -9.096  -1.479  -28.615 1.00 18.06  ? 47  GLU D C   1 
ATOM   6884  O  O   . GLU D  1 47  ? -8.726  -0.308  -28.428 1.00 18.58  ? 47  GLU D O   1 
ATOM   6885  C  CB  . GLU D  1 47  ? -10.394 -2.433  -26.700 1.00 29.41  ? 47  GLU D CB  1 
ATOM   6886  C  CG  . GLU D  1 47  ? -10.640 -3.783  -25.954 1.00 39.49  ? 47  GLU D CG  1 
ATOM   6887  C  CD  . GLU D  1 47  ? -11.759 -3.796  -24.927 1.00 51.91  ? 47  GLU D CD  1 
ATOM   6888  O  OE1 . GLU D  1 47  ? -12.696 -2.983  -25.052 1.00 63.55  ? 47  GLU D OE1 1 
ATOM   6889  O  OE2 . GLU D  1 47  ? -11.643 -4.669  -24.030 1.00 54.97  ? 47  GLU D OE2 1 
ATOM   6890  N  N   . PHE D  1 48  ? -9.416  -2.071  -29.803 1.00 17.91  ? 48  PHE D N   1 
ATOM   6891  C  CA  . PHE D  1 48  ? -9.361  -1.273  -31.106 1.00 17.90  ? 48  PHE D CA  1 
ATOM   6892  C  C   . PHE D  1 48  ? -10.770 -0.908  -31.519 1.00 21.37  ? 48  PHE D C   1 
ATOM   6893  O  O   . PHE D  1 48  ? -11.532 -1.804  -31.888 1.00 24.53  ? 48  PHE D O   1 
ATOM   6894  C  CB  . PHE D  1 48  ? -8.692  -2.093  -32.197 1.00 17.57  ? 48  PHE D CB  1 
ATOM   6895  C  CG  . PHE D  1 48  ? -7.380  -2.676  -31.750 1.00 16.39  ? 48  PHE D CG  1 
ATOM   6896  C  CD1 . PHE D  1 48  ? -6.301  -1.875  -31.493 1.00 15.62  ? 48  PHE D CD1 1 
ATOM   6897  C  CD2 . PHE D  1 48  ? -7.270  -4.023  -31.466 1.00 18.49  ? 48  PHE D CD2 1 
ATOM   6898  C  CE1 . PHE D  1 48  ? -5.106  -2.401  -30.977 1.00 15.95  ? 48  PHE D CE1 1 
ATOM   6899  C  CE2 . PHE D  1 48  ? -6.103  -4.513  -30.938 1.00 18.24  ? 48  PHE D CE2 1 
ATOM   6900  C  CZ  . PHE D  1 48  ? -4.990  -3.722  -30.694 1.00 16.52  ? 48  PHE D CZ  1 
ATOM   6901  N  N   . GLN D  1 49  ? -11.140 0.357   -31.386 1.00 18.61  ? 49  GLN D N   1 
ATOM   6902  C  CA  . GLN D  1 49  ? -12.516 0.780   -31.517 1.00 23.39  ? 49  GLN D CA  1 
ATOM   6903  C  C   . GLN D  1 49  ? -12.607 1.634   -32.772 1.00 17.80  ? 49  GLN D C   1 
ATOM   6904  O  O   . GLN D  1 49  ? -11.785 2.525   -33.029 1.00 15.87  ? 49  GLN D O   1 
ATOM   6905  C  CB  . GLN D  1 49  ? -12.886 1.646   -30.374 1.00 25.56  ? 49  GLN D CB  1 
ATOM   6906  C  CG  . GLN D  1 49  ? -12.974 0.893   -29.059 1.00 31.33  ? 49  GLN D CG  1 
ATOM   6907  C  CD  . GLN D  1 49  ? -13.789 -0.412  -29.136 1.00 36.41  ? 49  GLN D CD  1 
ATOM   6908  O  OE1 . GLN D  1 49  ? -13.248 -1.481  -28.964 1.00 46.27  ? 49  GLN D OE1 1 
ATOM   6909  N  NE2 . GLN D  1 49  ? -15.076 -0.320  -29.389 1.00 35.86  ? 49  GLN D NE2 1 
ATOM   6910  N  N   . GLY D  1 50  ? -13.640 1.394   -33.552 1.00 16.83  ? 50  GLY D N   1 
ATOM   6911  C  CA  . GLY D  1 50  ? -13.891 2.140   -34.777 1.00 18.75  ? 50  GLY D CA  1 
ATOM   6912  C  C   . GLY D  1 50  ? -12.777 1.943   -35.845 1.00 14.03  ? 50  GLY D C   1 
ATOM   6913  O  O   . GLY D  1 50  ? -12.662 2.744   -36.739 1.00 14.71  ? 50  GLY D O   1 
ATOM   6914  N  N   . TYR D  1 51  ? -12.080 0.790   -35.742 1.00 14.84  ? 51  TYR D N   1 
ATOM   6915  C  CA  . TYR D  1 51  ? -11.119 0.437   -36.758 1.00 13.59  ? 51  TYR D CA  1 
ATOM   6916  C  C   . TYR D  1 51  ? -11.801 -0.092  -38.039 1.00 13.47  ? 51  TYR D C   1 
ATOM   6917  O  O   . TYR D  1 51  ? -11.179 -0.156  -39.133 1.00 13.40  ? 51  TYR D O   1 
ATOM   6918  C  CB  . TYR D  1 51  ? -10.159 -0.663  -36.284 1.00 13.44  ? 51  TYR D CB  1 
ATOM   6919  C  CG  . TYR D  1 51  ? -8.954  -0.118  -35.544 1.00 10.79  ? 51  TYR D CG  1 
ATOM   6920  C  CD1 . TYR D  1 51  ? -9.091  0.871   -34.572 1.00 12.51  ? 51  TYR D CD1 1 
ATOM   6921  C  CD2 . TYR D  1 51  ? -7.682  -0.593  -35.816 1.00 11.85  ? 51  TYR D CD2 1 
ATOM   6922  C  CE1 . TYR D  1 51  ? -7.989  1.363   -33.892 1.00 11.74  ? 51  TYR D CE1 1 
ATOM   6923  C  CE2 . TYR D  1 51  ? -6.577  -0.110  -35.144 1.00 11.53  ? 51  TYR D CE2 1 
ATOM   6924  C  CZ  . TYR D  1 51  ? -6.730  0.865   -34.184 1.00 11.35  ? 51  TYR D CZ  1 
ATOM   6925  O  OH  . TYR D  1 51  ? -5.604  1.326   -33.539 1.00 13.01  ? 51  TYR D OH  1 
ATOM   6926  N  N   . ASN D  1 52  ? -13.068 -0.499  -37.966 1.00 16.21  ? 52  ASN D N   1 
ATOM   6927  C  CA  . ASN D  1 52  ? -13.716 -1.056  -39.133 1.00 15.91  ? 52  ASN D CA  1 
ATOM   6928  C  C   . ASN D  1 52  ? -14.312 0.076   -39.999 1.00 17.10  ? 52  ASN D C   1 
ATOM   6929  O  O   . ASN D  1 52  ? -15.491 0.469   -39.807 1.00 18.75  ? 52  ASN D O   1 
ATOM   6930  C  CB  . ASN D  1 52  ? -14.790 -2.072  -38.686 1.00 18.70  ? 52  ASN D CB  1 
ATOM   6931  C  CG  . ASN D  1 52  ? -15.391 -2.802  -39.837 1.00 19.50  ? 52  ASN D CG  1 
ATOM   6932  O  OD1 . ASN D  1 52  ? -15.129 -2.525  -40.982 1.00 29.15  ? 52  ASN D OD1 1 
ATOM   6933  N  ND2 . ASN D  1 52  ? -16.237 -3.753  -39.523 1.00 30.20  ? 52  ASN D ND2 1 
ATOM   6934  N  N   . LEU D  1 53  ? -13.524 0.580   -40.942 1.00 15.02  ? 53  LEU D N   1 
ATOM   6935  C  CA  . LEU D  1 53  ? -13.942 1.753   -41.735 1.00 14.64  ? 53  LEU D CA  1 
ATOM   6936  C  C   . LEU D  1 53  ? -14.874 1.328   -42.872 1.00 14.54  ? 53  LEU D C   1 
ATOM   6937  O  O   . LEU D  1 53  ? -14.669 0.297   -43.575 1.00 18.09  ? 53  LEU D O   1 
ATOM   6938  C  CB  . LEU D  1 53  ? -12.727 2.473   -42.249 1.00 14.29  ? 53  LEU D CB  1 
ATOM   6939  C  CG  . LEU D  1 53  ? -11.666 2.876   -41.236 1.00 15.09  ? 53  LEU D CG  1 
ATOM   6940  C  CD1 . LEU D  1 53  ? -10.525 3.565   -41.942 1.00 18.86  ? 53  LEU D CD1 1 
ATOM   6941  C  CD2 . LEU D  1 53  ? -12.237 3.753   -40.120 1.00 18.33  ? 53  LEU D CD2 1 
ATOM   6942  N  N   . SER D  1 54  ? -15.925 2.107   -43.065 1.00 15.04  ? 54  SER D N   1 
ATOM   6943  C  CA  . SER D  1 54  ? -16.898 1.815   -44.094 1.00 16.01  ? 54  SER D CA  1 
ATOM   6944  C  C   . SER D  1 54  ? -16.304 1.821   -45.545 1.00 16.45  ? 54  SER D C   1 
ATOM   6945  O  O   . SER D  1 54  ? -15.651 2.793   -45.926 1.00 15.96  ? 54  SER D O   1 
ATOM   6946  C  CB  . SER D  1 54  ? -18.029 2.833   -44.050 1.00 15.65  ? 54  SER D CB  1 
ATOM   6947  O  OG  . SER D  1 54  ? -18.904 2.526   -45.112 1.00 17.23  ? 54  SER D OG  1 
ATOM   6948  N  N   . ALA D  1 55  ? -16.657 0.846   -46.387 1.00 17.14  ? 55  ALA D N   1 
ATOM   6949  C  CA  . ALA D  1 55  ? -16.223 0.784   -47.810 1.00 19.29  ? 55  ALA D CA  1 
ATOM   6950  C  C   . ALA D  1 55  ? -16.867 1.905   -48.593 1.00 18.31  ? 55  ALA D C   1 
ATOM   6951  O  O   . ALA D  1 55  ? -16.447 2.193   -49.739 1.00 19.20  ? 55  ALA D O   1 
ATOM   6952  C  CB  . ALA D  1 55  ? -16.642 -0.560  -48.372 1.00 30.54  ? 55  ALA D CB  1 
ATOM   6953  N  N   . ASN D  1 56  ? -17.949 2.483   -48.064 1.00 18.54  ? 56  ASN D N   1 
ATOM   6954  C  CA  . ASN D  1 56  ? -18.568 3.638   -48.756 1.00 17.04  ? 56  ASN D CA  1 
ATOM   6955  C  C   . ASN D  1 56  ? -18.046 4.999   -48.298 1.00 17.83  ? 56  ASN D C   1 
ATOM   6956  O  O   . ASN D  1 56  ? -18.560 5.993   -48.727 1.00 24.94  ? 56  ASN D O   1 
ATOM   6957  C  CB  . ASN D  1 56  ? -20.117 3.670   -48.564 1.00 21.17  ? 56  ASN D CB  1 
ATOM   6958  C  CG  . ASN D  1 56  ? -20.832 2.602   -49.329 1.00 45.36  ? 56  ASN D CG  1 
ATOM   6959  O  OD1 . ASN D  1 56  ? -20.248 2.005   -50.225 1.00 46.13  ? 56  ASN D OD1 1 
ATOM   6960  N  ND2 . ASN D  1 56  ? -22.124 2.303   -48.962 1.00 95.89  ? 56  ASN D ND2 1 
ATOM   6961  N  N   A LYS D  1 57  ? -17.006 4.969   -47.472 0.50 16.74  ? 57  LYS D N   1 
ATOM   6962  N  N   B LYS D  1 57  ? -17.057 5.037   -47.410 0.50 13.71  ? 57  LYS D N   1 
ATOM   6963  C  CA  A LYS D  1 57  ? -16.296 6.147   -47.051 0.50 17.02  ? 57  LYS D CA  1 
ATOM   6964  C  CA  B LYS D  1 57  ? -16.326 6.244   -47.070 0.50 14.47  ? 57  LYS D CA  1 
ATOM   6965  C  C   A LYS D  1 57  ? -14.910 6.085   -47.672 0.50 15.54  ? 57  LYS D C   1 
ATOM   6966  C  C   B LYS D  1 57  ? -14.967 6.116   -47.731 0.50 13.93  ? 57  LYS D C   1 
ATOM   6967  O  O   A LYS D  1 57  ? -14.378 5.000   -47.975 0.50 18.87  ? 57  LYS D O   1 
ATOM   6968  O  O   B LYS D  1 57  ? -14.502 5.021   -48.101 0.50 17.31  ? 57  LYS D O   1 
ATOM   6969  C  CB  A LYS D  1 57  ? -16.279 6.216   -45.508 0.50 21.24  ? 57  LYS D CB  1 
ATOM   6970  C  CB  B LYS D  1 57  ? -16.264 6.387   -45.518 0.50 14.89  ? 57  LYS D CB  1 
ATOM   6971  C  CG  A LYS D  1 57  ? -17.677 6.394   -44.895 0.50 19.50  ? 57  LYS D CG  1 
ATOM   6972  C  CG  B LYS D  1 57  ? -17.542 6.937   -44.927 0.50 20.28  ? 57  LYS D CG  1 
ATOM   6973  C  CD  A LYS D  1 57  ? -17.562 7.106   -43.559 0.50 30.03  ? 57  LYS D CD  1 
ATOM   6974  C  CD  B LYS D  1 57  ? -17.453 6.859   -43.437 0.50 26.12  ? 57  LYS D CD  1 
ATOM   6975  C  CE  A LYS D  1 57  ? -18.801 7.902   -43.167 0.50 32.61  ? 57  LYS D CE  1 
ATOM   6976  C  CE  B LYS D  1 57  ? -18.660 7.531   -42.824 0.50 29.17  ? 57  LYS D CE  1 
ATOM   6977  N  NZ  A LYS D  1 57  ? -19.072 9.015   -44.115 0.50 29.43  ? 57  LYS D NZ  1 
ATOM   6978  N  NZ  B LYS D  1 57  ? -18.366 7.903   -41.427 0.50 29.26  ? 57  LYS D NZ  1 
ATOM   6979  N  N   . GLN D  1 58  ? -14.298 7.248   -47.875 1.00 14.83  ? 58  GLN D N   1 
ATOM   6980  C  CA  . GLN D  1 58  ? -12.992 7.337   -48.512 1.00 15.79  ? 58  GLN D CA  1 
ATOM   6981  C  C   . GLN D  1 58  ? -12.044 8.012   -47.575 1.00 12.16  ? 58  GLN D C   1 
ATOM   6982  O  O   . GLN D  1 58  ? -12.401 8.931   -46.832 1.00 15.18  ? 58  GLN D O   1 
ATOM   6983  C  CB  . GLN D  1 58  ? -13.102 8.172   -49.805 1.00 25.57  ? 58  GLN D CB  1 
ATOM   6984  C  CG  . GLN D  1 58  ? -13.895 7.571   -50.957 1.00 39.42  ? 58  GLN D CG  1 
ATOM   6985  C  CD  . GLN D  1 58  ? -13.322 7.948   -52.318 1.00 52.09  ? 58  GLN D CD  1 
ATOM   6986  O  OE1 . GLN D  1 58  ? -12.620 7.155   -52.944 1.00 73.79  ? 58  GLN D OE1 1 
ATOM   6987  N  NE2 . GLN D  1 58  ? -13.619 9.159   -52.780 1.00 127.69 ? 58  GLN D NE2 1 
ATOM   6988  N  N   . PHE D  1 59  ? -10.765 7.604   -47.620 1.00 12.60  ? 59  PHE D N   1 
ATOM   6989  C  CA  . PHE D  1 59  ? -9.735  8.101   -46.750 1.00 11.62  ? 59  PHE D CA  1 
ATOM   6990  C  C   . PHE D  1 59  ? -8.541  8.521   -47.572 1.00 11.70  ? 59  PHE D C   1 
ATOM   6991  O  O   . PHE D  1 59  ? -8.175  7.835   -48.539 1.00 12.21  ? 59  PHE D O   1 
ATOM   6992  C  CB  . PHE D  1 59  ? -9.360  7.010   -45.717 1.00 12.27  ? 59  PHE D CB  1 
ATOM   6993  C  CG  . PHE D  1 59  ? -10.554 6.640   -44.900 1.00 11.39  ? 59  PHE D CG  1 
ATOM   6994  C  CD1 . PHE D  1 59  ? -11.495 5.717   -45.356 1.00 11.85  ? 59  PHE D CD1 1 
ATOM   6995  C  CD2 . PHE D  1 59  ? -10.874 7.392   -43.764 1.00 13.14  ? 59  PHE D CD2 1 
ATOM   6996  C  CE1 . PHE D  1 59  ? -12.689 5.506   -44.637 1.00 12.80  ? 59  PHE D CE1 1 
ATOM   6997  C  CE2 . PHE D  1 59  ? -12.064 7.170   -43.069 1.00 13.41  ? 59  PHE D CE2 1 
ATOM   6998  C  CZ  . PHE D  1 59  ? -12.950 6.247   -43.531 1.00 12.73  ? 59  PHE D CZ  1 
ATOM   6999  N  N   . LEU D  1 60  ? -7.947  9.634   -47.218 1.00 11.68  ? 60  LEU D N   1 
ATOM   7000  C  CA  . LEU D  1 60  ? -6.896  10.233  -48.041 1.00 11.80  ? 60  LEU D CA  1 
ATOM   7001  C  C   . LEU D  1 60  ? -5.547  9.616   -47.839 1.00 11.78  ? 60  LEU D C   1 
ATOM   7002  O  O   . LEU D  1 60  ? -5.028  9.598   -46.717 1.00 12.06  ? 60  LEU D O   1 
ATOM   7003  C  CB  . LEU D  1 60  ? -6.835  11.706  -47.655 1.00 14.71  ? 60  LEU D CB  1 
ATOM   7004  C  CG  . LEU D  1 60  ? -5.990  12.569  -48.558 1.00 20.13  ? 60  LEU D CG  1 
ATOM   7005  C  CD1 . LEU D  1 60  ? -6.604  12.529  -49.956 1.00 20.74  ? 60  LEU D CD1 1 
ATOM   7006  C  CD2 . LEU D  1 60  ? -5.948  13.986  -48.050 1.00 23.67  ? 60  LEU D CD2 1 
ATOM   7007  N  N   . LEU D  1 61  ? -4.963  9.138   -48.966 1.00 11.90  ? 61  LEU D N   1 
ATOM   7008  C  CA  . LEU D  1 61  ? -3.602  8.645   -48.967 1.00 11.89  ? 61  LEU D CA  1 
ATOM   7009  C  C   . LEU D  1 61  ? -2.731  9.752   -49.566 1.00 12.90  ? 61  LEU D C   1 
ATOM   7010  O  O   . LEU D  1 61  ? -3.115  10.362  -50.569 1.00 14.31  ? 61  LEU D O   1 
ATOM   7011  C  CB  . LEU D  1 61  ? -3.559  7.419   -49.885 1.00 13.17  ? 61  LEU D CB  1 
ATOM   7012  C  CG  . LEU D  1 61  ? -2.307  6.581   -49.893 1.00 12.67  ? 61  LEU D CG  1 
ATOM   7013  C  CD1 . LEU D  1 61  ? -2.129  5.774   -48.654 1.00 12.57  ? 61  LEU D CD1 1 
ATOM   7014  C  CD2 . LEU D  1 61  ? -2.348  5.642   -51.093 1.00 17.12  ? 61  LEU D CD2 1 
ATOM   7015  N  N   . THR D  1 62  ? -1.610  10.040  -48.943 1.00 13.88  ? 62  THR D N   1 
ATOM   7016  C  CA  . THR D  1 62  ? -0.737  11.136  -49.411 1.00 17.09  ? 62  THR D CA  1 
ATOM   7017  C  C   . THR D  1 62  ? 0.711   10.645  -49.321 1.00 18.14  ? 62  THR D C   1 
ATOM   7018  O  O   . THR D  1 62  ? 1.150   10.012  -48.375 1.00 20.83  ? 62  THR D O   1 
ATOM   7019  C  CB  . THR D  1 62  ? -0.731  12.252  -48.413 1.00 22.99  ? 62  THR D CB  1 
ATOM   7020  O  OG1 . THR D  1 62  ? -2.044  12.730  -48.264 1.00 21.60  ? 62  THR D OG1 1 
ATOM   7021  C  CG2 . THR D  1 62  ? 0.099   13.414  -48.873 1.00 31.89  ? 62  THR D CG2 1 
ATOM   7022  N  N   . ASN D  1 63  ? 1.512   10.943  -50.353 1.00 14.67  ? 63  ASN D N   1 
ATOM   7023  C  CA  . ASN D  1 63  ? 2.967   10.856  -50.269 1.00 15.20  ? 63  ASN D CA  1 
ATOM   7024  C  C   . ASN D  1 63  ? 3.470   12.125  -49.717 1.00 13.11  ? 63  ASN D C   1 
ATOM   7025  O  O   . ASN D  1 63  ? 3.321   13.190  -50.184 1.00 14.61  ? 63  ASN D O   1 
ATOM   7026  C  CB  . ASN D  1 63  ? 3.452   10.794  -51.691 1.00 14.38  ? 63  ASN D CB  1 
ATOM   7027  C  CG  . ASN D  1 63  ? 4.969   10.792  -51.797 1.00 13.25  ? 63  ASN D CG  1 
ATOM   7028  O  OD1 . ASN D  1 63  ? 5.666   11.362  -50.936 1.00 14.39  ? 63  ASN D OD1 1 
ATOM   7029  N  ND2 . ASN D  1 63  ? 5.479   10.106  -52.769 1.00 15.42  ? 63  ASN D ND2 1 
ATOM   7030  N  N   . ASN D  1 64  ? 4.050   12.041  -48.497 1.00 13.99  ? 64  ASN D N   1 
ATOM   7031  C  CA  . ASN D  1 64  ? 4.479   13.324  -47.880 1.00 17.81  ? 64  ASN D CA  1 
ATOM   7032  C  C   . ASN D  1 64  ? 5.973   13.548  -47.982 1.00 14.80  ? 64  ASN D C   1 
ATOM   7033  O  O   . ASN D  1 64  ? 6.539   14.404  -47.306 1.00 16.54  ? 64  ASN D O   1 
ATOM   7034  C  CB  . ASN D  1 64  ? 4.127   13.252  -46.343 1.00 17.55  ? 64  ASN D CB  1 
ATOM   7035  C  CG  . ASN D  1 64  ? 4.924   12.196  -45.569 1.00 15.31  ? 64  ASN D CG  1 
ATOM   7036  O  OD1 . ASN D  1 64  ? 5.853   11.516  -46.114 1.00 13.93  ? 64  ASN D OD1 1 
ATOM   7037  N  ND2 . ASN D  1 64  ? 4.628   12.053  -44.274 1.00 19.99  ? 64  ASN D ND2 1 
ATOM   7038  N  N   . GLY D  1 65  ? 6.663   12.924  -48.939 1.00 17.48  ? 65  GLY D N   1 
ATOM   7039  C  CA  . GLY D  1 65  ? 8.125   13.148  -49.091 1.00 18.98  ? 65  GLY D CA  1 
ATOM   7040  C  C   . GLY D  1 65  ? 8.992   12.173  -48.272 1.00 17.79  ? 65  GLY D C   1 
ATOM   7041  O  O   . GLY D  1 65  ? 10.173  12.124  -48.522 1.00 20.93  ? 65  GLY D O   1 
ATOM   7042  N  N   . HIS D  1 66  ? 8.369   11.469  -47.303 1.00 13.88  ? 66  HIS D N   1 
ATOM   7043  C  CA  . HIS D  1 66  ? 9.102   10.604  -46.305 1.00 13.29  ? 66  HIS D CA  1 
ATOM   7044  C  C   . HIS D  1 66  ? 8.623   9.232   -46.152 1.00 12.21  ? 66  HIS D C   1 
ATOM   7045  O  O   . HIS D  1 66  ? 9.380   8.252   -45.823 1.00 12.60  ? 66  HIS D O   1 
ATOM   7046  C  CB  . HIS D  1 66  ? 9.151   11.262  -44.929 1.00 14.35  ? 66  HIS D CB  1 
ATOM   7047  C  CG  . HIS D  1 66  ? 9.686   12.668  -44.975 1.00 15.04  ? 66  HIS D CG  1 
ATOM   7048  N  ND1 . HIS D  1 66  ? 11.035  12.986  -45.237 1.00 14.69  ? 66  HIS D ND1 1 
ATOM   7049  C  CD2 . HIS D  1 66  ? 9.064   13.857  -44.809 1.00 15.64  ? 66  HIS D CD2 1 
ATOM   7050  C  CE1 . HIS D  1 66  ? 11.178  14.271  -45.230 1.00 12.33  ? 66  HIS D CE1 1 
ATOM   7051  N  NE2 . HIS D  1 66  ? 9.954   14.819  -44.921 1.00 17.15  ? 66  HIS D NE2 1 
ATOM   7052  N  N   A SER D  1 67  ? 7.323   9.072   -46.395 0.50 12.33  ? 67  SER D N   1 
ATOM   7053  N  N   B SER D  1 67  ? 7.314   9.047   -46.335 0.50 12.36  ? 67  SER D N   1 
ATOM   7054  C  CA  A SER D  1 67  ? 6.600   7.811   -46.377 0.50 11.96  ? 67  SER D CA  1 
ATOM   7055  C  CA  B SER D  1 67  ? 6.599   7.755   -46.261 0.50 12.45  ? 67  SER D CA  1 
ATOM   7056  C  C   A SER D  1 67  ? 5.294   7.981   -47.166 0.50 12.23  ? 67  SER D C   1 
ATOM   7057  C  C   B SER D  1 67  ? 5.316   7.966   -47.142 0.50 12.21  ? 67  SER D C   1 
ATOM   7058  O  O   A SER D  1 67  ? 5.081   9.035   -47.775 0.50 13.71  ? 67  SER D O   1 
ATOM   7059  O  O   B SER D  1 67  ? 5.106   9.027   -47.761 0.50 13.72  ? 67  SER D O   1 
ATOM   7060  C  CB  A SER D  1 67  ? 6.318   7.452   -44.921 0.50 12.59  ? 67  SER D CB  1 
ATOM   7061  C  CB  B SER D  1 67  ? 6.172   7.400   -44.766 0.50 14.84  ? 67  SER D CB  1 
ATOM   7062  O  OG  A SER D  1 67  ? 5.646   6.152   -44.814 0.50 7.37   ? 67  SER D OG  1 
ATOM   7063  O  OG  B SER D  1 67  ? 6.993   6.728   -43.688 0.50 12.54  ? 67  SER D OG  1 
ATOM   7064  N  N   A VAL D  1 68  ? 4.509   6.922   -47.217 0.50 12.68  ? 68  VAL D N   1 
ATOM   7065  N  N   B VAL D  1 68  ? 4.502   6.943   -47.226 0.50 12.69  ? 68  VAL D N   1 
ATOM   7066  C  CA  A VAL D  1 68  ? 3.142   6.969   -47.694 0.50 13.78  ? 68  VAL D CA  1 
ATOM   7067  C  CA  B VAL D  1 68  ? 3.174   7.107   -47.713 0.50 14.74  ? 68  VAL D CA  1 
ATOM   7068  C  C   A VAL D  1 68  ? 2.201   6.968   -46.468 0.50 14.96  ? 68  VAL D C   1 
ATOM   7069  C  C   B VAL D  1 68  ? 2.288   7.104   -46.435 0.50 15.46  ? 68  VAL D C   1 
ATOM   7070  O  O   A VAL D  1 68  ? 2.329   6.012   -45.777 0.50 13.81  ? 68  VAL D O   1 
ATOM   7071  O  O   B VAL D  1 68  ? 2.465   6.228   -45.703 0.50 14.29  ? 68  VAL D O   1 
ATOM   7072  C  CB  A VAL D  1 68  ? 2.842   5.885   -48.787 0.50 13.34  ? 68  VAL D CB  1 
ATOM   7073  C  CB  B VAL D  1 68  ? 2.828   6.001   -48.773 0.50 14.68  ? 68  VAL D CB  1 
ATOM   7074  C  CG1 A VAL D  1 68  ? 3.124   4.477   -48.361 0.50 10.82  ? 68  VAL D CG1 1 
ATOM   7075  C  CG1 B VAL D  1 68  ? 3.074   4.567   -48.309 0.50 18.63  ? 68  VAL D CG1 1 
ATOM   7076  C  CG2 A VAL D  1 68  ? 1.495   6.205   -49.355 0.50 20.68  ? 68  VAL D CG2 1 
ATOM   7077  C  CG2 B VAL D  1 68  ? 1.446   6.267   -49.242 0.50 14.49  ? 68  VAL D CG2 1 
ATOM   7078  N  N   . LYS D  1 69  ? 1.306   8.033   -46.290 1.00 14.64  ? 69  LYS D N   1 
ATOM   7079  C  CA  . LYS D  1 69  ? 0.340   8.016   -45.108 1.00 11.05  ? 69  LYS D CA  1 
ATOM   7080  C  C   . LYS D  1 69  ? -1.079  7.937   -45.575 1.00 9.77   ? 69  LYS D C   1 
ATOM   7081  O  O   . LYS D  1 69  ? -1.478  8.515   -46.563 1.00 13.73  ? 69  LYS D O   1 
ATOM   7082  C  CB  . LYS D  1 69  ? 0.552   9.114   -44.042 1.00 15.07  ? 69  LYS D CB  1 
ATOM   7083  C  CG  . LYS D  1 69  ? 0.122   10.439  -44.520 1.00 17.53  ? 69  LYS D CG  1 
ATOM   7084  C  CD  . LYS D  1 69  ? 0.224   11.472  -43.411 1.00 21.54  ? 69  LYS D CD  1 
ATOM   7085  C  CE  . LYS D  1 69  ? -0.099  12.736  -44.159 1.00 22.08  ? 69  LYS D CE  1 
ATOM   7086  N  NZ  . LYS D  1 69  ? 0.125   13.860  -43.265 1.00 25.61  ? 69  LYS D NZ  1 
ATOM   7087  N  N   . LEU D  1 70  ? -1.857  7.215   -44.777 1.00 8.63   ? 70  LEU D N   1 
ATOM   7088  C  CA  . LEU D  1 70  ? -3.286  7.144   -44.910 1.00 9.04   ? 70  LEU D CA  1 
ATOM   7089  C  C   . LEU D  1 70  ? -3.909  7.889   -43.750 1.00 9.24   ? 70  LEU D C   1 
ATOM   7090  O  O   . LEU D  1 70  ? -3.646  7.523   -42.578 1.00 9.14   ? 70  LEU D O   1 
ATOM   7091  C  CB  . LEU D  1 70  ? -3.771  5.702   -44.927 1.00 9.65   ? 70  LEU D CB  1 
ATOM   7092  C  CG  . LEU D  1 70  ? -5.243  5.520   -45.131 1.00 10.15  ? 70  LEU D CG  1 
ATOM   7093  C  CD1 . LEU D  1 70  ? -5.701  5.985   -46.511 1.00 12.08  ? 70  LEU D CD1 1 
ATOM   7094  C  CD2 . LEU D  1 70  ? -5.638  4.052   -44.888 1.00 12.92  ? 70  LEU D CD2 1 
ATOM   7095  N  N   . ASN D  1 71  ? -4.701  8.898   -44.003 1.00 8.97   ? 71  ASN D N   1 
ATOM   7096  C  CA  . ASN D  1 71  ? -5.397  9.596   -42.918 1.00 10.10  ? 71  ASN D CA  1 
ATOM   7097  C  C   . ASN D  1 71  ? -6.482  8.743   -42.343 1.00 10.42  ? 71  ASN D C   1 
ATOM   7098  O  O   . ASN D  1 71  ? -7.165  7.983   -43.077 1.00 12.96  ? 71  ASN D O   1 
ATOM   7099  C  CB  . ASN D  1 71  ? -5.999  10.846  -43.434 1.00 14.22  ? 71  ASN D CB  1 
ATOM   7100  C  CG  . ASN D  1 71  ? -5.023  11.930  -43.650 1.00 17.15  ? 71  ASN D CG  1 
ATOM   7101  O  OD1 . ASN D  1 71  ? -3.843  11.817  -43.368 1.00 20.52  ? 71  ASN D OD1 1 
ATOM   7102  N  ND2 . ASN D  1 71  ? -5.538  13.065  -44.158 1.00 23.97  ? 71  ASN D ND2 1 
ATOM   7103  N  N   . LEU D  1 72  ? -6.670  8.827   -41.027 1.00 10.59  ? 72  LEU D N   1 
ATOM   7104  C  CA  . LEU D  1 72  ? -7.648  8.022   -40.302 1.00 10.93  ? 72  LEU D CA  1 
ATOM   7105  C  C   . LEU D  1 72  ? -8.577  8.979   -39.540 1.00 10.86  ? 72  LEU D C   1 
ATOM   7106  O  O   . LEU D  1 72  ? -8.169  10.074  -39.130 1.00 13.34  ? 72  LEU D O   1 
ATOM   7107  C  CB  . LEU D  1 72  ? -6.892  7.147   -39.315 1.00 10.12  ? 72  LEU D CB  1 
ATOM   7108  C  CG  . LEU D  1 72  ? -6.015  6.098   -40.017 1.00 11.06  ? 72  LEU D CG  1 
ATOM   7109  C  CD1 . LEU D  1 72  ? -5.152  5.372   -39.017 1.00 10.70  ? 72  LEU D CD1 1 
ATOM   7110  C  CD2 . LEU D  1 72  ? -6.796  5.101   -40.866 1.00 12.49  ? 72  LEU D CD2 1 
ATOM   7111  N  N   . PRO D  1 73  ? -9.818  8.528   -39.284 1.00 11.79  ? 73  PRO D N   1 
ATOM   7112  C  CA  . PRO D  1 73  ? -10.818 9.361   -38.642 1.00 13.46  ? 73  PRO D CA  1 
ATOM   7113  C  C   . PRO D  1 73  ? -10.654 9.361   -37.115 1.00 13.79  ? 73  PRO D C   1 
ATOM   7114  O  O   . PRO D  1 73  ? -10.210 8.326   -36.533 1.00 16.01  ? 73  PRO D O   1 
ATOM   7115  C  CB  . PRO D  1 73  ? -12.119 8.718   -39.108 1.00 15.59  ? 73  PRO D CB  1 
ATOM   7116  C  CG  . PRO D  1 73  ? -11.813 7.252   -39.243 1.00 14.84  ? 73  PRO D CG  1 
ATOM   7117  C  CD  . PRO D  1 73  ? -10.366 7.216   -39.730 1.00 13.12  ? 73  PRO D CD  1 
ATOM   7118  N  N   . SER D  1 74  ? -10.883 10.476  -36.429 1.00 17.52  ? 74  SER D N   1 
ATOM   7119  C  CA  . SER D  1 74  ? -10.690 10.501  -34.974 1.00 17.35  ? 74  SER D CA  1 
ATOM   7120  C  C   . SER D  1 74  ? -11.676 9.641   -34.186 1.00 20.11  ? 74  SER D C   1 
ATOM   7121  O  O   . SER D  1 74  ? -11.406 9.399   -32.998 1.00 23.06  ? 74  SER D O   1 
ATOM   7122  C  CB  . SER D  1 74  ? -10.684 11.955  -34.494 1.00 23.02  ? 74  SER D CB  1 
ATOM   7123  O  OG  . SER D  1 74  ? -11.939 12.577  -34.798 1.00 25.79  ? 74  SER D OG  1 
ATOM   7124  N  N   A ASP D  1 75  ? -12.753 9.144   -34.830 0.50 18.94  ? 75  ASP D N   1 
ATOM   7125  N  N   B ASP D  1 75  ? -12.762 9.164   -34.810 0.50 19.09  ? 75  ASP D N   1 
ATOM   7126  C  CA  A ASP D  1 75  ? -13.718 8.243   -34.117 0.50 21.82  ? 75  ASP D CA  1 
ATOM   7127  C  CA  B ASP D  1 75  ? -13.716 8.236   -34.166 0.50 22.41  ? 75  ASP D CA  1 
ATOM   7128  C  C   A ASP D  1 75  ? -13.046 6.864   -33.927 0.50 18.51  ? 75  ASP D C   1 
ATOM   7129  C  C   B ASP D  1 75  ? -13.014 6.878   -33.919 0.50 18.70  ? 75  ASP D C   1 
ATOM   7130  O  O   A ASP D  1 75  ? -13.467 6.073   -33.088 0.50 22.31  ? 75  ASP D O   1 
ATOM   7131  O  O   B ASP D  1 75  ? -13.403 6.138   -33.077 0.50 22.18  ? 75  ASP D O   1 
ATOM   7132  C  CB  A ASP D  1 75  ? -15.127 8.190   -34.756 0.50 25.70  ? 75  ASP D CB  1 
ATOM   7133  C  CB  B ASP D  1 75  ? -14.997 8.059   -34.992 0.50 30.87  ? 75  ASP D CB  1 
ATOM   7134  C  CG  A ASP D  1 75  ? -15.182 7.387   -36.042 0.50 32.06  ? 75  ASP D CG  1 
ATOM   7135  C  CG  B ASP D  1 75  ? -15.981 9.204   -34.798 0.50 34.76  ? 75  ASP D CG  1 
ATOM   7136  O  OD1 A ASP D  1 75  ? -14.366 7.637   -36.953 0.50 34.78  ? 75  ASP D OD1 1 
ATOM   7137  O  OD1 B ASP D  1 75  ? -15.724 10.086  -33.948 0.50 37.72  ? 75  ASP D OD1 1 
ATOM   7138  O  OD2 A ASP D  1 75  ? -16.081 6.516   -36.166 0.50 54.13  ? 75  ASP D OD2 1 
ATOM   7139  O  OD2 B ASP D  1 75  ? -17.020 9.223   -35.502 0.50 56.24  ? 75  ASP D OD2 1 
ATOM   7140  N  N   . MET D  1 76  ? -11.970 6.614   -34.678 1.00 16.63  ? 76  MET D N   1 
ATOM   7141  C  CA  . MET D  1 76  ? -11.155 5.423   -34.512 1.00 15.15  ? 76  MET D CA  1 
ATOM   7142  C  C   . MET D  1 76  ? -10.201 5.654   -33.318 1.00 14.21  ? 76  MET D C   1 
ATOM   7143  O  O   . MET D  1 76  ? -9.536  6.692   -33.260 1.00 14.29  ? 76  MET D O   1 
ATOM   7144  C  CB  . MET D  1 76  ? -10.462 5.177   -35.864 1.00 16.51  ? 76  MET D CB  1 
ATOM   7145  C  CG  . MET D  1 76  ? -9.505  4.037   -35.799 1.00 13.92  ? 76  MET D CG  1 
ATOM   7146  S  SD  . MET D  1 76  ? -8.784  3.861   -37.475 1.00 14.20  ? 76  MET D SD  1 
ATOM   7147  C  CE  . MET D  1 76  ? -7.368  2.911   -37.023 1.00 13.36  ? 76  MET D CE  1 
ATOM   7148  N  N   . HIS D  1 77  ? -10.161 4.712   -32.357 1.00 16.33  ? 77  HIS D N   1 
ATOM   7149  C  CA  . HIS D  1 77  ? -9.384  4.929   -31.172 1.00 15.08  ? 77  HIS D CA  1 
ATOM   7150  C  C   . HIS D  1 77  ? -8.950  3.709   -30.506 1.00 15.37  ? 77  HIS D C   1 
ATOM   7151  O  O   . HIS D  1 77  ? -9.499  2.619   -30.808 1.00 16.74  ? 77  HIS D O   1 
ATOM   7152  C  CB  . HIS D  1 77  ? -10.123 5.877   -30.266 1.00 18.44  ? 77  HIS D CB  1 
ATOM   7153  C  CG  . HIS D  1 77  ? -11.409 5.304   -29.700 1.00 20.24  ? 77  HIS D CG  1 
ATOM   7154  N  ND1 . HIS D  1 77  ? -12.634 5.317   -30.363 1.00 24.55  ? 77  HIS D ND1 1 
ATOM   7155  C  CD2 . HIS D  1 77  ? -11.664 4.748   -28.465 1.00 26.38  ? 77  HIS D CD2 1 
ATOM   7156  C  CE1 . HIS D  1 77  ? -13.601 4.749   -29.579 1.00 24.35  ? 77  HIS D CE1 1 
ATOM   7157  N  NE2 . HIS D  1 77  ? -13.026 4.442   -28.396 1.00 28.94  ? 77  HIS D NE2 1 
ATOM   7158  N  N   A ILE D  1 78  ? -8.013  3.786   -29.600 0.50 14.15  ? 78  ILE D N   1 
ATOM   7159  N  N   B ILE D  1 78  ? -7.949  3.877   -29.611 0.50 16.11  ? 78  ILE D N   1 
ATOM   7160  C  CA  A ILE D  1 78  ? -7.677  2.606   -28.812 0.50 15.13  ? 78  ILE D CA  1 
ATOM   7161  C  CA  B ILE D  1 78  ? -7.494  2.813   -28.639 0.50 12.84  ? 78  ILE D CA  1 
ATOM   7162  C  C   A ILE D  1 78  ? -8.250  2.954   -27.441 0.50 16.24  ? 78  ILE D C   1 
ATOM   7163  C  C   B ILE D  1 78  ? -7.800  3.071   -27.137 0.50 13.16  ? 78  ILE D C   1 
ATOM   7164  O  O   A ILE D  1 78  ? -8.391  4.070   -27.140 0.50 18.12  ? 78  ILE D O   1 
ATOM   7165  O  O   B ILE D  1 78  ? -7.648  4.210   -26.563 0.50 9.37   ? 78  ILE D O   1 
ATOM   7166  C  CB  A ILE D  1 78  ? -6.188  2.619   -28.646 0.50 11.83  ? 78  ILE D CB  1 
ATOM   7167  C  CB  B ILE D  1 78  ? -6.038  2.338   -28.799 0.50 13.75  ? 78  ILE D CB  1 
ATOM   7168  C  CG1 A ILE D  1 78  ? -5.459  2.380   -29.971 0.50 14.25  ? 78  ILE D CG1 1 
ATOM   7169  C  CG1 B ILE D  1 78  ? -5.083  3.509   -28.525 0.50 12.50  ? 78  ILE D CG1 1 
ATOM   7170  C  CG2 A ILE D  1 78  ? -5.772  1.597   -27.659 0.50 16.24  ? 78  ILE D CG2 1 
ATOM   7171  C  CG2 B ILE D  1 78  ? -5.809  1.637   -30.143 0.50 12.63  ? 78  ILE D CG2 1 
ATOM   7172  C  CD1 A ILE D  1 78  ? -3.999  2.793   -29.902 0.50 13.31  ? 78  ILE D CD1 1 
ATOM   7173  C  CD1 B ILE D  1 78  ? -3.606  3.219   -28.830 0.50 13.05  ? 78  ILE D CD1 1 
ATOM   7174  N  N   . GLN D  1 79  ? -8.320  1.987   -26.545 1.00 17.65  ? 79  GLN D N   1 
ATOM   7175  C  CA  . GLN D  1 79  ? -8.598  2.047   -25.140 1.00 22.64  ? 79  GLN D CA  1 
ATOM   7176  C  C   . GLN D  1 79  ? -7.692  1.054   -24.380 1.00 21.16  ? 79  GLN D C   1 
ATOM   7177  O  O   . GLN D  1 79  ? -7.316  -0.001  -25.017 1.00 27.40  ? 79  GLN D O   1 
ATOM   7178  C  CB  . GLN D  1 79  ? -10.029 1.573   -24.874 1.00 33.72  ? 79  GLN D CB  1 
ATOM   7179  C  CG  . GLN D  1 79  ? -11.104 2.544   -25.326 1.00 41.79  ? 79  GLN D CG  1 
ATOM   7180  N  N   . GLY D  1 80  ? -7.189  1.505   -23.204 1.00 25.22  ? 80  GLY D N   1 
ATOM   7181  C  CA  . GLY D  1 80  ? -6.397  0.651   -22.348 1.00 19.89  ? 80  GLY D CA  1 
ATOM   7182  C  C   . GLY D  1 80  ? -5.196  1.335   -21.795 1.00 46.44  ? 80  GLY D C   1 
ATOM   7183  O  O   . GLY D  1 80  ? -4.519  0.769   -20.886 1.00 214.17 ? 80  GLY D O   1 
ATOM   7184  N  N   . LEU D  1 81  ? -4.939  2.547   -22.406 1.00 14.83  ? 81  LEU D N   1 
ATOM   7185  C  CA  . LEU D  1 81  ? -3.800  3.359   -21.883 1.00 15.06  ? 81  LEU D CA  1 
ATOM   7186  C  C   . LEU D  1 81  ? -4.285  4.337   -20.838 1.00 15.26  ? 81  LEU D C   1 
ATOM   7187  O  O   . LEU D  1 81  ? -5.354  4.206   -20.361 1.00 21.33  ? 81  LEU D O   1 
ATOM   7188  C  CB  . LEU D  1 81  ? -3.199  4.026   -23.131 1.00 19.43  ? 81  LEU D CB  1 
ATOM   7189  C  CG  . LEU D  1 81  ? -2.846  3.046   -24.261 1.00 17.96  ? 81  LEU D CG  1 
ATOM   7190  C  CD1 . LEU D  1 81  ? -2.405  3.833   -25.514 1.00 21.16  ? 81  LEU D CD1 1 
ATOM   7191  C  CD2 . LEU D  1 81  ? -1.719  2.187   -23.717 1.00 19.15  ? 81  LEU D CD2 1 
ATOM   7192  N  N   . GLN D  1 82  ? -3.424  5.205   -20.381 1.00 14.21  ? 82  GLN D N   1 
ATOM   7193  C  CA  . GLN D  1 82  ? -3.808  6.106   -19.286 1.00 14.83  ? 82  GLN D CA  1 
ATOM   7194  C  C   . GLN D  1 82  ? -4.823  7.160   -19.697 1.00 13.96  ? 82  GLN D C   1 
ATOM   7195  O  O   . GLN D  1 82  ? -5.379  7.782   -18.870 1.00 14.71  ? 82  GLN D O   1 
ATOM   7196  C  CB  . GLN D  1 82  ? -2.517  6.728   -18.688 1.00 15.97  ? 82  GLN D CB  1 
ATOM   7197  C  CG  . GLN D  1 82  ? -2.099  8.088   -19.206 1.00 17.99  ? 82  GLN D CG  1 
ATOM   7198  C  CD  . GLN D  1 82  ? -1.665  7.968   -20.655 1.00 17.71  ? 82  GLN D CD  1 
ATOM   7199  O  OE1 . GLN D  1 82  ? -1.361  6.906   -21.234 1.00 20.09  ? 82  GLN D OE1 1 
ATOM   7200  N  NE2 . GLN D  1 82  ? -1.551  9.105   -21.307 1.00 18.09  ? 82  GLN D NE2 1 
ATOM   7201  N  N   . SER D  1 83  ? -4.954  7.369   -21.005 1.00 14.92  ? 83  SER D N   1 
ATOM   7202  C  CA  . SER D  1 83  ? -5.889  8.347   -21.641 1.00 14.71  ? 83  SER D CA  1 
ATOM   7203  C  C   . SER D  1 83  ? -6.463  7.674   -22.897 1.00 13.52  ? 83  SER D C   1 
ATOM   7204  O  O   . SER D  1 83  ? -5.860  6.730   -23.434 1.00 16.77  ? 83  SER D O   1 
ATOM   7205  C  CB  . SER D  1 83  ? -5.127  9.616   -22.051 1.00 14.94  ? 83  SER D CB  1 
ATOM   7206  O  OG  . SER D  1 83  ? -4.562  10.305  -20.894 1.00 18.05  ? 83  SER D OG  1 
ATOM   7207  N  N   . ARG D  1 84  ? -7.556  8.161   -23.489 1.00 15.48  ? 84  ARG D N   1 
ATOM   7208  C  CA  . ARG D  1 84  ? -7.986  7.832   -24.840 1.00 14.91  ? 84  ARG D CA  1 
ATOM   7209  C  C   . ARG D  1 84  ? -7.051  8.372   -25.915 1.00 14.26  ? 84  ARG D C   1 
ATOM   7210  O  O   . ARG D  1 84  ? -6.766  9.569   -25.895 1.00 16.17  ? 84  ARG D O   1 
ATOM   7211  C  CB  . ARG D  1 84  ? -9.356  8.428   -25.195 1.00 17.18  ? 84  ARG D CB  1 
ATOM   7212  C  CG  . ARG D  1 84  ? -9.740  8.208   -26.608 1.00 18.99  ? 84  ARG D CG  1 
ATOM   7213  C  CD  . ARG D  1 84  ? -11.211 8.444   -26.997 1.00 25.21  ? 84  ARG D CD  1 
ATOM   7214  N  NE  . ARG D  1 84  ? -11.353 8.629   -28.448 1.00 22.06  ? 84  ARG D NE  1 
ATOM   7215  C  CZ  . ARG D  1 84  ? -12.492 8.571   -29.148 1.00 21.53  ? 84  ARG D CZ  1 
ATOM   7216  N  NH1 . ARG D  1 84  ? -13.676 8.395   -28.497 1.00 34.57  ? 84  ARG D NH1 1 
ATOM   7217  N  NH2 . ARG D  1 84  ? -12.509 8.727   -30.499 1.00 29.35  ? 84  ARG D NH2 1 
ATOM   7218  N  N   . TYR D  1 85  ? -6.649  7.519   -26.854 1.00 13.04  ? 85  TYR D N   1 
ATOM   7219  C  CA  . TYR D  1 85  ? -5.839  7.901   -27.964 1.00 11.98  ? 85  TYR D CA  1 
ATOM   7220  C  C   . TYR D  1 85  ? -6.613  7.712   -29.232 1.00 13.20  ? 85  TYR D C   1 
ATOM   7221  O  O   . TYR D  1 85  ? -7.063  6.585   -29.536 1.00 13.68  ? 85  TYR D O   1 
ATOM   7222  C  CB  . TYR D  1 85  ? -4.493  7.179   -27.922 1.00 12.15  ? 85  TYR D CB  1 
ATOM   7223  C  CG  . TYR D  1 85  ? -3.504  7.689   -26.934 1.00 10.71  ? 85  TYR D CG  1 
ATOM   7224  C  CD1 . TYR D  1 85  ? -3.543  7.232   -25.571 1.00 12.29  ? 85  TYR D CD1 1 
ATOM   7225  C  CD2 . TYR D  1 85  ? -2.533  8.620   -27.280 1.00 11.32  ? 85  TYR D CD2 1 
ATOM   7226  C  CE1 . TYR D  1 85  ? -2.616  7.720   -24.662 1.00 13.26  ? 85  TYR D CE1 1 
ATOM   7227  C  CE2 . TYR D  1 85  ? -1.629  9.106   -26.358 1.00 11.76  ? 85  TYR D CE2 1 
ATOM   7228  C  CZ  . TYR D  1 85  ? -1.647  8.638   -25.018 1.00 11.95  ? 85  TYR D CZ  1 
ATOM   7229  O  OH  . TYR D  1 85  ? -0.712  9.135   -24.104 1.00 14.22  ? 85  TYR D OH  1 
ATOM   7230  N  N   . SER D  1 86  ? -6.789  8.788   -29.998 1.00 11.68  ? 86  SER D N   1 
ATOM   7231  C  CA  . SER D  1 86  ? -7.567  8.732   -31.194 1.00 11.64  ? 86  SER D CA  1 
ATOM   7232  C  C   . SER D  1 86  ? -6.637  8.652   -32.430 1.00 10.66  ? 86  SER D C   1 
ATOM   7233  O  O   . SER D  1 86  ? -5.584  9.268   -32.453 1.00 11.47  ? 86  SER D O   1 
ATOM   7234  C  CB  . SER D  1 86  ? -8.414  9.999   -31.379 1.00 14.21  ? 86  SER D CB  1 
ATOM   7235  O  OG  . SER D  1 86  ? -9.402  10.016  -30.316 1.00 14.84  ? 86  SER D OG  1 
ATOM   7236  N  N   . ALA D  1 87  ? -7.047  7.878   -33.431 1.00 11.32  ? 87  ALA D N   1 
ATOM   7237  C  CA  . ALA D  1 87  ? -6.164  7.720   -34.634 1.00 11.31  ? 87  ALA D CA  1 
ATOM   7238  C  C   . ALA D  1 87  ? -6.047  8.997   -35.400 1.00 11.71  ? 87  ALA D C   1 
ATOM   7239  O  O   . ALA D  1 87  ? -7.012  9.790   -35.468 1.00 12.23  ? 87  ALA D O   1 
ATOM   7240  C  CB  . ALA D  1 87  ? -6.768  6.693   -35.512 1.00 12.40  ? 87  ALA D CB  1 
ATOM   7241  N  N   . THR D  1 88  ? -4.904  9.136   -36.061 1.00 10.22  ? 88  THR D N   1 
ATOM   7242  C  CA  . THR D  1 88  ? -4.708  10.231  -37.008 1.00 10.50  ? 88  THR D CA  1 
ATOM   7243  C  C   . THR D  1 88  ? -4.189  9.782   -38.364 1.00 8.16   ? 88  THR D C   1 
ATOM   7244  O  O   . THR D  1 88  ? -4.657  10.279  -39.361 1.00 9.49   ? 88  THR D O   1 
ATOM   7245  C  CB  . THR D  1 88  ? -3.818  11.333  -36.374 1.00 11.94  ? 88  THR D CB  1 
ATOM   7246  O  OG1 . THR D  1 88  ? -3.700  12.413  -37.279 1.00 14.74  ? 88  THR D OG1 1 
ATOM   7247  C  CG2 . THR D  1 88  ? -2.459  10.856  -35.939 1.00 13.39  ? 88  THR D CG2 1 
ATOM   7248  N  N   . GLN D  1 89  ? -3.281  8.792   -38.413 1.00 8.56   ? 89  GLN D N   1 
ATOM   7249  C  CA  . GLN D  1 89  ? -2.790  8.342   -39.718 1.00 8.14   ? 89  GLN D CA  1 
ATOM   7250  C  C   . GLN D  1 89  ? -2.072  7.011   -39.486 1.00 7.69   ? 89  GLN D C   1 
ATOM   7251  O  O   . GLN D  1 89  ? -1.660  6.709   -38.392 1.00 8.35   ? 89  GLN D O   1 
ATOM   7252  C  CB  . GLN D  1 89  ? -1.849  9.401   -40.351 1.00 9.14   ? 89  GLN D CB  1 
ATOM   7253  C  CG  . GLN D  1 89  ? -0.740  9.825   -39.513 1.00 10.27  ? 89  GLN D CG  1 
ATOM   7254  C  CD  . GLN D  1 89  ? 0.575   9.336   -39.975 1.00 9.88   ? 89  GLN D CD  1 
ATOM   7255  O  OE1 . GLN D  1 89  ? 0.708   8.131   -40.238 1.00 10.21  ? 89  GLN D OE1 1 
ATOM   7256  N  NE2 . GLN D  1 89  ? 1.551   10.136  -40.109 1.00 14.49  ? 89  GLN D NE2 1 
ATOM   7257  N  N   . LEU D  1 90  ? -1.861  6.288   -40.594 1.00 7.49   ? 90  LEU D N   1 
ATOM   7258  C  CA  . LEU D  1 90  ? -0.924  5.191   -40.579 1.00 7.10   ? 90  LEU D CA  1 
ATOM   7259  C  C   . LEU D  1 90  ? 0.069   5.379   -41.757 1.00 6.83   ? 90  LEU D C   1 
ATOM   7260  O  O   . LEU D  1 90  ? -0.233  6.048   -42.740 1.00 7.69   ? 90  LEU D O   1 
ATOM   7261  C  CB  . LEU D  1 90  ? -1.606  3.821   -40.619 1.00 8.52   ? 90  LEU D CB  1 
ATOM   7262  C  CG  . LEU D  1 90  ? -2.565  3.486   -41.740 1.00 8.71   ? 90  LEU D CG  1 
ATOM   7263  C  CD1 . LEU D  1 90  ? -1.852  3.124   -43.042 1.00 9.67   ? 90  LEU D CD1 1 
ATOM   7264  C  CD2 . LEU D  1 90  ? -3.460  2.317   -41.339 1.00 10.33  ? 90  LEU D CD2 1 
ATOM   7265  N  N   . HIS D  1 91  ? 1.208   4.740   -41.654 1.00 6.93   ? 91  HIS D N   1 
ATOM   7266  C  CA  . HIS D  1 91  ? 2.246   4.830   -42.671 1.00 6.87   ? 91  HIS D CA  1 
ATOM   7267  C  C   . HIS D  1 91  ? 3.179   3.651   -42.472 1.00 7.15   ? 91  HIS D C   1 
ATOM   7268  O  O   . HIS D  1 91  ? 3.098   2.917   -41.470 1.00 7.42   ? 91  HIS D O   1 
ATOM   7269  C  CB  . HIS D  1 91  ? 2.981   6.183   -42.578 1.00 7.23   ? 91  HIS D CB  1 
ATOM   7270  C  CG  . HIS D  1 91  ? 3.730   6.348   -41.307 1.00 6.99   ? 91  HIS D CG  1 
ATOM   7271  N  ND1 . HIS D  1 91  ? 3.171   6.919   -40.182 1.00 7.63   ? 91  HIS D ND1 1 
ATOM   7272  C  CD2 . HIS D  1 91  ? 4.937   5.886   -40.885 1.00 7.24   ? 91  HIS D CD2 1 
ATOM   7273  C  CE1 . HIS D  1 91  ? 4.036   6.819   -39.194 1.00 7.68   ? 91  HIS D CE1 1 
ATOM   7274  N  NE2 . HIS D  1 91  ? 5.108   6.173   -39.587 1.00 6.81   ? 91  HIS D NE2 1 
ATOM   7275  N  N   . LEU D  1 92  ? 4.155   3.536   -43.393 1.00 7.34   ? 92  LEU D N   1 
ATOM   7276  C  CA  . LEU D  1 92  ? 5.070   2.423   -43.382 1.00 7.07   ? 92  LEU D CA  1 
ATOM   7277  C  C   . LEU D  1 92  ? 6.533   2.877   -43.459 1.00 6.56   ? 92  LEU D C   1 
ATOM   7278  O  O   . LEU D  1 92  ? 6.842   4.023   -43.857 1.00 7.70   ? 92  LEU D O   1 
ATOM   7279  C  CB  . LEU D  1 92  ? 4.783   1.384   -44.446 1.00 9.44   ? 92  LEU D CB  1 
ATOM   7280  C  CG  . LEU D  1 92  ? 3.418   0.715   -44.370 1.00 9.95   ? 92  LEU D CG  1 
ATOM   7281  C  CD1 . LEU D  1 92  ? 2.396   1.429   -45.153 1.00 13.86  ? 92  LEU D CD1 1 
ATOM   7282  C  CD2 . LEU D  1 92  ? 3.494   -0.731  -44.655 1.00 13.24  ? 92  LEU D CD2 1 
ATOM   7283  N  N   . HIS D  1 93  ? 7.421   1.966   -43.167 1.00 6.92   ? 93  HIS D N   1 
ATOM   7284  C  CA  . HIS D  1 93  ? 8.877   2.074   -43.340 1.00 6.92   ? 93  HIS D CA  1 
ATOM   7285  C  C   . HIS D  1 93  ? 9.382   0.828   -43.974 1.00 6.03   ? 93  HIS D C   1 
ATOM   7286  O  O   . HIS D  1 93  ? 8.908   -0.268  -43.646 1.00 7.15   ? 93  HIS D O   1 
ATOM   7287  C  CB  . HIS D  1 93  ? 9.580   2.303   -41.972 1.00 7.28   ? 93  HIS D CB  1 
ATOM   7288  C  CG  . HIS D  1 93  ? 9.091   3.480   -41.211 1.00 6.75   ? 93  HIS D CG  1 
ATOM   7289  N  ND1 . HIS D  1 93  ? 9.657   4.713   -41.288 1.00 7.04   ? 93  HIS D ND1 1 
ATOM   7290  C  CD2 . HIS D  1 93  ? 8.020   3.638   -40.351 1.00 6.71   ? 93  HIS D CD2 1 
ATOM   7291  C  CE1 . HIS D  1 93  ? 8.965   5.564   -40.521 1.00 7.34   ? 93  HIS D CE1 1 
ATOM   7292  N  NE2 . HIS D  1 93  ? 7.988   4.936   -39.900 1.00 6.50   ? 93  HIS D NE2 1 
ATOM   7293  N  N   . TRP D  1 94  ? 10.324  0.973   -44.899 1.00 6.63   ? 94  TRP D N   1 
ATOM   7294  C  CA  . TRP D  1 94  ? 10.818  -0.148  -45.677 1.00 7.15   ? 94  TRP D CA  1 
ATOM   7295  C  C   . TRP D  1 94  ? 12.245  0.080   -46.154 1.00 7.06   ? 94  TRP D C   1 
ATOM   7296  O  O   . TRP D  1 94  ? 12.853  1.135   -45.935 1.00 7.36   ? 94  TRP D O   1 
ATOM   7297  C  CB  . TRP D  1 94  ? 9.866   -0.449  -46.847 1.00 7.61   ? 94  TRP D CB  1 
ATOM   7298  C  CG  . TRP D  1 94  ? 9.746   0.710   -47.787 1.00 7.20   ? 94  TRP D CG  1 
ATOM   7299  C  CD1 . TRP D  1 94  ? 10.581  1.051   -48.833 1.00 7.54   ? 94  TRP D CD1 1 
ATOM   7300  C  CD2 . TRP D  1 94  ? 8.753   1.745   -47.750 1.00 7.52   ? 94  TRP D CD2 1 
ATOM   7301  N  NE1 . TRP D  1 94  ? 10.130  2.187   -49.447 1.00 8.33   ? 94  TRP D NE1 1 
ATOM   7302  C  CE2 . TRP D  1 94  ? 9.024   2.638   -48.812 1.00 7.64   ? 94  TRP D CE2 1 
ATOM   7303  C  CE3 . TRP D  1 94  ? 7.659   2.021   -46.881 1.00 8.20   ? 94  TRP D CE3 1 
ATOM   7304  C  CZ2 . TRP D  1 94  ? 8.208   3.740   -49.078 1.00 8.76   ? 94  TRP D CZ2 1 
ATOM   7305  C  CZ3 . TRP D  1 94  ? 6.880   3.167   -47.122 1.00 8.72   ? 94  TRP D CZ3 1 
ATOM   7306  C  CH2 . TRP D  1 94  ? 7.160   4.001   -48.210 1.00 8.80   ? 94  TRP D CH2 1 
ATOM   7307  N  N   . GLY D  1 95  ? 12.798  -0.972  -46.783 1.00 7.80   ? 95  GLY D N   1 
ATOM   7308  C  CA  . GLY D  1 95  ? 14.173  -0.975  -47.233 1.00 8.07   ? 95  GLY D CA  1 
ATOM   7309  C  C   . GLY D  1 95  ? 14.228  -0.701  -48.727 1.00 8.57   ? 95  GLY D C   1 
ATOM   7310  O  O   . GLY D  1 95  ? 13.746  0.322   -49.221 1.00 8.62   ? 95  GLY D O   1 
ATOM   7311  N  N   . ASN D  1 96  ? 14.799  -1.650  -49.477 1.00 9.51   ? 96  ASN D N   1 
ATOM   7312  C  CA  . ASN D  1 96  ? 14.895  -1.456  -50.926 1.00 10.36  ? 96  ASN D CA  1 
ATOM   7313  C  C   . ASN D  1 96  ? 15.064  -2.812  -51.532 1.00 10.75  ? 96  ASN D C   1 
ATOM   7314  O  O   . ASN D  1 96  ? 15.277  -3.840  -50.810 1.00 11.83  ? 96  ASN D O   1 
ATOM   7315  C  CB  . ASN D  1 96  ? 16.047  -0.520  -51.330 1.00 12.65  ? 96  ASN D CB  1 
ATOM   7316  C  CG  . ASN D  1 96  ? 17.401  -1.176  -51.222 1.00 16.27  ? 96  ASN D CG  1 
ATOM   7317  O  OD1 . ASN D  1 96  ? 17.846  -1.849  -52.172 1.00 22.54  ? 96  ASN D OD1 1 
ATOM   7318  N  ND2 . ASN D  1 96  ? 18.046  -1.089  -50.086 1.00 15.58  ? 96  ASN D ND2 1 
ATOM   7319  N  N   . PRO D  1 97  ? 15.018  -2.948  -52.882 1.00 13.67  ? 97  PRO D N   1 
ATOM   7320  C  CA  . PRO D  1 97  ? 14.993  -4.255  -53.471 1.00 17.25  ? 97  PRO D CA  1 
ATOM   7321  C  C   . PRO D  1 97  ? 16.208  -5.101  -53.126 1.00 15.36  ? 97  PRO D C   1 
ATOM   7322  O  O   . PRO D  1 97  ? 16.105  -6.336  -53.015 1.00 24.16  ? 97  PRO D O   1 
ATOM   7323  C  CB  . PRO D  1 97  ? 14.881  -3.956  -54.964 1.00 21.18  ? 97  PRO D CB  1 
ATOM   7324  C  CG  . PRO D  1 97  ? 14.142  -2.664  -55.065 1.00 21.64  ? 97  PRO D CG  1 
ATOM   7325  C  CD  . PRO D  1 97  ? 14.704  -1.937  -53.894 1.00 16.47  ? 97  PRO D CD  1 
ATOM   7326  N  N   . ASN D  1 98  ? 17.388  -4.482  -52.977 1.00 14.56  ? 98  ASN D N   1 
ATOM   7327  C  CA  . ASN D  1 98  ? 18.624  -5.230  -52.646 1.00 17.78  ? 98  ASN D CA  1 
ATOM   7328  C  C   . ASN D  1 98  ? 18.831  -5.430  -51.157 1.00 18.10  ? 98  ASN D C   1 
ATOM   7329  O  O   . ASN D  1 98  ? 19.763  -6.148  -50.741 1.00 25.26  ? 98  ASN D O   1 
ATOM   7330  C  CB  . ASN D  1 98  ? 19.756  -4.462  -53.238 1.00 24.03  ? 98  ASN D CB  1 
ATOM   7331  C  CG  . ASN D  1 98  ? 19.742  -4.524  -54.754 1.00 42.85  ? 98  ASN D CG  1 
ATOM   7332  O  OD1 . ASN D  1 98  ? 19.292  -5.474  -55.420 1.00 201.05 ? 98  ASN D OD1 1 
ATOM   7333  N  ND2 . ASN D  1 98  ? 20.338  -3.521  -55.279 1.00 40.69  ? 98  ASN D ND2 1 
ATOM   7334  N  N   . ASP D  1 99  ? 17.940  -4.846  -50.350 1.00 13.29  ? 99  ASP D N   1 
ATOM   7335  C  CA  . ASP D  1 99  ? 18.025  -5.031  -48.904 1.00 14.27  ? 99  ASP D CA  1 
ATOM   7336  C  C   . ASP D  1 99  ? 16.621  -4.902  -48.348 1.00 10.81  ? 99  ASP D C   1 
ATOM   7337  O  O   . ASP D  1 99  ? 16.292  -3.833  -47.798 1.00 11.16  ? 99  ASP D O   1 
ATOM   7338  C  CB  . ASP D  1 99  ? 18.943  -4.008  -48.250 1.00 14.90  ? 99  ASP D CB  1 
ATOM   7339  C  CG  . ASP D  1 99  ? 19.089  -4.218  -46.735 1.00 16.49  ? 99  ASP D CG  1 
ATOM   7340  O  OD1 . ASP D  1 99  ? 18.822  -5.333  -46.274 1.00 17.78  ? 99  ASP D OD1 1 
ATOM   7341  O  OD2 . ASP D  1 99  ? 19.415  -3.253  -45.974 1.00 18.84  ? 99  ASP D OD2 1 
ATOM   7342  N  N   . PRO D  1 100 ? 15.801  -5.921  -48.448 1.00 10.76  ? 100 PRO D N   1 
ATOM   7343  C  CA  . PRO D  1 100 ? 14.374  -5.816  -48.021 1.00 11.32  ? 100 PRO D CA  1 
ATOM   7344  C  C   . PRO D  1 100 ? 14.311  -6.090  -46.514 1.00 9.96   ? 100 PRO D C   1 
ATOM   7345  O  O   . PRO D  1 100 ? 13.662  -7.005  -46.044 1.00 12.11  ? 100 PRO D O   1 
ATOM   7346  C  CB  . PRO D  1 100 ? 13.684  -6.921  -48.801 1.00 14.33  ? 100 PRO D CB  1 
ATOM   7347  C  CG  . PRO D  1 100 ? 14.763  -7.955  -49.041 1.00 14.79  ? 100 PRO D CG  1 
ATOM   7348  C  CD  . PRO D  1 100 ? 16.044  -7.163  -49.225 1.00 13.59  ? 100 PRO D CD  1 
ATOM   7349  N  N   . HIS D  1 101 ? 14.946  -5.224  -45.756 1.00 9.66   ? 101 HIS D N   1 
ATOM   7350  C  CA  . HIS D  1 101 ? 15.083  -5.367  -44.287 1.00 10.36  ? 101 HIS D CA  1 
ATOM   7351  C  C   . HIS D  1 101 ? 15.013  -3.993  -43.671 1.00 9.40   ? 101 HIS D C   1 
ATOM   7352  O  O   . HIS D  1 101 ? 15.969  -3.540  -43.039 1.00 11.96  ? 101 HIS D O   1 
ATOM   7353  C  CB  . HIS D  1 101 ? 16.405  -6.111  -43.955 1.00 13.02  ? 101 HIS D CB  1 
ATOM   7354  C  CG  . HIS D  1 101 ? 16.494  -7.461  -44.640 1.00 15.18  ? 101 HIS D CG  1 
ATOM   7355  N  ND1 . HIS D  1 101 ? 15.833  -8.590  -44.221 1.00 19.42  ? 101 HIS D ND1 1 
ATOM   7356  C  CD2 . HIS D  1 101 ? 17.160  -7.820  -45.761 1.00 14.99  ? 101 HIS D CD2 1 
ATOM   7357  C  CE1 . HIS D  1 101 ? 16.084  -9.607  -45.076 1.00 19.74  ? 101 HIS D CE1 1 
ATOM   7358  N  NE2 . HIS D  1 101 ? 16.900  -9.140  -46.018 1.00 18.39  ? 101 HIS D NE2 1 
ATOM   7359  N  N   . GLY D  1 102 ? 13.876  -3.347  -43.824 1.00 8.47   ? 102 GLY D N   1 
ATOM   7360  C  CA  . GLY D  1 102 ? 13.704  -1.946  -43.456 1.00 8.86   ? 102 GLY D CA  1 
ATOM   7361  C  C   . GLY D  1 102 ? 12.737  -1.672  -42.353 1.00 7.54   ? 102 GLY D C   1 
ATOM   7362  O  O   . GLY D  1 102 ? 12.264  -0.540  -42.233 1.00 8.67   ? 102 GLY D O   1 
ATOM   7363  N  N   . SER D  1 103 ? 12.484  -2.652  -41.469 1.00 7.69   ? 103 SER D N   1 
ATOM   7364  C  CA  . SER D  1 103 ? 11.769  -2.309  -40.228 1.00 7.39   ? 103 SER D CA  1 
ATOM   7365  C  C   . SER D  1 103 ? 12.601  -1.285  -39.439 1.00 7.39   ? 103 SER D C   1 
ATOM   7366  O  O   . SER D  1 103 ? 13.812  -1.227  -39.539 1.00 8.72   ? 103 SER D O   1 
ATOM   7367  C  CB  . SER D  1 103 ? 11.430  -3.511  -39.384 1.00 7.87   ? 103 SER D CB  1 
ATOM   7368  O  OG  . SER D  1 103 ? 12.617  -4.096  -38.830 1.00 8.01   ? 103 SER D OG  1 
ATOM   7369  N  N   . GLU D  1 104 ? 11.909  -0.542  -38.579 1.00 6.98   ? 104 GLU D N   1 
ATOM   7370  C  CA  . GLU D  1 104 ? 12.595  0.388   -37.658 1.00 7.41   ? 104 GLU D CA  1 
ATOM   7371  C  C   . GLU D  1 104 ? 13.005  -0.339  -36.379 1.00 6.67   ? 104 GLU D C   1 
ATOM   7372  O  O   . GLU D  1 104 ? 14.171  -0.368  -36.038 1.00 7.59   ? 104 GLU D O   1 
ATOM   7373  C  CB  . GLU D  1 104 ? 11.695  1.565   -37.354 1.00 8.34   ? 104 GLU D CB  1 
ATOM   7374  C  CG  . GLU D  1 104 ? 11.235  2.313   -38.620 1.00 8.05   ? 104 GLU D CG  1 
ATOM   7375  C  CD  . GLU D  1 104 ? 11.219  3.794   -38.371 1.00 7.56   ? 104 GLU D CD  1 
ATOM   7376  O  OE1 . GLU D  1 104 ? 10.218  4.243   -37.773 1.00 7.94   ? 104 GLU D OE1 1 
ATOM   7377  O  OE2 . GLU D  1 104 ? 12.206  4.484   -38.696 1.00 8.49   ? 104 GLU D OE2 1 
ATOM   7378  N  N   . HIS D  1 105 ? 12.037  -0.911  -35.666 1.00 7.28   ? 105 HIS D N   1 
ATOM   7379  C  CA  . HIS D  1 105 ? 12.391  -1.791  -34.579 1.00 7.44   ? 105 HIS D CA  1 
ATOM   7380  C  C   . HIS D  1 105 ? 13.009  -3.069  -35.085 1.00 7.83   ? 105 HIS D C   1 
ATOM   7381  O  O   . HIS D  1 105 ? 12.680  -3.564  -36.151 1.00 8.26   ? 105 HIS D O   1 
ATOM   7382  C  CB  . HIS D  1 105 ? 11.121  -2.106  -33.731 1.00 8.25   ? 105 HIS D CB  1 
ATOM   7383  C  CG  . HIS D  1 105 ? 10.613  -0.879  -33.054 1.00 8.23   ? 105 HIS D CG  1 
ATOM   7384  N  ND1 . HIS D  1 105 ? 9.703   -0.041  -33.611 1.00 8.11   ? 105 HIS D ND1 1 
ATOM   7385  C  CD2 . HIS D  1 105 ? 10.986  -0.306  -31.844 1.00 8.45   ? 105 HIS D CD2 1 
ATOM   7386  C  CE1 . HIS D  1 105 ? 9.512   0.996   -32.763 1.00 9.15   ? 105 HIS D CE1 1 
ATOM   7387  N  NE2 . HIS D  1 105 ? 10.289  0.855   -31.681 1.00 9.03   ? 105 HIS D NE2 1 
ATOM   7388  N  N   . THR D  1 106 ? 13.935  -3.580  -34.308 1.00 8.51   ? 106 THR D N   1 
ATOM   7389  C  CA  . THR D  1 106 ? 14.549  -4.875  -34.599 1.00 9.00   ? 106 THR D CA  1 
ATOM   7390  C  C   . THR D  1 106 ? 14.268  -5.794  -33.402 1.00 9.27   ? 106 THR D C   1 
ATOM   7391  O  O   . THR D  1 106 ? 13.964  -5.312  -32.298 1.00 9.31   ? 106 THR D O   1 
ATOM   7392  C  CB  . THR D  1 106 ? 16.044  -4.711  -34.878 1.00 9.36   ? 106 THR D CB  1 
ATOM   7393  O  OG1 . THR D  1 106 ? 16.718  -4.160  -33.753 1.00 9.97   ? 106 THR D OG1 1 
ATOM   7394  C  CG2 . THR D  1 106 ? 16.296  -3.862  -36.081 1.00 9.90   ? 106 THR D CG2 1 
ATOM   7395  N  N   . VAL D  1 107 ? 14.357  -7.109  -33.634 1.00 9.09   ? 107 VAL D N   1 
ATOM   7396  C  CA  . VAL D  1 107 ? 14.142  -8.059  -32.539 1.00 10.09  ? 107 VAL D CA  1 
ATOM   7397  C  C   . VAL D  1 107 ? 15.386  -8.940  -32.529 1.00 10.41  ? 107 VAL D C   1 
ATOM   7398  O  O   . VAL D  1 107 ? 15.773  -9.577  -33.551 1.00 11.61  ? 107 VAL D O   1 
ATOM   7399  C  CB  . VAL D  1 107 ? 12.877  -8.918  -32.742 1.00 11.98  ? 107 VAL D CB  1 
ATOM   7400  C  CG1 . VAL D  1 107 ? 12.778  -9.946  -31.620 1.00 14.43  ? 107 VAL D CG1 1 
ATOM   7401  C  CG2 . VAL D  1 107 ? 11.612  -8.043  -32.771 1.00 13.14  ? 107 VAL D CG2 1 
ATOM   7402  N  N   . SER D  1 108 ? 16.061  -8.948  -31.397 1.00 11.08  ? 108 SER D N   1 
ATOM   7403  C  CA  . SER D  1 108 ? 17.314  -9.732  -31.217 1.00 12.55  ? 108 SER D CA  1 
ATOM   7404  C  C   . SER D  1 108 ? 18.255  -9.439  -32.388 1.00 10.54  ? 108 SER D C   1 
ATOM   7405  O  O   . SER D  1 108 ? 18.886  -10.360 -32.942 1.00 12.49  ? 108 SER D O   1 
ATOM   7406  C  CB  . SER D  1 108 ? 16.992  -11.212 -31.098 1.00 15.76  ? 108 SER D CB  1 
ATOM   7407  O  OG  . SER D  1 108 ? 16.194  -11.374 -29.928 1.00 17.18  ? 108 SER D OG  1 
ATOM   7408  N  N   . GLY D  1 109 ? 18.415  -8.167  -32.715 1.00 10.64  ? 109 GLY D N   1 
ATOM   7409  C  CA  . GLY D  1 109 ? 19.377  -7.696  -33.726 1.00 11.55  ? 109 GLY D CA  1 
ATOM   7410  C  C   . GLY D  1 109 ? 18.928  -7.853  -35.144 1.00 12.75  ? 109 GLY D C   1 
ATOM   7411  O  O   . GLY D  1 109 ? 19.712  -7.546  -36.047 1.00 18.38  ? 109 GLY D O   1 
ATOM   7412  N  N   A GLN D  1 110 ? 17.734  -8.340  -35.398 0.50 11.87  ? 110 GLN D N   1 
ATOM   7413  N  N   B GLN D  1 110 ? 17.735  -8.328  -35.399 0.50 11.93  ? 110 GLN D N   1 
ATOM   7414  C  CA  A GLN D  1 110 ? 17.273  -8.614  -36.766 0.50 12.64  ? 110 GLN D CA  1 
ATOM   7415  C  CA  B GLN D  1 110 ? 17.307  -8.554  -36.778 0.50 13.00  ? 110 GLN D CA  1 
ATOM   7416  C  C   A GLN D  1 110 ? 16.196  -7.661  -37.182 0.50 10.75  ? 110 GLN D C   1 
ATOM   7417  C  C   B GLN D  1 110 ? 16.197  -7.645  -37.182 0.50 10.78  ? 110 GLN D C   1 
ATOM   7418  O  O   A GLN D  1 110 ? 15.220  -7.475  -36.449 0.50 9.86   ? 110 GLN D O   1 
ATOM   7419  O  O   B GLN D  1 110 ? 15.214  -7.470  -36.455 0.50 9.84   ? 110 GLN D O   1 
ATOM   7420  C  CB  A GLN D  1 110 ? 16.663  -10.028 -36.822 0.50 15.09  ? 110 GLN D CB  1 
ATOM   7421  C  CB  B GLN D  1 110 ? 16.818  -9.993  -36.933 0.50 14.30  ? 110 GLN D CB  1 
ATOM   7422  C  CG  A GLN D  1 110 ? 17.553  -11.146 -36.256 0.50 16.83  ? 110 GLN D CG  1 
ATOM   7423  C  CG  B GLN D  1 110 ? 17.848  -11.017 -36.505 0.50 22.52  ? 110 GLN D CG  1 
ATOM   7424  C  CD  A GLN D  1 110 ? 18.987  -11.010 -36.762 0.50 14.77  ? 110 GLN D CD  1 
ATOM   7425  C  CD  B GLN D  1 110 ? 17.339  -12.381 -36.742 0.50 23.35  ? 110 GLN D CD  1 
ATOM   7426  O  OE1 A GLN D  1 110 ? 19.211  -11.157 -37.931 0.50 17.76  ? 110 GLN D OE1 1 
ATOM   7427  O  OE1 B GLN D  1 110 ? 16.513  -12.880 -35.980 0.50 36.55  ? 110 GLN D OE1 1 
ATOM   7428  N  NE2 A GLN D  1 110 ? 19.957  -10.867 -35.840 0.50 17.93  ? 110 GLN D NE2 1 
ATOM   7429  N  NE2 B GLN D  1 110 ? 17.788  -13.000 -37.834 0.50 34.74  ? 110 GLN D NE2 1 
ATOM   7430  N  N   . HIS D  1 111 ? 16.354  -7.067  -38.369 1.00 10.90  ? 111 HIS D N   1 
ATOM   7431  C  CA  . HIS D  1 111 ? 15.290  -6.353  -38.993 1.00 9.89   ? 111 HIS D CA  1 
ATOM   7432  C  C   . HIS D  1 111 ? 14.250  -7.294  -39.528 1.00 10.34  ? 111 HIS D C   1 
ATOM   7433  O  O   . HIS D  1 111 ? 14.551  -8.444  -39.869 1.00 14.53  ? 111 HIS D O   1 
ATOM   7434  C  CB  . HIS D  1 111 ? 15.748  -5.521  -40.190 1.00 10.62  ? 111 HIS D CB  1 
ATOM   7435  C  CG  . HIS D  1 111 ? 16.499  -4.282  -39.842 1.00 9.75   ? 111 HIS D CG  1 
ATOM   7436  N  ND1 . HIS D  1 111 ? 15.882  -3.072  -39.664 1.00 10.70  ? 111 HIS D ND1 1 
ATOM   7437  C  CD2 . HIS D  1 111 ? 17.790  -4.075  -39.642 1.00 11.30  ? 111 HIS D CD2 1 
ATOM   7438  C  CE1 . HIS D  1 111 ? 16.826  -2.142  -39.359 1.00 11.65  ? 111 HIS D CE1 1 
ATOM   7439  N  NE2 . HIS D  1 111 ? 17.983  -2.727  -39.408 1.00 13.53  ? 111 HIS D NE2 1 
ATOM   7440  N  N   . PHE D  1 112 ? 13.046  -6.816  -39.579 1.00 8.82   ? 112 PHE D N   1 
ATOM   7441  C  CA  . PHE D  1 112 ? 12.031  -7.340  -40.447 1.00 8.71   ? 112 PHE D CA  1 
ATOM   7442  C  C   . PHE D  1 112 ? 12.021  -6.609  -41.764 1.00 7.65   ? 112 PHE D C   1 
ATOM   7443  O  O   . PHE D  1 112 ? 12.682  -5.611  -41.909 1.00 8.64   ? 112 PHE D O   1 
ATOM   7444  C  CB  . PHE D  1 112 ? 10.679  -7.292  -39.694 1.00 10.36  ? 112 PHE D CB  1 
ATOM   7445  C  CG  . PHE D  1 112 ? 10.596  -8.314  -38.607 1.00 11.71  ? 112 PHE D CG  1 
ATOM   7446  C  CD1 . PHE D  1 112 ? 11.186  -8.152  -37.377 1.00 16.34  ? 112 PHE D CD1 1 
ATOM   7447  C  CD2 . PHE D  1 112 ? 9.863   -9.492  -38.828 1.00 16.74  ? 112 PHE D CD2 1 
ATOM   7448  C  CE1 . PHE D  1 112 ? 11.098  -9.209  -36.469 1.00 18.48  ? 112 PHE D CE1 1 
ATOM   7449  C  CE2 . PHE D  1 112 ? 9.797   -10.553 -37.949 1.00 20.94  ? 112 PHE D CE2 1 
ATOM   7450  C  CZ  . PHE D  1 112 ? 10.414  -10.348 -36.770 1.00 21.51  ? 112 PHE D CZ  1 
ATOM   7451  N  N   . ALA D  1 113 ? 11.218  -7.095  -42.718 1.00 7.91   ? 113 ALA D N   1 
ATOM   7452  C  CA  . ALA D  1 113 ? 11.203  -6.479  -44.060 1.00 8.41   ? 113 ALA D CA  1 
ATOM   7453  C  C   . ALA D  1 113 ? 10.706  -5.039  -44.010 1.00 7.27   ? 113 ALA D C   1 
ATOM   7454  O  O   . ALA D  1 113 ? 11.208  -4.193  -44.759 1.00 8.19   ? 113 ALA D O   1 
ATOM   7455  C  CB  . ALA D  1 113 ? 10.343  -7.307  -44.984 1.00 10.55  ? 113 ALA D CB  1 
ATOM   7456  N  N   . ALA D  1 114 ? 9.668   -4.766  -43.201 1.00 7.01   ? 114 ALA D N   1 
ATOM   7457  C  CA  . ALA D  1 114 ? 9.032   -3.439  -43.213 1.00 7.16   ? 114 ALA D CA  1 
ATOM   7458  C  C   . ALA D  1 114 ? 8.340   -3.281  -41.873 1.00 6.72   ? 114 ALA D C   1 
ATOM   7459  O  O   . ALA D  1 114 ? 8.324   -4.226  -41.036 1.00 7.10   ? 114 ALA D O   1 
ATOM   7460  C  CB  . ALA D  1 114 ? 8.098   -3.278  -44.395 1.00 8.01   ? 114 ALA D CB  1 
ATOM   7461  N  N   . GLU D  1 115 ? 7.701   -2.132  -41.669 1.00 6.58   ? 115 GLU D N   1 
ATOM   7462  C  CA  . GLU D  1 115 ? 6.997   -1.870  -40.422 1.00 7.05   ? 115 GLU D CA  1 
ATOM   7463  C  C   . GLU D  1 115 ? 5.866   -0.931  -40.697 1.00 6.29   ? 115 GLU D C   1 
ATOM   7464  O  O   . GLU D  1 115 ? 6.032   0.051   -41.404 1.00 7.63   ? 115 GLU D O   1 
ATOM   7465  C  CB  . GLU D  1 115 ? 7.973   -1.330  -39.367 1.00 7.54   ? 115 GLU D CB  1 
ATOM   7466  C  CG  . GLU D  1 115 ? 7.444   -1.143  -37.968 1.00 7.59   ? 115 GLU D CG  1 
ATOM   7467  C  CD  . GLU D  1 115 ? 8.500   -0.935  -36.942 1.00 7.09   ? 115 GLU D CD  1 
ATOM   7468  O  OE1 . GLU D  1 115 ? 9.655   -1.412  -37.135 1.00 8.27   ? 115 GLU D OE1 1 
ATOM   7469  O  OE2 . GLU D  1 115 ? 8.228   -0.251  -35.898 1.00 8.52   ? 115 GLU D OE2 1 
ATOM   7470  N  N   . LEU D  1 116 ? 4.704   -1.215  -40.110 1.00 6.70   ? 116 LEU D N   1 
ATOM   7471  C  CA  . LEU D  1 116 ? 3.530   -0.342  -40.166 1.00 6.92   ? 116 LEU D CA  1 
ATOM   7472  C  C   . LEU D  1 116 ? 3.402   0.386   -38.858 1.00 6.97   ? 116 LEU D C   1 
ATOM   7473  O  O   . LEU D  1 116 ? 3.515   -0.245  -37.786 1.00 7.66   ? 116 LEU D O   1 
ATOM   7474  C  CB  . LEU D  1 116 ? 2.269   -1.206  -40.337 1.00 8.31   ? 116 LEU D CB  1 
ATOM   7475  C  CG  . LEU D  1 116 ? 0.947   -0.467  -40.258 1.00 8.54   ? 116 LEU D CG  1 
ATOM   7476  C  CD1 . LEU D  1 116 ? 0.680   0.403   -41.464 1.00 10.00  ? 116 LEU D CD1 1 
ATOM   7477  C  CD2 . LEU D  1 116 ? -0.236  -1.434  -40.038 1.00 11.12  ? 116 LEU D CD2 1 
ATOM   7478  N  N   . HIS D  1 117 ? 3.140   1.685   -38.897 1.00 6.31   ? 117 HIS D N   1 
ATOM   7479  C  CA  . HIS D  1 117 ? 2.845   2.499   -37.715 1.00 7.10   ? 117 HIS D CA  1 
ATOM   7480  C  C   . HIS D  1 117 ? 1.475   3.058   -37.824 1.00 6.27   ? 117 HIS D C   1 
ATOM   7481  O  O   . HIS D  1 117 ? 1.137   3.708   -38.825 1.00 7.87   ? 117 HIS D O   1 
ATOM   7482  C  CB  . HIS D  1 117 ? 3.877   3.634   -37.617 1.00 7.21   ? 117 HIS D CB  1 
ATOM   7483  C  CG  . HIS D  1 117 ? 5.210   3.163   -37.275 1.00 6.73   ? 117 HIS D CG  1 
ATOM   7484  N  ND1 . HIS D  1 117 ? 6.367   3.866   -37.521 1.00 6.82   ? 117 HIS D ND1 1 
ATOM   7485  C  CD2 . HIS D  1 117 ? 5.585   1.988   -36.671 1.00 7.56   ? 117 HIS D CD2 1 
ATOM   7486  C  CE1 . HIS D  1 117 ? 7.387   3.138   -37.091 1.00 6.95   ? 117 HIS D CE1 1 
ATOM   7487  N  NE2 . HIS D  1 117 ? 6.943   1.985   -36.566 1.00 7.53   ? 117 HIS D NE2 1 
ATOM   7488  N  N   . ILE D  1 118 ? 0.658   2.815   -36.799 1.00 7.64   ? 118 ILE D N   1 
ATOM   7489  C  CA  . ILE D  1 118 ? -0.684  3.412   -36.723 1.00 8.30   ? 118 ILE D CA  1 
ATOM   7490  C  C   . ILE D  1 118 ? -0.630  4.472   -35.627 1.00 7.52   ? 118 ILE D C   1 
ATOM   7491  O  O   . ILE D  1 118 ? -0.463  4.130   -34.424 1.00 8.42   ? 118 ILE D O   1 
ATOM   7492  C  CB  . ILE D  1 118 ? -1.808  2.396   -36.437 1.00 8.83   ? 118 ILE D CB  1 
ATOM   7493  C  CG1 . ILE D  1 118 ? -1.677  1.189   -37.429 1.00 9.80   ? 118 ILE D CG1 1 
ATOM   7494  C  CG2 . ILE D  1 118 ? -3.143  3.103   -36.589 1.00 10.03  ? 118 ILE D CG2 1 
ATOM   7495  C  CD1 . ILE D  1 118 ? -2.722  0.129   -37.156 1.00 12.21  ? 118 ILE D CD1 1 
ATOM   7496  N  N   . VAL D  1 119 ? -0.620  5.745   -35.990 1.00 8.44   ? 119 VAL D N   1 
ATOM   7497  C  CA  . VAL D  1 119 ? -0.390  6.842   -35.096 1.00 8.55   ? 119 VAL D CA  1 
ATOM   7498  C  C   . VAL D  1 119 ? -1.697  7.323   -34.495 1.00 8.87   ? 119 VAL D C   1 
ATOM   7499  O  O   . VAL D  1 119 ? -2.644  7.600   -35.208 1.00 9.54   ? 119 VAL D O   1 
ATOM   7500  C  CB  . VAL D  1 119 ? 0.320   8.001   -35.844 1.00 8.93   ? 119 VAL D CB  1 
ATOM   7501  C  CG1 . VAL D  1 119 ? 0.693   9.134   -34.865 1.00 10.57  ? 119 VAL D CG1 1 
ATOM   7502  C  CG2 . VAL D  1 119 ? 1.558   7.457   -36.585 1.00 9.39   ? 119 VAL D CG2 1 
ATOM   7503  N  N   . HIS D  1 120 ? -1.652  7.497   -33.166 1.00 8.93   ? 120 HIS D N   1 
ATOM   7504  C  CA  . HIS D  1 120 ? -2.805  8.075   -32.433 1.00 9.55   ? 120 HIS D CA  1 
ATOM   7505  C  C   . HIS D  1 120 ? -2.295  9.197   -31.537 1.00 9.85   ? 120 HIS D C   1 
ATOM   7506  O  O   . HIS D  1 120 ? -1.154  9.235   -31.162 1.00 10.77  ? 120 HIS D O   1 
ATOM   7507  C  CB  . HIS D  1 120 ? -3.371  6.966   -31.497 1.00 10.41  ? 120 HIS D CB  1 
ATOM   7508  C  CG  . HIS D  1 120 ? -3.809  5.686   -32.155 1.00 9.43   ? 120 HIS D CG  1 
ATOM   7509  N  ND1 . HIS D  1 120 ? -2.904  4.795   -32.721 1.00 10.84  ? 120 HIS D ND1 1 
ATOM   7510  C  CD2 . HIS D  1 120 ? -5.046  5.142   -32.332 1.00 10.77  ? 120 HIS D CD2 1 
ATOM   7511  C  CE1 . HIS D  1 120 ? -3.586  3.775   -33.176 1.00 10.20  ? 120 HIS D CE1 1 
ATOM   7512  N  NE2 . HIS D  1 120 ? -4.893  3.938   -32.932 1.00 10.86  ? 120 HIS D NE2 1 
ATOM   7513  N  N   . TYR D  1 121 ? -3.246  10.116  -31.201 1.00 10.49  ? 121 TYR D N   1 
ATOM   7514  C  CA  . TYR D  1 121 ? -2.920  11.237  -30.341 1.00 11.13  ? 121 TYR D CA  1 
ATOM   7515  C  C   . TYR D  1 121 ? -3.813  11.231  -29.128 1.00 10.54  ? 121 TYR D C   1 
ATOM   7516  O  O   . TYR D  1 121 ? -4.925  10.713  -29.170 1.00 11.51  ? 121 TYR D O   1 
ATOM   7517  C  CB  . TYR D  1 121 ? -2.944  12.566  -31.076 1.00 10.56  ? 121 TYR D CB  1 
ATOM   7518  C  CG  . TYR D  1 121 ? -4.323  13.040  -31.470 1.00 11.23  ? 121 TYR D CG  1 
ATOM   7519  C  CD1 . TYR D  1 121 ? -4.983  12.525  -32.564 1.00 12.24  ? 121 TYR D CD1 1 
ATOM   7520  C  CD2 . TYR D  1 121 ? -5.015  13.982  -30.685 1.00 10.95  ? 121 TYR D CD2 1 
ATOM   7521  C  CE1 . TYR D  1 121 ? -6.250  12.904  -32.947 1.00 15.36  ? 121 TYR D CE1 1 
ATOM   7522  C  CE2 . TYR D  1 121 ? -6.288  14.385  -31.060 1.00 14.61  ? 121 TYR D CE2 1 
ATOM   7523  C  CZ  . TYR D  1 121 ? -6.925  13.808  -32.158 1.00 16.57  ? 121 TYR D CZ  1 
ATOM   7524  O  OH  . TYR D  1 121 ? -8.197  14.230  -32.486 1.00 21.58  ? 121 TYR D OH  1 
ATOM   7525  N  N   . ASN D  1 122 ? -3.346  11.910  -28.097 1.00 10.59  ? 122 ASN D N   1 
ATOM   7526  C  CA  . ASN D  1 122 ? -4.048  11.997  -26.785 1.00 11.68  ? 122 ASN D CA  1 
ATOM   7527  C  C   . ASN D  1 122 ? -5.151  13.013  -26.944 1.00 11.62  ? 122 ASN D C   1 
ATOM   7528  O  O   . ASN D  1 122 ? -4.956  14.204  -26.718 1.00 13.18  ? 122 ASN D O   1 
ATOM   7529  C  CB  . ASN D  1 122 ? -3.061  12.315  -25.665 1.00 12.17  ? 122 ASN D CB  1 
ATOM   7530  C  CG  . ASN D  1 122 ? -3.688  12.185  -24.321 1.00 13.32  ? 122 ASN D CG  1 
ATOM   7531  O  OD1 . ASN D  1 122 ? -4.947  12.321  -24.170 1.00 14.38  ? 122 ASN D OD1 1 
ATOM   7532  N  ND2 . ASN D  1 122 ? -2.816  11.910  -23.349 1.00 15.22  ? 122 ASN D ND2 1 
ATOM   7533  N  N   . SER D  1 123 ? -6.347  12.520  -27.280 1.00 12.09  ? 123 SER D N   1 
ATOM   7534  C  CA  . SER D  1 123 ? -7.456  13.431  -27.479 1.00 14.02  ? 123 SER D CA  1 
ATOM   7535  C  C   . SER D  1 123 ? -8.149  13.810  -26.204 1.00 14.78  ? 123 SER D C   1 
ATOM   7536  O  O   . SER D  1 123 ? -9.022  14.667  -26.205 1.00 18.34  ? 123 SER D O   1 
ATOM   7537  C  CB  . SER D  1 123 ? -8.466  12.783  -28.457 1.00 14.74  ? 123 SER D CB  1 
ATOM   7538  O  OG  . SER D  1 123 ? -8.784  11.428  -28.151 1.00 16.33  ? 123 SER D OG  1 
ATOM   7539  N  N   . ASP D  1 124 ? -7.806  13.175  -25.085 1.00 15.65  ? 124 ASP D N   1 
ATOM   7540  C  CA  . ASP D  1 124 ? -8.219  13.731  -23.752 1.00 15.20  ? 124 ASP D CA  1 
ATOM   7541  C  C   . ASP D  1 124 ? -7.508  15.032  -23.417 1.00 15.49  ? 124 ASP D C   1 
ATOM   7542  O  O   . ASP D  1 124 ? -8.069  15.835  -22.660 1.00 19.72  ? 124 ASP D O   1 
ATOM   7543  C  CB  . ASP D  1 124 ? -7.889  12.735  -22.626 1.00 15.28  ? 124 ASP D CB  1 
ATOM   7544  C  CG  . ASP D  1 124 ? -8.725  11.544  -22.653 1.00 15.37  ? 124 ASP D CG  1 
ATOM   7545  O  OD1 . ASP D  1 124 ? -9.765  11.484  -23.395 1.00 14.44  ? 124 ASP D OD1 1 
ATOM   7546  O  OD2 . ASP D  1 124 ? -8.436  10.567  -21.872 1.00 16.83  ? 124 ASP D OD2 1 
ATOM   7547  N  N   . LEU D  1 125 ? -6.260  15.243  -23.807 1.00 13.64  ? 125 LEU D N   1 
ATOM   7548  C  CA  . LEU D  1 125 ? -5.492  16.412  -23.513 1.00 14.19  ? 125 LEU D CA  1 
ATOM   7549  C  C   . LEU D  1 125 ? -5.468  17.404  -24.601 1.00 13.39  ? 125 LEU D C   1 
ATOM   7550  O  O   . LEU D  1 125 ? -5.320  18.560  -24.316 1.00 15.62  ? 125 LEU D O   1 
ATOM   7551  C  CB  . LEU D  1 125 ? -4.070  16.058  -23.107 1.00 14.51  ? 125 LEU D CB  1 
ATOM   7552  C  CG  . LEU D  1 125 ? -3.815  15.590  -21.670 1.00 16.50  ? 125 LEU D CG  1 
ATOM   7553  C  CD1 . LEU D  1 125 ? -4.762  14.444  -21.296 1.00 19.35  ? 125 LEU D CD1 1 
ATOM   7554  C  CD2 . LEU D  1 125 ? -2.372  15.242  -21.424 1.00 20.48  ? 125 LEU D CD2 1 
ATOM   7555  N  N   . TYR D  1 126 ? -5.454  16.960  -25.875 1.00 12.51  ? 126 TYR D N   1 
ATOM   7556  C  CA  . TYR D  1 126 ? -5.149  17.815  -26.960 1.00 12.93  ? 126 TYR D CA  1 
ATOM   7557  C  C   . TYR D  1 126 ? -6.194  17.813  -28.019 1.00 13.94  ? 126 TYR D C   1 
ATOM   7558  O  O   . TYR D  1 126 ? -6.861  16.785  -28.286 1.00 13.99  ? 126 TYR D O   1 
ATOM   7559  C  CB  . TYR D  1 126 ? -3.765  17.378  -27.556 1.00 12.85  ? 126 TYR D CB  1 
ATOM   7560  C  CG  . TYR D  1 126 ? -2.686  17.339  -26.488 1.00 12.33  ? 126 TYR D CG  1 
ATOM   7561  C  CD1 . TYR D  1 126 ? -2.286  18.491  -25.791 1.00 14.70  ? 126 TYR D CD1 1 
ATOM   7562  C  CD2 . TYR D  1 126 ? -2.101  16.123  -26.106 1.00 11.78  ? 126 TYR D CD2 1 
ATOM   7563  C  CE1 . TYR D  1 126 ? -1.393  18.426  -24.730 1.00 14.27  ? 126 TYR D CE1 1 
ATOM   7564  C  CE2 . TYR D  1 126 ? -1.168  16.062  -25.100 1.00 11.93  ? 126 TYR D CE2 1 
ATOM   7565  C  CZ  . TYR D  1 126 ? -0.825  17.209  -24.409 1.00 13.21  ? 126 TYR D CZ  1 
ATOM   7566  O  OH  . TYR D  1 126 ? 0.074   17.193  -23.363 1.00 13.25  ? 126 TYR D OH  1 
ATOM   7567  N  N   . PRO D  1 127 ? -6.268  18.927  -28.786 1.00 14.44  ? 127 PRO D N   1 
ATOM   7568  C  CA  . PRO D  1 127 ? -7.357  19.050  -29.723 1.00 17.25  ? 127 PRO D CA  1 
ATOM   7569  C  C   . PRO D  1 127 ? -7.123  18.364  -31.068 1.00 17.34  ? 127 PRO D C   1 
ATOM   7570  O  O   . PRO D  1 127 ? -8.046  18.269  -31.863 1.00 21.71  ? 127 PRO D O   1 
ATOM   7571  C  CB  . PRO D  1 127 ? -7.436  20.572  -29.982 1.00 21.23  ? 127 PRO D CB  1 
ATOM   7572  C  CG  . PRO D  1 127 ? -6.056  21.127  -29.612 1.00 20.45  ? 127 PRO D CG  1 
ATOM   7573  C  CD  . PRO D  1 127 ? -5.613  20.227  -28.508 1.00 16.15  ? 127 PRO D CD  1 
ATOM   7574  N  N   . ASP D  1 128 ? -5.865  18.022  -31.364 1.00 15.13  ? 128 ASP D N   1 
ATOM   7575  C  CA  . ASP D  1 128 ? -5.504  17.544  -32.651 1.00 14.73  ? 128 ASP D CA  1 
ATOM   7576  C  C   . ASP D  1 128 ? -4.100  16.966  -32.548 1.00 13.77  ? 128 ASP D C   1 
ATOM   7577  O  O   . ASP D  1 128 ? -3.366  17.216  -31.573 1.00 13.84  ? 128 ASP D O   1 
ATOM   7578  C  CB  . ASP D  1 128 ? -5.555  18.647  -33.778 1.00 18.95  ? 128 ASP D CB  1 
ATOM   7579  C  CG  . ASP D  1 128 ? -4.642  19.811  -33.453 1.00 16.97  ? 128 ASP D CG  1 
ATOM   7580  O  OD1 . ASP D  1 128 ? -5.116  20.758  -32.793 1.00 20.63  ? 128 ASP D OD1 1 
ATOM   7581  O  OD2 . ASP D  1 128 ? -3.440  19.753  -33.794 1.00 22.91  ? 128 ASP D OD2 1 
ATOM   7582  N  N   . ALA D  1 129 ? -3.706  16.166  -33.536 1.00 14.51  ? 129 ALA D N   1 
ATOM   7583  C  CA  . ALA D  1 129 ? -2.459  15.447  -33.480 1.00 13.30  ? 129 ALA D CA  1 
ATOM   7584  C  C   . ALA D  1 129 ? -1.231  16.368  -33.511 1.00 12.61  ? 129 ALA D C   1 
ATOM   7585  O  O   . ALA D  1 129 ? -0.209  16.127  -32.845 1.00 14.05  ? 129 ALA D O   1 
ATOM   7586  C  CB  . ALA D  1 129 ? -2.358  14.411  -34.594 1.00 18.15  ? 129 ALA D CB  1 
ATOM   7587  N  N   A SER D  1 130 ? -1.326  17.425  -34.334 0.50 13.62  ? 130 SER D N   1 
ATOM   7588  N  N   B SER D  1 130 ? -1.248  17.418  -34.332 0.50 13.51  ? 130 SER D N   1 
ATOM   7589  C  CA  A SER D  1 130 ? -0.214  18.371  -34.455 0.50 15.33  ? 130 SER D CA  1 
ATOM   7590  C  CA  B SER D  1 130 ? -0.081  18.316  -34.433 0.50 12.67  ? 130 SER D CA  1 
ATOM   7591  C  C   A SER D  1 130 ? 0.108   18.925  -33.096 0.50 12.16  ? 130 SER D C   1 
ATOM   7592  C  C   B SER D  1 130 ? 0.162   19.028  -33.093 0.50 12.42  ? 130 SER D C   1 
ATOM   7593  O  O   A SER D  1 130 ? 1.248   18.822  -32.629 0.50 16.39  ? 130 SER D O   1 
ATOM   7594  O  O   B SER D  1 130 ? 1.314   19.141  -32.622 0.50 13.82  ? 130 SER D O   1 
ATOM   7595  C  CB  A SER D  1 130 ? -0.590  19.474  -35.422 0.50 16.33  ? 130 SER D CB  1 
ATOM   7596  C  CB  B SER D  1 130 ? -0.347  19.320  -35.558 0.50 13.31  ? 130 SER D CB  1 
ATOM   7597  O  OG  A SER D  1 130 ? -0.616  18.834  -36.666 0.50 25.08  ? 130 SER D OG  1 
ATOM   7598  O  OG  B SER D  1 130 ? 0.693   20.238  -35.628 0.50 15.65  ? 130 SER D OG  1 
ATOM   7599  N  N   . THR D  1 131 ? -0.934  19.422  -32.439 1.00 12.60  ? 131 THR D N   1 
ATOM   7600  C  CA  . THR D  1 131 ? -0.748  20.040  -31.123 1.00 13.52  ? 131 THR D CA  1 
ATOM   7601  C  C   . THR D  1 131 ? -0.181  19.049  -30.100 1.00 12.41  ? 131 THR D C   1 
ATOM   7602  O  O   . THR D  1 131 ? 0.683   19.403  -29.266 1.00 13.67  ? 131 THR D O   1 
ATOM   7603  C  CB  . THR D  1 131 ? -2.081  20.583  -30.617 1.00 14.18  ? 131 THR D CB  1 
ATOM   7604  O  OG1 . THR D  1 131 ? -2.533  21.567  -31.576 1.00 15.53  ? 131 THR D OG1 1 
ATOM   7605  C  CG2 . THR D  1 131 ? -1.925  21.247  -29.272 1.00 16.05  ? 131 THR D CG2 1 
ATOM   7606  N  N   . ALA D  1 132 ? -0.654  17.799  -30.168 1.00 11.41  ? 132 ALA D N   1 
ATOM   7607  C  CA  . ALA D  1 132 ? -0.220  16.808  -29.248 1.00 11.83  ? 132 ALA D CA  1 
ATOM   7608  C  C   . ALA D  1 132 ? 1.227   16.385  -29.415 1.00 12.54  ? 132 ALA D C   1 
ATOM   7609  O  O   . ALA D  1 132 ? 1.902   15.934  -28.458 1.00 12.51  ? 132 ALA D O   1 
ATOM   7610  C  CB  . ALA D  1 132 ? -1.067  15.590  -29.428 1.00 11.93  ? 132 ALA D CB  1 
ATOM   7611  N  N   . SER D  1 133 ? 1.737   16.491  -30.650 1.00 12.66  ? 133 SER D N   1 
ATOM   7612  C  CA  . SER D  1 133 ? 2.940   15.803  -30.979 1.00 12.95  ? 133 SER D CA  1 
ATOM   7613  C  C   . SER D  1 133 ? 4.154   16.237  -30.201 1.00 11.86  ? 133 SER D C   1 
ATOM   7614  O  O   . SER D  1 133 ? 5.098   15.453  -30.078 1.00 13.28  ? 133 SER D O   1 
ATOM   7615  C  CB  . SER D  1 133 ? 3.151   15.897  -32.508 1.00 15.99  ? 133 SER D CB  1 
ATOM   7616  O  OG  . SER D  1 133 ? 3.571   17.154  -32.857 1.00 18.76  ? 133 SER D OG  1 
ATOM   7617  N  N   . ASN D  1 134 ? 4.202   17.486  -29.732 1.00 13.25  ? 134 ASN D N   1 
ATOM   7618  C  CA  . ASN D  1 134 ? 5.370   17.974  -28.945 1.00 13.03  ? 134 ASN D CA  1 
ATOM   7619  C  C   . ASN D  1 134 ? 5.077   18.152  -27.493 1.00 12.80  ? 134 ASN D C   1 
ATOM   7620  O  O   . ASN D  1 134 ? 5.807   18.846  -26.785 1.00 16.56  ? 134 ASN D O   1 
ATOM   7621  C  CB  . ASN D  1 134 ? 6.058   19.195  -29.537 1.00 15.92  ? 134 ASN D CB  1 
ATOM   7622  C  CG  . ASN D  1 134 ? 5.195   20.427  -29.408 1.00 17.70  ? 134 ASN D CG  1 
ATOM   7623  O  OD1 . ASN D  1 134 ? 3.975   20.334  -29.295 1.00 16.27  ? 134 ASN D OD1 1 
ATOM   7624  N  ND2 . ASN D  1 134 ? 5.804   21.586  -29.378 1.00 17.55  ? 134 ASN D ND2 1 
ATOM   7625  N  N   . LYS D  1 135 ? 4.039   17.483  -26.997 1.00 12.30  ? 135 LYS D N   1 
ATOM   7626  C  CA  . LYS D  1 135 ? 3.598   17.700  -25.607 1.00 12.74  ? 135 LYS D CA  1 
ATOM   7627  C  C   . LYS D  1 135 ? 3.495   16.413  -24.868 1.00 12.33  ? 135 LYS D C   1 
ATOM   7628  O  O   . LYS D  1 135 ? 3.395   15.300  -25.430 1.00 12.43  ? 135 LYS D O   1 
ATOM   7629  C  CB  . LYS D  1 135 ? 2.226   18.444  -25.638 1.00 13.15  ? 135 LYS D CB  1 
ATOM   7630  C  CG  . LYS D  1 135 ? 2.458   19.861  -26.246 1.00 14.19  ? 135 LYS D CG  1 
ATOM   7631  C  CD  . LYS D  1 135 ? 1.191   20.647  -26.227 1.00 15.43  ? 135 LYS D CD  1 
ATOM   7632  C  CE  . LYS D  1 135 ? 1.265   22.006  -26.931 1.00 16.23  ? 135 LYS D CE  1 
ATOM   7633  N  NZ  . LYS D  1 135 ? 1.745   21.800  -28.343 1.00 17.13  ? 135 LYS D NZ  1 
ATOM   7634  N  N   A SER D  1 136 ? 3.395   16.563  -23.588 0.50 13.58  ? 136 SER D N   1 
ATOM   7635  N  N   B SER D  1 136 ? 3.695   16.536  -23.559 0.50 12.15  ? 136 SER D N   1 
ATOM   7636  C  CA  A SER D  1 136 ? 3.441   15.455  -22.669 0.50 17.83  ? 136 SER D CA  1 
ATOM   7637  C  CA  B SER D  1 136 ? 3.532   15.408  -22.597 0.50 12.73  ? 136 SER D CA  1 
ATOM   7638  C  C   A SER D  1 136 ? 2.353   14.405  -22.927 0.50 13.97  ? 136 SER D C   1 
ATOM   7639  C  C   B SER D  1 136 ? 2.443   14.424  -22.970 0.50 11.08  ? 136 SER D C   1 
ATOM   7640  O  O   A SER D  1 136 ? 1.150   14.718  -23.113 0.50 10.34  ? 136 SER D O   1 
ATOM   7641  O  O   B SER D  1 136 ? 1.285   14.812  -23.149 0.50 12.80  ? 136 SER D O   1 
ATOM   7642  C  CB  A SER D  1 136 ? 3.325   16.033  -21.273 0.50 18.86  ? 136 SER D CB  1 
ATOM   7643  C  CB  B SER D  1 136 ? 3.076   15.923  -21.244 0.50 12.29  ? 136 SER D CB  1 
ATOM   7644  O  OG  A SER D  1 136 ? 3.495   15.024  -20.347 0.50 17.98  ? 136 SER D OG  1 
ATOM   7645  O  OG  B SER D  1 136 ? 4.027   16.756  -20.685 0.50 15.49  ? 136 SER D OG  1 
ATOM   7646  N  N   . GLU D  1 137 ? 2.766   13.155  -23.000 1.00 13.63  ? 137 GLU D N   1 
ATOM   7647  C  CA  . GLU D  1 137 ? 1.850   12.098  -23.191 1.00 12.92  ? 137 GLU D CA  1 
ATOM   7648  C  C   . GLU D  1 137 ? 1.122   12.260  -24.538 1.00 12.21  ? 137 GLU D C   1 
ATOM   7649  O  O   . GLU D  1 137 ? -0.001  11.742  -24.724 1.00 11.61  ? 137 GLU D O   1 
ATOM   7650  C  CB  . GLU D  1 137 ? 0.753   11.933  -22.055 1.00 13.58  ? 137 GLU D CB  1 
ATOM   7651  C  CG  . GLU D  1 137 ? 1.379   11.867  -20.718 1.00 17.83  ? 137 GLU D CG  1 
ATOM   7652  C  CD  . GLU D  1 137 ? 2.245   10.609  -20.452 1.00 28.14  ? 137 GLU D CD  1 
ATOM   7653  O  OE1 . GLU D  1 137 ? 2.199   9.625   -21.152 1.00 29.82  ? 137 GLU D OE1 1 
ATOM   7654  O  OE2 . GLU D  1 137 ? 3.042   10.647  -19.542 1.00 43.83  ? 137 GLU D OE2 1 
ATOM   7655  N  N   . GLY D  1 138 ? 1.665   12.948  -25.549 1.00 11.61  ? 138 GLY D N   1 
ATOM   7656  C  CA  . GLY D  1 138 ? 0.861   13.342  -26.689 1.00 12.09  ? 138 GLY D CA  1 
ATOM   7657  C  C   . GLY D  1 138 ? 0.460   12.212  -27.621 1.00 9.98   ? 138 GLY D C   1 
ATOM   7658  O  O   . GLY D  1 138 ? -0.564  12.314  -28.262 1.00 10.09  ? 138 GLY D O   1 
ATOM   7659  N  N   . LEU D  1 139 ? 1.321   11.178  -27.810 1.00 10.55  ? 139 LEU D N   1 
ATOM   7660  C  CA  . LEU D  1 139 ? 1.084   10.245  -28.934 1.00 10.23  ? 139 LEU D CA  1 
ATOM   7661  C  C   . LEU D  1 139 ? 1.211   8.803   -28.421 1.00 9.69   ? 139 LEU D C   1 
ATOM   7662  O  O   . LEU D  1 139 ? 1.931   8.493   -27.477 1.00 10.47  ? 139 LEU D O   1 
ATOM   7663  C  CB  . LEU D  1 139 ? 2.161   10.456  -29.980 1.00 10.21  ? 139 LEU D CB  1 
ATOM   7664  C  CG  . LEU D  1 139 ? 2.115   11.818  -30.686 1.00 10.30  ? 139 LEU D CG  1 
ATOM   7665  C  CD1 . LEU D  1 139 ? 3.345   11.974  -31.546 1.00 11.77  ? 139 LEU D CD1 1 
ATOM   7666  C  CD2 . LEU D  1 139 ? 0.835   12.101  -31.445 1.00 12.10  ? 139 LEU D CD2 1 
ATOM   7667  N  N   . ALA D  1 140 ? 0.517   7.953   -29.124 1.00 9.85   ? 140 ALA D N   1 
ATOM   7668  C  CA  . ALA D  1 140 ? 0.631   6.451   -28.964 1.00 10.25  ? 140 ALA D CA  1 
ATOM   7669  C  C   . ALA D  1 140 ? 0.670   5.855   -30.361 1.00 8.87   ? 140 ALA D C   1 
ATOM   7670  O  O   . ALA D  1 140 ? -0.210  6.116   -31.159 1.00 10.39  ? 140 ALA D O   1 
ATOM   7671  C  CB  . ALA D  1 140 ? -0.554  5.875   -28.192 1.00 12.90  ? 140 ALA D CB  1 
ATOM   7672  N  N   . VAL D  1 141 ? 1.719   5.084   -30.624 1.00 8.57   ? 141 VAL D N   1 
ATOM   7673  C  CA  . VAL D  1 141 ? 1.836   4.466   -31.901 1.00 8.05   ? 141 VAL D CA  1 
ATOM   7674  C  C   . VAL D  1 141 ? 1.790   2.960   -31.766 1.00 8.76   ? 141 VAL D C   1 
ATOM   7675  O  O   . VAL D  1 141 ? 2.433   2.388   -30.843 1.00 9.33   ? 141 VAL D O   1 
ATOM   7676  C  CB  . VAL D  1 141 ? 3.145   4.898   -32.647 1.00 8.69   ? 141 VAL D CB  1 
ATOM   7677  C  CG1 . VAL D  1 141 ? 3.263   4.217   -34.040 1.00 9.67   ? 141 VAL D CG1 1 
ATOM   7678  C  CG2 . VAL D  1 141 ? 3.128   6.417   -32.833 1.00 9.42   ? 141 VAL D CG2 1 
ATOM   7679  N  N   . LEU D  1 142 ? 1.047   2.290   -32.640 1.00 8.49   ? 142 LEU D N   1 
ATOM   7680  C  CA  . LEU D  1 142 ? 1.071   0.852   -32.750 1.00 7.98   ? 142 LEU D CA  1 
ATOM   7681  C  C   . LEU D  1 142 ? 2.014   0.465   -33.856 1.00 7.85   ? 142 LEU D C   1 
ATOM   7682  O  O   . LEU D  1 142 ? 1.868   0.994   -34.985 1.00 9.55   ? 142 LEU D O   1 
ATOM   7683  C  CB  . LEU D  1 142 ? -0.298  0.301   -33.048 1.00 9.42   ? 142 LEU D CB  1 
ATOM   7684  C  CG  . LEU D  1 142 ? -1.417  0.699   -32.117 1.00 10.60  ? 142 LEU D CG  1 
ATOM   7685  C  CD1 . LEU D  1 142 ? -2.756  0.069   -32.563 1.00 12.24  ? 142 LEU D CD1 1 
ATOM   7686  C  CD2 . LEU D  1 142 ? -1.062  0.321   -30.653 1.00 13.31  ? 142 LEU D CD2 1 
ATOM   7687  N  N   . ALA D  1 143 ? 2.891   -0.468  -33.616 1.00 8.12   ? 143 ALA D N   1 
ATOM   7688  C  CA  . ALA D  1 143 ? 3.829   -0.957  -34.645 1.00 8.01   ? 143 ALA D CA  1 
ATOM   7689  C  C   . ALA D  1 143 ? 3.583   -2.403  -34.940 1.00 7.56   ? 143 ALA D C   1 
ATOM   7690  O  O   . ALA D  1 143 ? 3.534   -3.242  -34.010 1.00 8.70   ? 143 ALA D O   1 
ATOM   7691  C  CB  . ALA D  1 143 ? 5.236   -0.738  -34.140 1.00 8.97   ? 143 ALA D CB  1 
ATOM   7692  N  N   . VAL D  1 144 ? 3.466   -2.682  -36.218 1.00 7.84   ? 144 VAL D N   1 
ATOM   7693  C  CA  . VAL D  1 144 ? 3.347   -4.053  -36.719 1.00 7.76   ? 144 VAL D CA  1 
ATOM   7694  C  C   . VAL D  1 144 ? 4.605   -4.347  -37.548 1.00 7.45   ? 144 VAL D C   1 
ATOM   7695  O  O   . VAL D  1 144 ? 4.893   -3.662  -38.538 1.00 8.23   ? 144 VAL D O   1 
ATOM   7696  C  CB  . VAL D  1 144 ? 2.108   -4.230  -37.568 1.00 8.85   ? 144 VAL D CB  1 
ATOM   7697  C  CG1 . VAL D  1 144 ? 2.018   -5.681  -38.007 1.00 10.14  ? 144 VAL D CG1 1 
ATOM   7698  C  CG2 . VAL D  1 144 ? 0.829   -3.822  -36.847 1.00 9.65   ? 144 VAL D CG2 1 
ATOM   7699  N  N   . LEU D  1 145 ? 5.314   -5.371  -37.149 1.00 7.77   ? 145 LEU D N   1 
ATOM   7700  C  CA  . LEU D  1 145 ? 6.476   -5.863  -37.880 1.00 8.35   ? 145 LEU D CA  1 
ATOM   7701  C  C   . LEU D  1 145 ? 5.993   -6.670  -39.063 1.00 8.05   ? 145 LEU D C   1 
ATOM   7702  O  O   . LEU D  1 145 ? 5.032   -7.453  -38.953 1.00 9.36   ? 145 LEU D O   1 
ATOM   7703  C  CB  . LEU D  1 145 ? 7.341   -6.736  -36.951 1.00 9.64   ? 145 LEU D CB  1 
ATOM   7704  C  CG  . LEU D  1 145 ? 7.878   -5.963  -35.748 1.00 11.09  ? 145 LEU D CG  1 
ATOM   7705  C  CD1 . LEU D  1 145 ? 8.387   -6.984  -34.717 1.00 12.64  ? 145 LEU D CD1 1 
ATOM   7706  C  CD2 . LEU D  1 145 ? 8.949   -4.982  -36.213 1.00 13.46  ? 145 LEU D CD2 1 
ATOM   7707  N  N   . ILE D  1 146 ? 6.637   -6.474  -40.232 1.00 8.22   ? 146 ILE D N   1 
ATOM   7708  C  CA  . ILE D  1 146 ? 6.189   -7.100  -41.478 1.00 7.85   ? 146 ILE D CA  1 
ATOM   7709  C  C   . ILE D  1 146 ? 7.292   -7.949  -42.028 1.00 7.82   ? 146 ILE D C   1 
ATOM   7710  O  O   . ILE D  1 146 ? 8.404   -7.453  -42.240 1.00 8.97   ? 146 ILE D O   1 
ATOM   7711  C  CB  . ILE D  1 146 ? 5.772   -6.020  -42.513 1.00 8.24   ? 146 ILE D CB  1 
ATOM   7712  C  CG1 . ILE D  1 146 ? 4.631   -5.167  -41.993 1.00 9.45   ? 146 ILE D CG1 1 
ATOM   7713  C  CG2 . ILE D  1 146 ? 5.436   -6.655  -43.839 1.00 10.22  ? 146 ILE D CG2 1 
ATOM   7714  C  CD1 . ILE D  1 146 ? 4.398   -3.910  -42.845 1.00 10.51  ? 146 ILE D CD1 1 
ATOM   7715  N  N   A GLU D  1 147 ? 7.100   -9.258  -42.161 0.50 6.98   ? 147 GLU D N   1 
ATOM   7716  N  N   B GLU D  1 147 ? 6.909   -9.173  -42.392 0.50 7.85   ? 147 GLU D N   1 
ATOM   7717  C  CA  A GLU D  1 147 ? 8.124   -10.154 -42.736 0.50 9.66   ? 147 GLU D CA  1 
ATOM   7718  C  CA  B GLU D  1 147 ? 7.800   -10.180 -42.876 0.50 8.61   ? 147 GLU D CA  1 
ATOM   7719  C  C   A GLU D  1 147 ? 7.625   -10.576 -44.160 0.50 8.36   ? 147 GLU D C   1 
ATOM   7720  C  C   B GLU D  1 147 ? 7.509   -10.532 -44.307 0.50 8.72   ? 147 GLU D C   1 
ATOM   7721  O  O   A GLU D  1 147 ? 6.439   -10.611 -44.442 0.50 7.95   ? 147 GLU D O   1 
ATOM   7722  O  O   B GLU D  1 147 ? 6.356   -10.457 -44.759 0.50 9.90   ? 147 GLU D O   1 
ATOM   7723  C  CB  A GLU D  1 147 ? 8.329   -11.424 -41.874 0.50 14.03  ? 147 GLU D CB  1 
ATOM   7724  C  CB  B GLU D  1 147 ? 7.646   -11.424 -42.005 0.50 9.49   ? 147 GLU D CB  1 
ATOM   7725  C  CG  A GLU D  1 147 ? 7.202   -12.444 -41.913 0.50 18.79  ? 147 GLU D CG  1 
ATOM   7726  C  CG  B GLU D  1 147 ? 8.703   -12.460 -42.264 0.50 12.08  ? 147 GLU D CG  1 
ATOM   7727  C  CD  A GLU D  1 147 ? 7.376   -13.624 -40.960 0.50 24.14  ? 147 GLU D CD  1 
ATOM   7728  C  CD  B GLU D  1 147 ? 8.949   -13.383 -41.083 0.50 16.39  ? 147 GLU D CD  1 
ATOM   7729  O  OE1 A GLU D  1 147 ? 8.499   -13.821 -40.445 0.50 22.14  ? 147 GLU D OE1 1 
ATOM   7730  O  OE1 B GLU D  1 147 ? 8.382   -13.129 -39.999 0.50 20.67  ? 147 GLU D OE1 1 
ATOM   7731  O  OE2 A GLU D  1 147 ? 6.401   -14.381 -40.747 0.50 24.66  ? 147 GLU D OE2 1 
ATOM   7732  O  OE2 B GLU D  1 147 ? 9.711   -14.350 -41.269 0.50 24.72  ? 147 GLU D OE2 1 
ATOM   7733  N  N   . MET D  1 148 ? 8.587   -10.871 -45.059 1.00 8.74   ? 148 MET D N   1 
ATOM   7734  C  CA  . MET D  1 148 ? 8.339   -11.360 -46.377 1.00 8.94   ? 148 MET D CA  1 
ATOM   7735  C  C   . MET D  1 148 ? 7.736   -12.789 -46.261 1.00 8.62   ? 148 MET D C   1 
ATOM   7736  O  O   . MET D  1 148 ? 8.336   -13.658 -45.661 1.00 11.22  ? 148 MET D O   1 
ATOM   7737  C  CB  . MET D  1 148 ? 9.613   -11.380 -47.170 1.00 10.83  ? 148 MET D CB  1 
ATOM   7738  C  CG  . MET D  1 148 ? 9.433   -11.781 -48.580 1.00 12.37  ? 148 MET D CG  1 
ATOM   7739  S  SD  . MET D  1 148 ? 10.971  -11.845 -49.546 1.00 13.73  ? 148 MET D SD  1 
ATOM   7740  C  CE  . MET D  1 148 ? 11.458  -10.150 -49.541 1.00 15.02  ? 148 MET D CE  1 
ATOM   7741  N  N   . GLY D  1 149 ? 6.565   -12.966 -46.837 1.00 8.95   ? 149 GLY D N   1 
ATOM   7742  C  CA  . GLY D  1 149 ? 5.860   -14.244 -46.741 1.00 9.28   ? 149 GLY D CA  1 
ATOM   7743  C  C   . GLY D  1 149 ? 4.745   -14.308 -47.726 1.00 8.66   ? 149 GLY D C   1 
ATOM   7744  O  O   . GLY D  1 149 ? 4.932   -14.058 -48.945 1.00 9.67   ? 149 GLY D O   1 
ATOM   7745  N  N   . SER D  1 150 ? 3.553   -14.684 -47.313 1.00 9.59   ? 150 SER D N   1 
ATOM   7746  C  CA  . SER D  1 150 ? 2.421   -14.807 -48.180 1.00 9.22   ? 150 SER D CA  1 
ATOM   7747  C  C   . SER D  1 150 ? 1.821   -13.440 -48.553 1.00 9.94   ? 150 SER D C   1 
ATOM   7748  O  O   . SER D  1 150 ? 1.878   -12.484 -47.808 1.00 11.30  ? 150 SER D O   1 
ATOM   7749  C  CB  . SER D  1 150 ? 1.319   -15.624 -47.500 1.00 10.53  ? 150 SER D CB  1 
ATOM   7750  O  OG  . SER D  1 150 ? 1.754   -16.984 -47.361 1.00 11.07  ? 150 SER D OG  1 
ATOM   7751  N  N   . PHE D  1 151 ? 1.222   -13.406 -49.729 1.00 10.31  ? 151 PHE D N   1 
ATOM   7752  C  CA  . PHE D  1 151 ? 0.421   -12.254 -50.164 1.00 9.95   ? 151 PHE D CA  1 
ATOM   7753  C  C   . PHE D  1 151 ? -0.623  -11.886 -49.139 1.00 10.18  ? 151 PHE D C   1 
ATOM   7754  O  O   . PHE D  1 151 ? -1.282  -12.773 -48.594 1.00 11.73  ? 151 PHE D O   1 
ATOM   7755  C  CB  . PHE D  1 151 ? -0.246  -12.592 -51.490 1.00 11.25  ? 151 PHE D CB  1 
ATOM   7756  C  CG  . PHE D  1 151 ? -1.083  -11.469 -52.044 1.00 11.77  ? 151 PHE D CG  1 
ATOM   7757  C  CD1 . PHE D  1 151 ? -0.470  -10.381 -52.636 1.00 12.86  ? 151 PHE D CD1 1 
ATOM   7758  C  CD2 . PHE D  1 151 ? -2.448  -11.476 -51.907 1.00 14.55  ? 151 PHE D CD2 1 
ATOM   7759  C  CE1 . PHE D  1 151 ? -1.225  -9.305  -53.161 1.00 14.38  ? 151 PHE D CE1 1 
ATOM   7760  C  CE2 . PHE D  1 151 ? -3.200  -10.445 -52.394 1.00 14.35  ? 151 PHE D CE2 1 
ATOM   7761  C  CZ  . PHE D  1 151 ? -2.592  -9.359  -52.999 1.00 14.78  ? 151 PHE D CZ  1 
ATOM   7762  N  N   . ASN D  1 152 ? -0.771  -10.579 -48.907 1.00 9.73   ? 152 ASN D N   1 
ATOM   7763  C  CA  . ASN D  1 152 ? -1.651  -10.071 -47.884 1.00 10.98  ? 152 ASN D CA  1 
ATOM   7764  C  C   . ASN D  1 152 ? -2.710  -9.207  -48.525 1.00 10.49  ? 152 ASN D C   1 
ATOM   7765  O  O   . ASN D  1 152 ? -2.440  -8.048  -48.918 1.00 10.93  ? 152 ASN D O   1 
ATOM   7766  C  CB  . ASN D  1 152 ? -0.864  -9.316  -46.819 1.00 10.48  ? 152 ASN D CB  1 
ATOM   7767  C  CG  . ASN D  1 152 ? -1.677  -9.043  -45.625 1.00 10.77  ? 152 ASN D CG  1 
ATOM   7768  O  OD1 . ASN D  1 152 ? -2.799  -8.512  -45.718 1.00 11.41  ? 152 ASN D OD1 1 
ATOM   7769  N  ND2 . ASN D  1 152 ? -1.126  -9.353  -44.492 1.00 10.68  ? 152 ASN D ND2 1 
ATOM   7770  N  N   A PRO D  1 153 ? -3.920  -9.754  -48.788 0.50 11.28  ? 153 PRO D N   1 
ATOM   7771  N  N   B PRO D  1 153 ? -3.928  -9.738  -48.644 0.50 12.02  ? 153 PRO D N   1 
ATOM   7772  C  CA  A PRO D  1 153 ? -5.015  -8.971  -49.403 0.50 12.61  ? 153 PRO D CA  1 
ATOM   7773  C  CA  B PRO D  1 153 ? -4.905  -8.938  -49.383 0.50 13.58  ? 153 PRO D CA  1 
ATOM   7774  C  C   A PRO D  1 153 ? -5.355  -7.704  -48.645 0.50 11.80  ? 153 PRO D C   1 
ATOM   7775  C  C   B PRO D  1 153 ? -5.264  -7.674  -48.640 0.50 13.64  ? 153 PRO D C   1 
ATOM   7776  O  O   A PRO D  1 153 ? -5.783  -6.738  -49.279 0.50 14.14  ? 153 PRO D O   1 
ATOM   7777  O  O   B PRO D  1 153 ? -5.585  -6.681  -49.277 0.50 15.51  ? 153 PRO D O   1 
ATOM   7778  C  CB  A PRO D  1 153 ? -6.204  -9.963  -49.400 0.50 15.58  ? 153 PRO D CB  1 
ATOM   7779  C  CB  B PRO D  1 153 ? -6.120  -9.889  -49.574 0.50 18.38  ? 153 PRO D CB  1 
ATOM   7780  C  CG  A PRO D  1 153 ? -5.519  -11.305 -49.550 0.50 12.85  ? 153 PRO D CG  1 
ATOM   7781  C  CG  B PRO D  1 153 ? -5.898  -11.041 -48.615 0.50 19.89  ? 153 PRO D CG  1 
ATOM   7782  C  CD  A PRO D  1 153 ? -4.311  -11.196 -48.646 0.50 15.13  ? 153 PRO D CD  1 
ATOM   7783  C  CD  B PRO D  1 153 ? -4.446  -11.087 -48.246 0.50 14.46  ? 153 PRO D CD  1 
ATOM   7784  N  N   . SER D  1 154 ? -5.215  -7.661  -47.323 1.00 13.01  ? 154 SER D N   1 
ATOM   7785  C  CA  . SER D  1 154 ? -5.582  -6.474  -46.585 1.00 13.63  ? 154 SER D CA  1 
ATOM   7786  C  C   . SER D  1 154 ? -4.583  -5.369  -46.775 1.00 12.42  ? 154 SER D C   1 
ATOM   7787  O  O   . SER D  1 154 ? -4.965  -4.214  -47.033 1.00 13.31  ? 154 SER D O   1 
ATOM   7788  C  CB  . SER D  1 154 ? -5.712  -6.874  -45.105 1.00 15.15  ? 154 SER D CB  1 
ATOM   7789  O  OG  . SER D  1 154 ? -6.749  -7.832  -44.960 1.00 18.56  ? 154 SER D OG  1 
ATOM   7790  N  N   . TYR D  1 155 ? -3.263  -5.660  -46.713 1.00 11.65  ? 155 TYR D N   1 
ATOM   7791  C  CA  . TYR D  1 155 ? -2.282  -4.607  -47.013 1.00 10.70  ? 155 TYR D CA  1 
ATOM   7792  C  C   . TYR D  1 155 ? -2.386  -4.178  -48.456 1.00 11.21  ? 155 TYR D C   1 
ATOM   7793  O  O   . TYR D  1 155 ? -2.146  -3.010  -48.785 1.00 12.23  ? 155 TYR D O   1 
ATOM   7794  C  CB  . TYR D  1 155 ? -0.834  -5.073  -46.647 1.00 10.95  ? 155 TYR D CB  1 
ATOM   7795  C  CG  . TYR D  1 155 ? -0.489  -4.959  -45.222 1.00 10.71  ? 155 TYR D CG  1 
ATOM   7796  C  CD1 . TYR D  1 155 ? -0.940  -5.904  -44.286 1.00 11.23  ? 155 TYR D CD1 1 
ATOM   7797  C  CD2 . TYR D  1 155 ? 0.254   -3.894  -44.771 1.00 10.90  ? 155 TYR D CD2 1 
ATOM   7798  C  CE1 . TYR D  1 155 ? -0.649  -5.791  -42.950 1.00 11.17  ? 155 TYR D CE1 1 
ATOM   7799  C  CE2 . TYR D  1 155 ? 0.549   -3.757  -43.420 1.00 11.49  ? 155 TYR D CE2 1 
ATOM   7800  C  CZ  . TYR D  1 155 ? 0.080   -4.727  -42.485 1.00 10.36  ? 155 TYR D CZ  1 
ATOM   7801  O  OH  . TYR D  1 155 ? 0.400   -4.516  -41.173 1.00 10.94  ? 155 TYR D OH  1 
ATOM   7802  N  N   . ASP D  1 156 ? -2.793  -5.060  -49.355 1.00 11.33  ? 156 ASP D N   1 
ATOM   7803  C  CA  . ASP D  1 156 ? -2.988  -4.673  -50.741 1.00 12.61  ? 156 ASP D CA  1 
ATOM   7804  C  C   . ASP D  1 156 ? -4.099  -3.596  -50.966 1.00 11.93  ? 156 ASP D C   1 
ATOM   7805  O  O   . ASP D  1 156 ? -4.084  -2.924  -51.970 1.00 13.53  ? 156 ASP D O   1 
ATOM   7806  C  CB  . ASP D  1 156 ? -3.272  -5.859  -51.655 1.00 14.68  ? 156 ASP D CB  1 
ATOM   7807  C  CG  . ASP D  1 156 ? -2.395  -5.812  -52.892 1.00 15.81  ? 156 ASP D CG  1 
ATOM   7808  O  OD1 . ASP D  1 156 ? -1.165  -5.669  -52.716 1.00 14.87  ? 156 ASP D OD1 1 
ATOM   7809  O  OD2 . ASP D  1 156 ? -2.918  -5.860  -54.024 1.00 17.21  ? 156 ASP D OD2 1 
ATOM   7810  N  N   . LYS D  1 157 ? -5.018  -3.479  -49.984 1.00 12.45  ? 157 LYS D N   1 
ATOM   7811  C  CA  . LYS D  1 157 ? -6.044  -2.456  -50.085 1.00 13.83  ? 157 LYS D CA  1 
ATOM   7812  C  C   . LYS D  1 157 ? -5.371  -1.076  -50.013 1.00 15.73  ? 157 LYS D C   1 
ATOM   7813  O  O   . LYS D  1 157 ? -5.930  -0.126  -50.562 1.00 19.24  ? 157 LYS D O   1 
ATOM   7814  C  CB  . LYS D  1 157 ? -7.036  -2.651  -48.944 1.00 15.98  ? 157 LYS D CB  1 
ATOM   7815  C  CG  . LYS D  1 157 ? -7.885  -3.894  -49.192 1.00 16.10  ? 157 LYS D CG  1 
ATOM   7816  C  CD  . LYS D  1 157 ? -8.780  -4.247  -47.977 1.00 18.92  ? 157 LYS D CD  1 
ATOM   7817  C  CE  . LYS D  1 157 ? -9.474  -5.601  -48.139 1.00 20.17  ? 157 LYS D CE  1 
ATOM   7818  N  NZ  . LYS D  1 157 ? -10.314 -6.023  -46.954 1.00 23.48  ? 157 LYS D NZ  1 
ATOM   7819  N  N   . ILE D  1 158 ? -4.199  -0.948  -49.400 1.00 13.17  ? 158 ILE D N   1 
ATOM   7820  C  CA  . ILE D  1 158 ? -3.359  0.256   -49.439 1.00 13.72  ? 158 ILE D CA  1 
ATOM   7821  C  C   . ILE D  1 158 ? -2.493  0.231   -50.664 1.00 11.82  ? 158 ILE D C   1 
ATOM   7822  O  O   . ILE D  1 158 ? -2.416  1.190   -51.451 1.00 13.13  ? 158 ILE D O   1 
ATOM   7823  C  CB  . ILE D  1 158 ? -2.520  0.395   -48.155 1.00 15.22  ? 158 ILE D CB  1 
ATOM   7824  C  CG1 . ILE D  1 158 ? -3.450  0.536   -46.942 1.00 19.84  ? 158 ILE D CG1 1 
ATOM   7825  C  CG2 . ILE D  1 158 ? -1.536  1.594   -48.299 1.00 15.23  ? 158 ILE D CG2 1 
ATOM   7826  C  CD1 . ILE D  1 158 ? -2.742  0.371   -45.603 1.00 21.83  ? 158 ILE D CD1 1 
ATOM   7827  N  N   . PHE D  1 159 ? -1.735  -0.880  -50.835 1.00 12.38  ? 159 PHE D N   1 
ATOM   7828  C  CA  . PHE D  1 159 ? -0.685  -0.893  -51.834 1.00 12.83  ? 159 PHE D CA  1 
ATOM   7829  C  C   . PHE D  1 159 ? -1.167  -0.748  -53.258 1.00 12.81  ? 159 PHE D C   1 
ATOM   7830  O  O   . PHE D  1 159 ? -0.442  -0.237  -54.120 1.00 14.61  ? 159 PHE D O   1 
ATOM   7831  C  CB  . PHE D  1 159 ? 0.162   -2.193  -51.718 1.00 12.63  ? 159 PHE D CB  1 
ATOM   7832  C  CG  . PHE D  1 159 ? 0.870   -2.429  -50.409 1.00 11.63  ? 159 PHE D CG  1 
ATOM   7833  C  CD1 . PHE D  1 159 ? 1.253   -1.406  -49.556 1.00 14.64  ? 159 PHE D CD1 1 
ATOM   7834  C  CD2 . PHE D  1 159 ? 1.214   -3.733  -50.082 1.00 12.93  ? 159 PHE D CD2 1 
ATOM   7835  C  CE1 . PHE D  1 159 ? 1.935   -1.702  -48.380 1.00 14.06  ? 159 PHE D CE1 1 
ATOM   7836  C  CE2 . PHE D  1 159 ? 1.888   -4.029  -48.922 1.00 13.97  ? 159 PHE D CE2 1 
ATOM   7837  C  CZ  . PHE D  1 159 ? 2.251   -3.009  -48.065 1.00 14.33  ? 159 PHE D CZ  1 
ATOM   7838  N  N   . SER D  1 160 ? -2.394  -1.142  -53.551 1.00 12.72  ? 160 SER D N   1 
ATOM   7839  C  CA  . SER D  1 160 ? -2.914  -1.009  -54.880 1.00 13.43  ? 160 SER D CA  1 
ATOM   7840  C  C   . SER D  1 160 ? -3.026  0.471   -55.340 1.00 14.09  ? 160 SER D C   1 
ATOM   7841  O  O   . SER D  1 160 ? -3.154  0.726   -56.546 1.00 15.60  ? 160 SER D O   1 
ATOM   7842  C  CB  . SER D  1 160 ? -4.278  -1.703  -55.062 1.00 17.15  ? 160 SER D CB  1 
ATOM   7843  O  OG  . SER D  1 160 ? -5.222  -1.049  -54.270 1.00 16.54  ? 160 SER D OG  1 
ATOM   7844  N  N   . HIS D  1 161 ? -2.993  1.418   -54.411 1.00 12.77  ? 161 HIS D N   1 
ATOM   7845  C  CA  . HIS D  1 161 ? -3.162  2.819   -54.746 1.00 13.95  ? 161 HIS D CA  1 
ATOM   7846  C  C   . HIS D  1 161 ? -1.827  3.553   -54.884 1.00 14.33  ? 161 HIS D C   1 
ATOM   7847  O  O   . HIS D  1 161 ? -1.822  4.743   -55.178 1.00 15.67  ? 161 HIS D O   1 
ATOM   7848  C  CB  . HIS D  1 161 ? -3.976  3.509   -53.643 1.00 13.54  ? 161 HIS D CB  1 
ATOM   7849  C  CG  . HIS D  1 161 ? -5.363  3.041   -53.590 1.00 13.34  ? 161 HIS D CG  1 
ATOM   7850  N  ND1 . HIS D  1 161 ? -6.357  3.626   -54.328 1.00 15.47  ? 161 HIS D ND1 1 
ATOM   7851  C  CD2 . HIS D  1 161 ? -5.926  1.986   -52.931 1.00 14.69  ? 161 HIS D CD2 1 
ATOM   7852  C  CE1 . HIS D  1 161 ? -7.524  2.977   -54.117 1.00 16.98  ? 161 HIS D CE1 1 
ATOM   7853  N  NE2 . HIS D  1 161 ? -7.240  1.954   -53.256 1.00 15.30  ? 161 HIS D NE2 1 
ATOM   7854  N  N   . LEU D  1 162 ? -0.682  2.844   -54.677 1.00 16.21  ? 162 LEU D N   1 
ATOM   7855  C  CA  . LEU D  1 162 ? 0.632   3.551   -54.627 1.00 19.24  ? 162 LEU D CA  1 
ATOM   7856  C  C   . LEU D  1 162 ? 0.975   4.331   -55.855 1.00 15.98  ? 162 LEU D C   1 
ATOM   7857  O  O   . LEU D  1 162 ? 1.586   5.436   -55.748 1.00 20.32  ? 162 LEU D O   1 
ATOM   7858  C  CB  . LEU D  1 162 ? 1.751   2.567   -54.265 1.00 21.87  ? 162 LEU D CB  1 
ATOM   7859  C  CG  . LEU D  1 162 ? 1.636   1.980   -52.872 1.00 23.46  ? 162 LEU D CG  1 
ATOM   7860  C  CD1 . LEU D  1 162 ? 2.782   1.013   -52.643 1.00 40.09  ? 162 LEU D CD1 1 
ATOM   7861  C  CD2 . LEU D  1 162 ? 1.560   3.011   -51.731 1.00 30.66  ? 162 LEU D CD2 1 
ATOM   7862  N  N   . GLN D  1 163 ? 0.571   3.853   -57.001 1.00 19.77  ? 163 GLN D N   1 
ATOM   7863  C  CA  . GLN D  1 163 ? 1.016   4.502   -58.186 1.00 21.34  ? 163 GLN D CA  1 
ATOM   7864  C  C   . GLN D  1 163 ? 0.341   5.905   -58.261 1.00 20.72  ? 163 GLN D C   1 
ATOM   7865  O  O   . GLN D  1 163 ? 0.880   6.809   -58.928 1.00 25.51  ? 163 GLN D O   1 
ATOM   7866  C  CB  . GLN D  1 163 ? 0.936   3.585   -59.431 1.00 34.86  ? 163 GLN D CB  1 
ATOM   7867  C  CG  . GLN D  1 163 ? 2.357   3.232   -60.046 1.00 60.22  ? 163 GLN D CG  1 
ATOM   7868  C  CD  . GLN D  1 163 ? 3.555   2.895   -59.073 1.00 37.55  ? 163 GLN D CD  1 
ATOM   7869  O  OE1 . GLN D  1 163 ? 3.816   1.664   -58.743 1.00 31.14  ? 163 GLN D OE1 1 
ATOM   7870  N  NE2 . GLN D  1 163 ? 4.274   4.002   -58.567 1.00 28.07  ? 163 GLN D NE2 1 
ATOM   7871  N  N   . HIS D  1 164 ? -0.751  6.149   -57.544 1.00 16.59  ? 164 HIS D N   1 
ATOM   7872  C  CA  . HIS D  1 164 ? -1.439  7.424   -57.554 1.00 15.99  ? 164 HIS D CA  1 
ATOM   7873  C  C   . HIS D  1 164 ? -0.842  8.463   -56.612 1.00 15.08  ? 164 HIS D C   1 
ATOM   7874  O  O   . HIS D  1 164 ? -1.276  9.610   -56.599 1.00 16.76  ? 164 HIS D O   1 
ATOM   7875  C  CB  . HIS D  1 164 ? -2.926  7.202   -57.334 1.00 18.06  ? 164 HIS D CB  1 
ATOM   7876  C  CG  . HIS D  1 164 ? -3.514  6.205   -58.317 1.00 22.06  ? 164 HIS D CG  1 
ATOM   7877  N  ND1 . HIS D  1 164 ? -3.662  6.467   -59.621 1.00 31.81  ? 164 HIS D ND1 1 
ATOM   7878  C  CD2 . HIS D  1 164 ? -3.914  4.896   -58.120 1.00 35.91  ? 164 HIS D CD2 1 
ATOM   7879  C  CE1 . HIS D  1 164 ? -4.239  5.404   -60.230 1.00 35.91  ? 164 HIS D CE1 1 
ATOM   7880  N  NE2 . HIS D  1 164 ? -4.391  4.438   -59.310 1.00 44.19  ? 164 HIS D NE2 1 
ATOM   7881  N  N   . VAL D  1 165 ? 0.127   8.056   -55.768 1.00 13.92  ? 165 VAL D N   1 
ATOM   7882  C  CA  . VAL D  1 165 ? 0.787   8.962   -54.865 1.00 14.52  ? 165 VAL D CA  1 
ATOM   7883  C  C   . VAL D  1 165 ? 2.310   8.817   -55.017 1.00 15.07  ? 165 VAL D C   1 
ATOM   7884  O  O   . VAL D  1 165 ? 3.069   8.966   -54.082 1.00 13.42  ? 165 VAL D O   1 
ATOM   7885  C  CB  . VAL D  1 165 ? 0.345   8.653   -53.432 1.00 16.78  ? 165 VAL D CB  1 
ATOM   7886  C  CG1 . VAL D  1 165 ? -1.128  9.056   -53.238 1.00 17.28  ? 165 VAL D CG1 1 
ATOM   7887  C  CG2 . VAL D  1 165 ? 0.668   7.211   -52.990 1.00 17.49  ? 165 VAL D CG2 1 
ATOM   7888  N  N   . LYS D  1 166 ? 2.724   8.653   -56.261 1.00 13.65  ? 166 LYS D N   1 
ATOM   7889  C  CA  . LYS D  1 166 ? 4.123   8.373   -56.526 1.00 14.03  ? 166 LYS D CA  1 
ATOM   7890  C  C   . LYS D  1 166 ? 5.051   9.511   -56.063 1.00 12.00  ? 166 LYS D C   1 
ATOM   7891  O  O   . LYS D  1 166 ? 6.146   9.257   -55.621 1.00 12.21  ? 166 LYS D O   1 
ATOM   7892  C  CB  . LYS D  1 166 ? 4.291   8.196   -58.026 1.00 16.13  ? 166 LYS D CB  1 
ATOM   7893  C  CG  . LYS D  1 166 ? 5.681   7.963   -58.520 1.00 18.98  ? 166 LYS D CG  1 
ATOM   7894  C  CD  . LYS D  1 166 ? 5.686   7.576   -60.046 1.00 25.44  ? 166 LYS D CD  1 
ATOM   7895  C  CE  . LYS D  1 166 ? 4.743   6.445   -60.390 1.00 47.56  ? 166 LYS D CE  1 
ATOM   7896  N  NZ  . LYS D  1 166 ? 5.440   5.127   -60.327 1.00 50.94  ? 166 LYS D NZ  1 
ATOM   7897  N  N   . TYR D  1 167 ? 4.613   10.781  -56.197 1.00 11.36  ? 167 TYR D N   1 
ATOM   7898  C  CA  . TYR D  1 167 ? 5.493   11.917  -55.947 1.00 10.50  ? 167 TYR D CA  1 
ATOM   7899  C  C   . TYR D  1 167 ? 4.979   12.746  -54.801 1.00 11.18  ? 167 TYR D C   1 
ATOM   7900  O  O   . TYR D  1 167 ? 3.783   12.739  -54.458 1.00 11.63  ? 167 TYR D O   1 
ATOM   7901  C  CB  . TYR D  1 167 ? 5.559   12.804  -57.184 1.00 11.47  ? 167 TYR D CB  1 
ATOM   7902  C  CG  . TYR D  1 167 ? 6.291   12.101  -58.295 1.00 12.28  ? 167 TYR D CG  1 
ATOM   7903  C  CD1 . TYR D  1 167 ? 7.668   11.980  -58.259 1.00 13.99  ? 167 TYR D CD1 1 
ATOM   7904  C  CD2 . TYR D  1 167 ? 5.588   11.671  -59.391 1.00 14.33  ? 167 TYR D CD2 1 
ATOM   7905  C  CE1 . TYR D  1 167 ? 8.389   11.332  -59.266 1.00 15.12  ? 167 TYR D CE1 1 
ATOM   7906  C  CE2 . TYR D  1 167 ? 6.279   11.022  -60.438 1.00 16.66  ? 167 TYR D CE2 1 
ATOM   7907  C  CZ  . TYR D  1 167 ? 7.662   10.881  -60.343 1.00 17.28  ? 167 TYR D CZ  1 
ATOM   7908  O  OH  . TYR D  1 167 ? 8.221   10.219  -61.430 1.00 25.08  ? 167 TYR D OH  1 
ATOM   7909  N  N   . LYS D  1 168 ? 5.907   13.504  -54.207 1.00 12.32  ? 168 LYS D N   1 
ATOM   7910  C  CA  . LYS D  1 168 ? 5.602   14.339  -53.118 1.00 16.21  ? 168 LYS D CA  1 
ATOM   7911  C  C   . LYS D  1 168 ? 4.415   15.235  -53.441 1.00 16.49  ? 168 LYS D C   1 
ATOM   7912  O  O   . LYS D  1 168 ? 4.382   15.902  -54.464 1.00 15.51  ? 168 LYS D O   1 
ATOM   7913  C  CB  . LYS D  1 168 ? 6.807   15.167  -52.730 1.00 16.81  ? 168 LYS D CB  1 
ATOM   7914  C  CG  . LYS D  1 168 ? 6.557   15.959  -51.452 1.00 20.88  ? 168 LYS D CG  1 
ATOM   7915  C  CD  . LYS D  1 168 ? 7.852   16.557  -50.955 1.00 19.96  ? 168 LYS D CD  1 
ATOM   7916  C  CE  . LYS D  1 168 ? 7.531   17.755  -50.040 1.00 43.28  ? 168 LYS D CE  1 
ATOM   7917  N  NZ  . LYS D  1 168 ? 8.746   18.318  -49.383 1.00 45.50  ? 168 LYS D NZ  1 
ATOM   7918  N  N   . GLY D  1 169 ? 3.453   15.289  -52.522 1.00 18.82  ? 169 GLY D N   1 
ATOM   7919  C  CA  . GLY D  1 169 ? 2.270   16.114  -52.714 1.00 22.38  ? 169 GLY D CA  1 
ATOM   7920  C  C   . GLY D  1 169 ? 1.090   15.516  -53.412 1.00 21.94  ? 169 GLY D C   1 
ATOM   7921  O  O   . GLY D  1 169 ? -0.030  16.025  -53.328 1.00 24.13  ? 169 GLY D O   1 
ATOM   7922  N  N   . GLN D  1 170 ? 1.268   14.351  -53.998 1.00 14.65  ? 170 GLN D N   1 
ATOM   7923  C  CA  . GLN D  1 170 ? 0.162   13.661  -54.647 1.00 13.66  ? 170 GLN D CA  1 
ATOM   7924  C  C   . GLN D  1 170 ? -0.695  12.978  -53.570 1.00 14.92  ? 170 GLN D C   1 
ATOM   7925  O  O   . GLN D  1 170 ? -0.206  12.535  -52.511 1.00 15.86  ? 170 GLN D O   1 
ATOM   7926  C  CB  . GLN D  1 170 ? 0.696   12.714  -55.659 1.00 14.08  ? 170 GLN D CB  1 
ATOM   7927  C  CG  . GLN D  1 170 ? 1.394   13.469  -56.791 1.00 15.29  ? 170 GLN D CG  1 
ATOM   7928  C  CD  . GLN D  1 170 ? 1.785   12.560  -57.941 1.00 15.39  ? 170 GLN D CD  1 
ATOM   7929  O  OE1 . GLN D  1 170 ? 2.167   11.434  -57.745 1.00 14.75  ? 170 GLN D OE1 1 
ATOM   7930  N  NE2 . GLN D  1 170 ? 1.849   13.094  -59.144 1.00 19.99  ? 170 GLN D NE2 1 
ATOM   7931  N  N   . GLU D  1 171 ? -1.956  12.820  -53.915 1.00 16.31  ? 171 GLU D N   1 
ATOM   7932  C  CA  . GLU D  1 171 ? -3.010  12.343  -53.033 1.00 16.04  ? 171 GLU D CA  1 
ATOM   7933  C  C   . GLU D  1 171 ? -3.945  11.457  -53.794 1.00 19.08  ? 171 GLU D C   1 
ATOM   7934  O  O   . GLU D  1 171 ? -4.161  11.635  -55.023 1.00 22.66  ? 171 GLU D O   1 
ATOM   7935  C  CB  . GLU D  1 171 ? -3.780  13.510  -52.375 1.00 22.34  ? 171 GLU D CB  1 
ATOM   7936  C  CG  . GLU D  1 171 ? -2.944  14.410  -51.466 1.00 25.37  ? 171 GLU D CG  1 
ATOM   7937  C  CD  . GLU D  1 171 ? -3.729  15.613  -50.945 1.00 42.16  ? 171 GLU D CD  1 
ATOM   7938  O  OE1 . GLU D  1 171 ? -4.847  15.861  -51.438 1.00 43.89  ? 171 GLU D OE1 1 
ATOM   7939  O  OE2 . GLU D  1 171 ? -3.217  16.289  -50.030 1.00 52.64  ? 171 GLU D OE2 1 
ATOM   7940  N  N   . ALA D  1 172 ? -4.560  10.507  -53.088 1.00 17.89  ? 172 ALA D N   1 
ATOM   7941  C  CA  . ALA D  1 172 ? -5.523  9.587   -53.679 1.00 18.47  ? 172 ALA D CA  1 
ATOM   7942  C  C   . ALA D  1 172 ? -6.450  9.144   -52.583 1.00 15.04  ? 172 ALA D C   1 
ATOM   7943  O  O   . ALA D  1 172 ? -6.077  9.101   -51.455 1.00 17.70  ? 172 ALA D O   1 
ATOM   7944  C  CB  . ALA D  1 172 ? -4.798  8.379   -54.276 1.00 21.02  ? 172 ALA D CB  1 
ATOM   7945  N  N   . PHE D  1 173 ? -7.662  8.813   -52.934 1.00 16.76  ? 173 PHE D N   1 
ATOM   7946  C  CA  . PHE D  1 173 ? -8.605  8.305   -51.981 1.00 14.88  ? 173 PHE D CA  1 
ATOM   7947  C  C   . PHE D  1 173 ? -8.651  6.770   -51.959 1.00 15.02  ? 173 PHE D C   1 
ATOM   7948  O  O   . PHE D  1 173 ? -8.663  6.126   -53.036 1.00 21.04  ? 173 PHE D O   1 
ATOM   7949  C  CB  . PHE D  1 173 ? -9.967  8.906   -52.287 1.00 18.55  ? 173 PHE D CB  1 
ATOM   7950  C  CG  . PHE D  1 173 ? -10.138 10.305  -51.681 1.00 21.03  ? 173 PHE D CG  1 
ATOM   7951  C  CD1 . PHE D  1 173 ? -10.227 10.475  -50.239 1.00 21.38  ? 173 PHE D CD1 1 
ATOM   7952  C  CD2 . PHE D  1 173 ? -10.247 11.449  -52.494 1.00 32.10  ? 173 PHE D CD2 1 
ATOM   7953  C  CE1 . PHE D  1 173 ? -10.412 11.743  -49.676 1.00 29.63  ? 173 PHE D CE1 1 
ATOM   7954  C  CE2 . PHE D  1 173 ? -10.400 12.711  -51.917 1.00 36.82  ? 173 PHE D CE2 1 
ATOM   7955  C  CZ  . PHE D  1 173 ? -10.505 12.857  -50.499 1.00 31.73  ? 173 PHE D CZ  1 
ATOM   7956  N  N   . VAL D  1 174 ? -8.722  6.196   -50.787 1.00 13.83  ? 174 VAL D N   1 
ATOM   7957  C  CA  . VAL D  1 174 ? -8.764  4.765   -50.511 1.00 14.32  ? 174 VAL D CA  1 
ATOM   7958  C  C   . VAL D  1 174 ? -10.126 4.488   -49.890 1.00 13.31  ? 174 VAL D C   1 
ATOM   7959  O  O   . VAL D  1 174 ? -10.445 5.109   -48.880 1.00 14.18  ? 174 VAL D O   1 
ATOM   7960  C  CB  . VAL D  1 174 ? -7.592  4.344   -49.581 1.00 14.44  ? 174 VAL D CB  1 
ATOM   7961  C  CG1 . VAL D  1 174 ? -7.668  2.808   -49.257 1.00 17.64  ? 174 VAL D CG1 1 
ATOM   7962  C  CG2 . VAL D  1 174 ? -6.282  4.677   -50.293 1.00 16.44  ? 174 VAL D CG2 1 
ATOM   7963  N  N   . PRO D  1 175 ? -10.911 3.576   -50.438 1.00 13.65  ? 175 PRO D N   1 
ATOM   7964  C  CA  . PRO D  1 175 ? -12.140 3.204   -49.754 1.00 13.65  ? 175 PRO D CA  1 
ATOM   7965  C  C   . PRO D  1 175 ? -11.820 2.600   -48.387 1.00 12.83  ? 175 PRO D C   1 
ATOM   7966  O  O   . PRO D  1 175 ? -10.862 1.865   -48.224 1.00 13.86  ? 175 PRO D O   1 
ATOM   7967  C  CB  . PRO D  1 175 ? -12.715 2.098   -50.647 1.00 16.65  ? 175 PRO D CB  1 
ATOM   7968  C  CG  . PRO D  1 175 ? -12.168 2.344   -52.011 1.00 19.36  ? 175 PRO D CG  1 
ATOM   7969  C  CD  . PRO D  1 175 ? -10.752 2.820   -51.689 1.00 15.28  ? 175 PRO D CD  1 
ATOM   7970  N  N   . GLY D  1 176 ? -12.688 2.807   -47.398 1.00 13.46  ? 176 GLY D N   1 
ATOM   7971  C  CA  . GLY D  1 176 ? -12.524 2.223   -46.095 1.00 13.72  ? 176 GLY D CA  1 
ATOM   7972  C  C   . GLY D  1 176 ? -12.457 0.715   -46.115 1.00 13.15  ? 176 GLY D C   1 
ATOM   7973  O  O   . GLY D  1 176 ? -13.154 0.044   -46.914 1.00 15.74  ? 176 GLY D O   1 
ATOM   7974  N  N   . PHE D  1 177 ? -11.717 0.204   -45.154 1.00 15.19  ? 177 PHE D N   1 
ATOM   7975  C  CA  . PHE D  1 177 ? -11.705 -1.241  -44.880 1.00 15.60  ? 177 PHE D CA  1 
ATOM   7976  C  C   . PHE D  1 177 ? -11.356 -1.353  -43.408 1.00 13.97  ? 177 PHE D C   1 
ATOM   7977  O  O   . PHE D  1 177 ? -11.129 -0.388  -42.691 1.00 14.41  ? 177 PHE D O   1 
ATOM   7978  C  CB  . PHE D  1 177 ? -10.704 -1.962  -45.782 1.00 15.89  ? 177 PHE D CB  1 
ATOM   7979  C  CG  . PHE D  1 177 ? -9.256  -1.627  -45.527 1.00 15.10  ? 177 PHE D CG  1 
ATOM   7980  C  CD1 . PHE D  1 177 ? -8.709  -0.458  -46.116 1.00 14.93  ? 177 PHE D CD1 1 
ATOM   7981  C  CD2 . PHE D  1 177 ? -8.452  -2.460  -44.750 1.00 18.21  ? 177 PHE D CD2 1 
ATOM   7982  C  CE1 . PHE D  1 177 ? -7.359  -0.190  -45.881 1.00 15.47  ? 177 PHE D CE1 1 
ATOM   7983  C  CE2 . PHE D  1 177 ? -7.082  -2.176  -44.543 1.00 17.01  ? 177 PHE D CE2 1 
ATOM   7984  C  CZ  . PHE D  1 177 ? -6.549  -1.006  -45.108 1.00 18.20  ? 177 PHE D CZ  1 
ATOM   7985  N  N   . ASN D  1 178 ? -11.416 -2.594  -42.919 1.00 18.64  ? 178 ASN D N   1 
ATOM   7986  C  CA  . ASN D  1 178 ? -11.223 -2.846  -41.517 1.00 17.46  ? 178 ASN D CA  1 
ATOM   7987  C  C   . ASN D  1 178 ? -9.694  -2.828  -41.238 1.00 14.41  ? 178 ASN D C   1 
ATOM   7988  O  O   . ASN D  1 178 ? -8.975  -3.786  -41.534 1.00 14.87  ? 178 ASN D O   1 
ATOM   7989  C  CB  . ASN D  1 178 ? -11.868 -4.206  -41.136 1.00 20.09  ? 178 ASN D CB  1 
ATOM   7990  C  CG  . ASN D  1 178 ? -11.692 -4.503  -39.717 1.00 19.99  ? 178 ASN D CG  1 
ATOM   7991  O  OD1 . ASN D  1 178 ? -11.243 -3.668  -38.874 1.00 18.81  ? 178 ASN D OD1 1 
ATOM   7992  N  ND2 . ASN D  1 178 ? -11.973 -5.787  -39.399 1.00 25.02  ? 178 ASN D ND2 1 
ATOM   7993  N  N   . ILE D  1 179 ? -9.239  -1.772  -40.595 1.00 14.18  ? 179 ILE D N   1 
ATOM   7994  C  CA  . ILE D  1 179 ? -7.817  -1.582  -40.238 1.00 12.43  ? 179 ILE D CA  1 
ATOM   7995  C  C   . ILE D  1 179 ? -7.314  -2.688  -39.314 1.00 14.00  ? 179 ILE D C   1 
ATOM   7996  O  O   . ILE D  1 179 ? -6.093  -2.968  -39.281 1.00 12.94  ? 179 ILE D O   1 
ATOM   7997  C  CB  . ILE D  1 179 ? -7.570  -0.134  -39.670 1.00 12.48  ? 179 ILE D CB  1 
ATOM   7998  C  CG1 . ILE D  1 179 ? -8.137  0.923   -40.622 1.00 14.09  ? 179 ILE D CG1 1 
ATOM   7999  C  CG2 . ILE D  1 179 ? -6.109  0.018   -39.261 1.00 14.11  ? 179 ILE D CG2 1 
ATOM   8000  C  CD1 . ILE D  1 179 ? -7.473  0.862   -42.000 1.00 15.06  ? 179 ILE D CD1 1 
ATOM   8001  N  N   A GLU D  1 180 ? -8.072  -3.270  -38.392 0.50 11.78  ? 180 GLU D N   1 
ATOM   8002  N  N   B GLU D  1 180 ? -8.296  -3.378  -38.712 0.50 14.11  ? 180 GLU D N   1 
ATOM   8003  C  CA  A GLU D  1 180 ? -7.518  -4.428  -37.627 0.50 13.21  ? 180 GLU D CA  1 
ATOM   8004  C  CA  B GLU D  1 180 ? -7.902  -4.416  -37.772 0.50 14.44  ? 180 GLU D CA  1 
ATOM   8005  C  C   A GLU D  1 180 ? -7.086  -5.610  -38.536 0.50 13.14  ? 180 GLU D C   1 
ATOM   8006  C  C   B GLU D  1 180 ? -7.198  -5.513  -38.477 0.50 12.58  ? 180 GLU D C   1 
ATOM   8007  O  O   A GLU D  1 180 ? -6.369  -6.519  -38.146 0.50 12.33  ? 180 GLU D O   1 
ATOM   8008  O  O   B GLU D  1 180 ? -6.353  -6.180  -37.861 0.50 13.60  ? 180 GLU D O   1 
ATOM   8009  C  CB  A GLU D  1 180 ? -8.592  -4.920  -36.664 0.50 15.08  ? 180 GLU D CB  1 
ATOM   8010  C  CB  B GLU D  1 180 ? -9.073  -4.980  -36.925 0.50 16.21  ? 180 GLU D CB  1 
ATOM   8011  C  CG  A GLU D  1 180 ? -8.148  -5.569  -35.400 0.50 20.41  ? 180 GLU D CG  1 
ATOM   8012  C  CG  B GLU D  1 180 ? -9.228  -4.166  -35.621 0.50 16.92  ? 180 GLU D CG  1 
ATOM   8013  C  CD  A GLU D  1 180 ? -9.343  -6.026  -34.600 0.50 18.43  ? 180 GLU D CD  1 
ATOM   8014  C  CD  B GLU D  1 180 ? -9.991  -4.916  -34.501 0.50 18.62  ? 180 GLU D CD  1 
ATOM   8015  O  OE1 A GLU D  1 180 ? -10.495 -5.540  -34.879 0.50 18.92  ? 180 GLU D OE1 1 
ATOM   8016  O  OE1 B GLU D  1 180 ? -9.425  -5.748  -33.724 0.50 20.45  ? 180 GLU D OE1 1 
ATOM   8017  O  OE2 A GLU D  1 180 ? -9.064  -6.793  -33.654 0.50 29.12  ? 180 GLU D OE2 1 
ATOM   8018  O  OE2 B GLU D  1 180 ? -11.170 -4.618  -34.356 0.50 32.51  ? 180 GLU D OE2 1 
ATOM   8019  N  N   . GLU D  1 181 ? -7.518  -5.648  -39.773 1.00 13.20  ? 181 GLU D N   1 
ATOM   8020  C  CA  . GLU D  1 181 ? -6.971  -6.652  -40.652 1.00 13.38  ? 181 GLU D CA  1 
ATOM   8021  C  C   . GLU D  1 181 ? -5.463  -6.462  -40.870 1.00 12.05  ? 181 GLU D C   1 
ATOM   8022  O  O   . GLU D  1 181 ? -4.839  -7.402  -41.365 1.00 13.30  ? 181 GLU D O   1 
ATOM   8023  C  CB  . GLU D  1 181 ? -7.613  -6.670  -42.034 1.00 15.76  ? 181 GLU D CB  1 
ATOM   8024  C  CG  . GLU D  1 181 ? -9.097  -7.000  -42.033 1.00 17.09  ? 181 GLU D CG  1 
ATOM   8025  C  CD  . GLU D  1 181 ? -9.786  -6.823  -43.409 1.00 21.60  ? 181 GLU D CD  1 
ATOM   8026  O  OE1 . GLU D  1 181 ? -9.090  -6.538  -44.469 1.00 23.58  ? 181 GLU D OE1 1 
ATOM   8027  O  OE2 . GLU D  1 181 ? -11.031 -6.942  -43.457 1.00 22.12  ? 181 GLU D OE2 1 
ATOM   8028  N  N   . LEU D  1 182 ? -4.917  -5.313  -40.553 1.00 11.48  ? 182 LEU D N   1 
ATOM   8029  C  CA  . LEU D  1 182 ? -3.504  -5.087  -40.681 1.00 11.77  ? 182 LEU D CA  1 
ATOM   8030  C  C   . LEU D  1 182 ? -2.700  -5.543  -39.488 1.00 10.61  ? 182 LEU D C   1 
ATOM   8031  O  O   . LEU D  1 182 ? -1.483  -5.561  -39.521 1.00 11.36  ? 182 LEU D O   1 
ATOM   8032  C  CB  . LEU D  1 182 ? -3.229  -3.579  -40.928 1.00 11.36  ? 182 LEU D CB  1 
ATOM   8033  C  CG  . LEU D  1 182 ? -3.958  -2.930  -42.111 1.00 10.42  ? 182 LEU D CG  1 
ATOM   8034  C  CD1 . LEU D  1 182 ? -3.608  -1.457  -42.189 1.00 12.91  ? 182 LEU D CD1 1 
ATOM   8035  C  CD2 . LEU D  1 182 ? -3.642  -3.621  -43.416 1.00 11.91  ? 182 LEU D CD2 1 
ATOM   8036  N  N   . LEU D  1 183 ? -3.410  -5.864  -38.374 1.00 11.78  ? 183 LEU D N   1 
ATOM   8037  C  CA  . LEU D  1 183 ? -2.772  -6.274  -37.153 1.00 11.85  ? 183 LEU D CA  1 
ATOM   8038  C  C   . LEU D  1 183 ? -2.455  -7.749  -37.163 1.00 11.02  ? 183 LEU D C   1 
ATOM   8039  O  O   . LEU D  1 183 ? -3.154  -8.514  -37.797 1.00 12.88  ? 183 LEU D O   1 
ATOM   8040  C  CB  . LEU D  1 183 ? -3.674  -5.938  -35.959 1.00 13.90  ? 183 LEU D CB  1 
ATOM   8041  C  CG  . LEU D  1 183 ? -4.096  -4.457  -35.805 1.00 13.76  ? 183 LEU D CG  1 
ATOM   8042  C  CD1 . LEU D  1 183 ? -4.817  -4.235  -34.508 1.00 18.75  ? 183 LEU D CD1 1 
ATOM   8043  C  CD2 . LEU D  1 183 ? -2.852  -3.544  -35.768 1.00 16.42  ? 183 LEU D CD2 1 
ATOM   8044  N  N   . PRO D  1 184 ? -1.456  -8.183  -36.376 1.00 10.87  ? 184 PRO D N   1 
ATOM   8045  C  CA  . PRO D  1 184 ? -1.082  -9.588  -36.312 1.00 12.69  ? 184 PRO D CA  1 
ATOM   8046  C  C   . PRO D  1 184 ? -1.933  -10.373 -35.376 1.00 15.18  ? 184 PRO D C   1 
ATOM   8047  O  O   . PRO D  1 184 ? -2.840  -9.858  -34.687 1.00 15.71  ? 184 PRO D O   1 
ATOM   8048  C  CB  . PRO D  1 184 ? 0.366   -9.468  -35.784 1.00 12.83  ? 184 PRO D CB  1 
ATOM   8049  C  CG  . PRO D  1 184 ? 0.314   -8.305  -34.856 1.00 12.55  ? 184 PRO D CG  1 
ATOM   8050  C  CD  . PRO D  1 184 ? -0.591  -7.345  -35.527 1.00 11.57  ? 184 PRO D CD  1 
ATOM   8051  N  N   . GLU D  1 185 ? -1.561  -11.669 -35.295 1.00 14.19  ? 185 GLU D N   1 
ATOM   8052  C  CA  . GLU D  1 185 ? -2.173  -12.542 -34.293 1.00 15.80  ? 185 GLU D CA  1 
ATOM   8053  C  C   . GLU D  1 185 ? -1.771  -12.165 -32.881 1.00 15.14  ? 185 GLU D C   1 
ATOM   8054  O  O   . GLU D  1 185 ? -0.656  -11.689 -32.662 1.00 16.73  ? 185 GLU D O   1 
ATOM   8055  C  CB  . GLU D  1 185 ? -1.734  -13.993 -34.523 1.00 18.34  ? 185 GLU D CB  1 
ATOM   8056  C  CG  . GLU D  1 185 ? -2.158  -14.478 -35.881 1.00 23.17  ? 185 GLU D CG  1 
ATOM   8057  C  CD  . GLU D  1 185 ? -1.850  -15.943 -36.170 1.00 46.01  ? 185 GLU D CD  1 
ATOM   8058  O  OE1 . GLU D  1 185 ? -0.804  -16.487 -35.728 1.00 43.39  ? 185 GLU D OE1 1 
ATOM   8059  O  OE2 . GLU D  1 185 ? -2.646  -16.560 -36.924 1.00 65.66  ? 185 GLU D OE2 1 
ATOM   8060  N  N   . ARG D  1 186 ? -2.733  -12.445 -31.970 1.00 15.66  ? 186 ARG D N   1 
ATOM   8061  C  CA  . ARG D  1 186 ? -2.425  -12.344 -30.506 1.00 15.65  ? 186 ARG D CA  1 
ATOM   8062  C  C   . ARG D  1 186 ? -1.936  -10.924 -30.220 1.00 15.54  ? 186 ARG D C   1 
ATOM   8063  O  O   . ARG D  1 186 ? -0.840  -10.721 -29.616 1.00 15.38  ? 186 ARG D O   1 
ATOM   8064  C  CB  . ARG D  1 186 ? -1.487  -13.452 -30.021 1.00 19.43  ? 186 ARG D CB  1 
ATOM   8065  C  CG  . ARG D  1 186 ? -2.144  -14.812 -30.139 1.00 25.28  ? 186 ARG D CG  1 
ATOM   8066  C  CD  . ARG D  1 186 ? -1.171  -15.978 -29.795 1.00 27.78  ? 186 ARG D CD  1 
ATOM   8067  N  NE  . ARG D  1 186 ? -0.063  -16.124 -30.795 1.00 27.83  ? 186 ARG D NE  1 
ATOM   8068  C  CZ  . ARG D  1 186 ? -0.226  -16.644 -32.017 1.00 34.04  ? 186 ARG D CZ  1 
ATOM   8069  N  NH1 . ARG D  1 186 ? -1.448  -17.079 -32.387 1.00 41.51  ? 186 ARG D NH1 1 
ATOM   8070  N  NH2 . ARG D  1 186 ? 0.819   -16.719 -32.872 1.00 43.03  ? 186 ARG D NH2 1 
ATOM   8071  N  N   . THR D  1 187 ? -2.772  -9.982  -30.564 1.00 14.66  ? 187 THR D N   1 
ATOM   8072  C  CA  . THR D  1 187 ? -2.437  -8.623  -30.215 1.00 13.87  ? 187 THR D CA  1 
ATOM   8073  C  C   . THR D  1 187 ? -2.283  -8.335  -28.727 1.00 14.09  ? 187 THR D C   1 
ATOM   8074  O  O   . THR D  1 187 ? -1.712  -7.336  -28.378 1.00 13.85  ? 187 THR D O   1 
ATOM   8075  C  CB  . THR D  1 187 ? -3.404  -7.629  -30.834 1.00 13.48  ? 187 THR D CB  1 
ATOM   8076  O  OG1 . THR D  1 187 ? -4.745  -7.933  -30.454 1.00 16.31  ? 187 THR D OG1 1 
ATOM   8077  C  CG2 . THR D  1 187 ? -3.304  -7.631  -32.318 1.00 15.84  ? 187 THR D CG2 1 
ATOM   8078  N  N   . ALA D  1 188 ? -2.800  -9.243  -27.810 1.00 14.75  ? 188 ALA D N   1 
ATOM   8079  C  CA  . ALA D  1 188 ? -2.549  -9.107  -26.394 1.00 16.22  ? 188 ALA D CA  1 
ATOM   8080  C  C   . ALA D  1 188 ? -1.077  -9.256  -26.033 1.00 13.35  ? 188 ALA D C   1 
ATOM   8081  O  O   . ALA D  1 188 ? -0.689  -8.798  -24.921 1.00 14.93  ? 188 ALA D O   1 
ATOM   8082  C  CB  . ALA D  1 188 ? -3.317  -10.181 -25.680 1.00 19.04  ? 188 ALA D CB  1 
ATOM   8083  N  N   A GLU D  1 189 ? -0.279  -9.736  -27.003 0.50 14.38  ? 189 GLU D N   1 
ATOM   8084  N  N   B GLU D  1 189 ? -0.224  -9.878  -26.895 0.50 13.98  ? 189 GLU D N   1 
ATOM   8085  C  CA  A GLU D  1 189 ? 1.143   -10.001 -26.826 0.50 13.56  ? 189 GLU D CA  1 
ATOM   8086  C  CA  B GLU D  1 189 ? 1.209   -9.962  -26.600 0.50 10.98  ? 189 GLU D CA  1 
ATOM   8087  C  C   A GLU D  1 189 ? 1.943   -8.826  -27.457 0.50 10.31  ? 189 GLU D C   1 
ATOM   8088  C  C   B GLU D  1 189 ? 1.941   -8.830  -27.361 0.50 9.81   ? 189 GLU D C   1 
ATOM   8089  O  O   A GLU D  1 189 ? 1.933   -8.737  -28.695 0.50 12.14  ? 189 GLU D O   1 
ATOM   8090  O  O   B GLU D  1 189 ? 1.941   -8.806  -28.564 0.50 11.53  ? 189 GLU D O   1 
ATOM   8091  C  CB  A GLU D  1 189 ? 1.471   -11.317 -27.541 0.50 12.34  ? 189 GLU D CB  1 
ATOM   8092  C  CB  B GLU D  1 189 ? 1.786   -11.329 -27.038 0.50 11.97  ? 189 GLU D CB  1 
ATOM   8093  C  CG  A GLU D  1 189 ? 0.617   -12.434 -26.923 0.50 16.11  ? 189 GLU D CG  1 
ATOM   8094  C  CG  B GLU D  1 189 ? 1.077   -12.459 -26.281 0.50 14.21  ? 189 GLU D CG  1 
ATOM   8095  C  CD  A GLU D  1 189 ? 1.191   -13.796 -27.149 0.50 19.40  ? 189 GLU D CD  1 
ATOM   8096  C  CD  B GLU D  1 189 ? 1.326   -13.818 -26.921 0.50 20.47  ? 189 GLU D CD  1 
ATOM   8097  O  OE1 A GLU D  1 189 ? 2.454   -13.965 -27.181 0.50 18.01  ? 189 GLU D OE1 1 
ATOM   8098  O  OE1 B GLU D  1 189 ? 2.014   -14.032 -28.002 0.50 25.03  ? 189 GLU D OE1 1 
ATOM   8099  O  OE2 A GLU D  1 189 ? 0.331   -14.745 -27.204 0.50 21.96  ? 189 GLU D OE2 1 
ATOM   8100  O  OE2 B GLU D  1 189 ? 0.776   -14.750 -26.281 0.50 21.60  ? 189 GLU D OE2 1 
ATOM   8101  N  N   . TYR D  1 190 ? 2.591   -7.992  -26.631 1.00 11.24  ? 190 TYR D N   1 
ATOM   8102  C  CA  . TYR D  1 190 ? 3.249   -6.844  -27.168 1.00 9.86   ? 190 TYR D CA  1 
ATOM   8103  C  C   . TYR D  1 190 ? 4.369   -6.383  -26.250 1.00 10.37  ? 190 TYR D C   1 
ATOM   8104  O  O   . TYR D  1 190 ? 4.420   -6.763  -25.084 1.00 11.44  ? 190 TYR D O   1 
ATOM   8105  C  CB  . TYR D  1 190 ? 2.218   -5.691  -27.439 1.00 11.24  ? 190 TYR D CB  1 
ATOM   8106  C  CG  . TYR D  1 190 ? 1.465   -5.247  -26.174 1.00 10.46  ? 190 TYR D CG  1 
ATOM   8107  C  CD1 . TYR D  1 190 ? 2.036   -4.380  -25.243 1.00 10.60  ? 190 TYR D CD1 1 
ATOM   8108  C  CD2 . TYR D  1 190 ? 0.139   -5.702  -25.983 1.00 12.25  ? 190 TYR D CD2 1 
ATOM   8109  C  CE1 . TYR D  1 190 ? 1.302   -3.941  -24.138 1.00 12.28  ? 190 TYR D CE1 1 
ATOM   8110  C  CE2 . TYR D  1 190 ? -0.580  -5.261  -24.854 1.00 11.99  ? 190 TYR D CE2 1 
ATOM   8111  C  CZ  . TYR D  1 190 ? 0.038   -4.404  -23.976 1.00 12.19  ? 190 TYR D CZ  1 
ATOM   8112  O  OH  . TYR D  1 190 ? -0.716  -3.942  -22.852 1.00 14.16  ? 190 TYR D OH  1 
ATOM   8113  N  N   . TYR D  1 191 ? 5.232   -5.576  -26.862 1.00 9.84   ? 191 TYR D N   1 
ATOM   8114  C  CA  . TYR D  1 191 ? 6.255   -4.828  -26.182 1.00 10.60  ? 191 TYR D CA  1 
ATOM   8115  C  C   . TYR D  1 191 ? 5.755   -3.400  -25.985 1.00 9.32   ? 191 TYR D C   1 
ATOM   8116  O  O   . TYR D  1 191 ? 5.118   -2.853  -26.889 1.00 10.50  ? 191 TYR D O   1 
ATOM   8117  C  CB  . TYR D  1 191 ? 7.524   -4.746  -27.063 1.00 10.26  ? 191 TYR D CB  1 
ATOM   8118  C  CG  . TYR D  1 191 ? 8.045   -6.065  -27.570 1.00 9.25   ? 191 TYR D CG  1 
ATOM   8119  C  CD1 . TYR D  1 191 ? 9.023   -6.754  -26.879 1.00 10.49  ? 191 TYR D CD1 1 
ATOM   8120  C  CD2 . TYR D  1 191 ? 7.652   -6.540  -28.800 1.00 9.53   ? 191 TYR D CD2 1 
ATOM   8121  C  CE1 . TYR D  1 191 ? 9.608   -7.909  -27.403 1.00 11.75  ? 191 TYR D CE1 1 
ATOM   8122  C  CE2 . TYR D  1 191 ? 8.206   -7.742  -29.373 1.00 10.80  ? 191 TYR D CE2 1 
ATOM   8123  C  CZ  . TYR D  1 191 ? 9.167   -8.409  -28.631 1.00 11.19  ? 191 TYR D CZ  1 
ATOM   8124  O  OH  . TYR D  1 191 ? 9.771   -9.525  -29.151 1.00 14.65  ? 191 TYR D OH  1 
ATOM   8125  N  N   . ARG D  1 192 ? 6.052   -2.789  -24.831 1.00 10.55  ? 192 ARG D N   1 
ATOM   8126  C  CA  . ARG D  1 192 ? 5.648   -1.400  -24.542 1.00 10.71  ? 192 ARG D CA  1 
ATOM   8127  C  C   . ARG D  1 192 ? 6.845   -0.613  -24.030 1.00 10.37  ? 192 ARG D C   1 
ATOM   8128  O  O   . ARG D  1 192 ? 7.547   -1.098  -23.141 1.00 10.90  ? 192 ARG D O   1 
ATOM   8129  C  CB  . ARG D  1 192 ? 4.525   -1.463  -23.553 1.00 13.13  ? 192 ARG D CB  1 
ATOM   8130  C  CG  . ARG D  1 192 ? 4.180   -0.232  -22.766 1.00 19.60  ? 192 ARG D CG  1 
ATOM   8131  C  CD  . ARG D  1 192 ? 3.467   0.634   -23.714 1.00 18.39  ? 192 ARG D CD  1 
ATOM   8132  N  NE  . ARG D  1 192 ? 2.372   0.010   -24.446 1.00 18.51  ? 192 ARG D NE  1 
ATOM   8133  C  CZ  . ARG D  1 192 ? 1.181   -0.254  -23.922 1.00 16.22  ? 192 ARG D CZ  1 
ATOM   8134  N  NH1 . ARG D  1 192 ? 0.941   0.026   -22.649 1.00 22.01  ? 192 ARG D NH1 1 
ATOM   8135  N  NH2 . ARG D  1 192 ? 0.237   -0.809  -24.668 1.00 16.00  ? 192 ARG D NH2 1 
ATOM   8136  N  N   . TYR D  1 193 ? 7.087   0.578   -24.535 1.00 10.50  ? 193 TYR D N   1 
ATOM   8137  C  CA  . TYR D  1 193 ? 8.103   1.430   -23.938 1.00 10.75  ? 193 TYR D CA  1 
ATOM   8138  C  C   . TYR D  1 193 ? 7.824   2.866   -24.277 1.00 10.39  ? 193 TYR D C   1 
ATOM   8139  O  O   . TYR D  1 193 ? 7.078   3.186   -25.194 1.00 11.40  ? 193 TYR D O   1 
ATOM   8140  C  CB  . TYR D  1 193 ? 9.496   0.985   -24.381 1.00 10.95  ? 193 TYR D CB  1 
ATOM   8141  C  CG  . TYR D  1 193 ? 9.864   1.382   -25.812 1.00 9.72   ? 193 TYR D CG  1 
ATOM   8142  C  CD1 . TYR D  1 193 ? 9.418   0.608   -26.904 1.00 10.02  ? 193 TYR D CD1 1 
ATOM   8143  C  CD2 . TYR D  1 193 ? 10.625  2.504   -26.055 1.00 10.45  ? 193 TYR D CD2 1 
ATOM   8144  C  CE1 . TYR D  1 193 ? 9.709   0.969   -28.236 1.00 9.60   ? 193 TYR D CE1 1 
ATOM   8145  C  CE2 . TYR D  1 193 ? 10.920  2.884   -27.369 1.00 9.55   ? 193 TYR D CE2 1 
ATOM   8146  C  CZ  . TYR D  1 193 ? 10.463  2.113   -28.415 1.00 9.48   ? 193 TYR D CZ  1 
ATOM   8147  O  OH  . TYR D  1 193 ? 10.801  2.531   -29.689 1.00 9.15   ? 193 TYR D OH  1 
ATOM   8148  N  N   A ARG D  1 194 ? 8.474   3.748   -23.558 0.50 12.32  ? 194 ARG D N   1 
ATOM   8149  N  N   B ARG D  1 194 ? 8.465   3.747   -23.551 0.50 12.33  ? 194 ARG D N   1 
ATOM   8150  C  CA  A ARG D  1 194 ? 8.399   5.191   -23.800 0.50 14.13  ? 194 ARG D CA  1 
ATOM   8151  C  CA  B ARG D  1 194 ? 8.355   5.206   -23.779 0.50 14.11  ? 194 ARG D CA  1 
ATOM   8152  C  C   A ARG D  1 194 ? 9.483   5.626   -24.756 0.50 11.33  ? 194 ARG D C   1 
ATOM   8153  C  C   B ARG D  1 194 ? 9.476   5.627   -24.730 0.50 11.31  ? 194 ARG D C   1 
ATOM   8154  O  O   A ARG D  1 194 ? 10.667  5.394   -24.510 0.50 14.03  ? 194 ARG D O   1 
ATOM   8155  O  O   B ARG D  1 194 ? 10.657  5.410   -24.499 0.50 14.03  ? 194 ARG D O   1 
ATOM   8156  C  CB  A ARG D  1 194 ? 8.532   5.975   -22.490 0.50 18.54  ? 194 ARG D CB  1 
ATOM   8157  C  CB  B ARG D  1 194 ? 8.442   5.955   -22.437 0.50 18.67  ? 194 ARG D CB  1 
ATOM   8158  C  CG  A ARG D  1 194 ? 7.403   5.627   -21.572 0.50 28.93  ? 194 ARG D CG  1 
ATOM   8159  C  CG  B ARG D  1 194 ? 7.163   5.752   -21.574 0.50 30.19  ? 194 ARG D CG  1 
ATOM   8160  C  CD  A ARG D  1 194 ? 6.841   6.834   -20.842 0.50 34.24  ? 194 ARG D CD  1 
ATOM   8161  C  CD  B ARG D  1 194 ? 7.221   6.394   -20.192 0.50 37.10  ? 194 ARG D CD  1 
ATOM   8162  N  NE  A ARG D  1 194 ? 5.499   6.562   -20.332 0.50 50.60  ? 194 ARG D NE  1 
ATOM   8163  N  NE  B ARG D  1 194 ? 7.098   7.854   -20.191 0.50 47.50  ? 194 ARG D NE  1 
ATOM   8164  C  CZ  A ARG D  1 194 ? 4.498   7.434   -20.353 0.50 81.35  ? 194 ARG D CZ  1 
ATOM   8165  C  CZ  B ARG D  1 194 ? 6.013   8.530   -20.549 0.50 83.46  ? 194 ARG D CZ  1 
ATOM   8166  N  NH1 A ARG D  1 194 ? 4.683   8.647   -20.855 0.50 79.50  ? 194 ARG D NH1 1 
ATOM   8167  N  NH1 B ARG D  1 194 ? 4.921   7.897   -20.960 0.50 88.30  ? 194 ARG D NH1 1 
ATOM   8168  N  NH2 A ARG D  1 194 ? 3.310   7.095   -19.871 0.50 114.37 ? 194 ARG D NH2 1 
ATOM   8169  N  NH2 B ARG D  1 194 ? 6.012   9.853   -20.504 0.50 100.96 ? 194 ARG D NH2 1 
ATOM   8170  N  N   . GLY D  1 195 ? 9.086   6.263   -25.849 1.00 10.67  ? 195 GLY D N   1 
ATOM   8171  C  CA  . GLY D  1 195 ? 10.087  6.707   -26.812 1.00 10.64  ? 195 GLY D CA  1 
ATOM   8172  C  C   . GLY D  1 195 ? 9.594   7.929   -27.548 1.00 10.27  ? 195 GLY D C   1 
ATOM   8173  O  O   . GLY D  1 195 ? 8.993   8.833   -26.960 1.00 10.49  ? 195 GLY D O   1 
ATOM   8174  N  N   . SER D  1 196 ? 9.959   7.999   -28.803 1.00 9.02   ? 196 SER D N   1 
ATOM   8175  C  CA  . SER D  1 196 ? 9.898   9.207   -29.588 1.00 9.01   ? 196 SER D CA  1 
ATOM   8176  C  C   . SER D  1 196 ? 9.298   8.962   -30.923 1.00 8.69   ? 196 SER D C   1 
ATOM   8177  O  O   . SER D  1 196 ? 9.189   7.820   -31.420 1.00 8.73   ? 196 SER D O   1 
ATOM   8178  C  CB  . SER D  1 196 ? 11.285  9.857   -29.732 1.00 9.73   ? 196 SER D CB  1 
ATOM   8179  O  OG  . SER D  1 196 ? 12.049  9.136   -30.698 1.00 9.32   ? 196 SER D OG  1 
ATOM   8180  N  N   A LEU D  1 197 ? 9.025   10.049  -31.630 0.50 8.89   ? 197 LEU D N   1 
ATOM   8181  N  N   B LEU D  1 197 ? 9.025   10.049  -31.632 0.50 8.84   ? 197 LEU D N   1 
ATOM   8182  C  CA  A LEU D  1 197 ? 8.852   9.942   -33.067 0.50 8.69   ? 197 LEU D CA  1 
ATOM   8183  C  CA  B LEU D  1 197 ? 8.845   9.940   -33.068 0.50 8.58   ? 197 LEU D CA  1 
ATOM   8184  C  C   A LEU D  1 197 ? 10.166  9.471   -33.671 0.50 7.87   ? 197 LEU D C   1 
ATOM   8185  C  C   B LEU D  1 197 ? 10.164  9.471   -33.671 0.50 7.88   ? 197 LEU D C   1 
ATOM   8186  O  O   A LEU D  1 197 ? 11.235  9.846   -33.210 0.50 8.46   ? 197 LEU D O   1 
ATOM   8187  O  O   B LEU D  1 197 ? 11.235  9.847   -33.209 0.50 8.44   ? 197 LEU D O   1 
ATOM   8188  C  CB  A LEU D  1 197 ? 8.588   11.355  -33.668 0.50 8.67   ? 197 LEU D CB  1 
ATOM   8189  C  CB  B LEU D  1 197 ? 8.575   11.358  -33.671 0.50 9.65   ? 197 LEU D CB  1 
ATOM   8190  C  CG  A LEU D  1 197 ? 7.161   11.876  -33.512 0.50 11.60  ? 197 LEU D CG  1 
ATOM   8191  C  CG  B LEU D  1 197 ? 7.273   12.024  -33.259 0.50 10.06  ? 197 LEU D CG  1 
ATOM   8192  C  CD1 A LEU D  1 197 ? 6.987   12.485  -32.115 0.50 9.89   ? 197 LEU D CD1 1 
ATOM   8193  C  CD1 B LEU D  1 197 ? 7.274   13.465  -33.812 0.50 13.25  ? 197 LEU D CD1 1 
ATOM   8194  C  CD2 A LEU D  1 197 ? 6.901   12.885  -34.665 0.50 13.90  ? 197 LEU D CD2 1 
ATOM   8195  C  CD2 B LEU D  1 197 ? 6.118   11.252  -33.800 0.50 12.38  ? 197 LEU D CD2 1 
ATOM   8196  N  N   . THR D  1 198 ? 10.087  8.610   -34.693 1.00 8.01   ? 198 THR D N   1 
ATOM   8197  C  CA  . THR D  1 198 ? 11.307  8.095   -35.337 1.00 7.46   ? 198 THR D CA  1 
ATOM   8198  C  C   . THR D  1 198 ? 11.737  8.968   -36.458 1.00 7.65   ? 198 THR D C   1 
ATOM   8199  O  O   . THR D  1 198 ? 12.719  8.659   -37.143 1.00 8.19   ? 198 THR D O   1 
ATOM   8200  C  CB  . THR D  1 198 ? 11.119  6.699   -35.833 1.00 7.42   ? 198 THR D CB  1 
ATOM   8201  O  OG1 . THR D  1 198 ? 10.181  6.711   -36.889 1.00 7.56   ? 198 THR D OG1 1 
ATOM   8202  C  CG2 . THR D  1 198 ? 10.691  5.700   -34.737 1.00 8.64   ? 198 THR D CG2 1 
ATOM   8203  N  N   . THR D  1 199 ? 11.025  10.089  -36.684 1.00 8.44   ? 199 THR D N   1 
ATOM   8204  C  CA  . THR D  1 199 ? 11.322  11.045  -37.738 1.00 10.26  ? 199 THR D CA  1 
ATOM   8205  C  C   . THR D  1 199 ? 11.480  12.402  -37.048 1.00 8.86   ? 199 THR D C   1 
ATOM   8206  O  O   . THR D  1 199 ? 10.922  12.580  -35.951 1.00 9.66   ? 199 THR D O   1 
ATOM   8207  C  CB  . THR D  1 199 ? 10.173  11.130  -38.754 1.00 14.04  ? 199 THR D CB  1 
ATOM   8208  O  OG1 . THR D  1 199 ? 8.944   11.394  -38.065 1.00 19.74  ? 199 THR D OG1 1 
ATOM   8209  C  CG2 . THR D  1 199 ? 10.042  9.822   -39.518 1.00 14.79  ? 199 THR D CG2 1 
ATOM   8210  N  N   . PRO D  1 200 ? 12.183  13.375  -37.640 1.00 8.36   ? 200 PRO D N   1 
ATOM   8211  C  CA  . PRO D  1 200 ? 12.092  14.746  -37.152 1.00 8.75   ? 200 PRO D CA  1 
ATOM   8212  C  C   . PRO D  1 200 ? 10.656  15.151  -37.027 1.00 8.71   ? 200 PRO D C   1 
ATOM   8213  O  O   . PRO D  1 200 ? 9.839   14.839  -37.883 1.00 10.75  ? 200 PRO D O   1 
ATOM   8214  C  CB  . PRO D  1 200 ? 12.796  15.514  -38.271 1.00 9.44   ? 200 PRO D CB  1 
ATOM   8215  C  CG  . PRO D  1 200 ? 13.854  14.533  -38.733 1.00 10.14  ? 200 PRO D CG  1 
ATOM   8216  C  CD  . PRO D  1 200 ? 13.079  13.237  -38.802 1.00 9.11   ? 200 PRO D CD  1 
ATOM   8217  N  N   A PRO D  1 201 ? 10.276  15.863  -35.945 0.50 9.12   ? 201 PRO D N   1 
ATOM   8218  N  N   B PRO D  1 201 ? 10.318  15.875  -35.947 0.50 9.54   ? 201 PRO D N   1 
ATOM   8219  C  CA  A PRO D  1 201 ? 11.203  16.456  -34.960 0.50 8.92   ? 201 PRO D CA  1 
ATOM   8220  C  CA  B PRO D  1 201 ? 11.271  16.462  -34.978 0.50 9.57   ? 201 PRO D CA  1 
ATOM   8221  C  C   A PRO D  1 201 ? 11.611  15.560  -33.798 0.50 9.14   ? 201 PRO D C   1 
ATOM   8222  C  C   B PRO D  1 201 ? 11.674  15.554  -33.804 0.50 9.53   ? 201 PRO D C   1 
ATOM   8223  O  O   A PRO D  1 201 ? 12.226  16.059  -32.868 0.50 10.42  ? 201 PRO D O   1 
ATOM   8224  O  O   B PRO D  1 201 ? 12.333  16.041  -32.870 0.50 10.39  ? 201 PRO D O   1 
ATOM   8225  C  CB  A PRO D  1 201 ? 10.434  17.696  -34.391 0.50 11.29  ? 201 PRO D CB  1 
ATOM   8226  C  CB  B PRO D  1 201 ? 10.516  17.711  -34.448 0.50 11.63  ? 201 PRO D CB  1 
ATOM   8227  C  CG  A PRO D  1 201 ? 9.329   17.885  -35.310 0.50 13.10  ? 201 PRO D CG  1 
ATOM   8228  C  CG  B PRO D  1 201 ? 9.091   17.293  -34.588 0.50 15.32  ? 201 PRO D CG  1 
ATOM   8229  C  CD  A PRO D  1 201 ? 8.968   16.517  -35.866 0.50 11.73  ? 201 PRO D CD  1 
ATOM   8230  C  CD  B PRO D  1 201 ? 8.971   16.430  -35.792 0.50 11.77  ? 201 PRO D CD  1 
ATOM   8231  N  N   . CYS D  1 202 ? 11.331  14.257  -33.838 1.00 8.44   ? 202 CYS D N   1 
ATOM   8232  C  CA  . CYS D  1 202 ? 11.897  13.284  -32.888 1.00 8.77   ? 202 CYS D CA  1 
ATOM   8233  C  C   . CYS D  1 202 ? 11.369  13.530  -31.452 1.00 8.82   ? 202 CYS D C   1 
ATOM   8234  O  O   . CYS D  1 202 ? 12.041  13.149  -30.518 1.00 10.01  ? 202 CYS D O   1 
ATOM   8235  C  CB  . CYS D  1 202 ? 13.411  13.236  -32.870 1.00 9.60   ? 202 CYS D CB  1 
ATOM   8236  S  SG  . CYS D  1 202 ? 14.151  12.861  -34.469 1.00 9.40   ? 202 CYS D SG  1 
ATOM   8237  N  N   A ASN D  1 203 ? 10.241  14.190  -31.282 0.50 9.23   ? 203 ASN D N   1 
ATOM   8238  N  N   B ASN D  1 203 ? 10.183  14.178  -31.335 0.50 10.59  ? 203 ASN D N   1 
ATOM   8239  C  CA  A ASN D  1 203 ? 9.777   14.522  -29.935 0.50 8.25   ? 203 ASN D CA  1 
ATOM   8240  C  CA  B ASN D  1 203 ? 9.662   14.452  -29.988 0.50 13.11  ? 203 ASN D CA  1 
ATOM   8241  C  C   A ASN D  1 203 ? 9.592   13.272  -29.077 0.50 9.19   ? 203 ASN D C   1 
ATOM   8242  C  C   B ASN D  1 203 ? 9.655   13.202  -29.101 0.50 9.92   ? 203 ASN D C   1 
ATOM   8243  O  O   A ASN D  1 203 ? 9.030   12.281  -29.541 0.50 7.94   ? 203 ASN D O   1 
ATOM   8244  O  O   B ASN D  1 203 ? 9.266   12.130  -29.568 0.50 7.58   ? 203 ASN D O   1 
ATOM   8245  C  CB  A ASN D  1 203 ? 8.483   15.337  -29.995 0.50 7.98   ? 203 ASN D CB  1 
ATOM   8246  C  CB  B ASN D  1 203 ? 8.250   15.030  -30.063 0.50 13.13  ? 203 ASN D CB  1 
ATOM   8247  C  CG  A ASN D  1 203 ? 8.584   16.519  -30.939 0.50 7.57   ? 203 ASN D CG  1 
ATOM   8248  C  CG  B ASN D  1 203 ? 8.151   16.211  -31.006 0.50 16.97  ? 203 ASN D CG  1 
ATOM   8249  O  OD1 A ASN D  1 203 ? 8.487   16.365  -32.157 0.50 9.50   ? 203 ASN D OD1 1 
ATOM   8250  O  OD1 B ASN D  1 203 ? 9.108   16.966  -31.173 0.50 16.94  ? 203 ASN D OD1 1 
ATOM   8251  N  ND2 A ASN D  1 203 ? 8.781   17.708  -30.381 0.50 11.69  ? 203 ASN D ND2 1 
ATOM   8252  N  ND2 B ASN D  1 203 ? 6.989   16.377  -31.629 0.50 19.36  ? 203 ASN D ND2 1 
ATOM   8253  N  N   . PRO D  1 204 ? 10.069  13.309  -27.833 1.00 10.54  ? 204 PRO D N   1 
ATOM   8254  C  CA  . PRO D  1 204 ? 9.976   12.101  -26.962 1.00 10.51  ? 204 PRO D CA  1 
ATOM   8255  C  C   . PRO D  1 204 ? 8.621   11.958  -26.281 1.00 10.29  ? 204 PRO D C   1 
ATOM   8256  O  O   . PRO D  1 204 ? 8.472   11.950  -25.074 1.00 13.55  ? 204 PRO D O   1 
ATOM   8257  C  CB  . PRO D  1 204 ? 11.107  12.397  -25.972 1.00 12.72  ? 204 PRO D CB  1 
ATOM   8258  C  CG  . PRO D  1 204 ? 11.143  13.911  -25.833 1.00 13.91  ? 204 PRO D CG  1 
ATOM   8259  C  CD  . PRO D  1 204 ? 10.898  14.381  -27.233 1.00 12.40  ? 204 PRO D CD  1 
ATOM   8260  N  N   . THR D  1 205 ? 7.590   11.862  -27.110 1.00 9.98   ? 205 THR D N   1 
ATOM   8261  C  CA  . THR D  1 205 ? 6.231   12.005  -26.700 1.00 10.40  ? 205 THR D CA  1 
ATOM   8262  C  C   . THR D  1 205 ? 5.404   10.795  -27.088 1.00 9.74   ? 205 THR D C   1 
ATOM   8263  O  O   . THR D  1 205 ? 4.152   10.826  -27.057 1.00 10.77  ? 205 THR D O   1 
ATOM   8264  C  CB  . THR D  1 205 ? 5.646   13.272  -27.293 1.00 10.63  ? 205 THR D CB  1 
ATOM   8265  O  OG1 . THR D  1 205 ? 5.789   13.085  -28.704 1.00 11.43  ? 205 THR D OG1 1 
ATOM   8266  C  CG2 . THR D  1 205 ? 6.305   14.534  -26.783 1.00 12.00  ? 205 THR D CG2 1 
ATOM   8267  N  N   . VAL D  1 206 ? 6.065   9.668   -27.466 1.00 10.06  ? 206 VAL D N   1 
ATOM   8268  C  CA  . VAL D  1 206 ? 5.333   8.532   -27.960 1.00 9.45   ? 206 VAL D CA  1 
ATOM   8269  C  C   . VAL D  1 206 ? 5.363   7.338   -27.004 1.00 10.72  ? 206 VAL D C   1 
ATOM   8270  O  O   . VAL D  1 206 ? 6.451   6.885   -26.600 1.00 11.38  ? 206 VAL D O   1 
ATOM   8271  C  CB  . VAL D  1 206 ? 5.928   8.025   -29.339 1.00 9.95   ? 206 VAL D CB  1 
ATOM   8272  C  CG1 . VAL D  1 206 ? 5.159   6.786   -29.783 1.00 9.81   ? 206 VAL D CG1 1 
ATOM   8273  C  CG2 . VAL D  1 206 ? 5.858   9.148   -30.379 1.00 10.47  ? 206 VAL D CG2 1 
ATOM   8274  N  N   . LEU D  1 207 ? 4.172   6.868   -26.686 1.00 9.74   ? 207 LEU D N   1 
ATOM   8275  C  CA  . LEU D  1 207 ? 4.087   5.545   -26.013 1.00 10.78  ? 207 LEU D CA  1 
ATOM   8276  C  C   . LEU D  1 207 ? 3.998   4.480   -27.103 1.00 10.31  ? 207 LEU D C   1 
ATOM   8277  O  O   . LEU D  1 207 ? 3.065   4.482   -27.867 1.00 10.30  ? 207 LEU D O   1 
ATOM   8278  C  CB  . LEU D  1 207 ? 2.815   5.537   -25.183 1.00 14.10  ? 207 LEU D CB  1 
ATOM   8279  C  CG  . LEU D  1 207 ? 2.781   4.305   -24.287 1.00 16.73  ? 207 LEU D CG  1 
ATOM   8280  C  CD1 . LEU D  1 207 ? 3.918   4.230   -23.237 1.00 18.22  ? 207 LEU D CD1 1 
ATOM   8281  C  CD2 . LEU D  1 207 ? 1.458   4.317   -23.613 1.00 26.81  ? 207 LEU D CD2 1 
ATOM   8282  N  N   . TRP D  1 208 ? 5.029   3.686   -27.187 1.00 9.81   ? 208 TRP D N   1 
ATOM   8283  C  CA  . TRP D  1 208 ? 5.107   2.670   -28.260 1.00 9.76   ? 208 TRP D CA  1 
ATOM   8284  C  C   . TRP D  1 208 ? 4.545   1.354   -27.803 1.00 9.29   ? 208 TRP D C   1 
ATOM   8285  O  O   . TRP D  1 208 ? 4.781   0.901   -26.690 1.00 11.49  ? 208 TRP D O   1 
ATOM   8286  C  CB  . TRP D  1 208 ? 6.591   2.448   -28.620 1.00 10.06  ? 208 TRP D CB  1 
ATOM   8287  C  CG  . TRP D  1 208 ? 7.151   3.477   -29.523 1.00 9.30   ? 208 TRP D CG  1 
ATOM   8288  C  CD1 . TRP D  1 208 ? 7.823   4.636   -29.191 1.00 9.56   ? 208 TRP D CD1 1 
ATOM   8289  C  CD2 . TRP D  1 208 ? 6.925   3.506   -30.957 1.00 9.15   ? 208 TRP D CD2 1 
ATOM   8290  N  NE1 . TRP D  1 208 ? 8.044   5.354   -30.332 1.00 8.86   ? 208 TRP D NE1 1 
ATOM   8291  C  CE2 . TRP D  1 208 ? 7.521   4.707   -31.420 1.00 8.44   ? 208 TRP D CE2 1 
ATOM   8292  C  CE3 . TRP D  1 208 ? 6.285   2.666   -31.864 1.00 9.17   ? 208 TRP D CE3 1 
ATOM   8293  C  CZ2 . TRP D  1 208 ? 7.453   5.082   -32.767 1.00 8.49   ? 208 TRP D CZ2 1 
ATOM   8294  C  CZ3 . TRP D  1 208 ? 6.269   3.029   -33.227 1.00 8.99   ? 208 TRP D CZ3 1 
ATOM   8295  C  CH2 . TRP D  1 208 ? 6.855   4.220   -33.647 1.00 9.12   ? 208 TRP D CH2 1 
ATOM   8296  N  N   . THR D  1 209 ? 3.775   0.731   -28.689 1.00 8.84   ? 209 THR D N   1 
ATOM   8297  C  CA  . THR D  1 209 ? 3.348   -0.626  -28.537 1.00 9.60   ? 209 THR D CA  1 
ATOM   8298  C  C   . THR D  1 209 ? 3.743   -1.396  -29.829 1.00 8.27   ? 209 THR D C   1 
ATOM   8299  O  O   . THR D  1 209 ? 3.289   -1.021  -30.882 1.00 9.63   ? 209 THR D O   1 
ATOM   8300  C  CB  . THR D  1 209 ? 1.810   -0.700  -28.381 1.00 10.30  ? 209 THR D CB  1 
ATOM   8301  O  OG1 . THR D  1 209 ? 1.419   0.031   -27.217 1.00 11.38  ? 209 THR D OG1 1 
ATOM   8302  C  CG2 . THR D  1 209 ? 1.356   -2.155  -28.242 1.00 12.83  ? 209 THR D CG2 1 
ATOM   8303  N  N   . VAL D  1 210 ? 4.631   -2.361  -29.664 1.00 8.72   ? 210 VAL D N   1 
ATOM   8304  C  CA  . VAL D  1 210 ? 5.113   -3.131  -30.814 1.00 8.41   ? 210 VAL D CA  1 
ATOM   8305  C  C   . VAL D  1 210 ? 4.574   -4.517  -30.647 1.00 8.95   ? 210 VAL D C   1 
ATOM   8306  O  O   . VAL D  1 210 ? 4.827   -5.185  -29.637 1.00 9.41   ? 210 VAL D O   1 
ATOM   8307  C  CB  . VAL D  1 210 ? 6.648   -3.191  -30.904 1.00 8.88   ? 210 VAL D CB  1 
ATOM   8308  C  CG1 . VAL D  1 210 ? 7.096   -3.982  -32.132 1.00 10.34  ? 210 VAL D CG1 1 
ATOM   8309  C  CG2 . VAL D  1 210 ? 7.263   -1.813  -30.902 1.00 9.89   ? 210 VAL D CG2 1 
ATOM   8310  N  N   . PHE D  1 211 ? 3.724   -4.974  -31.516 1.00 8.11   ? 211 PHE D N   1 
ATOM   8311  C  CA  . PHE D  1 211 ? 3.147   -6.290  -31.346 1.00 9.04   ? 211 PHE D CA  1 
ATOM   8312  C  C   . PHE D  1 211 ? 4.219   -7.356  -31.425 1.00 9.63   ? 211 PHE D C   1 
ATOM   8313  O  O   . PHE D  1 211 ? 5.150   -7.272  -32.239 1.00 9.95   ? 211 PHE D O   1 
ATOM   8314  C  CB  . PHE D  1 211 ? 2.048   -6.534  -32.272 1.00 10.11  ? 211 PHE D CB  1 
ATOM   8315  C  CG  . PHE D  1 211 ? 0.877   -5.633  -32.047 1.00 10.12  ? 211 PHE D CG  1 
ATOM   8316  C  CD1 . PHE D  1 211 ? 0.055   -5.795  -30.899 1.00 10.36  ? 211 PHE D CD1 1 
ATOM   8317  C  CD2 . PHE D  1 211 ? 0.540   -4.580  -32.950 1.00 10.73  ? 211 PHE D CD2 1 
ATOM   8318  C  CE1 . PHE D  1 211 ? -0.989  -4.895  -30.663 1.00 12.25  ? 211 PHE D CE1 1 
ATOM   8319  C  CE2 . PHE D  1 211 ? -0.482  -3.706  -32.680 1.00 12.63  ? 211 PHE D CE2 1 
ATOM   8320  C  CZ  . PHE D  1 211 ? -1.241  -3.844  -31.548 1.00 13.02  ? 211 PHE D CZ  1 
ATOM   8321  N  N   . ARG D  1 212 ? 4.086   -8.405  -30.606 1.00 10.23  ? 212 ARG D N   1 
ATOM   8322  C  CA  . ARG D  1 212 ? 5.056   -9.487  -30.665 1.00 10.30  ? 212 ARG D CA  1 
ATOM   8323  C  C   . ARG D  1 212 ? 5.135   -10.201 -31.982 1.00 9.62   ? 212 ARG D C   1 
ATOM   8324  O  O   . ARG D  1 212 ? 6.244   -10.552 -32.447 1.00 12.35  ? 212 ARG D O   1 
ATOM   8325  C  CB  . ARG D  1 212 ? 4.693   -10.482 -29.546 1.00 11.95  ? 212 ARG D CB  1 
ATOM   8326  C  CG  . ARG D  1 212 ? 5.777   -11.584 -29.398 1.00 13.05  ? 212 ARG D CG  1 
ATOM   8327  C  CD  . ARG D  1 212 ? 5.261   -12.659 -28.413 1.00 14.18  ? 212 ARG D CD  1 
ATOM   8328  N  NE  . ARG D  1 212 ? 6.376   -13.525 -28.054 1.00 16.63  ? 212 ARG D NE  1 
ATOM   8329  C  CZ  . ARG D  1 212 ? 6.289   -14.550 -27.211 1.00 19.36  ? 212 ARG D CZ  1 
ATOM   8330  N  NH1 . ARG D  1 212 ? 5.123   -14.834 -26.647 1.00 22.22  ? 212 ARG D NH1 1 
ATOM   8331  N  NH2 . ARG D  1 212 ? 7.359   -15.289 -26.954 1.00 23.13  ? 212 ARG D NH2 1 
ATOM   8332  N  N   . ASN D  1 213 ? 4.002   -10.470 -32.601 1.00 10.16  ? 213 ASN D N   1 
ATOM   8333  C  CA  . ASN D  1 213 ? 3.967   -11.271 -33.783 1.00 10.55  ? 213 ASN D CA  1 
ATOM   8334  C  C   . ASN D  1 213 ? 3.959   -10.408 -35.048 1.00 10.66  ? 213 ASN D C   1 
ATOM   8335  O  O   . ASN D  1 213 ? 3.254   -9.430  -35.087 1.00 11.09  ? 213 ASN D O   1 
ATOM   8336  C  CB  . ASN D  1 213 ? 2.707   -12.138 -33.777 1.00 13.26  ? 213 ASN D CB  1 
ATOM   8337  C  CG  . ASN D  1 213 ? 2.764   -13.101 -32.637 1.00 15.49  ? 213 ASN D CG  1 
ATOM   8338  O  OD1 . ASN D  1 213 ? 3.764   -13.767 -32.460 1.00 25.23  ? 213 ASN D OD1 1 
ATOM   8339  N  ND2 . ASN D  1 213 ? 1.779   -13.115 -31.787 1.00 22.30  ? 213 ASN D ND2 1 
ATOM   8340  N  N   . PRO D  1 214 ? 4.723   -10.785 -36.076 1.00 10.36  ? 214 PRO D N   1 
ATOM   8341  C  CA  . PRO D  1 214 ? 4.699   -10.079 -37.332 1.00 9.76   ? 214 PRO D CA  1 
ATOM   8342  C  C   . PRO D  1 214 ? 3.510   -10.485 -38.165 1.00 9.32   ? 214 PRO D C   1 
ATOM   8343  O  O   . PRO D  1 214 ? 2.888   -11.551 -37.939 1.00 11.98  ? 214 PRO D O   1 
ATOM   8344  C  CB  . PRO D  1 214 ? 6.000   -10.489 -38.025 1.00 11.89  ? 214 PRO D CB  1 
ATOM   8345  C  CG  . PRO D  1 214 ? 6.219   -11.908 -37.512 1.00 14.52  ? 214 PRO D CG  1 
ATOM   8346  C  CD  . PRO D  1 214 ? 5.747   -11.877 -36.074 1.00 12.74  ? 214 PRO D CD  1 
ATOM   8347  N  N   . VAL D  1 215 ? 3.226   -9.706  -39.211 1.00 9.80   ? 215 VAL D N   1 
ATOM   8348  C  CA  . VAL D  1 215 ? 2.395   -10.114 -40.319 1.00 9.12   ? 215 VAL D CA  1 
ATOM   8349  C  C   . VAL D  1 215 ? 3.275   -10.430 -41.509 1.00 9.23   ? 215 VAL D C   1 
ATOM   8350  O  O   . VAL D  1 215 ? 4.466   -10.108 -41.476 1.00 9.90   ? 215 VAL D O   1 
ATOM   8351  C  CB  . VAL D  1 215 ? 1.340   -9.050  -40.698 1.00 9.47   ? 215 VAL D CB  1 
ATOM   8352  C  CG1 . VAL D  1 215 ? 0.445   -8.737  -39.501 1.00 11.88  ? 215 VAL D CG1 1 
ATOM   8353  C  CG2 . VAL D  1 215 ? 2.015   -7.781  -41.207 1.00 10.24  ? 215 VAL D CG2 1 
ATOM   8354  N  N   . GLN D  1 216 ? 2.701   -11.006 -42.567 1.00 9.07   ? 216 GLN D N   1 
ATOM   8355  C  CA  . GLN D  1 216 ? 3.415   -11.260 -43.793 1.00 9.72   ? 216 GLN D CA  1 
ATOM   8356  C  C   . GLN D  1 216 ? 2.807   -10.466 -44.919 1.00 9.07   ? 216 GLN D C   1 
ATOM   8357  O  O   . GLN D  1 216 ? 1.585   -10.361 -45.022 1.00 10.47  ? 216 GLN D O   1 
ATOM   8358  C  CB  . GLN D  1 216 ? 3.339   -12.746 -44.190 1.00 10.52  ? 216 GLN D CB  1 
ATOM   8359  C  CG  . GLN D  1 216 ? 4.110   -13.583 -43.214 1.00 11.94  ? 216 GLN D CG  1 
ATOM   8360  C  CD  . GLN D  1 216 ? 4.103   -15.064 -43.589 1.00 13.12  ? 216 GLN D CD  1 
ATOM   8361  O  OE1 . GLN D  1 216 ? 3.561   -15.526 -44.602 1.00 12.20  ? 216 GLN D OE1 1 
ATOM   8362  N  NE2 . GLN D  1 216 ? 4.835   -15.819 -42.804 1.00 22.64  ? 216 GLN D NE2 1 
ATOM   8363  N  N   . ILE D  1 217 ? 3.674   -10.006 -45.854 1.00 8.91   ? 217 ILE D N   1 
ATOM   8364  C  CA  . ILE D  1 217 ? 3.283   -9.551  -47.178 1.00 8.90   ? 217 ILE D CA  1 
ATOM   8365  C  C   . ILE D  1 217 ? 4.227   -10.226 -48.176 1.00 8.37   ? 217 ILE D C   1 
ATOM   8366  O  O   . ILE D  1 217 ? 5.292   -10.708 -47.780 1.00 8.89   ? 217 ILE D O   1 
ATOM   8367  C  CB  . ILE D  1 217 ? 3.281   -8.010  -47.343 1.00 9.34   ? 217 ILE D CB  1 
ATOM   8368  C  CG1 . ILE D  1 217 ? 4.717   -7.478  -47.283 1.00 9.94   ? 217 ILE D CG1 1 
ATOM   8369  C  CG2 . ILE D  1 217 ? 2.411   -7.381  -46.257 1.00 10.20  ? 217 ILE D CG2 1 
ATOM   8370  C  CD1 . ILE D  1 217 ? 4.755   -5.943  -47.524 1.00 12.02  ? 217 ILE D CD1 1 
ATOM   8371  N  N   . SER D  1 218 ? 3.826   -10.313 -49.428 1.00 8.98   ? 218 SER D N   1 
ATOM   8372  C  CA  . SER D  1 218 ? 4.671   -11.045 -50.349 1.00 9.08   ? 218 SER D CA  1 
ATOM   8373  C  C   . SER D  1 218 ? 5.877   -10.278 -50.836 1.00 9.02   ? 218 SER D C   1 
ATOM   8374  O  O   . SER D  1 218 ? 5.921   -9.046  -50.760 1.00 10.06  ? 218 SER D O   1 
ATOM   8375  C  CB  . SER D  1 218 ? 3.883   -11.556 -51.514 1.00 9.99   ? 218 SER D CB  1 
ATOM   8376  O  OG  . SER D  1 218 ? 3.483   -10.458 -52.340 1.00 10.22  ? 218 SER D OG  1 
ATOM   8377  N  N   . GLN D  1 219 ? 6.815   -11.010 -51.429 1.00 9.55   ? 219 GLN D N   1 
ATOM   8378  C  CA  . GLN D  1 219 ? 7.942   -10.390 -52.075 1.00 11.26  ? 219 GLN D CA  1 
ATOM   8379  C  C   . GLN D  1 219 ? 7.450   -9.383  -53.147 1.00 9.94   ? 219 GLN D C   1 
ATOM   8380  O  O   . GLN D  1 219 ? 8.034   -8.308  -53.287 1.00 10.97  ? 219 GLN D O   1 
ATOM   8381  C  CB  . GLN D  1 219 ? 8.830   -11.449 -52.693 1.00 16.47  ? 219 GLN D CB  1 
ATOM   8382  C  CG  . GLN D  1 219 ? 10.155  -10.785 -53.169 1.00 21.29  ? 219 GLN D CG  1 
ATOM   8383  C  CD  . GLN D  1 219 ? 10.119  -10.138 -54.472 1.00 21.50  ? 219 GLN D CD  1 
ATOM   8384  O  OE1 . GLN D  1 219 ? 9.323   -10.536 -55.345 1.00 25.63  ? 219 GLN D OE1 1 
ATOM   8385  N  NE2 . GLN D  1 219 ? 10.946  -9.104  -54.645 1.00 29.51  ? 219 GLN D NE2 1 
ATOM   8386  N  N   . GLU D  1 220 ? 6.412   -9.756  -53.892 1.00 10.55  ? 220 GLU D N   1 
ATOM   8387  C  CA  . GLU D  1 220 ? 5.943   -8.842  -54.941 1.00 11.33  ? 220 GLU D CA  1 
ATOM   8388  C  C   . GLU D  1 220 ? 5.361   -7.636  -54.330 1.00 10.00  ? 220 GLU D C   1 
ATOM   8389  O  O   . GLU D  1 220 ? 5.553   -6.514  -54.869 1.00 10.37  ? 220 GLU D O   1 
ATOM   8390  C  CB  . GLU D  1 220 ? 4.883   -9.556  -55.811 1.00 13.76  ? 220 GLU D CB  1 
ATOM   8391  C  CG  . GLU D  1 220 ? 5.559   -10.651 -56.672 1.00 14.49  ? 220 GLU D CG  1 
ATOM   8392  C  CD  . GLU D  1 220 ? 5.731   -11.982 -55.971 1.00 17.98  ? 220 GLU D CD  1 
ATOM   8393  O  OE1 . GLU D  1 220 ? 5.360   -12.096 -54.785 1.00 16.93  ? 220 GLU D OE1 1 
ATOM   8394  O  OE2 . GLU D  1 220 ? 6.246   -12.919 -56.619 1.00 32.31  ? 220 GLU D OE2 1 
ATOM   8395  N  N   . GLN D  1 221 ? 4.640   -7.735  -53.208 1.00 9.81   ? 221 GLN D N   1 
ATOM   8396  C  CA  . GLN D  1 221 ? 4.130   -6.522  -52.558 1.00 9.96   ? 221 GLN D CA  1 
ATOM   8397  C  C   . GLN D  1 221 ? 5.233   -5.668  -52.046 1.00 9.70   ? 221 GLN D C   1 
ATOM   8398  O  O   . GLN D  1 221 ? 5.210   -4.435  -52.188 1.00 10.07  ? 221 GLN D O   1 
ATOM   8399  C  CB  . GLN D  1 221 ? 3.204   -6.977  -51.405 1.00 10.05  ? 221 GLN D CB  1 
ATOM   8400  C  CG  . GLN D  1 221 ? 1.904   -7.571  -51.872 1.00 10.58  ? 221 GLN D CG  1 
ATOM   8401  C  CD  . GLN D  1 221 ? 0.991   -7.949  -50.764 1.00 9.53   ? 221 GLN D CD  1 
ATOM   8402  O  OE1 . GLN D  1 221 ? 1.306   -8.877  -49.966 1.00 9.95   ? 221 GLN D OE1 1 
ATOM   8403  N  NE2 . GLN D  1 221 ? -0.136  -7.256  -50.593 1.00 10.92  ? 221 GLN D NE2 1 
ATOM   8404  N  N   . LEU D  1 222 ? 6.267   -6.285  -51.442 1.00 9.17   ? 222 LEU D N   1 
ATOM   8405  C  CA  . LEU D  1 222 ? 7.411   -5.523  -50.967 1.00 9.32   ? 222 LEU D CA  1 
ATOM   8406  C  C   . LEU D  1 222 ? 8.129   -4.820  -52.092 1.00 8.81   ? 222 LEU D C   1 
ATOM   8407  O  O   . LEU D  1 222 ? 8.500   -3.670  -51.981 1.00 9.46   ? 222 LEU D O   1 
ATOM   8408  C  CB  . LEU D  1 222 ? 8.367   -6.425  -50.202 1.00 10.45  ? 222 LEU D CB  1 
ATOM   8409  C  CG  . LEU D  1 222 ? 8.022   -6.711  -48.774 1.00 11.73  ? 222 LEU D CG  1 
ATOM   8410  C  CD1 . LEU D  1 222 ? 8.694   -8.005  -48.297 1.00 13.19  ? 222 LEU D CD1 1 
ATOM   8411  C  CD2 . LEU D  1 222 ? 8.433   -5.442  -47.930 1.00 13.07  ? 222 LEU D CD2 1 
ATOM   8412  N  N   . LEU D  1 223 ? 8.354   -5.518  -53.211 1.00 9.49   ? 223 LEU D N   1 
ATOM   8413  C  CA  . LEU D  1 223 ? 9.063   -4.884  -54.327 1.00 10.31  ? 223 LEU D CA  1 
ATOM   8414  C  C   . LEU D  1 223 ? 8.245   -3.707  -54.867 1.00 9.77   ? 223 LEU D C   1 
ATOM   8415  O  O   . LEU D  1 223 ? 8.789   -2.657  -55.210 1.00 11.09  ? 223 LEU D O   1 
ATOM   8416  C  CB  . LEU D  1 223 ? 9.286   -5.935  -55.444 1.00 11.15  ? 223 LEU D CB  1 
ATOM   8417  C  CG  . LEU D  1 223 ? 10.031  -5.431  -56.665 1.00 12.04  ? 223 LEU D CG  1 
ATOM   8418  C  CD1 . LEU D  1 223 ? 11.432  -4.951  -56.297 1.00 14.70  ? 223 LEU D CD1 1 
ATOM   8419  C  CD2 . LEU D  1 223 ? 10.124  -6.514  -57.708 1.00 13.00  ? 223 LEU D CD2 1 
ATOM   8420  N  N   . ALA D  1 224 ? 6.929   -3.878  -54.966 1.00 10.91  ? 224 ALA D N   1 
ATOM   8421  C  CA  . ALA D  1 224 ? 6.075   -2.793  -55.434 1.00 11.91  ? 224 ALA D CA  1 
ATOM   8422  C  C   . ALA D  1 224 ? 6.232   -1.586  -54.497 1.00 10.84  ? 224 ALA D C   1 
ATOM   8423  O  O   . ALA D  1 224 ? 6.389   -0.460  -54.969 1.00 12.99  ? 224 ALA D O   1 
ATOM   8424  C  CB  . ALA D  1 224 ? 4.622   -3.270  -55.606 1.00 14.60  ? 224 ALA D CB  1 
ATOM   8425  N  N   . LEU D  1 225 ? 6.132   -1.821  -53.190 1.00 11.07  ? 225 LEU D N   1 
ATOM   8426  C  CA  . LEU D  1 225 ? 6.263   -0.750  -52.212 1.00 10.32  ? 225 LEU D CA  1 
ATOM   8427  C  C   . LEU D  1 225 ? 7.605   -0.048  -52.337 1.00 10.15  ? 225 LEU D C   1 
ATOM   8428  O  O   . LEU D  1 225 ? 7.689   1.174   -52.281 1.00 11.88  ? 225 LEU D O   1 
ATOM   8429  C  CB  . LEU D  1 225 ? 6.074   -1.341  -50.805 1.00 10.74  ? 225 LEU D CB  1 
ATOM   8430  C  CG  . LEU D  1 225 ? 6.249   -0.391  -49.648 1.00 11.84  ? 225 LEU D CG  1 
ATOM   8431  C  CD1 . LEU D  1 225 ? 5.281   0.776   -49.685 1.00 12.23  ? 225 LEU D CD1 1 
ATOM   8432  C  CD2 . LEU D  1 225 ? 6.186   -1.138  -48.337 1.00 12.12  ? 225 LEU D CD2 1 
ATOM   8433  N  N   . GLU D  1 226 ? 8.668   -0.879  -52.465 1.00 9.93   ? 226 GLU D N   1 
ATOM   8434  C  CA  . GLU D  1 226 ? 10.031  -0.388  -52.538 1.00 10.41  ? 226 GLU D CA  1 
ATOM   8435  C  C   . GLU D  1 226 ? 10.361  0.387   -53.807 1.00 10.60  ? 226 GLU D C   1 
ATOM   8436  O  O   . GLU D  1 226 ? 11.394  1.064   -53.830 1.00 15.44  ? 226 GLU D O   1 
ATOM   8437  C  CB  . GLU D  1 226 ? 11.004  -1.555  -52.377 1.00 10.01  ? 226 GLU D CB  1 
ATOM   8438  C  CG  . GLU D  1 226 ? 11.053  -2.176  -50.982 1.00 10.10  ? 226 GLU D CG  1 
ATOM   8439  C  CD  . GLU D  1 226 ? 11.450  -3.639  -51.009 1.00 10.68  ? 226 GLU D CD  1 
ATOM   8440  O  OE1 . GLU D  1 226 ? 11.736  -4.154  -52.109 1.00 12.14  ? 226 GLU D OE1 1 
ATOM   8441  O  OE2 . GLU D  1 226 ? 11.482  -4.272  -49.932 1.00 13.40  ? 226 GLU D OE2 1 
ATOM   8442  N  N   . THR D  1 227 ? 9.546   0.268   -54.804 1.00 9.76   ? 227 THR D N   1 
ATOM   8443  C  CA  . THR D  1 227 ? 9.824   0.891   -56.116 1.00 11.13  ? 227 THR D CA  1 
ATOM   8444  C  C   . THR D  1 227 ? 8.739   1.873   -56.537 1.00 11.50  ? 227 THR D C   1 
ATOM   8445  O  O   . THR D  1 227 ? 8.898   2.480   -57.568 1.00 14.81  ? 227 THR D O   1 
ATOM   8446  C  CB  . THR D  1 227 ? 10.044  -0.129  -57.221 1.00 12.25  ? 227 THR D CB  1 
ATOM   8447  O  OG1 . THR D  1 227 ? 8.849   -0.914  -57.376 1.00 13.18  ? 227 THR D OG1 1 
ATOM   8448  C  CG2 . THR D  1 227 ? 11.217  -1.074  -56.901 1.00 13.92  ? 227 THR D CG2 1 
ATOM   8449  N  N   . ALA D  1 228 ? 7.676   2.054   -55.735 1.00 11.44  ? 228 ALA D N   1 
ATOM   8450  C  CA  . ALA D  1 228 ? 6.517   2.844   -56.175 1.00 12.75  ? 228 ALA D CA  1 
ATOM   8451  C  C   . ALA D  1 228 ? 6.707   4.353   -55.943 1.00 13.45  ? 228 ALA D C   1 
ATOM   8452  O  O   . ALA D  1 228 ? 6.024   5.122   -56.600 1.00 17.41  ? 228 ALA D O   1 
ATOM   8453  C  CB  . ALA D  1 228 ? 5.266   2.433   -55.439 1.00 15.02  ? 228 ALA D CB  1 
ATOM   8454  N  N   . LEU D  1 229 ? 7.529   4.760   -54.994 1.00 11.23  ? 229 LEU D N   1 
ATOM   8455  C  CA  . LEU D  1 229 ? 7.377   6.132   -54.463 1.00 12.17  ? 229 LEU D CA  1 
ATOM   8456  C  C   . LEU D  1 229 ? 8.711   6.896   -54.551 1.00 12.07  ? 229 LEU D C   1 
ATOM   8457  O  O   . LEU D  1 229 ? 9.784   6.318   -54.477 1.00 12.07  ? 229 LEU D O   1 
ATOM   8458  C  CB  . LEU D  1 229 ? 6.898   6.060   -52.990 1.00 12.84  ? 229 LEU D CB  1 
ATOM   8459  C  CG  . LEU D  1 229 ? 5.596   5.330   -52.758 1.00 11.93  ? 229 LEU D CG  1 
ATOM   8460  C  CD1 . LEU D  1 229 ? 5.377   5.101   -51.278 1.00 15.98  ? 229 LEU D CD1 1 
ATOM   8461  C  CD2 . LEU D  1 229 ? 4.443   5.916   -53.499 1.00 17.75  ? 229 LEU D CD2 1 
ATOM   8462  N  N   . TYR D  1 230 ? 8.559   8.218   -54.648 1.00 13.10  ? 230 TYR D N   1 
ATOM   8463  C  CA  . TYR D  1 230 ? 9.652   9.167   -54.622 1.00 12.93  ? 230 TYR D CA  1 
ATOM   8464  C  C   . TYR D  1 230 ? 9.412   10.181  -53.511 1.00 12.99  ? 230 TYR D C   1 
ATOM   8465  O  O   . TYR D  1 230 ? 8.294   10.540  -53.171 1.00 13.86  ? 230 TYR D O   1 
ATOM   8466  C  CB  . TYR D  1 230 ? 9.685   9.891   -55.963 1.00 14.00  ? 230 TYR D CB  1 
ATOM   8467  C  CG  . TYR D  1 230 ? 10.193  9.077   -57.058 1.00 14.46  ? 230 TYR D CG  1 
ATOM   8468  C  CD1 . TYR D  1 230 ? 9.353   8.149   -57.665 1.00 21.14  ? 230 TYR D CD1 1 
ATOM   8469  C  CD2 . TYR D  1 230 ? 11.519  9.120   -57.425 1.00 16.38  ? 230 TYR D CD2 1 
ATOM   8470  C  CE1 . TYR D  1 230 ? 9.799   7.290   -58.648 1.00 26.73  ? 230 TYR D CE1 1 
ATOM   8471  C  CE2 . TYR D  1 230 ? 12.033  8.243   -58.434 1.00 18.91  ? 230 TYR D CE2 1 
ATOM   8472  C  CZ  . TYR D  1 230 ? 11.143  7.370   -59.063 1.00 27.66  ? 230 TYR D CZ  1 
ATOM   8473  O  OH  . TYR D  1 230 ? 11.550  6.497   -60.040 1.00 35.94  ? 230 TYR D OH  1 
ATOM   8474  N  N   . CYS D  1 231 ? 10.522  10.641  -52.965 1.00 13.24  ? 231 CYS D N   1 
ATOM   8475  C  CA  . CYS D  1 231 ? 10.498  11.694  -51.946 1.00 14.13  ? 231 CYS D CA  1 
ATOM   8476  C  C   . CYS D  1 231 ? 10.251  13.065  -52.520 1.00 13.42  ? 231 CYS D C   1 
ATOM   8477  O  O   . CYS D  1 231 ? 9.896   13.999  -51.811 1.00 15.53  ? 231 CYS D O   1 
ATOM   8478  C  CB  . CYS D  1 231 ? 11.831  11.723  -51.242 1.00 16.71  ? 231 CYS D CB  1 
ATOM   8479  S  SG  . CYS D  1 231 ? 12.363  10.202  -50.389 1.00 16.59  ? 231 CYS D SG  1 
ATOM   8480  N  N   . THR D  1 232 ? 10.566  13.178  -53.826 1.00 13.07  ? 232 THR D N   1 
ATOM   8481  C  CA  . THR D  1 232 ? 10.623  14.466  -54.494 1.00 12.16  ? 232 THR D CA  1 
ATOM   8482  C  C   . THR D  1 232 ? 9.332   14.772  -55.256 1.00 11.35  ? 232 THR D C   1 
ATOM   8483  O  O   . THR D  1 232 ? 8.529   13.870  -55.559 1.00 11.65  ? 232 THR D O   1 
ATOM   8484  C  CB  . THR D  1 232 ? 11.846  14.436  -55.423 1.00 12.74  ? 232 THR D CB  1 
ATOM   8485  O  OG1 . THR D  1 232 ? 11.947  13.175  -56.039 1.00 12.53  ? 232 THR D OG1 1 
ATOM   8486  C  CG2 . THR D  1 232 ? 13.129  14.709  -54.595 1.00 15.90  ? 232 THR D CG2 1 
ATOM   8487  N  N   A HIS D  1 233 ? 9.133   16.060  -55.570 0.50 12.51  ? 233 HIS D N   1 
ATOM   8488  N  N   B HIS D  1 233 ? 9.124   16.059  -55.564 0.50 12.52  ? 233 HIS D N   1 
ATOM   8489  C  CA  A HIS D  1 233 ? 8.040   16.422  -56.404 0.50 12.85  ? 233 HIS D CA  1 
ATOM   8490  C  CA  B HIS D  1 233 ? 8.017   16.464  -56.396 0.50 13.05  ? 233 HIS D CA  1 
ATOM   8491  C  C   A HIS D  1 233 ? 8.254   15.918  -57.777 0.50 12.84  ? 233 HIS D C   1 
ATOM   8492  C  C   B HIS D  1 233 ? 8.243   15.944  -57.768 0.50 12.86  ? 233 HIS D C   1 
ATOM   8493  O  O   A HIS D  1 233 ? 9.421   15.704  -58.260 0.50 13.06  ? 233 HIS D O   1 
ATOM   8494  O  O   B HIS D  1 233 ? 9.399   15.735  -58.211 0.50 13.24  ? 233 HIS D O   1 
ATOM   8495  C  CB  A HIS D  1 233 ? 7.949   17.951  -56.436 0.50 15.75  ? 233 HIS D CB  1 
ATOM   8496  C  CB  B HIS D  1 233 ? 7.889   18.029  -56.433 0.50 17.63  ? 233 HIS D CB  1 
ATOM   8497  C  CG  A HIS D  1 233 ? 7.432   18.539  -55.147 0.50 17.59  ? 233 HIS D CG  1 
ATOM   8498  C  CG  B HIS D  1 233 ? 6.755   18.557  -57.340 0.50 23.39  ? 233 HIS D CG  1 
ATOM   8499  N  ND1 A HIS D  1 233 ? 8.101   19.492  -54.462 0.50 27.12  ? 233 HIS D ND1 1 
ATOM   8500  N  ND1 B HIS D  1 233 ? 6.847   18.564  -58.696 0.50 31.78  ? 233 HIS D ND1 1 
ATOM   8501  C  CD2 A HIS D  1 233 ? 6.281   18.277  -54.407 0.50 20.21  ? 233 HIS D CD2 1 
ATOM   8502  C  CD2 B HIS D  1 233 ? 5.479   19.097  -57.039 0.50 29.77  ? 233 HIS D CD2 1 
ATOM   8503  C  CE1 A HIS D  1 233 ? 7.419   19.830  -53.345 0.50 35.41  ? 233 HIS D CE1 1 
ATOM   8504  C  CE1 B HIS D  1 233 ? 5.718   19.012  -59.241 0.50 31.75  ? 233 HIS D CE1 1 
ATOM   8505  N  NE2 A HIS D  1 233 ? 6.315   19.077  -53.300 0.50 29.35  ? 233 HIS D NE2 1 
ATOM   8506  N  NE2 B HIS D  1 233 ? 4.880   19.380  -58.224 0.50 41.66  ? 233 HIS D NE2 1 
ATOM   8507  N  N   . MET D  1 234 ? 7.168   15.749  -58.505 1.00 12.82  ? 234 MET D N   1 
ATOM   8508  C  CA  . MET D  1 234 ? 7.246   15.216  -59.839 1.00 13.99  ? 234 MET D CA  1 
ATOM   8509  C  C   . MET D  1 234 ? 8.214   15.918  -60.777 1.00 15.29  ? 234 MET D C   1 
ATOM   8510  O  O   . MET D  1 234 ? 8.896   15.257  -61.571 1.00 17.87  ? 234 MET D O   1 
ATOM   8511  C  CB  . MET D  1 234 ? 5.847   15.154  -60.403 1.00 15.78  ? 234 MET D CB  1 
ATOM   8512  C  CG  . MET D  1 234 ? 5.757   14.487  -61.735 1.00 18.07  ? 234 MET D CG  1 
ATOM   8513  S  SD  . MET D  1 234 ? 4.013   14.461  -62.240 1.00 27.63  ? 234 MET D SD  1 
ATOM   8514  C  CE  . MET D  1 234 ? 4.281   13.392  -63.651 1.00 27.48  ? 234 MET D CE  1 
ATOM   8515  N  N   A ASP D  1 235 ? 8.249   17.240  -60.585 0.50 19.53  ? 235 ASP D N   1 
ATOM   8516  N  N   B ASP D  1 235 ? 8.345   17.236  -60.750 0.50 15.24  ? 235 ASP D N   1 
ATOM   8517  C  CA  A ASP D  1 235 ? 9.027   18.154  -61.409 0.50 19.38  ? 235 ASP D CA  1 
ATOM   8518  C  CA  B ASP D  1 235 ? 9.294   17.802  -61.716 0.50 16.56  ? 235 ASP D CA  1 
ATOM   8519  C  C   A ASP D  1 235 ? 10.410  18.484  -60.855 0.50 20.17  ? 235 ASP D C   1 
ATOM   8520  C  C   B ASP D  1 235 ? 10.634  18.168  -61.115 0.50 16.08  ? 235 ASP D C   1 
ATOM   8521  O  O   A ASP D  1 235 ? 11.016  19.447  -61.343 0.50 22.71  ? 235 ASP D O   1 
ATOM   8522  O  O   B ASP D  1 235 ? 11.406  18.880  -61.732 0.50 14.53  ? 235 ASP D O   1 
ATOM   8523  C  CB  A ASP D  1 235 ? 8.237   19.447  -61.672 0.50 16.59  ? 235 ASP D CB  1 
ATOM   8524  C  CB  B ASP D  1 235 ? 8.693   18.939  -62.563 0.50 20.28  ? 235 ASP D CB  1 
ATOM   8525  C  CG  A ASP D  1 235 ? 8.248   20.383  -60.503 0.50 21.02  ? 235 ASP D CG  1 
ATOM   8526  C  CG  B ASP D  1 235 ? 7.279   18.671  -62.951 0.50 28.77  ? 235 ASP D CG  1 
ATOM   8527  O  OD1 A ASP D  1 235 ? 8.669   20.013  -59.379 0.50 23.18  ? 235 ASP D OD1 1 
ATOM   8528  O  OD1 B ASP D  1 235 ? 7.015   17.733  -63.752 0.50 36.45  ? 235 ASP D OD1 1 
ATOM   8529  O  OD2 A ASP D  1 235 ? 7.738   21.490  -60.672 0.50 27.82  ? 235 ASP D OD2 1 
ATOM   8530  O  OD2 B ASP D  1 235 ? 6.429   19.416  -62.438 0.50 37.70  ? 235 ASP D OD2 1 
ATOM   8531  N  N   . ASP D  1 236 ? 10.943  17.675  -59.933 1.00 16.13  ? 236 ASP D N   1 
ATOM   8532  C  CA  . ASP D  1 236 ? 12.247  17.909  -59.397 1.00 17.83  ? 236 ASP D CA  1 
ATOM   8533  C  C   . ASP D  1 236 ? 13.319  17.392  -60.365 1.00 19.97  ? 236 ASP D C   1 
ATOM   8534  O  O   . ASP D  1 236 ? 13.256  16.218  -60.749 1.00 19.94  ? 236 ASP D O   1 
ATOM   8535  C  CB  . ASP D  1 236 ? 12.385  17.184  -58.053 1.00 19.02  ? 236 ASP D CB  1 
ATOM   8536  C  CG  . ASP D  1 236 ? 13.550  17.693  -57.263 1.00 18.02  ? 236 ASP D CG  1 
ATOM   8537  O  OD1 . ASP D  1 236 ? 14.646  17.853  -57.834 1.00 19.79  ? 236 ASP D OD1 1 
ATOM   8538  O  OD2 . ASP D  1 236 ? 13.407  17.891  -56.056 1.00 21.80  ? 236 ASP D OD2 1 
ATOM   8539  N  N   . PRO D  1 237 ? 14.303  18.221  -60.741 1.00 21.14  ? 237 PRO D N   1 
ATOM   8540  C  CA  . PRO D  1 237 ? 15.376  17.713  -61.616 1.00 24.61  ? 237 PRO D CA  1 
ATOM   8541  C  C   . PRO D  1 237 ? 16.347  16.753  -60.942 1.00 23.93  ? 237 PRO D C   1 
ATOM   8542  O  O   . PRO D  1 237 ? 17.147  16.118  -61.633 1.00 26.43  ? 237 PRO D O   1 
ATOM   8543  C  CB  . PRO D  1 237 ? 16.113  18.973  -62.033 1.00 23.78  ? 237 PRO D CB  1 
ATOM   8544  C  CG  . PRO D  1 237 ? 15.832  19.944  -60.930 1.00 29.70  ? 237 PRO D CG  1 
ATOM   8545  C  CD  . PRO D  1 237 ? 14.450  19.664  -60.452 1.00 22.16  ? 237 PRO D CD  1 
ATOM   8546  N  N   . SER D  1 238 ? 16.216  16.559  -59.626 1.00 21.07  ? 238 SER D N   1 
ATOM   8547  C  CA  . SER D  1 238 ? 17.086  15.607  -58.898 1.00 20.95  ? 238 SER D CA  1 
ATOM   8548  C  C   . SER D  1 238 ? 16.171  14.669  -58.119 1.00 17.12  ? 238 SER D C   1 
ATOM   8549  O  O   . SER D  1 238 ? 16.056  14.736  -56.888 1.00 18.15  ? 238 SER D O   1 
ATOM   8550  C  CB  . SER D  1 238 ? 18.073  16.263  -57.891 1.00 27.01  ? 238 SER D CB  1 
ATOM   8551  O  OG  . SER D  1 238 ? 19.023  17.040  -58.585 1.00 34.32  ? 238 SER D OG  1 
ATOM   8552  N  N   . PRO D  1 239 ? 15.526  13.744  -58.813 1.00 17.00  ? 239 PRO D N   1 
ATOM   8553  C  CA  . PRO D  1 239 ? 14.581  12.858  -58.097 1.00 15.93  ? 239 PRO D CA  1 
ATOM   8554  C  C   . PRO D  1 239 ? 15.242  11.987  -57.113 1.00 14.64  ? 239 PRO D C   1 
ATOM   8555  O  O   . PRO D  1 239 ? 16.386  11.583  -57.245 1.00 16.46  ? 239 PRO D O   1 
ATOM   8556  C  CB  . PRO D  1 239 ? 13.984  11.981  -59.205 1.00 16.96  ? 239 PRO D CB  1 
ATOM   8557  C  CG  . PRO D  1 239 ? 14.557  12.449  -60.504 1.00 27.56  ? 239 PRO D CG  1 
ATOM   8558  C  CD  . PRO D  1 239 ? 15.585  13.496  -60.269 1.00 19.43  ? 239 PRO D CD  1 
ATOM   8559  N  N   . ARG D  1 240 ? 14.516  11.646  -56.037 1.00 13.17  ? 240 ARG D N   1 
ATOM   8560  C  CA  . ARG D  1 240 ? 15.073  10.730  -55.018 1.00 13.87  ? 240 ARG D CA  1 
ATOM   8561  C  C   . ARG D  1 240 ? 13.995  9.685   -54.725 1.00 15.46  ? 240 ARG D C   1 
ATOM   8562  O  O   . ARG D  1 240 ? 12.848  10.034  -54.383 1.00 14.49  ? 240 ARG D O   1 
ATOM   8563  C  CB  . ARG D  1 240 ? 15.392  11.489  -53.749 1.00 15.99  ? 240 ARG D CB  1 
ATOM   8564  C  CG  . ARG D  1 240 ? 16.554  12.493  -53.937 1.00 17.89  ? 240 ARG D CG  1 
ATOM   8565  C  CD  . ARG D  1 240 ? 16.919  13.218  -52.661 1.00 21.87  ? 240 ARG D CD  1 
ATOM   8566  N  NE  . ARG D  1 240 ? 15.848  14.189  -52.320 1.00 21.58  ? 240 ARG D NE  1 
ATOM   8567  C  CZ  . ARG D  1 240 ? 14.925  14.077  -51.355 1.00 20.54  ? 240 ARG D CZ  1 
ATOM   8568  N  NH1 . ARG D  1 240 ? 14.875  13.011  -50.562 1.00 19.92  ? 240 ARG D NH1 1 
ATOM   8569  N  NH2 . ARG D  1 240 ? 14.025  15.048  -51.182 1.00 28.09  ? 240 ARG D NH2 1 
ATOM   8570  N  N   . GLU D  1 241 ? 14.374  8.414   -54.868 1.00 14.19  ? 241 GLU D N   1 
ATOM   8571  C  CA  . GLU D  1 241 ? 13.431  7.332   -54.559 1.00 14.19  ? 241 GLU D CA  1 
ATOM   8572  C  C   . GLU D  1 241 ? 13.168  7.276   -53.065 1.00 12.78  ? 241 GLU D C   1 
ATOM   8573  O  O   . GLU D  1 241 ? 14.082  7.451   -52.196 1.00 14.26  ? 241 GLU D O   1 
ATOM   8574  C  CB  . GLU D  1 241 ? 14.088  5.997   -54.960 1.00 17.82  ? 241 GLU D CB  1 
ATOM   8575  C  CG  . GLU D  1 241 ? 14.186  5.862   -56.486 1.00 20.08  ? 241 GLU D CG  1 
ATOM   8576  C  CD  . GLU D  1 241 ? 15.050  4.731   -56.906 1.00 30.14  ? 241 GLU D CD  1 
ATOM   8577  O  OE1 . GLU D  1 241 ? 16.263  4.801   -56.703 1.00 40.35  ? 241 GLU D OE1 1 
ATOM   8578  O  OE2 . GLU D  1 241 ? 14.479  3.756   -57.345 1.00 46.08  ? 241 GLU D OE2 1 
ATOM   8579  N  N   . MET D  1 242 ? 11.966  6.876   -52.701 1.00 12.29  ? 242 MET D N   1 
ATOM   8580  C  CA  . MET D  1 242 ? 11.593  6.706   -51.284 1.00 11.49  ? 242 MET D CA  1 
ATOM   8581  C  C   . MET D  1 242 ? 11.915  5.267   -50.919 1.00 10.29  ? 242 MET D C   1 
ATOM   8582  O  O   . MET D  1 242 ? 11.096  4.347   -51.107 1.00 11.37  ? 242 MET D O   1 
ATOM   8583  C  CB  . MET D  1 242 ? 10.146  7.048   -51.099 1.00 12.31  ? 242 MET D CB  1 
ATOM   8584  C  CG  . MET D  1 242 ? 9.786   7.070   -49.605 1.00 12.93  ? 242 MET D CG  1 
ATOM   8585  S  SD  . MET D  1 242 ? 8.087   7.432   -49.305 1.00 12.30  ? 242 MET D SD  1 
ATOM   8586  C  CE  . MET D  1 242 ? 8.003   9.137   -49.894 1.00 15.05  ? 242 MET D CE  1 
ATOM   8587  N  N   . ILE D  1 243 ? 13.143  5.049   -50.452 1.00 10.00  ? 243 ILE D N   1 
ATOM   8588  C  CA  . ILE D  1 243 ? 13.706  3.763   -50.086 1.00 9.65   ? 243 ILE D CA  1 
ATOM   8589  C  C   . ILE D  1 243 ? 14.455  3.919   -48.795 1.00 8.21   ? 243 ILE D C   1 
ATOM   8590  O  O   . ILE D  1 243 ? 14.908  5.024   -48.451 1.00 8.80   ? 243 ILE D O   1 
ATOM   8591  C  CB  . ILE D  1 243 ? 14.616  3.171   -51.175 1.00 11.17  ? 243 ILE D CB  1 
ATOM   8592  C  CG1 . ILE D  1 243 ? 15.736  4.175   -51.565 1.00 13.01  ? 243 ILE D CG1 1 
ATOM   8593  C  CG2 . ILE D  1 243 ? 13.785  2.692   -52.377 1.00 13.76  ? 243 ILE D CG2 1 
ATOM   8594  C  CD1 . ILE D  1 243 ? 16.787  3.583   -52.485 1.00 16.59  ? 243 ILE D CD1 1 
ATOM   8595  N  N   . ASN D  1 244 ? 14.603  2.820   -48.066 1.00 7.40   ? 244 ASN D N   1 
ATOM   8596  C  CA  . ASN D  1 244 ? 15.407  2.825   -46.859 1.00 7.90   ? 244 ASN D CA  1 
ATOM   8597  C  C   . ASN D  1 244 ? 14.990  3.939   -45.901 1.00 7.62   ? 244 ASN D C   1 
ATOM   8598  O  O   . ASN D  1 244 ? 15.824  4.590   -45.286 1.00 8.19   ? 244 ASN D O   1 
ATOM   8599  C  CB  . ASN D  1 244 ? 16.910  2.915   -47.191 1.00 8.86   ? 244 ASN D CB  1 
ATOM   8600  C  CG  . ASN D  1 244 ? 17.331  1.869   -48.181 1.00 9.82   ? 244 ASN D CG  1 
ATOM   8601  O  OD1 . ASN D  1 244 ? 16.927  0.689   -48.093 1.00 11.02  ? 244 ASN D OD1 1 
ATOM   8602  N  ND2 . ASN D  1 244 ? 18.101  2.278   -49.155 1.00 13.81  ? 244 ASN D ND2 1 
ATOM   8603  N  N   . ASN D  1 245 ? 13.688  4.069   -45.727 1.00 6.99   ? 245 ASN D N   1 
ATOM   8604  C  CA  . ASN D  1 245 ? 13.141  5.160   -44.931 1.00 6.86   ? 245 ASN D CA  1 
ATOM   8605  C  C   . ASN D  1 245 ? 12.884  4.698   -43.506 1.00 6.40   ? 245 ASN D C   1 
ATOM   8606  O  O   . ASN D  1 245 ? 11.773  4.785   -42.995 1.00 8.37   ? 245 ASN D O   1 
ATOM   8607  C  CB  . ASN D  1 245 ? 11.890  5.715   -45.588 1.00 7.72   ? 245 ASN D CB  1 
ATOM   8608  C  CG  . ASN D  1 245 ? 10.767  4.762   -45.765 1.00 7.10   ? 245 ASN D CG  1 
ATOM   8609  O  OD1 . ASN D  1 245 ? 10.980  3.550   -45.823 1.00 8.39   ? 245 ASN D OD1 1 
ATOM   8610  N  ND2 . ASN D  1 245 ? 9.552   5.248   -45.902 1.00 9.63   ? 245 ASN D ND2 1 
ATOM   8611  N  N   . PHE D  1 246 ? 13.950  4.184   -42.895 1.00 7.00   ? 246 PHE D N   1 
ATOM   8612  C  CA  . PHE D  1 246 ? 13.908  3.746   -41.470 1.00 6.82   ? 246 PHE D CA  1 
ATOM   8613  C  C   . PHE D  1 246 ? 15.081  4.374   -40.778 1.00 6.62   ? 246 PHE D C   1 
ATOM   8614  O  O   . PHE D  1 246 ? 16.155  4.508   -41.367 1.00 6.96   ? 246 PHE D O   1 
ATOM   8615  C  CB  . PHE D  1 246 ? 13.951  2.183   -41.378 1.00 7.54   ? 246 PHE D CB  1 
ATOM   8616  C  CG  . PHE D  1 246 ? 15.167  1.551   -41.972 1.00 7.96   ? 246 PHE D CG  1 
ATOM   8617  C  CD1 . PHE D  1 246 ? 15.235  1.257   -43.350 1.00 7.98   ? 246 PHE D CD1 1 
ATOM   8618  C  CD2 . PHE D  1 246 ? 16.282  1.243   -41.184 1.00 9.25   ? 246 PHE D CD2 1 
ATOM   8619  C  CE1 . PHE D  1 246 ? 16.366  0.639   -43.905 1.00 8.43   ? 246 PHE D CE1 1 
ATOM   8620  C  CE2 . PHE D  1 246 ? 17.395  0.648   -41.745 1.00 9.93   ? 246 PHE D CE2 1 
ATOM   8621  C  CZ  . PHE D  1 246 ? 17.440  0.359   -43.114 1.00 9.34   ? 246 PHE D CZ  1 
ATOM   8622  N  N   . ARG D  1 247 ? 14.901  4.672   -39.502 1.00 6.55   ? 247 ARG D N   1 
ATOM   8623  C  CA  . ARG D  1 247 ? 15.968  5.174   -38.681 1.00 7.02   ? 247 ARG D CA  1 
ATOM   8624  C  C   . ARG D  1 247 ? 16.722  3.990   -38.024 1.00 7.05   ? 247 ARG D C   1 
ATOM   8625  O  O   . ARG D  1 247 ? 16.101  2.988   -37.715 1.00 7.42   ? 247 ARG D O   1 
ATOM   8626  C  CB  . ARG D  1 247 ? 15.378  6.058   -37.571 1.00 7.64   ? 247 ARG D CB  1 
ATOM   8627  C  CG  . ARG D  1 247 ? 16.376  6.931   -36.820 1.00 7.57   ? 247 ARG D CG  1 
ATOM   8628  C  CD  . ARG D  1 247 ? 15.753  7.600   -35.669 1.00 7.70   ? 247 ARG D CD  1 
ATOM   8629  N  NE  . ARG D  1 247 ? 16.590  8.670   -35.119 1.00 8.12   ? 247 ARG D NE  1 
ATOM   8630  C  CZ  . ARG D  1 247 ? 16.260  9.387   -34.037 1.00 8.18   ? 247 ARG D CZ  1 
ATOM   8631  N  NH1 . ARG D  1 247 ? 15.190  9.118   -33.341 1.00 9.08   ? 247 ARG D NH1 1 
ATOM   8632  N  NH2 . ARG D  1 247 ? 17.040  10.409  -33.705 1.00 8.62   ? 247 ARG D NH2 1 
ATOM   8633  N  N   . GLN D  1 248 ? 18.046  4.118   -37.845 1.00 6.76   ? 248 GLN D N   1 
ATOM   8634  C  CA  . GLN D  1 248 ? 18.776  3.096   -37.076 1.00 7.18   ? 248 GLN D CA  1 
ATOM   8635  C  C   . GLN D  1 248 ? 18.282  3.055   -35.664 1.00 7.24   ? 248 GLN D C   1 
ATOM   8636  O  O   . GLN D  1 248 ? 17.761  4.043   -35.100 1.00 8.06   ? 248 GLN D O   1 
ATOM   8637  C  CB  . GLN D  1 248 ? 20.271  3.473   -37.038 1.00 7.95   ? 248 GLN D CB  1 
ATOM   8638  C  CG  . GLN D  1 248 ? 20.970  3.496   -38.400 1.00 7.87   ? 248 GLN D CG  1 
ATOM   8639  C  CD  . GLN D  1 248 ? 20.954  2.102   -39.039 1.00 7.38   ? 248 GLN D CD  1 
ATOM   8640  O  OE1 . GLN D  1 248 ? 20.036  1.784   -39.776 1.00 8.09   ? 248 GLN D OE1 1 
ATOM   8641  N  NE2 . GLN D  1 248 ? 21.979  1.321   -38.739 1.00 9.44   ? 248 GLN D NE2 1 
ATOM   8642  N  N   . VAL D  1 249 ? 18.466  1.901   -35.005 1.00 7.64   ? 249 VAL D N   1 
ATOM   8643  C  CA  . VAL D  1 249 ? 18.096  1.778   -33.598 1.00 7.71   ? 249 VAL D CA  1 
ATOM   8644  C  C   . VAL D  1 249 ? 18.999  2.688   -32.746 1.00 7.97   ? 249 VAL D C   1 
ATOM   8645  O  O   . VAL D  1 249 ? 20.146  3.000   -33.067 1.00 8.83   ? 249 VAL D O   1 
ATOM   8646  C  CB  . VAL D  1 249 ? 18.124  0.320   -33.126 1.00 8.99   ? 249 VAL D CB  1 
ATOM   8647  C  CG1 . VAL D  1 249 ? 17.045  -0.474  -33.835 1.00 10.33  ? 249 VAL D CG1 1 
ATOM   8648  C  CG2 . VAL D  1 249 ? 19.543  -0.291  -33.259 1.00 11.00  ? 249 VAL D CG2 1 
ATOM   8649  N  N   . GLN D  1 250 ? 18.401  3.080   -31.583 1.00 8.67   ? 250 GLN D N   1 
ATOM   8650  C  CA  . GLN D  1 250 ? 18.931  4.068   -30.695 1.00 8.70   ? 250 GLN D CA  1 
ATOM   8651  C  C   . GLN D  1 250 ? 19.444  3.461   -29.411 1.00 9.34   ? 250 GLN D C   1 
ATOM   8652  O  O   . GLN D  1 250 ? 18.988  2.415   -28.997 1.00 11.04  ? 250 GLN D O   1 
ATOM   8653  C  CB  . GLN D  1 250 ? 17.829  5.086   -30.364 1.00 9.38   ? 250 GLN D CB  1 
ATOM   8654  C  CG  . GLN D  1 250 ? 17.179  5.715   -31.563 1.00 9.70   ? 250 GLN D CG  1 
ATOM   8655  C  CD  . GLN D  1 250 ? 18.098  6.639   -32.333 1.00 8.49   ? 250 GLN D CD  1 
ATOM   8656  O  OE1 . GLN D  1 250 ? 18.524  7.670   -31.749 1.00 9.76   ? 250 GLN D OE1 1 
ATOM   8657  N  NE2 . GLN D  1 250 ? 18.375  6.360   -33.580 1.00 9.10   ? 250 GLN D NE2 1 
ATOM   8658  N  N   . LYS D  1 251 ? 20.349  4.137   -28.741 1.00 10.58  ? 251 LYS D N   1 
ATOM   8659  C  CA  . LYS D  1 251 ? 20.756  3.723   -27.382 1.00 12.61  ? 251 LYS D CA  1 
ATOM   8660  C  C   . LYS D  1 251 ? 19.530  3.655   -26.489 1.00 12.21  ? 251 LYS D C   1 
ATOM   8661  O  O   . LYS D  1 251 ? 18.634  4.476   -26.544 1.00 11.54  ? 251 LYS D O   1 
ATOM   8662  C  CB  . LYS D  1 251 ? 21.733  4.726   -26.819 1.00 14.55  ? 251 LYS D CB  1 
ATOM   8663  C  CG  . LYS D  1 251 ? 23.144  4.848   -27.420 1.00 14.34  ? 251 LYS D CG  1 
ATOM   8664  C  CD  . LYS D  1 251 ? 23.987  3.753   -26.957 1.00 17.45  ? 251 LYS D CD  1 
ATOM   8665  C  CE  . LYS D  1 251 ? 25.460  3.769   -27.364 1.00 14.69  ? 251 LYS D CE  1 
ATOM   8666  N  NZ  . LYS D  1 251 ? 25.641  3.712   -28.829 1.00 12.72  ? 251 LYS D NZ  1 
ATOM   8667  N  N   . PHE D  1 252 ? 19.586  2.694   -25.592 1.00 12.61  ? 252 PHE D N   1 
ATOM   8668  C  CA  . PHE D  1 252 ? 18.554  2.624   -24.542 1.00 11.85  ? 252 PHE D CA  1 
ATOM   8669  C  C   . PHE D  1 252 ? 18.373  3.767   -23.515 1.00 12.42  ? 252 PHE D C   1 
ATOM   8670  O  O   . PHE D  1 252 ? 17.247  4.040   -23.103 1.00 12.83  ? 252 PHE D O   1 
ATOM   8671  C  CB  . PHE D  1 252 ? 18.588  1.259   -23.862 1.00 13.11  ? 252 PHE D CB  1 
ATOM   8672  C  CG  . PHE D  1 252 ? 17.895  0.210   -24.662 1.00 13.50  ? 252 PHE D CG  1 
ATOM   8673  C  CD1 . PHE D  1 252 ? 16.610  -0.174  -24.346 1.00 15.93  ? 252 PHE D CD1 1 
ATOM   8674  C  CD2 . PHE D  1 252 ? 18.502  -0.315  -25.783 1.00 20.38  ? 252 PHE D CD2 1 
ATOM   8675  C  CE1 . PHE D  1 252 ? 15.956  -1.114  -25.108 1.00 17.79  ? 252 PHE D CE1 1 
ATOM   8676  C  CE2 . PHE D  1 252 ? 17.859  -1.256  -26.553 1.00 21.20  ? 252 PHE D CE2 1 
ATOM   8677  C  CZ  . PHE D  1 252 ? 16.581  -1.656  -26.215 1.00 14.47  ? 252 PHE D CZ  1 
ATOM   8678  N  N   . ASP D  1 253 ? 19.447  4.438   -23.095 1.00 14.31  ? 253 ASP D N   1 
ATOM   8679  C  CA  . ASP D  1 253 ? 19.321  5.565   -22.150 1.00 18.16  ? 253 ASP D CA  1 
ATOM   8680  C  C   . ASP D  1 253 ? 18.797  5.130   -20.774 1.00 19.99  ? 253 ASP D C   1 
ATOM   8681  O  O   . ASP D  1 253 ? 18.239  5.926   -20.022 1.00 26.40  ? 253 ASP D O   1 
ATOM   8682  C  CB  . ASP D  1 253 ? 18.410  6.661   -22.723 1.00 22.77  ? 253 ASP D CB  1 
ATOM   8683  C  CG  . ASP D  1 253 ? 19.082  7.470   -23.821 1.00 16.75  ? 253 ASP D CG  1 
ATOM   8684  O  OD1 . ASP D  1 253 ? 20.331  7.458   -23.896 1.00 22.08  ? 253 ASP D OD1 1 
ATOM   8685  O  OD2 . ASP D  1 253 ? 18.362  8.117   -24.609 1.00 15.86  ? 253 ASP D OD2 1 
ATOM   8686  N  N   . GLU D  1 254 ? 19.000  3.856   -20.473 1.00 24.18  ? 254 GLU D N   1 
ATOM   8687  C  CA  . GLU D  1 254 ? 18.640  3.235   -19.239 1.00 26.54  ? 254 GLU D CA  1 
ATOM   8688  C  C   . GLU D  1 254 ? 17.190  2.670   -19.224 1.00 28.15  ? 254 GLU D C   1 
ATOM   8689  O  O   . GLU D  1 254 ? 16.777  2.040   -18.235 1.00 30.52  ? 254 GLU D O   1 
ATOM   8690  C  CB  . GLU D  1 254 ? 18.933  4.119   -17.987 1.00 33.63  ? 254 GLU D CB  1 
ATOM   8691  C  CG  . GLU D  1 254 ? 20.166  3.657   -17.191 1.00 55.67  ? 254 GLU D CG  1 
ATOM   8692  C  CD  . GLU D  1 254 ? 21.456  4.278   -17.703 1.00 68.09  ? 254 GLU D CD  1 
ATOM   8693  O  OE1 . GLU D  1 254 ? 21.432  5.488   -18.003 1.00 128.09 ? 254 GLU D OE1 1 
ATOM   8694  O  OE2 . GLU D  1 254 ? 22.487  3.566   -17.819 1.00 74.16  ? 254 GLU D OE2 1 
ATOM   8695  N  N   . ARG D  1 255 ? 16.450  2.879   -20.305 1.00 22.39  ? 255 ARG D N   1 
ATOM   8696  C  CA  . ARG D  1 255 ? 15.100  2.315   -20.408 1.00 16.88  ? 255 ARG D CA  1 
ATOM   8697  C  C   . ARG D  1 255 ? 15.082  0.708   -20.337 1.00 19.91  ? 255 ARG D C   1 
ATOM   8698  O  O   . ARG D  1 255 ? 16.036  -0.056  -20.776 1.00 26.25  ? 255 ARG D O   1 
ATOM   8699  C  CB  . ARG D  1 255 ? 14.493  2.809   -21.768 1.00 19.03  ? 255 ARG D CB  1 
ATOM   8700  C  CG  . ARG D  1 255 ? 14.246  4.335   -21.827 1.00 21.14  ? 255 ARG D CG  1 
ATOM   8701  C  CD  . ARG D  1 255 ? 13.781  4.740   -23.271 1.00 22.57  ? 255 ARG D CD  1 
ATOM   8702  N  NE  . ARG D  1 255 ? 14.849  4.759   -24.242 1.00 18.86  ? 255 ARG D NE  1 
ATOM   8703  C  CZ  . ARG D  1 255 ? 14.646  5.005   -25.527 1.00 19.79  ? 255 ARG D CZ  1 
ATOM   8704  N  NH1 . ARG D  1 255 ? 13.419  5.246   -25.973 1.00 14.34  ? 255 ARG D NH1 1 
ATOM   8705  N  NH2 . ARG D  1 255 ? 15.666  5.010   -26.365 1.00 17.05  ? 255 ARG D NH2 1 
ATOM   8706  N  N   . LEU D  1 256 ? 13.949  0.206   -19.850 1.00 19.62  ? 256 LEU D N   1 
ATOM   8707  C  CA  . LEU D  1 256 ? 13.469  -1.188  -20.066 1.00 17.80  ? 256 LEU D CA  1 
ATOM   8708  C  C   . LEU D  1 256 ? 12.287  -1.163  -21.050 1.00 16.78  ? 256 LEU D C   1 
ATOM   8709  O  O   . LEU D  1 256 ? 11.646  -0.154  -21.294 1.00 19.58  ? 256 LEU D O   1 
ATOM   8710  C  CB  . LEU D  1 256 ? 13.001  -1.784  -18.781 1.00 21.22  ? 256 LEU D CB  1 
ATOM   8711  C  CG  . LEU D  1 256 ? 14.113  -1.950  -17.789 1.00 22.49  ? 256 LEU D CG  1 
ATOM   8712  C  CD1 . LEU D  1 256 ? 13.550  -2.562  -16.521 1.00 33.40  ? 256 LEU D CD1 1 
ATOM   8713  C  CD2 . LEU D  1 256 ? 15.274  -2.823  -18.330 1.00 28.25  ? 256 LEU D CD2 1 
ATOM   8714  N  N   . VAL D  1 257 ? 12.067  -2.299  -21.654 1.00 14.98  ? 257 VAL D N   1 
ATOM   8715  C  CA  . VAL D  1 257 ? 10.879  -2.530  -22.489 1.00 12.90  ? 257 VAL D CA  1 
ATOM   8716  C  C   . VAL D  1 257 ? 10.047  -3.522  -21.716 1.00 12.96  ? 257 VAL D C   1 
ATOM   8717  O  O   . VAL D  1 257 ? 10.520  -4.616  -21.325 1.00 15.23  ? 257 VAL D O   1 
ATOM   8718  C  CB  . VAL D  1 257 ? 11.290  -3.124  -23.836 1.00 13.59  ? 257 VAL D CB  1 
ATOM   8719  C  CG1 . VAL D  1 257 ? 10.042  -3.516  -24.624 1.00 13.88  ? 257 VAL D CG1 1 
ATOM   8720  C  CG2 . VAL D  1 257 ? 12.147  -2.109  -24.587 1.00 14.16  ? 257 VAL D CG2 1 
ATOM   8721  N  N   . TYR D  1 258 ? 8.824   -3.161  -21.496 1.00 12.09  ? 258 TYR D N   1 
ATOM   8722  C  CA  . TYR D  1 258 ? 7.917   -3.998  -20.739 1.00 12.51  ? 258 TYR D CA  1 
ATOM   8723  C  C   . TYR D  1 258 ? 7.101   -4.861  -21.674 1.00 11.83  ? 258 TYR D C   1 
ATOM   8724  O  O   . TYR D  1 258 ? 6.696   -4.453  -22.764 1.00 13.91  ? 258 TYR D O   1 
ATOM   8725  C  CB  . TYR D  1 258 ? 7.051   -3.089  -19.822 1.00 14.44  ? 258 TYR D CB  1 
ATOM   8726  C  CG  . TYR D  1 258 ? 7.957   -2.228  -18.948 1.00 15.63  ? 258 TYR D CG  1 
ATOM   8727  C  CD1 . TYR D  1 258 ? 8.474   -2.713  -17.748 1.00 18.48  ? 258 TYR D CD1 1 
ATOM   8728  C  CD2 . TYR D  1 258 ? 8.349   -0.958  -19.356 1.00 17.02  ? 258 TYR D CD2 1 
ATOM   8729  C  CE1 . TYR D  1 258 ? 9.321   -1.942  -16.966 1.00 20.08  ? 258 TYR D CE1 1 
ATOM   8730  C  CE2 . TYR D  1 258 ? 9.194   -0.183  -18.581 1.00 20.91  ? 258 TYR D CE2 1 
ATOM   8731  C  CZ  . TYR D  1 258 ? 9.678   -0.676  -17.389 1.00 19.04  ? 258 TYR D CZ  1 
ATOM   8732  O  OH  . TYR D  1 258 ? 10.517  0.105   -16.625 1.00 25.26  ? 258 TYR D OH  1 
ATOM   8733  N  N   . THR D  1 259 ? 6.870   -6.090  -21.245 1.00 11.70  ? 259 THR D N   1 
ATOM   8734  C  CA  . THR D  1 259 ? 6.193   -7.049  -22.108 1.00 11.18  ? 259 THR D CA  1 
ATOM   8735  C  C   . THR D  1 259 ? 4.942   -7.544  -21.452 1.00 11.80  ? 259 THR D C   1 
ATOM   8736  O  O   . THR D  1 259 ? 4.880   -7.699  -20.238 1.00 13.04  ? 259 THR D O   1 
ATOM   8737  C  CB  . THR D  1 259 ? 7.051   -8.232  -22.558 1.00 11.69  ? 259 THR D CB  1 
ATOM   8738  O  OG1 . THR D  1 259 ? 7.467   -8.918  -21.383 1.00 14.19  ? 259 THR D OG1 1 
ATOM   8739  C  CG2 . THR D  1 259 ? 8.308   -7.750  -23.312 1.00 13.50  ? 259 THR D CG2 1 
ATOM   8740  N  N   . SER D  1 260 ? 3.952   -7.869  -22.270 1.00 12.12  ? 260 SER D N   1 
ATOM   8741  C  CA  . SER D  1 260 ? 2.695   -8.463  -21.783 1.00 14.37  ? 260 SER D CA  1 
ATOM   8742  C  C   . SER D  1 260 ? 2.732   -9.996  -21.836 1.00 17.15  ? 260 SER D C   1 
ATOM   8743  O  O   . SER D  1 260 ? 1.727   -10.635 -21.544 1.00 21.38  ? 260 SER D O   1 
ATOM   8744  C  CB  . SER D  1 260 ? 1.524   -7.955  -22.574 1.00 15.87  ? 260 SER D CB  1 
ATOM   8745  O  OG  . SER D  1 260 ? 1.642   -8.437  -23.940 1.00 14.60  ? 260 SER D OG  1 
ATOM   8746  N  N   . PHE D  1 261 ? 3.898   -10.544 -22.122 1.00 15.89  ? 261 PHE D N   1 
ATOM   8747  C  CA  . PHE D  1 261 ? 4.105   -11.963 -22.222 1.00 16.68  ? 261 PHE D CA  1 
ATOM   8748  C  C   . PHE D  1 261 ? 5.383   -12.299 -21.529 1.00 18.57  ? 261 PHE D C   1 
ATOM   8749  O  O   . PHE D  1 261 ? 6.254   -11.470 -21.421 1.00 18.60  ? 261 PHE D O   1 
ATOM   8750  C  CB  . PHE D  1 261 ? 4.124   -12.441 -23.694 1.00 15.60  ? 261 PHE D CB  1 
ATOM   8751  C  CG  . PHE D  1 261 ? 5.167   -11.722 -24.548 1.00 14.86  ? 261 PHE D CG  1 
ATOM   8752  C  CD1 . PHE D  1 261 ? 6.406   -12.303 -24.702 1.00 17.80  ? 261 PHE D CD1 1 
ATOM   8753  C  CD2 . PHE D  1 261 ? 4.900   -10.480 -25.083 1.00 14.85  ? 261 PHE D CD2 1 
ATOM   8754  C  CE1 . PHE D  1 261 ? 7.369   -11.687 -25.429 1.00 17.53  ? 261 PHE D CE1 1 
ATOM   8755  C  CE2 . PHE D  1 261 ? 5.905   -9.820  -25.793 1.00 14.55  ? 261 PHE D CE2 1 
ATOM   8756  C  CZ  . PHE D  1 261 ? 7.133   -10.427 -25.987 1.00 15.81  ? 261 PHE D CZ  1 
ATOM   8757  N  N   . SER D  1 262 ? 5.511   -13.558 -21.152 1.00 35.80  ? 262 SER D N   1 
ATOM   8758  C  CA  . SER D  1 262 ? 6.802   -13.993 -20.635 1.00 37.95  ? 262 SER D CA  1 
ATOM   8759  C  C   . SER D  1 262 ? 7.240   -15.053 -21.608 1.00 60.37  ? 262 SER D C   1 
ATOM   8760  O  O   . SER D  1 262 ? 8.403   -15.245 -21.891 1.00 64.72  ? 262 SER D O   1 
ATOM   8761  C  CB  . SER D  1 262 ? 6.649   -14.588 -19.234 1.00 52.69  ? 262 SER D CB  1 
ATOM   8762  O  OG  . SER D  1 262 ? 5.967   -13.698 -18.367 1.00 57.23  ? 262 SER D OG  1 
ATOM   8763  N  N   . GLN D  1 263 ? 6.213   -15.686 -22.085 1.00 61.39  ? 263 GLN D N   1 
ATOM   8764  C  CA  . GLN D  1 263 ? 5.959   -16.948 -22.725 1.00 72.69  ? 263 GLN D CA  1 
ATOM   8765  C  CB  . GLN D  1 263 ? 5.160   -16.726 -24.037 1.00 82.46  ? 263 GLN D CB  1 
ATOM   8766  C  CG  . GLN D  1 263 ? 3.606   -16.866 -23.892 1.00 82.28  ? 263 GLN D CG  1 
ATOM   8767  C  CD  . GLN D  1 263 ? 2.877   -15.810 -23.010 1.00 62.69  ? 263 GLN D CD  1 
ATOM   8768  O  OE1 . GLN D  1 263 ? 3.221   -15.604 -21.831 1.00 53.01  ? 263 GLN D OE1 1 
ATOM   8769  N  NE2 . GLN D  1 263 ? 1.812   -15.176 -23.579 1.00 59.57  ? 263 GLN D NE2 1 
HETATM 8770  ZN ZN  . ZN  E  2 .   ? 22.924  0.596   12.279  1.00 7.89   ? 301 ZN  A ZN  1 
HETATM 8771  F  F18 A 3TV F  3 .   ? 27.416  5.286   8.487   0.50 15.48  ? 302 3TV A F18 1 
HETATM 8772  F  F18 B 3TV F  3 .   ? 27.359  5.448   8.403   0.50 26.47  ? 302 3TV A F18 1 
HETATM 8773  C  C7  A 3TV F  3 .   ? 26.577  4.981   9.498   0.50 11.50  ? 302 3TV A C7  1 
HETATM 8774  C  C7  B 3TV F  3 .   ? 26.520  5.164   9.404   0.50 18.34  ? 302 3TV A C7  1 
HETATM 8775  C  C6  A 3TV F  3 .   ? 25.686  3.926   9.281   0.50 12.11  ? 302 3TV A C6  1 
HETATM 8776  C  C6  B 3TV F  3 .   ? 25.661  4.059   9.261   0.50 15.19  ? 302 3TV A C6  1 
HETATM 8777  F  F17 A 3TV F  3 .   ? 25.751  3.286   8.089   0.50 12.61  ? 302 3TV A F17 1 
HETATM 8778  F  F17 B 3TV F  3 .   ? 25.737  3.387   8.091   0.50 15.99  ? 302 3TV A F17 1 
HETATM 8779  C  C8  A 3TV F  3 .   ? 26.493  5.652   10.711  0.50 14.47  ? 302 3TV A C8  1 
HETATM 8780  C  C8  B 3TV F  3 .   ? 26.478  5.862   10.595  0.50 26.13  ? 302 3TV A C8  1 
HETATM 8781  S  S11 A 3TV F  3 .   ? 27.575  7.008   11.041  0.50 24.78  ? 302 3TV A S11 1 
HETATM 8782  S  S11 B 3TV F  3 .   ? 27.557  7.291   10.865  0.50 50.47  ? 302 3TV A S11 1 
HETATM 8783  C  C12 A 3TV F  3 .   ? 29.217  6.288   10.795  0.50 28.00  ? 302 3TV A C12 1 
HETATM 8784  C  C12 B 3TV F  3 .   ? 26.223  8.509   10.725  0.50 21.91  ? 302 3TV A C12 1 
HETATM 8785  C  C13 A 3TV F  3 .   ? 30.063  7.018   9.740   0.50 31.45  ? 302 3TV A C13 1 
HETATM 8786  C  C13 B 3TV F  3 .   ? 26.331  9.850   11.505  0.50 27.70  ? 302 3TV A C13 1 
HETATM 8787  C  C14 A 3TV F  3 .   ? 29.837  8.502   9.612   0.50 30.86  ? 302 3TV A C14 1 
HETATM 8788  C  C14 B 3TV F  3 .   ? 24.967  10.344  11.939  0.50 29.04  ? 302 3TV A C14 1 
HETATM 8789  C  C9  A 3TV F  3 .   ? 25.492  5.252   11.599  0.50 15.19  ? 302 3TV A C9  1 
HETATM 8790  C  C9  B 3TV F  3 .   ? 25.532  5.493   11.531  0.50 18.31  ? 302 3TV A C9  1 
HETATM 8791  F  F15 A 3TV F  3 .   ? 25.315  5.766   12.797  0.50 25.89  ? 302 3TV A F15 1 
HETATM 8792  F  F15 B 3TV F  3 .   ? 25.388  6.085   12.669  0.50 20.35  ? 302 3TV A F15 1 
HETATM 8793  C  C10 A 3TV F  3 .   ? 24.653  4.219   11.365  0.50 13.64  ? 302 3TV A C10 1 
HETATM 8794  C  C10 B 3TV F  3 .   ? 24.690  4.442   11.376  0.50 15.65  ? 302 3TV A C10 1 
HETATM 8795  F  F16 A 3TV F  3 .   ? 23.767  3.901   12.295  0.50 16.50  ? 302 3TV A F16 1 
HETATM 8796  F  F16 B 3TV F  3 .   ? 23.841  4.168   12.359  0.50 27.60  ? 302 3TV A F16 1 
HETATM 8797  C  C5  A 3TV F  3 .   ? 24.699  3.594   10.184  0.50 10.41  ? 302 3TV A C5  1 
HETATM 8798  C  C5  B 3TV F  3 .   ? 24.707  3.733   10.211  0.50 11.73  ? 302 3TV A C5  1 
HETATM 8799  S  S1  A 3TV F  3 .   ? 23.645  2.193   9.829   0.50 8.91   ? 302 3TV A S1  1 
HETATM 8800  S  S1  B 3TV F  3 .   ? 23.683  2.294   9.888   0.50 10.60  ? 302 3TV A S1  1 
HETATM 8801  O  O3  A 3TV F  3 .   ? 24.616  1.129   9.818   0.50 9.89   ? 302 3TV A O3  1 
HETATM 8802  O  O3  B 3TV F  3 .   ? 24.656  1.273   9.921   0.50 10.82  ? 302 3TV A O3  1 
HETATM 8803  O  O4  A 3TV F  3 .   ? 22.943  2.459   8.600   0.50 9.23   ? 302 3TV A O4  1 
HETATM 8804  O  O4  B 3TV F  3 .   ? 23.065  2.603   8.656   0.50 9.83   ? 302 3TV A O4  1 
HETATM 8805  N  N2  A 3TV F  3 .   ? 22.652  1.945   11.068  0.50 9.44   ? 302 3TV A N2  1 
HETATM 8806  N  N2  B 3TV F  3 .   ? 22.579  2.142   10.945  0.50 9.89   ? 302 3TV A N2  1 
HETATM 8807  C  C1  . EDO G  4 .   ? 36.349  6.125   14.301  1.00 23.91  ? 303 EDO A C1  1 
HETATM 8808  O  O1  . EDO G  4 .   ? 36.844  4.839   14.557  1.00 27.92  ? 303 EDO A O1  1 
HETATM 8809  C  C2  . EDO G  4 .   ? 37.096  6.699   13.068  1.00 32.81  ? 303 EDO A C2  1 
HETATM 8810  O  O2  . EDO G  4 .   ? 36.859  6.144   11.720  1.00 22.04  ? 303 EDO A O2  1 
HETATM 8811  C  C1  . EDO H  4 .   ? 29.228  10.639  22.830  1.00 59.82  ? 304 EDO A C1  1 
HETATM 8812  O  O1  . EDO H  4 .   ? 27.800  10.921  22.713  1.00 47.74  ? 304 EDO A O1  1 
HETATM 8813  C  C2  . EDO H  4 .   ? 30.065  11.703  23.579  1.00 46.62  ? 304 EDO A C2  1 
HETATM 8814  O  O2  . EDO H  4 .   ? 31.208  11.095  24.265  1.00 41.01  ? 304 EDO A O2  1 
HETATM 8815  C  C1  . EDO I  4 .   ? 27.257  -9.295  30.918  1.00 31.70  ? 305 EDO A C1  1 
HETATM 8816  O  O1  . EDO I  4 .   ? 28.621  -9.398  30.469  1.00 29.69  ? 305 EDO A O1  1 
HETATM 8817  C  C2  . EDO I  4 .   ? 26.308  -8.806  29.849  1.00 27.00  ? 305 EDO A C2  1 
HETATM 8818  O  O2  . EDO I  4 .   ? 25.947  -9.895  28.891  1.00 27.76  ? 305 EDO A O2  1 
HETATM 8819  C  C1  . PEG J  5 .   ? 23.779  -20.233 27.557  1.00 35.92  ? 306 PEG A C1  1 
HETATM 8820  O  O1  . PEG J  5 .   ? 24.027  -21.201 26.505  1.00 27.42  ? 306 PEG A O1  1 
HETATM 8821  C  C2  . PEG J  5 .   ? 24.350  -20.582 28.944  1.00 46.59  ? 306 PEG A C2  1 
HETATM 8822  O  O2  . PEG J  5 .   ? 24.257  -19.389 29.768  1.00 44.48  ? 306 PEG A O2  1 
HETATM 8823  C  C3  . PEG J  5 .   ? 25.365  -18.484 30.063  1.00 26.67  ? 306 PEG A C3  1 
HETATM 8824  C  C4  . PEG J  5 .   ? 26.742  -19.177 30.269  1.00 50.87  ? 306 PEG A C4  1 
HETATM 8825  O  O4  . PEG J  5 .   ? 27.896  -18.273 30.224  1.00 54.45  ? 306 PEG A O4  1 
HETATM 8826  C  C1  . EDO K  4 .   ? 6.362   -9.542  4.671   1.00 22.38  ? 307 EDO A C1  1 
HETATM 8827  O  O1  . EDO K  4 .   ? 5.713   -8.264  4.806   1.00 30.74  ? 307 EDO A O1  1 
HETATM 8828  C  C2  . EDO K  4 .   ? 6.946   -9.792  3.383   1.00 26.60  ? 307 EDO A C2  1 
HETATM 8829  O  O2  . EDO K  4 .   ? 7.678   -10.935 3.463   1.00 23.68  ? 307 EDO A O2  1 
HETATM 8830  C  C1  . EDO L  4 .   ? 28.701  -18.913 -6.207  1.00 29.16  ? 308 EDO A C1  1 
HETATM 8831  O  O1  . EDO L  4 .   ? 27.652  -18.485 -5.335  1.00 33.14  ? 308 EDO A O1  1 
HETATM 8832  C  C2  . EDO L  4 .   ? 28.828  -17.780 -7.219  1.00 27.34  ? 308 EDO A C2  1 
HETATM 8833  O  O2  . EDO L  4 .   ? 30.178  -17.349 -7.441  1.00 30.10  ? 308 EDO A O2  1 
HETATM 8834  C  C1  . EDO M  4 .   ? 44.279  -3.149  15.567  1.00 20.89  ? 309 EDO A C1  1 
HETATM 8835  O  O1  . EDO M  4 .   ? 44.989  -4.391  15.330  1.00 24.36  ? 309 EDO A O1  1 
HETATM 8836  C  C2  . EDO M  4 .   ? 44.335  -1.911  14.680  1.00 24.47  ? 309 EDO A C2  1 
HETATM 8837  O  O2  . EDO M  4 .   ? 45.333  -1.050  14.128  1.00 27.24  ? 309 EDO A O2  1 
HETATM 8838  C  C1  . EDO N  4 .   ? 21.270  -6.709  32.840  1.00 25.96  ? 310 EDO A C1  1 
HETATM 8839  O  O1  . EDO N  4 .   ? 20.136  -7.423  32.266  1.00 22.67  ? 310 EDO A O1  1 
HETATM 8840  C  C2  . EDO N  4 .   ? 21.466  -5.328  32.041  1.00 25.54  ? 310 EDO A C2  1 
HETATM 8841  O  O2  . EDO N  4 .   ? 20.827  -4.272  32.715  1.00 27.26  ? 310 EDO A O2  1 
HETATM 8842  ZN ZN  . ZN  O  2 .   ? -8.188  3.687   4.798   1.00 6.08   ? 301 ZN  B ZN  1 
HETATM 8843  F  F18 A 3TV P  3 .   ? -7.321  10.654  6.246   0.50 11.54  ? 302 3TV B F18 1 
HETATM 8844  F  F18 B 3TV P  3 .   ? -9.348  9.520   4.338   0.50 23.86  ? 302 3TV B F18 1 
HETATM 8845  C  C7  A 3TV P  3 .   ? -8.312  9.733   6.224   0.50 10.17  ? 302 3TV B C7  1 
HETATM 8846  C  C7  B 3TV P  3 .   ? -9.611  8.909   5.464   0.50 17.03  ? 302 3TV B C7  1 
HETATM 8847  C  C6  A 3TV P  3 .   ? -7.980  8.418   6.508   0.50 8.59   ? 302 3TV B C6  1 
HETATM 8848  C  C6  B 3TV P  3 .   ? -8.945  7.730   5.701   0.50 14.44  ? 302 3TV B C6  1 
HETATM 8849  F  F17 A 3TV P  3 .   ? -6.696  8.121   6.578   0.50 8.46   ? 302 3TV B F17 1 
HETATM 8850  F  F17 B 3TV P  3 .   ? -8.061  7.283   4.795   0.50 26.32  ? 302 3TV B F17 1 
HETATM 8851  C  C8  A 3TV P  3 .   ? -9.615  10.159  6.142   0.50 11.39  ? 302 3TV B C8  1 
HETATM 8852  C  C8  B 3TV P  3 .   ? -10.542 9.409   6.341   0.50 17.03  ? 302 3TV B C8  1 
HETATM 8853  S  S11 A 3TV P  3 .   ? -9.839  11.933  5.868   0.50 15.69  ? 302 3TV B S11 1 
HETATM 8854  S  S11 B 3TV P  3 .   ? -11.346 10.937  5.940   0.50 27.33  ? 302 3TV B S11 1 
HETATM 8855  C  C12 A 3TV P  3 .   ? -11.572 12.228  6.394   0.50 15.46  ? 302 3TV B C12 1 
HETATM 8856  C  C12 B 3TV P  3 .   ? -10.697 12.148  7.131   0.50 37.43  ? 302 3TV B C12 1 
HETATM 8857  C  C13 A 3TV P  3 .   ? -11.758 11.918  7.905   0.50 15.20  ? 302 3TV B C13 1 
HETATM 8858  C  C13 B 3TV P  3 .   ? -11.538 12.072  8.397   0.50 36.37  ? 302 3TV B C13 1 
HETATM 8859  C  C14 A 3TV P  3 .   ? -13.206 12.121  8.329   0.50 20.21  ? 302 3TV B C14 1 
HETATM 8860  C  C14 B 3TV P  3 .   ? -12.987 12.328  8.080   0.50 43.54  ? 302 3TV B C14 1 
HETATM 8861  C  C9  A 3TV P  3 .   ? -10.596 9.201   6.225   0.50 10.69  ? 302 3TV B C9  1 
HETATM 8862  C  C9  B 3TV P  3 .   ? -10.839 8.746   7.509   0.50 13.45  ? 302 3TV B C9  1 
HETATM 8863  F  F15 A 3TV P  3 .   ? -11.858 9.483   6.111   0.50 17.14  ? 302 3TV B F15 1 
HETATM 8864  F  F15 B 3TV P  3 .   ? -11.711 9.150   8.424   0.50 22.65  ? 302 3TV B F15 1 
HETATM 8865  C  C10 A 3TV P  3 .   ? -10.257 7.855   6.495   0.50 10.75  ? 302 3TV B C10 1 
HETATM 8866  C  C10 B 3TV P  3 .   ? -10.197 7.573   7.741   0.50 12.11  ? 302 3TV B C10 1 
HETATM 8867  F  F16 A 3TV P  3 .   ? -11.247 7.038   6.581   0.50 14.37  ? 302 3TV B F16 1 
HETATM 8868  F  F16 B 3TV P  3 .   ? -10.403 6.907   8.888   0.50 15.28  ? 302 3TV B F16 1 
HETATM 8869  C  C5  A 3TV P  3 .   ? -8.906  7.360   6.650   0.50 8.71   ? 302 3TV B C5  1 
HETATM 8870  C  C5  B 3TV P  3 .   ? -9.224  7.130   6.855   0.50 11.64  ? 302 3TV B C5  1 
HETATM 8871  S  S1  A 3TV P  3 .   ? -8.458  5.588   7.079   0.50 8.33   ? 302 3TV B S1  1 
HETATM 8872  S  S1  B 3TV P  3 .   ? -8.428  5.600   7.137   0.50 9.60   ? 302 3TV B S1  1 
HETATM 8873  O  O3  A 3TV P  3 .   ? -9.587  4.815   7.194   0.50 12.79  ? 302 3TV B O3  1 
HETATM 8874  O  O3  B 3TV P  3 .   ? -9.593  4.723   7.175   0.50 8.59   ? 302 3TV B O3  1 
HETATM 8875  O  O4  A 3TV P  3 .   ? -7.693  5.771   8.279   0.50 8.82   ? 302 3TV B O4  1 
HETATM 8876  O  O4  B 3TV P  3 .   ? -7.655  5.792   8.318   0.50 8.53   ? 302 3TV B O4  1 
HETATM 8877  N  N2  A 3TV P  3 .   ? -7.450  5.140   6.003   0.50 7.99   ? 302 3TV B N2  1 
HETATM 8878  N  N2  B 3TV P  3 .   ? -7.529  5.130   5.793   0.50 9.87   ? 302 3TV B N2  1 
HETATM 8879  C  C1  . EDO Q  4 .   ? -17.123 -3.476  22.839  1.00 29.91  ? 303 EDO B C1  1 
HETATM 8880  O  O1  . EDO Q  4 .   ? -15.974 -2.572  22.934  1.00 26.15  ? 303 EDO B O1  1 
HETATM 8881  C  C2  . EDO Q  4 .   ? -17.565 -3.565  21.353  1.00 27.85  ? 303 EDO B C2  1 
HETATM 8882  O  O2  . EDO Q  4 .   ? -16.472 -3.689  20.395  1.00 15.33  ? 303 EDO B O2  1 
HETATM 8883  C  C1  . PEG R  5 .   ? -19.543 -15.684 -10.888 1.00 61.55  ? 304 PEG B C1  1 
HETATM 8884  O  O1  . PEG R  5 .   ? -18.816 -14.670 -11.592 1.00 47.52  ? 304 PEG B O1  1 
HETATM 8885  C  C2  . PEG R  5 .   ? -19.948 -15.096 -9.553  1.00 35.61  ? 304 PEG B C2  1 
HETATM 8886  O  O2  . PEG R  5 .   ? -19.910 -15.874 -8.361  1.00 46.52  ? 304 PEG B O2  1 
HETATM 8887  C  C3  . PEG R  5 .   ? -18.613 -16.480 -8.221  1.00 24.50  ? 304 PEG B C3  1 
HETATM 8888  C  C4  . PEG R  5 .   ? -17.736 -16.141 -7.014  1.00 24.74  ? 304 PEG B C4  1 
HETATM 8889  O  O4  . PEG R  5 .   ? -17.075 -16.874 -6.011  1.00 35.97  ? 304 PEG B O4  1 
HETATM 8890  C  C1  . CIT S  6 .   ? -11.571 13.423  0.163   0.50 19.28  ? 305 CIT B C1  1 
HETATM 8891  O  O1  . CIT S  6 .   ? -12.201 14.239  -0.558  0.50 31.92  ? 305 CIT B O1  1 
HETATM 8892  O  O2  . CIT S  6 .   ? -10.423 13.687  0.536   0.50 34.41  ? 305 CIT B O2  1 
HETATM 8893  C  C2  . CIT S  6 .   ? -12.136 12.024  0.471   0.50 14.61  ? 305 CIT B C2  1 
HETATM 8894  C  C3  . CIT S  6 .   ? -12.352 11.866  2.051   0.50 22.56  ? 305 CIT B C3  1 
HETATM 8895  O  O7  . CIT S  6 .   ? -12.831 12.969  2.829   0.50 35.64  ? 305 CIT B O7  1 
HETATM 8896  C  C4  . CIT S  6 .   ? -13.214 10.705  2.317   0.50 23.17  ? 305 CIT B C4  1 
HETATM 8897  C  C5  . CIT S  6 .   ? -14.311 11.022  3.250   0.50 17.34  ? 305 CIT B C5  1 
HETATM 8898  O  O3  . CIT S  6 .   ? -15.360 11.481  2.740   0.50 35.63  ? 305 CIT B O3  1 
HETATM 8899  O  O4  . CIT S  6 .   ? -14.187 10.836  4.427   0.50 20.26  ? 305 CIT B O4  1 
HETATM 8900  C  C6  . CIT S  6 .   ? -11.033 11.390  2.439   0.50 25.01  ? 305 CIT B C6  1 
HETATM 8901  O  O5  . CIT S  6 .   ? -10.763 10.502  1.708   0.50 22.41  ? 305 CIT B O5  1 
HETATM 8902  O  O6  . CIT S  6 .   ? -10.302 11.970  3.220   0.50 36.43  ? 305 CIT B O6  1 
HETATM 8903  ZN ZN  . ZN  T  2 .   ? 37.532  2.450   -30.999 1.00 11.58  ? 301 ZN  C ZN  1 
HETATM 8904  F  F18 . 3TV U  3 .   ? 40.048  7.939   -30.525 1.00 23.27  ? 302 3TV C F18 1 
HETATM 8905  C  C7  . 3TV U  3 .   ? 40.125  7.278   -31.694 1.00 19.18  ? 302 3TV C C7  1 
HETATM 8906  C  C6  . 3TV U  3 .   ? 39.267  6.224   -31.920 1.00 13.98  ? 302 3TV C C6  1 
HETATM 8907  F  F17 . 3TV U  3 .   ? 38.448  5.942   -30.913 1.00 17.60  ? 302 3TV C F17 1 
HETATM 8908  C  C8  . 3TV U  3 .   ? 41.064  7.657   -32.592 1.00 19.65  ? 302 3TV C C8  1 
HETATM 8909  S  S11 . 3TV U  3 .   ? 42.006  9.115   -32.247 1.00 33.88  ? 302 3TV C S11 1 
HETATM 8910  C  C12 . 3TV U  3 .   ? 43.675  8.333   -32.468 1.00 33.87  ? 302 3TV C C12 1 
HETATM 8911  C  C13 . 3TV U  3 .   ? 44.353  8.606   -33.823 1.00 40.73  ? 302 3TV C C13 1 
HETATM 8912  C  C14 . 3TV U  3 .   ? 44.721  10.050  -33.974 1.00 33.99  ? 302 3TV C C14 1 
HETATM 8913  C  C9  . 3TV U  3 .   ? 41.120  6.975   -33.807 1.00 15.58  ? 302 3TV C C9  1 
HETATM 8914  F  F15 . 3TV U  3 .   ? 41.972  7.316   -34.789 1.00 17.57  ? 302 3TV C F15 1 
HETATM 8915  C  C10 . 3TV U  3 .   ? 40.278  5.913   -34.034 1.00 14.18  ? 302 3TV C C10 1 
HETATM 8916  F  F16 . 3TV U  3 .   ? 40.408  5.264   -35.178 1.00 14.32  ? 302 3TV C F16 1 
HETATM 8917  C  C5  . 3TV U  3 .   ? 39.330  5.505   -33.078 1.00 12.63  ? 302 3TV C C5  1 
HETATM 8918  S  S1  . 3TV U  3 .   ? 38.322  4.085   -33.421 1.00 11.01  ? 302 3TV C S1  1 
HETATM 8919  O  O3  . 3TV U  3 .   ? 39.253  2.997   -33.391 1.00 12.22  ? 302 3TV C O3  1 
HETATM 8920  O  O4  . 3TV U  3 .   ? 37.747  4.349   -34.670 1.00 10.79  ? 302 3TV C O4  1 
HETATM 8921  N  N2  . 3TV U  3 .   ? 37.256  3.869   -32.281 1.00 10.67  ? 302 3TV C N2  1 
HETATM 8922  C  C1  . EDO V  4 .   ? 50.523  8.552   -28.907 1.00 18.87  ? 303 EDO C C1  1 
HETATM 8923  O  O1  . EDO V  4 .   ? 51.150  7.328   -28.608 1.00 20.69  ? 303 EDO C O1  1 
HETATM 8924  C  C2  . EDO V  4 .   ? 51.380  9.162   -30.032 1.00 22.65  ? 303 EDO C C2  1 
HETATM 8925  O  O2  . EDO V  4 .   ? 51.275  8.372   -31.267 1.00 21.13  ? 303 EDO C O2  1 
HETATM 8926  C  C1  . PEG W  5 .   ? 32.718  22.269  -38.635 1.00 30.11  ? 304 PEG C C1  1 
HETATM 8927  O  O1  . PEG W  5 .   ? 34.209  22.119  -38.709 1.00 52.14  ? 304 PEG C O1  1 
HETATM 8928  C  C2  . PEG W  5 .   ? 32.126  22.131  -37.231 1.00 27.57  ? 304 PEG C C2  1 
HETATM 8929  O  O2  . PEG W  5 .   ? 32.950  22.978  -36.405 1.00 49.77  ? 304 PEG C O2  1 
HETATM 8930  C  C3  . PEG W  5 .   ? 33.456  22.451  -35.155 1.00 28.62  ? 304 PEG C C3  1 
HETATM 8931  C  C4  . PEG W  5 .   ? 34.695  23.235  -34.717 1.00 45.97  ? 304 PEG C C4  1 
HETATM 8932  O  O4  . PEG W  5 .   ? 34.638  23.574  -33.310 1.00 53.42  ? 304 PEG C O4  1 
HETATM 8933  C  C1  . EDO X  4 .   ? 34.159  -7.881  -10.828 1.00 28.19  ? 305 EDO C C1  1 
HETATM 8934  O  O1  . EDO X  4 .   ? 34.253  -6.531  -10.886 1.00 27.28  ? 305 EDO C O1  1 
HETATM 8935  C  C2  . EDO X  4 .   ? 35.353  -8.365  -11.537 1.00 24.51  ? 305 EDO C C2  1 
HETATM 8936  O  O2  . EDO X  4 .   ? 35.167  -9.695  -11.588 1.00 26.27  ? 305 EDO C O2  1 
HETATM 8937  ZN ZN  . ZN  Y  2 .   ? 6.705   5.592   -38.518 1.00 6.94   ? 301 ZN  D ZN  1 
HETATM 8938  F  F18 A 3TV Z  3 .   ? 3.460   11.253  -34.866 0.50 11.47  ? 302 3TV D F18 1 
HETATM 8939  F  F18 B 3TV Z  3 .   ? 3.076   11.732  -37.493 0.50 24.33  ? 302 3TV D F18 1 
HETATM 8940  C  C7  A 3TV Z  3 .   ? 4.243   10.728  -35.851 0.50 8.92   ? 302 3TV D C7  1 
HETATM 8941  C  C7  B 3TV Z  3 .   ? 4.313   11.209  -37.273 0.50 24.32  ? 302 3TV D C7  1 
HETATM 8942  C  C6  A 3TV Z  3 .   ? 4.866   9.561   -35.604 0.50 7.41   ? 302 3TV D C6  1 
HETATM 8943  C  C6  B 3TV Z  3 .   ? 4.666   9.837   -36.960 0.50 22.65  ? 302 3TV D C6  1 
HETATM 8944  F  F17 A 3TV Z  3 .   ? 4.623   9.011   -34.425 0.50 9.59   ? 302 3TV D F17 1 
HETATM 8945  F  F17 B 3TV Z  3 .   ? 3.628   9.074   -36.892 0.50 21.24  ? 302 3TV D F17 1 
HETATM 8946  C  C8  A 3TV Z  3 .   ? 4.482   11.365  -37.089 0.50 11.00  ? 302 3TV D C8  1 
HETATM 8947  C  C8  B 3TV Z  3 .   ? 5.359   12.096  -37.377 0.50 20.86  ? 302 3TV D C8  1 
HETATM 8948  S  S11 A 3TV Z  3 .   ? 3.690   12.914  -37.565 0.50 20.13  ? 302 3TV D S11 1 
HETATM 8949  S  S11 B 3TV Z  3 .   ? 5.087   13.844  -37.774 0.50 41.05  ? 302 3TV D S11 1 
HETATM 8950  C  C12 A 3TV Z  3 .   ? 5.173   14.017  -37.686 0.50 16.13  ? 302 3TV D C12 1 
HETATM 8951  C  C12 B 3TV Z  3 .   ? 3.417   14.254  -37.121 0.50 29.95  ? 302 3TV D C12 1 
HETATM 8952  C  C13 A 3TV Z  3 .   ? 5.111   15.469  -38.119 0.50 29.92  ? 302 3TV D C13 1 
HETATM 8953  C  C13 B 3TV Z  3 .   ? 3.147   13.831  -35.671 0.50 18.67  ? 302 3TV D C13 1 
HETATM 8954  C  C14 A 3TV Z  3 .   ? 4.082   15.741  -39.183 0.50 35.19  ? 302 3TV D C14 1 
HETATM 8955  C  C14 B 3TV Z  3 .   ? 1.719   14.108  -35.325 0.50 21.61  ? 302 3TV D C14 1 
HETATM 8956  C  C9  A 3TV Z  3 .   ? 5.331   10.810  -38.001 0.50 9.93   ? 302 3TV D C9  1 
HETATM 8957  C  C9  B 3TV Z  3 .   ? 6.654   11.661  -37.215 0.50 15.60  ? 302 3TV D C9  1 
HETATM 8958  F  F15 A 3TV Z  3 .   ? 5.528   11.313  -39.199 0.50 14.69  ? 302 3TV D F15 1 
HETATM 8959  F  F15 B 3TV Z  3 .   ? 7.650   12.587  -37.291 0.50 19.62  ? 302 3TV D F15 1 
HETATM 8960  C  C10 A 3TV Z  3 .   ? 5.914   9.613   -37.706 0.50 7.65   ? 302 3TV D C10 1 
HETATM 8961  C  C10 B 3TV Z  3 .   ? 6.958   10.330  -36.915 0.50 17.67  ? 302 3TV D C10 1 
HETATM 8962  F  F16 A 3TV Z  3 .   ? 6.675   9.121   -38.700 0.50 14.95  ? 302 3TV D F16 1 
HETATM 8963  F  F16 B 3TV Z  3 .   ? 8.262   10.053  -36.811 0.50 15.00  ? 302 3TV D F16 1 
HETATM 8964  C  C5  A 3TV Z  3 .   ? 5.677   8.960   -36.541 0.50 7.62   ? 302 3TV D C5  1 
HETATM 8965  C  C5  B 3TV Z  3 .   ? 5.992   9.303   -36.747 0.50 14.57  ? 302 3TV D C5  1 
HETATM 8966  S  S1  A 3TV Z  3 .   ? 6.476   7.460   -36.165 0.50 8.22   ? 302 3TV D S1  1 
HETATM 8967  S  S1  B 3TV Z  3 .   ? 6.459   7.538   -36.219 0.50 10.51  ? 302 3TV D S1  1 
HETATM 8968  O  O3  A 3TV Z  3 .   ? 5.385   6.551   -36.069 0.50 9.16   ? 302 3TV D O3  1 
HETATM 8969  O  O3  B 3TV Z  3 .   ? 5.272   6.721   -36.075 0.50 11.83  ? 302 3TV D O3  1 
HETATM 8970  O  O4  A 3TV Z  3 .   ? 7.228   7.786   -35.007 0.50 8.74   ? 302 3TV D O4  1 
HETATM 8971  O  O4  B 3TV Z  3 .   ? 7.281   7.682   -35.017 0.50 10.90  ? 302 3TV D O4  1 
HETATM 8972  N  N2  A 3TV Z  3 .   ? 7.492   6.982   -37.273 0.50 9.78   ? 302 3TV D N2  1 
HETATM 8973  N  N2  B 3TV Z  3 .   ? 7.302   7.087   -37.504 0.50 8.05   ? 302 3TV D N2  1 
HETATM 8974  C  C1  . PEG AA 5 .   ? 1.512   17.773  -48.958 1.00 60.37  ? 303 PEG D C1  1 
HETATM 8975  O  O1  . PEG AA 5 .   ? 0.613   16.660  -48.788 1.00 70.01  ? 303 PEG D O1  1 
HETATM 8976  C  C2  . PEG AA 5 .   ? 2.959   17.395  -48.571 1.00 59.89  ? 303 PEG D C2  1 
HETATM 8977  O  O2  . PEG AA 5 .   ? 4.015   18.134  -49.227 1.00 61.34  ? 303 PEG D O2  1 
HETATM 8978  C  C3  . PEG AA 5 .   ? 3.883   18.397  -50.625 1.00 34.54  ? 303 PEG D C3  1 
HETATM 8979  C  C4  . PEG AA 5 .   ? 3.916   19.855  -51.012 1.00 49.20  ? 303 PEG D C4  1 
HETATM 8980  O  O4  . PEG AA 5 .   ? 3.913   19.755  -52.424 1.00 56.93  ? 303 PEG D O4  1 
HETATM 8981  C  C1  . CIT BA 6 .   ? 8.193   21.094  -36.062 1.00 52.78  ? 304 CIT D C1  1 
HETATM 8982  O  O1  . CIT BA 6 .   ? 7.499   21.865  -36.799 1.00 79.47  ? 304 CIT D O1  1 
HETATM 8983  O  O2  . CIT BA 6 .   ? 9.459   20.994  -36.220 1.00 111.02 ? 304 CIT D O2  1 
HETATM 8984  C  C2  . CIT BA 6 .   ? 7.473   20.228  -35.038 1.00 42.49  ? 304 CIT D C2  1 
HETATM 8985  C  C3  . CIT BA 6 .   ? 7.571   20.647  -33.534 1.00 24.82  ? 304 CIT D C3  1 
HETATM 8986  O  O7  . CIT BA 6 .   ? 7.238   22.040  -33.519 1.00 65.54  ? 304 CIT D O7  1 
HETATM 8987  C  C4  . CIT BA 6 .   ? 6.590   19.856  -32.668 1.00 38.05  ? 304 CIT D C4  1 
HETATM 8988  C  C5  . CIT BA 6 .   ? 5.878   18.754  -33.397 1.00 29.95  ? 304 CIT D C5  1 
HETATM 8989  O  O3  . CIT BA 6 .   ? 4.863   19.105  -34.040 1.00 65.86  ? 304 CIT D O3  1 
HETATM 8990  O  O4  . CIT BA 6 .   ? 6.306   17.552  -33.353 1.00 25.51  ? 304 CIT D O4  1 
HETATM 8991  C  C6  . CIT BA 6 .   ? 8.980   20.607  -32.865 1.00 37.01  ? 304 CIT D C6  1 
HETATM 8992  O  O5  . CIT BA 6 .   ? 9.892   21.233  -33.477 1.00 60.72  ? 304 CIT D O5  1 
HETATM 8993  O  O6  . CIT BA 6 .   ? 9.332   20.046  -31.746 1.00 16.28  ? 304 CIT D O6  1 
HETATM 8994  C  C1  . EDO CA 4 .   ? 12.035  22.806  -59.786 1.00 56.87  ? 305 EDO D C1  1 
HETATM 8995  O  O1  . EDO CA 4 .   ? 13.409  23.238  -59.852 1.00 47.29  ? 305 EDO D O1  1 
HETATM 8996  C  C2  . EDO CA 4 .   ? 11.354  23.017  -61.151 1.00 40.72  ? 305 EDO D C2  1 
HETATM 8997  O  O2  . EDO CA 4 .   ? 11.552  21.866  -61.992 1.00 33.41  ? 305 EDO D O2  1 
HETATM 8998  C  C1  . CIT DA 6 .   ? 2.803   15.574  -43.681 0.50 24.51  ? 306 CIT D C1  1 
HETATM 8999  O  O1  . CIT DA 6 .   ? 3.811   16.136  -44.061 0.50 30.79  ? 306 CIT D O1  1 
HETATM 9000  O  O2  . CIT DA 6 .   ? 1.727   16.173  -43.859 0.50 26.41  ? 306 CIT D O2  1 
HETATM 9001  C  C2  . CIT DA 6 .   ? 2.922   14.155  -43.112 0.50 14.44  ? 306 CIT D C2  1 
HETATM 9002  C  C3  . CIT DA 6 .   ? 2.662   13.917  -41.560 0.50 25.05  ? 306 CIT D C3  1 
HETATM 9003  O  O7  . CIT DA 6 .   ? 2.205   15.030  -40.744 0.50 37.09  ? 306 CIT D O7  1 
HETATM 9004  C  C4  . CIT DA 6 .   ? 1.765   12.721  -41.329 0.50 28.01  ? 306 CIT D C4  1 
HETATM 9005  C  C5  . CIT DA 6 .   ? 0.701   13.106  -40.369 0.50 15.13  ? 306 CIT D C5  1 
HETATM 9006  O  O3  . CIT DA 6 .   ? -0.271  13.667  -40.893 0.50 34.22  ? 306 CIT D O3  1 
HETATM 9007  O  O4  . CIT DA 6 .   ? 0.839   12.895  -39.206 0.50 22.78  ? 306 CIT D O4  1 
HETATM 9008  C  C6  . CIT DA 6 .   ? 3.868   13.369  -40.941 0.50 26.08  ? 306 CIT D C6  1 
HETATM 9009  O  O5  . CIT DA 6 .   ? 4.426   12.596  -41.703 0.50 22.79  ? 306 CIT D O5  1 
HETATM 9010  O  O6  . CIT DA 6 .   ? 4.225   13.791  -39.821 0.50 47.41  ? 306 CIT D O6  1 
HETATM 9011  C  C1  . EDO EA 4 .   ? -7.944  8.444   -55.778 1.00 25.12  ? 307 EDO D C1  1 
HETATM 9012  O  O1  . EDO EA 4 .   ? -8.535  9.689   -55.588 1.00 22.22  ? 307 EDO D O1  1 
HETATM 9013  C  C2  . EDO EA 4 .   ? -7.755  8.174   -57.220 1.00 25.77  ? 307 EDO D C2  1 
HETATM 9014  O  O2  . EDO EA 4 .   ? -6.487  8.038   -57.626 1.00 24.52  ? 307 EDO D O2  1 
HETATM 9015  O  O   . HOH FA 7 .   ? 14.604  -16.759 31.573  1.00 34.52  ? 401 HOH A O   1 
HETATM 9016  O  O   . HOH FA 7 .   ? 4.667   -0.247  -8.411  1.00 30.54  ? 402 HOH A O   1 
HETATM 9017  O  O   . HOH FA 7 .   ? 5.883   -4.005  -8.142  1.00 28.84  ? 403 HOH A O   1 
HETATM 9018  O  O   . HOH FA 7 .   ? 8.853   -16.222 -4.081  1.00 37.21  ? 404 HOH A O   1 
HETATM 9019  O  O   . HOH FA 7 .   ? 19.296  6.719   35.649  1.00 36.74  ? 405 HOH A O   1 
HETATM 9020  O  O   . HOH FA 7 .   ? 31.371  -16.995 -5.351  1.00 37.75  ? 406 HOH A O   1 
HETATM 9021  O  O   . HOH FA 7 .   ? 45.355  -5.923  13.459  1.00 32.44  ? 407 HOH A O   1 
HETATM 9022  O  O   . HOH FA 7 .   ? 4.179   -6.007  24.669  1.00 35.96  ? 408 HOH A O   1 
HETATM 9023  O  O   . HOH FA 7 .   ? 10.992  12.346  20.410  1.00 30.72  ? 409 HOH A O   1 
HETATM 9024  O  O   . HOH FA 7 .   ? 34.943  -11.094 -3.059  1.00 30.54  ? 410 HOH A O   1 
HETATM 9025  O  O   . HOH FA 7 .   ? 4.779   -9.097  25.547  1.00 23.91  ? 411 HOH A O   1 
HETATM 9026  O  O   . HOH FA 7 .   ? 26.534  -20.556 -9.480  1.00 42.89  ? 412 HOH A O   1 
HETATM 9027  O  O   . HOH FA 7 .   ? 6.878   7.570   7.881   1.00 22.25  ? 413 HOH A O   1 
HETATM 9028  O  O   . HOH FA 7 .   ? 11.787  16.267  15.184  1.00 33.14  ? 414 HOH A O   1 
HETATM 9029  O  O   . HOH FA 7 .   ? 14.315  4.747   23.857  1.00 35.92  ? 415 HOH A O   1 
HETATM 9030  O  O   . HOH FA 7 .   ? 41.508  6.008   5.437   1.00 27.22  ? 416 HOH A O   1 
HETATM 9031  O  O   . HOH FA 7 .   ? 36.782  -14.383 -1.675  1.00 42.19  ? 417 HOH A O   1 
HETATM 9032  O  O   . HOH FA 7 .   ? 19.783  13.894  28.556  1.00 24.07  ? 418 HOH A O   1 
HETATM 9033  O  O   . HOH FA 7 .   ? 37.088  7.854   9.825   1.00 27.75  ? 419 HOH A O   1 
HETATM 9034  O  O   . HOH FA 7 .   ? 41.896  2.326   29.171  1.00 28.36  ? 420 HOH A O   1 
HETATM 9035  O  O   . HOH FA 7 .   ? 26.312  -22.234 27.079  1.00 38.88  ? 421 HOH A O   1 
HETATM 9036  O  O   . HOH FA 7 .   ? 14.471  -10.039 25.960  1.00 13.49  ? 422 HOH A O   1 
HETATM 9037  O  O   . HOH FA 7 .   ? 24.479  -11.605 30.150  1.00 25.85  ? 423 HOH A O   1 
HETATM 9038  O  O   . HOH FA 7 .   ? 42.562  0.394   5.213   1.00 46.15  ? 424 HOH A O   1 
HETATM 9039  O  O   . HOH FA 7 .   ? 43.621  -4.426  12.786  1.00 21.71  ? 425 HOH A O   1 
HETATM 9040  O  O   . HOH FA 7 .   ? 26.164  2.765   -2.480  1.00 28.36  ? 426 HOH A O   1 
HETATM 9041  O  O   . HOH FA 7 .   ? 11.237  3.340   19.116  1.00 19.97  ? 427 HOH A O   1 
HETATM 9042  O  O   . HOH FA 7 .   ? 23.794  8.471   11.726  1.00 25.71  ? 428 HOH A O   1 
HETATM 9043  O  O   . HOH FA 7 .   ? 6.034   -3.518  20.993  1.00 23.60  ? 429 HOH A O   1 
HETATM 9044  O  O   . HOH FA 7 .   ? 28.435  -24.144 8.061   1.00 36.56  ? 430 HOH A O   1 
HETATM 9045  O  O   . HOH FA 7 .   ? 17.922  3.145   12.762  1.00 11.04  ? 431 HOH A O   1 
HETATM 9046  O  O   . HOH FA 7 .   ? 34.709  4.003   31.499  1.00 33.97  ? 432 HOH A O   1 
HETATM 9047  O  O   . HOH FA 7 .   ? 18.415  -3.136  -5.730  1.00 25.37  ? 433 HOH A O   1 
HETATM 9048  O  O   . HOH FA 7 .   ? 42.863  -10.269 18.935  1.00 26.38  ? 434 HOH A O   1 
HETATM 9049  O  O   . HOH FA 7 .   ? 7.680   -8.204  11.766  1.00 21.02  ? 435 HOH A O   1 
HETATM 9050  O  O   . HOH FA 7 .   ? 27.971  -21.548 2.015   1.00 36.36  ? 436 HOH A O   1 
HETATM 9051  O  O   . HOH FA 7 .   ? 20.556  17.940  7.686   1.00 39.31  ? 437 HOH A O   1 
HETATM 9052  O  O   . HOH FA 7 .   ? 33.004  4.887   20.188  1.00 20.49  ? 438 HOH A O   1 
HETATM 9053  O  O   . HOH FA 7 .   ? 21.258  -11.780 -10.969 1.00 34.25  ? 439 HOH A O   1 
HETATM 9054  O  O   . HOH FA 7 .   ? 31.701  0.510   -4.332  1.00 41.37  ? 440 HOH A O   1 
HETATM 9055  O  O   . HOH FA 7 .   ? 10.610  6.160   15.375  1.00 12.34  ? 441 HOH A O   1 
HETATM 9056  O  O   . HOH FA 7 .   ? 15.420  16.812  31.182  1.00 50.04  ? 442 HOH A O   1 
HETATM 9057  O  O   . HOH FA 7 .   ? 19.305  9.602   32.313  1.00 19.35  ? 443 HOH A O   1 
HETATM 9058  O  O   . HOH FA 7 .   ? 35.231  -1.080  30.525  1.00 29.67  ? 444 HOH A O   1 
HETATM 9059  O  O   . HOH FA 7 .   ? 39.544  -12.717 19.761  1.00 21.64  ? 445 HOH A O   1 
HETATM 9060  O  O   . HOH FA 7 .   ? 28.053  -2.556  37.036  1.00 34.89  ? 446 HOH A O   1 
HETATM 9061  O  O   . HOH FA 7 .   ? 3.968   -9.250  3.048   1.00 22.29  ? 447 HOH A O   1 
HETATM 9062  O  O   . HOH FA 7 .   ? 15.433  -15.465 2.549   1.00 24.01  ? 448 HOH A O   1 
HETATM 9063  O  O   . HOH FA 7 .   ? 18.061  -15.174 6.104   1.00 20.51  ? 449 HOH A O   1 
HETATM 9064  O  O   . HOH FA 7 .   ? 39.441  4.578   15.107  1.00 34.73  ? 450 HOH A O   1 
HETATM 9065  O  O   . HOH FA 7 .   ? 23.714  -16.237 29.539  1.00 27.07  ? 451 HOH A O   1 
HETATM 9066  O  O   . HOH FA 7 .   ? 10.490  -3.344  2.720   1.00 13.09  ? 452 HOH A O   1 
HETATM 9067  O  O   . HOH FA 7 .   ? 39.592  -13.723 7.814   1.00 39.48  ? 453 HOH A O   1 
HETATM 9068  O  O   . HOH FA 7 .   ? 46.925  -3.848  9.899   1.00 25.82  ? 454 HOH A O   1 
HETATM 9069  O  O   . HOH FA 7 .   ? 35.736  -14.844 3.956   1.00 27.50  ? 455 HOH A O   1 
HETATM 9070  O  O   . HOH FA 7 .   ? 41.923  2.406   0.955   1.00 18.04  ? 456 HOH A O   1 
HETATM 9071  O  O   . HOH FA 7 .   ? 6.460   15.737  16.053  1.00 24.78  ? 457 HOH A O   1 
HETATM 9072  O  O   . HOH FA 7 .   ? 28.090  8.781   17.157  1.00 36.45  ? 458 HOH A O   1 
HETATM 9073  O  O   . HOH FA 7 .   ? 30.316  14.506  4.534   1.00 34.64  ? 459 HOH A O   1 
HETATM 9074  O  O   . HOH FA 7 .   ? 12.489  14.472  2.426   1.00 13.20  ? 460 HOH A O   1 
HETATM 9075  O  O   . HOH FA 7 .   ? 36.567  -4.212  -0.825  1.00 21.37  ? 461 HOH A O   1 
HETATM 9076  O  O   . HOH FA 7 .   ? 31.650  5.448   32.497  1.00 35.58  ? 462 HOH A O   1 
HETATM 9077  O  O   . HOH FA 7 .   ? 10.272  -9.025  -8.029  1.00 38.84  ? 463 HOH A O   1 
HETATM 9078  O  O   . HOH FA 7 .   ? 9.239   11.421  1.191   1.00 14.69  ? 464 HOH A O   1 
HETATM 9079  O  O   . HOH FA 7 .   ? 12.106  -10.576 27.219  1.00 15.96  ? 465 HOH A O   1 
HETATM 9080  O  O   . HOH FA 7 .   ? 17.904  -16.189 -3.745  1.00 43.32  ? 466 HOH A O   1 
HETATM 9081  O  O   . HOH FA 7 .   ? 9.464   -14.349 1.633   1.00 35.64  ? 467 HOH A O   1 
HETATM 9082  O  O   . HOH FA 7 .   ? 18.981  11.859  -0.666  1.00 18.74  ? 468 HOH A O   1 
HETATM 9083  O  O   . HOH FA 7 .   ? 28.406  -4.164  2.601   1.00 10.91  ? 469 HOH A O   1 
HETATM 9084  O  O   . HOH FA 7 .   ? 36.852  -15.277 6.363   1.00 33.90  ? 470 HOH A O   1 
HETATM 9085  O  O   . HOH FA 7 .   ? 27.630  -21.213 24.489  1.00 30.52  ? 471 HOH A O   1 
HETATM 9086  O  O   . HOH FA 7 .   ? 26.083  11.818  6.649   1.00 23.40  ? 472 HOH A O   1 
HETATM 9087  O  O   . HOH FA 7 .   ? 22.882  14.864  13.122  1.00 38.90  ? 473 HOH A O   1 
HETATM 9088  O  O   . HOH FA 7 .   ? 41.011  -10.423 9.663   1.00 16.35  ? 474 HOH A O   1 
HETATM 9089  O  O   . HOH FA 7 .   ? 10.266  4.753   8.750   1.00 11.04  ? 475 HOH A O   1 
HETATM 9090  O  O   . HOH FA 7 .   ? 36.282  -7.197  26.340  1.00 20.52  ? 476 HOH A O   1 
HETATM 9091  O  O   . HOH FA 7 .   ? 25.604  -18.488 12.495  1.00 22.86  ? 477 HOH A O   1 
HETATM 9092  O  O   . HOH FA 7 .   ? 10.962  -4.463  -5.118  1.00 26.41  ? 478 HOH A O   1 
HETATM 9093  O  O   . HOH FA 7 .   ? 37.169  10.217  23.825  1.00 37.54  ? 479 HOH A O   1 
HETATM 9094  O  O   . HOH FA 7 .   ? 9.562   -5.039  16.577  1.00 29.07  ? 480 HOH A O   1 
HETATM 9095  O  O   . HOH FA 7 .   ? 12.681  -12.324 16.379  1.00 20.02  ? 481 HOH A O   1 
HETATM 9096  O  O   . HOH FA 7 .   ? 13.866  1.611   -0.211  1.00 16.74  ? 482 HOH A O   1 
HETATM 9097  O  O   . HOH FA 7 .   ? 15.206  -6.892  21.073  1.00 11.02  ? 483 HOH A O   1 
HETATM 9098  O  O   . HOH FA 7 .   ? 20.871  3.994   16.407  1.00 20.88  ? 484 HOH A O   1 
HETATM 9099  O  O   . HOH FA 7 .   ? 32.843  6.734   15.860  1.00 25.97  ? 485 HOH A O   1 
HETATM 9100  O  O   . HOH FA 7 .   ? 33.813  -13.519 26.552  1.00 26.34  ? 486 HOH A O   1 
HETATM 9101  O  O   . HOH FA 7 .   ? 19.927  -19.629 8.581   1.00 41.89  ? 487 HOH A O   1 
HETATM 9102  O  O   . HOH FA 7 .   ? 38.526  4.012   11.338  1.00 18.39  ? 488 HOH A O   1 
HETATM 9103  O  O   . HOH FA 7 .   ? 11.358  5.291   2.238   1.00 10.24  ? 489 HOH A O   1 
HETATM 9104  O  O   . HOH FA 7 .   ? 17.089  0.732   -0.482  1.00 15.14  ? 490 HOH A O   1 
HETATM 9105  O  O   . HOH FA 7 .   ? 22.490  7.106   -4.143  1.00 32.19  ? 491 HOH A O   1 
HETATM 9106  O  O   . HOH FA 7 .   ? 20.767  -10.041 31.778  1.00 18.34  ? 492 HOH A O   1 
HETATM 9107  O  O   . HOH FA 7 .   ? 12.431  -2.684  10.997  1.00 8.61   ? 493 HOH A O   1 
HETATM 9108  O  O   . HOH FA 7 .   ? 39.202  -15.764 16.671  1.00 30.00  ? 494 HOH A O   1 
HETATM 9109  O  O   . HOH FA 7 .   ? 13.913  -16.080 26.895  1.00 30.40  ? 495 HOH A O   1 
HETATM 9110  O  O   . HOH FA 7 .   ? 32.189  -17.001 10.286  1.00 29.65  ? 496 HOH A O   1 
HETATM 9111  O  O   . HOH FA 7 .   ? 41.845  -9.022  24.199  1.00 37.69  ? 497 HOH A O   1 
HETATM 9112  O  O   . HOH FA 7 .   ? 39.800  7.426   9.013   1.00 37.10  ? 498 HOH A O   1 
HETATM 9113  O  O   . HOH FA 7 .   ? 32.727  -16.093 12.808  1.00 27.37  ? 499 HOH A O   1 
HETATM 9114  O  O   . HOH FA 7 .   ? 32.713  6.593   13.066  1.00 25.65  ? 500 HOH A O   1 
HETATM 9115  O  O   . HOH FA 7 .   ? 39.764  -12.215 11.484  1.00 18.41  ? 501 HOH A O   1 
HETATM 9116  O  O   . HOH FA 7 .   ? 13.960  1.882   -2.874  1.00 20.22  ? 502 HOH A O   1 
HETATM 9117  O  O   . HOH FA 7 .   ? 24.960  -0.299  31.780  1.00 21.46  ? 503 HOH A O   1 
HETATM 9118  O  O   . HOH FA 7 .   ? 29.099  -16.938 14.823  1.00 23.58  ? 504 HOH A O   1 
HETATM 9119  O  O   . HOH FA 7 .   ? 33.644  1.903   -5.503  1.00 33.30  ? 505 HOH A O   1 
HETATM 9120  O  O   . HOH FA 7 .   ? 20.426  15.400  2.003   1.00 31.37  ? 506 HOH A O   1 
HETATM 9121  O  O   . HOH FA 7 .   ? 13.699  16.422  11.784  1.00 14.97  ? 507 HOH A O   1 
HETATM 9122  O  O   . HOH FA 7 .   ? 7.488   -6.809  2.316   1.00 23.75  ? 508 HOH A O   1 
HETATM 9123  O  O   . HOH FA 7 .   ? 13.086  14.031  14.180  1.00 22.34  ? 509 HOH A O   1 
HETATM 9124  O  O   . HOH FA 7 .   ? 11.052  -5.070  0.644   1.00 19.40  ? 510 HOH A O   1 
HETATM 9125  O  O   . HOH FA 7 .   ? 26.609  13.583  24.772  1.00 46.05  ? 511 HOH A O   1 
HETATM 9126  O  O   . HOH FA 7 .   ? 15.904  -12.210 26.795  1.00 15.55  ? 512 HOH A O   1 
HETATM 9127  O  O   . HOH FA 7 .   ? 19.669  -0.716  26.630  1.00 13.26  ? 513 HOH A O   1 
HETATM 9128  O  O   . HOH FA 7 .   ? 33.638  -15.352 8.481   1.00 30.64  ? 514 HOH A O   1 
HETATM 9129  O  O   . HOH FA 7 .   ? 16.649  -18.392 12.341  1.00 25.40  ? 515 HOH A O   1 
HETATM 9130  O  O   . HOH FA 7 .   ? 15.717  14.221  27.753  1.00 45.28  ? 516 HOH A O   1 
HETATM 9131  O  O   . HOH FA 7 .   ? 24.474  -7.622  -7.609  1.00 41.51  ? 517 HOH A O   1 
HETATM 9132  O  O   . HOH FA 7 .   ? 30.382  -8.793  -2.527  1.00 17.17  ? 518 HOH A O   1 
HETATM 9133  O  O   . HOH FA 7 .   ? 41.409  -3.769  -0.176  1.00 36.32  ? 519 HOH A O   1 
HETATM 9134  O  O   . HOH FA 7 .   ? 5.016   1.448   -10.653 1.00 39.30  ? 520 HOH A O   1 
HETATM 9135  O  O   . HOH FA 7 .   ? 34.731  -6.610  30.643  1.00 44.98  ? 521 HOH A O   1 
HETATM 9136  O  O   . HOH FA 7 .   ? 27.122  -15.781 -5.649  1.00 27.16  ? 522 HOH A O   1 
HETATM 9137  O  O   . HOH FA 7 .   ? 29.847  -15.592 -1.754  1.00 21.76  ? 523 HOH A O   1 
HETATM 9138  O  O   . HOH FA 7 .   ? 26.035  -18.563 20.504  1.00 18.35  ? 524 HOH A O   1 
HETATM 9139  O  O   . HOH FA 7 .   ? 33.077  -15.001 3.550   1.00 28.02  ? 525 HOH A O   1 
HETATM 9140  O  O   . HOH FA 7 .   ? 12.046  -17.010 4.894   1.00 46.95  ? 526 HOH A O   1 
HETATM 9141  O  O   . HOH FA 7 .   ? 8.627   2.937   7.334   1.00 8.49   ? 527 HOH A O   1 
HETATM 9142  O  O   . HOH FA 7 .   ? 26.007  10.911  30.959  1.00 22.24  ? 528 HOH A O   1 
HETATM 9143  O  O   . HOH FA 7 .   ? 23.034  -12.351 9.679   1.00 9.55   ? 529 HOH A O   1 
HETATM 9144  O  O   . HOH FA 7 .   ? 11.368  -6.471  -7.941  1.00 28.83  ? 530 HOH A O   1 
HETATM 9145  O  O   . HOH FA 7 .   ? 19.350  14.174  5.154   1.00 12.81  ? 531 HOH A O   1 
HETATM 9146  O  O   . HOH FA 7 .   ? 17.691  7.935   19.704  1.00 29.63  ? 532 HOH A O   1 
HETATM 9147  O  O   . HOH FA 7 .   ? 8.145   -10.545 26.477  1.00 21.60  ? 533 HOH A O   1 
HETATM 9148  O  O   . HOH FA 7 .   ? 11.919  -15.307 8.419   1.00 18.74  ? 534 HOH A O   1 
HETATM 9149  O  O   . HOH FA 7 .   ? 25.683  -11.502 -12.540 1.00 34.91  ? 535 HOH A O   1 
HETATM 9150  O  O   . HOH FA 7 .   ? 28.607  2.430   -1.337  1.00 25.05  ? 536 HOH A O   1 
HETATM 9151  O  O   . HOH FA 7 .   ? 26.387  5.597   -3.510  1.00 27.87  ? 537 HOH A O   1 
HETATM 9152  O  O   . HOH FA 7 .   ? 31.447  -13.186 2.460   1.00 23.90  ? 538 HOH A O   1 
HETATM 9153  O  O   . HOH FA 7 .   ? 11.347  3.886   -0.056  1.00 18.67  ? 539 HOH A O   1 
HETATM 9154  O  O   . HOH FA 7 .   ? 9.873   -2.556  27.581  1.00 46.21  ? 540 HOH A O   1 
HETATM 9155  O  O   . HOH FA 7 .   ? 5.484   -11.995 13.289  1.00 16.70  ? 541 HOH A O   1 
HETATM 9156  O  O   . HOH FA 7 .   ? 18.136  12.435  20.819  1.00 33.59  ? 542 HOH A O   1 
HETATM 9157  O  O   . HOH FA 7 .   ? 6.027   11.679  7.957   1.00 10.40  ? 543 HOH A O   1 
HETATM 9158  O  O   . HOH FA 7 .   ? 29.284  -8.365  -8.234  1.00 40.54  ? 544 HOH A O   1 
HETATM 9159  O  O   . HOH FA 7 .   ? 45.043  -4.669  7.457   1.00 24.86  ? 545 HOH A O   1 
HETATM 9160  O  O   . HOH FA 7 .   ? 7.356   4.920   11.239  1.00 10.02  ? 546 HOH A O   1 
HETATM 9161  O  O   . HOH FA 7 .   ? 7.972   -1.986  15.060  1.00 25.29  ? 547 HOH A O   1 
HETATM 9162  O  O   . HOH FA 7 .   ? 15.849  4.412   21.589  1.00 23.99  ? 548 HOH A O   1 
HETATM 9163  O  O   . HOH FA 7 .   ? 36.243  -3.011  -11.680 1.00 29.70  ? 549 HOH A O   1 
HETATM 9164  O  O   . HOH FA 7 .   ? 13.698  -12.576 20.733  1.00 14.86  ? 550 HOH A O   1 
HETATM 9165  O  O   . HOH FA 7 .   ? 31.741  -16.952 20.514  1.00 28.94  ? 551 HOH A O   1 
HETATM 9166  O  O   . HOH FA 7 .   ? 11.003  11.130  8.111   1.00 10.90  ? 552 HOH A O   1 
HETATM 9167  O  O   . HOH FA 7 .   ? 38.096  -7.787  24.363  1.00 23.08  ? 553 HOH A O   1 
HETATM 9168  O  O   . HOH FA 7 .   ? 10.961  2.294   28.919  1.00 56.91  ? 554 HOH A O   1 
HETATM 9169  O  O   . HOH FA 7 .   ? 17.395  0.130   28.612  1.00 16.98  ? 555 HOH A O   1 
HETATM 9170  O  O   . HOH FA 7 .   ? 12.458  4.771   29.673  1.00 38.63  ? 556 HOH A O   1 
HETATM 9171  O  O   . HOH FA 7 .   ? 8.726   -6.441  7.351   1.00 15.95  ? 557 HOH A O   1 
HETATM 9172  O  O   . HOH FA 7 .   ? 41.543  7.147   3.104   1.00 33.80  ? 558 HOH A O   1 
HETATM 9173  O  O   . HOH FA 7 .   ? 14.435  4.380   -4.030  1.00 18.84  ? 559 HOH A O   1 
HETATM 9174  O  O   . HOH FA 7 .   ? 29.113  -15.001 16.897  1.00 16.51  ? 560 HOH A O   1 
HETATM 9175  O  O   . HOH FA 7 .   ? 11.427  1.559   -4.087  1.00 27.14  ? 561 HOH A O   1 
HETATM 9176  O  O   . HOH FA 7 .   ? 33.539  16.948  1.547   1.00 59.85  ? 562 HOH A O   1 
HETATM 9177  O  O   . HOH FA 7 .   ? 10.167  -4.197  19.386  1.00 18.05  ? 563 HOH A O   1 
HETATM 9178  O  O   . HOH FA 7 .   ? 9.611   -5.383  -1.535  1.00 33.78  ? 564 HOH A O   1 
HETATM 9179  O  O   . HOH FA 7 .   ? 22.335  -19.528 12.382  1.00 31.46  ? 565 HOH A O   1 
HETATM 9180  O  O   . HOH FA 7 .   ? 19.320  -18.451 26.154  1.00 25.13  ? 566 HOH A O   1 
HETATM 9181  O  O   . HOH FA 7 .   ? 14.630  -12.470 29.335  1.00 17.67  ? 567 HOH A O   1 
HETATM 9182  O  O   . HOH FA 7 .   ? 20.868  -2.595  -5.254  1.00 26.95  ? 568 HOH A O   1 
HETATM 9183  O  O   . HOH FA 7 .   ? 42.961  9.531   5.648   1.00 44.61  ? 569 HOH A O   1 
HETATM 9184  O  O   . HOH FA 7 .   ? 17.727  9.561   0.183   1.00 12.08  ? 570 HOH A O   1 
HETATM 9185  O  O   . HOH FA 7 .   ? 31.549  -2.281  -4.605  1.00 27.09  ? 571 HOH A O   1 
HETATM 9186  O  O   . HOH FA 7 .   ? 8.426   -2.416  20.753  1.00 40.00  ? 572 HOH A O   1 
HETATM 9187  O  O   . HOH FA 7 .   ? 31.090  -20.993 8.600   1.00 29.35  ? 573 HOH A O   1 
HETATM 9188  O  O   . HOH FA 7 .   ? 43.205  -5.912  0.965   1.00 35.40  ? 574 HOH A O   1 
HETATM 9189  O  O   . HOH FA 7 .   ? 32.266  -16.810 17.192  1.00 32.73  ? 575 HOH A O   1 
HETATM 9190  O  O   . HOH FA 7 .   ? 31.959  -18.291 6.945   1.00 27.87  ? 576 HOH A O   1 
HETATM 9191  O  O   . HOH FA 7 .   ? 37.384  16.049  4.521   1.00 47.44  ? 577 HOH A O   1 
HETATM 9192  O  O   . HOH FA 7 .   ? 9.286   -10.824 14.096  1.00 25.88  ? 578 HOH A O   1 
HETATM 9193  O  O   . HOH FA 7 .   ? 7.689   9.064   14.189  1.00 16.53  ? 579 HOH A O   1 
HETATM 9194  O  O   . HOH FA 7 .   ? 11.950  7.440   8.666   1.00 10.74  ? 580 HOH A O   1 
HETATM 9195  O  O   . HOH FA 7 .   ? 18.107  9.852   21.989  1.00 34.89  ? 581 HOH A O   1 
HETATM 9196  O  O   . HOH FA 7 .   ? 44.069  -9.734  8.040   1.00 25.62  ? 582 HOH A O   1 
HETATM 9197  O  O   . HOH FA 7 .   ? 33.101  8.883   21.331  1.00 36.65  ? 583 HOH A O   1 
HETATM 9198  O  O   . HOH FA 7 .   ? 13.199  0.967   -9.036  1.00 37.28  ? 584 HOH A O   1 
HETATM 9199  O  O   . HOH FA 7 .   ? 27.346  -5.446  -5.168  1.00 22.17  ? 585 HOH A O   1 
HETATM 9200  O  O   . HOH FA 7 .   ? 38.429  -13.290 5.323   1.00 23.95  ? 586 HOH A O   1 
HETATM 9201  O  O   . HOH FA 7 .   ? 26.028  -17.846 17.361  1.00 20.89  ? 587 HOH A O   1 
HETATM 9202  O  O   . HOH FA 7 .   ? 28.256  3.762   33.246  1.00 25.97  ? 588 HOH A O   1 
HETATM 9203  O  O   . HOH FA 7 .   ? 23.417  3.329   -2.004  1.00 16.97  ? 589 HOH A O   1 
HETATM 9204  O  O   . HOH FA 7 .   ? 17.251  -3.599  -8.274  1.00 30.99  ? 590 HOH A O   1 
HETATM 9205  O  O   . HOH FA 7 .   ? 28.139  -4.843  31.278  1.00 24.61  ? 591 HOH A O   1 
HETATM 9206  O  O   . HOH FA 7 .   ? 19.500  9.165   35.173  1.00 30.64  ? 592 HOH A O   1 
HETATM 9207  O  O   . HOH FA 7 .   ? 9.691   -2.572  10.414  1.00 16.31  ? 593 HOH A O   1 
HETATM 9208  O  O   . HOH FA 7 .   ? 24.162  -21.959 18.403  1.00 45.10  ? 594 HOH A O   1 
HETATM 9209  O  O   . HOH FA 7 .   ? 45.382  1.450   22.309  1.00 41.45  ? 595 HOH A O   1 
HETATM 9210  O  O   . HOH FA 7 .   ? 38.686  6.133   18.888  1.00 33.18  ? 596 HOH A O   1 
HETATM 9211  O  O   . HOH FA 7 .   ? 15.391  13.852  -0.414  1.00 24.41  ? 597 HOH A O   1 
HETATM 9212  O  O   . HOH FA 7 .   ? 7.799   -7.157  16.871  1.00 18.21  ? 598 HOH A O   1 
HETATM 9213  O  O   . HOH FA 7 .   ? 15.182  -14.430 19.171  1.00 14.76  ? 599 HOH A O   1 
HETATM 9214  O  O   . HOH FA 7 .   ? 30.942  10.315  15.987  1.00 34.79  ? 600 HOH A O   1 
HETATM 9215  O  O   . HOH FA 7 .   ? 8.901   -13.749 14.080  1.00 41.04  ? 601 HOH A O   1 
HETATM 9216  O  O   . HOH FA 7 .   ? 11.556  2.402   -6.928  1.00 33.92  ? 602 HOH A O   1 
HETATM 9217  O  O   . HOH FA 7 .   ? 14.954  -15.799 14.946  1.00 18.94  ? 603 HOH A O   1 
HETATM 9218  O  O   . HOH FA 7 .   ? 39.771  -12.079 22.794  1.00 36.90  ? 604 HOH A O   1 
HETATM 9219  O  O   . HOH FA 7 .   ? 16.679  -0.212  31.427  1.00 33.66  ? 605 HOH A O   1 
HETATM 9220  O  O   . HOH FA 7 .   ? 43.310  -9.566  11.165  1.00 21.06  ? 606 HOH A O   1 
HETATM 9221  O  O   . HOH FA 7 .   ? 29.541  12.143  -4.463  1.00 38.85  ? 607 HOH A O   1 
HETATM 9222  O  O   . HOH FA 7 .   ? 29.747  10.026  33.760  1.00 34.75  ? 608 HOH A O   1 
HETATM 9223  O  O   . HOH FA 7 .   ? 7.401   -15.559 7.333   1.00 31.72  ? 609 HOH A O   1 
HETATM 9224  O  O   . HOH FA 7 .   ? 25.588  -15.951 6.538   1.00 12.09  ? 610 HOH A O   1 
HETATM 9225  O  O   . HOH FA 7 .   ? 37.217  0.921   30.150  1.00 33.31  ? 611 HOH A O   1 
HETATM 9226  O  O   . HOH FA 7 .   ? 8.921   4.008   2.641   1.00 13.08  ? 612 HOH A O   1 
HETATM 9227  O  O   . HOH FA 7 .   ? 24.839  16.144  2.405   1.00 31.09  ? 613 HOH A O   1 
HETATM 9228  O  O   . HOH FA 7 .   ? 7.775   -12.742 -1.213  1.00 48.44  ? 614 HOH A O   1 
HETATM 9229  O  O   . HOH FA 7 .   ? 23.238  4.912   37.650  1.00 32.15  ? 615 HOH A O   1 
HETATM 9230  O  O   . HOH FA 7 .   ? 14.727  7.051   21.039  1.00 26.36  ? 616 HOH A O   1 
HETATM 9231  O  O   . HOH FA 7 .   ? 16.698  11.042  -3.095  1.00 21.15  ? 617 HOH A O   1 
HETATM 9232  O  O   . HOH FA 7 .   ? 18.143  5.338   20.731  1.00 20.21  ? 618 HOH A O   1 
HETATM 9233  O  O   . HOH FA 7 .   ? 17.718  -6.346  33.515  1.00 26.84  ? 619 HOH A O   1 
HETATM 9234  O  O   . HOH FA 7 .   ? 13.421  5.092   -0.549  1.00 24.46  ? 620 HOH A O   1 
HETATM 9235  O  O   . HOH FA 7 .   ? 7.383   -1.883  -0.768  1.00 21.37  ? 621 HOH A O   1 
HETATM 9236  O  O   . HOH FA 7 .   ? 11.604  7.937   1.639   1.00 14.33  ? 622 HOH A O   1 
HETATM 9237  O  O   . HOH FA 7 .   ? 39.257  3.568   19.458  1.00 26.77  ? 623 HOH A O   1 
HETATM 9238  O  O   . HOH FA 7 .   ? 23.990  12.048  0.483   1.00 23.56  ? 624 HOH A O   1 
HETATM 9239  O  O   . HOH FA 7 .   ? 27.031  -18.773 -1.271  1.00 44.24  ? 625 HOH A O   1 
HETATM 9240  O  O   . HOH FA 7 .   ? 42.252  3.091   5.291   1.00 35.64  ? 626 HOH A O   1 
HETATM 9241  O  O   . HOH FA 7 .   ? 18.870  16.731  15.635  1.00 40.20  ? 627 HOH A O   1 
HETATM 9242  O  O   . HOH FA 7 .   ? 23.773  -15.437 -11.695 1.00 30.77  ? 628 HOH A O   1 
HETATM 9243  O  O   . HOH FA 7 .   ? 24.099  -21.374 -3.283  1.00 39.53  ? 629 HOH A O   1 
HETATM 9244  O  O   . HOH FA 7 .   ? 23.338  11.961  14.665  1.00 41.18  ? 630 HOH A O   1 
HETATM 9245  O  O   . HOH FA 7 .   ? 25.016  13.868  32.946  1.00 40.11  ? 631 HOH A O   1 
HETATM 9246  O  O   . HOH FA 7 .   ? 11.415  9.545   -2.094  1.00 29.62  ? 632 HOH A O   1 
HETATM 9247  O  O   . HOH FA 7 .   ? 8.507   -0.516  24.465  1.00 20.96  ? 633 HOH A O   1 
HETATM 9248  O  O   . HOH FA 7 .   ? 23.755  14.771  4.714   1.00 23.80  ? 634 HOH A O   1 
HETATM 9249  O  O   . HOH FA 7 .   ? 45.309  -13.664 17.718  1.00 50.49  ? 635 HOH A O   1 
HETATM 9250  O  O   . HOH FA 7 .   ? 38.342  -15.464 12.201  1.00 27.42  ? 636 HOH A O   1 
HETATM 9251  O  O   . HOH FA 7 .   ? 9.356   17.149  14.876  1.00 38.72  ? 637 HOH A O   1 
HETATM 9252  O  O   . HOH FA 7 .   ? 32.466  7.648   30.796  1.00 25.52  ? 638 HOH A O   1 
HETATM 9253  O  O   . HOH FA 7 .   ? 12.304  4.238   22.295  1.00 27.88  ? 639 HOH A O   1 
HETATM 9254  O  O   . HOH FA 7 .   ? 34.546  8.636   18.882  1.00 35.99  ? 640 HOH A O   1 
HETATM 9255  O  O   . HOH FA 7 .   ? 41.609  4.381   12.839  1.00 38.42  ? 641 HOH A O   1 
HETATM 9256  O  O   . HOH FA 7 .   ? 17.596  -18.155 4.859   1.00 39.50  ? 642 HOH A O   1 
HETATM 9257  O  O   . HOH FA 7 .   ? 15.072  -13.593 16.598  1.00 13.50  ? 643 HOH A O   1 
HETATM 9258  O  O   . HOH FA 7 .   ? 31.377  -19.029 4.134   1.00 27.70  ? 644 HOH A O   1 
HETATM 9259  O  O   . HOH FA 7 .   ? 20.282  -19.079 28.652  1.00 40.99  ? 645 HOH A O   1 
HETATM 9260  O  O   . HOH FA 7 .   ? 13.073  -14.225 2.237   1.00 24.65  ? 646 HOH A O   1 
HETATM 9261  O  O   . HOH FA 7 .   ? 14.313  -2.172  28.797  1.00 21.79  ? 647 HOH A O   1 
HETATM 9262  O  O   . HOH FA 7 .   ? 6.174   -2.877  13.235  1.00 19.79  ? 648 HOH A O   1 
HETATM 9263  O  O   . HOH FA 7 .   ? 24.733  -23.338 10.777  1.00 35.10  ? 649 HOH A O   1 
HETATM 9264  O  O   . HOH FA 7 .   ? 13.146  -14.391 12.890  1.00 28.39  ? 650 HOH A O   1 
HETATM 9265  O  O   . HOH FA 7 .   ? 30.227  6.916   13.737  1.00 35.98  ? 651 HOH A O   1 
HETATM 9266  O  O   . HOH FA 7 .   ? 41.255  12.323  7.654   1.00 40.00  ? 652 HOH A O   1 
HETATM 9267  O  O   . HOH FA 7 .   ? 27.275  5.930   35.442  1.00 23.57  ? 653 HOH A O   1 
HETATM 9268  O  O   . HOH FA 7 .   ? 26.187  4.567   15.656  1.00 23.59  ? 654 HOH A O   1 
HETATM 9269  O  O   . HOH FA 7 .   ? 8.880   2.301   -8.014  1.00 36.11  ? 655 HOH A O   1 
HETATM 9270  O  O   . HOH FA 7 .   ? 7.248   -5.624  5.178   1.00 23.76  ? 656 HOH A O   1 
HETATM 9271  O  O   . HOH FA 7 .   ? 20.385  11.121  21.885  1.00 40.00  ? 657 HOH A O   1 
HETATM 9272  O  O   . HOH FA 7 .   ? 34.037  -3.823  32.111  1.00 35.12  ? 658 HOH A O   1 
HETATM 9273  O  O   . HOH FA 7 .   ? 13.348  -14.835 29.402  1.00 26.94  ? 659 HOH A O   1 
HETATM 9274  O  O   . HOH FA 7 .   ? 14.297  14.463  21.849  1.00 42.47  ? 660 HOH A O   1 
HETATM 9275  O  O   . HOH FA 7 .   ? 35.124  9.975   10.436  1.00 29.20  ? 661 HOH A O   1 
HETATM 9276  O  O   . HOH FA 7 .   ? 14.854  -17.088 19.230  1.00 45.65  ? 662 HOH A O   1 
HETATM 9277  O  O   . HOH FA 7 .   ? 7.177   -0.728  8.355   1.00 28.98  ? 663 HOH A O   1 
HETATM 9278  O  O   . HOH FA 7 .   ? 38.853  -16.370 21.196  1.00 46.13  ? 664 HOH A O   1 
HETATM 9279  O  O   . HOH FA 7 .   ? 42.144  5.323   -5.273  1.00 50.00  ? 665 HOH A O   1 
HETATM 9280  O  O   . HOH FA 7 .   ? 41.147  10.563  0.604   1.00 36.46  ? 666 HOH A O   1 
HETATM 9281  O  O   . HOH FA 7 .   ? 30.745  -1.493  -8.990  1.00 46.28  ? 667 HOH A O   1 
HETATM 9282  O  O   . HOH FA 7 .   ? 6.941   -2.404  26.063  1.00 33.43  ? 668 HOH A O   1 
HETATM 9283  O  O   . HOH FA 7 .   ? 34.037  -10.862 28.078  1.00 57.45  ? 669 HOH A O   1 
HETATM 9284  O  O   . HOH FA 7 .   ? 4.578   13.143  19.437  1.00 29.39  ? 670 HOH A O   1 
HETATM 9285  O  O   . HOH FA 7 .   ? 34.983  12.283  22.450  1.00 70.38  ? 671 HOH A O   1 
HETATM 9286  O  O   . HOH FA 7 .   ? 13.759  21.367  11.507  1.00 29.87  ? 672 HOH A O   1 
HETATM 9287  O  O   . HOH FA 7 .   ? 20.328  -23.896 -7.704  1.00 32.80  ? 673 HOH A O   1 
HETATM 9288  O  O   . HOH FA 7 .   ? 21.906  -23.799 9.770   1.00 54.24  ? 674 HOH A O   1 
HETATM 9289  O  O   . HOH FA 7 .   ? 4.273   -6.678  30.272  1.00 32.86  ? 675 HOH A O   1 
HETATM 9290  O  O   . HOH FA 7 .   ? 44.432  -3.708  -1.924  1.00 31.37  ? 676 HOH A O   1 
HETATM 9291  O  O   . HOH FA 7 .   ? 31.325  10.278  19.353  1.00 39.89  ? 677 HOH A O   1 
HETATM 9292  O  O   . HOH FA 7 .   ? 30.999  -9.446  -5.188  1.00 35.43  ? 678 HOH A O   1 
HETATM 9293  O  O   . HOH FA 7 .   ? 38.450  -5.901  29.256  1.00 38.95  ? 679 HOH A O   1 
HETATM 9294  O  O   . HOH FA 7 .   ? 21.407  -23.393 21.032  1.00 40.17  ? 680 HOH A O   1 
HETATM 9295  O  O   . HOH FA 7 .   ? 26.784  7.325   14.878  1.00 25.45  ? 681 HOH A O   1 
HETATM 9296  O  O   . HOH FA 7 .   ? 29.333  12.098  9.309   1.00 40.12  ? 682 HOH A O   1 
HETATM 9297  O  O   . HOH FA 7 .   ? 33.903  -1.288  37.303  1.00 21.70  ? 683 HOH A O   1 
HETATM 9298  O  O   . HOH FA 7 .   ? 28.756  -18.603 20.518  1.00 22.00  ? 684 HOH A O   1 
HETATM 9299  O  O   . HOH FA 7 .   ? 30.249  -17.507 18.606  1.00 36.38  ? 685 HOH A O   1 
HETATM 9300  O  O   . HOH FA 7 .   ? 39.350  -13.958 2.925   1.00 36.13  ? 686 HOH A O   1 
HETATM 9301  O  O   . HOH FA 7 .   ? 35.878  -16.146 13.148  1.00 36.98  ? 687 HOH A O   1 
HETATM 9302  O  O   . HOH FA 7 .   ? 5.915   3.127   -7.770  1.00 93.31  ? 688 HOH A O   1 
HETATM 9303  O  O   . HOH FA 7 .   ? 39.788  2.621   16.749  1.00 34.58  ? 689 HOH A O   1 
HETATM 9304  O  O   . HOH FA 7 .   ? 8.048   -3.952  11.932  1.00 36.45  ? 690 HOH A O   1 
HETATM 9305  O  O   . HOH FA 7 .   ? 6.277   -3.821  23.613  1.00 34.74  ? 691 HOH A O   1 
HETATM 9306  O  O   . HOH FA 7 .   ? 12.068  9.942   23.112  1.00 36.17  ? 692 HOH A O   1 
HETATM 9307  O  O   . HOH FA 7 .   ? 23.625  5.494   15.870  1.00 47.23  ? 693 HOH A O   1 
HETATM 9308  O  O   . HOH FA 7 .   ? 30.045  -18.110 -2.596  1.00 29.23  ? 694 HOH A O   1 
HETATM 9309  O  O   . HOH FA 7 .   ? 10.956  -14.702 17.144  1.00 33.24  ? 695 HOH A O   1 
HETATM 9310  O  O   . HOH FA 7 .   ? 20.729  -22.688 14.934  1.00 36.62  ? 696 HOH A O   1 
HETATM 9311  O  O   . HOH FA 7 .   ? 27.486  -21.423 14.959  1.00 44.80  ? 697 HOH A O   1 
HETATM 9312  O  O   . HOH FA 7 .   ? 16.999  2.303   -7.815  1.00 39.00  ? 698 HOH A O   1 
HETATM 9313  O  O   . HOH FA 7 .   ? 39.105  -3.253  -7.633  1.00 43.93  ? 699 HOH A O   1 
HETATM 9314  O  O   . HOH FA 7 .   ? 24.687  -2.746  33.028  1.00 36.37  ? 700 HOH A O   1 
HETATM 9315  O  O   . HOH FA 7 .   ? 13.160  13.539  -1.952  1.00 26.06  ? 701 HOH A O   1 
HETATM 9316  O  O   . HOH FA 7 .   ? 26.744  11.586  9.317   1.00 34.50  ? 702 HOH A O   1 
HETATM 9317  O  O   . HOH FA 7 .   ? 6.636   6.491   17.957  1.00 28.92  ? 703 HOH A O   1 
HETATM 9318  O  O   . HOH FA 7 .   ? 34.703  -17.641 17.790  1.00 44.12  ? 704 HOH A O   1 
HETATM 9319  O  O   . HOH FA 7 .   ? 29.721  -3.717  -5.672  1.00 38.69  ? 705 HOH A O   1 
HETATM 9320  O  O   . HOH FA 7 .   ? 10.379  -4.311  29.961  1.00 31.41  ? 706 HOH A O   1 
HETATM 9321  O  O   . HOH FA 7 .   ? 19.947  -20.132 12.028  1.00 114.88 ? 707 HOH A O   1 
HETATM 9322  O  O   . HOH FA 7 .   ? 30.827  3.921   34.602  1.00 25.26  ? 708 HOH A O   1 
HETATM 9323  O  O   . HOH FA 7 .   ? 5.010   -7.298  1.156   1.00 21.11  ? 709 HOH A O   1 
HETATM 9324  O  O   . HOH FA 7 .   ? 20.753  -0.238  -7.016  1.00 106.44 ? 710 HOH A O   1 
HETATM 9325  O  O   . HOH FA 7 .   ? 33.531  -17.532 2.735   1.00 30.13  ? 711 HOH A O   1 
HETATM 9326  O  O   . HOH FA 7 .   ? 26.481  -6.771  -7.739  1.00 35.97  ? 712 HOH A O   1 
HETATM 9327  O  O   . HOH FA 7 .   ? 32.694  16.364  5.146   1.00 53.19  ? 713 HOH A O   1 
HETATM 9328  O  O   . HOH FA 7 .   ? 47.264  -4.512  -0.869  1.00 20.28  ? 714 HOH A O   1 
HETATM 9329  O  O   . HOH FA 7 .   ? 41.970  -13.765 11.865  1.00 39.42  ? 715 HOH A O   1 
HETATM 9330  O  O   . HOH FA 7 .   ? 10.062  4.057   -2.466  1.00 31.46  ? 716 HOH A O   1 
HETATM 9331  O  O   . HOH FA 7 .   ? 33.965  9.341   16.063  1.00 59.22  ? 717 HOH A O   1 
HETATM 9332  O  O   . HOH FA 7 .   ? 7.920   6.503   15.548  1.00 15.75  ? 718 HOH A O   1 
HETATM 9333  O  O   . HOH FA 7 .   ? 39.403  -9.924  24.525  1.00 35.78  ? 719 HOH A O   1 
HETATM 9334  O  O   . HOH FA 7 .   ? 27.033  -18.338 14.757  1.00 32.07  ? 720 HOH A O   1 
HETATM 9335  O  O   . HOH FA 7 .   ? 23.400  -4.127  -5.491  1.00 31.33  ? 721 HOH A O   1 
HETATM 9336  O  O   . HOH FA 7 .   ? 37.432  -10.813 -4.191  1.00 35.17  ? 722 HOH A O   1 
HETATM 9337  O  O   . HOH FA 7 .   ? 27.230  -9.336  -13.467 1.00 32.55  ? 723 HOH A O   1 
HETATM 9338  O  O   . HOH FA 7 .   ? 15.270  17.975  15.734  1.00 58.25  ? 724 HOH A O   1 
HETATM 9339  O  O   . HOH FA 7 .   ? 27.056  -6.923  -11.570 1.00 35.69  ? 725 HOH A O   1 
HETATM 9340  O  O   . HOH FA 7 .   ? 12.207  -5.938  -10.383 1.00 36.38  ? 726 HOH A O   1 
HETATM 9341  O  O   . HOH FA 7 .   ? 23.598  -10.076 32.399  1.00 34.43  ? 727 HOH A O   1 
HETATM 9342  O  O   . HOH FA 7 .   ? 10.886  -15.246 13.671  1.00 34.78  ? 728 HOH A O   1 
HETATM 9343  O  O   . HOH FA 7 .   ? 30.147  -20.681 21.490  1.00 33.37  ? 729 HOH A O   1 
HETATM 9344  O  O   . HOH FA 7 .   ? 23.161  14.930  0.412   1.00 33.93  ? 730 HOH A O   1 
HETATM 9345  O  O   . HOH FA 7 .   ? 15.145  15.020  13.567  1.00 28.71  ? 731 HOH A O   1 
HETATM 9346  O  O   . HOH FA 7 .   ? 39.247  -4.015  30.032  1.00 38.98  ? 732 HOH A O   1 
HETATM 9347  O  O   . HOH FA 7 .   ? 30.310  -21.383 24.605  1.00 41.26  ? 733 HOH A O   1 
HETATM 9348  O  O   . HOH FA 7 .   ? 37.005  3.311   31.281  1.00 34.21  ? 734 HOH A O   1 
HETATM 9349  O  O   . HOH FA 7 .   ? 16.343  -16.297 7.840   1.00 29.78  ? 735 HOH A O   1 
HETATM 9350  O  O   . HOH FA 7 .   ? 32.498  -15.158 28.069  1.00 34.42  ? 736 HOH A O   1 
HETATM 9351  O  O   . HOH FA 7 .   ? 37.066  -16.395 2.280   1.00 37.13  ? 737 HOH A O   1 
HETATM 9352  O  O   . HOH FA 7 .   ? 36.463  -9.663  27.633  1.00 35.53  ? 738 HOH A O   1 
HETATM 9353  O  O   . HOH FA 7 .   ? 12.573  -3.511  30.649  1.00 27.90  ? 739 HOH A O   1 
HETATM 9354  O  O   . HOH FA 7 .   ? 33.172  9.300   12.139  1.00 34.99  ? 740 HOH A O   1 
HETATM 9355  O  O   . HOH FA 7 .   ? 13.350  -17.678 15.962  1.00 37.92  ? 741 HOH A O   1 
HETATM 9356  O  O   . HOH FA 7 .   ? 25.430  6.672   37.425  1.00 26.80  ? 742 HOH A O   1 
HETATM 9357  O  O   . HOH FA 7 .   ? 23.623  10.836  -2.069  1.00 35.75  ? 743 HOH A O   1 
HETATM 9358  O  O   . HOH FA 7 .   ? 24.253  -21.072 11.802  1.00 37.39  ? 744 HOH A O   1 
HETATM 9359  O  O   . HOH FA 7 .   ? 24.496  8.452   14.305  1.00 35.40  ? 745 HOH A O   1 
HETATM 9360  O  O   . HOH FA 7 .   ? 24.954  -5.092  31.564  1.00 36.11  ? 746 HOH A O   1 
HETATM 9361  O  O   . HOH FA 7 .   ? 31.721  9.980   31.927  1.00 33.92  ? 747 HOH A O   1 
HETATM 9362  O  O   . HOH FA 7 .   ? 25.810  14.658  6.351   1.00 36.73  ? 748 HOH A O   1 
HETATM 9363  O  O   . HOH FA 7 .   ? 9.820   -16.872 7.844   1.00 40.98  ? 749 HOH A O   1 
HETATM 9364  O  O   . HOH FA 7 .   ? 17.263  13.469  -1.848  1.00 38.20  ? 750 HOH A O   1 
HETATM 9365  O  O   . HOH FA 7 .   ? 25.267  -14.098 30.882  1.00 36.31  ? 751 HOH A O   1 
HETATM 9366  O  O   . HOH FA 7 .   ? 36.109  13.936  -1.009  1.00 47.61  ? 752 HOH A O   1 
HETATM 9367  O  O   . HOH FA 7 .   ? 21.084  11.899  -2.425  1.00 30.84  ? 753 HOH A O   1 
HETATM 9368  O  O   . HOH FA 7 .   ? 11.580  -13.093 25.865  1.00 27.49  ? 754 HOH A O   1 
HETATM 9369  O  O   . HOH FA 7 .   ? 8.099   -4.704  9.365   1.00 27.17  ? 755 HOH A O   1 
HETATM 9370  O  O   . HOH FA 7 .   ? 21.318  15.974  5.130   1.00 25.62  ? 756 HOH A O   1 
HETATM 9371  O  O   . HOH FA 7 .   ? 17.390  -18.260 9.515   1.00 38.19  ? 757 HOH A O   1 
HETATM 9372  O  O   . HOH FA 7 .   ? 19.813  7.780   -4.572  1.00 32.89  ? 758 HOH A O   1 
HETATM 9373  O  O   . HOH FA 7 .   ? 25.483  -16.670 -13.616 1.00 43.42  ? 759 HOH A O   1 
HETATM 9374  O  O   . HOH FA 7 .   ? 15.270  4.443   -6.559  1.00 36.32  ? 760 HOH A O   1 
HETATM 9375  O  O   . HOH FA 7 .   ? 4.262   13.689  22.426  1.00 34.19  ? 761 HOH A O   1 
HETATM 9376  O  O   . HOH FA 7 .   ? 30.478  -21.252 3.250   1.00 37.79  ? 762 HOH A O   1 
HETATM 9377  O  O   . HOH FA 7 .   ? 11.941  5.432   -4.114  1.00 26.95  ? 763 HOH A O   1 
HETATM 9378  O  O   . HOH FA 7 .   ? 20.765  17.814  3.506   1.00 42.63  ? 764 HOH A O   1 
HETATM 9379  O  O   . HOH FA 7 .   ? 19.158  10.294  -4.291  1.00 27.77  ? 765 HOH A O   1 
HETATM 9380  O  O   . HOH FA 7 .   ? 13.740  -16.945 7.196   1.00 25.44  ? 766 HOH A O   1 
HETATM 9381  O  O   . HOH FA 7 .   ? 12.559  -15.724 11.049  1.00 29.65  ? 767 HOH A O   1 
HETATM 9382  O  O   . HOH FA 7 .   ? 32.913  -19.483 21.064  1.00 35.11  ? 768 HOH A O   1 
HETATM 9383  O  O   . HOH FA 7 .   ? 13.565  -13.436 23.339  1.00 30.22  ? 769 HOH A O   1 
HETATM 9384  O  O   . HOH FA 7 .   ? 22.708  16.472  8.331   1.00 44.62  ? 770 HOH A O   1 
HETATM 9385  O  O   . HOH FA 7 .   ? 15.674  12.180  -5.372  1.00 48.91  ? 771 HOH A O   1 
HETATM 9386  O  O   . HOH FA 7 .   ? 13.980  -17.952 11.144  1.00 42.60  ? 772 HOH A O   1 
HETATM 9387  O  O   . HOH FA 7 .   ? 8.074   -13.182 27.724  1.00 27.29  ? 773 HOH A O   1 
HETATM 9388  O  O   . HOH FA 7 .   ? 32.930  -18.496 27.682  1.00 65.33  ? 774 HOH A O   1 
HETATM 9389  O  O   . HOH FA 7 .   ? 26.601  10.713  14.497  1.00 38.41  ? 775 HOH A O   1 
HETATM 9390  O  O   . HOH FA 7 .   ? 21.694  2.590   -6.741  1.00 37.52  ? 776 HOH A O   1 
HETATM 9391  O  O   . HOH FA 7 .   ? 38.202  -11.297 26.898  1.00 45.44  ? 777 HOH A O   1 
HETATM 9392  O  O   . HOH FA 7 .   ? 31.699  -19.893 -1.557  1.00 44.46  ? 778 HOH A O   1 
HETATM 9393  O  O   . HOH FA 7 .   ? 4.649   17.536  19.565  1.00 51.20  ? 779 HOH A O   1 
HETATM 9394  O  O   . HOH FA 7 .   ? 18.902  6.569   -6.904  1.00 38.83  ? 780 HOH A O   1 
HETATM 9395  O  O   . HOH GA 7 .   ? 8.828   14.726  8.325   1.00 25.71  ? 401 HOH B O   1 
HETATM 9396  O  O   . HOH GA 7 .   ? -8.315  14.022  0.627   1.00 46.98  ? 402 HOH B O   1 
HETATM 9397  O  O   . HOH GA 7 .   ? -11.592 -17.457 13.116  1.00 38.22  ? 403 HOH B O   1 
HETATM 9398  O  O   . HOH GA 7 .   ? -10.680 2.867   -2.608  1.00 17.52  ? 404 HOH B O   1 
HETATM 9399  O  O   . HOH GA 7 .   ? -3.208  17.240  -0.945  1.00 46.33  ? 405 HOH B O   1 
HETATM 9400  O  O   . HOH GA 7 .   ? -8.291  11.892  2.123   1.00 29.02  ? 406 HOH B O   1 
HETATM 9401  O  O   . HOH GA 7 .   ? -9.370  -1.784  -14.489 1.00 32.17  ? 407 HOH B O   1 
HETATM 9402  O  O   . HOH GA 7 .   ? -17.379 11.105  1.613   1.00 26.18  ? 408 HOH B O   1 
HETATM 9403  O  O   . HOH GA 7 .   ? 9.928   2.778   22.638  1.00 25.56  ? 409 HOH B O   1 
HETATM 9404  O  O   . HOH GA 7 .   ? -0.432  -10.882 0.842   1.00 31.44  ? 410 HOH B O   1 
HETATM 9405  O  O   . HOH GA 7 .   ? -17.100 11.046  4.390   1.00 25.27  ? 411 HOH B O   1 
HETATM 9406  O  O   . HOH GA 7 .   ? 3.203   1.403   -12.574 1.00 47.48  ? 412 HOH B O   1 
HETATM 9407  O  O   . HOH GA 7 .   ? -21.157 11.324  6.029   1.00 26.68  ? 413 HOH B O   1 
HETATM 9408  O  O   . HOH GA 7 .   ? -28.847 -6.713  15.498  1.00 63.24  ? 414 HOH B O   1 
HETATM 9409  O  O   . HOH GA 7 .   ? -27.131 -3.579  -5.879  1.00 25.80  ? 415 HOH B O   1 
HETATM 9410  O  O   . HOH GA 7 .   ? -0.092  16.735  -11.134 1.00 26.63  ? 416 HOH B O   1 
HETATM 9411  O  O   . HOH GA 7 .   ? -29.241 0.772   16.987  1.00 30.85  ? 417 HOH B O   1 
HETATM 9412  O  O   . HOH GA 7 .   ? -18.423 8.390   -13.816 1.00 31.38  ? 418 HOH B O   1 
HETATM 9413  O  O   . HOH GA 7 .   ? -3.663  13.954  -7.112  1.00 28.09  ? 419 HOH B O   1 
HETATM 9414  O  O   . HOH GA 7 .   ? -0.810  18.213  0.501   1.00 39.70  ? 420 HOH B O   1 
HETATM 9415  O  O   . HOH GA 7 .   ? -10.805 16.828  -18.800 1.00 32.05  ? 421 HOH B O   1 
HETATM 9416  O  O   . HOH GA 7 .   ? -10.704 7.981   2.114   1.00 24.39  ? 422 HOH B O   1 
HETATM 9417  O  O   . HOH GA 7 .   ? -18.472 7.056   23.272  1.00 43.33  ? 423 HOH B O   1 
HETATM 9418  O  O   . HOH GA 7 .   ? 2.844   15.674  -5.117  1.00 36.77  ? 424 HOH B O   1 
HETATM 9419  O  O   . HOH GA 7 .   ? 7.773   11.874  14.849  1.00 21.20  ? 425 HOH B O   1 
HETATM 9420  O  O   . HOH GA 7 .   ? -21.443 -9.850  9.758   1.00 33.74  ? 426 HOH B O   1 
HETATM 9421  O  O   . HOH GA 7 .   ? -4.547  16.177  13.936  1.00 38.03  ? 427 HOH B O   1 
HETATM 9422  O  O   . HOH GA 7 .   ? -27.826 6.987   19.546  1.00 43.43  ? 428 HOH B O   1 
HETATM 9423  O  O   . HOH GA 7 .   ? -0.689  4.113   -16.889 1.00 35.92  ? 429 HOH B O   1 
HETATM 9424  O  O   . HOH GA 7 .   ? -2.613  5.110   3.995   1.00 10.08  ? 430 HOH B O   1 
HETATM 9425  O  O   . HOH GA 7 .   ? -2.666  -8.384  -9.127  1.00 36.54  ? 431 HOH B O   1 
HETATM 9426  O  O   . HOH GA 7 .   ? -3.578  19.152  -20.080 1.00 29.50  ? 432 HOH B O   1 
HETATM 9427  O  O   . HOH GA 7 .   ? -11.432 -17.083 26.126  1.00 41.65  ? 433 HOH B O   1 
HETATM 9428  O  O   . HOH GA 7 .   ? -26.304 9.062   16.434  1.00 22.94  ? 434 HOH B O   1 
HETATM 9429  O  O   . HOH GA 7 .   ? -19.676 -7.483  -11.876 1.00 29.02  ? 435 HOH B O   1 
HETATM 9430  O  O   . HOH GA 7 .   ? -4.119  16.163  -11.305 1.00 16.46  ? 436 HOH B O   1 
HETATM 9431  O  O   . HOH GA 7 .   ? -5.606  -11.567 -15.073 1.00 35.10  ? 437 HOH B O   1 
HETATM 9432  O  O   . HOH GA 7 .   ? -3.888  12.605  -18.289 1.00 15.51  ? 438 HOH B O   1 
HETATM 9433  O  O   . HOH GA 7 .   ? -13.639 13.583  -2.689  1.00 47.48  ? 439 HOH B O   1 
HETATM 9434  O  O   . HOH GA 7 .   ? -20.165 -11.839 8.108   1.00 25.54  ? 440 HOH B O   1 
HETATM 9435  O  O   . HOH GA 7 .   ? -12.322 16.602  7.054   1.00 38.46  ? 441 HOH B O   1 
HETATM 9436  O  O   . HOH GA 7 .   ? 7.858   0.936   19.612  1.00 29.10  ? 442 HOH B O   1 
HETATM 9437  O  O   . HOH GA 7 .   ? -3.203  -12.916 15.465  1.00 30.63  ? 443 HOH B O   1 
HETATM 9438  O  O   . HOH GA 7 .   ? -15.581 16.386  -8.391  1.00 41.00  ? 444 HOH B O   1 
HETATM 9439  O  O   . HOH GA 7 .   ? -21.024 -5.165  21.751  1.00 26.66  ? 445 HOH B O   1 
HETATM 9440  O  O   . HOH GA 7 .   ? 1.665   6.481   -8.157  1.00 19.10  ? 446 HOH B O   1 
HETATM 9441  O  O   . HOH GA 7 .   ? -17.580 13.326  -4.149  1.00 33.00  ? 447 HOH B O   1 
HETATM 9442  O  O   . HOH GA 7 .   ? -14.589 13.665  -16.329 1.00 44.23  ? 448 HOH B O   1 
HETATM 9443  O  O   . HOH GA 7 .   ? -5.796  -12.550 11.842  1.00 15.48  ? 449 HOH B O   1 
HETATM 9444  O  O   . HOH GA 7 .   ? -1.661  20.695  7.695   1.00 43.25  ? 450 HOH B O   1 
HETATM 9445  O  O   . HOH GA 7 .   ? -25.192 -4.281  20.913  1.00 35.35  ? 451 HOH B O   1 
HETATM 9446  O  O   . HOH GA 7 .   ? 5.822   12.219  -4.278  1.00 16.40  ? 452 HOH B O   1 
HETATM 9447  O  O   . HOH GA 7 .   ? 6.810   -11.470 17.378  1.00 20.04  ? 453 HOH B O   1 
HETATM 9448  O  O   . HOH GA 7 .   ? -0.694  -14.659 13.336  1.00 51.38  ? 454 HOH B O   1 
HETATM 9449  O  O   . HOH GA 7 .   ? 7.294   -11.342 24.051  1.00 27.38  ? 455 HOH B O   1 
HETATM 9450  O  O   . HOH GA 7 .   ? 5.845   -9.396  13.477  1.00 14.28  ? 456 HOH B O   1 
HETATM 9451  O  O   . HOH GA 7 .   ? -20.058 -12.141 -2.541  1.00 23.86  ? 457 HOH B O   1 
HETATM 9452  O  O   . HOH GA 7 .   ? -21.912 1.568   18.565  1.00 21.41  ? 458 HOH B O   1 
HETATM 9453  O  O   . HOH GA 7 .   ? 6.264   16.685  0.912   1.00 21.53  ? 459 HOH B O   1 
HETATM 9454  O  O   . HOH GA 7 .   ? 3.737   3.461   -2.362  1.00 15.62  ? 460 HOH B O   1 
HETATM 9455  O  O   . HOH GA 7 .   ? -19.195 -16.577 -4.392  1.00 46.12  ? 461 HOH B O   1 
HETATM 9456  O  O   . HOH GA 7 .   ? 9.146   7.138   8.468   1.00 14.67  ? 462 HOH B O   1 
HETATM 9457  O  O   . HOH GA 7 .   ? -26.665 -7.072  -1.755  1.00 22.07  ? 463 HOH B O   1 
HETATM 9458  O  O   . HOH GA 7 .   ? 4.174   12.976  -18.518 1.00 32.03  ? 464 HOH B O   1 
HETATM 9459  O  O   . HOH GA 7 .   ? -5.521  6.412   0.511   1.00 18.61  ? 465 HOH B O   1 
HETATM 9460  O  O   . HOH GA 7 .   ? -20.778 -11.201 5.413   1.00 35.50  ? 466 HOH B O   1 
HETATM 9461  O  O   . HOH GA 7 .   ? -21.574 -2.473  -12.818 1.00 37.76  ? 467 HOH B O   1 
HETATM 9462  O  O   . HOH GA 7 .   ? -27.042 -7.556  10.257  1.00 38.82  ? 468 HOH B O   1 
HETATM 9463  O  O   . HOH GA 7 .   ? -17.200 -0.232  23.485  1.00 40.06  ? 469 HOH B O   1 
HETATM 9464  O  O   . HOH GA 7 .   ? -16.527 9.654   20.609  1.00 32.03  ? 470 HOH B O   1 
HETATM 9465  O  O   . HOH GA 7 .   ? -13.386 -6.845  -11.164 1.00 16.19  ? 471 HOH B O   1 
HETATM 9466  O  O   . HOH GA 7 .   ? -12.258 -6.385  30.257  1.00 32.86  ? 472 HOH B O   1 
HETATM 9467  O  O   . HOH GA 7 .   ? 5.147   6.371   1.009   1.00 10.62  ? 473 HOH B O   1 
HETATM 9468  O  O   . HOH GA 7 .   ? -20.613 -15.647 4.520   1.00 51.45  ? 474 HOH B O   1 
HETATM 9469  O  O   . HOH GA 7 .   ? -13.932 0.342   14.917  1.00 9.23   ? 475 HOH B O   1 
HETATM 9470  O  O   . HOH GA 7 .   ? -4.516  11.278  -14.976 1.00 16.48  ? 476 HOH B O   1 
HETATM 9471  O  O   . HOH GA 7 .   ? -25.192 13.371  14.245  1.00 36.30  ? 477 HOH B O   1 
HETATM 9472  O  O   . HOH GA 7 .   ? -5.623  1.578   -9.788  1.00 12.33  ? 478 HOH B O   1 
HETATM 9473  O  O   . HOH GA 7 .   ? -17.372 -12.593 3.298   1.00 18.51  ? 479 HOH B O   1 
HETATM 9474  O  O   . HOH GA 7 .   ? 3.801   11.174  -14.404 1.00 39.89  ? 480 HOH B O   1 
HETATM 9475  O  O   . HOH GA 7 .   ? 1.431   14.378  -11.203 1.00 18.90  ? 481 HOH B O   1 
HETATM 9476  O  O   . HOH GA 7 .   ? 4.373   6.423   14.171  1.00 10.86  ? 482 HOH B O   1 
HETATM 9477  O  O   . HOH GA 7 .   ? -27.132 -10.080 1.554   1.00 24.06  ? 483 HOH B O   1 
HETATM 9478  O  O   . HOH GA 7 .   ? 3.958   -2.275  -3.243  1.00 24.76  ? 484 HOH B O   1 
HETATM 9479  O  O   . HOH GA 7 .   ? -21.681 -8.740  -8.508  1.00 19.64  ? 485 HOH B O   1 
HETATM 9480  O  O   . HOH GA 7 .   ? -16.496 -12.293 25.577  1.00 17.94  ? 486 HOH B O   1 
HETATM 9481  O  O   . HOH GA 7 .   ? -20.336 -9.482  14.924  1.00 20.26  ? 487 HOH B O   1 
HETATM 9482  O  O   . HOH GA 7 .   ? 8.926   2.757   20.149  1.00 23.97  ? 488 HOH B O   1 
HETATM 9483  O  O   . HOH GA 7 .   ? -2.838  -5.324  -4.150  1.00 10.82  ? 489 HOH B O   1 
HETATM 9484  O  O   . HOH GA 7 .   ? -13.498 7.425   -15.615 1.00 24.03  ? 490 HOH B O   1 
HETATM 9485  O  O   . HOH GA 7 .   ? 1.075   18.170  -13.869 1.00 26.22  ? 491 HOH B O   1 
HETATM 9486  O  O   . HOH GA 7 .   ? -20.284 -12.053 0.936   1.00 34.35  ? 492 HOH B O   1 
HETATM 9487  O  O   . HOH GA 7 .   ? 3.687   -2.218  14.004  1.00 16.37  ? 493 HOH B O   1 
HETATM 9488  O  O   . HOH GA 7 .   ? -13.104 -19.086 -0.871  1.00 35.80  ? 494 HOH B O   1 
HETATM 9489  O  O   . HOH GA 7 .   ? 1.138   0.509   -16.103 1.00 29.00  ? 495 HOH B O   1 
HETATM 9490  O  O   . HOH GA 7 .   ? -12.116 -13.504 -11.416 1.00 17.25  ? 496 HOH B O   1 
HETATM 9491  O  O   . HOH GA 7 .   ? -22.842 -2.201  -8.704  1.00 15.33  ? 497 HOH B O   1 
HETATM 9492  O  O   . HOH GA 7 .   ? 1.705   -1.617  5.808   1.00 8.84   ? 498 HOH B O   1 
HETATM 9493  O  O   . HOH GA 7 .   ? 4.490   17.150  3.776   1.00 23.37  ? 499 HOH B O   1 
HETATM 9494  O  O   . HOH GA 7 .   ? 5.319   5.475   7.728   1.00 10.34  ? 500 HOH B O   1 
HETATM 9495  O  O   . HOH GA 7 .   ? -20.838 3.682   -13.026 1.00 21.67  ? 501 HOH B O   1 
HETATM 9496  O  O   . HOH GA 7 .   ? -23.195 9.487   6.343   1.00 17.63  ? 502 HOH B O   1 
HETATM 9497  O  O   . HOH GA 7 .   ? -7.199  13.618  3.928   1.00 22.11  ? 503 HOH B O   1 
HETATM 9498  O  O   . HOH GA 7 .   ? -23.265 11.351  -1.184  1.00 24.27  ? 504 HOH B O   1 
HETATM 9499  O  O   . HOH GA 7 .   ? -7.540  -7.349  28.412  1.00 31.53  ? 505 HOH B O   1 
HETATM 9500  O  O   . HOH GA 7 .   ? 4.867   -9.642  -12.354 1.00 26.73  ? 506 HOH B O   1 
HETATM 9501  O  O   . HOH GA 7 .   ? 4.709   -5.931  9.127   1.00 19.96  ? 507 HOH B O   1 
HETATM 9502  O  O   . HOH GA 7 .   ? -26.954 -6.330  6.553   1.00 16.40  ? 508 HOH B O   1 
HETATM 9503  O  O   . HOH GA 7 .   ? -30.647 1.958   10.526  1.00 35.65  ? 509 HOH B O   1 
HETATM 9504  O  O   . HOH GA 7 .   ? -14.019 -14.720 5.816   1.00 16.81  ? 510 HOH B O   1 
HETATM 9505  O  O   . HOH GA 7 .   ? 4.103   10.008  -6.649  1.00 22.92  ? 511 HOH B O   1 
HETATM 9506  O  O   . HOH GA 7 .   ? -1.576  16.613  11.002  1.00 12.69  ? 512 HOH B O   1 
HETATM 9507  O  O   . HOH GA 7 .   ? -26.754 8.991   -2.713  1.00 28.10  ? 513 HOH B O   1 
HETATM 9508  O  O   . HOH GA 7 .   ? 8.948   16.592  0.876   1.00 17.29  ? 514 HOH B O   1 
HETATM 9509  O  O   . HOH GA 7 .   ? 3.661   -4.088  -1.825  1.00 32.16  ? 515 HOH B O   1 
HETATM 9510  O  O   . HOH GA 7 .   ? -27.161 12.771  20.241  1.00 34.90  ? 516 HOH B O   1 
HETATM 9511  O  O   . HOH GA 7 .   ? -1.945  -11.363 -3.161  1.00 16.69  ? 517 HOH B O   1 
HETATM 9512  O  O   . HOH GA 7 .   ? -29.374 2.114   5.405   1.00 31.12  ? 518 HOH B O   1 
HETATM 9513  O  O   . HOH GA 7 .   ? -17.870 9.280   -2.598  1.00 17.74  ? 519 HOH B O   1 
HETATM 9514  O  O   . HOH GA 7 .   ? -18.242 -8.057  15.994  1.00 18.25  ? 520 HOH B O   1 
HETATM 9515  O  O   . HOH GA 7 .   ? -17.722 -3.739  26.793  1.00 21.38  ? 521 HOH B O   1 
HETATM 9516  O  O   . HOH GA 7 .   ? -10.975 17.455  -8.473  1.00 37.54  ? 522 HOH B O   1 
HETATM 9517  O  O   . HOH GA 7 .   ? -6.617  -11.429 29.074  1.00 27.86  ? 523 HOH B O   1 
HETATM 9518  O  O   . HOH GA 7 .   ? -1.568  14.569  16.907  1.00 18.85  ? 524 HOH B O   1 
HETATM 9519  O  O   . HOH GA 7 .   ? 2.632   -13.132 16.010  1.00 19.13  ? 525 HOH B O   1 
HETATM 9520  O  O   . HOH GA 7 .   ? -14.574 -14.196 19.749  1.00 33.80  ? 526 HOH B O   1 
HETATM 9521  O  O   . HOH GA 7 .   ? -27.657 -4.322  8.443   1.00 15.58  ? 527 HOH B O   1 
HETATM 9522  O  O   . HOH GA 7 .   ? 8.118   4.599   5.163   1.00 9.86   ? 528 HOH B O   1 
HETATM 9523  O  O   . HOH GA 7 .   ? -24.547 -2.489  -6.536  1.00 15.23  ? 529 HOH B O   1 
HETATM 9524  O  O   . HOH GA 7 .   ? -0.106  -13.841 8.961   1.00 28.63  ? 530 HOH B O   1 
HETATM 9525  O  O   . HOH GA 7 .   ? -5.246  18.147  -7.723  1.00 46.23  ? 531 HOH B O   1 
HETATM 9526  O  O   . HOH GA 7 .   ? 5.271   15.813  13.457  1.00 22.70  ? 532 HOH B O   1 
HETATM 9527  O  O   . HOH GA 7 .   ? -16.579 5.776   22.057  1.00 32.34  ? 533 HOH B O   1 
HETATM 9528  O  O   . HOH GA 7 .   ? -24.015 0.695   21.113  1.00 27.69  ? 534 HOH B O   1 
HETATM 9529  O  O   . HOH GA 7 .   ? -6.930  9.820   2.342   1.00 31.50  ? 535 HOH B O   1 
HETATM 9530  O  O   . HOH GA 7 .   ? -7.769  -15.606 -7.901  1.00 12.84  ? 536 HOH B O   1 
HETATM 9531  O  O   . HOH GA 7 .   ? 6.582   3.293   9.159   1.00 8.50   ? 537 HOH B O   1 
HETATM 9532  O  O   . HOH GA 7 .   ? -8.788  -8.003  -14.513 1.00 17.67  ? 538 HOH B O   1 
HETATM 9533  O  O   . HOH GA 7 .   ? -3.248  2.661   21.299  1.00 19.37  ? 539 HOH B O   1 
HETATM 9534  O  O   . HOH GA 7 .   ? -24.109 8.369   23.319  1.00 34.21  ? 540 HOH B O   1 
HETATM 9535  O  O   . HOH GA 7 .   ? -10.308 -8.952  8.142   1.00 8.83   ? 541 HOH B O   1 
HETATM 9536  O  O   . HOH GA 7 .   ? -16.866 -10.740 1.197   1.00 13.07  ? 542 HOH B O   1 
HETATM 9537  O  O   . HOH GA 7 .   ? -5.908  11.228  20.604  1.00 30.10  ? 543 HOH B O   1 
HETATM 9538  O  O   . HOH GA 7 .   ? 4.302   14.774  1.839   1.00 22.61  ? 544 HOH B O   1 
HETATM 9539  O  O   . HOH GA 7 .   ? -17.009 -10.396 20.120  1.00 15.36  ? 545 HOH B O   1 
HETATM 9540  O  O   . HOH GA 7 .   ? -5.849  -15.228 13.238  1.00 23.74  ? 546 HOH B O   1 
HETATM 9541  O  O   . HOH GA 7 .   ? -1.876  9.691   -3.238  1.00 21.73  ? 547 HOH B O   1 
HETATM 9542  O  O   . HOH GA 7 .   ? 0.882   -9.295  25.107  1.00 39.44  ? 548 HOH B O   1 
HETATM 9543  O  O   . HOH GA 7 .   ? -3.104  7.321   -3.776  1.00 15.62  ? 549 HOH B O   1 
HETATM 9544  O  O   . HOH GA 7 .   ? -3.700  2.264   -11.938 1.00 16.13  ? 550 HOH B O   1 
HETATM 9545  O  O   . HOH GA 7 .   ? 4.140   -14.981 10.148  1.00 35.38  ? 551 HOH B O   1 
HETATM 9546  O  O   . HOH GA 7 .   ? -12.965 -17.373 6.565   1.00 69.66  ? 552 HOH B O   1 
HETATM 9547  O  O   . HOH GA 7 .   ? -1.332  14.085  -4.473  1.00 28.17  ? 553 HOH B O   1 
HETATM 9548  O  O   . HOH GA 7 .   ? -6.221  -18.333 -2.304  1.00 27.01  ? 554 HOH B O   1 
HETATM 9549  O  O   . HOH GA 7 .   ? -14.658 -2.834  25.410  1.00 38.50  ? 555 HOH B O   1 
HETATM 9550  O  O   . HOH GA 7 .   ? -10.540 14.342  -13.807 1.00 16.95  ? 556 HOH B O   1 
HETATM 9551  O  O   . HOH GA 7 .   ? -14.685 -13.494 23.779  1.00 25.38  ? 557 HOH B O   1 
HETATM 9552  O  O   . HOH GA 7 .   ? -2.767  1.547   -14.479 1.00 33.10  ? 558 HOH B O   1 
HETATM 9553  O  O   . HOH GA 7 .   ? -1.272  -6.925  30.894  1.00 88.94  ? 559 HOH B O   1 
HETATM 9554  O  O   . HOH GA 7 .   ? -31.667 5.186   -7.683  1.00 19.93  ? 560 HOH B O   1 
HETATM 9555  O  O   . HOH GA 7 .   ? -16.801 -16.679 16.457  1.00 33.78  ? 561 HOH B O   1 
HETATM 9556  O  O   . HOH GA 7 .   ? -19.736 -15.916 10.172  1.00 27.61  ? 562 HOH B O   1 
HETATM 9557  O  O   . HOH GA 7 .   ? -23.292 -9.083  14.132  1.00 32.29  ? 563 HOH B O   1 
HETATM 9558  O  O   . HOH GA 7 .   ? 5.437   19.891  10.763  1.00 22.70  ? 564 HOH B O   1 
HETATM 9559  O  O   . HOH GA 7 .   ? -10.451 -3.130  24.723  1.00 36.63  ? 565 HOH B O   1 
HETATM 9560  O  O   . HOH GA 7 .   ? 3.122   -3.603  16.128  1.00 27.89  ? 566 HOH B O   1 
HETATM 9561  O  O   . HOH GA 7 .   ? -1.218  -0.644  -12.584 1.00 18.96  ? 567 HOH B O   1 
HETATM 9562  O  O   . HOH GA 7 .   ? 2.117   6.019   -12.359 1.00 23.86  ? 568 HOH B O   1 
HETATM 9563  O  O   . HOH GA 7 .   ? -10.772 -10.303 29.769  1.00 20.52  ? 569 HOH B O   1 
HETATM 9564  O  O   . HOH GA 7 .   ? -15.759 -0.334  -14.922 1.00 29.01  ? 570 HOH B O   1 
HETATM 9565  O  O   . HOH GA 7 .   ? -29.872 -3.170  6.862   1.00 26.19  ? 571 HOH B O   1 
HETATM 9566  O  O   . HOH GA 7 .   ? -0.891  16.061  -8.563  1.00 30.96  ? 572 HOH B O   1 
HETATM 9567  O  O   . HOH GA 7 .   ? 1.611   6.510   20.587  1.00 37.63  ? 573 HOH B O   1 
HETATM 9568  O  O   . HOH GA 7 .   ? -3.208  -12.685 -1.228  1.00 17.17  ? 574 HOH B O   1 
HETATM 9569  O  O   . HOH GA 7 .   ? 11.458  14.469  -0.098  1.00 21.55  ? 575 HOH B O   1 
HETATM 9570  O  O   . HOH GA 7 .   ? -5.760  15.223  2.105   1.00 25.71  ? 576 HOH B O   1 
HETATM 9571  O  O   . HOH GA 7 .   ? -27.150 -6.308  -4.896  1.00 25.93  ? 577 HOH B O   1 
HETATM 9572  O  O   . HOH GA 7 .   ? -0.785  12.016  16.122  1.00 12.89  ? 578 HOH B O   1 
HETATM 9573  O  O   . HOH GA 7 .   ? -1.147  5.894   -4.872  1.00 14.73  ? 579 HOH B O   1 
HETATM 9574  O  O   . HOH GA 7 .   ? 1.647   8.986   -6.861  1.00 17.85  ? 580 HOH B O   1 
HETATM 9575  O  O   . HOH GA 7 .   ? 2.192   5.133   -5.695  1.00 18.02  ? 581 HOH B O   1 
HETATM 9576  O  O   . HOH GA 7 .   ? 0.793   13.285  19.326  1.00 31.43  ? 582 HOH B O   1 
HETATM 9577  O  O   . HOH GA 7 .   ? -27.282 6.830   -11.960 1.00 28.33  ? 583 HOH B O   1 
HETATM 9578  O  O   . HOH GA 7 .   ? -15.955 -8.744  -13.255 1.00 36.33  ? 584 HOH B O   1 
HETATM 9579  O  O   . HOH GA 7 .   ? -16.207 -5.806  -12.897 1.00 30.21  ? 585 HOH B O   1 
HETATM 9580  O  O   . HOH GA 7 .   ? -28.992 7.378   -1.647  1.00 30.11  ? 586 HOH B O   1 
HETATM 9581  O  O   . HOH GA 7 .   ? -38.148 -2.939  -4.369  1.00 36.14  ? 587 HOH B O   1 
HETATM 9582  O  O   . HOH GA 7 .   ? -29.020 9.218   10.492  1.00 30.98  ? 588 HOH B O   1 
HETATM 9583  O  O   . HOH GA 7 .   ? -23.884 -8.130  20.026  1.00 32.90  ? 589 HOH B O   1 
HETATM 9584  O  O   . HOH GA 7 .   ? -5.747  2.799   -17.161 1.00 37.75  ? 590 HOH B O   1 
HETATM 9585  O  O   . HOH GA 7 .   ? 5.983   -2.305  1.865   1.00 22.47  ? 591 HOH B O   1 
HETATM 9586  O  O   . HOH GA 7 .   ? 6.175   -9.822  -9.980  1.00 35.41  ? 592 HOH B O   1 
HETATM 9587  O  O   . HOH GA 7 .   ? -14.510 -14.056 0.556   1.00 17.11  ? 593 HOH B O   1 
HETATM 9588  O  O   . HOH GA 7 .   ? 6.506   4.766   13.790  1.00 11.88  ? 594 HOH B O   1 
HETATM 9589  O  O   . HOH GA 7 .   ? 4.233   8.208   7.731   1.00 9.93   ? 595 HOH B O   1 
HETATM 9590  O  O   . HOH GA 7 .   ? 4.820   9.146   14.465  1.00 16.03  ? 596 HOH B O   1 
HETATM 9591  O  O   . HOH GA 7 .   ? 4.262   3.341   -6.021  1.00 25.88  ? 597 HOH B O   1 
HETATM 9592  O  O   . HOH GA 7 .   ? 8.675   8.664   1.972   1.00 15.86  ? 598 HOH B O   1 
HETATM 9593  O  O   . HOH GA 7 .   ? 5.792   20.685  -5.389  1.00 33.46  ? 599 HOH B O   1 
HETATM 9594  O  O   . HOH GA 7 .   ? 4.348   -2.086  6.458   1.00 16.72  ? 600 HOH B O   1 
HETATM 9595  O  O   . HOH GA 7 .   ? -7.235  6.948   19.023  1.00 22.37  ? 601 HOH B O   1 
HETATM 9596  O  O   . HOH GA 7 .   ? -12.751 -0.407  22.586  1.00 18.98  ? 602 HOH B O   1 
HETATM 9597  O  O   . HOH GA 7 .   ? 8.505   17.713  -2.934  1.00 34.38  ? 603 HOH B O   1 
HETATM 9598  O  O   . HOH GA 7 .   ? 3.995   -4.637  0.822   1.00 34.81  ? 604 HOH B O   1 
HETATM 9599  O  O   . HOH GA 7 .   ? -2.718  -0.250  25.308  1.00 34.53  ? 605 HOH B O   1 
HETATM 9600  O  O   . HOH GA 7 .   ? 9.996   8.425   -0.630  1.00 26.17  ? 606 HOH B O   1 
HETATM 9601  O  O   . HOH GA 7 .   ? 5.993   -6.125  14.819  1.00 18.66  ? 607 HOH B O   1 
HETATM 9602  O  O   . HOH GA 7 .   ? -16.642 3.039   21.885  1.00 31.46  ? 608 HOH B O   1 
HETATM 9603  O  O   . HOH GA 7 .   ? -14.241 -10.848 23.810  1.00 19.64  ? 609 HOH B O   1 
HETATM 9604  O  O   . HOH GA 7 .   ? 0.504   8.161   -4.454  1.00 18.86  ? 610 HOH B O   1 
HETATM 9605  O  O   . HOH GA 7 .   ? -19.518 -13.593 14.387  1.00 20.73  ? 611 HOH B O   1 
HETATM 9606  O  O   . HOH GA 7 .   ? -30.671 7.264   -4.584  1.00 28.08  ? 612 HOH B O   1 
HETATM 9607  O  O   . HOH GA 7 .   ? -13.322 -11.931 11.634  1.00 10.79  ? 613 HOH B O   1 
HETATM 9608  O  O   . HOH GA 7 .   ? -13.830 14.923  5.566   1.00 45.21  ? 614 HOH B O   1 
HETATM 9609  O  O   . HOH GA 7 .   ? -13.588 20.130  14.505  1.00 38.57  ? 615 HOH B O   1 
HETATM 9610  O  O   . HOH GA 7 .   ? -0.425  -13.183 22.431  1.00 36.63  ? 616 HOH B O   1 
HETATM 9611  O  O   . HOH GA 7 .   ? -25.384 -7.441  12.786  1.00 24.06  ? 617 HOH B O   1 
HETATM 9612  O  O   . HOH GA 7 .   ? -25.465 -10.630 -5.136  1.00 53.71  ? 618 HOH B O   1 
HETATM 9613  O  O   . HOH GA 7 .   ? -17.761 12.618  -12.773 1.00 27.55  ? 619 HOH B O   1 
HETATM 9614  O  O   . HOH GA 7 .   ? -0.395  -9.412  27.913  1.00 44.45  ? 620 HOH B O   1 
HETATM 9615  O  O   . HOH GA 7 .   ? -22.632 6.337   -12.568 1.00 33.30  ? 621 HOH B O   1 
HETATM 9616  O  O   . HOH GA 7 .   ? 6.894   -1.222  17.513  1.00 19.70  ? 622 HOH B O   1 
HETATM 9617  O  O   . HOH GA 7 .   ? -26.073 -9.712  6.001   1.00 25.82  ? 623 HOH B O   1 
HETATM 9618  O  O   . HOH GA 7 .   ? 5.475   -8.240  -1.430  1.00 28.87  ? 624 HOH B O   1 
HETATM 9619  O  O   . HOH GA 7 .   ? 4.110   -13.299 22.454  1.00 31.76  ? 625 HOH B O   1 
HETATM 9620  O  O   . HOH GA 7 .   ? -26.800 10.222  4.907   1.00 35.15  ? 626 HOH B O   1 
HETATM 9621  O  O   . HOH GA 7 .   ? -11.259 -15.709 3.053   1.00 31.29  ? 627 HOH B O   1 
HETATM 9622  O  O   . HOH GA 7 .   ? -8.465  17.368  10.762  1.00 37.74  ? 628 HOH B O   1 
HETATM 9623  O  O   . HOH GA 7 .   ? 7.773   -3.213  3.553   1.00 17.65  ? 629 HOH B O   1 
HETATM 9624  O  O   . HOH GA 7 .   ? -11.763 -17.292 21.545  1.00 38.54  ? 630 HOH B O   1 
HETATM 9625  O  O   . HOH GA 7 .   ? -8.516  -16.623 9.082   1.00 49.98  ? 631 HOH B O   1 
HETATM 9626  O  O   . HOH GA 7 .   ? 4.732   -3.168  17.505  1.00 26.38  ? 632 HOH B O   1 
HETATM 9627  O  O   . HOH GA 7 .   ? -22.169 3.997   26.800  1.00 36.92  ? 633 HOH B O   1 
HETATM 9628  O  O   . HOH GA 7 .   ? -24.244 8.891   -1.695  1.00 18.03  ? 634 HOH B O   1 
HETATM 9629  O  O   . HOH GA 7 .   ? -31.851 -6.611  5.829   1.00 25.19  ? 635 HOH B O   1 
HETATM 9630  O  O   . HOH GA 7 .   ? 3.444   -11.017 3.470   1.00 25.93  ? 636 HOH B O   1 
HETATM 9631  O  O   . HOH GA 7 .   ? -0.658  -12.476 15.420  1.00 26.74  ? 637 HOH B O   1 
HETATM 9632  O  O   . HOH GA 7 .   ? -5.037  0.528   21.994  1.00 21.11  ? 638 HOH B O   1 
HETATM 9633  O  O   . HOH GA 7 .   ? -2.023  11.856  -5.080  1.00 24.50  ? 639 HOH B O   1 
HETATM 9634  O  O   . HOH GA 7 .   ? 2.439   15.935  16.442  1.00 29.69  ? 640 HOH B O   1 
HETATM 9635  O  O   . HOH GA 7 .   ? -5.404  -13.185 20.554  1.00 31.55  ? 641 HOH B O   1 
HETATM 9636  O  O   . HOH GA 7 .   ? -26.725 3.396   -10.681 1.00 43.44  ? 642 HOH B O   1 
HETATM 9637  O  O   . HOH GA 7 .   ? -30.763 2.135   2.095   1.00 25.36  ? 643 HOH B O   1 
HETATM 9638  O  O   . HOH GA 7 .   ? 2.733   6.576   16.635  1.00 20.43  ? 644 HOH B O   1 
HETATM 9639  O  O   . HOH GA 7 .   ? -1.000  -12.806 4.205   1.00 34.58  ? 645 HOH B O   1 
HETATM 9640  O  O   . HOH GA 7 .   ? -14.755 -14.634 -2.523  1.00 14.31  ? 646 HOH B O   1 
HETATM 9641  O  O   . HOH GA 7 .   ? 8.600   6.368   -1.866  1.00 23.14  ? 647 HOH B O   1 
HETATM 9642  O  O   . HOH GA 7 .   ? -26.839 9.386   12.282  1.00 28.89  ? 648 HOH B O   1 
HETATM 9643  O  O   . HOH GA 7 .   ? -9.505  16.795  -16.196 1.00 25.12  ? 649 HOH B O   1 
HETATM 9644  O  O   . HOH GA 7 .   ? -3.256  -14.232 2.816   1.00 30.86  ? 650 HOH B O   1 
HETATM 9645  O  O   . HOH GA 7 .   ? 6.621   -13.575 20.208  1.00 38.93  ? 651 HOH B O   1 
HETATM 9646  O  O   . HOH GA 7 .   ? -20.198 -13.260 11.587  1.00 30.08  ? 652 HOH B O   1 
HETATM 9647  O  O   . HOH GA 7 .   ? -8.572  -4.730  28.550  1.00 38.77  ? 653 HOH B O   1 
HETATM 9648  O  O   . HOH GA 7 .   ? -18.044 14.786  7.015   1.00 30.11  ? 654 HOH B O   1 
HETATM 9649  O  O   . HOH GA 7 .   ? -20.467 12.109  -13.102 1.00 32.87  ? 655 HOH B O   1 
HETATM 9650  O  O   . HOH GA 7 .   ? -2.245  -12.692 24.683  1.00 37.45  ? 656 HOH B O   1 
HETATM 9651  O  O   . HOH GA 7 .   ? -3.129  -11.922 1.156   1.00 20.92  ? 657 HOH B O   1 
HETATM 9652  O  O   . HOH GA 7 .   ? -34.898 -2.504  -2.329  1.00 45.11  ? 658 HOH B O   1 
HETATM 9653  O  O   . HOH GA 7 .   ? -29.467 8.235   6.061   1.00 36.17  ? 659 HOH B O   1 
HETATM 9654  O  O   . HOH GA 7 .   ? -24.565 -1.156  -11.684 1.00 29.16  ? 660 HOH B O   1 
HETATM 9655  O  O   . HOH GA 7 .   ? -22.788 -15.373 -6.939  1.00 57.76  ? 661 HOH B O   1 
HETATM 9656  O  O   . HOH GA 7 .   ? -13.357 -16.287 23.849  1.00 40.18  ? 662 HOH B O   1 
HETATM 9657  O  O   . HOH GA 7 .   ? -21.662 -13.455 -9.700  1.00 43.78  ? 663 HOH B O   1 
HETATM 9658  O  O   . HOH GA 7 .   ? -12.588 -2.514  -13.052 1.00 42.21  ? 664 HOH B O   1 
HETATM 9659  O  O   . HOH GA 7 .   ? -24.490 16.549  16.385  1.00 44.98  ? 665 HOH B O   1 
HETATM 9660  O  O   . HOH GA 7 .   ? -2.444  -10.848 -14.998 1.00 43.93  ? 666 HOH B O   1 
HETATM 9661  O  O   . HOH GA 7 .   ? -5.888  1.927   24.277  1.00 39.26  ? 667 HOH B O   1 
HETATM 9662  O  O   . HOH GA 7 .   ? -13.466 -16.649 19.366  1.00 36.07  ? 668 HOH B O   1 
HETATM 9663  O  O   . HOH GA 7 .   ? -8.145  7.060   2.899   1.00 29.27  ? 669 HOH B O   1 
HETATM 9664  O  O   . HOH GA 7 .   ? -16.773 -17.053 3.251   1.00 38.57  ? 670 HOH B O   1 
HETATM 9665  O  O   . HOH GA 7 .   ? -12.767 14.755  -15.376 1.00 39.65  ? 671 HOH B O   1 
HETATM 9666  O  O   . HOH GA 7 .   ? -31.764 9.303   1.063   1.00 50.79  ? 672 HOH B O   1 
HETATM 9667  O  O   . HOH GA 7 .   ? -24.831 8.269   1.047   1.00 21.76  ? 673 HOH B O   1 
HETATM 9668  O  O   . HOH GA 7 .   ? -11.795 0.624   26.676  1.00 39.54  ? 674 HOH B O   1 
HETATM 9669  O  O   . HOH GA 7 .   ? -17.548 -14.151 -2.297  1.00 21.03  ? 675 HOH B O   1 
HETATM 9670  O  O   . HOH GA 7 .   ? -10.063 -3.940  -15.843 1.00 29.77  ? 676 HOH B O   1 
HETATM 9671  O  O   . HOH GA 7 .   ? -16.422 13.804  5.208   1.00 49.18  ? 677 HOH B O   1 
HETATM 9672  O  O   . HOH GA 7 .   ? -29.642 -6.067  11.156  1.00 52.37  ? 678 HOH B O   1 
HETATM 9673  O  O   . HOH GA 7 .   ? -7.969  8.185   1.127   1.00 31.70  ? 679 HOH B O   1 
HETATM 9674  O  O   . HOH GA 7 .   ? -30.129 4.929   2.458   1.00 33.90  ? 680 HOH B O   1 
HETATM 9675  O  O   . HOH GA 7 .   ? -21.608 -6.539  -9.884  1.00 29.64  ? 681 HOH B O   1 
HETATM 9676  O  O   . HOH GA 7 .   ? 12.703  11.366  -3.644  1.00 33.86  ? 682 HOH B O   1 
HETATM 9677  O  O   . HOH GA 7 .   ? -38.387 2.169   -5.841  1.00 29.37  ? 683 HOH B O   1 
HETATM 9678  O  O   . HOH GA 7 .   ? -4.140  21.207  -18.392 1.00 38.80  ? 684 HOH B O   1 
HETATM 9679  O  O   . HOH GA 7 .   ? 8.173   10.556  -7.307  1.00 40.93  ? 685 HOH B O   1 
HETATM 9680  O  O   . HOH GA 7 .   ? -18.112 -13.781 0.062   1.00 37.30  ? 686 HOH B O   1 
HETATM 9681  O  O   . HOH GA 7 .   ? -13.896 -4.897  -13.045 1.00 27.32  ? 687 HOH B O   1 
HETATM 9682  O  O   . HOH GA 7 .   ? -15.697 8.419   -17.006 1.00 37.52  ? 688 HOH B O   1 
HETATM 9683  O  O   . HOH GA 7 .   ? -23.171 -4.518  -10.106 1.00 29.16  ? 689 HOH B O   1 
HETATM 9684  O  O   . HOH GA 7 .   ? -33.436 2.727   2.578   1.00 36.66  ? 690 HOH B O   1 
HETATM 9685  O  O   . HOH GA 7 .   ? -23.950 -10.927 5.085   1.00 43.32  ? 691 HOH B O   1 
HETATM 9686  O  O   . HOH GA 7 .   ? -31.767 -0.095  5.942   1.00 45.15  ? 692 HOH B O   1 
HETATM 9687  O  O   . HOH GA 7 .   ? -29.527 7.228   1.004   1.00 32.40  ? 693 HOH B O   1 
HETATM 9688  O  O   . HOH GA 7 .   ? 6.393   -5.617  11.191  1.00 27.79  ? 694 HOH B O   1 
HETATM 9689  O  O   . HOH GA 7 .   ? -13.563 14.508  -5.275  1.00 52.31  ? 695 HOH B O   1 
HETATM 9690  O  O   . HOH GA 7 .   ? -21.296 -11.930 15.722  1.00 26.32  ? 696 HOH B O   1 
HETATM 9691  O  O   . HOH GA 7 .   ? 1.387   -0.682  -12.047 1.00 30.33  ? 697 HOH B O   1 
HETATM 9692  O  O   . HOH GA 7 .   ? 5.855   2.230   -3.497  1.00 23.81  ? 698 HOH B O   1 
HETATM 9693  O  O   . HOH GA 7 .   ? -6.525  15.355  16.090  1.00 31.77  ? 699 HOH B O   1 
HETATM 9694  O  O   . HOH GA 7 .   ? -15.682 -14.672 3.852   1.00 32.14  ? 700 HOH B O   1 
HETATM 9695  O  O   . HOH GA 7 .   ? 4.552   15.340  17.885  1.00 27.92  ? 701 HOH B O   1 
HETATM 9696  O  O   . HOH GA 7 .   ? 7.770   6.043   0.870   1.00 15.84  ? 702 HOH B O   1 
HETATM 9697  O  O   . HOH GA 7 .   ? -8.051  -5.699  -15.731 1.00 24.58  ? 703 HOH B O   1 
HETATM 9698  O  O   . HOH GA 7 .   ? -11.440 -8.286  -14.938 1.00 23.88  ? 704 HOH B O   1 
HETATM 9699  O  O   . HOH GA 7 .   ? -13.453 -16.430 1.509   1.00 41.28  ? 705 HOH B O   1 
HETATM 9700  O  O   . HOH GA 7 .   ? -9.441  -8.141  30.466  1.00 40.23  ? 706 HOH B O   1 
HETATM 9701  O  O   . HOH GA 7 .   ? -3.583  16.307  -8.661  1.00 28.55  ? 707 HOH B O   1 
HETATM 9702  O  O   . HOH GA 7 .   ? -12.916 -9.009  -12.666 1.00 25.25  ? 708 HOH B O   1 
HETATM 9703  O  O   . HOH GA 7 .   ? -29.339 -7.624  6.400   1.00 27.66  ? 709 HOH B O   1 
HETATM 9704  O  O   . HOH GA 7 .   ? -16.481 -13.330 1.988   1.00 29.03  ? 710 HOH B O   1 
HETATM 9705  O  O   . HOH GA 7 .   ? -14.836 1.272   23.091  1.00 29.16  ? 711 HOH B O   1 
HETATM 9706  O  O   . HOH GA 7 .   ? 1.789   -15.739 16.533  1.00 32.93  ? 712 HOH B O   1 
HETATM 9707  O  O   . HOH GA 7 .   ? -31.538 1.927   7.911   1.00 32.04  ? 713 HOH B O   1 
HETATM 9708  O  O   . HOH GA 7 .   ? -8.957  15.341  5.012   1.00 37.82  ? 714 HOH B O   1 
HETATM 9709  O  O   . HOH GA 7 .   ? -25.226 5.296   -13.096 1.00 35.64  ? 715 HOH B O   1 
HETATM 9710  O  O   . HOH GA 7 .   ? 5.794   -4.287  7.244   1.00 29.31  ? 716 HOH B O   1 
HETATM 9711  O  O   . HOH GA 7 .   ? -15.481 -17.251 -1.532  1.00 34.61  ? 717 HOH B O   1 
HETATM 9712  O  O   . HOH GA 7 .   ? -0.789  -12.054 -9.017  1.00 37.68  ? 718 HOH B O   1 
HETATM 9713  O  O   . HOH GA 7 .   ? -20.236 -10.050 -12.274 1.00 37.63  ? 719 HOH B O   1 
HETATM 9714  O  O   . HOH GA 7 .   ? -4.475  -13.594 9.661   1.00 30.24  ? 720 HOH B O   1 
HETATM 9715  O  O   . HOH GA 7 .   ? 4.604   -11.778 24.729  1.00 35.84  ? 721 HOH B O   1 
HETATM 9716  O  O   . HOH GA 7 .   ? -16.897 9.374   23.616  1.00 38.67  ? 722 HOH B O   1 
HETATM 9717  O  O   . HOH GA 7 .   ? -12.050 -1.579  24.898  1.00 35.74  ? 723 HOH B O   1 
HETATM 9718  O  O   . HOH GA 7 .   ? -28.450 -3.376  -7.886  1.00 45.18  ? 724 HOH B O   1 
HETATM 9719  O  O   . HOH GA 7 .   ? -5.718  6.312   23.610  1.00 55.91  ? 725 HOH B O   1 
HETATM 9720  O  O   . HOH GA 7 .   ? -17.499 -12.897 21.120  1.00 26.02  ? 726 HOH B O   1 
HETATM 9721  O  O   . HOH GA 7 .   ? -18.540 -11.863 23.728  1.00 27.99  ? 727 HOH B O   1 
HETATM 9722  O  O   . HOH GA 7 .   ? 7.539   -9.477  15.646  1.00 15.78  ? 728 HOH B O   1 
HETATM 9723  O  O   . HOH GA 7 .   ? 5.334   -13.080 15.754  1.00 20.76  ? 729 HOH B O   1 
HETATM 9724  O  O   . HOH GA 7 .   ? -6.734  7.182   21.729  1.00 40.96  ? 730 HOH B O   1 
HETATM 9725  O  O   . HOH GA 7 .   ? 5.661   -0.521  -2.394  1.00 26.57  ? 731 HOH B O   1 
HETATM 9726  O  O   . HOH GA 7 .   ? 2.460   -11.437 -12.149 1.00 34.51  ? 732 HOH B O   1 
HETATM 9727  O  O   . HOH GA 7 .   ? 3.551   6.159   -10.126 1.00 27.63  ? 733 HOH B O   1 
HETATM 9728  O  O   . HOH GA 7 .   ? 1.495   -15.324 22.946  1.00 37.98  ? 734 HOH B O   1 
HETATM 9729  O  O   . HOH GA 7 .   ? -10.391 17.787  -14.144 1.00 51.14  ? 735 HOH B O   1 
HETATM 9730  O  O   . HOH GA 7 .   ? -20.747 -10.839 -9.960  1.00 26.39  ? 736 HOH B O   1 
HETATM 9731  O  O   . HOH GA 7 .   ? -9.740  15.346  7.239   1.00 37.32  ? 737 HOH B O   1 
HETATM 9732  O  O   . HOH GA 7 .   ? -3.847  15.289  18.385  1.00 40.73  ? 738 HOH B O   1 
HETATM 9733  O  O   . HOH GA 7 .   ? -12.620 -17.528 3.362   1.00 35.08  ? 739 HOH B O   1 
HETATM 9734  O  O   . HOH GA 7 .   ? -24.055 -9.678  -8.097  1.00 47.83  ? 740 HOH B O   1 
HETATM 9735  O  O   . HOH GA 7 .   ? -1.196  21.853  11.023  1.00 53.69  ? 741 HOH B O   1 
HETATM 9736  O  O   . HOH GA 7 .   ? 0.533   15.776  17.940  1.00 34.27  ? 742 HOH B O   1 
HETATM 9737  O  O   . HOH GA 7 .   ? -27.417 8.938   1.487   1.00 33.43  ? 743 HOH B O   1 
HETATM 9738  O  O   . HOH GA 7 .   ? -13.316 -11.766 -13.120 1.00 24.51  ? 744 HOH B O   1 
HETATM 9739  O  O   . HOH GA 7 .   ? -8.361  -13.048 30.398  1.00 27.91  ? 745 HOH B O   1 
HETATM 9740  O  O   . HOH GA 7 .   ? 11.221  17.337  -2.765  1.00 48.83  ? 746 HOH B O   1 
HETATM 9741  O  O   . HOH GA 7 .   ? -2.970  18.860  10.582  1.00 29.72  ? 747 HOH B O   1 
HETATM 9742  O  O   . HOH GA 7 .   ? 1.081   6.904   22.956  1.00 34.31  ? 748 HOH B O   1 
HETATM 9743  O  O   . HOH GA 7 .   ? -2.893  10.872  21.026  1.00 35.95  ? 749 HOH B O   1 
HETATM 9744  O  O   . HOH GA 7 .   ? -21.846 -14.277 -3.243  1.00 37.68  ? 750 HOH B O   1 
HETATM 9745  O  O   . HOH GA 7 .   ? -1.381  -14.355 19.911  1.00 32.97  ? 751 HOH B O   1 
HETATM 9746  O  O   . HOH GA 7 .   ? -2.341  -14.520 8.747   1.00 46.03  ? 752 HOH B O   1 
HETATM 9747  O  O   . HOH GA 7 .   ? -7.651  -10.060 -15.997 1.00 20.17  ? 753 HOH B O   1 
HETATM 9748  O  O   . HOH GA 7 .   ? -5.635  -15.195 7.878   1.00 40.20  ? 754 HOH B O   1 
HETATM 9749  O  O   . HOH GA 7 .   ? -19.108 -15.999 15.595  1.00 30.91  ? 755 HOH B O   1 
HETATM 9750  O  O   . HOH GA 7 .   ? -4.041  -14.069 18.872  1.00 41.37  ? 756 HOH B O   1 
HETATM 9751  O  O   . HOH GA 7 .   ? -4.049  4.127   23.554  1.00 38.01  ? 757 HOH B O   1 
HETATM 9752  O  O   . HOH GA 7 .   ? -10.530 -12.976 30.651  1.00 28.04  ? 758 HOH B O   1 
HETATM 9753  O  O   . HOH GA 7 .   ? -1.934  -15.303 10.930  1.00 36.55  ? 759 HOH B O   1 
HETATM 9754  O  O   . HOH GA 7 .   ? -0.864  -14.254 6.432   1.00 28.28  ? 760 HOH B O   1 
HETATM 9755  O  O   . HOH GA 7 .   ? 12.945  11.475  -6.374  1.00 35.88  ? 761 HOH B O   1 
HETATM 9756  O  O   . HOH GA 7 .   ? -12.038 -12.400 -15.470 1.00 36.91  ? 762 HOH B O   1 
HETATM 9757  O  O   . HOH GA 7 .   ? -2.064  12.972  20.503  1.00 52.54  ? 763 HOH B O   1 
HETATM 9758  O  O   . HOH GA 7 .   ? 0.723   -13.078 -7.120  1.00 48.80  ? 764 HOH B O   1 
HETATM 9759  O  O   . HOH GA 7 .   ? -9.785  -11.538 -17.098 1.00 34.55  ? 765 HOH B O   1 
HETATM 9760  O  O   . HOH GA 7 .   ? 1.882   14.268  21.756  1.00 40.11  ? 766 HOH B O   1 
HETATM 9761  O  O   . HOH GA 7 .   ? -3.403  -15.772 -9.529  1.00 25.82  ? 767 HOH B O   1 
HETATM 9762  O  O   . HOH GA 7 .   ? 0.903   -16.525 6.293   1.00 50.37  ? 768 HOH B O   1 
HETATM 9763  O  O   . HOH GA 7 .   ? -21.238 -11.999 24.171  1.00 36.71  ? 769 HOH B O   1 
HETATM 9764  O  O   . HOH GA 7 .   ? -25.690 -5.972  -8.846  1.00 41.07  ? 770 HOH B O   1 
HETATM 9765  O  O   . HOH GA 7 .   ? -26.071 -3.120  -10.215 1.00 41.03  ? 771 HOH B O   1 
HETATM 9766  O  O   . HOH GA 7 .   ? 0.296   23.833  4.326   1.00 31.65  ? 772 HOH B O   1 
HETATM 9767  O  O   . HOH GA 7 .   ? -18.709 -16.239 1.366   1.00 39.46  ? 773 HOH B O   1 
HETATM 9768  O  O   . HOH GA 7 .   ? -12.183 -5.392  -15.359 1.00 35.65  ? 774 HOH B O   1 
HETATM 9769  O  O   . HOH GA 7 .   ? -1.502  9.575   23.358  1.00 65.54  ? 775 HOH B O   1 
HETATM 9770  O  O   . HOH GA 7 .   ? 13.323  15.592  -3.857  1.00 33.89  ? 776 HOH B O   1 
HETATM 9771  O  O   . HOH GA 7 .   ? -19.382 -14.388 20.053  1.00 34.61  ? 777 HOH B O   1 
HETATM 9772  O  O   . HOH GA 7 .   ? 12.208  15.646  -6.328  1.00 46.49  ? 778 HOH B O   1 
HETATM 9773  O  O   . HOH GA 7 .   ? -21.782 -13.490 18.090  1.00 36.10  ? 779 HOH B O   1 
HETATM 9774  O  O   . HOH GA 7 .   ? -8.781  -15.430 29.573  1.00 17.08  ? 780 HOH B O   1 
HETATM 9775  O  O   . HOH GA 7 .   ? 2.589   22.902  13.110  1.00 54.13  ? 781 HOH B O   1 
HETATM 9776  O  O   . HOH HA 7 .   ? 20.671  -1.810  -50.770 1.00 27.90  ? 401 HOH C O   1 
HETATM 9777  O  O   . HOH HA 7 .   ? 59.675  -2.705  -25.869 1.00 31.76  ? 402 HOH C O   1 
HETATM 9778  O  O   . HOH HA 7 .   ? 19.637  1.587   -51.653 1.00 23.06  ? 403 HOH C O   1 
HETATM 9779  O  O   . HOH HA 7 .   ? 26.524  18.188  -28.392 1.00 34.78  ? 404 HOH C O   1 
HETATM 9780  O  O   . HOH HA 7 .   ? 21.432  17.642  -27.366 1.00 29.88  ? 405 HOH C O   1 
HETATM 9781  O  O   . HOH HA 7 .   ? 36.296  -9.502  -53.856 1.00 30.01  ? 406 HOH C O   1 
HETATM 9782  O  O   . HOH HA 7 .   ? 56.188  8.114   -37.639 1.00 33.55  ? 407 HOH C O   1 
HETATM 9783  O  O   . HOH HA 7 .   ? 32.572  -19.576 -50.004 1.00 29.60  ? 408 HOH C O   1 
HETATM 9784  O  O   . HOH HA 7 .   ? 22.674  -2.174  -31.399 1.00 38.09  ? 409 HOH C O   1 
HETATM 9785  O  O   . HOH HA 7 .   ? 28.314  6.886   -19.163 1.00 38.50  ? 410 HOH C O   1 
HETATM 9786  O  O   . HOH HA 7 .   ? 38.619  10.434  -31.698 1.00 23.12  ? 411 HOH C O   1 
HETATM 9787  O  O   . HOH HA 7 .   ? 54.566  -10.044 -31.328 1.00 37.29  ? 412 HOH C O   1 
HETATM 9788  O  O   . HOH HA 7 .   ? 28.506  18.312  -31.725 1.00 16.02  ? 413 HOH C O   1 
HETATM 9789  O  O   . HOH HA 7 .   ? 47.129  8.627   -30.081 1.00 31.93  ? 414 HOH C O   1 
HETATM 9790  O  O   . HOH HA 7 .   ? 33.449  11.638  -11.010 1.00 37.65  ? 415 HOH C O   1 
HETATM 9791  O  O   . HOH HA 7 .   ? 47.639  -1.635  -10.214 1.00 35.46  ? 416 HOH C O   1 
HETATM 9792  O  O   . HOH HA 7 .   ? 37.438  16.565  -29.975 1.00 47.00  ? 417 HOH C O   1 
HETATM 9793  O  O   . HOH HA 7 .   ? 42.005  -17.914 -53.501 1.00 37.34  ? 418 HOH C O   1 
HETATM 9794  O  O   . HOH HA 7 .   ? 35.180  -17.577 -15.058 1.00 46.18  ? 419 HOH C O   1 
HETATM 9795  O  O   . HOH HA 7 .   ? 47.104  11.351  -21.931 1.00 31.31  ? 420 HOH C O   1 
HETATM 9796  O  O   . HOH HA 7 .   ? 36.581  -5.484  -10.289 1.00 38.98  ? 421 HOH C O   1 
HETATM 9797  O  O   . HOH HA 7 .   ? 59.259  3.363   -20.659 1.00 32.18  ? 422 HOH C O   1 
HETATM 9798  O  O   . HOH HA 7 .   ? 41.823  6.786   -9.773  1.00 33.44  ? 423 HOH C O   1 
HETATM 9799  O  O   . HOH HA 7 .   ? 32.591  5.018   -30.604 1.00 15.05  ? 424 HOH C O   1 
HETATM 9800  O  O   . HOH HA 7 .   ? 40.795  -5.349  -52.736 1.00 31.00  ? 425 HOH C O   1 
HETATM 9801  O  O   . HOH HA 7 .   ? 37.723  -9.461  -10.995 1.00 35.11  ? 426 HOH C O   1 
HETATM 9802  O  O   . HOH HA 7 .   ? 24.622  -12.943 -41.700 1.00 29.05  ? 427 HOH C O   1 
HETATM 9803  O  O   . HOH HA 7 .   ? 33.233  -11.176 -10.576 1.00 38.32  ? 428 HOH C O   1 
HETATM 9804  O  O   . HOH HA 7 .   ? 22.321  -8.870  -39.932 1.00 22.56  ? 429 HOH C O   1 
HETATM 9805  O  O   . HOH HA 7 .   ? 36.766  15.714  -26.468 1.00 43.08  ? 430 HOH C O   1 
HETATM 9806  O  O   . HOH HA 7 .   ? 46.497  8.085   -11.580 1.00 23.64  ? 431 HOH C O   1 
HETATM 9807  O  O   . HOH HA 7 .   ? 28.896  -8.375  -17.463 1.00 26.97  ? 432 HOH C O   1 
HETATM 9808  O  O   . HOH HA 7 .   ? 25.785  -7.700  -51.552 1.00 44.54  ? 433 HOH C O   1 
HETATM 9809  O  O   . HOH HA 7 .   ? 57.021  2.177   -37.701 1.00 45.13  ? 434 HOH C O   1 
HETATM 9810  O  O   . HOH HA 7 .   ? 22.392  -6.327  -31.610 1.00 20.56  ? 435 HOH C O   1 
HETATM 9811  O  O   . HOH HA 7 .   ? 22.872  -8.710  -17.236 1.00 40.77  ? 436 HOH C O   1 
HETATM 9812  O  O   . HOH HA 7 .   ? 29.833  -5.092  -22.266 1.00 17.40  ? 437 HOH C O   1 
HETATM 9813  O  O   . HOH HA 7 .   ? 43.837  -5.559  -50.445 1.00 23.68  ? 438 HOH C O   1 
HETATM 9814  O  O   . HOH HA 7 .   ? 48.008  -13.157 -39.477 1.00 35.09  ? 439 HOH C O   1 
HETATM 9815  O  O   . HOH HA 7 .   ? 54.394  9.710   -34.348 1.00 36.90  ? 440 HOH C O   1 
HETATM 9816  O  O   . HOH HA 7 .   ? 40.792  13.726  -36.822 1.00 22.04  ? 441 HOH C O   1 
HETATM 9817  O  O   . HOH HA 7 .   ? 26.625  -8.882  -16.249 1.00 25.37  ? 442 HOH C O   1 
HETATM 9818  O  O   . HOH HA 7 .   ? 43.773  -12.965 -26.296 1.00 30.82  ? 443 HOH C O   1 
HETATM 9819  O  O   . HOH HA 7 .   ? 52.946  6.303   -31.514 1.00 20.01  ? 444 HOH C O   1 
HETATM 9820  O  O   . HOH HA 7 .   ? 44.893  13.376  -19.013 1.00 37.81  ? 445 HOH C O   1 
HETATM 9821  O  O   . HOH HA 7 .   ? 25.947  5.263   -24.152 1.00 26.75  ? 446 HOH C O   1 
HETATM 9822  O  O   . HOH HA 7 .   ? 24.065  13.147  -42.349 1.00 16.04  ? 447 HOH C O   1 
HETATM 9823  O  O   . HOH HA 7 .   ? 47.028  9.164   -27.252 1.00 22.06  ? 448 HOH C O   1 
HETATM 9824  O  O   . HOH HA 7 .   ? 27.425  16.189  -41.112 1.00 13.99  ? 449 HOH C O   1 
HETATM 9825  O  O   . HOH HA 7 .   ? 32.805  -13.336 -37.208 1.00 20.83  ? 450 HOH C O   1 
HETATM 9826  O  O   . HOH HA 7 .   ? 33.259  -1.392  -49.073 1.00 16.02  ? 451 HOH C O   1 
HETATM 9827  O  O   . HOH HA 7 .   ? 25.439  8.158   -28.072 1.00 15.38  ? 452 HOH C O   1 
HETATM 9828  O  O   . HOH HA 7 .   ? 56.653  4.481   -42.161 1.00 19.57  ? 453 HOH C O   1 
HETATM 9829  O  O   . HOH HA 7 .   ? 24.433  4.461   -20.803 1.00 33.41  ? 454 HOH C O   1 
HETATM 9830  O  O   . HOH HA 7 .   ? 35.430  5.833   -26.819 1.00 30.18  ? 455 HOH C O   1 
HETATM 9831  O  O   . HOH HA 7 .   ? 26.111  5.504   -43.422 1.00 13.78  ? 456 HOH C O   1 
HETATM 9832  O  O   . HOH HA 7 .   ? 46.578  -0.681  -47.505 1.00 38.05  ? 457 HOH C O   1 
HETATM 9833  O  O   . HOH HA 7 .   ? 45.040  16.568  -38.661 1.00 27.88  ? 458 HOH C O   1 
HETATM 9834  O  O   . HOH HA 7 .   ? 38.515  -14.883 -14.076 1.00 40.17  ? 459 HOH C O   1 
HETATM 9835  O  O   . HOH HA 7 .   ? 20.663  -1.545  -22.539 1.00 35.27  ? 460 HOH C O   1 
HETATM 9836  O  O   . HOH HA 7 .   ? 51.455  -2.340  -43.761 1.00 24.49  ? 461 HOH C O   1 
HETATM 9837  O  O   . HOH HA 7 .   ? 28.040  15.906  -29.306 1.00 32.06  ? 462 HOH C O   1 
HETATM 9838  O  O   . HOH HA 7 .   ? 35.728  -13.614 -54.690 1.00 19.34  ? 463 HOH C O   1 
HETATM 9839  O  O   . HOH HA 7 .   ? 26.143  7.020   -41.171 1.00 9.63   ? 464 HOH C O   1 
HETATM 9840  O  O   . HOH HA 7 .   ? 53.747  7.049   -27.893 1.00 25.09  ? 465 HOH C O   1 
HETATM 9841  O  O   . HOH HA 7 .   ? 37.335  8.749   -47.500 1.00 25.61  ? 466 HOH C O   1 
HETATM 9842  O  O   . HOH HA 7 .   ? 25.069  6.540   -34.705 1.00 10.96  ? 467 HOH C O   1 
HETATM 9843  O  O   . HOH HA 7 .   ? 47.004  2.342   -47.529 1.00 31.34  ? 468 HOH C O   1 
HETATM 9844  O  O   . HOH HA 7 .   ? 58.360  -2.048  -30.277 1.00 28.84  ? 469 HOH C O   1 
HETATM 9845  O  O   . HOH HA 7 .   ? 47.110  7.288   -22.941 1.00 22.71  ? 470 HOH C O   1 
HETATM 9846  O  O   . HOH HA 7 .   ? 53.493  14.376  -44.628 1.00 39.34  ? 471 HOH C O   1 
HETATM 9847  O  O   . HOH HA 7 .   ? 28.681  3.229   -43.593 1.00 13.56  ? 472 HOH C O   1 
HETATM 9848  O  O   . HOH HA 7 .   ? 25.341  -1.681  -40.787 1.00 11.38  ? 473 HOH C O   1 
HETATM 9849  O  O   . HOH HA 7 .   ? 35.301  17.107  -41.609 1.00 25.92  ? 474 HOH C O   1 
HETATM 9850  O  O   . HOH HA 7 .   ? 21.691  -1.839  -46.608 1.00 22.82  ? 475 HOH C O   1 
HETATM 9851  O  O   . HOH HA 7 .   ? 34.162  15.911  -38.359 1.00 12.31  ? 476 HOH C O   1 
HETATM 9852  O  O   . HOH HA 7 .   ? 42.375  16.762  -44.722 1.00 29.62  ? 477 HOH C O   1 
HETATM 9853  O  O   . HOH HA 7 .   ? 33.980  -16.863 -17.405 1.00 34.79  ? 478 HOH C O   1 
HETATM 9854  O  O   . HOH HA 7 .   ? 45.287  -6.938  -45.666 1.00 17.29  ? 479 HOH C O   1 
HETATM 9855  O  O   . HOH HA 7 .   ? 56.107  0.795   -46.788 1.00 33.69  ? 480 HOH C O   1 
HETATM 9856  O  O   . HOH HA 7 .   ? 53.286  -3.606  -46.359 1.00 37.93  ? 481 HOH C O   1 
HETATM 9857  O  O   . HOH HA 7 .   ? 35.458  19.647  -35.840 1.00 33.71  ? 482 HOH C O   1 
HETATM 9858  O  O   . HOH HA 7 .   ? 43.268  -2.285  -40.545 1.00 11.58  ? 483 HOH C O   1 
HETATM 9859  O  O   . HOH HA 7 .   ? 27.336  -10.402 -26.908 1.00 22.93  ? 484 HOH C O   1 
HETATM 9860  O  O   . HOH HA 7 .   ? 25.995  -3.399  -42.762 1.00 16.27  ? 485 HOH C O   1 
HETATM 9861  O  O   . HOH HA 7 .   ? 41.782  -8.350  -55.096 1.00 18.26  ? 486 HOH C O   1 
HETATM 9862  O  O   . HOH HA 7 .   ? 47.828  18.942  -41.006 1.00 41.00  ? 487 HOH C O   1 
HETATM 9863  O  O   . HOH HA 7 .   ? 46.315  -11.406 -40.733 1.00 25.18  ? 488 HOH C O   1 
HETATM 9864  O  O   . HOH HA 7 .   ? 40.332  -16.605 -30.670 1.00 29.29  ? 489 HOH C O   1 
HETATM 9865  O  O   . HOH HA 7 .   ? 24.208  -3.072  -27.183 1.00 37.69  ? 490 HOH C O   1 
HETATM 9866  O  O   . HOH HA 7 .   ? 32.584  7.228   -22.486 1.00 29.01  ? 491 HOH C O   1 
HETATM 9867  O  O   . HOH HA 7 .   ? 31.263  -16.628 -31.009 1.00 31.87  ? 492 HOH C O   1 
HETATM 9868  O  O   . HOH HA 7 .   ? 20.168  -10.185 -30.108 1.00 17.49  ? 493 HOH C O   1 
HETATM 9869  O  O   . HOH HA 7 .   ? 51.616  10.075  -33.405 1.00 21.45  ? 494 HOH C O   1 
HETATM 9870  O  O   . HOH HA 7 .   ? 42.249  -17.132 -45.244 1.00 49.36  ? 495 HOH C O   1 
HETATM 9871  O  O   . HOH HA 7 .   ? 33.871  13.568  -44.129 1.00 15.62  ? 496 HOH C O   1 
HETATM 9872  O  O   . HOH HA 7 .   ? 43.687  4.197   -44.485 1.00 17.91  ? 497 HOH C O   1 
HETATM 9873  O  O   . HOH HA 7 .   ? 27.149  -0.830  -32.386 1.00 9.75   ? 498 HOH C O   1 
HETATM 9874  O  O   . HOH HA 7 .   ? 55.786  -8.207  -32.965 1.00 29.82  ? 499 HOH C O   1 
HETATM 9875  O  O   . HOH HA 7 .   ? 25.745  -2.916  -48.362 1.00 16.04  ? 500 HOH C O   1 
HETATM 9876  O  O   . HOH HA 7 .   ? 37.772  -10.507 -33.534 1.00 14.60  ? 501 HOH C O   1 
HETATM 9877  O  O   . HOH HA 7 .   ? 38.659  -19.164 -16.857 1.00 42.15  ? 502 HOH C O   1 
HETATM 9878  O  O   . HOH HA 7 .   ? 22.387  -5.170  -41.127 1.00 22.45  ? 503 HOH C O   1 
HETATM 9879  O  O   . HOH HA 7 .   ? 59.873  -2.136  -35.641 1.00 31.93  ? 504 HOH C O   1 
HETATM 9880  O  O   . HOH HA 7 .   ? 51.659  12.908  -47.517 1.00 26.75  ? 505 HOH C O   1 
HETATM 9881  O  O   . HOH HA 7 .   ? 23.551  -4.581  -36.130 1.00 16.18  ? 506 HOH C O   1 
HETATM 9882  O  O   . HOH HA 7 .   ? 29.316  -11.095 -14.295 1.00 28.61  ? 507 HOH C O   1 
HETATM 9883  O  O   . HOH HA 7 .   ? 30.156  15.616  -43.773 1.00 25.13  ? 508 HOH C O   1 
HETATM 9884  O  O   . HOH HA 7 .   ? 38.955  -2.719  -11.858 1.00 38.06  ? 509 HOH C O   1 
HETATM 9885  O  O   . HOH HA 7 .   ? 36.396  -17.213 -28.281 1.00 40.65  ? 510 HOH C O   1 
HETATM 9886  O  O   . HOH HA 7 .   ? 49.956  -9.147  -46.202 1.00 29.36  ? 511 HOH C O   1 
HETATM 9887  O  O   . HOH HA 7 .   ? 41.182  7.476   -46.830 1.00 24.97  ? 512 HOH C O   1 
HETATM 9888  O  O   . HOH HA 7 .   ? 20.910  13.573  -35.551 1.00 10.64  ? 513 HOH C O   1 
HETATM 9889  O  O   . HOH HA 7 .   ? 20.455  17.669  -29.830 1.00 30.37  ? 514 HOH C O   1 
HETATM 9890  O  O   . HOH HA 7 .   ? 22.047  -13.626 -36.043 1.00 33.64  ? 515 HOH C O   1 
HETATM 9891  O  O   . HOH HA 7 .   ? 35.845  -19.316 -37.597 1.00 48.28  ? 516 HOH C O   1 
HETATM 9892  O  O   . HOH HA 7 .   ? 26.454  -5.060  -51.389 1.00 24.66  ? 517 HOH C O   1 
HETATM 9893  O  O   . HOH HA 7 .   ? 26.583  -13.493 -34.858 1.00 20.47  ? 518 HOH C O   1 
HETATM 9894  O  O   . HOH HA 7 .   ? 31.956  2.500   -43.792 1.00 12.42  ? 519 HOH C O   1 
HETATM 9895  O  O   . HOH HA 7 .   ? 44.861  -13.721 -44.811 1.00 17.64  ? 520 HOH C O   1 
HETATM 9896  O  O   . HOH HA 7 .   ? 23.428  4.762   -36.054 1.00 8.46   ? 521 HOH C O   1 
HETATM 9897  O  O   . HOH HA 7 .   ? 33.970  1.237   -16.704 1.00 25.56  ? 522 HOH C O   1 
HETATM 9898  O  O   . HOH HA 7 .   ? 48.197  -11.302 -16.316 1.00 82.67  ? 523 HOH C O   1 
HETATM 9899  O  O   . HOH HA 7 .   ? 35.164  13.351  -22.044 1.00 41.97  ? 524 HOH C O   1 
HETATM 9900  O  O   . HOH HA 7 .   ? 31.815  1.835   -14.628 1.00 25.71  ? 525 HOH C O   1 
HETATM 9901  O  O   . HOH HA 7 .   ? 22.194  6.825   -32.164 1.00 10.22  ? 526 HOH C O   1 
HETATM 9902  O  O   . HOH HA 7 .   ? 47.019  -13.114 -53.206 1.00 17.93  ? 527 HOH C O   1 
HETATM 9903  O  O   . HOH HA 7 .   ? 52.796  8.531   -24.166 1.00 28.41  ? 528 HOH C O   1 
HETATM 9904  O  O   . HOH HA 7 .   ? 25.888  12.997  -35.417 1.00 11.13  ? 529 HOH C O   1 
HETATM 9905  O  O   . HOH HA 7 .   ? 44.671  -14.956 -50.423 1.00 28.86  ? 530 HOH C O   1 
HETATM 9906  O  O   . HOH HA 7 .   ? 24.346  18.783  -28.555 1.00 41.89  ? 531 HOH C O   1 
HETATM 9907  O  O   . HOH HA 7 .   ? 23.062  -11.495 -44.843 1.00 24.94  ? 532 HOH C O   1 
HETATM 9908  O  O   . HOH HA 7 .   ? 58.836  -7.552  -34.696 1.00 40.33  ? 533 HOH C O   1 
HETATM 9909  O  O   . HOH HA 7 .   ? 30.290  6.244   -21.877 1.00 40.21  ? 534 HOH C O   1 
HETATM 9910  O  O   . HOH HA 7 .   ? 47.775  -9.081  -51.752 1.00 33.22  ? 535 HOH C O   1 
HETATM 9911  O  O   . HOH HA 7 .   ? 41.072  4.441   -45.755 1.00 26.32  ? 536 HOH C O   1 
HETATM 9912  O  O   . HOH HA 7 .   ? 28.277  -10.789 -22.641 1.00 23.53  ? 537 HOH C O   1 
HETATM 9913  O  O   . HOH HA 7 .   ? 22.713  -0.094  -28.239 1.00 26.82  ? 538 HOH C O   1 
HETATM 9914  O  O   . HOH HA 7 .   ? 29.106  9.000   -22.414 1.00 34.63  ? 539 HOH C O   1 
HETATM 9915  O  O   . HOH HA 7 .   ? 26.325  11.569  -45.578 1.00 27.84  ? 540 HOH C O   1 
HETATM 9916  O  O   . HOH HA 7 .   ? 30.375  -10.722 -16.803 1.00 30.39  ? 541 HOH C O   1 
HETATM 9917  O  O   . HOH HA 7 .   ? 26.787  9.317   -34.781 1.00 11.01  ? 542 HOH C O   1 
HETATM 9918  O  O   . HOH HA 7 .   ? 29.262  6.109   -47.393 1.00 13.80  ? 543 HOH C O   1 
HETATM 9919  O  O   . HOH HA 7 .   ? 42.055  -3.792  -48.474 1.00 21.75  ? 544 HOH C O   1 
HETATM 9920  O  O   . HOH HA 7 .   ? 35.866  -0.937  -48.566 1.00 16.92  ? 545 HOH C O   1 
HETATM 9921  O  O   . HOH HA 7 .   ? 43.247  -1.528  -11.078 1.00 32.57  ? 546 HOH C O   1 
HETATM 9922  O  O   . HOH HA 7 .   ? 53.406  -11.083 -37.395 1.00 33.23  ? 547 HOH C O   1 
HETATM 9923  O  O   . HOH HA 7 .   ? 26.331  3.233   -47.395 1.00 20.59  ? 548 HOH C O   1 
HETATM 9924  O  O   . HOH HA 7 .   ? 40.000  -11.908 -55.295 1.00 22.52  ? 549 HOH C O   1 
HETATM 9925  O  O   . HOH HA 7 .   ? 24.354  -0.719  -32.976 1.00 18.73  ? 550 HOH C O   1 
HETATM 9926  O  O   . HOH HA 7 .   ? 32.551  11.341  -43.281 1.00 10.36  ? 551 HOH C O   1 
HETATM 9927  O  O   . HOH HA 7 .   ? 29.697  -12.599 -40.951 1.00 44.44  ? 552 HOH C O   1 
HETATM 9928  O  O   . HOH HA 7 .   ? 23.989  -8.995  -29.230 1.00 26.42  ? 553 HOH C O   1 
HETATM 9929  O  O   . HOH HA 7 .   ? 38.331  5.094   -45.285 1.00 14.75  ? 554 HOH C O   1 
HETATM 9930  O  O   . HOH HA 7 .   ? 25.829  14.437  -23.104 1.00 34.18  ? 555 HOH C O   1 
HETATM 9931  O  O   . HOH HA 7 .   ? 39.159  -19.515 -46.402 1.00 36.47  ? 556 HOH C O   1 
HETATM 9932  O  O   . HOH HA 7 .   ? 44.089  13.999  -47.727 1.00 30.33  ? 557 HOH C O   1 
HETATM 9933  O  O   . HOH HA 7 .   ? 22.556  10.993  -29.329 1.00 18.03  ? 558 HOH C O   1 
HETATM 9934  O  O   . HOH HA 7 .   ? 33.046  -14.704 -47.035 1.00 35.16  ? 559 HOH C O   1 
HETATM 9935  O  O   . HOH HA 7 .   ? 22.873  -2.995  -50.354 1.00 29.99  ? 560 HOH C O   1 
HETATM 9936  O  O   . HOH HA 7 .   ? 60.122  -7.876  -21.243 1.00 49.26  ? 561 HOH C O   1 
HETATM 9937  O  O   . HOH HA 7 .   ? 32.676  -14.602 -51.671 1.00 19.80  ? 562 HOH C O   1 
HETATM 9938  O  O   . HOH HA 7 .   ? 19.572  -7.859  -17.795 1.00 36.55  ? 563 HOH C O   1 
HETATM 9939  O  O   . HOH HA 7 .   ? 28.403  6.859   -44.106 1.00 15.93  ? 564 HOH C O   1 
HETATM 9940  O  O   . HOH HA 7 .   ? 57.615  11.624  -37.896 1.00 41.69  ? 565 HOH C O   1 
HETATM 9941  O  O   . HOH HA 7 .   ? 24.834  -2.245  -23.851 1.00 23.72  ? 566 HOH C O   1 
HETATM 9942  O  O   . HOH HA 7 .   ? 38.563  16.594  -38.702 1.00 18.23  ? 567 HOH C O   1 
HETATM 9943  O  O   . HOH HA 7 .   ? 39.494  17.996  -40.964 1.00 26.00  ? 568 HOH C O   1 
HETATM 9944  O  O   . HOH HA 7 .   ? 31.546  12.764  -46.509 1.00 20.52  ? 569 HOH C O   1 
HETATM 9945  O  O   . HOH HA 7 .   ? 29.739  -12.712 -24.212 1.00 22.38  ? 570 HOH C O   1 
HETATM 9946  O  O   . HOH HA 7 .   ? 24.406  -3.724  -44.798 1.00 22.66  ? 571 HOH C O   1 
HETATM 9947  O  O   . HOH HA 7 .   ? 40.576  -16.192 -25.932 1.00 32.21  ? 572 HOH C O   1 
HETATM 9948  O  O   . HOH HA 7 .   ? 32.693  0.853   -50.960 1.00 40.54  ? 573 HOH C O   1 
HETATM 9949  O  O   . HOH HA 7 .   ? 53.457  5.866   -23.594 1.00 31.51  ? 574 HOH C O   1 
HETATM 9950  O  O   . HOH HA 7 .   ? 40.973  3.955   -7.050  1.00 43.06  ? 575 HOH C O   1 
HETATM 9951  O  O   . HOH HA 7 .   ? 29.532  -13.925 -28.402 1.00 25.26  ? 576 HOH C O   1 
HETATM 9952  O  O   . HOH HA 7 .   ? 23.724  5.692   -40.733 1.00 11.95  ? 577 HOH C O   1 
HETATM 9953  O  O   . HOH HA 7 .   ? 42.196  11.558  -26.104 1.00 41.31  ? 578 HOH C O   1 
HETATM 9954  O  O   . HOH HA 7 .   ? 28.746  3.695   -46.225 1.00 14.77  ? 579 HOH C O   1 
HETATM 9955  O  O   . HOH HA 7 .   ? 40.387  -14.138 -36.680 1.00 18.89  ? 580 HOH C O   1 
HETATM 9956  O  O   . HOH HA 7 .   ? 46.296  -17.003 -38.828 1.00 29.68  ? 581 HOH C O   1 
HETATM 9957  O  O   . HOH HA 7 .   ? 22.241  -0.250  -44.294 1.00 15.67  ? 582 HOH C O   1 
HETATM 9958  O  O   . HOH HA 7 .   ? 26.047  4.056   -50.054 1.00 29.17  ? 583 HOH C O   1 
HETATM 9959  O  O   . HOH HA 7 .   ? 40.743  6.698   -27.494 1.00 26.38  ? 584 HOH C O   1 
HETATM 9960  O  O   . HOH HA 7 .   ? 28.838  -0.497  -14.472 1.00 25.73  ? 585 HOH C O   1 
HETATM 9961  O  O   . HOH HA 7 .   ? 52.119  17.975  -39.140 1.00 48.58  ? 586 HOH C O   1 
HETATM 9962  O  O   . HOH HA 7 .   ? 53.723  -10.140 -22.682 1.00 36.80  ? 587 HOH C O   1 
HETATM 9963  O  O   . HOH HA 7 .   ? 42.411  -13.853 -48.800 1.00 26.16  ? 588 HOH C O   1 
HETATM 9964  O  O   . HOH HA 7 .   ? 28.173  -10.312 -51.592 1.00 32.81  ? 589 HOH C O   1 
HETATM 9965  O  O   . HOH HA 7 .   ? 46.904  -16.610 -36.166 1.00 40.60  ? 590 HOH C O   1 
HETATM 9966  O  O   . HOH HA 7 .   ? 27.553  2.552   -52.256 1.00 30.00  ? 591 HOH C O   1 
HETATM 9967  O  O   . HOH HA 7 .   ? 26.467  9.688   -41.816 1.00 12.55  ? 592 HOH C O   1 
HETATM 9968  O  O   . HOH HA 7 .   ? 26.459  6.616   -14.224 1.00 40.14  ? 593 HOH C O   1 
HETATM 9969  O  O   . HOH HA 7 .   ? 48.579  -13.257 -34.535 1.00 34.66  ? 594 HOH C O   1 
HETATM 9970  O  O   . HOH HA 7 .   ? 44.719  9.058   -29.098 1.00 31.31  ? 595 HOH C O   1 
HETATM 9971  O  O   . HOH HA 7 .   ? 38.698  13.942  -42.909 1.00 20.45  ? 596 HOH C O   1 
HETATM 9972  O  O   . HOH HA 7 .   ? 55.815  6.625   -29.996 1.00 35.29  ? 597 HOH C O   1 
HETATM 9973  O  O   . HOH HA 7 .   ? 37.948  14.186  -30.913 1.00 36.25  ? 598 HOH C O   1 
HETATM 9974  O  O   . HOH HA 7 .   ? 29.721  -11.750 -26.765 1.00 18.20  ? 599 HOH C O   1 
HETATM 9975  O  O   . HOH HA 7 .   ? 58.089  -7.308  -31.393 1.00 36.49  ? 600 HOH C O   1 
HETATM 9976  O  O   . HOH HA 7 .   ? 22.507  -5.108  -26.526 1.00 24.25  ? 601 HOH C O   1 
HETATM 9977  O  O   . HOH HA 7 .   ? 56.482  -1.846  -43.633 1.00 36.68  ? 602 HOH C O   1 
HETATM 9978  O  O   . HOH HA 7 .   ? 27.712  -12.482 -30.264 1.00 28.56  ? 603 HOH C O   1 
HETATM 9979  O  O   . HOH HA 7 .   ? 43.827  13.225  -34.145 1.00 54.45  ? 604 HOH C O   1 
HETATM 9980  O  O   . HOH HA 7 .   ? 45.461  12.782  -27.574 1.00 50.42  ? 605 HOH C O   1 
HETATM 9981  O  O   . HOH HA 7 .   ? 42.330  -19.611 -19.213 1.00 49.76  ? 606 HOH C O   1 
HETATM 9982  O  O   . HOH HA 7 .   ? 40.529  -16.869 -23.047 1.00 41.48  ? 607 HOH C O   1 
HETATM 9983  O  O   . HOH HA 7 .   ? 38.333  -19.679 -49.172 1.00 35.61  ? 608 HOH C O   1 
HETATM 9984  O  O   . HOH HA 7 .   ? 49.304  12.157  -48.633 1.00 33.39  ? 609 HOH C O   1 
HETATM 9985  O  O   . HOH HA 7 .   ? 48.834  11.317  -24.319 1.00 26.53  ? 610 HOH C O   1 
HETATM 9986  O  O   . HOH HA 7 .   ? 20.980  -1.069  -30.158 1.00 20.26  ? 611 HOH C O   1 
HETATM 9987  O  O   . HOH HA 7 .   ? 39.509  -5.188  -49.577 1.00 20.90  ? 612 HOH C O   1 
HETATM 9988  O  O   . HOH HA 7 .   ? 32.664  -14.755 -9.834  1.00 43.83  ? 613 HOH C O   1 
HETATM 9989  O  O   . HOH HA 7 .   ? 57.830  -0.596  -16.492 1.00 35.74  ? 614 HOH C O   1 
HETATM 9990  O  O   . HOH HA 7 .   ? 56.805  5.409   -37.685 1.00 34.62  ? 615 HOH C O   1 
HETATM 9991  O  O   . HOH HA 7 .   ? 22.033  1.120   -35.048 1.00 29.80  ? 616 HOH C O   1 
HETATM 9992  O  O   . HOH HA 7 .   ? 49.924  12.072  -32.856 1.00 30.10  ? 617 HOH C O   1 
HETATM 9993  O  O   . HOH HA 7 .   ? 44.189  18.187  -43.571 1.00 32.90  ? 618 HOH C O   1 
HETATM 9994  O  O   . HOH HA 7 .   ? 44.323  -4.482  -9.597  1.00 51.86  ? 619 HOH C O   1 
HETATM 9995  O  O   . HOH HA 7 .   ? 53.997  -9.386  -19.433 1.00 35.56  ? 620 HOH C O   1 
HETATM 9996  O  O   . HOH HA 7 .   ? 26.811  6.274   -21.102 1.00 46.83  ? 621 HOH C O   1 
HETATM 9997  O  O   . HOH HA 7 .   ? 45.396  -5.672  -48.212 1.00 32.72  ? 622 HOH C O   1 
HETATM 9998  O  O   . HOH HA 7 .   ? 29.244  -2.681  -54.068 1.00 35.46  ? 623 HOH C O   1 
HETATM 9999  O  O   . HOH HA 7 .   ? 35.125  -20.954 -27.922 1.00 55.36  ? 624 HOH C O   1 
HETATM 10000 O  O   . HOH HA 7 .   ? 55.844  12.439  -42.714 1.00 37.60  ? 625 HOH C O   1 
HETATM 10001 O  O   . HOH HA 7 .   ? 23.467  3.697   -51.315 1.00 37.16  ? 626 HOH C O   1 
HETATM 10002 O  O   . HOH HA 7 .   ? 23.846  -15.458 -42.202 1.00 40.65  ? 627 HOH C O   1 
HETATM 10003 O  O   . HOH HA 7 .   ? 59.472  -12.281 -25.102 1.00 48.37  ? 628 HOH C O   1 
HETATM 10004 O  O   . HOH HA 7 .   ? 32.211  -1.519  -52.212 1.00 32.15  ? 629 HOH C O   1 
HETATM 10005 O  O   . HOH HA 7 .   ? 50.802  13.949  -31.635 1.00 35.08  ? 630 HOH C O   1 
HETATM 10006 O  O   . HOH HA 7 .   ? 40.620  13.695  -46.595 1.00 53.75  ? 631 HOH C O   1 
HETATM 10007 O  O   . HOH HA 7 .   ? 41.429  9.440   -28.238 1.00 30.25  ? 632 HOH C O   1 
HETATM 10008 O  O   . HOH HA 7 .   ? 54.118  -0.844  -47.758 1.00 33.51  ? 633 HOH C O   1 
HETATM 10009 O  O   . HOH HA 7 .   ? 60.079  -3.919  -29.762 1.00 56.67  ? 634 HOH C O   1 
HETATM 10010 O  O   . HOH HA 7 .   ? 35.730  19.424  -40.319 1.00 36.61  ? 635 HOH C O   1 
HETATM 10011 O  O   . HOH HA 7 .   ? 23.205  -3.961  -47.759 1.00 27.72  ? 636 HOH C O   1 
HETATM 10012 O  O   . HOH HA 7 .   ? 32.103  9.971   -23.966 1.00 37.51  ? 637 HOH C O   1 
HETATM 10013 O  O   . HOH HA 7 .   ? 19.124  15.142  -23.854 1.00 39.30  ? 638 HOH C O   1 
HETATM 10014 O  O   . HOH HA 7 .   ? 42.909  -5.713  -54.542 1.00 21.51  ? 639 HOH C O   1 
HETATM 10015 O  O   . HOH HA 7 .   ? 25.583  -12.713 -26.138 1.00 33.43  ? 640 HOH C O   1 
HETATM 10016 O  O   . HOH HA 7 .   ? 22.186  -6.356  -47.196 1.00 37.33  ? 641 HOH C O   1 
HETATM 10017 O  O   . HOH HA 7 .   ? 54.082  4.943   -26.068 1.00 27.95  ? 642 HOH C O   1 
HETATM 10018 O  O   . HOH HA 7 .   ? 45.041  -4.968  -52.873 1.00 26.11  ? 643 HOH C O   1 
HETATM 10019 O  O   . HOH HA 7 .   ? 38.870  -10.514 -12.904 1.00 109.53 ? 644 HOH C O   1 
HETATM 10020 O  O   . HOH HA 7 .   ? 41.393  13.424  -34.028 1.00 35.74  ? 645 HOH C O   1 
HETATM 10021 O  O   . HOH HA 7 .   ? 27.993  15.269  -45.407 1.00 23.79  ? 646 HOH C O   1 
HETATM 10022 O  O   . HOH HA 7 .   ? 43.562  -16.703 -22.824 1.00 45.48  ? 647 HOH C O   1 
HETATM 10023 O  O   . HOH HA 7 .   ? 48.044  11.935  -26.942 1.00 54.41  ? 648 HOH C O   1 
HETATM 10024 O  O   . HOH HA 7 .   ? 21.225  -3.861  -32.248 1.00 29.35  ? 649 HOH C O   1 
HETATM 10025 O  O   . HOH HA 7 .   ? 24.951  5.691   -45.872 1.00 28.63  ? 650 HOH C O   1 
HETATM 10026 O  O   . HOH HA 7 .   ? 48.409  -15.956 -40.168 1.00 32.69  ? 651 HOH C O   1 
HETATM 10027 O  O   . HOH HA 7 .   ? 46.027  10.791  -10.603 1.00 43.50  ? 652 HOH C O   1 
HETATM 10028 O  O   . HOH HA 7 .   ? 33.301  -12.855 -55.847 1.00 40.79  ? 653 HOH C O   1 
HETATM 10029 O  O   . HOH HA 7 .   ? 54.677  -2.110  -45.244 1.00 36.04  ? 654 HOH C O   1 
HETATM 10030 O  O   . HOH HA 7 .   ? 35.702  1.281   -50.374 1.00 44.62  ? 655 HOH C O   1 
HETATM 10031 O  O   . HOH HA 7 .   ? 38.355  7.078   -27.546 1.00 33.11  ? 656 HOH C O   1 
HETATM 10032 O  O   . HOH HA 7 .   ? 20.363  1.325   -45.518 1.00 22.77  ? 657 HOH C O   1 
HETATM 10033 O  O   . HOH HA 7 .   ? 48.028  11.324  -30.905 1.00 42.71  ? 658 HOH C O   1 
HETATM 10034 O  O   . HOH HA 7 .   ? 22.787  -2.693  -34.262 1.00 27.25  ? 659 HOH C O   1 
HETATM 10035 O  O   . HOH HA 7 .   ? 37.836  16.693  -42.868 1.00 33.12  ? 660 HOH C O   1 
HETATM 10036 O  O   . HOH HA 7 .   ? 21.985  -3.958  -38.222 1.00 21.24  ? 661 HOH C O   1 
HETATM 10037 O  O   . HOH HA 7 .   ? 22.716  8.509   -27.907 1.00 17.73  ? 662 HOH C O   1 
HETATM 10038 O  O   . HOH HA 7 .   ? 62.034  -6.491  -16.934 1.00 48.64  ? 663 HOH C O   1 
HETATM 10039 O  O   . HOH HA 7 .   ? 46.084  -15.436 -48.303 1.00 31.52  ? 664 HOH C O   1 
HETATM 10040 O  O   . HOH HA 7 .   ? 38.287  -2.500  -48.847 1.00 28.19  ? 665 HOH C O   1 
HETATM 10041 O  O   . HOH HA 7 .   ? 38.212  -13.357 -56.198 1.00 38.62  ? 666 HOH C O   1 
HETATM 10042 O  O   . HOH HA 7 .   ? 25.757  -13.444 -29.778 1.00 35.29  ? 667 HOH C O   1 
HETATM 10043 O  O   . HOH HA 7 .   ? 41.965  -16.282 -28.232 1.00 34.05  ? 668 HOH C O   1 
HETATM 10044 O  O   . HOH HA 7 .   ? 45.346  12.364  -32.064 1.00 44.33  ? 669 HOH C O   1 
HETATM 10045 O  O   . HOH HA 7 .   ? 44.696  -2.236  -48.835 1.00 34.07  ? 670 HOH C O   1 
HETATM 10046 O  O   . HOH HA 7 .   ? 39.143  10.391  -28.856 1.00 32.82  ? 671 HOH C O   1 
HETATM 10047 O  O   . HOH HA 7 .   ? 38.536  12.642  -45.384 1.00 32.89  ? 672 HOH C O   1 
HETATM 10048 O  O   . HOH HA 7 .   ? 54.162  9.388   -26.530 1.00 33.36  ? 673 HOH C O   1 
HETATM 10049 O  O   . HOH HA 7 .   ? 38.136  -9.682  -55.840 1.00 33.13  ? 674 HOH C O   1 
HETATM 10050 O  O   . HOH HA 7 .   ? 45.100  -16.095 -45.814 1.00 27.48  ? 675 HOH C O   1 
HETATM 10051 O  O   . HOH HA 7 .   ? 40.874  12.502  -31.723 1.00 45.63  ? 676 HOH C O   1 
HETATM 10052 O  O   . HOH HA 7 .   ? 31.070  -14.641 -35.733 1.00 33.45  ? 677 HOH C O   1 
HETATM 10053 O  O   . HOH HA 7 .   ? 27.717  20.336  -30.228 1.00 51.30  ? 678 HOH C O   1 
HETATM 10054 O  O   . HOH HA 7 .   ? 32.142  15.095  -45.248 1.00 34.48  ? 679 HOH C O   1 
HETATM 10055 O  O   . HOH HA 7 .   ? 33.013  21.299  -42.870 1.00 35.61  ? 680 HOH C O   1 
HETATM 10056 O  O   . HOH HA 7 .   ? 38.602  -7.156  -10.491 1.00 35.82  ? 681 HOH C O   1 
HETATM 10057 O  O   . HOH HA 7 .   ? 42.105  -10.661 -56.614 1.00 16.13  ? 682 HOH C O   1 
HETATM 10058 O  O   . HOH HA 7 .   ? 50.658  -12.559 -16.598 1.00 62.68  ? 683 HOH C O   1 
HETATM 10059 O  O   . HOH HA 7 .   ? 47.159  -13.426 -15.121 1.00 47.51  ? 684 HOH C O   1 
HETATM 10060 O  O   . HOH HA 7 .   ? 36.518  4.221   -50.081 1.00 34.78  ? 685 HOH C O   1 
HETATM 10061 O  O   . HOH HA 7 .   ? 40.570  16.566  -36.931 1.00 29.92  ? 686 HOH C O   1 
HETATM 10062 O  O   . HOH HA 7 .   ? 50.648  15.414  -46.908 1.00 37.26  ? 687 HOH C O   1 
HETATM 10063 O  O   . HOH HA 7 .   ? 36.118  17.817  -38.279 1.00 23.33  ? 688 HOH C O   1 
HETATM 10064 O  O   . HOH HA 7 .   ? 34.530  9.412   -47.925 1.00 28.75  ? 689 HOH C O   1 
HETATM 10065 O  O   . HOH HA 7 .   ? 43.234  16.484  -47.275 1.00 41.40  ? 690 HOH C O   1 
HETATM 10066 O  O   . HOH HA 7 .   ? 50.031  16.127  -44.674 1.00 34.06  ? 691 HOH C O   1 
HETATM 10067 O  O   . HOH HA 7 .   ? 25.896  -11.447 -17.538 1.00 39.18  ? 692 HOH C O   1 
HETATM 10068 O  O   . HOH HA 7 .   ? 50.981  12.938  -23.672 1.00 47.75  ? 693 HOH C O   1 
HETATM 10069 O  O   . HOH HA 7 .   ? 24.683  -15.216 -31.002 1.00 46.25  ? 694 HOH C O   1 
HETATM 10070 O  O   . HOH HA 7 .   ? 35.952  13.527  -45.989 1.00 26.78  ? 695 HOH C O   1 
HETATM 10071 O  O   . HOH HA 7 .   ? 47.897  -15.776 -52.788 1.00 29.28  ? 696 HOH C O   1 
HETATM 10072 O  O   . HOH HA 7 .   ? 28.396  -15.127 -36.174 1.00 27.93  ? 697 HOH C O   1 
HETATM 10073 O  O   . HOH HA 7 .   ? 49.049  -11.347 -52.855 1.00 25.61  ? 698 HOH C O   1 
HETATM 10074 O  O   . HOH HA 7 .   ? 26.823  7.195   -47.466 1.00 23.13  ? 699 HOH C O   1 
HETATM 10075 O  O   . HOH HA 7 .   ? 19.077  15.769  -21.034 1.00 31.74  ? 700 HOH C O   1 
HETATM 10076 O  O   . HOH HA 7 .   ? 32.139  -16.789 -33.986 1.00 42.04  ? 701 HOH C O   1 
HETATM 10077 O  O   . HOH HA 7 .   ? 40.394  -15.095 -56.513 1.00 25.47  ? 702 HOH C O   1 
HETATM 10078 O  O   . HOH HA 7 .   ? 27.199  -13.810 -32.202 1.00 29.89  ? 703 HOH C O   1 
HETATM 10079 O  O   . HOH HA 7 .   ? 30.218  13.802  -48.850 1.00 41.38  ? 704 HOH C O   1 
HETATM 10080 O  O   . HOH HA 7 .   ? 30.044  5.935   -50.005 1.00 28.54  ? 705 HOH C O   1 
HETATM 10081 O  O   . HOH HA 7 .   ? 34.080  12.000  -47.709 1.00 25.03  ? 706 HOH C O   1 
HETATM 10082 O  O   . HOH HA 7 .   ? 39.990  15.820  -32.607 1.00 46.11  ? 707 HOH C O   1 
HETATM 10083 O  O   . HOH HA 7 .   ? 49.101  -15.792 -48.685 1.00 41.70  ? 708 HOH C O   1 
HETATM 10084 O  O   . HOH HA 7 .   ? 37.585  18.430  -34.923 1.00 40.85  ? 709 HOH C O   1 
HETATM 10085 O  O   . HOH HA 7 .   ? 50.984  -12.970 -51.696 1.00 40.25  ? 710 HOH C O   1 
HETATM 10086 O  O   . HOH HA 7 .   ? 46.803  -17.926 -44.743 1.00 42.22  ? 711 HOH C O   1 
HETATM 10087 O  O   . HOH HA 7 .   ? 48.578  -17.642 -42.437 1.00 35.96  ? 712 HOH C O   1 
HETATM 10088 O  O   . HOH HA 7 .   ? 33.602  8.136   -50.308 1.00 39.25  ? 713 HOH C O   1 
HETATM 10089 O  O   . HOH HA 7 .   ? 33.484  12.790  -50.373 1.00 51.39  ? 714 HOH C O   1 
HETATM 10090 O  O   . HOH IA 7 .   ? 6.687   23.320  -32.577 1.00 33.75  ? 401 HOH D O   1 
HETATM 10091 O  O   . HOH IA 7 .   ? -2.815  -1.608  -17.233 1.00 110.11 ? 402 HOH D O   1 
HETATM 10092 O  O   . HOH IA 7 .   ? 4.133   4.756   -45.869 1.00 19.42  ? 403 HOH D O   1 
HETATM 10093 O  O   . HOH IA 7 .   ? 11.401  22.001  -34.932 1.00 32.79  ? 404 HOH D O   1 
HETATM 10094 O  O   . HOH IA 7 .   ? -2.337  13.470  -41.734 1.00 27.12  ? 405 HOH D O   1 
HETATM 10095 O  O   . HOH IA 7 .   ? 16.310  -14.076 -34.025 1.00 37.03  ? 406 HOH D O   1 
HETATM 10096 O  O   . HOH IA 7 .   ? 2.614   -15.278 -29.854 1.00 29.75  ? 407 HOH D O   1 
HETATM 10097 O  O   . HOH IA 7 .   ? -0.130  -10.261 -18.063 1.00 31.39  ? 408 HOH D O   1 
HETATM 10098 O  O   . HOH IA 7 .   ? -7.437  3.609   -21.280 1.00 31.58  ? 409 HOH D O   1 
HETATM 10099 O  O   . HOH IA 7 .   ? 1.438   5.727   -20.312 1.00 42.11  ? 410 HOH D O   1 
HETATM 10100 O  O   . HOH IA 7 .   ? -12.260 -3.822  -36.298 1.00 25.84  ? 411 HOH D O   1 
HETATM 10101 O  O   . HOH IA 7 .   ? -6.880  15.377  -52.558 1.00 41.26  ? 412 HOH D O   1 
HETATM 10102 O  O   . HOH IA 7 .   ? -5.286  -5.526  -53.791 1.00 30.36  ? 413 HOH D O   1 
HETATM 10103 O  O   . HOH IA 7 .   ? 12.051  20.801  -32.511 1.00 19.12  ? 414 HOH D O   1 
HETATM 10104 O  O   . HOH IA 7 .   ? 1.323   -16.960 -27.078 1.00 81.48  ? 415 HOH D O   1 
HETATM 10105 O  O   . HOH IA 7 .   ? 1.075   -15.229 -36.680 1.00 35.76  ? 416 HOH D O   1 
HETATM 10106 O  O   . HOH IA 7 .   ? -8.262  -6.277  -28.435 1.00 43.84  ? 417 HOH D O   1 
HETATM 10107 O  O   . HOH IA 7 .   ? 18.516  -0.465  -20.734 1.00 32.78  ? 418 HOH D O   1 
HETATM 10108 O  O   . HOH IA 7 .   ? -1.956  13.321  -39.032 1.00 24.61  ? 419 HOH D O   1 
HETATM 10109 O  O   . HOH IA 7 .   ? 1.466   7.703   -22.641 1.00 29.48  ? 420 HOH D O   1 
HETATM 10110 O  O   . HOH IA 7 .   ? -1.819  -8.902  -16.892 1.00 23.71  ? 421 HOH D O   1 
HETATM 10111 O  O   . HOH IA 7 .   ? -6.646  -7.508  -33.250 1.00 37.50  ? 422 HOH D O   1 
HETATM 10112 O  O   . HOH IA 7 .   ? 14.130  -9.062  -42.361 1.00 26.13  ? 423 HOH D O   1 
HETATM 10113 O  O   . HOH IA 7 .   ? -5.988  13.573  -37.233 1.00 24.04  ? 424 HOH D O   1 
HETATM 10114 O  O   . HOH IA 7 .   ? 15.298  18.375  -54.382 1.00 30.84  ? 425 HOH D O   1 
HETATM 10115 O  O   . HOH IA 7 .   ? 21.155  18.520  -42.601 1.00 23.44  ? 426 HOH D O   1 
HETATM 10116 O  O   . HOH IA 7 .   ? -6.112  4.250   -24.490 1.00 22.02  ? 427 HOH D O   1 
HETATM 10117 O  O   . HOH IA 7 .   ? 22.826  13.820  -28.612 1.00 23.81  ? 428 HOH D O   1 
HETATM 10118 O  O   . HOH IA 7 .   ? -2.599  11.328  -58.020 1.00 41.12  ? 429 HOH D O   1 
HETATM 10119 O  O   . HOH IA 7 .   ? 20.418  -6.503  -44.596 1.00 27.73  ? 430 HOH D O   1 
HETATM 10120 O  O   . HOH IA 7 .   ? 12.196  7.014   -39.371 1.00 9.71   ? 431 HOH D O   1 
HETATM 10121 O  O   . HOH IA 7 .   ? 13.427  22.646  -35.938 1.00 44.74  ? 432 HOH D O   1 
HETATM 10122 O  O   . HOH IA 7 .   ? 23.108  1.328   -19.001 1.00 31.44  ? 433 HOH D O   1 
HETATM 10123 O  O   . HOH IA 7 .   ? 14.625  -11.913 -34.466 1.00 28.47  ? 434 HOH D O   1 
HETATM 10124 O  O   . HOH IA 7 .   ? -15.312 -2.206  -43.920 1.00 26.76  ? 435 HOH D O   1 
HETATM 10125 O  O   . HOH IA 7 .   ? -6.202  -9.052  -37.550 1.00 34.99  ? 436 HOH D O   1 
HETATM 10126 O  O   . HOH IA 7 .   ? -5.431  19.611  -21.916 1.00 30.96  ? 437 HOH D O   1 
HETATM 10127 O  O   . HOH IA 7 .   ? 13.435  15.851  -47.636 1.00 27.41  ? 438 HOH D O   1 
HETATM 10128 O  O   . HOH IA 7 .   ? 14.438  19.788  -42.620 1.00 35.33  ? 439 HOH D O   1 
HETATM 10129 O  O   . HOH IA 7 .   ? 10.979  13.509  -58.472 1.00 17.25  ? 440 HOH D O   1 
HETATM 10130 O  O   . HOH IA 7 .   ? 8.093   11.475  -20.619 1.00 45.62  ? 441 HOH D O   1 
HETATM 10131 O  O   . HOH IA 7 .   ? 1.189   9.400   -59.346 1.00 25.15  ? 442 HOH D O   1 
HETATM 10132 O  O   . HOH IA 7 .   ? 20.539  -7.562  -29.878 1.00 14.51  ? 443 HOH D O   1 
HETATM 10133 O  O   . HOH IA 7 .   ? 14.267  -8.215  -52.703 1.00 25.40  ? 444 HOH D O   1 
HETATM 10134 O  O   . HOH IA 7 .   ? 8.760   -10.730 -31.283 1.00 17.37  ? 445 HOH D O   1 
HETATM 10135 O  O   . HOH IA 7 .   ? 4.469   16.961  -18.080 1.00 38.15  ? 446 HOH D O   1 
HETATM 10136 O  O   . HOH IA 7 .   ? -0.618  15.952  -45.074 1.00 50.70  ? 447 HOH D O   1 
HETATM 10137 O  O   . HOH IA 7 .   ? 11.136  17.926  -54.687 1.00 22.66  ? 448 HOH D O   1 
HETATM 10138 O  O   . HOH IA 7 .   ? -12.184 -4.828  -44.572 1.00 25.43  ? 449 HOH D O   1 
HETATM 10139 O  O   . HOH IA 7 .   ? 14.163  6.036   -60.158 1.00 25.00  ? 450 HOH D O   1 
HETATM 10140 O  O   . HOH IA 7 .   ? 16.335  19.810  -57.217 1.00 34.65  ? 451 HOH D O   1 
HETATM 10141 O  O   . HOH IA 7 .   ? 8.359   9.655   -21.740 1.00 39.00  ? 452 HOH D O   1 
HETATM 10142 O  O   . HOH IA 7 .   ? -10.609 11.692  -26.232 1.00 23.50  ? 453 HOH D O   1 
HETATM 10143 O  O   . HOH IA 7 .   ? -2.319  11.657  -20.406 1.00 21.97  ? 454 HOH D O   1 
HETATM 10144 O  O   . HOH IA 7 .   ? 16.544  8.187   -51.489 1.00 20.25  ? 455 HOH D O   1 
HETATM 10145 O  O   . HOH IA 7 .   ? 10.875  10.480  -61.471 1.00 36.62  ? 456 HOH D O   1 
HETATM 10146 O  O   . HOH IA 7 .   ? -9.662  8.520   -20.677 1.00 30.75  ? 457 HOH D O   1 
HETATM 10147 O  O   . HOH IA 7 .   ? 12.157  -6.789  -52.214 1.00 23.52  ? 458 HOH D O   1 
HETATM 10148 O  O   . HOH IA 7 .   ? -18.703 5.363   -40.674 1.00 36.36  ? 459 HOH D O   1 
HETATM 10149 O  O   . HOH IA 7 .   ? 0.075   -11.915 -23.207 1.00 43.66  ? 460 HOH D O   1 
HETATM 10150 O  O   . HOH IA 7 .   ? -7.008  -6.794  -51.654 1.00 23.94  ? 461 HOH D O   1 
HETATM 10151 O  O   . HOH IA 7 .   ? 2.287   -11.690 -54.392 1.00 17.99  ? 462 HOH D O   1 
HETATM 10152 O  O   . HOH IA 7 .   ? 1.511   15.487  -46.552 1.00 48.96  ? 463 HOH D O   1 
HETATM 10153 O  O   . HOH IA 7 .   ? -8.142  13.607  -44.499 1.00 30.74  ? 464 HOH D O   1 
HETATM 10154 O  O   . HOH IA 7 .   ? 11.545  -11.096 -27.892 1.00 27.55  ? 465 HOH D O   1 
HETATM 10155 O  O   . HOH IA 7 .   ? -6.834  11.014  -19.654 1.00 14.54  ? 466 HOH D O   1 
HETATM 10156 O  O   . HOH IA 7 .   ? 19.941  8.148   -42.384 1.00 10.50  ? 467 HOH D O   1 
HETATM 10157 O  O   . HOH IA 7 .   ? -5.509  -9.650  -34.919 1.00 30.38  ? 468 HOH D O   1 
HETATM 10158 O  O   . HOH IA 7 .   ? 23.941  9.000   -35.011 1.00 13.54  ? 469 HOH D O   1 
HETATM 10159 O  O   . HOH IA 7 .   ? 11.296  15.717  -50.275 1.00 37.60  ? 470 HOH D O   1 
HETATM 10160 O  O   . HOH IA 7 .   ? -12.439 -7.769  -41.311 1.00 27.00  ? 471 HOH D O   1 
HETATM 10161 O  O   . HOH IA 7 .   ? -6.300  5.248   -56.482 1.00 31.40  ? 472 HOH D O   1 
HETATM 10162 O  O   . HOH IA 7 .   ? 7.770   15.610  -39.432 1.00 27.78  ? 473 HOH D O   1 
HETATM 10163 O  O   . HOH IA 7 .   ? 21.747  -9.624  -19.251 1.00 33.61  ? 474 HOH D O   1 
HETATM 10164 O  O   . HOH IA 7 .   ? 9.304   8.239   -42.878 1.00 16.40  ? 475 HOH D O   1 
HETATM 10165 O  O   . HOH IA 7 .   ? -1.876  -1.504  -22.974 1.00 25.19  ? 476 HOH D O   1 
HETATM 10166 O  O   . HOH IA 7 .   ? 0.497   -12.048 -14.249 1.00 36.62  ? 477 HOH D O   1 
HETATM 10167 O  O   . HOH IA 7 .   ? 19.541  18.951  -39.848 1.00 30.73  ? 478 HOH D O   1 
HETATM 10168 O  O   . HOH IA 7 .   ? -14.442 4.698   -37.339 1.00 22.92  ? 479 HOH D O   1 
HETATM 10169 O  O   . HOH IA 7 .   ? 18.532  5.212   -45.747 1.00 13.31  ? 480 HOH D O   1 
HETATM 10170 O  O   . HOH IA 7 .   ? 4.142   9.900   -41.652 1.00 21.30  ? 481 HOH D O   1 
HETATM 10171 O  O   . HOH IA 7 .   ? -5.603  -7.055  -28.035 1.00 23.07  ? 482 HOH D O   1 
HETATM 10172 O  O   . HOH IA 7 .   ? -6.725  -2.787  -21.300 1.00 33.75  ? 483 HOH D O   1 
HETATM 10173 O  O   . HOH IA 7 .   ? 19.285  8.342   -29.228 1.00 12.21  ? 484 HOH D O   1 
HETATM 10174 O  O   . HOH IA 7 .   ? 20.179  7.383   -35.718 1.00 11.34  ? 485 HOH D O   1 
HETATM 10175 O  O   . HOH IA 7 .   ? 20.676  -6.979  -38.525 1.00 39.55  ? 486 HOH D O   1 
HETATM 10176 O  O   . HOH IA 7 .   ? 20.659  14.004  -47.706 1.00 15.79  ? 487 HOH D O   1 
HETATM 10177 O  O   . HOH IA 7 .   ? 5.297   17.101  -35.838 1.00 38.97  ? 488 HOH D O   1 
HETATM 10178 O  O   . HOH IA 7 .   ? 1.049   2.515   -28.262 1.00 11.73  ? 489 HOH D O   1 
HETATM 10179 O  O   . HOH IA 7 .   ? 15.740  2.405   -59.341 1.00 38.97  ? 490 HOH D O   1 
HETATM 10180 O  O   . HOH IA 7 .   ? -13.388 12.271  -32.516 1.00 35.83  ? 491 HOH D O   1 
HETATM 10181 O  O   . HOH IA 7 .   ? -10.040 15.143  -20.915 1.00 22.25  ? 492 HOH D O   1 
HETATM 10182 O  O   . HOH IA 7 .   ? 4.808   -0.768  -14.736 1.00 43.98  ? 493 HOH D O   1 
HETATM 10183 O  O   . HOH IA 7 .   ? 19.392  -4.077  -34.275 1.00 18.93  ? 494 HOH D O   1 
HETATM 10184 O  O   . HOH IA 7 .   ? -5.303  -10.093 -45.439 1.00 27.21  ? 495 HOH D O   1 
HETATM 10185 O  O   . HOH IA 7 .   ? 0.520   -12.625 -37.116 1.00 16.39  ? 496 HOH D O   1 
HETATM 10186 O  O   . HOH IA 7 .   ? 21.572  -9.656  -26.104 1.00 23.01  ? 497 HOH D O   1 
HETATM 10187 O  O   . HOH IA 7 .   ? 8.683   -14.675 -37.771 1.00 32.90  ? 498 HOH D O   1 
HETATM 10188 O  O   . HOH IA 7 .   ? -2.824  -10.479 -39.662 1.00 22.57  ? 499 HOH D O   1 
HETATM 10189 O  O   . HOH IA 7 .   ? -0.299  19.243  -21.596 1.00 37.90  ? 500 HOH D O   1 
HETATM 10190 O  O   . HOH IA 7 .   ? 8.370   -9.102  -14.103 1.00 32.70  ? 501 HOH D O   1 
HETATM 10191 O  O   . HOH IA 7 .   ? 12.484  20.024  -29.228 1.00 29.26  ? 502 HOH D O   1 
HETATM 10192 O  O   . HOH IA 7 .   ? -11.695 11.353  -45.775 1.00 35.93  ? 503 HOH D O   1 
HETATM 10193 O  O   . HOH IA 7 .   ? 9.449   12.780  -22.657 1.00 28.22  ? 504 HOH D O   1 
HETATM 10194 O  O   . HOH IA 7 .   ? 18.048  7.241   -27.182 1.00 21.23  ? 505 HOH D O   1 
HETATM 10195 O  O   . HOH IA 7 .   ? -5.799  -9.894  -41.972 1.00 32.14  ? 506 HOH D O   1 
HETATM 10196 O  O   . HOH IA 7 .   ? 16.454  0.278   -37.494 1.00 8.60   ? 507 HOH D O   1 
HETATM 10197 O  O   . HOH IA 7 .   ? 9.112   3.411   -52.982 1.00 12.14  ? 508 HOH D O   1 
HETATM 10198 O  O   . HOH IA 7 .   ? -12.825 -1.709  -34.306 1.00 22.56  ? 509 HOH D O   1 
HETATM 10199 O  O   . HOH IA 7 .   ? 11.962  -3.545  -47.317 1.00 11.22  ? 510 HOH D O   1 
HETATM 10200 O  O   . HOH IA 7 .   ? 20.121  21.729  -32.795 1.00 27.08  ? 511 HOH D O   1 
HETATM 10201 O  O   . HOH IA 7 .   ? 0.742   -8.171  -19.062 1.00 21.21  ? 512 HOH D O   1 
HETATM 10202 O  O   . HOH IA 7 .   ? 12.952  11.499  -46.531 1.00 22.31  ? 513 HOH D O   1 
HETATM 10203 O  O   . HOH IA 7 .   ? 10.801  13.301  -61.184 1.00 27.01  ? 514 HOH D O   1 
HETATM 10204 O  O   . HOH IA 7 .   ? -11.587 -7.283  -36.716 1.00 35.89  ? 515 HOH D O   1 
HETATM 10205 O  O   . HOH IA 7 .   ? -8.387  -0.111  -51.817 1.00 17.93  ? 516 HOH D O   1 
HETATM 10206 O  O   . HOH IA 7 .   ? 10.054  -15.099 -27.519 1.00 44.98  ? 517 HOH D O   1 
HETATM 10207 O  O   . HOH IA 7 .   ? 3.569   -13.811 -39.370 1.00 40.46  ? 518 HOH D O   1 
HETATM 10208 O  O   . HOH IA 7 .   ? -12.226 -8.591  -45.325 1.00 39.38  ? 519 HOH D O   1 
HETATM 10209 O  O   . HOH IA 7 .   ? 4.376   -6.908  -34.934 1.00 10.78  ? 520 HOH D O   1 
HETATM 10210 O  O   . HOH IA 7 .   ? 19.075  -11.575 -21.278 1.00 45.81  ? 521 HOH D O   1 
HETATM 10211 O  O   . HOH IA 7 .   ? -7.968  11.904  -36.973 1.00 19.53  ? 522 HOH D O   1 
HETATM 10212 O  O   . HOH IA 7 .   ? 6.745   -13.830 -51.023 1.00 12.26  ? 523 HOH D O   1 
HETATM 10213 O  O   . HOH IA 7 .   ? 13.496  18.513  -32.419 1.00 10.58  ? 524 HOH D O   1 
HETATM 10214 O  O   . HOH IA 7 .   ? -7.042  -3.014  -53.567 1.00 37.94  ? 525 HOH D O   1 
HETATM 10215 O  O   . HOH IA 7 .   ? 18.678  12.863  -58.142 1.00 35.55  ? 526 HOH D O   1 
HETATM 10216 O  O   . HOH IA 7 .   ? 21.421  5.163   -34.250 1.00 9.31   ? 527 HOH D O   1 
HETATM 10217 O  O   . HOH IA 7 .   ? 9.749   8.425   -19.598 1.00 39.07  ? 528 HOH D O   1 
HETATM 10218 O  O   . HOH IA 7 .   ? 8.520   -16.408 -45.329 1.00 29.70  ? 529 HOH D O   1 
HETATM 10219 O  O   . HOH IA 7 .   ? -2.891  11.311  -46.033 1.00 20.68  ? 530 HOH D O   1 
HETATM 10220 O  O   . HOH IA 7 .   ? 7.529   -5.092  -14.631 1.00 30.69  ? 531 HOH D O   1 
HETATM 10221 O  O   . HOH IA 7 .   ? 18.620  -0.538  -46.265 1.00 19.51  ? 532 HOH D O   1 
HETATM 10222 O  O   . HOH IA 7 .   ? -5.146  -13.695 -32.544 1.00 35.46  ? 533 HOH D O   1 
HETATM 10223 O  O   . HOH IA 7 .   ? 6.047   -6.397  -57.602 1.00 14.99  ? 534 HOH D O   1 
HETATM 10224 O  O   . HOH IA 7 .   ? 4.619   16.067  -57.229 1.00 18.33  ? 535 HOH D O   1 
HETATM 10225 O  O   . HOH IA 7 .   ? -12.082 9.953   -23.267 1.00 30.63  ? 536 HOH D O   1 
HETATM 10226 O  O   . HOH IA 7 .   ? -3.370  -5.627  -26.938 1.00 18.45  ? 537 HOH D O   1 
HETATM 10227 O  O   . HOH IA 7 .   ? -9.940  -0.369  -49.601 1.00 18.91  ? 538 HOH D O   1 
HETATM 10228 O  O   . HOH IA 7 .   ? 18.771  -13.115 -33.312 1.00 32.17  ? 539 HOH D O   1 
HETATM 10229 O  O   . HOH IA 7 .   ? 9.170   17.013  -65.360 1.00 33.06  ? 540 HOH D O   1 
HETATM 10230 O  O   . HOH IA 7 .   ? 2.668   21.335  -31.566 1.00 38.62  ? 541 HOH D O   1 
HETATM 10231 O  O   . HOH IA 7 .   ? 22.904  6.394   -38.253 1.00 9.25   ? 542 HOH D O   1 
HETATM 10232 O  O   . HOH IA 7 .   ? 18.861  -3.329  -43.244 1.00 18.00  ? 543 HOH D O   1 
HETATM 10233 O  O   . HOH IA 7 .   ? 18.935  11.782  -50.091 1.00 22.64  ? 544 HOH D O   1 
HETATM 10234 O  O   . HOH IA 7 .   ? 17.430  -11.422 -27.427 1.00 22.41  ? 545 HOH D O   1 
HETATM 10235 O  O   . HOH IA 7 .   ? -8.605  18.560  -22.932 1.00 44.97  ? 546 HOH D O   1 
HETATM 10236 O  O   . HOH IA 7 .   ? -2.216  -7.922  -22.755 1.00 21.53  ? 547 HOH D O   1 
HETATM 10237 O  O   . HOH IA 7 .   ? 20.194  -1.058  -39.772 1.00 24.50  ? 548 HOH D O   1 
HETATM 10238 O  O   . HOH IA 7 .   ? 11.747  4.564   -22.069 1.00 26.74  ? 549 HOH D O   1 
HETATM 10239 O  O   . HOH IA 7 .   ? -10.593 -4.603  -29.686 1.00 29.41  ? 550 HOH D O   1 
HETATM 10240 O  O   . HOH IA 7 .   ? 11.425  19.116  -44.461 1.00 57.25  ? 551 HOH D O   1 
HETATM 10241 O  O   . HOH IA 7 .   ? -12.668 8.428   -55.435 1.00 34.69  ? 552 HOH D O   1 
HETATM 10242 O  O   . HOH IA 7 .   ? 16.494  16.082  -54.474 1.00 24.40  ? 553 HOH D O   1 
HETATM 10243 O  O   . HOH IA 7 .   ? 1.550   -17.391 -44.046 1.00 34.31  ? 554 HOH D O   1 
HETATM 10244 O  O   . HOH IA 7 .   ? 2.837   -3.239  -53.068 1.00 27.43  ? 555 HOH D O   1 
HETATM 10245 O  O   . HOH IA 7 .   ? 17.273  9.018   -57.933 1.00 40.19  ? 556 HOH D O   1 
HETATM 10246 O  O   . HOH IA 7 .   ? 13.865  -12.451 -36.793 1.00 35.90  ? 557 HOH D O   1 
HETATM 10247 O  O   . HOH IA 7 .   ? 18.505  -0.300  -29.531 1.00 13.46  ? 558 HOH D O   1 
HETATM 10248 O  O   . HOH IA 7 .   ? 23.878  18.495  -42.641 1.00 18.88  ? 559 HOH D O   1 
HETATM 10249 O  O   . HOH IA 7 .   ? 18.910  16.722  -41.735 1.00 25.86  ? 560 HOH D O   1 
HETATM 10250 O  O   . HOH IA 7 .   ? 17.013  7.809   -55.626 1.00 29.41  ? 561 HOH D O   1 
HETATM 10251 O  O   . HOH IA 7 .   ? 5.417   12.218  -22.974 1.00 27.53  ? 562 HOH D O   1 
HETATM 10252 O  O   . HOH IA 7 .   ? 16.483  10.729  -50.193 1.00 18.12  ? 563 HOH D O   1 
HETATM 10253 O  O   . HOH IA 7 .   ? 13.953  -13.054 -30.235 1.00 48.51  ? 564 HOH D O   1 
HETATM 10254 O  O   . HOH IA 7 .   ? 12.710  -9.658  -46.235 1.00 15.50  ? 565 HOH D O   1 
HETATM 10255 O  O   . HOH IA 7 .   ? 11.164  3.949   -55.161 1.00 15.57  ? 566 HOH D O   1 
HETATM 10256 O  O   . HOH IA 7 .   ? -15.805 9.631   -47.645 1.00 29.07  ? 567 HOH D O   1 
HETATM 10257 O  O   . HOH IA 7 .   ? 6.251   -14.402 -33.661 1.00 41.05  ? 568 HOH D O   1 
HETATM 10258 O  O   . HOH IA 7 .   ? -2.323  -14.259 -26.337 1.00 32.63  ? 569 HOH D O   1 
HETATM 10259 O  O   . HOH IA 7 .   ? -12.500 -4.402  -47.748 1.00 31.03  ? 570 HOH D O   1 
HETATM 10260 O  O   . HOH IA 7 .   ? 13.640  -11.072 -39.290 1.00 37.13  ? 571 HOH D O   1 
HETATM 10261 O  O   . HOH IA 7 .   ? 13.646  16.385  -26.389 1.00 20.11  ? 572 HOH D O   1 
HETATM 10262 O  O   . HOH IA 7 .   ? 26.307  16.210  -43.554 1.00 20.84  ? 573 HOH D O   1 
HETATM 10263 O  O   . HOH IA 7 .   ? 19.799  11.109  -29.036 1.00 17.41  ? 574 HOH D O   1 
HETATM 10264 O  O   . HOH IA 7 .   ? 2.553   9.341   -24.834 1.00 17.38  ? 575 HOH D O   1 
HETATM 10265 O  O   . HOH IA 7 .   ? -9.492  15.980  -29.021 1.00 36.35  ? 576 HOH D O   1 
HETATM 10266 O  O   . HOH IA 7 .   ? 17.544  17.904  -27.154 1.00 39.81  ? 577 HOH D O   1 
HETATM 10267 O  O   . HOH IA 7 .   ? 16.880  18.807  -42.934 1.00 37.54  ? 578 HOH D O   1 
HETATM 10268 O  O   . HOH IA 7 .   ? 17.711  -10.689 -48.268 1.00 37.30  ? 579 HOH D O   1 
HETATM 10269 O  O   . HOH IA 7 .   ? 6.034   21.469  -25.692 1.00 18.89  ? 580 HOH D O   1 
HETATM 10270 O  O   . HOH IA 7 .   ? -2.323  -8.642  -41.882 1.00 14.84  ? 581 HOH D O   1 
HETATM 10271 O  O   . HOH IA 7 .   ? 0.075   -12.116 -42.480 1.00 17.62  ? 582 HOH D O   1 
HETATM 10272 O  O   . HOH IA 7 .   ? 13.731  7.618   -48.246 1.00 14.16  ? 583 HOH D O   1 
HETATM 10273 O  O   . HOH IA 7 .   ? 15.411  9.888   -47.840 1.00 19.32  ? 584 HOH D O   1 
HETATM 10274 O  O   . HOH IA 7 .   ? 14.298  17.793  -51.936 1.00 35.71  ? 585 HOH D O   1 
HETATM 10275 O  O   . HOH IA 7 .   ? -14.219 9.474   -44.692 1.00 26.15  ? 586 HOH D O   1 
HETATM 10276 O  O   . HOH IA 7 .   ? 5.909   -0.085  -57.878 1.00 21.70  ? 587 HOH D O   1 
HETATM 10277 O  O   . HOH IA 7 .   ? -6.793  0.382   -56.189 1.00 27.81  ? 588 HOH D O   1 
HETATM 10278 O  O   . HOH IA 7 .   ? 23.279  19.619  -46.438 1.00 34.82  ? 589 HOH D O   1 
HETATM 10279 O  O   . HOH IA 7 .   ? 7.769   9.070   -24.379 1.00 16.65  ? 590 HOH D O   1 
HETATM 10280 O  O   . HOH IA 7 .   ? 4.469   23.891  -28.313 1.00 38.88  ? 591 HOH D O   1 
HETATM 10281 O  O   . HOH IA 7 .   ? -16.103 4.403   -41.350 1.00 20.43  ? 592 HOH D O   1 
HETATM 10282 O  O   . HOH IA 7 .   ? 19.149  4.951   -49.269 1.00 19.54  ? 593 HOH D O   1 
HETATM 10283 O  O   . HOH IA 7 .   ? 14.350  13.894  -27.218 1.00 13.96  ? 594 HOH D O   1 
HETATM 10284 O  O   . HOH IA 7 .   ? 2.056   1.276   -20.311 1.00 56.32  ? 595 HOH D O   1 
HETATM 10285 O  O   . HOH IA 7 .   ? 23.528  10.430  -41.421 1.00 17.03  ? 596 HOH D O   1 
HETATM 10286 O  O   . HOH IA 7 .   ? 4.635   19.120  -22.707 1.00 31.78  ? 597 HOH D O   1 
HETATM 10287 O  O   . HOH IA 7 .   ? 11.805  9.071   -47.145 1.00 15.38  ? 598 HOH D O   1 
HETATM 10288 O  O   . HOH IA 7 .   ? 9.055   -10.040 -58.173 1.00 20.79  ? 599 HOH D O   1 
HETATM 10289 O  O   . HOH IA 7 .   ? 12.301  1.827   -18.126 1.00 21.04  ? 600 HOH D O   1 
HETATM 10290 O  O   . HOH IA 7 .   ? 0.763   24.283  -29.435 1.00 88.34  ? 601 HOH D O   1 
HETATM 10291 O  O   . HOH IA 7 .   ? 8.677   -13.358 -29.787 1.00 27.62  ? 602 HOH D O   1 
HETATM 10292 O  O   . HOH IA 7 .   ? 17.139  6.791   -48.930 1.00 18.21  ? 603 HOH D O   1 
HETATM 10293 O  O   . HOH IA 7 .   ? 21.392  6.683   -29.624 1.00 12.93  ? 604 HOH D O   1 
HETATM 10294 O  O   . HOH IA 7 .   ? 19.103  10.082  -35.702 1.00 9.75   ? 605 HOH D O   1 
HETATM 10295 O  O   . HOH IA 7 .   ? -9.149  -5.724  -23.018 1.00 34.11  ? 606 HOH D O   1 
HETATM 10296 O  O   . HOH IA 7 .   ? 11.312  -10.732 -44.102 1.00 26.70  ? 607 HOH D O   1 
HETATM 10297 O  O   . HOH IA 7 .   ? -8.586  16.298  -34.471 1.00 50.17  ? 608 HOH D O   1 
HETATM 10298 O  O   . HOH IA 7 .   ? -15.062 -0.627  -35.867 1.00 31.87  ? 609 HOH D O   1 
HETATM 10299 O  O   . HOH IA 7 .   ? 13.489  -8.594  -55.940 1.00 67.08  ? 610 HOH D O   1 
HETATM 10300 O  O   . HOH IA 7 .   ? 16.255  24.168  -34.181 1.00 22.23  ? 611 HOH D O   1 
HETATM 10301 O  O   . HOH IA 7 .   ? 1.291   -9.886  -31.400 1.00 12.64  ? 612 HOH D O   1 
HETATM 10302 O  O   . HOH IA 7 .   ? -1.469  -7.323  -56.069 1.00 36.31  ? 613 HOH D O   1 
HETATM 10303 O  O   . HOH IA 7 .   ? -11.253 12.225  -30.678 1.00 32.25  ? 614 HOH D O   1 
HETATM 10304 O  O   . HOH IA 7 .   ? 15.823  15.176  -24.109 1.00 31.54  ? 615 HOH D O   1 
HETATM 10305 O  O   . HOH IA 7 .   ? 18.579  -7.538  -40.179 1.00 19.59  ? 616 HOH D O   1 
HETATM 10306 O  O   . HOH IA 7 .   ? 10.502  -10.631 -17.177 1.00 34.60  ? 617 HOH D O   1 
HETATM 10307 O  O   . HOH IA 7 .   ? -18.451 -1.214  -45.387 1.00 40.94  ? 618 HOH D O   1 
HETATM 10308 O  O   . HOH IA 7 .   ? 9.077   17.187  -41.478 1.00 27.44  ? 619 HOH D O   1 
HETATM 10309 O  O   . HOH IA 7 .   ? 19.070  -0.210  -36.916 1.00 14.63  ? 620 HOH D O   1 
HETATM 10310 O  O   . HOH IA 7 .   ? 21.699  0.695   -25.802 1.00 27.95  ? 621 HOH D O   1 
HETATM 10311 O  O   . HOH IA 7 .   ? -14.241 10.552  -36.970 1.00 34.45  ? 622 HOH D O   1 
HETATM 10312 O  O   . HOH IA 7 .   ? 21.973  -11.823 -22.900 1.00 52.00  ? 623 HOH D O   1 
HETATM 10313 O  O   . HOH IA 7 .   ? 10.211  2.384   -21.435 1.00 21.15  ? 624 HOH D O   1 
HETATM 10314 O  O   . HOH IA 7 .   ? 18.775  -4.530  -18.282 1.00 40.07  ? 625 HOH D O   1 
HETATM 10315 O  O   . HOH IA 7 .   ? 12.989  13.553  -48.395 1.00 25.32  ? 626 HOH D O   1 
HETATM 10316 O  O   . HOH IA 7 .   ? 13.684  1.320   -55.654 1.00 25.38  ? 627 HOH D O   1 
HETATM 10317 O  O   . HOH IA 7 .   ? 1.306   16.959  -37.879 1.00 40.79  ? 628 HOH D O   1 
HETATM 10318 O  O   . HOH IA 7 .   ? 9.829   -13.422 -55.663 1.00 34.99  ? 629 HOH D O   1 
HETATM 10319 O  O   . HOH IA 7 .   ? -10.642 19.439  -31.100 1.00 24.72  ? 630 HOH D O   1 
HETATM 10320 O  O   . HOH IA 7 .   ? -2.574  14.004  -56.548 1.00 29.33  ? 631 HOH D O   1 
HETATM 10321 O  O   . HOH IA 7 .   ? -11.689 12.613  -38.300 1.00 34.09  ? 632 HOH D O   1 
HETATM 10322 O  O   . HOH IA 7 .   ? 20.655  -4.189  -28.593 1.00 22.08  ? 633 HOH D O   1 
HETATM 10323 O  O   . HOH IA 7 .   ? 18.467  23.175  -34.001 1.00 23.28  ? 634 HOH D O   1 
HETATM 10324 O  O   . HOH IA 7 .   ? -9.212  11.166  -45.021 1.00 18.77  ? 635 HOH D O   1 
HETATM 10325 O  O   . HOH IA 7 .   ? -16.916 -4.384  -36.699 1.00 44.48  ? 636 HOH D O   1 
HETATM 10326 O  O   . HOH IA 7 .   ? 20.836  9.471   -26.030 1.00 30.77  ? 637 HOH D O   1 
HETATM 10327 O  O   . HOH IA 7 .   ? 24.886  10.192  -44.062 1.00 24.82  ? 638 HOH D O   1 
HETATM 10328 O  O   . HOH IA 7 .   ? -4.942  -11.191 -28.503 1.00 25.63  ? 639 HOH D O   1 
HETATM 10329 O  O   . HOH IA 7 .   ? 22.591  -1.358  -39.900 1.00 21.68  ? 640 HOH D O   1 
HETATM 10330 O  O   . HOH IA 7 .   ? -0.215  -12.709 -45.466 1.00 14.99  ? 641 HOH D O   1 
HETATM 10331 O  O   . HOH IA 7 .   ? -4.005  10.002  -17.407 1.00 15.36  ? 642 HOH D O   1 
HETATM 10332 O  O   . HOH IA 7 .   ? 5.034   9.280   -23.769 1.00 27.62  ? 643 HOH D O   1 
HETATM 10333 O  O   . HOH IA 7 .   ? -5.939  15.684  -35.490 1.00 22.21  ? 644 HOH D O   1 
HETATM 10334 O  O   . HOH IA 7 .   ? 10.694  20.932  -54.956 1.00 36.50  ? 645 HOH D O   1 
HETATM 10335 O  O   . HOH IA 7 .   ? 23.459  8.223   -45.242 1.00 22.70  ? 646 HOH D O   1 
HETATM 10336 O  O   . HOH IA 7 .   ? 8.552   17.723  -27.370 1.00 21.72  ? 647 HOH D O   1 
HETATM 10337 O  O   . HOH IA 7 .   ? 1.194   -4.890  -54.437 1.00 21.47  ? 648 HOH D O   1 
HETATM 10338 O  O   . HOH IA 7 .   ? -2.119  -3.892  -56.178 1.00 35.52  ? 649 HOH D O   1 
HETATM 10339 O  O   . HOH IA 7 .   ? 7.401   12.877  -41.168 1.00 37.21  ? 650 HOH D O   1 
HETATM 10340 O  O   . HOH IA 7 .   ? 15.471  -7.087  -17.760 1.00 40.38  ? 651 HOH D O   1 
HETATM 10341 O  O   . HOH IA 7 .   ? -5.565  -11.038 -31.144 1.00 30.77  ? 652 HOH D O   1 
HETATM 10342 O  O   . HOH IA 7 .   ? -20.872 9.088   -40.104 1.00 33.71  ? 653 HOH D O   1 
HETATM 10343 O  O   . HOH IA 7 .   ? 2.243   11.391  -61.701 1.00 35.59  ? 654 HOH D O   1 
HETATM 10344 O  O   . HOH IA 7 .   ? 11.728  -2.454  -12.780 1.00 56.04  ? 655 HOH D O   1 
HETATM 10345 O  O   . HOH IA 7 .   ? -3.529  15.332  -44.874 1.00 44.93  ? 656 HOH D O   1 
HETATM 10346 O  O   . HOH IA 7 .   ? 13.985  -10.650 -27.826 1.00 30.58  ? 657 HOH D O   1 
HETATM 10347 O  O   . HOH IA 7 .   ? 11.276  -15.197 -23.155 1.00 46.20  ? 658 HOH D O   1 
HETATM 10348 O  O   . HOH IA 7 .   ? -16.102 3.364   -38.721 1.00 33.58  ? 659 HOH D O   1 
HETATM 10349 O  O   . HOH IA 7 .   ? -0.753  3.518   -20.036 1.00 46.93  ? 660 HOH D O   1 
HETATM 10350 O  O   . HOH IA 7 .   ? 11.503  -10.182 -41.964 1.00 20.51  ? 661 HOH D O   1 
HETATM 10351 O  O   . HOH IA 7 .   ? 10.376  20.331  -51.269 1.00 41.44  ? 662 HOH D O   1 
HETATM 10352 O  O   . HOH IA 7 .   ? 7.996   -12.477 -59.279 1.00 46.10  ? 663 HOH D O   1 
HETATM 10353 O  O   . HOH IA 7 .   ? -1.388  16.142  -38.265 1.00 32.49  ? 664 HOH D O   1 
HETATM 10354 O  O   . HOH IA 7 .   ? -15.284 7.111   -40.872 1.00 29.39  ? 665 HOH D O   1 
HETATM 10355 O  O   . HOH IA 7 .   ? 10.094  -10.762 -20.855 1.00 45.49  ? 666 HOH D O   1 
HETATM 10356 O  O   . HOH IA 7 .   ? -8.267  19.486  -26.267 1.00 32.52  ? 667 HOH D O   1 
HETATM 10357 O  O   . HOH IA 7 .   ? 7.389   0.919   -60.011 1.00 42.31  ? 668 HOH D O   1 
HETATM 10358 O  O   . HOH IA 7 .   ? 13.062  18.382  -64.509 1.00 39.65  ? 669 HOH D O   1 
HETATM 10359 O  O   . HOH IA 7 .   ? -15.711 -1.086  -32.720 1.00 76.00  ? 670 HOH D O   1 
HETATM 10360 O  O   . HOH IA 7 .   ? -1.882  -1.220  -20.331 1.00 33.46  ? 671 HOH D O   1 
HETATM 10361 O  O   . HOH IA 7 .   ? 17.385  -9.575  -41.321 1.00 46.50  ? 672 HOH D O   1 
HETATM 10362 O  O   . HOH IA 7 .   ? 9.044   -13.154 -17.069 1.00 34.36  ? 673 HOH D O   1 
HETATM 10363 O  O   . HOH IA 7 .   ? -2.474  -14.710 -39.755 1.00 32.16  ? 674 HOH D O   1 
HETATM 10364 O  O   . HOH IA 7 .   ? -0.827  23.106  -34.119 1.00 61.31  ? 675 HOH D O   1 
HETATM 10365 O  O   . HOH IA 7 .   ? -2.957  -12.128 -45.367 1.00 21.53  ? 676 HOH D O   1 
HETATM 10366 O  O   . HOH IA 7 .   ? -9.753  10.545  -42.174 1.00 20.44  ? 677 HOH D O   1 
HETATM 10367 O  O   . HOH IA 7 .   ? 10.333  24.684  -33.347 1.00 42.25  ? 678 HOH D O   1 
HETATM 10368 O  O   . HOH IA 7 .   ? -17.065 2.023   -37.078 1.00 39.58  ? 679 HOH D O   1 
HETATM 10369 O  O   . HOH IA 7 .   ? 6.962   10.235  -42.347 1.00 25.49  ? 680 HOH D O   1 
HETATM 10370 O  O   . HOH IA 7 .   ? 11.733  -10.069 -58.033 1.00 17.88  ? 681 HOH D O   1 
HETATM 10371 O  O   . HOH IA 7 .   ? 7.223   -4.072  -58.565 1.00 21.95  ? 682 HOH D O   1 
HETATM 10372 O  O   . HOH IA 7 .   ? 15.439  -11.981 -42.955 1.00 50.55  ? 683 HOH D O   1 
HETATM 10373 O  O   . HOH IA 7 .   ? 8.580   16.937  -25.290 1.00 49.38  ? 684 HOH D O   1 
HETATM 10374 O  O   . HOH IA 7 .   ? 12.067  -12.512 -56.808 1.00 20.54  ? 685 HOH D O   1 
HETATM 10375 O  O   . HOH IA 7 .   ? 2.040   -7.203  -55.796 1.00 24.81  ? 686 HOH D O   1 
HETATM 10376 O  O   . HOH IA 7 .   ? -18.253 10.815  -47.240 1.00 53.05  ? 687 HOH D O   1 
HETATM 10377 O  O   . HOH IA 7 .   ? 3.393   -18.014 -40.189 1.00 183.00 ? 688 HOH D O   1 
HETATM 10378 O  O   . HOH IA 7 .   ? 27.633  13.179  -47.105 1.00 34.36  ? 689 HOH D O   1 
HETATM 10379 O  O   . HOH IA 7 .   ? 11.465  18.181  -52.025 1.00 30.43  ? 690 HOH D O   1 
HETATM 10380 O  O   . HOH IA 7 .   ? 20.654  3.928   -46.885 1.00 17.60  ? 691 HOH D O   1 
HETATM 10381 O  O   . HOH IA 7 .   ? 20.269  -2.611  -36.326 1.00 27.21  ? 692 HOH D O   1 
HETATM 10382 O  O   . HOH IA 7 .   ? -14.557 -5.273  -36.403 1.00 43.46  ? 693 HOH D O   1 
HETATM 10383 O  O   . HOH IA 7 .   ? -6.610  -9.427  -27.183 1.00 31.91  ? 694 HOH D O   1 
HETATM 10384 O  O   . HOH IA 7 .   ? 22.613  7.751   -42.484 1.00 16.14  ? 695 HOH D O   1 
HETATM 10385 O  O   . HOH IA 7 .   ? 3.385   -6.637  -58.124 1.00 21.67  ? 696 HOH D O   1 
HETATM 10386 O  O   . HOH IA 7 .   ? -1.164  10.341  -60.448 1.00 34.19  ? 697 HOH D O   1 
HETATM 10387 O  O   . HOH IA 7 .   ? 14.130  -11.508 -47.462 1.00 35.14  ? 698 HOH D O   1 
HETATM 10388 O  O   . HOH IA 7 .   ? -3.985  -11.524 -42.900 1.00 39.65  ? 699 HOH D O   1 
HETATM 10389 O  O   . HOH IA 7 .   ? 16.530  1.073   -55.286 1.00 52.33  ? 700 HOH D O   1 
HETATM 10390 O  O   . HOH IA 7 .   ? -1.167  -12.496 -39.161 1.00 28.92  ? 701 HOH D O   1 
HETATM 10391 O  O   . HOH IA 7 .   ? -1.885  -11.234 -41.053 1.00 26.31  ? 702 HOH D O   1 
HETATM 10392 O  O   . HOH IA 7 .   ? 22.216  -7.525  -27.676 1.00 20.48  ? 703 HOH D O   1 
HETATM 10393 O  O   . HOH IA 7 .   ? -1.548  1.965   -60.754 1.00 42.84  ? 704 HOH D O   1 
HETATM 10394 O  O   . HOH IA 7 .   ? 23.417  11.996  -50.872 1.00 42.96  ? 705 HOH D O   1 
HETATM 10395 O  O   . HOH IA 7 .   ? 6.246   2.142   -20.554 1.00 39.76  ? 706 HOH D O   1 
HETATM 10396 O  O   . HOH IA 7 .   ? -14.675 9.469   -42.132 1.00 34.01  ? 707 HOH D O   1 
HETATM 10397 O  O   . HOH IA 7 .   ? 19.234  17.397  -25.474 1.00 40.07  ? 708 HOH D O   1 
HETATM 10398 O  O   . HOH IA 7 .   ? 10.052  -11.779 -33.526 1.00 30.07  ? 709 HOH D O   1 
HETATM 10399 O  O   . HOH IA 7 .   ? 0.862   -3.377  -56.491 1.00 36.47  ? 710 HOH D O   1 
HETATM 10400 O  O   . HOH IA 7 .   ? -1.032  -15.365 -44.748 1.00 29.55  ? 711 HOH D O   1 
HETATM 10401 O  O   . HOH IA 7 .   ? -8.387  -10.509 -42.239 1.00 31.33  ? 712 HOH D O   1 
HETATM 10402 O  O   . HOH IA 7 .   ? -3.099  -9.966  -21.293 1.00 28.04  ? 713 HOH D O   1 
HETATM 10403 O  O   . HOH IA 7 .   ? 20.004  -11.295 -27.606 1.00 26.99  ? 714 HOH D O   1 
HETATM 10404 O  O   . HOH IA 7 .   ? 5.207   -2.288  -59.199 1.00 22.65  ? 715 HOH D O   1 
HETATM 10405 O  O   . HOH IA 7 .   ? -3.927  -8.870  -18.823 1.00 28.17  ? 716 HOH D O   1 
HETATM 10406 O  O   . HOH IA 7 .   ? 0.556   -14.749 -41.739 1.00 37.02  ? 717 HOH D O   1 
HETATM 10407 O  O   . HOH IA 7 .   ? 20.882  -1.574  -42.380 1.00 22.04  ? 718 HOH D O   1 
HETATM 10408 O  O   . HOH IA 7 .   ? -15.190 -3.952  -32.110 1.00 52.38  ? 719 HOH D O   1 
HETATM 10409 O  O   . HOH IA 7 .   ? -11.407 -2.532  -49.821 1.00 23.90  ? 720 HOH D O   1 
HETATM 10410 O  O   . HOH IA 7 .   ? 4.333   24.172  -25.904 1.00 29.97  ? 721 HOH D O   1 
HETATM 10411 O  O   . HOH IA 7 .   ? 18.377  8.128   -53.364 1.00 40.20  ? 722 HOH D O   1 
HETATM 10412 O  O   . HOH IA 7 .   ? 19.767  -5.689  -41.983 1.00 19.19  ? 723 HOH D O   1 
HETATM 10413 O  O   . HOH IA 7 .   ? 1.800   -15.634 -39.736 1.00 33.12  ? 724 HOH D O   1 
HETATM 10414 O  O   . HOH IA 7 .   ? -8.946  -5.152  -20.205 1.00 38.03  ? 725 HOH D O   1 
HETATM 10415 O  O   . HOH IA 7 .   ? 11.290  17.142  -24.970 1.00 70.24  ? 726 HOH D O   1 
HETATM 10416 O  O   . HOH IA 7 .   ? -10.913 18.477  -28.472 1.00 38.59  ? 727 HOH D O   1 
HETATM 10417 O  O   . HOH IA 7 .   ? 12.967  22.839  -30.771 1.00 20.03  ? 728 HOH D O   1 
HETATM 10418 O  O   . HOH IA 7 .   ? -4.401  -4.221  -57.836 1.00 36.78  ? 729 HOH D O   1 
HETATM 10419 O  O   . HOH IA 7 .   ? -6.378  -9.048  -52.992 1.00 27.63  ? 730 HOH D O   1 
HETATM 10420 O  O   . HOH IA 7 .   ? 8.557   3.980   -18.412 1.00 43.43  ? 731 HOH D O   1 
HETATM 10421 O  O   . HOH IA 7 .   ? 1.295   -9.933  -56.177 1.00 25.54  ? 732 HOH D O   1 
HETATM 10422 O  O   . HOH IA 7 .   ? 9.185   -4.090  -60.532 1.00 29.11  ? 733 HOH D O   1 
HETATM 10423 O  O   . HOH IA 7 .   ? -12.468 11.036  -41.924 1.00 29.40  ? 734 HOH D O   1 
HETATM 10424 O  O   . HOH IA 7 .   ? -2.725  21.872  -25.944 1.00 34.14  ? 735 HOH D O   1 
HETATM 10425 O  O   . HOH IA 7 .   ? -1.452  16.028  -58.107 1.00 43.32  ? 736 HOH D O   1 
HETATM 10426 O  O   . HOH IA 7 .   ? -9.576  -2.191  -53.426 1.00 45.89  ? 737 HOH D O   1 
HETATM 10427 O  O   . HOH IA 7 .   ? 10.793  3.871   -19.262 1.00 28.65  ? 738 HOH D O   1 
HETATM 10428 O  O   . HOH IA 7 .   ? -8.090  -6.688  -18.421 1.00 37.59  ? 739 HOH D O   1 
HETATM 10429 O  O   . HOH IA 7 .   ? 12.165  -12.857 -34.299 1.00 36.56  ? 740 HOH D O   1 
HETATM 10430 O  O   . HOH IA 7 .   ? 12.199  12.864  -22.338 1.00 31.22  ? 741 HOH D O   1 
HETATM 10431 O  O   . HOH IA 7 .   ? 8.619   -13.630 -35.180 1.00 36.75  ? 742 HOH D O   1 
HETATM 10432 O  O   . HOH IA 7 .   ? 13.137  -12.946 -24.759 1.00 50.57  ? 743 HOH D O   1 
HETATM 10433 O  O   . HOH IA 7 .   ? 27.690  13.139  -49.718 1.00 27.75  ? 744 HOH D O   1 
HETATM 10434 O  O   . HOH IA 7 .   ? -4.667  -13.626 -27.403 1.00 42.12  ? 745 HOH D O   1 
HETATM 10435 O  O   . HOH IA 7 .   ? 11.536  6.116   -19.754 1.00 34.33  ? 746 HOH D O   1 
HETATM 10436 O  O   . HOH IA 7 .   ? 15.069  26.470  -35.230 1.00 29.86  ? 747 HOH D O   1 
HETATM 10437 O  O   . HOH IA 7 .   ? 13.795  7.058   -18.544 1.00 37.78  ? 748 HOH D O   1 
HETATM 10438 O  O   . HOH IA 7 .   ? -6.961  -12.534 -46.144 1.00 39.83  ? 749 HOH D O   1 
HETATM 10439 O  O   . HOH IA 7 .   ? 7.167   -8.367  -59.091 1.00 19.74  ? 750 HOH D O   1 
HETATM 10440 O  O   . HOH IA 7 .   ? 12.534  -13.588 -32.261 1.00 37.60  ? 751 HOH D O   1 
HETATM 10441 O  O   . HOH IA 7 .   ? 14.895  24.515  -31.846 1.00 32.12  ? 752 HOH D O   1 
HETATM 10442 O  O   . HOH IA 7 .   ? 11.613  -14.178 -36.477 1.00 38.55  ? 753 HOH D O   1 
HETATM 10443 O  O   . HOH IA 7 .   ? 14.042  22.111  -28.352 1.00 18.82  ? 754 HOH D O   1 
HETATM 10444 O  O   . HOH IA 7 .   ? 26.293  15.123  -51.267 1.00 35.97  ? 755 HOH D O   1 
HETATM 10445 O  O   . HOH IA 7 .   ? -6.631  -8.903  -18.395 1.00 25.30  ? 756 HOH D O   1 
HETATM 10446 O  O   . HOH IA 7 .   ? 13.176  15.387  -22.572 1.00 33.72  ? 757 HOH D O   1 
HETATM 10447 O  O   . HOH IA 7 .   ? -4.729  -11.420 -22.572 1.00 38.78  ? 758 HOH D O   1 
HETATM 10448 O  O   . HOH IA 7 .   ? -7.892  -10.232 -20.672 1.00 35.35  ? 759 HOH D O   1 
HETATM 10449 O  O   . HOH IA 7 .   ? 2.771   -3.722  -58.646 1.00 37.54  ? 760 HOH D O   1 
HETATM 10450 O  O   . HOH IA 7 .   ? 28.076  17.405  -47.392 1.00 39.58  ? 761 HOH D O   1 
HETATM 10451 O  O   . HOH IA 7 .   ? -4.119  -14.110 -41.798 1.00 34.34  ? 762 HOH D O   1 
HETATM 10452 O  O   . HOH IA 7 .   ? -11.220 -3.908  -52.158 1.00 38.95  ? 763 HOH D O   1 
HETATM 10453 O  O   . HOH IA 7 .   ? 3.148   -9.128  -59.537 1.00 39.00  ? 764 HOH D O   1 
HETATM 10454 O  O   . HOH IA 7 .   ? 16.679  22.944  -27.740 1.00 19.18  ? 765 HOH D O   1 
HETATM 10455 O  O   . HOH IA 7 .   ? 27.280  17.547  -49.831 1.00 43.56  ? 766 HOH D O   1 
HETATM 10456 O  O   . HOH IA 7 .   ? 12.835  11.429  -19.820 1.00 37.39  ? 767 HOH D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N  N   . LYS A  3   ? 1.2351 0.7003 0.5421 0.0425  0.0722  -0.2953 3   LYS A N   
2     C  CA  . LYS A  3   ? 0.5001 0.2445 0.5710 0.0281  -0.1063 -0.1334 3   LYS A CA  
3     C  C   . LYS A  3   ? 0.4945 0.2667 0.9484 -0.0083 -0.0447 -0.2863 3   LYS A C   
4     O  O   . LYS A  3   ? 0.5677 0.4620 0.8535 -0.1052 0.0185  -0.1952 3   LYS A O   
5     C  CB  . LYS A  3   ? 0.3652 0.3057 0.8707 -0.1292 -0.0266 -0.1758 3   LYS A CB  
6     C  CG  . LYS A  3   ? 0.5631 0.5072 0.5483 -0.0652 -0.2879 0.0362  3   LYS A CG  
7     C  CD  . LYS A  3   ? 0.5426 0.3041 0.8000 -0.0445 -0.1174 0.1370  3   LYS A CD  
8     C  CE  . LYS A  3   ? 0.7028 0.7569 0.5464 -0.0540 -0.1119 0.3905  3   LYS A CE  
9     N  NZ  . LYS A  3   ? 0.6567 1.2915 0.5791 -0.5008 -0.0825 0.1598  3   LYS A NZ  
10    N  N   . TRP A  4   ? 0.3652 0.1790 0.2509 -0.0577 -0.0683 -0.0028 4   TRP A N   
11    C  CA  . TRP A  4   ? 0.2619 0.1483 0.2549 -0.0263 -0.0449 0.0099  4   TRP A CA  
12    C  C   . TRP A  4   ? 0.1996 0.1588 0.1615 -0.0126 -0.0318 -0.0179 4   TRP A C   
13    O  O   . TRP A  4   ? 0.2355 0.1872 0.2231 -0.0120 -0.0648 -0.0027 4   TRP A O   
14    C  CB  . TRP A  4   ? 0.2357 0.1687 0.2409 -0.0131 -0.0705 0.0188  4   TRP A CB  
15    C  CG  . TRP A  4   ? 0.2199 0.1299 0.2001 -0.0465 -0.0355 -0.0182 4   TRP A CG  
16    C  CD1 . TRP A  4   ? 0.2145 0.1718 0.2343 -0.0549 -0.0027 0.0146  4   TRP A CD1 
17    C  CD2 . TRP A  4   ? 0.1874 0.1482 0.1890 -0.0366 -0.0373 0.0288  4   TRP A CD2 
18    N  NE1 . TRP A  4   ? 0.1811 0.1964 0.2497 -0.0710 -0.0335 0.0137  4   TRP A NE1 
19    C  CE2 . TRP A  4   ? 0.1908 0.1646 0.1606 -0.0344 -0.0324 0.0300  4   TRP A CE2 
20    C  CE3 . TRP A  4   ? 0.1897 0.1319 0.1847 -0.0252 -0.0566 0.0351  4   TRP A CE3 
21    C  CZ2 . TRP A  4   ? 0.2475 0.1994 0.1818 -0.0076 -0.0837 0.0344  4   TRP A CZ2 
22    C  CZ3 . TRP A  4   ? 0.2165 0.1788 0.1434 0.0310  -0.0302 0.0252  4   TRP A CZ3 
23    C  CH2 . TRP A  4   ? 0.2208 0.1719 0.1949 0.0309  -0.0384 0.0030  4   TRP A CH2 
24    N  N   . THR A  5   ? 0.1940 0.1414 0.2168 0.0055  -0.0405 0.0003  5   THR A N   
25    C  CA  . THR A  5   ? 0.2362 0.1678 0.1883 0.0119  -0.0252 -0.0087 5   THR A CA  
26    C  C   . THR A  5   ? 0.1495 0.1378 0.1641 0.0171  -0.0173 0.0138  5   THR A C   
27    O  O   . THR A  5   ? 0.1764 0.1669 0.1604 0.0198  -0.0292 0.0295  5   THR A O   
28    C  CB  . THR A  5   ? 0.2147 0.1752 0.2308 -0.0024 -0.0230 -0.0390 5   THR A CB  
29    O  OG1 . THR A  5   ? 0.2337 0.2262 0.2422 0.0052  0.0280  -0.0687 5   THR A OG1 
30    C  CG2 . THR A  5   ? 0.3127 0.1890 0.2728 0.0062  -0.0615 -0.0518 5   THR A CG2 
31    N  N   . TYR A  6   ? 0.2467 0.1538 0.1518 0.0392  -0.0212 0.0175  6   TYR A N   
32    C  CA  . TYR A  6   ? 0.2328 0.1204 0.1583 0.0258  0.0153  -0.0054 6   TYR A CA  
33    C  C   . TYR A  6   ? 0.2387 0.1316 0.1781 0.0275  0.0328  -0.0041 6   TYR A C   
34    O  O   . TYR A  6   ? 0.2382 0.1668 0.1732 0.0271  -0.0094 0.0015  6   TYR A O   
35    C  CB  . TYR A  6   ? 0.2467 0.1364 0.2434 0.0582  0.0754  0.0183  6   TYR A CB  
36    C  CG  . TYR A  6   ? 0.2161 0.0970 0.1649 0.0020  0.0300  0.0197  6   TYR A CG  
37    C  CD1 . TYR A  6   ? 0.2242 0.1206 0.1931 -0.0489 0.0384  0.0329  6   TYR A CD1 
38    C  CD2 . TYR A  6   ? 0.2091 0.1028 0.1601 0.0377  0.0346  0.0252  6   TYR A CD2 
39    C  CE1 . TYR A  6   ? 0.2036 0.1547 0.1628 -0.0573 0.0236  0.0511  6   TYR A CE1 
40    C  CE2 . TYR A  6   ? 0.1340 0.0917 0.1629 -0.0154 0.0091  0.0296  6   TYR A CE2 
41    C  CZ  . TYR A  6   ? 0.1525 0.1242 0.1757 -0.0441 0.0017  0.0351  6   TYR A CZ  
42    O  OH  . TYR A  6   ? 0.1599 0.1735 0.1461 -0.0557 0.0003  0.0416  6   TYR A OH  
43    N  N   . PHE A  7   ? 0.3149 0.1777 0.3034 -0.0038 0.1116  -0.0832 7   PHE A N   
44    C  CA  . PHE A  7   ? 0.3199 0.2500 0.2565 0.0108  0.1041  -0.0614 7   PHE A CA  
45    C  C   . PHE A  7   ? 0.3479 0.1895 0.6026 -0.0430 0.1851  -0.0649 7   PHE A C   
46    O  O   . PHE A  7   ? 0.4532 0.2140 0.8956 -0.0894 0.2957  -0.1727 7   PHE A O   
47    C  CB  . PHE A  7   ? 0.3824 0.5296 0.3269 0.0331  0.1697  0.0498  7   PHE A CB  
48    N  N   . GLY A  8   ? 0.3100 0.3204 0.4325 0.0066  0.1053  0.0059  8   GLY A N   
49    C  CA  . GLY A  8   ? 0.3657 0.2958 0.2698 0.0126  0.0049  -0.0113 8   GLY A CA  
50    C  C   . GLY A  8   ? 0.4614 0.2262 0.2917 0.0516  0.0121  -0.0515 8   GLY A C   
51    O  O   . GLY A  8   ? 0.4565 0.2874 0.2996 0.1894  -0.0171 -0.0759 8   GLY A O   
52    N  N   . PRO A  9   ? 0.4165 0.2011 0.3230 0.1141  0.0447  -0.0174 9   PRO A N   
53    C  CA  . PRO A  9   ? 0.4027 0.2628 0.2818 0.1231  0.0531  -0.0322 9   PRO A CA  
54    C  C   . PRO A  9   ? 0.3810 0.2005 0.2892 0.1084  0.0612  -0.0027 9   PRO A C   
55    O  O   . PRO A  9   ? 0.3314 0.2120 0.2748 0.0487  -0.0057 -0.0238 9   PRO A O   
56    C  CB  . PRO A  9   ? 0.6868 0.1341 0.5275 0.1861  0.1086  -0.0178 9   PRO A CB  
57    C  CG  . PRO A  9   ? 0.6134 0.3862 0.5151 0.1428  0.0813  -0.0200 9   PRO A CG  
58    C  CD  . PRO A  9   ? 0.5322 0.3341 0.3089 0.1287  0.0986  -0.0835 9   PRO A CD  
59    N  N   . ASP A  10  ? 0.3697 0.1590 0.2958 0.0806  0.0666  0.0096  10  ASP A N   
60    C  CA  . ASP A  10  ? 0.2811 0.1888 0.2660 -0.0013 -0.0003 -0.0577 10  ASP A CA  
61    C  C   . ASP A  10  ? 0.2610 0.1032 0.2203 -0.0077 0.0026  -0.0041 10  ASP A C   
62    O  O   . ASP A  10  ? 0.2211 0.1976 0.2558 0.0049  -0.0684 -0.0419 10  ASP A O   
63    C  CB  . ASP A  10  ? 0.3601 0.1777 0.2980 -0.0292 -0.0900 -0.0715 10  ASP A CB  
64    C  CG  . ASP A  10  ? 0.6541 0.2378 0.3283 0.0060  -0.0467 -0.0857 10  ASP A CG  
65    O  OD1 . ASP A  10  ? 0.6952 0.2035 0.3898 0.0082  -0.0138 -0.0485 10  ASP A OD1 
66    O  OD2 . ASP A  10  ? 1.0882 0.3231 0.3231 0.0817  -0.1597 -0.1208 10  ASP A OD2 
67    N  N   . GLY A  11  ? 0.2202 0.1371 0.2766 0.0372  -0.0104 -0.0236 11  GLY A N   
68    C  CA  . GLY A  11  ? 0.1906 0.1243 0.1829 0.0299  -0.0361 0.0077  11  GLY A CA  
69    C  C   . GLY A  11  ? 0.1377 0.1028 0.1823 -0.0164 -0.0223 0.0155  11  GLY A C   
70    O  O   . GLY A  11  ? 0.1393 0.0983 0.2037 0.0008  -0.0291 0.0062  11  GLY A O   
71    N  N   . GLU A  12  ? 0.1414 0.0961 0.1687 -0.0148 -0.0159 0.0132  12  GLU A N   
72    C  CA  . GLU A  12  ? 0.1212 0.0788 0.1702 -0.0076 -0.0136 0.0210  12  GLU A CA  
73    C  C   . GLU A  12  ? 0.1028 0.0822 0.1596 0.0062  0.0007  0.0105  12  GLU A C   
74    O  O   . GLU A  12  ? 0.1091 0.1084 0.1578 0.0000  0.0137  0.0342  12  GLU A O   
75    C  CB  . GLU A  12  ? 0.1102 0.0918 0.1841 -0.0098 -0.0241 0.0299  12  GLU A CB  
76    C  CG  . GLU A  12  ? 0.1176 0.0797 0.1702 -0.0017 -0.0126 0.0218  12  GLU A CG  
77    C  CD  . GLU A  12  ? 0.1143 0.0985 0.1611 -0.0044 -0.0054 0.0115  12  GLU A CD  
78    O  OE1 . GLU A  12  ? 0.1044 0.0843 0.1567 0.0020  0.0065  0.0233  12  GLU A OE1 
79    O  OE2 . GLU A  12  ? 0.1606 0.0960 0.1624 0.0085  -0.0020 0.0133  12  GLU A OE2 
80    N  N   . ASN A  13  ? 0.1054 0.0988 0.1669 -0.0081 -0.0048 0.0305  13  ASN A N   
81    C  CA  . ASN A  13  ? 0.1009 0.0710 0.1903 -0.0046 -0.0102 0.0102  13  ASN A CA  
82    C  C   . ASN A  13  ? 0.1012 0.0885 0.1676 -0.0031 -0.0065 0.0241  13  ASN A C   
83    O  O   . ASN A  13  ? 0.1235 0.0806 0.2018 -0.0001 -0.0260 0.0286  13  ASN A O   
84    C  CB  . ASN A  13  ? 0.0989 0.0865 0.1905 -0.0182 -0.0091 0.0250  13  ASN A CB  
85    C  CG  . ASN A  13  ? 0.1001 0.0723 0.1656 0.0021  -0.0163 0.0291  13  ASN A CG  
86    O  OD1 . ASN A  13  ? 0.1082 0.0780 0.2000 -0.0074 0.0109  0.0300  13  ASN A OD1 
87    N  ND2 . ASN A  13  ? 0.0976 0.0888 0.1629 -0.0143 -0.0055 0.0229  13  ASN A ND2 
88    N  N   . SER A  14  ? 0.1220 0.0739 0.1904 -0.0051 -0.0104 0.0275  14  SER A N   
89    C  CA  . SER A  14  ? 0.1462 0.0660 0.2037 -0.0013 -0.0012 0.0065  14  SER A CA  
90    C  C   . SER A  14  ? 0.1261 0.0845 0.1990 -0.0242 -0.0027 0.0138  14  SER A C   
91    O  O   . SER A  14  ? 0.1448 0.0777 0.1941 -0.0204 -0.0102 0.0021  14  SER A O   
92    C  CB  . SER A  14  ? 0.1624 0.0983 0.2348 -0.0194 0.0405  -0.0155 14  SER A CB  
93    O  OG  . SER A  14  ? 0.1971 0.1987 0.3296 -0.0023 0.0270  -0.0324 14  SER A OG  
94    N  N   . TRP A  15  ? 0.0997 0.0827 0.1849 -0.0122 -0.0167 0.0185  15  TRP A N   
95    C  CA  . TRP A  15  ? 0.1263 0.0728 0.1940 -0.0185 -0.0241 0.0410  15  TRP A CA  
96    C  C   . TRP A  15  ? 0.1267 0.0832 0.1696 0.0040  -0.0094 0.0080  15  TRP A C   
97    O  O   . TRP A  15  ? 0.1145 0.0877 0.1985 -0.0206 -0.0110 0.0192  15  TRP A O   
98    C  CB  . TRP A  15  ? 0.1393 0.1097 0.1563 0.0003  -0.0098 0.0295  15  TRP A CB  
99    C  CG  . TRP A  15  ? 0.1112 0.1085 0.1536 -0.0189 -0.0303 0.0208  15  TRP A CG  
100   C  CD1 . TRP A  15  ? 0.1272 0.0918 0.1856 -0.0197 -0.0265 0.0182  15  TRP A CD1 
101   C  CD2 . TRP A  15  ? 0.1045 0.1068 0.1750 -0.0099 -0.0177 0.0156  15  TRP A CD2 
102   N  NE1 . TRP A  15  ? 0.1209 0.0982 0.1797 -0.0077 -0.0163 0.0166  15  TRP A NE1 
103   C  CE2 . TRP A  15  ? 0.1168 0.0924 0.1658 -0.0120 -0.0221 0.0148  15  TRP A CE2 
104   C  CE3 . TRP A  15  ? 0.1125 0.0807 0.1754 -0.0070 -0.0148 0.0100  15  TRP A CE3 
105   C  CZ2 . TRP A  15  ? 0.1103 0.0949 0.1768 -0.0219 -0.0233 0.0333  15  TRP A CZ2 
106   C  CZ3 . TRP A  15  ? 0.1008 0.1071 0.1735 -0.0164 -0.0173 0.0281  15  TRP A CZ3 
107   C  CH2 . TRP A  15  ? 0.0961 0.1073 0.1736 -0.0172 -0.0174 0.0210  15  TRP A CH2 
108   N  N   . SER A  16  ? 0.1199 0.0892 0.1712 0.0017  -0.0153 0.0240  16  SER A N   
109   C  CA  . SER A  16  ? 0.1448 0.0838 0.1723 -0.0151 -0.0076 0.0266  16  SER A CA  
110   C  C   . SER A  16  ? 0.1209 0.0982 0.1834 -0.0035 -0.0204 0.0282  16  SER A C   
111   O  O   . SER A  16  ? 0.1481 0.0870 0.1808 -0.0151 -0.0041 0.0259  16  SER A O   
112   C  CB  . SER A  16  ? 0.1254 0.0847 0.1933 0.0046  -0.0092 0.0132  16  SER A CB  
113   O  OG  . SER A  16  ? 0.1401 0.0949 0.2212 -0.0190 -0.0098 0.0300  16  SER A OG  
114   N  N   A LYS A  17  ? 0.1590 0.0724 0.1832 -0.0103 -0.0082 0.0219  17  LYS A N   
115   N  N   B LYS A  17  ? 0.1441 0.0757 0.1789 -0.0263 -0.0099 0.0230  17  LYS A N   
116   C  CA  A LYS A  17  ? 0.1511 0.0739 0.1448 -0.0275 0.0085  0.0274  17  LYS A CA  
117   C  CA  B LYS A  17  ? 0.1142 0.0888 0.2242 -0.0078 0.0215  -0.0003 17  LYS A CA  
118   C  C   A LYS A  17  ? 0.1532 0.0689 0.1465 -0.0135 -0.0164 -0.0017 17  LYS A C   
119   C  C   B LYS A  17  ? 0.1208 0.0926 0.1657 -0.0126 0.0428  0.0283  17  LYS A C   
120   O  O   A LYS A  17  ? 0.1489 0.0892 0.1321 -0.0102 0.0131  0.0063  17  LYS A O   
121   O  O   B LYS A  17  ? 0.1439 0.0504 0.1554 -0.0121 0.0008  0.0186  17  LYS A O   
122   C  CB  A LYS A  17  ? 0.1333 0.1188 0.1771 -0.0200 0.0060  -0.0065 17  LYS A CB  
123   C  CB  B LYS A  17  ? 0.1371 0.1039 0.2493 0.0212  0.0199  0.0057  17  LYS A CB  
124   C  CG  A LYS A  17  ? 0.1193 0.1416 0.2389 -0.0238 0.0346  -0.0487 17  LYS A CG  
125   C  CG  B LYS A  17  ? 0.1890 0.0985 0.2316 0.0263  -0.0296 0.0060  17  LYS A CG  
126   C  CD  A LYS A  17  ? 0.1738 0.1230 0.2451 -0.0597 -0.0142 -0.0472 17  LYS A CD  
127   C  CD  B LYS A  17  ? 0.2334 0.0395 0.2975 -0.0284 -0.0188 -0.0501 17  LYS A CD  
128   C  CE  A LYS A  17  ? 0.1825 0.1741 0.3415 -0.0754 0.0454  0.1199  17  LYS A CE  
129   C  CE  B LYS A  17  ? 0.2402 0.2440 0.2071 -0.0864 0.0236  -0.1086 17  LYS A CE  
130   N  NZ  A LYS A  17  ? 0.1642 0.2488 0.3508 -0.0057 -0.0006 0.0318  17  LYS A NZ  
131   N  NZ  B LYS A  17  ? 0.2375 0.1759 0.2154 0.0189  -0.0089 -0.1040 17  LYS A NZ  
132   N  N   A LYS A  18  ? 0.1572 0.0573 0.1650 -0.0152 -0.0214 0.0291  18  LYS A N   
133   N  N   B LYS A  18  ? 0.1272 0.0920 0.1583 -0.0167 0.0109  0.0142  18  LYS A N   
134   C  CA  A LYS A  18  ? 0.1393 0.1459 0.1851 -0.0198 -0.0291 0.0441  18  LYS A CA  
135   C  CA  B LYS A  18  ? 0.1636 0.0529 0.2233 -0.0593 -0.0231 0.0300  18  LYS A CA  
136   C  C   A LYS A  18  ? 0.1639 0.1055 0.1951 -0.0408 -0.0135 0.0261  18  LYS A C   
137   C  C   B LYS A  18  ? 0.1358 0.0989 0.2030 -0.0454 -0.0231 0.0309  18  LYS A C   
138   O  O   A LYS A  18  ? 0.1504 0.1145 0.1947 -0.0086 -0.0410 0.0240  18  LYS A O   
139   O  O   B LYS A  18  ? 0.1395 0.1226 0.2073 -0.0527 -0.0498 0.0617  18  LYS A O   
140   C  CB  A LYS A  18  ? 0.1558 0.1757 0.1883 -0.0776 -0.0261 0.0659  18  LYS A CB  
141   C  CB  B LYS A  18  ? 0.1985 0.0631 0.2258 -0.0096 -0.0438 -0.0219 18  LYS A CB  
142   C  CG  A LYS A  18  ? 0.2583 0.2775 0.3016 -0.0900 -0.0445 -0.0456 18  LYS A CG  
143   C  CG  B LYS A  18  ? 0.2063 0.1559 0.2204 -0.0423 -0.0427 -0.0024 18  LYS A CG  
144   C  CD  A LYS A  18  ? 0.3504 0.2181 0.2772 0.0230  0.0560  0.0474  18  LYS A CD  
145   C  CE  A LYS A  18  ? 0.4713 0.2107 0.1897 0.0816  -0.0416 0.0637  18  LYS A CE  
146   N  NZ  A LYS A  18  ? 0.3637 0.4863 0.2587 -0.0456 -0.1090 0.0984  18  LYS A NZ  
147   N  N   . TYR A  19  ? 0.1498 0.0794 0.2166 -0.0133 -0.0110 0.0241  19  TYR A N   
148   C  CA  . TYR A  19  ? 0.1384 0.0987 0.1958 -0.0225 -0.0077 0.0377  19  TYR A CA  
149   C  C   . TYR A  19  ? 0.1188 0.0918 0.2071 -0.0193 -0.0080 0.0196  19  TYR A C   
150   O  O   . TYR A  19  ? 0.1221 0.0904 0.1999 -0.0175 -0.0017 0.0296  19  TYR A O   
151   C  CB  . TYR A  19  ? 0.1405 0.1077 0.1941 -0.0318 -0.0122 0.0461  19  TYR A CB  
152   C  CG  . TYR A  19  ? 0.1526 0.1024 0.2089 -0.0318 -0.0362 0.0357  19  TYR A CG  
153   C  CD1 . TYR A  19  ? 0.1565 0.1066 0.2590 -0.0386 -0.0212 0.0245  19  TYR A CD1 
154   C  CD2 . TYR A  19  ? 0.1991 0.0988 0.2066 -0.0076 -0.0230 0.0454  19  TYR A CD2 
155   C  CE1 . TYR A  19  ? 0.2221 0.1094 0.3012 -0.0060 -0.0785 0.0020  19  TYR A CE1 
156   C  CE2 . TYR A  19  ? 0.2187 0.1310 0.2384 -0.0102 -0.0403 0.0445  19  TYR A CE2 
157   C  CZ  . TYR A  19  ? 0.2736 0.1459 0.2786 -0.0296 -0.0833 0.0027  19  TYR A CZ  
158   O  OH  . TYR A  19  ? 0.3113 0.1942 0.2515 -0.0219 -0.1092 0.0274  19  TYR A OH  
159   N  N   A PRO A  20  ? 0.1356 0.0912 0.2479 -0.0269 -0.0005 0.0458  20  PRO A N   
160   N  N   B PRO A  20  ? 0.1599 0.1021 0.2212 -0.0331 -0.0370 0.0410  20  PRO A N   
161   C  CA  A PRO A  20  ? 0.1588 0.0733 0.2364 -0.0197 -0.0027 0.0410  20  PRO A CA  
162   C  CA  B PRO A  20  ? 0.1285 0.1288 0.2166 -0.0234 -0.0303 0.0581  20  PRO A CA  
163   C  C   A PRO A  20  ? 0.0969 0.0894 0.2027 -0.0304 0.0143  0.0313  20  PRO A C   
164   C  C   B PRO A  20  ? 0.1351 0.1319 0.1766 -0.0020 -0.0198 0.0763  20  PRO A C   
165   O  O   A PRO A  20  ? 0.0982 0.0879 0.2050 0.0060  -0.0170 0.0509  20  PRO A O   
166   O  O   B PRO A  20  ? 0.1328 0.1383 0.2005 -0.0337 0.0175  0.0516  20  PRO A O   
167   C  CB  A PRO A  20  ? 0.1134 0.1019 0.1896 0.0115  0.0208  0.0339  20  PRO A CB  
168   C  CB  B PRO A  20  ? 0.2793 0.1168 0.2682 -0.0430 -0.0443 0.0798  20  PRO A CB  
169   C  CG  A PRO A  20  ? 0.1653 0.0714 0.2052 -0.0436 0.0119  0.0623  20  PRO A CG  
170   C  CG  B PRO A  20  ? 0.2750 0.1466 0.2021 -0.0304 -0.0109 0.0564  20  PRO A CG  
171   C  CD  A PRO A  20  ? 0.1094 0.0868 0.2414 -0.0177 0.0003  0.0529  20  PRO A CD  
172   C  CD  B PRO A  20  ? 0.1949 0.0739 0.2032 -0.0306 -0.0232 0.0386  20  PRO A CD  
173   N  N   . SER A  21  ? 0.1091 0.1036 0.1887 -0.0168 0.0068  0.0654  21  SER A N   
174   C  CA  . SER A  21  ? 0.1222 0.0992 0.2206 -0.0252 0.0119  0.0366  21  SER A CA  
175   C  C   . SER A  21  ? 0.0940 0.1082 0.1732 -0.0126 0.0001  0.0496  21  SER A C   
176   O  O   . SER A  21  ? 0.0991 0.1059 0.1744 -0.0142 -0.0080 0.0421  21  SER A O   
177   C  CB  . SER A  21  ? 0.1075 0.1295 0.2046 -0.0203 0.0164  0.0582  21  SER A CB  
178   O  OG  . SER A  21  ? 0.1071 0.1682 0.2529 -0.0322 0.0262  0.0838  21  SER A OG  
179   N  N   . CYS A  22  ? 0.1096 0.1146 0.1684 -0.0212 -0.0006 0.0621  22  CYS A N   
180   C  CA  . CYS A  22  ? 0.0964 0.1039 0.1746 -0.0322 -0.0015 0.0504  22  CYS A CA  
181   C  C   . CYS A  22  ? 0.0974 0.0864 0.1919 -0.0073 0.0013  0.0504  22  CYS A C   
182   O  O   . CYS A  22  ? 0.1048 0.0967 0.1893 -0.0271 -0.0046 0.0478  22  CYS A O   
183   C  CB  . CYS A  22  ? 0.1068 0.1242 0.1905 -0.0250 0.0063  0.0432  22  CYS A CB  
184   S  SG  . CYS A  22  ? 0.1258 0.1107 0.1800 -0.0198 -0.0034 0.0366  22  CYS A SG  
185   N  N   . GLY A  23  ? 0.0996 0.1111 0.1969 -0.0070 -0.0116 0.0650  23  GLY A N   
186   C  CA  . GLY A  23  ? 0.0997 0.1272 0.1816 -0.0092 -0.0189 0.0476  23  GLY A CA  
187   C  C   . GLY A  23  ? 0.1100 0.1120 0.1980 -0.0211 -0.0010 0.0658  23  GLY A C   
188   O  O   . GLY A  23  ? 0.1193 0.1344 0.1917 -0.0132 -0.0103 0.0650  23  GLY A O   
189   N  N   . GLY A  24  ? 0.0971 0.1527 0.2057 -0.0233 0.0065  0.0917  24  GLY A N   
190   C  CA  . GLY A  24  ? 0.1421 0.1432 0.2032 -0.0082 0.0274  0.0899  24  GLY A CA  
191   C  C   . GLY A  24  ? 0.1675 0.1477 0.1655 -0.0015 -0.0220 0.0964  24  GLY A C   
192   O  O   . GLY A  24  ? 0.1799 0.1572 0.1982 -0.0359 -0.0315 0.0815  24  GLY A O   
193   N  N   . LEU A  25  ? 0.1919 0.1603 0.1583 -0.0114 -0.0168 0.0533  25  LEU A N   
194   C  CA  . LEU A  25  ? 0.2294 0.1597 0.1795 0.0183  -0.0214 0.0720  25  LEU A CA  
195   C  C   . LEU A  25  ? 0.1504 0.1653 0.1594 -0.0303 -0.0153 0.0649  25  LEU A C   
196   O  O   . LEU A  25  ? 0.1597 0.1421 0.1668 -0.0153 -0.0078 0.0700  25  LEU A O   
197   C  CB  . LEU A  25  ? 0.3937 0.2087 0.1111 -0.0003 -0.0505 0.0626  25  LEU A CB  
198   C  CG  . LEU A  25  ? 0.4388 0.1775 0.2077 0.0303  -0.0773 0.0662  25  LEU A CG  
199   C  CD1 . LEU A  25  ? 0.6309 0.2500 0.1768 -0.0379 -0.0337 0.0877  25  LEU A CD1 
200   C  CD2 . LEU A  25  ? 0.4899 0.2685 0.3411 -0.0019 -0.2136 0.0971  25  LEU A CD2 
201   N  N   . LEU A  26  ? 0.2228 0.1599 0.1470 -0.0159 -0.0226 0.0672  26  LEU A N   
202   C  CA  . LEU A  26  ? 0.1768 0.1906 0.1489 -0.0183 -0.0183 0.0428  26  LEU A CA  
203   C  C   . LEU A  26  ? 0.1304 0.1583 0.1263 -0.0146 -0.0104 0.0390  26  LEU A C   
204   O  O   . LEU A  26  ? 0.1217 0.2039 0.1517 0.0077  -0.0003 0.0480  26  LEU A O   
205   C  CB  . LEU A  26  ? 0.1929 0.2143 0.1736 -0.0181 0.0272  0.0731  26  LEU A CB  
206   C  CG  . LEU A  26  ? 0.2626 0.3849 0.2034 -0.0315 0.0706  -0.0174 26  LEU A CG  
207   C  CD1 . LEU A  26  ? 0.2389 0.4893 0.2490 0.0237  0.0450  -0.0214 26  LEU A CD1 
208   C  CD2 . LEU A  26  ? 0.4178 0.2989 0.1696 -0.0763 -0.0068 0.0685  26  LEU A CD2 
209   N  N   . GLN A  27  ? 0.1268 0.1364 0.1376 -0.0114 0.0093  0.0599  27  GLN A N   
210   C  CA  . GLN A  27  ? 0.0970 0.0926 0.1209 -0.0118 -0.0015 0.0432  27  GLN A CA  
211   C  C   . GLN A  27  ? 0.0973 0.1082 0.1240 -0.0204 -0.0044 0.0441  27  GLN A C   
212   O  O   . GLN A  27  ? 0.1606 0.1102 0.1508 -0.0214 -0.0309 0.0443  27  GLN A O   
213   C  CB  . GLN A  27  ? 0.0915 0.0927 0.1624 -0.0054 -0.0024 0.0381  27  GLN A CB  
214   C  CG  . GLN A  27  ? 0.1163 0.1070 0.1552 -0.0146 0.0003  0.0568  27  GLN A CG  
215   C  CD  . GLN A  27  ? 0.1136 0.1120 0.1335 -0.0028 0.0103  0.0625  27  GLN A CD  
216   O  OE1 . GLN A  27  ? 0.1054 0.1068 0.1396 -0.0096 0.0096  0.0494  27  GLN A OE1 
217   N  NE2 . GLN A  27  ? 0.1005 0.1150 0.1563 -0.0171 0.0032  0.0571  27  GLN A NE2 
218   N  N   . SER A  28  ? 0.0866 0.1021 0.1124 -0.0027 0.0081  0.0392  28  SER A N   
219   C  CA  . SER A  28  ? 0.0820 0.0989 0.1030 0.0049  0.0093  0.0377  28  SER A CA  
220   C  C   . SER A  28  ? 0.0863 0.1008 0.1130 -0.0049 -0.0020 0.0364  28  SER A C   
221   O  O   . SER A  28  ? 0.0904 0.0904 0.1326 -0.0051 0.0098  0.0309  28  SER A O   
222   C  CB  . SER A  28  ? 0.0816 0.1421 0.1049 0.0024  0.0253  0.0516  28  SER A CB  
223   O  OG  . SER A  28  ? 0.0922 0.1242 0.1106 -0.0038 0.0195  0.0423  28  SER A OG  
224   N  N   . PRO A  29  ? 0.0816 0.0917 0.1181 0.0001  0.0163  0.0280  29  PRO A N   
225   C  CA  . PRO A  29  ? 0.1027 0.0660 0.1224 -0.0057 0.0135  0.0263  29  PRO A CA  
226   C  C   . PRO A  29  ? 0.0791 0.0985 0.1057 -0.0005 0.0221  0.0203  29  PRO A C   
227   O  O   . PRO A  29  ? 0.0830 0.1120 0.1179 -0.0023 0.0046  0.0296  29  PRO A O   
228   C  CB  . PRO A  29  ? 0.1080 0.1075 0.1012 0.0003  0.0208  0.0344  29  PRO A CB  
229   C  CG  . PRO A  29  ? 0.0994 0.0856 0.1230 0.0057  0.0184  0.0179  29  PRO A CG  
230   C  CD  . PRO A  29  ? 0.1115 0.0913 0.1048 0.0096  0.0238  0.0359  29  PRO A CD  
231   N  N   . ILE A  30  ? 0.1046 0.0924 0.1230 -0.0085 0.0129  0.0179  30  ILE A N   
232   C  CA  . ILE A  30  ? 0.1033 0.0987 0.1181 -0.0204 -0.0020 0.0161  30  ILE A CA  
233   C  C   . ILE A  30  ? 0.0890 0.0992 0.1288 -0.0024 0.0164  0.0032  30  ILE A C   
234   O  O   . ILE A  30  ? 0.0854 0.1105 0.1556 -0.0077 0.0127  0.0148  30  ILE A O   
235   C  CB  . ILE A  30  ? 0.1225 0.1265 0.1073 -0.0198 0.0086  0.0155  30  ILE A CB  
236   C  CG1 . ILE A  30  ? 0.0967 0.1775 0.1130 -0.0144 0.0122  0.0065  30  ILE A CG1 
237   C  CG2 . ILE A  30  ? 0.2063 0.1216 0.1154 -0.0185 0.0218  0.0159  30  ILE A CG2 
238   C  CD1 . ILE A  30  ? 0.1544 0.2093 0.1208 -0.0031 0.0452  -0.0177 30  ILE A CD1 
239   N  N   . ASP A  31  ? 0.0992 0.1100 0.1468 -0.0227 0.0032  0.0206  31  ASP A N   
240   C  CA  . ASP A  31  ? 0.1064 0.1017 0.1511 -0.0307 0.0026  0.0215  31  ASP A CA  
241   C  C   . ASP A  31  ? 0.1362 0.0989 0.1155 -0.0266 -0.0043 0.0277  31  ASP A C   
242   O  O   . ASP A  31  ? 0.2236 0.1502 0.1356 -0.0154 -0.0260 0.0136  31  ASP A O   
243   C  CB  . ASP A  31  ? 0.1118 0.1518 0.1775 -0.0425 -0.0093 0.0450  31  ASP A CB  
244   C  CG  . ASP A  31  ? 0.1384 0.1640 0.1457 -0.0487 -0.0094 0.0287  31  ASP A CG  
245   O  OD1 . ASP A  31  ? 0.1163 0.1260 0.1639 -0.0282 0.0054  0.0272  31  ASP A OD1 
246   O  OD2 . ASP A  31  ? 0.1905 0.2217 0.2346 -0.0939 -0.0672 0.0874  31  ASP A OD2 
247   N  N   . LEU A  32  ? 0.1046 0.1310 0.1493 0.0021  0.0076  0.0175  32  LEU A N   
248   C  CA  . LEU A  32  ? 0.1277 0.1416 0.1404 -0.0110 0.0251  0.0167  32  LEU A CA  
249   C  C   . LEU A  32  ? 0.1599 0.2142 0.1224 -0.0344 0.0310  0.0171  32  LEU A C   
250   O  O   . LEU A  32  ? 0.1809 0.1568 0.1789 -0.0348 0.0200  0.0109  32  LEU A O   
251   C  CB  . LEU A  32  ? 0.1435 0.1432 0.1622 -0.0020 0.0230  0.0086  32  LEU A CB  
252   C  CG  . LEU A  32  ? 0.1249 0.1502 0.1366 0.0038  0.0384  0.0157  32  LEU A CG  
253   C  CD1 . LEU A  32  ? 0.1448 0.1739 0.1644 0.0329  0.0274  0.0003  32  LEU A CD1 
254   C  CD2 . LEU A  32  ? 0.1583 0.1976 0.1614 -0.0104 0.0432  0.0491  32  LEU A CD2 
255   N  N   . HIS A  33  ? 0.2536 0.3752 0.1466 -0.1469 -0.0238 0.0412  33  HIS A N   
256   C  CA  . HIS A  33  ? 0.2336 0.4092 0.2278 -0.1468 0.0132  0.0043  33  HIS A CA  
257   C  C   . HIS A  33  ? 0.2423 0.4052 0.2229 -0.1229 -0.0229 0.0515  33  HIS A C   
258   O  O   . HIS A  33  ? 0.2443 0.3594 0.1820 -0.1037 -0.0181 0.0071  33  HIS A O   
259   C  CB  . HIS A  33  ? 0.2608 0.3120 0.2206 -0.0912 -0.0289 0.0634  33  HIS A CB  
260   C  CG  . HIS A  33  ? 0.2010 0.3698 0.2350 -0.0410 -0.0271 0.0654  33  HIS A CG  
261   N  ND1 . HIS A  33  ? 0.2653 0.4395 0.4113 0.0153  -0.0322 0.1115  33  HIS A ND1 
262   C  CD2 . HIS A  33  ? 0.2017 0.5709 0.3438 0.0102  -0.1138 0.0230  33  HIS A CD2 
263   C  CE1 . HIS A  33  ? 0.3206 0.7063 0.3086 -0.1389 -0.0829 0.1282  33  HIS A CE1 
264   N  NE2 . HIS A  33  ? 0.3722 0.6683 0.4219 0.1062  -0.1221 0.0904  33  HIS A NE2 
265   N  N   . SER A  34  ? 0.2373 0.3440 0.3048 -0.0794 -0.0472 0.0901  34  SER A N   
266   C  CA  . SER A  34  ? 0.4115 0.4268 0.4322 -0.2313 -0.0088 0.0274  34  SER A CA  
267   C  C   . SER A  34  ? 0.2296 0.5375 0.4458 -0.1798 -0.0672 0.0423  34  SER A C   
268   O  O   . SER A  34  ? 0.4842 0.4810 0.3695 -0.2374 -0.0538 -0.1571 34  SER A O   
269   C  CB  . SER A  34  ? 0.5665 0.4623 0.7619 -0.3388 0.1327  -0.0524 34  SER A CB  
270   O  OG  . SER A  34  ? 0.7511 0.8169 0.3267 -0.1163 0.2032  -0.0680 34  SER A OG  
271   N  N   . ASP A  35  ? 0.2694 0.5013 0.2937 -0.1633 -0.0662 0.0808  35  ASP A N   
272   C  CA  . ASP A  35  ? 0.2619 0.5465 0.3332 -0.1827 -0.0957 0.0861  35  ASP A CA  
273   C  C   . ASP A  35  ? 0.2561 0.5601 0.2720 -0.1376 -0.1084 0.1121  35  ASP A C   
274   O  O   . ASP A  35  ? 0.3161 0.7767 0.2494 -0.1482 -0.1106 0.1190  35  ASP A O   
275   C  CB  . ASP A  35  ? 0.2027 0.9409 0.3122 -0.1446 -0.0542 0.0538  35  ASP A CB  
276   N  N   . ILE A  36  ? 0.2578 0.4016 0.2242 -0.0819 -0.0851 0.1001  36  ILE A N   
277   C  CA  . ILE A  36  ? 0.1958 0.4025 0.2016 -0.0859 -0.0292 0.0350  36  ILE A CA  
278   C  C   . ILE A  36  ? 0.2088 0.3440 0.2254 -0.0640 -0.0522 0.0353  36  ILE A C   
279   O  O   . ILE A  36  ? 0.2213 0.4151 0.2321 -0.1062 -0.0121 0.0461  36  ILE A O   
280   C  CB  . ILE A  36  ? 0.1985 0.4313 0.1942 -0.0406 -0.0086 0.0844  36  ILE A CB  
281   C  CG1 . ILE A  36  ? 0.3346 0.4178 0.1380 -0.0984 0.0227  0.0166  36  ILE A CG1 
282   C  CG2 . ILE A  36  ? 0.2818 0.3939 0.2533 0.0592  0.0577  0.0700  36  ILE A CG2 
283   C  CD1 . ILE A  36  ? 0.4079 0.4083 0.2054 -0.1317 0.0571  0.0223  36  ILE A CD1 
284   N  N   . LEU A  37  ? 0.2447 0.3626 0.1858 -0.0623 -0.0287 0.0178  37  LEU A N   
285   C  CA  . LEU A  37  ? 0.2630 0.3147 0.1834 -0.0333 -0.0236 0.0228  37  LEU A CA  
286   C  C   . LEU A  37  ? 0.2585 0.4095 0.2086 -0.0384 -0.0456 -0.0261 37  LEU A C   
287   O  O   . LEU A  37  ? 0.2928 0.4656 0.3131 -0.0581 -0.0627 -0.1101 37  LEU A O   
288   C  CB  . LEU A  37  ? 0.2745 0.3436 0.2084 -0.0469 -0.0200 0.0593  37  LEU A CB  
289   C  CG  . LEU A  37  ? 0.2310 0.3810 0.2330 -0.0776 0.0331  0.0706  37  LEU A CG  
290   C  CD1 . LEU A  37  ? 0.3079 0.4864 0.2784 -0.1037 -0.0588 0.1404  37  LEU A CD1 
291   C  CD2 . LEU A  37  ? 0.2063 0.3167 0.1888 -0.0153 0.0156  0.0218  37  LEU A CD2 
292   N  N   . GLN A  38  ? 0.2527 0.3851 0.1913 -0.0546 -0.0315 0.0078  38  GLN A N   
293   C  CA  . GLN A  38  ? 0.2939 0.3470 0.1791 -0.0702 -0.0305 -0.0012 38  GLN A CA  
294   C  C   . GLN A  38  ? 0.2928 0.2906 0.1174 0.0210  -0.0199 0.0043  38  GLN A C   
295   O  O   . GLN A  38  ? 0.3208 0.2754 0.1259 -0.0577 -0.0283 -0.0048 38  GLN A O   
296   C  CB  . GLN A  38  ? 0.3865 0.4568 0.1647 0.0049  -0.0280 0.0564  38  GLN A CB  
297   C  CG  . GLN A  38  ? 0.4313 0.5529 0.2082 0.0835  -0.0048 0.0843  38  GLN A CG  
298   C  CD  . GLN A  38  ? 0.4992 0.4185 0.2429 -0.0502 0.0518  0.0524  38  GLN A CD  
299   O  OE1 . GLN A  38  ? 0.6406 0.7835 0.2256 0.2048  -0.0122 -0.0225 38  GLN A OE1 
300   N  NE2 . GLN A  38  ? 0.3817 0.5709 0.2680 -0.0582 0.0137  0.0786  38  GLN A NE2 
301   N  N   . TYR A  39  ? 0.3864 0.2872 0.1441 -0.0586 -0.0188 -0.0318 39  TYR A N   
302   C  CA  . TYR A  39  ? 0.3982 0.1935 0.1895 -0.0661 0.0162  -0.0017 39  TYR A CA  
303   C  C   . TYR A  39  ? 0.3499 0.2800 0.1392 -0.0590 -0.0115 -0.0265 39  TYR A C   
304   O  O   . TYR A  39  ? 0.4013 0.2879 0.1407 -0.0841 -0.0335 0.0068  39  TYR A O   
305   C  CB  . TYR A  39  ? 0.3655 0.1852 0.1836 -0.0419 0.0037  -0.0527 39  TYR A CB  
306   C  CG  . TYR A  39  ? 0.4077 0.2158 0.1676 -0.0390 0.0015  -0.0394 39  TYR A CG  
307   C  CD1 . TYR A  39  ? 0.3831 0.2333 0.1367 -0.0816 0.0093  -0.0368 39  TYR A CD1 
308   C  CD2 . TYR A  39  ? 0.5020 0.2350 0.1359 -0.1257 -0.0003 -0.0511 39  TYR A CD2 
309   C  CE1 . TYR A  39  ? 0.4701 0.2290 0.2380 0.0238  0.0516  -0.0759 39  TYR A CE1 
310   C  CE2 . TYR A  39  ? 0.5803 0.3598 0.2260 -0.0617 0.1729  -0.1037 39  TYR A CE2 
311   C  CZ  . TYR A  39  ? 0.5626 0.1215 0.2610 -0.0288 0.0861  -0.0412 39  TYR A CZ  
312   O  OH  . TYR A  39  ? 0.6019 0.3876 0.3930 0.1504  0.0318  -0.1627 39  TYR A OH  
313   N  N   . ASP A  40  ? 0.3201 0.2606 0.1046 -0.0678 0.0443  -0.0471 40  ASP A N   
314   C  CA  . ASP A  40  ? 0.3350 0.2556 0.1414 -0.0439 0.0582  -0.0124 40  ASP A CA  
315   C  C   . ASP A  40  ? 0.3686 0.2414 0.1590 -0.0052 0.0926  -0.0115 40  ASP A C   
316   O  O   . ASP A  40  ? 0.3420 0.2470 0.1360 -0.0273 0.0920  -0.0311 40  ASP A O   
317   C  CB  . ASP A  40  ? 0.3707 0.2397 0.2314 -0.1107 0.0615  0.0267  40  ASP A CB  
318   C  CG  . ASP A  40  ? 0.4515 0.2538 0.3659 -0.1089 0.1383  0.0236  40  ASP A CG  
319   O  OD1 . ASP A  40  ? 0.3813 0.4212 0.2328 0.0038  0.0772  0.1146  40  ASP A OD1 
320   O  OD2 . ASP A  40  ? 0.6421 0.2748 0.5885 -0.0837 0.2122  0.0839  40  ASP A OD2 
321   N  N   . ALA A  41  ? 0.5059 0.3048 0.1475 0.0612  0.1014  -0.0520 41  ALA A N   
322   C  CA  . ALA A  41  ? 0.5289 0.2221 0.2718 0.0295  0.0763  -0.0917 41  ALA A CA  
323   C  C   . ALA A  41  ? 0.4429 0.3371 0.1642 -0.0094 0.0798  -0.0259 41  ALA A C   
324   O  O   . ALA A  41  ? 0.5655 0.4633 0.2797 0.2308  0.1392  0.0163  41  ALA A O   
325   C  CB  . ALA A  41  ? 0.7171 0.4052 0.2890 0.1247  0.1944  -0.1436 41  ALA A CB  
326   N  N   . SER A  42  ? 0.4907 0.3291 0.2003 -0.0181 0.2066  0.0283  42  SER A N   
327   C  CA  . SER A  42  ? 0.3745 0.3695 0.3950 0.0465  0.2037  0.1313  42  SER A CA  
328   C  C   . SER A  42  ? 0.4408 0.3885 0.4691 0.0741  0.2610  0.1620  42  SER A C   
329   O  O   . SER A  42  ? 0.2822 0.5188 0.7226 0.0423  0.2217  0.2334  42  SER A O   
330   C  CB  . SER A  42  ? 0.3064 0.3438 0.6115 0.0635  0.2186  0.2151  42  SER A CB  
331   O  OG  . SER A  42  ? 0.4450 0.3833 0.7123 0.1465  0.2915  0.2849  42  SER A OG  
332   N  N   . LEU A  43  ? 0.2876 0.2570 0.2854 -0.0051 0.1568  -0.0153 43  LEU A N   
333   C  CA  . LEU A  43  ? 0.2291 0.2251 0.3515 -0.0001 0.0914  -0.0348 43  LEU A CA  
334   C  C   . LEU A  43  ? 0.2430 0.2132 0.2750 -0.0107 0.1416  -0.0355 43  LEU A C   
335   O  O   . LEU A  43  ? 0.2264 0.2933 0.3212 -0.0337 0.0690  -0.0065 43  LEU A O   
336   C  CB  . LEU A  43  ? 0.2021 0.1883 0.2488 -0.0280 0.0623  -0.0013 43  LEU A CB  
337   C  CG  . LEU A  43  ? 0.2093 0.1906 0.2082 -0.0353 0.0507  -0.0173 43  LEU A CG  
338   C  CD1 . LEU A  43  ? 0.2293 0.1897 0.1669 -0.0335 0.0430  -0.0342 43  LEU A CD1 
339   C  CD2 . LEU A  43  ? 0.2587 0.2150 0.2077 -0.0350 0.0588  -0.0035 43  LEU A CD2 
340   N  N   . THR A  44  ? 0.2360 0.3691 0.1752 -0.0515 0.1010  -0.0934 44  THR A N   
341   C  CA  . THR A  44  ? 0.1921 0.4232 0.2206 -0.0263 0.0913  -0.1008 44  THR A CA  
342   C  C   . THR A  44  ? 0.2077 0.3264 0.2296 -0.0149 0.1055  -0.1196 44  THR A C   
343   O  O   . THR A  44  ? 0.2089 0.2802 0.2026 -0.0197 0.0763  -0.0724 44  THR A O   
344   C  CB  . THR A  44  ? 0.2680 0.5825 0.2786 -0.0454 0.1455  -0.0856 44  THR A CB  
345   O  OG1 . THR A  44  ? 0.2251 0.6363 0.2885 -0.0582 0.1178  0.0427  44  THR A OG1 
346   C  CG2 . THR A  44  ? 0.6007 0.7142 0.2761 0.0864  0.1922  -0.1515 44  THR A CG2 
347   N  N   A PRO A  45  ? 0.2269 0.3592 0.2037 0.0253  0.0524  -0.1318 45  PRO A N   
348   N  N   B PRO A  45  ? 0.1780 0.3869 0.2397 0.0361  0.0976  -0.1080 45  PRO A N   
349   C  CA  A PRO A  45  ? 0.1978 0.2971 0.1836 -0.0315 0.0549  -0.0636 45  PRO A CA  
350   C  CA  B PRO A  45  ? 0.1213 0.2948 0.2529 -0.0098 0.0683  -0.0463 45  PRO A CA  
351   C  C   A PRO A  45  ? 0.1493 0.2960 0.1412 -0.0197 0.0617  -0.0294 45  PRO A C   
352   C  C   B PRO A  45  ? 0.1933 0.2486 0.2398 0.0060  0.0590  -0.0520 45  PRO A C   
353   O  O   A PRO A  45  ? 0.1500 0.2784 0.2034 0.0487  0.0991  -0.0119 45  PRO A O   
354   O  O   B PRO A  45  ? 0.1951 0.3134 0.2050 -0.0632 0.0228  -0.0177 45  PRO A O   
355   C  CB  A PRO A  45  ? 0.2942 0.2257 0.2897 -0.0110 0.1072  -0.1101 45  PRO A CB  
356   C  CB  B PRO A  45  ? 0.2436 0.3129 0.2565 0.0366  0.0443  -0.0560 45  PRO A CB  
357   C  CG  A PRO A  45  ? 0.2183 0.2563 0.2867 -0.0586 0.0885  -0.0854 45  PRO A CG  
358   C  CG  B PRO A  45  ? 0.3671 0.3330 0.3012 0.1009  0.0737  -0.1216 45  PRO A CG  
359   C  CD  A PRO A  45  ? 0.1360 0.3495 0.3192 0.0186  0.1321  -0.0436 45  PRO A CD  
360   C  CD  B PRO A  45  ? 0.2991 0.3334 0.2373 0.0149  0.0173  -0.1668 45  PRO A CD  
361   N  N   . LEU A  46  ? 0.1971 0.2131 0.1631 -0.0111 0.0463  -0.0296 46  LEU A N   
362   C  CA  . LEU A  46  ? 0.1721 0.1953 0.1565 0.0210  0.0324  -0.0081 46  LEU A CA  
363   C  C   . LEU A  46  ? 0.2012 0.2093 0.1396 0.0229  0.0474  0.0048  46  LEU A C   
364   O  O   . LEU A  46  ? 0.2258 0.2442 0.1835 0.0027  0.0293  0.0148  46  LEU A O   
365   C  CB  . LEU A  46  ? 0.1906 0.2116 0.1545 0.0489  0.0408  0.0027  46  LEU A CB  
366   C  CG  . LEU A  46  ? 0.1780 0.2372 0.2339 0.0114  0.0351  0.0414  46  LEU A CG  
367   C  CD1 . LEU A  46  ? 0.1534 0.2509 0.3032 0.0456  0.0320  -0.0450 46  LEU A CD1 
368   C  CD2 . LEU A  46  ? 0.2229 0.2991 0.2720 0.0008  0.0176  0.1024  46  LEU A CD2 
369   N  N   . GLU A  47  ? 0.1683 0.2208 0.1732 0.0136  0.0344  -0.0275 47  GLU A N   
370   C  CA  . GLU A  47  ? 0.1459 0.2190 0.2120 0.0155  0.0096  -0.0186 47  GLU A CA  
371   C  C   . GLU A  47  ? 0.1477 0.1949 0.2339 0.0271  -0.0315 0.0161  47  GLU A C   
372   O  O   . GLU A  47  ? 0.2317 0.2416 0.1626 0.0430  0.0207  0.0381  47  GLU A O   
373   C  CB  . GLU A  47  ? 0.1621 0.3255 0.2962 0.0285  0.0666  -0.0511 47  GLU A CB  
374   C  CG  . GLU A  47  ? 0.3652 0.5034 0.3248 0.1239  0.1145  -0.1441 47  GLU A CG  
375   C  CD  . GLU A  47  ? 0.3169 0.7247 0.4835 -0.0083 0.1128  -0.3116 47  GLU A CD  
376   O  OE1 . GLU A  47  ? 0.6029 1.2725 0.6087 0.1789  0.1626  0.0274  47  GLU A OE1 
377   O  OE2 . GLU A  47  ? 0.4537 1.0877 0.6780 -0.0344 -0.0807 0.1405  47  GLU A OE2 
378   N  N   . PHE A  48  ? 0.1333 0.2246 0.2055 0.0377  0.0043  0.0317  48  PHE A N   
379   C  CA  . PHE A  48  ? 0.1308 0.2102 0.1863 -0.0137 0.0046  0.0138  48  PHE A CA  
380   C  C   . PHE A  48  ? 0.1441 0.2244 0.1863 0.0077  -0.0142 0.0299  48  PHE A C   
381   O  O   . PHE A  48  ? 0.1958 0.2236 0.3045 0.0049  -0.0847 0.0644  48  PHE A O   
382   C  CB  . PHE A  48  ? 0.1444 0.2222 0.2281 -0.0310 0.0081  0.0799  48  PHE A CB  
383   C  CG  . PHE A  48  ? 0.1437 0.2011 0.1337 -0.0059 0.0384  0.0281  48  PHE A CG  
384   C  CD1 . PHE A  48  ? 0.1738 0.2035 0.1455 0.0310  0.0248  -0.0146 48  PHE A CD1 
385   C  CD2 . PHE A  48  ? 0.2117 0.2113 0.1777 -0.0535 0.0579  0.0296  48  PHE A CD2 
386   C  CE1 . PHE A  48  ? 0.1405 0.2305 0.1658 0.0189  0.0366  -0.0357 48  PHE A CE1 
387   C  CE2 . PHE A  48  ? 0.2046 0.2217 0.1899 -0.0286 0.0750  -0.0355 48  PHE A CE2 
388   C  CZ  . PHE A  48  ? 0.1562 0.2506 0.1915 -0.0077 0.0672  -0.0313 48  PHE A CZ  
389   N  N   . GLN A  49  ? 0.1296 0.2438 0.1944 -0.0255 -0.0038 0.0463  49  GLN A N   
390   C  CA  . GLN A  49  ? 0.1188 0.2368 0.1978 0.0154  0.0293  0.0274  49  GLN A CA  
391   C  C   . GLN A  49  ? 0.1009 0.2158 0.1615 -0.0020 0.0120  0.0524  49  GLN A C   
392   O  O   . GLN A  49  ? 0.1121 0.2148 0.1563 0.0082  0.0109  0.0373  49  GLN A O   
393   C  CB  . GLN A  49  ? 0.1728 0.2985 0.1502 -0.0122 0.0645  0.0260  49  GLN A CB  
394   C  CG  . GLN A  49  ? 0.2782 0.3481 0.1536 -0.0381 0.0659  0.0082  49  GLN A CG  
395   C  CD  . GLN A  49  ? 0.4997 0.6711 0.4122 0.1702  0.1675  -0.1764 49  GLN A CD  
396   O  OE1 . GLN A  49  ? 0.5288 0.7042 0.4572 0.0287  0.2318  0.0386  49  GLN A OE1 
397   N  NE2 . GLN A  49  ? 0.5870 0.4874 0.3837 0.1023  0.2910  -0.0744 49  GLN A NE2 
398   N  N   . GLY A  50  ? 0.0996 0.2700 0.1529 0.0164  0.0129  0.0174  50  GLY A N   
399   C  CA  . GLY A  50  ? 0.0836 0.2878 0.1675 0.0023  0.0261  0.0173  50  GLY A CA  
400   C  C   . GLY A  50  ? 0.1315 0.2371 0.1750 -0.0005 0.0113  0.0505  50  GLY A C   
401   O  O   . GLY A  50  ? 0.0931 0.2836 0.1859 -0.0021 0.0219  0.0127  50  GLY A O   
402   N  N   . TYR A  51  ? 0.0973 0.2427 0.1561 0.0136  0.0322  0.0445  51  TYR A N   
403   C  CA  . TYR A  51  ? 0.1057 0.2205 0.1511 0.0111  0.0208  0.0467  51  TYR A CA  
404   C  C   . TYR A  51  ? 0.1141 0.2538 0.1650 0.0322  0.0179  0.0592  51  TYR A C   
405   O  O   . TYR A  51  ? 0.1172 0.2325 0.1459 0.0199  0.0092  0.0421  51  TYR A O   
406   C  CB  . TYR A  51  ? 0.0976 0.2001 0.1606 0.0147  0.0077  0.0074  51  TYR A CB  
407   C  CG  . TYR A  51  ? 0.0992 0.1955 0.1265 0.0154  0.0160  0.0068  51  TYR A CG  
408   C  CD1 . TYR A  51  ? 0.1064 0.1807 0.1416 0.0099  0.0184  0.0225  51  TYR A CD1 
409   C  CD2 . TYR A  51  ? 0.1064 0.1653 0.1525 0.0131  0.0113  0.0266  51  TYR A CD2 
410   C  CE1 . TYR A  51  ? 0.1204 0.1658 0.1475 0.0031  0.0175  0.0063  51  TYR A CE1 
411   C  CE2 . TYR A  51  ? 0.1094 0.1481 0.1358 0.0162  0.0098  0.0284  51  TYR A CE2 
412   C  CZ  . TYR A  51  ? 0.1186 0.1479 0.1678 0.0031  -0.0071 0.0273  51  TYR A CZ  
413   O  OH  . TYR A  51  ? 0.1220 0.1604 0.1729 0.0068  -0.0080 0.0372  51  TYR A OH  
414   N  N   . ASN A  52  ? 0.1109 0.2418 0.1872 0.0362  -0.0031 0.0436  52  ASN A N   
415   C  CA  . ASN A  52  ? 0.1562 0.2402 0.1823 0.0340  -0.0071 0.0381  52  ASN A CA  
416   C  C   . ASN A  52  ? 0.1368 0.2973 0.2044 0.0355  -0.0205 0.0000  52  ASN A C   
417   O  O   . ASN A  52  ? 0.1212 0.3752 0.2867 0.0148  -0.0149 -0.0031 52  ASN A O   
418   C  CB  . ASN A  52  ? 0.1624 0.3084 0.1808 0.0964  0.0201  0.0432  52  ASN A CB  
419   C  CG  . ASN A  52  ? 0.1940 0.3364 0.2712 0.0674  0.0076  0.0961  52  ASN A CG  
420   O  OD1 . ASN A  52  ? 0.1932 0.3950 0.2422 0.0662  0.0098  0.1389  52  ASN A OD1 
421   N  ND2 . ASN A  52  ? 0.3226 0.4684 0.3012 0.2281  0.0181  0.1018  52  ASN A ND2 
422   N  N   . LEU A  53  ? 0.1606 0.3080 0.1574 0.0351  -0.0070 -0.0170 53  LEU A N   
423   C  CA  . LEU A  53  ? 0.1617 0.2644 0.2001 0.0659  -0.0269 -0.0172 53  LEU A CA  
424   C  C   . LEU A  53  ? 0.1344 0.3935 0.2527 0.0724  -0.0584 -0.0829 53  LEU A C   
425   O  O   . LEU A  53  ? 0.2646 0.4271 0.2935 0.0830  -0.1127 0.0159  53  LEU A O   
426   C  CB  . LEU A  53  ? 0.1125 0.3009 0.1958 0.0219  -0.0080 -0.0028 53  LEU A CB  
427   C  CG  . LEU A  53  ? 0.1238 0.2585 0.1588 0.0041  0.0030  0.0320  53  LEU A CG  
428   C  CD1 . LEU A  53  ? 0.1622 0.2484 0.1947 0.0309  -0.0017 0.0197  53  LEU A CD1 
429   C  CD2 . LEU A  53  ? 0.2283 0.2603 0.1666 -0.0560 0.0015  0.0438  53  LEU A CD2 
430   N  N   . SER A  54  ? 0.1100 0.4511 0.3348 0.0640  -0.0518 -0.1226 54  SER A N   
431   C  CA  . SER A  54  ? 0.1712 0.5503 0.3337 0.0705  -0.0557 -0.0185 54  SER A CA  
432   C  C   . SER A  54  ? 0.1782 0.3878 0.3000 0.0162  -0.1013 -0.0208 54  SER A C   
433   O  O   . SER A  54  ? 0.1295 0.4232 0.3395 0.0339  -0.0454 -0.0177 54  SER A O   
434   C  CB  . SER A  54  ? 0.1181 0.6518 0.3549 -0.0254 -0.0560 -0.0832 54  SER A CB  
435   O  OG  . SER A  54  ? 0.1619 0.8260 0.3012 0.0348  -0.0093 -0.1819 54  SER A OG  
436   N  N   . ALA A  55  ? 0.3826 0.3917 0.5013 0.0483  -0.2739 0.0131  55  ALA A N   
437   C  CA  . ALA A  55  ? 0.3375 0.4192 0.4893 -0.0258 -0.2161 0.0771  55  ALA A CA  
438   C  C   . ALA A  55  ? 0.2070 0.4260 0.3889 0.0474  0.0108  -0.0795 55  ALA A C   
439   O  O   . ALA A  55  ? 0.2269 0.5040 0.2892 0.0263  -0.0549 0.0428  55  ALA A O   
440   C  CB  . ALA A  55  ? 0.4990 0.3993 0.5196 0.0034  -0.2779 0.0671  55  ALA A CB  
441   N  N   . ASN A  56  ? 0.1664 0.4726 0.2290 0.0581  -0.0460 -0.0458 56  ASN A N   
442   C  CA  . ASN A  56  ? 0.1534 0.4361 0.2479 0.0258  -0.0170 -0.0175 56  ASN A CA  
443   C  C   . ASN A  56  ? 0.1599 0.4555 0.3404 0.0520  -0.0601 -0.0701 56  ASN A C   
444   O  O   . ASN A  56  ? 0.2472 0.4499 0.4611 -0.0288 -0.1386 -0.0507 56  ASN A O   
445   C  CB  . ASN A  56  ? 0.1701 0.4767 0.2213 0.0582  -0.0116 -0.0148 56  ASN A CB  
446   C  CG  . ASN A  56  ? 0.2238 0.5967 0.3657 0.0788  -0.1006 -0.0709 56  ASN A CG  
447   O  OD1 . ASN A  56  ? 0.3754 0.6460 0.3156 0.1600  -0.1345 -0.0315 56  ASN A OD1 
448   N  ND2 . ASN A  56  ? 0.2588 0.7052 0.4167 0.0284  0.0781  -0.0864 56  ASN A ND2 
449   N  N   A LYS A  57  ? 0.1509 0.4580 0.1538 -0.0074 -0.0006 -0.0656 57  LYS A N   
450   N  N   B LYS A  57  ? 0.2240 0.4788 0.4363 -0.0076 -0.1509 -0.0010 57  LYS A N   
451   C  CA  A LYS A  57  ? 0.1455 0.4511 0.1608 -0.0524 0.0675  0.0571  57  LYS A CA  
452   C  CA  B LYS A  57  ? 0.0731 0.4939 0.5278 0.0048  -0.1548 -0.0003 57  LYS A CA  
453   C  C   A LYS A  57  ? 0.1438 0.3745 0.1405 -0.0680 0.0637  0.0412  57  LYS A C   
454   C  C   B LYS A  57  ? 0.1436 0.4497 0.3871 0.0502  -0.1492 0.0043  57  LYS A C   
455   O  O   A LYS A  57  ? 0.1274 0.2903 0.2269 0.0185  0.0979  0.0886  57  LYS A O   
456   O  O   B LYS A  57  ? 0.2502 0.4401 0.2822 0.0406  -0.1145 -0.0579 57  LYS A O   
457   C  CB  A LYS A  57  ? 0.2005 0.4851 0.1136 -0.0913 0.0676  -0.0551 57  LYS A CB  
458   C  CB  B LYS A  57  ? 0.0811 0.5408 0.4752 0.0291  0.0436  0.0601  57  LYS A CB  
459   C  CG  A LYS A  57  ? 0.0868 0.4720 0.1314 -0.0096 0.0288  -0.0038 57  LYS A CG  
460   C  CG  B LYS A  57  ? 0.2459 0.4788 0.3361 0.0657  -0.0074 -0.0247 57  LYS A CG  
461   C  CD  A LYS A  57  ? 0.1445 0.4189 0.1199 -0.0185 0.0394  -0.0070 57  LYS A CD  
462   C  CD  B LYS A  57  ? 0.1032 0.3113 0.3461 0.0584  0.1255  -0.0331 57  LYS A CD  
463   C  CE  A LYS A  57  ? 0.3756 0.4472 0.3037 0.0557  -0.0719 0.1230  57  LYS A CE  
464   C  CE  B LYS A  57  ? 0.2793 0.4081 0.3402 0.1535  -0.0253 -0.0513 57  LYS A CE  
465   N  NZ  A LYS A  57  ? 0.4025 0.4569 0.3190 0.0458  -0.1019 0.1226  57  LYS A NZ  
466   N  NZ  B LYS A  57  ? 0.1712 0.6611 0.4163 -0.0767 0.0712  -0.3571 57  LYS A NZ  
467   N  N   . GLN A  58  ? 0.1026 0.4108 0.2876 -0.0143 -0.0259 -0.0478 58  GLN A N   
468   C  CA  . GLN A  58  ? 0.1156 0.4774 0.2082 -0.0260 0.0065  -0.0309 58  GLN A CA  
469   C  C   . GLN A  58  ? 0.1145 0.4029 0.2264 -0.0445 0.0007  0.0078  58  GLN A C   
470   O  O   . GLN A  58  ? 0.1429 0.4519 0.2861 -0.0480 -0.0185 0.0599  58  GLN A O   
471   C  CB  . GLN A  58  ? 0.2017 0.5539 0.1996 0.0742  0.0105  -0.0311 58  GLN A CB  
472   C  CG  . GLN A  58  ? 0.2217 0.6229 0.2156 0.0368  -0.0568 -0.0560 58  GLN A CG  
473   C  CD  . GLN A  58  ? 0.1750 0.6646 0.2544 0.1190  -0.0428 -0.0381 58  GLN A CD  
474   O  OE1 . GLN A  58  ? 0.3815 0.4812 0.2730 0.0102  -0.1017 -0.0081 58  GLN A OE1 
475   N  NE2 . GLN A  58  ? 0.1829 0.6492 0.2904 0.0535  -0.0693 -0.1536 58  GLN A NE2 
476   N  N   . PHE A  59  ? 0.1220 0.3943 0.1675 -0.0216 0.0046  -0.0142 59  PHE A N   
477   C  CA  . PHE A  59  ? 0.1453 0.3731 0.1606 0.0233  -0.0187 -0.0194 59  PHE A CA  
478   C  C   . PHE A  59  ? 0.1420 0.3522 0.1380 -0.0110 0.0005  -0.0230 59  PHE A C   
479   O  O   . PHE A  59  ? 0.1355 0.3731 0.1468 -0.0221 -0.0089 0.0032  59  PHE A O   
480   C  CB  . PHE A  59  ? 0.1272 0.3332 0.1531 0.0395  0.0096  -0.0285 59  PHE A CB  
481   C  CG  . PHE A  59  ? 0.1071 0.3452 0.1682 0.0119  0.0105  -0.0216 59  PHE A CG  
482   C  CD1 . PHE A  59  ? 0.1421 0.3846 0.1459 -0.0443 0.0144  -0.0175 59  PHE A CD1 
483   C  CD2 . PHE A  59  ? 0.1216 0.3567 0.1622 0.0181  -0.0296 -0.0309 59  PHE A CD2 
484   C  CE1 . PHE A  59  ? 0.1233 0.3251 0.2583 -0.0170 0.0199  0.0152  59  PHE A CE1 
485   C  CE2 . PHE A  59  ? 0.1387 0.3224 0.1960 -0.0311 0.0196  -0.0315 59  PHE A CE2 
486   C  CZ  . PHE A  59  ? 0.1854 0.3194 0.2026 -0.0203 -0.0197 0.0233  59  PHE A CZ  
487   N  N   . LEU A  60  ? 0.1423 0.3472 0.1545 -0.0086 0.0138  0.0176  60  LEU A N   
488   C  CA  . LEU A  60  ? 0.1324 0.2759 0.1400 -0.0214 -0.0230 0.0182  60  LEU A CA  
489   C  C   . LEU A  60  ? 0.1314 0.2976 0.1188 -0.0250 -0.0105 -0.0153 60  LEU A C   
490   O  O   . LEU A  60  ? 0.1497 0.2996 0.1252 -0.0326 -0.0088 -0.0137 60  LEU A O   
491   C  CB  . LEU A  60  ? 0.1511 0.2755 0.2247 -0.0245 -0.0379 -0.0296 60  LEU A CB  
492   C  CG  . LEU A  60  ? 0.2579 0.2930 0.2416 -0.0706 0.0083  -0.0701 60  LEU A CG  
493   C  CD1 . LEU A  60  ? 0.2509 0.4465 0.2357 -0.0706 0.0186  -0.0951 60  LEU A CD1 
494   C  CD2 . LEU A  60  ? 0.2865 0.3307 0.2944 -0.0834 0.0037  -0.0015 60  LEU A CD2 
495   N  N   . LEU A  61  ? 0.1283 0.3061 0.1254 0.0104  -0.0110 -0.0041 61  LEU A N   
496   C  CA  . LEU A  61  ? 0.1324 0.2834 0.1493 0.0001  0.0046  -0.0181 61  LEU A CA  
497   C  C   . LEU A  61  ? 0.1723 0.2572 0.0935 -0.0241 -0.0040 -0.0041 61  LEU A C   
498   O  O   . LEU A  61  ? 0.1658 0.2888 0.1292 -0.0143 -0.0063 -0.0320 61  LEU A O   
499   C  CB  . LEU A  61  ? 0.1483 0.3698 0.1194 -0.0059 -0.0098 0.0307  61  LEU A CB  
500   C  CG  . LEU A  61  ? 0.1709 0.3400 0.1453 -0.0335 -0.0125 0.0390  61  LEU A CG  
501   C  CD1 . LEU A  61  ? 0.1870 0.3079 0.1614 -0.0529 0.0087  0.0351  61  LEU A CD1 
502   C  CD2 . LEU A  61  ? 0.2210 0.3140 0.1608 -0.0078 0.0000  0.0295  61  LEU A CD2 
503   N  N   A THR A  62  ? 0.1678 0.2529 0.1152 -0.0384 -0.0068 0.0350  62  THR A N   
504   N  N   B THR A  62  ? 0.1611 0.3332 0.1394 0.0649  0.0308  -0.0392 62  THR A N   
505   C  CA  A THR A  62  ? 0.1721 0.1910 0.1581 -0.0850 -0.0186 -0.0182 62  THR A CA  
506   C  CA  B THR A  62  ? 0.2141 0.2984 0.1091 0.0785  0.0097  -0.0339 62  THR A CA  
507   C  C   A THR A  62  ? 0.1541 0.1613 0.1574 -0.0491 -0.0017 -0.0164 62  THR A C   
508   C  C   B THR A  62  ? 0.2145 0.3556 0.1226 0.0524  -0.0133 -0.0198 62  THR A C   
509   O  O   A THR A  62  ? 0.1917 0.2053 0.1658 -0.0694 0.0261  -0.0461 62  THR A O   
510   O  O   B THR A  62  ? 0.1402 0.2205 0.1486 -0.0028 0.0091  0.0278  62  THR A O   
511   C  CB  A THR A  62  ? 0.1592 0.1929 0.1933 -0.0390 0.0013  0.0109  62  THR A CB  
512   C  CB  B THR A  62  ? 0.3172 0.2561 0.2442 0.0192  0.0043  -0.0644 62  THR A CB  
513   O  OG1 A THR A  62  ? 0.1536 0.2646 0.1479 -0.0535 0.0135  -0.0357 62  THR A OG1 
514   O  OG1 B THR A  62  ? 0.2026 0.3564 0.1976 0.0280  0.0273  -0.0048 62  THR A OG1 
515   C  CG2 A THR A  62  ? 0.3242 0.1957 0.2172 0.0292  0.0454  0.0863  62  THR A CG2 
516   C  CG2 B THR A  62  ? 0.3316 0.2885 0.3057 0.0208  -0.0031 -0.1563 62  THR A CG2 
517   N  N   . ASN A  63  ? 0.1475 0.2694 0.1577 -0.0171 0.0062  -0.0107 63  ASN A N   
518   C  CA  . ASN A  63  ? 0.1474 0.2572 0.1554 -0.0077 0.0222  -0.0141 63  ASN A CA  
519   C  C   . ASN A  63  ? 0.1899 0.2176 0.1696 -0.0419 -0.0208 -0.0461 63  ASN A C   
520   O  O   . ASN A  63  ? 0.1870 0.2309 0.1536 -0.0445 -0.0024 -0.0210 63  ASN A O   
521   C  CB  . ASN A  63  ? 0.1425 0.2610 0.1349 -0.0115 0.0174  -0.0271 63  ASN A CB  
522   C  CG  . ASN A  63  ? 0.1441 0.2396 0.1172 -0.0068 0.0125  -0.0461 63  ASN A CG  
523   O  OD1 . ASN A  63  ? 0.1741 0.2606 0.1393 -0.0031 0.0049  -0.0281 63  ASN A OD1 
524   N  ND2 . ASN A  63  ? 0.1790 0.2351 0.1455 -0.0096 0.0379  -0.0500 63  ASN A ND2 
525   N  N   . ASN A  64  ? 0.1832 0.2120 0.1414 -0.0342 -0.0007 0.0003  64  ASN A N   
526   C  CA  . ASN A  64  ? 0.1917 0.1874 0.1915 0.0006  0.0165  -0.0003 64  ASN A CA  
527   C  C   . ASN A  64  ? 0.2294 0.2005 0.1457 -0.0190 0.0060  -0.0458 64  ASN A C   
528   O  O   . ASN A  64  ? 0.2461 0.2257 0.2132 -0.0127 -0.0265 -0.0003 64  ASN A O   
529   C  CB  . ASN A  64  ? 0.2057 0.2452 0.1798 -0.0551 0.0148  -0.0205 64  ASN A CB  
530   C  CG  . ASN A  64  ? 0.1719 0.2917 0.1861 -0.0595 0.0122  -0.0340 64  ASN A CG  
531   O  OD1 . ASN A  64  ? 0.2154 0.1990 0.1536 -0.0410 0.0065  -0.0127 64  ASN A OD1 
532   N  ND2 . ASN A  64  ? 0.4199 0.5465 0.1802 -0.2450 0.1133  -0.0491 64  ASN A ND2 
533   N  N   . GLY A  65  ? 0.2066 0.2026 0.1741 -0.0103 0.0252  -0.0353 65  GLY A N   
534   C  CA  . GLY A  65  ? 0.1957 0.2442 0.1687 -0.0071 0.0359  -0.0060 65  GLY A CA  
535   C  C   . GLY A  65  ? 0.2016 0.2885 0.1901 0.0104  0.0199  -0.0406 65  GLY A C   
536   O  O   . GLY A  65  ? 0.2154 0.4444 0.2594 0.0644  0.0362  -0.0487 65  GLY A O   
537   N  N   . HIS A  66  ? 0.1865 0.1748 0.1691 0.0098  -0.0006 -0.0340 66  HIS A N   
538   C  CA  . HIS A  66  ? 0.1671 0.1735 0.1667 0.0063  -0.0006 -0.0010 66  HIS A CA  
539   C  C   . HIS A  66  ? 0.1606 0.1730 0.1671 0.0031  0.0136  0.0000  66  HIS A C   
540   O  O   . HIS A  66  ? 0.1710 0.1888 0.2773 -0.0265 -0.0210 0.0243  66  HIS A O   
541   C  CB  . HIS A  66  ? 0.2492 0.1711 0.1621 0.0001  -0.0430 0.0012  66  HIS A CB  
542   C  CG  . HIS A  66  ? 0.2370 0.1974 0.2145 0.0051  -0.0366 0.0197  66  HIS A CG  
543   N  ND1 . HIS A  66  ? 0.2380 0.1949 0.2413 -0.0023 -0.0252 0.0057  66  HIS A ND1 
544   C  CD2 . HIS A  66  ? 0.2231 0.2003 0.2168 -0.0194 -0.0286 -0.0074 66  HIS A CD2 
545   C  CE1 . HIS A  66  ? 0.2727 0.1818 0.2540 0.0346  -0.0690 -0.0124 66  HIS A CE1 
546   N  NE2 . HIS A  66  ? 0.2662 0.2118 0.2556 0.0121  -0.0498 0.0399  66  HIS A NE2 
547   N  N   . SER A  67  ? 0.1847 0.1662 0.1606 0.0104  -0.0007 -0.0102 67  SER A N   
548   C  CA  . SER A  67  ? 0.1633 0.1741 0.1545 0.0093  -0.0006 -0.0176 67  SER A CA  
549   C  C   . SER A  67  ? 0.1762 0.1813 0.1220 0.0065  -0.0092 -0.0083 67  SER A C   
550   O  O   . SER A  67  ? 0.1523 0.2129 0.1845 -0.0126 -0.0003 -0.0364 67  SER A O   
551   C  CB  . SER A  67  ? 0.1942 0.1317 0.1465 -0.0120 0.0062  -0.0073 67  SER A CB  
552   O  OG  . SER A  67  ? 0.1795 0.1863 0.1680 0.0132  -0.0138 -0.0207 67  SER A OG  
553   N  N   . VAL A  68  ? 0.1244 0.2003 0.1590 -0.0091 0.0083  0.0137  68  VAL A N   
554   C  CA  . VAL A  68  ? 0.1125 0.2260 0.1224 -0.0049 0.0129  -0.0027 68  VAL A CA  
555   C  C   . VAL A  68  ? 0.1195 0.2157 0.1246 0.0092  0.0221  -0.0250 68  VAL A C   
556   O  O   . VAL A  68  ? 0.1509 0.2296 0.1206 -0.0027 0.0109  0.0060  68  VAL A O   
557   C  CB  . VAL A  68  ? 0.1488 0.2366 0.1312 -0.0182 0.0122  -0.0013 68  VAL A CB  
558   C  CG1 . VAL A  68  ? 0.2222 0.2361 0.1409 -0.0452 0.0239  0.0344  68  VAL A CG1 
559   C  CG2 . VAL A  68  ? 0.1552 0.3966 0.1674 -0.0136 -0.0219 0.0465  68  VAL A CG2 
560   N  N   . LYS A  69  ? 0.1179 0.2599 0.1380 0.0034  0.0119  -0.0076 69  LYS A N   
561   C  CA  . LYS A  69  ? 0.1224 0.2420 0.1168 0.0170  0.0144  -0.0118 69  LYS A CA  
562   C  C   . LYS A  69  ? 0.1435 0.2400 0.0957 -0.0010 -0.0070 -0.0071 69  LYS A C   
563   O  O   . LYS A  69  ? 0.1516 0.3253 0.1260 0.0199  -0.0251 -0.0560 69  LYS A O   
564   C  CB  . LYS A  69  ? 0.1660 0.2093 0.2484 0.0222  -0.0208 0.0219  69  LYS A CB  
565   C  CG  . LYS A  69  ? 0.2682 0.2443 0.2463 0.0428  -0.0234 -0.0377 69  LYS A CG  
566   C  CD  . LYS A  69  ? 0.2531 0.2633 0.4435 -0.0421 -0.0631 0.0966  69  LYS A CD  
567   C  CE  . LYS A  69  ? 0.4081 0.3059 0.3206 -0.0829 0.0038  0.0571  69  LYS A CE  
568   N  NZ  . LYS A  69  ? 0.4857 0.3030 0.3738 -0.1289 -0.0914 0.1199  69  LYS A NZ  
569   N  N   . LEU A  70  ? 0.1017 0.1931 0.1177 -0.0135 0.0105  -0.0148 70  LEU A N   
570   C  CA  . LEU A  70  ? 0.0913 0.2281 0.1224 0.0026  0.0093  -0.0073 70  LEU A CA  
571   C  C   . LEU A  70  ? 0.1045 0.2149 0.1042 -0.0088 0.0102  -0.0104 70  LEU A C   
572   O  O   . LEU A  70  ? 0.1114 0.1967 0.1173 -0.0208 -0.0035 -0.0003 70  LEU A O   
573   C  CB  . LEU A  70  ? 0.1097 0.2166 0.1398 -0.0076 -0.0135 0.0040  70  LEU A CB  
574   C  CG  . LEU A  70  ? 0.1121 0.2082 0.1425 0.0183  0.0060  0.0170  70  LEU A CG  
575   C  CD1 . LEU A  70  ? 0.1240 0.3332 0.1805 -0.0582 -0.0328 0.0472  70  LEU A CD1 
576   C  CD2 . LEU A  70  ? 0.1587 0.2406 0.2143 0.0507  0.0035  -0.0070 70  LEU A CD2 
577   N  N   . ASN A  71  ? 0.1055 0.2178 0.1317 -0.0230 0.0015  0.0006  71  ASN A N   
578   C  CA  . ASN A  71  ? 0.1050 0.2411 0.1287 -0.0206 0.0212  -0.0082 71  ASN A CA  
579   C  C   . ASN A  71  ? 0.0976 0.2439 0.1571 -0.0177 0.0015  0.0057  71  ASN A C   
580   O  O   . ASN A  71  ? 0.1380 0.2994 0.1420 0.0203  -0.0068 0.0071  71  ASN A O   
581   C  CB  . ASN A  71  ? 0.1597 0.2443 0.1886 -0.0604 -0.0043 0.0436  71  ASN A CB  
582   C  CG  . ASN A  71  ? 0.2141 0.3016 0.2450 -0.0788 0.0082  -0.0472 71  ASN A CG  
583   O  OD1 . ASN A  71  ? 0.2240 0.3409 0.2639 -0.0627 0.0176  -0.0273 71  ASN A OD1 
584   N  ND2 . ASN A  71  ? 0.2856 0.2490 0.3361 -0.0956 0.0200  -0.0430 71  ASN A ND2 
585   N  N   . LEU A  72  ? 0.1251 0.2134 0.1321 -0.0260 0.0155  0.0040  72  LEU A N   
586   C  CA  . LEU A  72  ? 0.1021 0.1982 0.1477 0.0034  0.0086  0.0120  72  LEU A CA  
587   C  C   . LEU A  72  ? 0.1256 0.2325 0.1594 -0.0111 0.0198  -0.0136 72  LEU A C   
588   O  O   . LEU A  72  ? 0.1567 0.2246 0.1725 -0.0216 0.0362  0.0189  72  LEU A O   
589   C  CB  . LEU A  72  ? 0.0997 0.2127 0.1504 0.0003  0.0146  0.0057  72  LEU A CB  
590   C  CG  . LEU A  72  ? 0.0939 0.2020 0.1436 0.0041  0.0048  0.0256  72  LEU A CG  
591   C  CD1 . LEU A  72  ? 0.0987 0.1879 0.1615 0.0003  0.0127  0.0024  72  LEU A CD1 
592   C  CD2 . LEU A  72  ? 0.1423 0.2500 0.1565 0.0142  -0.0046 0.0430  72  LEU A CD2 
593   N  N   . PRO A  73  ? 0.1098 0.2208 0.1917 -0.0024 0.0186  0.0125  73  PRO A N   
594   C  CA  . PRO A  73  ? 0.1369 0.2725 0.1881 -0.0161 0.0193  0.0348  73  PRO A CA  
595   C  C   . PRO A  73  ? 0.1159 0.2445 0.1908 -0.0114 0.0037  0.0397  73  PRO A C   
596   O  O   . PRO A  73  ? 0.1150 0.2730 0.1944 0.0043  0.0186  0.0292  73  PRO A O   
597   C  CB  . PRO A  73  ? 0.1332 0.2608 0.2052 0.0035  0.0217  0.0370  73  PRO A CB  
598   C  CG  . PRO A  73  ? 0.1050 0.2325 0.1878 0.0008  0.0231  0.0122  73  PRO A CG  
599   C  CD  . PRO A  73  ? 0.1032 0.2398 0.2125 0.0098  0.0177  0.0142  73  PRO A CD  
600   N  N   . SER A  74  ? 0.1930 0.2458 0.2472 -0.0359 0.0733  0.0359  74  SER A N   
601   C  CA  . SER A  74  ? 0.1804 0.2919 0.2438 0.0020  0.0425  0.0351  74  SER A CA  
602   C  C   . SER A  74  ? 0.1578 0.2563 0.1890 -0.0046 0.0562  0.0489  74  SER A C   
603   O  O   . SER A  74  ? 0.1719 0.3528 0.2188 -0.0096 0.0498  0.0632  74  SER A O   
604   C  CB  . SER A  74  ? 0.2924 0.3822 0.3975 -0.0921 -0.0131 0.1465  74  SER A CB  
605   O  OG  . SER A  74  ? 0.2836 0.3350 0.3617 -0.1014 0.0238  0.0635  74  SER A OG  
606   N  N   . ASP A  75  ? 0.1319 0.2739 0.1967 -0.0116 0.0456  0.0239  75  ASP A N   
607   C  CA  . ASP A  75  ? 0.1033 0.2867 0.2134 -0.0162 0.0175  -0.0122 75  ASP A CA  
608   C  C   . ASP A  75  ? 0.1120 0.2425 0.1620 -0.0116 0.0253  -0.0285 75  ASP A C   
609   O  O   . ASP A  75  ? 0.1055 0.2960 0.2206 -0.0153 0.0399  -0.0366 75  ASP A O   
610   C  CB  . ASP A  75  ? 0.1130 0.3418 0.2542 0.0066  0.0109  0.0284  75  ASP A CB  
611   C  CG  . ASP A  75  ? 0.1653 0.3433 0.2238 0.0122  0.0167  -0.0377 75  ASP A CG  
612   O  OD1 . ASP A  75  ? 0.2597 0.4379 0.2475 0.1005  -0.0390 -0.0264 75  ASP A OD1 
613   O  OD2 . ASP A  75  ? 0.2187 0.4893 0.2723 -0.0649 0.0886  0.0377  75  ASP A OD2 
614   N  N   . MET A  76  ? 0.1118 0.2402 0.1272 -0.0046 0.0113  0.0226  76  MET A N   
615   C  CA  . MET A  76  ? 0.0811 0.2202 0.1421 0.0120  0.0294  0.0394  76  MET A CA  
616   C  C   . MET A  76  ? 0.0897 0.2220 0.1393 -0.0126 0.0130  0.0487  76  MET A C   
617   O  O   . MET A  76  ? 0.0983 0.2233 0.1492 0.0143  0.0294  0.0458  76  MET A O   
618   C  CB  . MET A  76  ? 0.1208 0.2014 0.1696 -0.0116 0.0296  0.0414  76  MET A CB  
619   C  CG  . MET A  76  ? 0.1071 0.2039 0.1553 -0.0043 0.0238  0.0269  76  MET A CG  
620   S  SD  . MET A  76  ? 0.1277 0.2158 0.1464 -0.0141 0.0362  0.0261  76  MET A SD  
621   C  CE  . MET A  76  ? 0.1254 0.2402 0.1509 -0.0170 0.0520  0.0155  76  MET A CE  
622   N  N   . HIS A  77  ? 0.0812 0.2132 0.1249 -0.0133 0.0098  0.0388  77  HIS A N   
623   C  CA  . HIS A  77  ? 0.1012 0.2245 0.1306 -0.0120 0.0142  0.0505  77  HIS A CA  
624   C  C   . HIS A  77  ? 0.0976 0.1833 0.1432 0.0013  0.0182  0.0368  77  HIS A C   
625   O  O   . HIS A  77  ? 0.1177 0.1858 0.1685 0.0077  0.0129  0.0381  77  HIS A O   
626   C  CB  . HIS A  77  ? 0.1226 0.2355 0.1621 -0.0082 0.0447  0.0654  77  HIS A CB  
627   C  CG  . HIS A  77  ? 0.1339 0.2370 0.1673 0.0146  0.0357  0.0661  77  HIS A CG  
628   N  ND1 . HIS A  77  ? 0.1238 0.3274 0.1691 -0.0070 0.0333  0.0296  77  HIS A ND1 
629   C  CD2 . HIS A  77  ? 0.1304 0.3009 0.1929 -0.0010 0.0564  0.0121  77  HIS A CD2 
630   C  CE1 . HIS A  77  ? 0.1124 0.3179 0.1714 -0.0148 0.0244  0.0443  77  HIS A CE1 
631   N  NE2 . HIS A  77  ? 0.1202 0.2829 0.2375 -0.0208 0.0414  0.0326  77  HIS A NE2 
632   N  N   A ILE A  78  ? 0.1125 0.1935 0.1337 -0.0052 -0.0013 0.0147  78  ILE A N   
633   N  N   B ILE A  78  ? 0.1177 0.2104 0.1306 -0.0020 0.0015  0.0184  78  ILE A N   
634   C  CA  A ILE A  78  ? 0.1489 0.1996 0.0976 -0.0212 -0.0001 0.0208  78  ILE A CA  
635   C  CA  B ILE A  78  ? 0.1833 0.2402 0.1128 -0.0395 0.0104  0.0126  78  ILE A CA  
636   C  C   A ILE A  78  ? 0.1233 0.2276 0.1384 -0.0126 0.0142  0.0557  78  ILE A C   
637   C  C   B ILE A  78  ? 0.1344 0.2312 0.1473 -0.0087 0.0227  0.0571  78  ILE A C   
638   O  O   A ILE A  78  ? 0.1377 0.2337 0.1285 -0.0187 0.0370  0.0452  78  ILE A O   
639   O  O   B ILE A  78  ? 0.1577 0.2472 0.1554 -0.0193 0.0230  0.0619  78  ILE A O   
640   C  CB  A ILE A  78  ? 0.0847 0.3831 0.1247 -0.1093 0.0469  -0.0207 78  ILE A CB  
641   C  CB  B ILE A  78  ? 0.1929 0.3959 0.1841 -0.0421 -0.0320 -0.0747 78  ILE A CB  
642   C  CG1 A ILE A  78  ? 0.1212 0.2536 0.0962 -0.0154 0.0399  0.0329  78  ILE A CG1 
643   C  CG1 B ILE A  78  ? 0.3373 0.3501 0.3014 0.0049  -0.0028 0.0310  78  ILE A CG1 
644   C  CG2 A ILE A  78  ? 0.1401 0.2737 0.1263 -0.0247 0.0126  0.0228  78  ILE A CG2 
645   C  CG2 B ILE A  78  ? 0.3434 0.4950 0.2682 0.0031  -0.0771 0.0196  78  ILE A CG2 
646   C  CD1 A ILE A  78  ? 0.0491 0.2502 0.1799 -0.0339 0.0390  0.0149  78  ILE A CD1 
647   C  CD1 B ILE A  78  ? 0.2427 0.3386 0.2138 0.0236  0.0773  0.0304  78  ILE A CD1 
648   N  N   . GLN A  79  ? 0.1601 0.2420 0.1563 0.0155  0.0157  0.0244  79  GLN A N   
649   C  CA  . GLN A  79  ? 0.1782 0.2644 0.1623 0.0308  0.0445  -0.0017 79  GLN A CA  
650   C  C   . GLN A  79  ? 0.1728 0.2709 0.1845 0.0414  0.0317  0.0297  79  GLN A C   
651   O  O   . GLN A  79  ? 0.2059 0.2745 0.1547 -0.0006 0.0326  0.0114  79  GLN A O   
652   C  CB  . GLN A  79  ? 0.1942 0.3650 0.2766 0.0366  0.0430  -0.0661 79  GLN A CB  
653   C  CG  . GLN A  79  ? 0.2524 0.3930 0.3025 0.0595  0.0901  -0.0606 79  GLN A CG  
654   C  CD  . GLN A  79  ? 0.3811 0.6212 0.3740 0.1790  0.0557  -0.0979 79  GLN A CD  
655   O  OE1 . GLN A  79  ? 0.6632 0.9071 0.4715 0.2233  -0.0230 -0.2029 79  GLN A OE1 
656   N  NE2 . GLN A  79  ? 0.7427 1.0679 0.6772 -0.1054 0.4456  -0.2685 79  GLN A NE2 
657   N  N   . GLY A  80  ? 0.2217 0.3147 0.1647 -0.0092 0.0542  0.0037  80  GLY A N   
658   C  CA  . GLY A  80  ? 0.2256 0.3160 0.1637 0.0020  0.0253  0.0096  80  GLY A CA  
659   C  C   . GLY A  80  ? 0.2003 0.3305 0.1283 -0.0156 0.0284  0.0372  80  GLY A C   
660   O  O   . GLY A  80  ? 0.2592 0.3883 0.1716 -0.0509 0.0148  0.0159  80  GLY A O   
661   N  N   . LEU A  81  ? 0.2337 0.3271 0.1561 -0.0348 0.0342  0.0383  81  LEU A N   
662   C  CA  . LEU A  81  ? 0.1572 0.3111 0.1804 -0.0454 0.0243  0.0797  81  LEU A CA  
663   C  C   . LEU A  81  ? 0.2122 0.2716 0.1872 -0.0340 0.0428  0.0700  81  LEU A C   
664   O  O   . LEU A  81  ? 0.2389 0.4271 0.1716 -0.0443 0.0851  0.0386  81  LEU A O   
665   C  CB  . LEU A  81  ? 0.1869 0.2960 0.1597 -0.0340 0.0324  0.0566  81  LEU A CB  
666   C  CG  . LEU A  81  ? 0.1581 0.2511 0.1991 -0.0450 0.0099  0.0663  81  LEU A CG  
667   C  CD1 . LEU A  81  ? 0.2344 0.3312 0.1712 -0.0637 0.0806  0.0229  81  LEU A CD1 
668   C  CD2 . LEU A  81  ? 0.1741 0.2666 0.3319 -0.0474 -0.0307 0.0643  81  LEU A CD2 
669   N  N   . GLN A  82  ? 0.2578 0.2969 0.1247 -0.0397 -0.0017 0.0366  82  GLN A N   
670   C  CA  . GLN A  82  ? 0.2691 0.3240 0.1384 -0.0715 -0.0086 0.0511  82  GLN A CA  
671   C  C   . GLN A  82  ? 0.2689 0.2684 0.1741 -0.0747 0.0520  -0.0210 82  GLN A C   
672   O  O   . GLN A  82  ? 0.3346 0.5415 0.2369 -0.1299 0.0939  0.0582  82  GLN A O   
673   C  CB  . GLN A  82  ? 0.3242 0.3136 0.2084 -0.0895 -0.0670 0.0549  82  GLN A CB  
674   C  CG  . GLN A  82  ? 0.3226 0.4099 0.1694 -0.0331 -0.0299 -0.0309 82  GLN A CG  
675   C  CD  . GLN A  82  ? 0.6211 0.6868 0.2412 -0.1462 0.0564  -0.1674 82  GLN A CD  
676   O  OE1 . GLN A  82  ? 0.5321 0.3377 0.3576 -0.0372 -0.0874 -0.0326 82  GLN A OE1 
677   N  NE2 . GLN A  82  ? 0.4810 0.4547 0.2014 0.0223  0.0071  -0.0439 82  GLN A NE2 
678   N  N   . SER A  83  ? 0.2294 0.3589 0.1420 -0.0930 -0.0313 0.0931  83  SER A N   
679   C  CA  . SER A  83  ? 0.1560 0.3492 0.1561 -0.0857 -0.0401 0.0833  83  SER A CA  
680   C  C   . SER A  83  ? 0.1366 0.3125 0.1263 -0.0560 0.0076  0.0632  83  SER A C   
681   O  O   . SER A  83  ? 0.1059 0.3233 0.1483 -0.0265 0.0052  0.0900  83  SER A O   
682   C  CB  . SER A  83  ? 0.1791 0.3932 0.1680 -0.0249 -0.0114 0.1313  83  SER A CB  
683   O  OG  . SER A  83  ? 0.2615 0.3422 0.2154 -0.0668 -0.0515 0.1433  83  SER A OG  
684   N  N   . ARG A  84  ? 0.1080 0.4054 0.1377 -0.0560 -0.0021 0.0942  84  ARG A N   
685   C  CA  . ARG A  84  ? 0.1042 0.3124 0.1348 -0.0059 0.0024  0.0666  84  ARG A CA  
686   C  C   . ARG A  84  ? 0.0921 0.2610 0.1531 -0.0379 -0.0027 0.0737  84  ARG A C   
687   O  O   . ARG A  84  ? 0.0924 0.2811 0.1841 -0.0229 0.0088  0.1103  84  ARG A O   
688   C  CB  . ARG A  84  ? 0.0908 0.3609 0.1400 -0.0218 0.0081  0.0891  84  ARG A CB  
689   C  CG  . ARG A  84  ? 0.0838 0.2921 0.1206 -0.0098 0.0199  0.0577  84  ARG A CG  
690   C  CD  . ARG A  84  ? 0.0804 0.3021 0.1676 0.0115  0.0087  0.0747  84  ARG A CD  
691   N  NE  . ARG A  84  ? 0.0996 0.3269 0.1474 0.0020  0.0179  0.0802  84  ARG A NE  
692   C  CZ  . ARG A  84  ? 0.0998 0.2800 0.1414 0.0032  0.0140  0.0727  84  ARG A CZ  
693   N  NH1 . ARG A  84  ? 0.1330 0.3242 0.1881 0.0289  0.0153  0.0182  84  ARG A NH1 
694   N  NH2 . ARG A  84  ? 0.1176 0.2748 0.2226 0.0092  0.0289  0.0694  84  ARG A NH2 
695   N  N   . TYR A  85  ? 0.0775 0.2687 0.1254 -0.0308 0.0178  0.0494  85  TYR A N   
696   C  CA  . TYR A  85  ? 0.0829 0.2075 0.1441 -0.0259 0.0111  0.0317  85  TYR A CA  
697   C  C   . TYR A  85  ? 0.0712 0.1831 0.1535 -0.0066 0.0108  0.0520  85  TYR A C   
698   O  O   . TYR A  85  ? 0.1243 0.1720 0.1427 -0.0082 0.0024  0.0427  85  TYR A O   
699   C  CB  . TYR A  85  ? 0.0746 0.2105 0.1732 -0.0210 -0.0046 0.0467  85  TYR A CB  
700   C  CG  . TYR A  85  ? 0.0730 0.2372 0.1601 -0.0496 0.0038  0.0478  85  TYR A CG  
701   C  CD1 . TYR A  85  ? 0.1116 0.2883 0.1691 -0.0326 -0.0008 0.0588  85  TYR A CD1 
702   C  CD2 . TYR A  85  ? 0.0856 0.2421 0.1691 -0.0320 0.0007  0.0873  85  TYR A CD2 
703   C  CE1 . TYR A  85  ? 0.1213 0.2529 0.1990 0.0005  -0.0107 0.0564  85  TYR A CE1 
704   C  CE2 . TYR A  85  ? 0.1023 0.2581 0.1639 -0.0449 0.0003  0.0945  85  TYR A CE2 
705   C  CZ  . TYR A  85  ? 0.1077 0.2761 0.1567 -0.0340 -0.0098 0.0935  85  TYR A CZ  
706   O  OH  . TYR A  85  ? 0.1912 0.3546 0.1876 0.0157  -0.0436 0.0957  85  TYR A OH  
707   N  N   . SER A  86  ? 0.0920 0.1962 0.1382 -0.0285 0.0135  0.0373  86  SER A N   
708   C  CA  . SER A  86  ? 0.0757 0.2257 0.1430 -0.0052 0.0108  0.0507  86  SER A CA  
709   C  C   . SER A  86  ? 0.0912 0.1933 0.1409 -0.0071 0.0089  0.0441  86  SER A C   
710   O  O   . SER A  86  ? 0.0913 0.1703 0.1676 -0.0108 0.0225  0.0509  86  SER A O   
711   C  CB  . SER A  86  ? 0.0974 0.2492 0.1453 -0.0509 0.0242  0.0438  86  SER A CB  
712   O  OG  . SER A  86  ? 0.0935 0.2811 0.1532 -0.0181 0.0200  0.0715  86  SER A OG  
713   N  N   . ALA A  87  ? 0.1075 0.1860 0.1313 -0.0046 0.0252  0.0346  87  ALA A N   
714   C  CA  . ALA A  87  ? 0.1118 0.1705 0.1134 0.0012  0.0178  0.0226  87  ALA A CA  
715   C  C   . ALA A  87  ? 0.0979 0.1479 0.1378 -0.0108 0.0170  0.0379  87  ALA A C   
716   O  O   . ALA A  87  ? 0.0899 0.2106 0.1809 -0.0233 0.0135  0.0190  87  ALA A O   
717   C  CB  . ALA A  87  ? 0.1592 0.1631 0.1517 0.0068  0.0266  0.0381  87  ALA A CB  
718   N  N   . THR A  88  ? 0.1137 0.1669 0.1486 -0.0077 0.0310  0.0243  88  THR A N   
719   C  CA  . THR A  88  ? 0.1059 0.1827 0.1477 -0.0303 0.0164  0.0230  88  THR A CA  
720   C  C   . THR A  88  ? 0.0821 0.1259 0.1500 -0.0111 0.0076  0.0140  88  THR A C   
721   O  O   . THR A  88  ? 0.1138 0.1737 0.1642 -0.0494 -0.0054 0.0037  88  THR A O   
722   C  CB  . THR A  88  ? 0.1346 0.1689 0.1392 -0.0229 0.0144  0.0209  88  THR A CB  
723   O  OG1 . THR A  88  ? 0.2035 0.1885 0.1868 -0.0188 -0.0093 0.0200  88  THR A OG1 
724   C  CG2 . THR A  88  ? 0.1244 0.1809 0.1990 -0.0200 0.0010  0.0526  88  THR A CG2 
725   N  N   . GLN A  89  ? 0.0883 0.1689 0.1332 -0.0254 0.0188  0.0114  89  GLN A N   
726   C  CA  . GLN A  89  ? 0.1021 0.1621 0.1490 -0.0324 0.0153  0.0114  89  GLN A CA  
727   C  C   . GLN A  89  ? 0.0802 0.1703 0.1158 0.0013  0.0068  0.0215  89  GLN A C   
728   O  O   . GLN A  89  ? 0.1030 0.1568 0.1199 -0.0124 0.0005  0.0068  89  GLN A O   
729   C  CB  . GLN A  89  ? 0.1280 0.1619 0.1421 -0.0200 0.0126  0.0222  89  GLN A CB  
730   C  CG  . GLN A  89  ? 0.1288 0.2009 0.1902 0.0023  0.0239  0.0524  89  GLN A CG  
731   C  CD  . GLN A  89  ? 0.1366 0.1902 0.1861 -0.0238 -0.0201 0.0318  89  GLN A CD  
732   O  OE1 . GLN A  89  ? 0.1170 0.1835 0.1784 -0.0245 0.0098  0.0273  89  GLN A OE1 
733   N  NE2 . GLN A  89  ? 0.1730 0.2364 0.3792 0.0068  -0.0288 -0.0344 89  GLN A NE2 
734   N  N   . LEU A  90  ? 0.0877 0.1583 0.1326 -0.0092 0.0141  0.0305  90  LEU A N   
735   C  CA  . LEU A  90  ? 0.0782 0.1231 0.1392 -0.0089 0.0250  0.0179  90  LEU A CA  
736   C  C   . LEU A  90  ? 0.0852 0.1562 0.1003 -0.0032 -0.0028 0.0156  90  LEU A C   
737   O  O   . LEU A  90  ? 0.0996 0.1580 0.1150 -0.0032 0.0030  0.0059  90  LEU A O   
738   C  CB  . LEU A  90  ? 0.1064 0.1450 0.1185 0.0013  -0.0019 0.0119  90  LEU A CB  
739   C  CG  . LEU A  90  ? 0.1118 0.1702 0.1242 0.0003  -0.0008 0.0297  90  LEU A CG  
740   C  CD1 . LEU A  90  ? 0.1190 0.1922 0.1331 -0.0038 0.0137  0.0353  90  LEU A CD1 
741   C  CD2 . LEU A  90  ? 0.1274 0.1843 0.2011 0.0571  -0.0006 0.0469  90  LEU A CD2 
742   N  N   . HIS A  91  ? 0.0856 0.1337 0.1050 0.0008  0.0065  0.0188  91  HIS A N   
743   C  CA  . HIS A  91  ? 0.0784 0.1262 0.1075 -0.0038 0.0052  0.0174  91  HIS A CA  
744   C  C   . HIS A  91  ? 0.0751 0.1286 0.0927 0.0111  0.0049  0.0133  91  HIS A C   
745   O  O   . HIS A  91  ? 0.0951 0.1177 0.1010 -0.0034 0.0035  -0.0003 91  HIS A O   
746   C  CB  . HIS A  91  ? 0.1094 0.1382 0.1019 -0.0040 -0.0020 0.0041  91  HIS A CB  
747   C  CG  . HIS A  91  ? 0.0988 0.1238 0.1086 0.0171  -0.0003 0.0091  91  HIS A CG  
748   N  ND1 . HIS A  91  ? 0.0978 0.1246 0.1073 -0.0077 0.0068  0.0313  91  HIS A ND1 
749   C  CD2 . HIS A  91  ? 0.1085 0.1297 0.1005 0.0078  -0.0027 0.0300  91  HIS A CD2 
750   C  CE1 . HIS A  91  ? 0.0806 0.1231 0.1333 -0.0098 0.0065  0.0166  91  HIS A CE1 
751   N  NE2 . HIS A  91  ? 0.0696 0.1170 0.1082 0.0013  -0.0155 0.0162  91  HIS A NE2 
752   N  N   . LEU A  92  ? 0.0759 0.1307 0.1032 0.0000  0.0166  0.0170  92  LEU A N   
753   C  CA  . LEU A  92  ? 0.0797 0.1176 0.1057 -0.0003 0.0230  0.0211  92  LEU A CA  
754   C  C   . LEU A  92  ? 0.0971 0.0992 0.0885 0.0008  0.0275  0.0076  92  LEU A C   
755   O  O   . LEU A  92  ? 0.0997 0.1121 0.1118 -0.0005 0.0164  0.0019  92  LEU A O   
756   C  CB  . LEU A  92  ? 0.1137 0.1181 0.1474 0.0144  0.0326  0.0423  92  LEU A CB  
757   C  CG  . LEU A  92  ? 0.1190 0.1231 0.1213 0.0397  0.0068  0.0041  92  LEU A CG  
758   C  CD1 . LEU A  92  ? 0.1535 0.1985 0.2230 0.0132  -0.0487 0.0012  92  LEU A CD1 
759   C  CD2 . LEU A  92  ? 0.1526 0.1389 0.2156 0.0203  0.0417  -0.0057 92  LEU A CD2 
760   N  N   . HIS A  93  ? 0.0807 0.1172 0.0967 -0.0063 0.0238  0.0094  93  HIS A N   
761   C  CA  . HIS A  93  ? 0.0639 0.1290 0.1115 -0.0059 0.0109  0.0247  93  HIS A CA  
762   C  C   . HIS A  93  ? 0.0714 0.1173 0.0994 0.0055  0.0206  0.0087  93  HIS A C   
763   O  O   . HIS A  93  ? 0.0978 0.1058 0.1068 0.0087  0.0274  0.0171  93  HIS A O   
764   C  CB  . HIS A  93  ? 0.0973 0.1228 0.1112 -0.0038 0.0071  0.0237  93  HIS A CB  
765   C  CG  . HIS A  93  ? 0.0936 0.1018 0.0969 0.0013  0.0087  0.0322  93  HIS A CG  
766   N  ND1 . HIS A  93  ? 0.0879 0.1073 0.1324 0.0140  0.0214  0.0266  93  HIS A ND1 
767   C  CD2 . HIS A  93  ? 0.0816 0.1163 0.1027 -0.0120 0.0161  0.0252  93  HIS A CD2 
768   C  CE1 . HIS A  93  ? 0.0793 0.1240 0.1190 0.0015  0.0331  0.0049  93  HIS A CE1 
769   N  NE2 . HIS A  93  ? 0.0991 0.1012 0.1057 -0.0034 0.0034  0.0211  93  HIS A NE2 
770   N  N   . TRP A  94  ? 0.0830 0.1116 0.0976 -0.0005 0.0249  0.0171  94  TRP A N   
771   C  CA  . TRP A  94  ? 0.0815 0.1109 0.1032 0.0044  0.0307  0.0255  94  TRP A CA  
772   C  C   . TRP A  94  ? 0.1067 0.1143 0.0961 0.0031  0.0265  0.0057  94  TRP A C   
773   O  O   . TRP A  94  ? 0.1098 0.1118 0.1015 0.0024  0.0274  0.0131  94  TRP A O   
774   C  CB  . TRP A  94  ? 0.1341 0.1206 0.0825 0.0030  0.0153  0.0104  94  TRP A CB  
775   C  CG  . TRP A  94  ? 0.1195 0.1105 0.0922 0.0219  0.0227  0.0193  94  TRP A CG  
776   C  CD1 . TRP A  94  ? 0.1161 0.1360 0.1014 0.0092  0.0137  0.0086  94  TRP A CD1 
777   C  CD2 . TRP A  94  ? 0.1156 0.1167 0.1021 0.0003  0.0126  0.0186  94  TRP A CD2 
778   N  NE1 . TRP A  94  ? 0.1097 0.1542 0.1179 -0.0129 0.0197  0.0023  94  TRP A NE1 
779   C  CE2 . TRP A  94  ? 0.1023 0.1583 0.1005 -0.0008 0.0185  0.0131  94  TRP A CE2 
780   C  CE3 . TRP A  94  ? 0.1085 0.1254 0.0965 -0.0013 0.0130  0.0239  94  TRP A CE3 
781   C  CZ2 . TRP A  94  ? 0.1052 0.1703 0.1242 -0.0021 0.0177  0.0241  94  TRP A CZ2 
782   C  CZ3 . TRP A  94  ? 0.1136 0.1211 0.1066 0.0087  0.0107  0.0097  94  TRP A CZ3 
783   C  CH2 . TRP A  94  ? 0.1091 0.1597 0.1042 0.0081  0.0099  0.0049  94  TRP A CH2 
784   N  N   . GLY A  95  ? 0.0803 0.1281 0.1260 -0.0030 0.0344  0.0219  95  GLY A N   
785   C  CA  . GLY A  95  ? 0.0947 0.1543 0.1118 -0.0017 0.0454  0.0116  95  GLY A CA  
786   C  C   . GLY A  95  ? 0.0920 0.1414 0.1159 -0.0043 0.0406  0.0266  95  GLY A C   
787   O  O   . GLY A  95  ? 0.1120 0.1553 0.1188 -0.0041 0.0386  0.0230  95  GLY A O   
788   N  N   . ASN A  96  ? 0.1120 0.1421 0.1179 0.0041  0.0489  0.0232  96  ASN A N   
789   C  CA  . ASN A  96  ? 0.1351 0.1583 0.0989 0.0041  0.0390  0.0233  96  ASN A CA  
790   C  C   . ASN A  96  ? 0.1124 0.1669 0.1172 -0.0131 0.0438  0.0197  96  ASN A C   
791   O  O   . ASN A  96  ? 0.1254 0.1502 0.1206 -0.0068 0.0271  0.0335  96  ASN A O   
792   C  CB  . ASN A  96  ? 0.1405 0.1545 0.1698 0.0054  0.0310  0.0242  96  ASN A CB  
793   C  CG  . ASN A  96  ? 0.1328 0.1295 0.1911 0.0234  0.0697  0.0280  96  ASN A CG  
794   O  OD1 . ASN A  96  ? 0.1662 0.2060 0.2662 0.0259  0.1136  0.0837  96  ASN A OD1 
795   N  ND2 . ASN A  96  ? 0.1421 0.1876 0.2404 0.0138  0.0368  0.0215  96  ASN A ND2 
796   N  N   . PRO A  97  ? 0.1221 0.1714 0.1199 -0.0097 0.0219  0.0417  97  PRO A N   
797   C  CA  . PRO A  97  ? 0.1409 0.1847 0.1272 -0.0085 0.0197  0.0395  97  PRO A CA  
798   C  C   . PRO A  97  ? 0.1429 0.1777 0.1147 0.0005  0.0388  0.0474  97  PRO A C   
799   O  O   . PRO A  97  ? 0.1466 0.1924 0.1834 -0.0126 0.0285  0.0544  97  PRO A O   
800   C  CB  . PRO A  97  ? 0.1608 0.2236 0.1457 -0.0197 0.0423  0.0196  97  PRO A CB  
801   C  CG  . PRO A  97  ? 0.1888 0.1955 0.1294 -0.0130 0.0153  0.0331  97  PRO A CG  
802   C  CD  . PRO A  97  ? 0.1620 0.1893 0.1405 -0.0153 0.0024  0.0259  97  PRO A CD  
803   N  N   A ASN A  98  ? 0.1260 0.1836 0.1073 0.0093  0.0450  0.0216  98  ASN A N   
804   N  N   B ASN A  98  ? 0.1272 0.1829 0.1106 0.0087  0.0432  0.0226  98  ASN A N   
805   C  CA  A ASN A  98  ? 0.1204 0.1836 0.1213 0.0328  0.0447  0.0271  98  ASN A CA  
806   C  CA  B ASN A  98  ? 0.1317 0.2097 0.1369 0.0046  0.0546  0.0100  98  ASN A CA  
807   C  C   A ASN A  98  ? 0.1191 0.1919 0.1346 -0.0013 0.0353  0.0344  98  ASN A C   
808   C  C   B ASN A  98  ? 0.1280 0.1976 0.1404 -0.0013 0.0401  0.0395  98  ASN A C   
809   O  O   A ASN A  98  ? 0.1277 0.2716 0.1554 -0.0439 0.0414  0.0113  98  ASN A O   
810   O  O   B ASN A  98  ? 0.1324 0.2804 0.1389 -0.0445 0.0575  0.0206  98  ASN A O   
811   C  CB  A ASN A  98  ? 0.1190 0.1741 0.1359 0.0186  0.0586  0.0219  98  ASN A CB  
812   C  CB  B ASN A  98  ? 0.2148 0.1879 0.2158 0.0487  0.0167  0.0445  98  ASN A CB  
813   C  CG  A ASN A  98  ? 0.1999 0.2123 0.1289 0.0278  0.0983  -0.0120 98  ASN A CG  
814   C  CG  B ASN A  98  ? 0.2332 0.3231 0.5005 -0.0335 -0.0115 -0.0467 98  ASN A CG  
815   O  OD1 A ASN A  98  ? 0.3231 0.2468 0.1341 -0.0148 0.1367  0.0109  98  ASN A OD1 
816   O  OD1 B ASN A  98  ? 0.3519 0.4352 0.6614 -0.0153 0.2138  0.2213  98  ASN A OD1 
817   N  ND2 A ASN A  98  ? 0.2786 0.2612 0.2937 0.0529  0.0728  -0.0702 98  ASN A ND2 
818   N  ND2 B ASN A  98  ? 0.5503 0.4891 0.4684 0.1660  -0.0480 0.1026  98  ASN A ND2 
819   N  N   . ASP A  99  ? 0.1369 0.1832 0.1156 0.0138  0.0406  0.0281  99  ASP A N   
820   C  CA  . ASP A  99  ? 0.1486 0.1617 0.1231 0.0285  0.0370  0.0118  99  ASP A CA  
821   C  C   . ASP A  99  ? 0.1145 0.1520 0.1215 -0.0048 0.0272  0.0287  99  ASP A C   
822   O  O   . ASP A  99  ? 0.1298 0.1577 0.1272 0.0003  0.0298  0.0197  99  ASP A O   
823   C  CB  . ASP A  99  ? 0.1136 0.1761 0.1631 0.0109  0.0142  0.0148  99  ASP A CB  
824   C  CG  . ASP A  99  ? 0.1466 0.1623 0.1567 -0.0070 0.0148  0.0335  99  ASP A CG  
825   O  OD1 . ASP A  99  ? 0.2592 0.2020 0.1314 -0.0113 0.0208  0.0357  99  ASP A OD1 
826   O  OD2 . ASP A  99  ? 0.1832 0.2522 0.2025 0.0157  -0.0432 0.0342  99  ASP A OD2 
827   N  N   . PRO A  100 ? 0.1238 0.1446 0.1258 -0.0024 0.0443  0.0324  100 PRO A N   
828   C  CA  . PRO A  100 ? 0.1106 0.1639 0.1344 0.0196  0.0331  0.0357  100 PRO A CA  
829   C  C   . PRO A  100 ? 0.1036 0.1057 0.1520 -0.0035 0.0452  0.0285  100 PRO A C   
830   O  O   . PRO A  100 ? 0.1459 0.1375 0.1847 0.0177  0.0696  0.0491  100 PRO A O   
831   C  CB  . PRO A  100 ? 0.1358 0.1435 0.1576 0.0038  0.0421  0.0522  100 PRO A CB  
832   C  CG  . PRO A  100 ? 0.1213 0.1629 0.1662 0.0000  0.0359  0.0370  100 PRO A CG  
833   C  CD  . PRO A  100 ? 0.1398 0.1468 0.1560 0.0074  0.0491  0.0612  100 PRO A CD  
834   N  N   . HIS A  101 ? 0.1185 0.1152 0.1423 0.0000  0.0460  0.0273  101 HIS A N   
835   C  CA  . HIS A  101 ? 0.1353 0.1651 0.1335 -0.0344 0.0465  0.0148  101 HIS A CA  
836   C  C   . HIS A  101 ? 0.1218 0.1308 0.1310 0.0059  0.0318  0.0247  101 HIS A C   
837   O  O   . HIS A  101 ? 0.1429 0.1759 0.2172 -0.0076 -0.0087 0.0549  101 HIS A O   
838   C  CB  . HIS A  101 ? 0.1551 0.2124 0.1341 -0.0555 0.0326  0.0197  101 HIS A CB  
839   C  CG  . HIS A  101 ? 0.1644 0.1865 0.1623 -0.0194 0.0544  0.0043  101 HIS A CG  
840   N  ND1 . HIS A  101 ? 0.1702 0.2075 0.2418 -0.0427 0.0540  0.0038  101 HIS A ND1 
841   C  CD2 . HIS A  101 ? 0.1596 0.1914 0.1332 -0.0403 0.0465  -0.0027 101 HIS A CD2 
842   C  CE1 . HIS A  101 ? 0.1529 0.1818 0.2843 -0.0181 0.0465  0.0174  101 HIS A CE1 
843   N  NE2 . HIS A  101 ? 0.1696 0.1887 0.2500 -0.0392 0.0571  0.0168  101 HIS A NE2 
844   N  N   . GLY A  102 ? 0.0994 0.1215 0.1263 -0.0088 0.0297  0.0071  102 GLY A N   
845   C  CA  . GLY A  102 ? 0.1244 0.1240 0.1229 0.0173  0.0412  0.0373  102 GLY A CA  
846   C  C   . GLY A  102 ? 0.1005 0.0996 0.1100 0.0013  0.0189  0.0135  102 GLY A C   
847   O  O   . GLY A  102 ? 0.1234 0.0985 0.1265 0.0000  0.0322  0.0081  102 GLY A O   
848   N  N   . SER A  103 ? 0.1163 0.1023 0.0904 0.0120  0.0361  0.0214  103 SER A N   
849   C  CA  . SER A  103 ? 0.0901 0.1001 0.1030 0.0154  0.0280  0.0174  103 SER A CA  
850   C  C   . SER A  103 ? 0.0856 0.1182 0.1019 0.0091  0.0259  0.0292  103 SER A C   
851   O  O   . SER A  103 ? 0.0978 0.1590 0.1261 0.0198  0.0299  0.0625  103 SER A O   
852   C  CB  . SER A  103 ? 0.0988 0.1028 0.1027 0.0094  0.0260  0.0230  103 SER A CB  
853   O  OG  . SER A  103 ? 0.1048 0.1009 0.1143 0.0013  0.0229  0.0263  103 SER A OG  
854   N  N   . GLU A  104 ? 0.0861 0.0958 0.0929 0.0010  0.0189  0.0188  104 GLU A N   
855   C  CA  . GLU A  104 ? 0.0901 0.1015 0.1006 0.0010  0.0024  0.0315  104 GLU A CA  
856   C  C   . GLU A  104 ? 0.0854 0.0978 0.1061 -0.0017 0.0120  0.0258  104 GLU A C   
857   O  O   . GLU A  104 ? 0.0818 0.0996 0.1142 0.0032  0.0081  0.0270  104 GLU A O   
858   C  CB  . GLU A  104 ? 0.1064 0.0992 0.1045 -0.0062 -0.0027 0.0281  104 GLU A CB  
859   C  CG  . GLU A  104 ? 0.1238 0.1100 0.1124 -0.0252 0.0119  0.0186  104 GLU A CG  
860   C  CD  . GLU A  104 ? 0.0741 0.1156 0.1105 -0.0013 0.0040  0.0144  104 GLU A CD  
861   O  OE1 . GLU A  104 ? 0.0960 0.1084 0.1371 -0.0017 0.0245  0.0395  104 GLU A OE1 
862   O  OE2 . GLU A  104 ? 0.0973 0.1246 0.1385 0.0044  0.0131  0.0238  104 GLU A OE2 
863   N  N   . HIS A  105 ? 0.0866 0.0913 0.1085 -0.0059 0.0154  0.0170  105 HIS A N   
864   C  CA  . HIS A  105 ? 0.0820 0.0866 0.1202 -0.0046 0.0171  0.0276  105 HIS A CA  
865   C  C   . HIS A  105 ? 0.0924 0.0962 0.1055 0.0010  0.0162  0.0307  105 HIS A C   
866   O  O   . HIS A  105 ? 0.1088 0.1118 0.1057 -0.0063 0.0077  0.0218  105 HIS A O   
867   C  CB  . HIS A  105 ? 0.0816 0.1120 0.1283 -0.0032 0.0307  0.0346  105 HIS A CB  
868   C  CG  . HIS A  105 ? 0.0795 0.1049 0.0957 0.0161  0.0255  0.0219  105 HIS A CG  
869   N  ND1 . HIS A  105 ? 0.0712 0.1339 0.1224 -0.0082 0.0324  0.0296  105 HIS A ND1 
870   C  CD2 . HIS A  105 ? 0.0791 0.1077 0.1082 0.0024  0.0229  0.0286  105 HIS A CD2 
871   C  CE1 . HIS A  105 ? 0.0906 0.1324 0.1005 0.0068  0.0109  0.0263  105 HIS A CE1 
872   N  NE2 . HIS A  105 ? 0.0882 0.1208 0.1185 0.0003  0.0172  0.0421  105 HIS A NE2 
873   N  N   . THR A  106 ? 0.0890 0.0909 0.1134 -0.0082 0.0054  0.0207  106 THR A N   
874   C  CA  . THR A  106 ? 0.0885 0.0899 0.1350 -0.0054 0.0236  0.0197  106 THR A CA  
875   C  C   . THR A  106 ? 0.1098 0.0942 0.1118 -0.0027 0.0024  0.0259  106 THR A C   
876   O  O   . THR A  106 ? 0.1088 0.1012 0.1190 0.0023  0.0140  0.0241  106 THR A O   
877   C  CB  . THR A  106 ? 0.1018 0.1193 0.1125 0.0089  0.0285  0.0264  106 THR A CB  
878   O  OG1 . THR A  106 ? 0.1042 0.1159 0.1405 -0.0028 0.0138  0.0344  106 THR A OG1 
879   C  CG2 . THR A  106 ? 0.0967 0.1272 0.1378 0.0043  0.0375  0.0206  106 THR A CG2 
880   N  N   . VAL A  107 ? 0.1064 0.0906 0.1299 -0.0013 0.0178  0.0091  107 VAL A N   
881   C  CA  . VAL A  107 ? 0.1039 0.1026 0.1508 0.0010  0.0153  0.0189  107 VAL A CA  
882   C  C   . VAL A  107 ? 0.1215 0.0832 0.1614 -0.0118 0.0037  0.0310  107 VAL A C   
883   O  O   . VAL A  107 ? 0.1340 0.1057 0.1665 -0.0076 0.0115  0.0331  107 VAL A O   
884   C  CB  . VAL A  107 ? 0.1134 0.0992 0.1829 0.0060  0.0143  0.0200  107 VAL A CB  
885   C  CG1 . VAL A  107 ? 0.1500 0.1317 0.2014 0.0006  0.0231  -0.0315 107 VAL A CG1 
886   C  CG2 . VAL A  107 ? 0.1174 0.1527 0.2143 0.0102  0.0172  0.0370  107 VAL A CG2 
887   N  N   . SER A  108 ? 0.1030 0.1347 0.1628 0.0048  0.0089  0.0107  108 SER A N   
888   C  CA  . SER A  108 ? 0.1202 0.1437 0.1611 -0.0264 0.0065  -0.0074 108 SER A CA  
889   C  C   . SER A  108 ? 0.1088 0.1170 0.1756 -0.0093 0.0063  0.0253  108 SER A C   
890   O  O   . SER A  108 ? 0.1231 0.1502 0.1896 -0.0283 0.0104  0.0197  108 SER A O   
891   C  CB  . SER A  108 ? 0.1849 0.1389 0.2443 -0.0353 0.0226  -0.0454 108 SER A CB  
892   O  OG  . SER A  108 ? 0.2053 0.2382 0.2867 -0.0684 0.0364  -0.0689 108 SER A OG  
893   N  N   . GLY A  109 ? 0.1208 0.1091 0.1574 0.0120  0.0086  0.0216  109 GLY A N   
894   C  CA  . GLY A  109 ? 0.1136 0.1163 0.1703 -0.0051 -0.0195 0.0195  109 GLY A CA  
895   C  C   . GLY A  109 ? 0.1058 0.1527 0.1926 -0.0092 0.0218  0.0172  109 GLY A C   
896   O  O   . GLY A  109 ? 0.1382 0.1951 0.1949 0.0133  0.0259  0.0035  109 GLY A O   
897   N  N   . GLN A  110 ? 0.1145 0.1337 0.1477 -0.0179 -0.0020 0.0430  110 GLN A N   
898   C  CA  . GLN A  110 ? 0.1321 0.1252 0.1428 -0.0357 0.0021  0.0384  110 GLN A CA  
899   C  C   . GLN A  110 ? 0.1111 0.1073 0.1168 -0.0080 0.0302  0.0207  110 GLN A C   
900   O  O   . GLN A  110 ? 0.1107 0.1112 0.1351 -0.0035 0.0300  0.0190  110 GLN A O   
901   C  CB  . GLN A  110 ? 0.1360 0.1191 0.1757 -0.0040 0.0000  0.0419  110 GLN A CB  
902   C  CG  . GLN A  110 ? 0.1386 0.1277 0.2327 0.0077  0.0111  -0.0043 110 GLN A CG  
903   C  CD  . GLN A  110 ? 0.1554 0.1527 0.2465 -0.0188 0.0266  0.0216  110 GLN A CD  
904   O  OE1 . GLN A  110 ? 0.1696 0.1860 0.2301 -0.0151 0.0353  0.0527  110 GLN A OE1 
905   N  NE2 . GLN A  110 ? 0.1768 0.1823 0.2518 -0.0059 0.0152  0.0228  110 GLN A NE2 
906   N  N   . HIS A  111 ? 0.0989 0.1523 0.1263 0.0151  0.0207  0.0242  111 HIS A N   
907   C  CA  . HIS A  111 ? 0.1082 0.1155 0.1509 0.0065  0.0020  0.0057  111 HIS A CA  
908   C  C   . HIS A  111 ? 0.1402 0.1459 0.1254 -0.0355 -0.0115 0.0637  111 HIS A C   
909   O  O   . HIS A  111 ? 0.1527 0.1738 0.2933 -0.0564 -0.0340 0.1177  111 HIS A O   
910   C  CB  . HIS A  111 ? 0.1628 0.1493 0.1412 -0.0054 0.0291  0.0100  111 HIS A CB  
911   C  CG  . HIS A  111 ? 0.1030 0.1298 0.1711 0.0024  0.0285  -0.0015 111 HIS A CG  
912   N  ND1 . HIS A  111 ? 0.1369 0.1438 0.3289 0.0183  0.0252  0.0346  111 HIS A ND1 
913   C  CD2 . HIS A  111 ? 0.1061 0.1267 0.1438 -0.0174 0.0322  0.0160  111 HIS A CD2 
914   C  CE1 . HIS A  111 ? 0.1107 0.1317 0.3066 0.0141  0.0568  0.0478  111 HIS A CE1 
915   N  NE2 . HIS A  111 ? 0.1454 0.1712 0.2831 0.0170  0.0737  0.0208  111 HIS A NE2 
916   N  N   . PHE A  112 ? 0.1154 0.1086 0.1386 -0.0097 0.0032  0.0292  112 PHE A N   
917   C  CA  . PHE A  112 ? 0.1075 0.1168 0.1341 0.0003  0.0113  0.0252  112 PHE A CA  
918   C  C   . PHE A  112 ? 0.1150 0.0945 0.1152 -0.0017 0.0275  0.0294  112 PHE A C   
919   O  O   . PHE A  112 ? 0.1158 0.1073 0.1277 0.0005  0.0189  0.0189  112 PHE A O   
920   C  CB  . PHE A  112 ? 0.1249 0.1019 0.1375 0.0087  0.0206  0.0185  112 PHE A CB  
921   C  CG  . PHE A  112 ? 0.1362 0.1346 0.1419 -0.0063 0.0423  0.0115  112 PHE A CG  
922   C  CD1 . PHE A  112 ? 0.2143 0.2091 0.1170 -0.0417 0.0342  -0.0054 112 PHE A CD1 
923   C  CD2 . PHE A  112 ? 0.1897 0.1195 0.2208 0.0142  0.0804  0.0167  112 PHE A CD2 
924   C  CE1 . PHE A  112 ? 0.2257 0.2820 0.1263 -0.0498 0.0487  -0.0306 112 PHE A CE1 
925   C  CE2 . PHE A  112 ? 0.2073 0.1522 0.3222 -0.0119 0.1023  -0.0322 112 PHE A CE2 
926   C  CZ  . PHE A  112 ? 0.2648 0.2545 0.3073 -0.0948 0.0771  -0.0716 112 PHE A CZ  
927   N  N   . ALA A  113 ? 0.1152 0.1085 0.1071 0.0019  0.0318  0.0362  113 ALA A N   
928   C  CA  . ALA A  113 ? 0.1028 0.1274 0.1116 0.0000  0.0329  0.0326  113 ALA A CA  
929   C  C   . ALA A  113 ? 0.1193 0.1225 0.0908 0.0020  0.0277  0.0239  113 ALA A C   
930   O  O   . ALA A  113 ? 0.1062 0.1204 0.0989 0.0057  0.0333  0.0253  113 ALA A O   
931   C  CB  . ALA A  113 ? 0.1491 0.1387 0.1292 0.0076  0.0241  0.0654  113 ALA A CB  
932   N  N   . ALA A  114 ? 0.0935 0.1145 0.1176 0.0003  0.0331  0.0295  114 ALA A N   
933   C  CA  . ALA A  114 ? 0.1061 0.1091 0.0958 -0.0166 0.0395  0.0140  114 ALA A CA  
934   C  C   . ALA A  114 ? 0.0759 0.0983 0.1040 0.0199  0.0196  0.0186  114 ALA A C   
935   O  O   . ALA A  114 ? 0.1048 0.0931 0.1019 0.0024  0.0320  0.0315  114 ALA A O   
936   C  CB  . ALA A  114 ? 0.1387 0.1224 0.0881 0.0208  0.0203  0.0167  114 ALA A CB  
937   N  N   . GLU A  115 ? 0.1001 0.0996 0.0897 0.0051  0.0271  0.0296  115 GLU A N   
938   C  CA  . GLU A  115 ? 0.0920 0.1127 0.0829 0.0074  0.0252  0.0172  115 GLU A CA  
939   C  C   . GLU A  115 ? 0.0983 0.1057 0.0957 0.0026  0.0164  0.0273  115 GLU A C   
940   O  O   . GLU A  115 ? 0.1035 0.1206 0.1179 -0.0019 0.0370  0.0017  115 GLU A O   
941   C  CB  . GLU A  115 ? 0.1012 0.1044 0.0886 0.0159  0.0296  0.0220  115 GLU A CB  
942   C  CG  . GLU A  115 ? 0.0966 0.1301 0.1001 0.0063  0.0199  0.0324  115 GLU A CG  
943   C  CD  . GLU A  115 ? 0.0929 0.1102 0.1003 0.0083  0.0280  0.0170  115 GLU A CD  
944   O  OE1 . GLU A  115 ? 0.0915 0.1260 0.1075 0.0008  0.0130  0.0390  115 GLU A OE1 
945   O  OE2 . GLU A  115 ? 0.0886 0.1378 0.0935 -0.0046 0.0135  0.0283  115 GLU A OE2 
946   N  N   . LEU A  116 ? 0.0793 0.1137 0.1019 0.0020  0.0174  0.0353  116 LEU A N   
947   C  CA  . LEU A  116 ? 0.0742 0.1154 0.1100 -0.0115 0.0007  0.0397  116 LEU A CA  
948   C  C   . LEU A  116 ? 0.0757 0.1228 0.0757 0.0035  0.0074  0.0091  116 LEU A C   
949   O  O   . LEU A  116 ? 0.0961 0.0987 0.0926 0.0003  0.0126  0.0116  116 LEU A O   
950   C  CB  . LEU A  116 ? 0.0996 0.1182 0.1195 0.0052  -0.0027 0.0266  116 LEU A CB  
951   C  CG  . LEU A  116 ? 0.1118 0.1098 0.1698 -0.0185 -0.0353 0.0485  116 LEU A CG  
952   C  CD1 . LEU A  116 ? 0.1567 0.1579 0.1874 0.0218  0.0015  0.0054  116 LEU A CD1 
953   C  CD2 . LEU A  116 ? 0.1377 0.1770 0.1905 0.0427  0.0124  0.0244  116 LEU A CD2 
954   N  N   . HIS A  117 ? 0.0806 0.1064 0.0924 0.0054  0.0148  0.0185  117 HIS A N   
955   C  CA  . HIS A  117 ? 0.0820 0.0992 0.0895 0.0062  0.0111  0.0208  117 HIS A CA  
956   C  C   . HIS A  117 ? 0.0869 0.1080 0.0811 0.0008  0.0035  0.0265  117 HIS A C   
957   O  O   . HIS A  117 ? 0.0769 0.1446 0.0949 -0.0081 0.0093  0.0177  117 HIS A O   
958   C  CB  . HIS A  117 ? 0.0881 0.1082 0.1142 -0.0019 0.0135  0.0263  117 HIS A CB  
959   C  CG  . HIS A  117 ? 0.0843 0.0988 0.0980 0.0093  0.0215  0.0203  117 HIS A CG  
960   N  ND1 . HIS A  117 ? 0.0998 0.0906 0.0987 0.0149  0.0157  0.0141  117 HIS A ND1 
961   C  CD2 . HIS A  117 ? 0.0904 0.1143 0.1066 -0.0006 0.0093  0.0432  117 HIS A CD2 
962   C  CE1 . HIS A  117 ? 0.0989 0.1008 0.0917 -0.0104 0.0171  0.0344  117 HIS A CE1 
963   N  NE2 . HIS A  117 ? 0.0841 0.1114 0.1118 0.0097  0.0091  0.0311  117 HIS A NE2 
964   N  N   . ILE A  118 ? 0.0710 0.1378 0.1100 0.0017  0.0230  0.0241  118 ILE A N   
965   C  CA  . ILE A  118 ? 0.0723 0.1270 0.1269 0.0000  0.0148  0.0272  118 ILE A CA  
966   C  C   . ILE A  118 ? 0.0702 0.1554 0.1150 -0.0210 0.0181  0.0189  118 ILE A C   
967   O  O   . ILE A  118 ? 0.0892 0.1366 0.1030 -0.0068 0.0177  0.0227  118 ILE A O   
968   C  CB  . ILE A  118 ? 0.0930 0.1373 0.1127 0.0146  0.0148  0.0207  118 ILE A CB  
969   C  CG1 . ILE A  118 ? 0.1100 0.1423 0.1278 0.0130  0.0137  0.0218  118 ILE A CG1 
970   C  CG2 . ILE A  118 ? 0.0906 0.1734 0.1466 0.0142  0.0093  0.0241  118 ILE A CG2 
971   C  CD1 . ILE A  118 ? 0.1430 0.1736 0.1576 0.0500  0.0013  0.0206  118 ILE A CD1 
972   N  N   . VAL A  119 ? 0.0838 0.1414 0.1208 -0.0231 0.0221  0.0209  119 VAL A N   
973   C  CA  . VAL A  119 ? 0.0864 0.1233 0.1497 -0.0076 0.0187  0.0329  119 VAL A CA  
974   C  C   . VAL A  119 ? 0.0784 0.1298 0.1206 0.0031  0.0227  0.0199  119 VAL A C   
975   O  O   . VAL A  119 ? 0.0730 0.1712 0.1596 -0.0054 0.0020  0.0149  119 VAL A O   
976   C  CB  . VAL A  119 ? 0.0951 0.1360 0.1606 -0.0059 0.0287  0.0254  119 VAL A CB  
977   C  CG1 . VAL A  119 ? 0.1055 0.1623 0.1879 -0.0096 0.0309  0.0480  119 VAL A CG1 
978   C  CG2 . VAL A  119 ? 0.1058 0.1595 0.1490 -0.0183 0.0377  0.0176  119 VAL A CG2 
979   N  N   . HIS A  120 ? 0.0994 0.1392 0.1398 -0.0255 0.0119  0.0294  120 HIS A N   
980   C  CA  . HIS A  120 ? 0.0852 0.1709 0.1441 -0.0210 0.0162  0.0513  120 HIS A CA  
981   C  C   . HIS A  120 ? 0.0781 0.1434 0.1571 -0.0111 0.0227  0.0472  120 HIS A C   
982   O  O   . HIS A  120 ? 0.0906 0.1515 0.1642 -0.0207 0.0114  0.0502  120 HIS A O   
983   C  CB  . HIS A  120 ? 0.1089 0.1745 0.1436 -0.0168 0.0305  0.0494  120 HIS A CB  
984   C  CG  . HIS A  120 ? 0.0924 0.1559 0.1387 -0.0114 0.0216  0.0348  120 HIS A CG  
985   N  ND1 . HIS A  120 ? 0.0942 0.1624 0.1362 -0.0006 0.0265  0.0339  120 HIS A ND1 
986   C  CD2 . HIS A  120 ? 0.0953 0.1552 0.1696 0.0010  0.0285  0.0482  120 HIS A CD2 
987   C  CE1 . HIS A  120 ? 0.0949 0.1529 0.1438 -0.0005 0.0161  0.0390  120 HIS A CE1 
988   N  NE2 . HIS A  120 ? 0.1062 0.1425 0.1479 0.0116  0.0125  0.0467  120 HIS A NE2 
989   N  N   . TYR A  121 ? 0.0965 0.1779 0.1829 -0.0269 0.0216  0.0701  121 TYR A N   
990   C  CA  . TYR A  121 ? 0.1021 0.1796 0.1826 -0.0204 0.0280  0.0841  121 TYR A CA  
991   C  C   . TYR A  121 ? 0.0881 0.1972 0.1929 -0.0230 0.0091  0.0991  121 TYR A C   
992   O  O   . TYR A  121 ? 0.0965 0.1969 0.1804 -0.0178 0.0085  0.0780  121 TYR A O   
993   C  CB  . TYR A  121 ? 0.1195 0.1535 0.2549 -0.0159 0.0230  0.0644  121 TYR A CB  
994   C  CG  . TYR A  121 ? 0.1292 0.1441 0.2423 -0.0024 0.0507  0.0516  121 TYR A CG  
995   C  CD1 . TYR A  121 ? 0.1531 0.1723 0.2026 -0.0292 0.0255  0.0357  121 TYR A CD1 
996   C  CD2 . TYR A  121 ? 0.1249 0.2384 0.2685 -0.0614 0.0181  0.0859  121 TYR A CD2 
997   C  CE1 . TYR A  121 ? 0.1626 0.2032 0.2782 -0.0315 0.0227  0.0265  121 TYR A CE1 
998   C  CE2 . TYR A  121 ? 0.1387 0.2084 0.3143 -0.0533 0.0076  0.0687  121 TYR A CE2 
999   C  CZ  . TYR A  121 ? 0.1483 0.2675 0.3030 -0.0461 -0.0031 0.0450  121 TYR A CZ  
1000  O  OH  . TYR A  121 ? 0.1518 0.3659 0.3043 -0.0406 -0.0176 -0.0194 121 TYR A OH  
1001  N  N   . ASN A  122 ? 0.1102 0.2157 0.1908 -0.0153 0.0147  0.1140  122 ASN A N   
1002  C  CA  . ASN A  122 ? 0.0818 0.3386 0.1730 -0.0456 0.0175  0.1325  122 ASN A CA  
1003  C  C   . ASN A  122 ? 0.0992 0.3127 0.2154 -0.0309 0.0318  0.1539  122 ASN A C   
1004  O  O   . ASN A  122 ? 0.1054 0.2878 0.2430 -0.0403 0.0071  0.1430  122 ASN A O   
1005  C  CB  . ASN A  122 ? 0.1149 0.3278 0.1730 -0.0348 -0.0129 0.1127  122 ASN A CB  
1006  C  CG  . ASN A  122 ? 0.1603 0.4348 0.1868 0.0278  -0.0007 0.1763  122 ASN A CG  
1007  O  OD1 . ASN A  122 ? 0.1461 0.4296 0.1969 -0.0273 0.0020  0.1664  122 ASN A OD1 
1008  N  ND2 . ASN A  122 ? 0.1962 0.4964 0.2167 -0.0412 -0.0425 0.1759  122 ASN A ND2 
1009  N  N   . SER A  123 ? 0.0676 0.3075 0.1735 -0.0163 0.0324  0.1077  123 SER A N   
1010  C  CA  . SER A  123 ? 0.1019 0.3204 0.1717 -0.0548 0.0119  0.1172  123 SER A CA  
1011  C  C   . SER A  123 ? 0.0958 0.3397 0.2138 -0.0261 0.0254  0.1409  123 SER A C   
1012  O  O   . SER A  123 ? 0.0987 0.3336 0.2554 -0.0460 0.0329  0.1492  123 SER A O   
1013  C  CB  . SER A  123 ? 0.1249 0.2958 0.1635 -0.0342 0.0020  0.0856  123 SER A CB  
1014  O  OG  . SER A  123 ? 0.1182 0.2931 0.1723 -0.0283 0.0192  0.0930  123 SER A OG  
1015  N  N   . ASP A  124 ? 0.1103 0.3294 0.1770 -0.0147 0.0193  0.1288  124 ASP A N   
1016  C  CA  . ASP A  124 ? 0.1563 0.4156 0.1744 -0.0209 0.0094  0.1634  124 ASP A CA  
1017  C  C   . ASP A  124 ? 0.1511 0.4716 0.2675 -0.0564 0.0163  0.2412  124 ASP A C   
1018  O  O   . ASP A  124 ? 0.2039 0.4896 0.3946 -0.0454 0.0573  0.2888  124 ASP A O   
1019  C  CB  . ASP A  124 ? 0.1400 0.3959 0.1811 -0.0417 0.0211  0.1532  124 ASP A CB  
1020  C  CG  . ASP A  124 ? 0.1387 0.4142 0.1416 -0.0715 0.0208  0.1349  124 ASP A CG  
1021  O  OD1 . ASP A  124 ? 0.1450 0.4129 0.1617 -0.0527 -0.0010 0.1028  124 ASP A OD1 
1022  O  OD2 . ASP A  124 ? 0.1439 0.4803 0.1611 -0.0829 0.0373  0.1058  124 ASP A OD2 
1023  N  N   . LEU A  125 ? 0.1726 0.3808 0.2754 -0.0346 -0.0060 0.2182  125 LEU A N   
1024  C  CA  . LEU A  125 ? 0.1632 0.4050 0.2727 -0.0233 0.0566  0.2145  125 LEU A CA  
1025  C  C   . LEU A  125 ? 0.1976 0.3734 0.4203 0.0105  0.0518  0.2337  125 LEU A C   
1026  O  O   . LEU A  125 ? 0.2561 0.4612 0.5551 -0.0129 0.0449  0.2980  125 LEU A O   
1027  C  CB  . LEU A  125 ? 0.1890 0.5414 0.3341 0.0130  -0.0172 0.2640  125 LEU A CB  
1028  C  CG  . LEU A  125 ? 0.2442 0.6137 0.3600 -0.0057 0.0458  0.2712  125 LEU A CG  
1029  C  CD1 . LEU A  125 ? 0.2994 0.7213 0.5756 0.0595  -0.1457 0.1648  125 LEU A CD1 
1030  C  CD2 . LEU A  125 ? 0.2685 0.7479 0.5439 -0.0575 -0.1120 0.3167  125 LEU A CD2 
1031  N  N   . TYR A  126 ? 0.1450 0.3655 0.3433 -0.0540 0.0281  0.2141  126 TYR A N   
1032  C  CA  . TYR A  126 ? 0.1580 0.3258 0.4228 -0.1244 -0.0068 0.1854  126 TYR A CA  
1033  C  C   . TYR A  126 ? 0.1545 0.2127 0.3486 -0.0410 0.0375  0.0910  126 TYR A C   
1034  O  O   . TYR A  126 ? 0.1502 0.2538 0.4749 -0.0482 -0.0119 0.1750  126 TYR A O   
1035  C  CB  . TYR A  126 ? 0.1520 0.2675 0.3970 -0.0230 0.0362  0.1692  126 TYR A CB  
1036  C  CG  . TYR A  126 ? 0.1826 0.3136 0.3898 -0.0395 0.0189  0.2101  126 TYR A CG  
1037  C  CD1 . TYR A  126 ? 0.2624 0.3129 0.4404 -0.0520 0.0274  0.2213  126 TYR A CD1 
1038  C  CD2 . TYR A  126 ? 0.1298 0.3450 0.4426 -0.0447 -0.0204 0.2284  126 TYR A CD2 
1039  C  CE1 . TYR A  126 ? 0.2084 0.4451 0.4614 -0.0350 -0.0280 0.3084  126 TYR A CE1 
1040  C  CE2 . TYR A  126 ? 0.1448 0.3181 0.4817 -0.0055 -0.0093 0.2046  126 TYR A CE2 
1041  C  CZ  . TYR A  126 ? 0.2418 0.3334 0.6509 -0.0450 0.0631  0.2383  126 TYR A CZ  
1042  O  OH  . TYR A  126 ? 0.1790 0.7692 0.9587 0.0653  -0.2871 0.4107  126 TYR A OH  
1043  N  N   . PRO A  127 ? 0.1608 0.2508 0.4673 -0.0652 0.0666  0.0843  127 PRO A N   
1044  C  CA  . PRO A  127 ? 0.1583 0.3404 0.4754 -0.0914 0.0205  0.0603  127 PRO A CA  
1045  C  C   . PRO A  127 ? 0.1463 0.3025 0.4587 -0.0315 -0.0274 0.0842  127 PRO A C   
1046  O  O   . PRO A  127 ? 0.1750 0.3395 0.5784 -0.0168 -0.0653 0.0776  127 PRO A O   
1047  C  CB  . PRO A  127 ? 0.2172 0.3088 0.6561 -0.1136 0.0020  0.1000  127 PRO A CB  
1048  C  CG  . PRO A  127 ? 0.3418 0.3057 0.5112 -0.0359 -0.0241 0.1316  127 PRO A CG  
1049  C  CD  . PRO A  127 ? 0.2366 0.2339 0.4537 -0.0099 0.0021  0.1028  127 PRO A CD  
1050  N  N   . ASP A  128 ? 0.1579 0.2628 0.3664 -0.0432 0.0320  0.0718  128 ASP A N   
1051  C  CA  . ASP A  128 ? 0.2064 0.2962 0.3630 -0.1062 -0.0491 0.0593  128 ASP A CA  
1052  C  C   . ASP A  128 ? 0.1544 0.2301 0.2671 -0.0164 0.0370  0.0568  128 ASP A C   
1053  O  O   . ASP A  128 ? 0.1780 0.2091 0.3298 -0.0403 -0.0209 0.0807  128 ASP A O   
1054  C  CB  . ASP A  128 ? 0.2698 0.2472 0.4733 -0.0639 -0.0992 0.0641  128 ASP A CB  
1055  C  CG  . ASP A  128 ? 0.3046 0.2572 0.6794 -0.0384 -0.1185 0.0908  128 ASP A CG  
1056  O  OD1 . ASP A  128 ? 0.4666 0.2284 0.9959 -0.0297 -0.2865 0.0111  128 ASP A OD1 
1057  O  OD2 . ASP A  128 ? 0.2939 0.2558 0.5432 -0.0406 -0.0781 0.0974  128 ASP A OD2 
1058  N  N   . ALA A  129 ? 0.1938 0.2346 0.2824 -0.0109 0.0276  0.0762  129 ALA A N   
1059  C  CA  . ALA A  129 ? 0.1923 0.1845 0.2984 0.0057  0.0649  0.0926  129 ALA A CA  
1060  C  C   . ALA A  129 ? 0.2402 0.1953 0.3513 0.0195  0.0350  0.0901  129 ALA A C   
1061  O  O   . ALA A  129 ? 0.1956 0.2003 0.3677 -0.0217 0.0252  0.1225  129 ALA A O   
1062  C  CB  . ALA A  129 ? 0.2919 0.2063 0.3093 0.0278  0.1005  0.1048  129 ALA A CB  
1063  N  N   A SER A  130 ? 0.2962 0.1951 0.2836 0.0099  0.0947  0.0887  130 SER A N   
1064  N  N   B SER A  130 ? 0.2773 0.2226 0.3061 0.0185  0.0156  0.0957  130 SER A N   
1065  C  CA  A SER A  130 ? 0.2707 0.2560 0.4049 0.0362  0.0934  0.0131  130 SER A CA  
1066  C  CA  B SER A  130 ? 0.3758 0.1173 0.3553 0.0217  -0.0155 0.0237  130 SER A CA  
1067  C  C   A SER A  130 ? 0.2175 0.2052 0.4898 0.0362  0.0575  0.0529  130 SER A C   
1068  C  C   B SER A  130 ? 0.2696 0.1863 0.4255 -0.0719 0.0538  0.1010  130 SER A C   
1069  O  O   A SER A  130 ? 0.2705 0.1008 0.4548 0.0784  0.0628  0.0157  130 SER A O   
1070  O  O   B SER A  130 ? 0.2495 0.0996 0.3856 0.0107  0.0857  0.0281  130 SER A O   
1071  C  CB  A SER A  130 ? 0.1897 0.2500 0.5278 0.0675  0.0403  -0.0046 130 SER A CB  
1072  C  CB  B SER A  130 ? 0.3093 0.1628 0.4129 0.0085  -0.0654 0.0028  130 SER A CB  
1073  O  OG  A SER A  130 ? 0.3799 0.2175 0.6100 0.0980  0.1140  0.0006  130 SER A OG  
1074  O  OG  B SER A  130 ? 0.2746 0.3874 0.4201 -0.0003 -0.0028 -0.0351 130 SER A OG  
1075  N  N   . THR A  131 ? 0.2418 0.1502 0.3718 -0.0460 0.0133  0.0548  131 THR A N   
1076  C  CA  . THR A  131 ? 0.2090 0.2129 0.4065 -0.0527 0.0275  0.0971  131 THR A CA  
1077  C  C   . THR A  131 ? 0.1960 0.1757 0.3276 -0.0571 0.0259  0.1081  131 THR A C   
1078  O  O   . THR A  131 ? 0.2105 0.2039 0.4302 -0.0480 -0.0344 0.1676  131 THR A O   
1079  C  CB  . THR A  131 ? 0.1872 0.2921 0.3494 -0.0715 -0.0005 0.1055  131 THR A CB  
1080  O  OG1 . THR A  131 ? 0.2793 0.2073 0.5792 -0.0895 -0.0738 0.0370  131 THR A OG1 
1081  C  CG2 . THR A  131 ? 0.1835 0.3179 0.3982 -0.0237 0.0297  0.1711  131 THR A CG2 
1082  N  N   . ALA A  132 ? 0.1693 0.1847 0.3689 -0.0665 0.0094  0.1286  132 ALA A N   
1083  C  CA  . ALA A  132 ? 0.1267 0.2099 0.3179 -0.0370 0.0030  0.1045  132 ALA A CA  
1084  C  C   . ALA A  132 ? 0.1263 0.2258 0.3458 -0.0531 0.0166  0.1272  132 ALA A C   
1085  O  O   . ALA A  132 ? 0.1290 0.2075 0.3470 -0.0449 -0.0057 0.1203  132 ALA A O   
1086  C  CB  . ALA A  132 ? 0.1374 0.1772 0.3671 0.0043  0.0225  0.1134  132 ALA A CB  
1087  N  N   . SER A  133 ? 0.1579 0.1878 0.3465 -0.0463 0.0141  0.1125  133 SER A N   
1088  C  CA  . SER A  133 ? 0.1265 0.1868 0.4174 -0.0164 0.0403  0.0786  133 SER A CA  
1089  C  C   . SER A  133 ? 0.1498 0.1421 0.3519 -0.0452 0.0277  0.0408  133 SER A C   
1090  O  O   . SER A  133 ? 0.1585 0.1903 0.3450 -0.0741 0.0383  0.0308  133 SER A O   
1091  C  CB  . SER A  133 ? 0.2082 0.2384 0.4108 -0.0071 0.0693  -0.0192 133 SER A CB  
1092  O  OG  . SER A  133 ? 0.2005 0.2556 0.4605 -0.0419 0.0443  -0.0225 133 SER A OG  
1093  N  N   . ASN A  134 ? 0.1064 0.1705 0.5400 -0.0469 -0.0318 0.1212  134 ASN A N   
1094  C  CA  . ASN A  134 ? 0.1346 0.2196 0.4891 -0.0645 -0.0520 0.1438  134 ASN A CA  
1095  C  C   . ASN A  134 ? 0.1432 0.1856 0.4950 -0.0372 -0.0197 0.1727  134 ASN A C   
1096  O  O   . ASN A  134 ? 0.2691 0.3510 0.5741 -0.0320 -0.0944 0.2439  134 ASN A O   
1097  C  CB  . ASN A  134 ? 0.1316 0.1892 0.7351 -0.0456 -0.0243 0.1956  134 ASN A CB  
1098  C  CG  . ASN A  134 ? 0.1523 0.1933 0.8490 -0.0588 -0.0149 0.1895  134 ASN A CG  
1099  O  OD1 . ASN A  134 ? 0.1858 0.2158 0.8389 -0.0151 0.0035  0.1368  134 ASN A OD1 
1100  N  ND2 . ASN A  134 ? 0.2673 0.1981 0.7616 -0.0491 -0.0208 0.1701  134 ASN A ND2 
1101  N  N   . LYS A  135 ? 0.1299 0.2364 0.4325 -0.0483 0.0000  0.1684  135 LYS A N   
1102  C  CA  . LYS A  135 ? 0.1543 0.2976 0.4386 -0.0212 -0.0083 0.1924  135 LYS A CA  
1103  C  C   . LYS A  135 ? 0.1624 0.3465 0.4018 0.0289  -0.0234 0.1917  135 LYS A C   
1104  O  O   . LYS A  135 ? 0.1486 0.3125 0.3181 0.0115  0.0163  0.1607  135 LYS A O   
1105  C  CB  . LYS A  135 ? 0.1893 0.4619 0.4590 -0.0687 0.0333  0.2460  135 LYS A CB  
1106  C  CG  . LYS A  135 ? 0.2757 0.5532 0.5417 -0.2170 -0.0912 0.1650  135 LYS A CG  
1107  C  CD  . LYS A  135 ? 0.3151 0.4799 0.6349 -0.1939 -0.0062 0.3174  135 LYS A CD  
1108  C  CE  . LYS A  135 ? 0.5327 0.4171 0.7293 0.0310  -0.1084 0.3556  135 LYS A CE  
1109  N  NZ  . LYS A  135 ? 0.2576 0.2872 0.7702 -0.0373 -0.1820 0.3037  135 LYS A NZ  
1110  N  N   . SER A  136 ? 0.2594 0.3926 0.3878 0.0133  0.0087  0.1985  136 SER A N   
1111  C  CA  . SER A  136 ? 0.3352 0.4508 0.2642 0.1115  0.0044  0.2013  136 SER A CA  
1112  C  C   . SER A  136 ? 0.2402 0.2673 0.2284 0.0103  -0.0340 0.1453  136 SER A C   
1113  O  O   . SER A  136 ? 0.2407 0.4120 0.3382 -0.0315 0.0048  0.2345  136 SER A O   
1114  C  CB  . SER A  136 ? 0.5397 0.4644 0.2438 0.0375  0.0153  0.1912  136 SER A CB  
1115  O  OG  . SER A  136 ? 0.7315 0.5112 0.3341 0.0962  -0.0384 0.1685  136 SER A OG  
1116  N  N   . GLU A  137 ? 0.2594 0.3316 0.3384 -0.0285 0.0241  0.2257  137 GLU A N   
1117  C  CA  . GLU A  137 ? 0.2533 0.3339 0.2488 -0.0318 -0.0110 0.1861  137 GLU A CA  
1118  C  C   . GLU A  137 ? 0.1563 0.3235 0.2445 -0.0601 0.0111  0.1627  137 GLU A C   
1119  O  O   . GLU A  137 ? 0.1875 0.3109 0.2666 0.0052  0.0318  0.1370  137 GLU A O   
1120  C  CB  . GLU A  137 ? 0.3066 0.3172 0.2802 -0.0171 -0.0535 0.1018  137 GLU A CB  
1121  C  CG  . GLU A  137 ? 0.4839 0.5243 0.2405 0.0670  -0.0586 0.0142  137 GLU A CG  
1122  N  N   . GLY A  138 ? 0.1464 0.2822 0.2581 -0.0350 0.0267  0.1713  138 GLY A N   
1123  C  CA  . GLY A  138 ? 0.1263 0.2161 0.2992 -0.0132 0.0052  0.1499  138 GLY A CA  
1124  C  C   . GLY A  138 ? 0.0989 0.2084 0.2484 -0.0215 0.0160  0.1203  138 GLY A C   
1125  O  O   . GLY A  138 ? 0.0784 0.2003 0.2951 -0.0238 0.0066  0.1238  138 GLY A O   
1126  N  N   . LEU A  139 ? 0.1123 0.1579 0.2098 -0.0311 0.0092  0.0891  139 LEU A N   
1127  C  CA  . LEU A  139 ? 0.1170 0.1771 0.1398 -0.0197 0.0105  0.0560  139 LEU A CA  
1128  C  C   . LEU A  139 ? 0.0912 0.1601 0.1471 0.0000  0.0308  0.0518  139 LEU A C   
1129  O  O   . LEU A  139 ? 0.0994 0.1800 0.1450 -0.0140 0.0210  0.0662  139 LEU A O   
1130  C  CB  . LEU A  139 ? 0.0958 0.1723 0.1896 -0.0244 0.0322  0.0278  139 LEU A CB  
1131  C  CG  . LEU A  139 ? 0.0994 0.1723 0.2398 -0.0159 -0.0024 0.0493  139 LEU A CG  
1132  C  CD1 . LEU A  139 ? 0.0992 0.1845 0.2406 -0.0135 0.0178  0.0074  139 LEU A CD1 
1133  C  CD2 . LEU A  139 ? 0.1224 0.2183 0.2404 -0.0432 -0.0126 0.0131  139 LEU A CD2 
1134  N  N   . ALA A  140 ? 0.0818 0.1729 0.1475 -0.0194 0.0217  0.0746  140 ALA A N   
1135  C  CA  . ALA A  140 ? 0.1041 0.1358 0.1238 -0.0271 0.0131  0.0568  140 ALA A CA  
1136  C  C   . ALA A  140 ? 0.0714 0.1389 0.1281 -0.0115 0.0085  0.0447  140 ALA A C   
1137  O  O   . ALA A  140 ? 0.0915 0.1682 0.1350 -0.0249 0.0065  0.0502  140 ALA A O   
1138  C  CB  . ALA A  140 ? 0.1001 0.1617 0.1434 -0.0020 0.0149  0.0491  140 ALA A CB  
1139  N  N   . VAL A  141 ? 0.0841 0.1475 0.1159 -0.0068 0.0231  0.0480  141 VAL A N   
1140  C  CA  . VAL A  141 ? 0.0918 0.1082 0.1091 -0.0070 0.0222  0.0305  141 VAL A CA  
1141  C  C   . VAL A  141 ? 0.0843 0.1136 0.1073 -0.0049 0.0285  0.0254  141 VAL A C   
1142  O  O   . VAL A  141 ? 0.0935 0.1286 0.1127 -0.0200 0.0115  0.0264  141 VAL A O   
1143  C  CB  . VAL A  141 ? 0.0960 0.1125 0.1102 0.0000  0.0157  0.0311  141 VAL A CB  
1144  C  CG1 . VAL A  141 ? 0.0921 0.1696 0.1216 0.0127  0.0065  0.0320  141 VAL A CG1 
1145  C  CG2 . VAL A  141 ? 0.1075 0.1204 0.1552 0.0071  0.0054  0.0163  141 VAL A CG2 
1146  N  N   . LEU A  142 ? 0.0811 0.1186 0.1005 0.0071  0.0244  0.0346  142 LEU A N   
1147  C  CA  . LEU A  142 ? 0.0969 0.1112 0.1037 0.0051  0.0339  0.0342  142 LEU A CA  
1148  C  C   . LEU A  142 ? 0.1118 0.1128 0.0790 -0.0218 0.0243  0.0253  142 LEU A C   
1149  O  O   . LEU A  142 ? 0.1120 0.1392 0.0958 -0.0171 0.0283  0.0100  142 LEU A O   
1150  C  CB  . LEU A  142 ? 0.1046 0.1238 0.1193 0.0098  0.0174  0.0222  142 LEU A CB  
1151  C  CG  . LEU A  142 ? 0.0834 0.1714 0.1483 -0.0060 0.0164  0.0153  142 LEU A CG  
1152  C  CD1 . LEU A  142 ? 0.1019 0.1586 0.1631 0.0102  0.0118  0.0227  142 LEU A CD1 
1153  C  CD2 . LEU A  142 ? 0.1360 0.1712 0.1306 0.0054  0.0254  -0.0074 142 LEU A CD2 
1154  N  N   . ALA A  143 ? 0.0908 0.1045 0.1028 -0.0024 0.0244  0.0254  143 ALA A N   
1155  C  CA  . ALA A  143 ? 0.0755 0.1028 0.1019 0.0129  0.0306  0.0233  143 ALA A CA  
1156  C  C   . ALA A  143 ? 0.0824 0.1073 0.0854 0.0052  0.0179  0.0088  143 ALA A C   
1157  O  O   . ALA A  143 ? 0.1118 0.1057 0.0891 -0.0020 0.0193  0.0137  143 ALA A O   
1158  C  CB  . ALA A  143 ? 0.0868 0.1279 0.1161 0.0136  0.0076  0.0152  143 ALA A CB  
1159  N  N   . VAL A  144 ? 0.1003 0.1027 0.0836 0.0148  0.0289  0.0174  144 VAL A N   
1160  C  CA  . VAL A  144 ? 0.1003 0.1012 0.0978 0.0052  0.0292  0.0377  144 VAL A CA  
1161  C  C   . VAL A  144 ? 0.0987 0.0935 0.0992 0.0083  0.0255  0.0136  144 VAL A C   
1162  O  O   . VAL A  144 ? 0.1181 0.1028 0.0976 0.0065  0.0274  0.0098  144 VAL A O   
1163  C  CB  . VAL A  144 ? 0.1026 0.1224 0.1125 0.0078  0.0148  0.0416  144 VAL A CB  
1164  C  CG1 . VAL A  144 ? 0.1315 0.1283 0.1348 0.0241  0.0320  0.0390  144 VAL A CG1 
1165  C  CG2 . VAL A  144 ? 0.1073 0.1534 0.1059 0.0232  0.0266  0.0419  144 VAL A CG2 
1166  N  N   . LEU A  145 ? 0.0948 0.1085 0.1012 0.0038  0.0252  0.0318  145 LEU A N   
1167  C  CA  . LEU A  145 ? 0.0998 0.1027 0.1005 0.0121  0.0253  0.0292  145 LEU A CA  
1168  C  C   . LEU A  145 ? 0.0957 0.1046 0.1094 0.0035  0.0263  0.0243  145 LEU A C   
1169  O  O   . LEU A  145 ? 0.1238 0.1167 0.1146 0.0339  0.0298  0.0359  145 LEU A O   
1170  C  CB  . LEU A  145 ? 0.1134 0.1256 0.1036 -0.0099 0.0194  0.0318  145 LEU A CB  
1171  C  CG  . LEU A  145 ? 0.1337 0.1414 0.1296 0.0060  -0.0005 0.0392  145 LEU A CG  
1172  C  CD1 . LEU A  145 ? 0.1647 0.2088 0.1098 -0.0243 -0.0068 0.0129  145 LEU A CD1 
1173  C  CD2 . LEU A  145 ? 0.1763 0.1479 0.1962 -0.0041 -0.0122 0.0749  145 LEU A CD2 
1174  N  N   . ILE A  146 ? 0.1026 0.1064 0.0910 0.0097  0.0335  0.0271  146 ILE A N   
1175  C  CA  . ILE A  146 ? 0.1116 0.1107 0.1021 0.0024  0.0242  0.0370  146 ILE A CA  
1176  C  C   . ILE A  146 ? 0.1039 0.1100 0.1186 0.0120  0.0317  0.0386  146 ILE A C   
1177  O  O   . ILE A  146 ? 0.1224 0.1197 0.1238 0.0240  0.0315  0.0465  146 ILE A O   
1178  C  CB  . ILE A  146 ? 0.1080 0.1194 0.0987 0.0089  0.0182  0.0276  146 ILE A CB  
1179  C  CG1 . ILE A  146 ? 0.1195 0.1234 0.1184 -0.0021 0.0255  0.0187  146 ILE A CG1 
1180  C  CG2 . ILE A  146 ? 0.1712 0.1465 0.0890 0.0305  0.0281  0.0289  146 ILE A CG2 
1181  C  CD1 . ILE A  146 ? 0.1522 0.1159 0.1314 -0.0003 0.0093  0.0151  146 ILE A CD1 
1182  N  N   . GLU A  147 ? 0.1260 0.1118 0.1304 0.0099  0.0392  0.0529  147 GLU A N   
1183  C  CA  . GLU A  147 ? 0.1358 0.1159 0.1518 -0.0043 0.0408  0.0571  147 GLU A CA  
1184  C  C   . GLU A  147 ? 0.1246 0.1331 0.1393 0.0280  0.0370  0.0529  147 GLU A C   
1185  O  O   . GLU A  147 ? 0.1323 0.1306 0.1416 0.0208  0.0311  0.0452  147 GLU A O   
1186  C  CB  . GLU A  147 ? 0.1662 0.1594 0.1662 -0.0344 0.0430  0.0518  147 GLU A CB  
1187  C  CG  . GLU A  147 ? 0.1624 0.1437 0.1938 0.0034  0.0432  0.0443  147 GLU A CG  
1188  C  CD  . GLU A  147 ? 0.1965 0.1631 0.2224 -0.0080 0.0483  0.0537  147 GLU A CD  
1189  O  OE1 . GLU A  147 ? 0.2226 0.2138 0.2560 0.0031  0.0406  0.0189  147 GLU A OE1 
1190  O  OE2 . GLU A  147 ? 0.3298 0.1509 0.3488 0.0317  -0.0162 0.0190  147 GLU A OE2 
1191  N  N   A MET A  148 ? 0.1515 0.1391 0.1578 0.0160  0.0676  0.0307  148 MET A N   
1192  N  N   B MET A  148 ? 0.1937 0.1425 0.1247 0.0208  0.0727  0.0842  148 MET A N   
1193  C  CA  A MET A  148 ? 0.1269 0.2188 0.1373 -0.0205 0.0577  0.0549  148 MET A CA  
1194  C  CA  B MET A  148 ? 0.2190 0.1811 0.1438 0.0740  0.0570  0.1064  148 MET A CA  
1195  C  C   A MET A  148 ? 0.1009 0.2229 0.2037 -0.0086 0.0518  0.0649  148 MET A C   
1196  C  C   B MET A  148 ? 0.1497 0.1863 0.1939 0.0606  0.0643  0.0755  148 MET A C   
1197  O  O   A MET A  148 ? 0.2202 0.1545 0.1611 -0.0096 0.0285  0.0355  148 MET A O   
1198  O  O   B MET A  148 ? 0.2080 0.2037 0.1994 0.0342  0.0450  0.0935  148 MET A O   
1199  C  CB  A MET A  148 ? 0.1193 0.2396 0.1290 -0.0483 0.0397  -0.0027 148 MET A CB  
1200  C  CB  B MET A  148 ? 0.2285 0.1860 0.1601 -0.0098 0.0597  0.1031  148 MET A CB  
1201  C  CG  A MET A  148 ? 0.2457 0.3533 0.1097 0.0130  0.0667  -0.0233 148 MET A CG  
1202  C  CG  B MET A  148 ? 0.2008 0.1914 0.2044 0.0131  0.0577  0.1412  148 MET A CG  
1203  S  SD  A MET A  148 ? 0.2610 0.4302 0.3819 0.0577  0.1425  0.2601  148 MET A SD  
1204  S  SD  B MET A  148 ? 0.2515 0.2230 0.1996 0.0168  0.0516  0.0680  148 MET A SD  
1205  C  CE  A MET A  148 ? 0.2978 0.5712 0.4027 -0.1500 -0.0711 0.2372  148 MET A CE  
1206  C  CE  B MET A  148 ? 0.1933 0.1545 0.3512 0.0005  -0.0837 0.1437  148 MET A CE  
1207  N  N   . GLY A  149 ? 0.1394 0.2124 0.1845 0.0262  0.0476  0.0803  149 GLY A N   
1208  C  CA  . GLY A  149 ? 0.1820 0.1994 0.1919 0.0566  0.0307  0.0869  149 GLY A CA  
1209  C  C   . GLY A  149 ? 0.1890 0.1421 0.1832 0.0342  0.0285  0.0593  149 GLY A C   
1210  O  O   . GLY A  149 ? 0.2079 0.1667 0.1694 0.0298  0.0392  0.0595  149 GLY A O   
1211  N  N   . SER A  150 ? 0.1817 0.1764 0.2357 0.0445  0.0421  0.0632  150 SER A N   
1212  C  CA  . SER A  150 ? 0.1990 0.2202 0.2380 0.0487  0.0238  0.0773  150 SER A CA  
1213  C  C   . SER A  150 ? 0.2282 0.1879 0.2010 0.0335  0.0566  0.0763  150 SER A C   
1214  O  O   . SER A  150 ? 0.1957 0.2222 0.1823 0.0500  0.0177  0.0741  150 SER A O   
1215  C  CB  . SER A  150 ? 0.1741 0.3332 0.5769 0.1333  0.1208  0.0690  150 SER A CB  
1216  O  OG  . SER A  150 ? 0.1976 0.3260 0.5554 0.0665  0.0876  -0.0460 150 SER A OG  
1217  N  N   . PHE A  151 ? 0.1989 0.1987 0.1883 0.0467  0.0469  0.0859  151 PHE A N   
1218  C  CA  . PHE A  151 ? 0.1847 0.2185 0.1914 0.0450  0.0379  0.1199  151 PHE A CA  
1219  C  C   . PHE A  151 ? 0.1874 0.2084 0.1308 0.0476  0.0357  0.0351  151 PHE A C   
1220  O  O   . PHE A  151 ? 0.1881 0.2233 0.2184 0.0728  0.0599  0.0803  151 PHE A O   
1221  C  CB  . PHE A  151 ? 0.1851 0.1870 0.2319 0.0668  0.0310  0.1081  151 PHE A CB  
1222  C  CG  . PHE A  151 ? 0.2296 0.2136 0.1710 0.0357  0.0184  0.0873  151 PHE A CG  
1223  C  CD1 . PHE A  151 ? 0.2885 0.2236 0.2082 0.0590  -0.0035 0.0872  151 PHE A CD1 
1224  C  CD2 . PHE A  151 ? 0.1924 0.2842 0.2183 0.0346  -0.0003 0.1019  151 PHE A CD2 
1225  C  CE1 . PHE A  151 ? 0.2707 0.2588 0.1592 0.0320  -0.0040 0.0864  151 PHE A CE1 
1226  C  CE2 . PHE A  151 ? 0.2355 0.3407 0.1696 0.0313  0.0217  0.1075  151 PHE A CE2 
1227  C  CZ  . PHE A  151 ? 0.2718 0.3305 0.2014 0.0610  -0.0007 0.1314  151 PHE A CZ  
1228  N  N   . ASN A  152 ? 0.1671 0.2305 0.1675 0.0428  0.0366  0.0973  152 ASN A N   
1229  C  CA  . ASN A  152 ? 0.1737 0.2087 0.1491 0.0566  0.0307  0.0740  152 ASN A CA  
1230  C  C   . ASN A  152 ? 0.1893 0.2495 0.1574 0.0772  0.0076  0.0753  152 ASN A C   
1231  O  O   . ASN A  152 ? 0.1474 0.2248 0.1508 0.0584  0.0291  0.0584  152 ASN A O   
1232  C  CB  . ASN A  152 ? 0.1641 0.2100 0.1500 0.0685  0.0450  0.0736  152 ASN A CB  
1233  C  CG  . ASN A  152 ? 0.1660 0.1647 0.1323 0.0377  0.0082  0.0474  152 ASN A CG  
1234  O  OD1 . ASN A  152 ? 0.1687 0.2054 0.1542 0.0529  0.0245  0.0627  152 ASN A OD1 
1235  N  ND2 . ASN A  152 ? 0.1926 0.1513 0.1308 0.0353  0.0307  0.0366  152 ASN A ND2 
1236  N  N   . PRO A  153 ? 0.1571 0.2264 0.1870 0.0701  0.0245  0.0560  153 PRO A N   
1237  C  CA  . PRO A  153 ? 0.1655 0.2662 0.2059 0.0419  0.0094  0.1119  153 PRO A CA  
1238  C  C   . PRO A  153 ? 0.1536 0.2691 0.1590 0.0540  0.0286  0.0522  153 PRO A C   
1239  O  O   . PRO A  153 ? 0.2147 0.2854 0.1820 0.0104  -0.0168 0.0690  153 PRO A O   
1240  C  CB  . PRO A  153 ? 0.1716 0.3343 0.3605 0.0969  0.0344  0.1938  153 PRO A CB  
1241  C  CG  . PRO A  153 ? 0.2165 0.2917 0.3278 0.1080  -0.0181 0.0212  153 PRO A CG  
1242  C  CD  . PRO A  153 ? 0.1928 0.1951 0.2357 0.0939  0.0035  0.0405  153 PRO A CD  
1243  N  N   . SER A  154 ? 0.1477 0.2398 0.1669 0.0608  0.0410  0.0588  154 SER A N   
1244  C  CA  . SER A  154 ? 0.1789 0.2082 0.1499 0.0619  0.0467  0.0364  154 SER A CA  
1245  C  C   . SER A  154 ? 0.1644 0.2149 0.1208 0.0350  0.0160  0.0152  154 SER A C   
1246  O  O   . SER A  154 ? 0.1595 0.2274 0.1342 0.0443  0.0153  0.0322  154 SER A O   
1247  C  CB  . SER A  154 ? 0.2204 0.2091 0.1518 0.0636  0.0456  0.0217  154 SER A CB  
1248  O  OG  . SER A  154 ? 0.2463 0.2558 0.2078 0.1013  0.0658  0.0546  154 SER A OG  
1249  N  N   . TYR A  155 ? 0.1574 0.1930 0.1459 0.0597  0.0151  0.0285  155 TYR A N   
1250  C  CA  . TYR A  155 ? 0.1506 0.1865 0.1281 0.0308  0.0068  0.0326  155 TYR A CA  
1251  C  C   . TYR A  155 ? 0.1482 0.1935 0.1337 0.0313  0.0186  0.0348  155 TYR A C   
1252  O  O   . TYR A  155 ? 0.1832 0.1863 0.1161 0.0441  0.0217  0.0315  155 TYR A O   
1253  C  CB  . TYR A  155 ? 0.1455 0.2181 0.1308 0.0303  0.0118  0.0370  155 TYR A CB  
1254  C  CG  . TYR A  155 ? 0.1421 0.1987 0.1337 0.0579  0.0306  0.0286  155 TYR A CG  
1255  C  CD1 . TYR A  155 ? 0.1297 0.1586 0.1263 0.0136  0.0219  0.0361  155 TYR A CD1 
1256  C  CD2 . TYR A  155 ? 0.1342 0.1702 0.1240 0.0208  0.0199  0.0186  155 TYR A CD2 
1257  C  CE1 . TYR A  155 ? 0.1134 0.1714 0.1286 0.0264  0.0171  0.0577  155 TYR A CE1 
1258  C  CE2 . TYR A  155 ? 0.1215 0.1791 0.1238 0.0248  0.0172  0.0194  155 TYR A CE2 
1259  C  CZ  . TYR A  155 ? 0.1052 0.1473 0.1217 0.0109  0.0222  0.0366  155 TYR A CZ  
1260  O  OH  . TYR A  155 ? 0.1288 0.1590 0.1278 0.0171  -0.0012 0.0419  155 TYR A OH  
1261  N  N   . ASP A  156 ? 0.1533 0.2084 0.1145 0.0282  0.0125  0.0359  156 ASP A N   
1262  C  CA  . ASP A  156 ? 0.1755 0.2373 0.1164 0.0368  0.0255  0.0527  156 ASP A CA  
1263  C  C   . ASP A  156 ? 0.1623 0.2305 0.1347 0.0346  0.0142  0.0659  156 ASP A C   
1264  O  O   . ASP A  156 ? 0.2158 0.2718 0.1365 0.0203  0.0148  0.0333  156 ASP A O   
1265  C  CB  . ASP A  156 ? 0.2296 0.2673 0.1308 0.0368  0.0228  0.0662  156 ASP A CB  
1266  C  CG  . ASP A  156 ? 0.2447 0.3271 0.1682 0.0408  0.0270  0.0942  156 ASP A CG  
1267  O  OD1 . ASP A  156 ? 0.2391 0.2271 0.1419 0.0223  0.0339  0.0001  156 ASP A OD1 
1268  O  OD2 . ASP A  156 ? 0.3702 0.4490 0.1536 0.1123  0.0179  0.0693  156 ASP A OD2 
1269  N  N   . LYS A  157 ? 0.1669 0.2425 0.1410 0.0197  0.0131  0.0564  157 LYS A N   
1270  C  CA  . LYS A  157 ? 0.1741 0.2053 0.1838 0.0077  0.0296  0.0485  157 LYS A CA  
1271  C  C   . LYS A  157 ? 0.1818 0.2238 0.1259 0.0151  0.0445  0.0339  157 LYS A C   
1272  O  O   . LYS A  157 ? 0.2172 0.2531 0.2522 -0.0148 0.0287  0.0043  157 LYS A O   
1273  C  CB  . LYS A  157 ? 0.1495 0.2172 0.1748 -0.0048 0.0397  0.0337  157 LYS A CB  
1274  C  CG  . LYS A  157 ? 0.2068 0.2316 0.1791 0.0401  0.0318  0.0318  157 LYS A CG  
1275  C  CD  . LYS A  157 ? 0.1965 0.3133 0.1676 0.0584  0.0397  0.0551  157 LYS A CD  
1276  C  CE  . LYS A  157 ? 0.2727 0.3210 0.2545 0.1384  -0.0273 0.0617  157 LYS A CE  
1277  N  NZ  . LYS A  157 ? 0.2407 0.3765 0.2057 0.1234  0.0071  0.0430  157 LYS A NZ  
1278  N  N   . ILE A  158 ? 0.2463 0.1899 0.1296 0.0305  0.0097  0.0242  158 ILE A N   
1279  C  CA  . ILE A  158 ? 0.2617 0.1944 0.1114 0.0227  0.0299  0.0071  158 ILE A CA  
1280  C  C   . ILE A  158 ? 0.2118 0.2143 0.1344 -0.0085 0.0193  0.0428  158 ILE A C   
1281  O  O   . ILE A  158 ? 0.2442 0.2278 0.1374 0.0020  0.0208  0.0244  158 ILE A O   
1282  C  CB  . ILE A  158 ? 0.3328 0.2037 0.1150 0.0631  0.0379  0.0328  158 ILE A CB  
1283  C  CG1 . ILE A  158 ? 0.4388 0.2041 0.1657 0.0461  0.0952  0.0339  158 ILE A CG1 
1284  C  CG2 . ILE A  158 ? 0.3481 0.2188 0.1085 0.0658  0.0386  0.0111  158 ILE A CG2 
1285  C  CD1 . ILE A  158 ? 0.6891 0.3197 0.0863 0.1336  0.0658  0.0425  158 ILE A CD1 
1286  N  N   . PHE A  159 ? 0.1901 0.1944 0.1125 0.0103  0.0207  0.0119  159 PHE A N   
1287  C  CA  . PHE A  159 ? 0.1703 0.2664 0.1134 0.0003  0.0219  0.0198  159 PHE A CA  
1288  C  C   . PHE A  159 ? 0.2055 0.2361 0.1030 0.0262  0.0467  0.0313  159 PHE A C   
1289  O  O   . PHE A  159 ? 0.1868 0.2364 0.1360 0.0054  0.0294  0.0114  159 PHE A O   
1290  C  CB  . PHE A  159 ? 0.1689 0.2372 0.1321 0.0085  0.0057  0.0093  159 PHE A CB  
1291  C  CG  . PHE A  159 ? 0.1696 0.2066 0.1312 0.0244  0.0135  0.0105  159 PHE A CG  
1292  C  CD1 . PHE A  159 ? 0.2721 0.1969 0.1341 0.0742  -0.0164 0.0155  159 PHE A CD1 
1293  C  CD2 . PHE A  159 ? 0.1729 0.2957 0.1500 -0.0267 0.0153  -0.0102 159 PHE A CD2 
1294  C  CE1 . PHE A  159 ? 0.2660 0.2725 0.1734 0.1086  -0.0302 -0.0225 159 PHE A CE1 
1295  C  CE2 . PHE A  159 ? 0.1955 0.3260 0.1425 -0.0138 0.0071  -0.0071 159 PHE A CE2 
1296  C  CZ  . PHE A  159 ? 0.1773 0.3231 0.1256 0.0734  0.0373  0.0114  159 PHE A CZ  
1297  N  N   . SER A  160 ? 0.1937 0.2111 0.1299 -0.0108 0.0020  0.0359  160 SER A N   
1298  C  CA  . SER A  160 ? 0.2296 0.2312 0.1303 -0.0043 -0.0146 0.0245  160 SER A CA  
1299  C  C   . SER A  160 ? 0.2052 0.2469 0.1520 0.0368  0.0353  0.0201  160 SER A C   
1300  O  O   . SER A  160 ? 0.2608 0.3201 0.1351 -0.0471 -0.0074 0.0296  160 SER A O   
1301  C  CB  . SER A  160 ? 0.2138 0.2800 0.1807 0.0028  -0.0141 0.0938  160 SER A CB  
1302  O  OG  . SER A  160 ? 0.2048 0.3846 0.2494 0.0339  0.0320  0.1262  160 SER A OG  
1303  N  N   . HIS A  161 ? 0.1861 0.2409 0.1495 -0.0328 0.0221  0.0164  161 HIS A N   
1304  C  CA  . HIS A  161 ? 0.1955 0.2287 0.1617 -0.0130 0.0377  0.0148  161 HIS A CA  
1305  C  C   . HIS A  161 ? 0.1879 0.2492 0.1588 -0.0239 0.0131  0.0259  161 HIS A C   
1306  O  O   . HIS A  161 ? 0.2233 0.2398 0.1736 -0.0502 0.0342  -0.0005 161 HIS A O   
1307  C  CB  . HIS A  161 ? 0.2066 0.2570 0.1782 0.0003  0.0709  0.0172  161 HIS A CB  
1308  C  CG  . HIS A  161 ? 0.1894 0.2084 0.2152 -0.0044 0.0234  0.0206  161 HIS A CG  
1309  N  ND1 . HIS A  161 ? 0.1879 0.2831 0.2479 -0.0188 0.0210  -0.0074 161 HIS A ND1 
1310  C  CD2 . HIS A  161 ? 0.2149 0.2610 0.2454 0.0317  0.0252  -0.0476 161 HIS A CD2 
1311  C  CE1 . HIS A  161 ? 0.2678 0.2579 0.4084 0.0041  0.0555  -0.0414 161 HIS A CE1 
1312  N  NE2 . HIS A  161 ? 0.1912 0.2757 0.2879 0.0093  0.0491  0.0162  161 HIS A NE2 
1313  N  N   . LEU A  162 ? 0.1826 0.2035 0.1753 -0.0010 0.0021  -0.0054 162 LEU A N   
1314  C  CA  . LEU A  162 ? 0.1924 0.2363 0.1813 -0.0020 0.0266  -0.0573 162 LEU A CA  
1315  C  C   . LEU A  162 ? 0.2346 0.2154 0.1569 -0.0296 0.0206  -0.0142 162 LEU A C   
1316  O  O   . LEU A  162 ? 0.1854 0.2197 0.2222 -0.0264 0.0461  -0.0335 162 LEU A O   
1317  C  CB  . LEU A  162 ? 0.2048 0.2339 0.1651 -0.0132 0.0028  -0.0456 162 LEU A CB  
1318  C  CG  . LEU A  162 ? 0.2420 0.2576 0.1649 0.0496  -0.0390 -0.0659 162 LEU A CG  
1319  C  CD1 . LEU A  162 ? 0.2278 0.4237 0.2116 0.0174  -0.0483 -0.1552 162 LEU A CD1 
1320  C  CD2 . LEU A  162 ? 0.3837 0.2705 0.1861 0.0996  -0.0637 -0.0261 162 LEU A CD2 
1321  N  N   . GLN A  163 ? 0.2143 0.2405 0.1619 -0.0399 0.0390  -0.0071 163 GLN A N   
1322  C  CA  . GLN A  163 ? 0.2836 0.2666 0.1405 -0.0430 0.0109  0.0026  163 GLN A CA  
1323  C  C   . GLN A  163 ? 0.2833 0.2354 0.2010 -0.0546 0.0627  -0.0353 163 GLN A C   
1324  O  O   . GLN A  163 ? 0.3402 0.3086 0.2350 -0.0658 0.0876  -0.0443 163 GLN A O   
1325  C  CB  . GLN A  163 ? 0.3172 0.2134 0.2064 -0.0359 0.0498  0.0406  163 GLN A CB  
1326  C  CG  . GLN A  163 ? 0.2957 0.3686 0.3082 0.0370  -0.0057 0.0577  163 GLN A CG  
1327  C  CD  . GLN A  163 ? 0.2748 0.5683 0.4760 0.0181  0.0244  0.2700  163 GLN A CD  
1328  O  OE1 . GLN A  163 ? 0.3729 0.3278 0.4099 -0.0540 -0.1124 0.0650  163 GLN A OE1 
1329  N  NE2 . GLN A  163 ? 0.3371 0.3968 0.6243 0.0599  0.0222  0.1825  163 GLN A NE2 
1330  N  N   . HIS A  164 ? 0.2185 0.2381 0.1445 -0.0399 0.0081  -0.0088 164 HIS A N   
1331  C  CA  . HIS A  164 ? 0.2294 0.2581 0.1277 -0.0234 -0.0012 -0.0264 164 HIS A CA  
1332  C  C   . HIS A  164 ? 0.1895 0.2447 0.1389 -0.0267 -0.0140 -0.0093 164 HIS A C   
1333  O  O   . HIS A  164 ? 0.2463 0.2662 0.2069 -0.0795 -0.0373 -0.0119 164 HIS A O   
1334  C  CB  . HIS A  164 ? 0.2246 0.3504 0.1500 -0.0244 0.0065  -0.0137 164 HIS A CB  
1335  C  CG  . HIS A  164 ? 0.2131 0.2118 0.1752 -0.0372 -0.0093 -0.0210 164 HIS A CG  
1336  N  ND1 . HIS A  164 ? 0.2296 0.2511 0.2202 -0.0644 -0.0331 -0.0012 164 HIS A ND1 
1337  C  CD2 . HIS A  164 ? 0.2256 0.3111 0.1730 0.0252  0.0165  -0.0161 164 HIS A CD2 
1338  C  CE1 . HIS A  164 ? 0.2474 0.1879 0.1653 -0.0315 0.0208  0.0017  164 HIS A CE1 
1339  N  NE2 . HIS A  164 ? 0.4135 0.2987 0.2248 0.0640  0.0082  -0.0020 164 HIS A NE2 
1340  N  N   . VAL A  165 ? 0.1849 0.2339 0.1249 -0.0209 -0.0109 -0.0280 165 VAL A N   
1341  C  CA  . VAL A  165 ? 0.1612 0.2131 0.2032 -0.0223 0.0040  0.0111  165 VAL A CA  
1342  C  C   . VAL A  165 ? 0.1599 0.2152 0.1439 -0.0308 0.0015  -0.0342 165 VAL A C   
1343  O  O   . VAL A  165 ? 0.1775 0.2303 0.1477 -0.0124 0.0165  -0.0339 165 VAL A O   
1344  C  CB  . VAL A  165 ? 0.2046 0.2448 0.1694 -0.0322 0.0346  0.0252  165 VAL A CB  
1345  C  CG1 . VAL A  165 ? 0.1653 0.2885 0.2443 -0.0292 0.0355  -0.0121 165 VAL A CG1 
1346  C  CG2 . VAL A  165 ? 0.1630 0.2465 0.1779 -0.0197 0.0099  -0.0274 165 VAL A CG2 
1347  N  N   . LYS A  166 ? 0.1703 0.2276 0.1601 -0.0315 0.0251  -0.0197 166 LYS A N   
1348  C  CA  . LYS A  166 ? 0.2034 0.1888 0.1306 -0.0170 0.0274  -0.0383 166 LYS A CA  
1349  C  C   . LYS A  166 ? 0.1823 0.1908 0.1371 -0.0326 0.0093  0.0099  166 LYS A C   
1350  O  O   . LYS A  166 ? 0.1757 0.2105 0.1912 -0.0163 0.0082  -0.0410 166 LYS A O   
1351  C  CB  . LYS A  166 ? 0.2165 0.2312 0.1554 -0.0399 0.0212  0.0430  166 LYS A CB  
1352  C  CG  . LYS A  166 ? 0.2285 0.2278 0.1750 -0.0593 0.0109  0.0077  166 LYS A CG  
1353  C  CD  . LYS A  166 ? 0.3219 0.4417 0.1772 -0.1670 0.0104  0.0031  166 LYS A CD  
1354  C  CE  . LYS A  166 ? 0.6086 0.6570 0.3282 0.0125  -0.1366 0.0606  166 LYS A CE  
1355  N  NZ  . LYS A  166 ? 0.8260 0.6269 0.1511 -0.3122 0.1411  -0.0324 166 LYS A NZ  
1356  N  N   . TYR A  167 ? 0.2196 0.1790 0.1441 -0.0273 0.0161  -0.0209 167 TYR A N   
1357  C  CA  . TYR A  167 ? 0.2372 0.1551 0.1594 -0.0460 0.0038  -0.0197 167 TYR A CA  
1358  C  C   . TYR A  167 ? 0.1863 0.1926 0.1685 -0.0258 0.0087  0.0000  167 TYR A C   
1359  O  O   . TYR A  167 ? 0.2079 0.2458 0.1480 -0.0342 0.0003  -0.0104 167 TYR A O   
1360  C  CB  . TYR A  167 ? 0.2910 0.2159 0.1206 -0.0494 0.0248  -0.0255 167 TYR A CB  
1361  C  CG  . TYR A  167 ? 0.2010 0.2222 0.1541 -0.0328 0.0337  -0.0705 167 TYR A CG  
1362  C  CD1 . TYR A  167 ? 0.2317 0.2172 0.2120 -0.0310 0.0430  -0.0657 167 TYR A CD1 
1363  C  CD2 . TYR A  167 ? 0.2285 0.3420 0.1269 -0.0667 0.0172  -0.0241 167 TYR A CD2 
1364  C  CE1 . TYR A  167 ? 0.2389 0.2382 0.2267 -0.0148 0.0812  -0.0392 167 TYR A CE1 
1365  C  CE2 . TYR A  167 ? 0.2597 0.3217 0.1702 -0.0859 0.0443  -0.0229 167 TYR A CE2 
1366  C  CZ  . TYR A  167 ? 0.2615 0.2775 0.1784 -0.0438 0.0685  -0.0305 167 TYR A CZ  
1367  O  OH  . TYR A  167 ? 0.3443 0.3352 0.2305 -0.0976 0.0961  0.0026  167 TYR A OH  
1368  N  N   . LYS A  168 ? 0.2351 0.2045 0.1856 0.0082  0.0032  0.0020  168 LYS A N   
1369  C  CA  . LYS A  168 ? 0.2296 0.1859 0.2073 -0.0013 0.0120  0.0226  168 LYS A CA  
1370  C  C   . LYS A  168 ? 0.2822 0.1766 0.2116 -0.0275 0.0199  0.0074  168 LYS A C   
1371  O  O   . LYS A  168 ? 0.2791 0.2176 0.2105 -0.0331 0.0324  -0.0390 168 LYS A O   
1372  C  CB  . LYS A  168 ? 0.2910 0.1822 0.2596 0.0140  -0.0359 -0.0244 168 LYS A CB  
1373  C  CG  . LYS A  168 ? 0.3510 0.2784 0.2312 -0.0006 -0.0575 0.0120  168 LYS A CG  
1374  C  CD  . LYS A  168 ? 0.4569 0.2447 0.2197 0.0324  -0.0662 0.0270  168 LYS A CD  
1375  C  CE  . LYS A  168 ? 0.6403 0.2262 0.4589 0.1231  -0.0222 0.1176  168 LYS A CE  
1376  N  NZ  . LYS A  168 ? 0.7017 0.3700 0.4730 0.2213  -0.0835 -0.0074 168 LYS A NZ  
1377  N  N   . GLY A  169 ? 0.3005 0.2389 0.1967 -0.0353 0.0593  0.0137  169 GLY A N   
1378  C  CA  . GLY A  169 ? 0.2567 0.2637 0.3021 -0.0384 0.0588  0.0130  169 GLY A CA  
1379  C  C   . GLY A  169 ? 0.2610 0.1966 0.3628 -0.0509 0.0846  0.0151  169 GLY A C   
1380  O  O   . GLY A  169 ? 0.2630 0.3504 0.4505 -0.0615 0.0861  0.1333  169 GLY A O   
1381  N  N   . GLN A  170 ? 0.2551 0.2066 0.1957 -0.0303 0.0165  0.0093  170 GLN A N   
1382  C  CA  . GLN A  170 ? 0.2111 0.2456 0.1551 -0.0465 0.0313  0.0015  170 GLN A CA  
1383  C  C   . GLN A  170 ? 0.1924 0.2694 0.1292 -0.0255 0.0209  0.0189  170 GLN A C   
1384  O  O   . GLN A  170 ? 0.2323 0.2827 0.1525 -0.0193 -0.0093 0.0152  170 GLN A O   
1385  C  CB  . GLN A  170 ? 0.2122 0.2161 0.1400 -0.0318 0.0399  -0.0270 170 GLN A CB  
1386  C  CG  . GLN A  170 ? 0.2472 0.1813 0.1567 -0.0163 0.0166  -0.0175 170 GLN A CG  
1387  C  CD  . GLN A  170 ? 0.2357 0.2714 0.1534 -0.0712 -0.0035 -0.0232 170 GLN A CD  
1388  O  OE1 . GLN A  170 ? 0.2267 0.2522 0.1836 -0.0454 -0.0116 -0.0055 170 GLN A OE1 
1389  N  NE2 . GLN A  170 ? 0.2366 0.3411 0.1773 -0.0834 0.0107  -0.0728 170 GLN A NE2 
1390  N  N   A GLU A  171 ? 0.1835 0.2912 0.2165 -0.0696 -0.0166 -0.0024 171 GLU A N   
1391  N  N   B GLU A  171 ? 0.1578 0.3303 0.1220 -0.0221 0.0212  -0.0381 171 GLU A N   
1392  C  CA  A GLU A  171 ? 0.2122 0.2233 0.1617 -0.0493 -0.0522 0.0087  171 GLU A CA  
1393  C  CA  B GLU A  171 ? 0.1994 0.3644 0.1569 0.0209  0.0861  0.0381  171 GLU A CA  
1394  C  C   A GLU A  171 ? 0.1874 0.3061 0.1182 -0.0194 -0.0186 0.0206  171 GLU A C   
1395  C  C   B GLU A  171 ? 0.1292 0.3337 0.1335 -0.0509 0.0175  -0.0201 171 GLU A C   
1396  O  O   A GLU A  171 ? 0.1572 0.2958 0.1472 -0.0377 -0.0300 -0.0115 171 GLU A O   
1397  O  O   B GLU A  171 ? 0.1924 0.3540 0.1382 -0.0237 0.0096  -0.0197 171 GLU A O   
1398  C  CB  A GLU A  171 ? 0.2010 0.2397 0.2266 0.0171  0.0467  0.0181  171 GLU A CB  
1399  C  CB  B GLU A  171 ? 0.1551 0.3754 0.1723 -0.0320 -0.0196 -0.0087 171 GLU A CB  
1400  C  CG  A GLU A  171 ? 0.3239 0.2781 0.2657 -0.0115 0.0103  0.0582  171 GLU A CG  
1401  C  CG  B GLU A  171 ? 0.2106 0.3889 0.2479 -0.1059 -0.0218 -0.0445 171 GLU A CG  
1402  C  CD  A GLU A  171 ? 0.3176 0.3084 0.2091 -0.0276 0.0201  -0.0031 171 GLU A CD  
1403  C  CD  B GLU A  171 ? 0.2278 0.4788 0.2863 -0.0848 -0.0626 0.0662  171 GLU A CD  
1404  O  OE1 A GLU A  171 ? 0.2851 0.3161 0.2973 -0.0573 0.0063  0.1076  171 GLU A OE1 
1405  O  OE1 B GLU A  171 ? 0.2468 0.2878 0.2657 -0.0121 -0.0208 0.0227  171 GLU A OE1 
1406  O  OE2 A GLU A  171 ? 0.4343 0.3533 0.2405 -0.0322 0.0471  0.0940  171 GLU A OE2 
1407  O  OE2 B GLU A  171 ? 0.1960 0.4126 0.2346 -0.0614 -0.0518 0.0230  171 GLU A OE2 
1408  N  N   . ALA A  172 ? 0.1461 0.3258 0.1412 -0.0041 0.0151  -0.0060 172 ALA A N   
1409  C  CA  . ALA A  172 ? 0.1484 0.3711 0.1768 0.0124  -0.0193 0.0165  172 ALA A CA  
1410  C  C   . ALA A  172 ? 0.1420 0.3937 0.1317 -0.0233 -0.0355 -0.0074 172 ALA A C   
1411  O  O   . ALA A  172 ? 0.1781 0.5411 0.1253 0.0491  -0.0285 0.0000  172 ALA A O   
1412  C  CB  . ALA A  172 ? 0.2087 0.3416 0.2248 0.0428  0.0307  0.0445  172 ALA A CB  
1413  N  N   . PHE A  173 ? 0.1601 0.4620 0.1532 0.0408  -0.0196 0.0035  173 PHE A N   
1414  C  CA  . PHE A  173 ? 0.1969 0.3544 0.1757 0.0247  -0.0318 -0.0496 173 PHE A CA  
1415  C  C   . PHE A  173 ? 0.2186 0.3350 0.1913 0.0544  -0.0441 -0.0222 173 PHE A C   
1416  O  O   . PHE A  173 ? 0.4744 0.5625 0.1712 0.0678  -0.0780 0.0518  173 PHE A O   
1417  C  CB  . PHE A  173 ? 0.1852 0.3907 0.3287 0.0019  -0.0586 -0.0309 173 PHE A CB  
1418  C  CG  . PHE A  173 ? 0.2026 0.3481 0.3673 -0.0060 -0.1340 -0.0364 173 PHE A CG  
1419  C  CD1 . PHE A  173 ? 0.2274 0.3546 0.4914 0.1121  -0.0681 0.0579  173 PHE A CD1 
1420  C  CD2 . PHE A  173 ? 0.2949 0.5109 0.5918 0.1114  -0.2030 -0.1743 173 PHE A CD2 
1421  C  CE1 . PHE A  173 ? 0.4207 0.3849 0.5040 0.1585  -0.1768 -0.0142 173 PHE A CE1 
1422  C  CE2 . PHE A  173 ? 0.5407 0.4194 0.4291 0.2358  -0.1969 -0.1490 173 PHE A CE2 
1423  C  CZ  . PHE A  173 ? 0.6764 0.6572 0.5059 0.0355  -0.1159 -0.1400 173 PHE A CZ  
1424  N  N   . VAL A  174 ? 0.1793 0.2933 0.1624 0.0000  -0.0104 -0.0049 174 VAL A N   
1425  C  CA  . VAL A  174 ? 0.1739 0.2969 0.1868 -0.0068 0.0046  0.0230  174 VAL A CA  
1426  C  C   . VAL A  174 ? 0.1269 0.3361 0.1771 -0.0080 -0.0397 0.0476  174 VAL A C   
1427  O  O   . VAL A  174 ? 0.1905 0.3470 0.2012 -0.0171 -0.0087 0.0537  174 VAL A O   
1428  C  CB  . VAL A  174 ? 0.1489 0.3041 0.1662 -0.0051 -0.0100 0.0458  174 VAL A CB  
1429  C  CG1 . VAL A  174 ? 0.2000 0.3140 0.2739 0.0197  -0.0107 0.0066  174 VAL A CG1 
1430  C  CG2 . VAL A  174 ? 0.1983 0.3494 0.1942 0.0035  0.0142  0.0509  174 VAL A CG2 
1431  N  N   . PRO A  175 ? 0.1779 0.3641 0.1470 0.0222  -0.0193 0.0223  175 PRO A N   
1432  C  CA  . PRO A  175 ? 0.1611 0.3289 0.2046 0.0395  -0.0368 0.0103  175 PRO A CA  
1433  C  C   . PRO A  175 ? 0.1128 0.3982 0.1491 0.0397  -0.0377 0.0232  175 PRO A C   
1434  O  O   . PRO A  175 ? 0.1459 0.3576 0.1879 0.0249  -0.0289 0.0337  175 PRO A O   
1435  C  CB  . PRO A  175 ? 0.2942 0.4171 0.1683 0.1544  -0.0617 0.0010  175 PRO A CB  
1436  C  CG  . PRO A  175 ? 0.2648 0.6011 0.2114 0.1796  -0.0236 0.0342  175 PRO A CG  
1437  C  CD  . PRO A  175 ? 0.2068 0.3305 0.2046 0.0189  -0.0392 0.0615  175 PRO A CD  
1438  N  N   . GLY A  176 ? 0.1559 0.3244 0.1861 0.0166  -0.0060 -0.0032 176 GLY A N   
1439  C  CA  . GLY A  176 ? 0.1516 0.2951 0.1962 0.0015  -0.0267 0.0135  176 GLY A CA  
1440  C  C   . GLY A  176 ? 0.1739 0.3391 0.1611 -0.0253 -0.0322 0.0720  176 GLY A C   
1441  O  O   . GLY A  176 ? 0.1707 0.3691 0.1929 0.0284  -0.0513 0.0227  176 GLY A O   
1442  N  N   . PHE A  177 ? 0.1351 0.3287 0.1669 0.0295  -0.0337 0.0221  177 PHE A N   
1443  C  CA  . PHE A  177 ? 0.1513 0.2924 0.1811 0.0144  0.0010  0.0601  177 PHE A CA  
1444  C  C   . PHE A  177 ? 0.1283 0.2639 0.1647 0.0373  0.0114  0.0707  177 PHE A C   
1445  O  O   . PHE A  177 ? 0.1429 0.2558 0.1854 0.0152  -0.0096 0.0737  177 PHE A O   
1446  C  CB  . PHE A  177 ? 0.1475 0.3034 0.2019 0.0303  -0.0135 0.0736  177 PHE A CB  
1447  C  CG  . PHE A  177 ? 0.1608 0.2811 0.1374 0.0423  -0.0027 0.0355  177 PHE A CG  
1448  C  CD1 . PHE A  177 ? 0.1651 0.2976 0.1385 0.0364  0.0214  0.0244  177 PHE A CD1 
1449  C  CD2 . PHE A  177 ? 0.1827 0.3231 0.1337 0.0313  -0.0098 0.0537  177 PHE A CD2 
1450  C  CE1 . PHE A  177 ? 0.1475 0.3285 0.1671 0.0258  -0.0020 0.0439  177 PHE A CE1 
1451  C  CE2 . PHE A  177 ? 0.1772 0.2991 0.1472 0.0259  0.0093  0.0474  177 PHE A CE2 
1452  C  CZ  . PHE A  177 ? 0.1531 0.2648 0.1513 0.0163  0.0104  0.0410  177 PHE A CZ  
1453  N  N   . ASN A  178 ? 0.1562 0.2538 0.1991 0.0461  -0.0187 0.0443  178 ASN A N   
1454  C  CA  . ASN A  178 ? 0.1427 0.2606 0.1879 0.0631  -0.0129 0.0208  178 ASN A CA  
1455  C  C   . ASN A  178 ? 0.1316 0.2388 0.1423 0.0348  -0.0013 0.0403  178 ASN A C   
1456  O  O   . ASN A  178 ? 0.1423 0.2184 0.1549 0.0252  0.0091  0.0483  178 ASN A O   
1457  C  CB  . ASN A  178 ? 0.1560 0.2583 0.2166 0.0864  -0.0071 0.0203  178 ASN A CB  
1458  C  CG  . ASN A  178 ? 0.1626 0.2284 0.2055 0.0952  0.0096  0.0234  178 ASN A CG  
1459  O  OD1 . ASN A  178 ? 0.1732 0.2623 0.2019 0.0860  0.0093  0.0480  178 ASN A OD1 
1460  N  ND2 . ASN A  178 ? 0.2653 0.2499 0.2851 0.1181  0.0476  0.0659  178 ASN A ND2 
1461  N  N   . ILE A  179 ? 0.1261 0.2175 0.1558 0.0401  -0.0057 0.0432  179 ILE A N   
1462  C  CA  . ILE A  179 ? 0.1080 0.1820 0.1624 0.0187  0.0185  0.0559  179 ILE A CA  
1463  C  C   . ILE A  179 ? 0.1265 0.1879 0.1251 0.0384  0.0131  0.0368  179 ILE A C   
1464  O  O   . ILE A  179 ? 0.1127 0.1851 0.1486 0.0196  0.0137  0.0403  179 ILE A O   
1465  C  CB  . ILE A  179 ? 0.1163 0.1741 0.1755 0.0091  0.0125  0.0447  179 ILE A CB  
1466  C  CG1 . ILE A  179 ? 0.1103 0.2293 0.1400 0.0092  0.0266  0.0140  179 ILE A CG1 
1467  C  CG2 . ILE A  179 ? 0.1270 0.1635 0.1788 0.0313  0.0076  0.0491  179 ILE A CG2 
1468  C  CD1 . ILE A  179 ? 0.1504 0.2228 0.1552 0.0166  0.0285  0.0326  179 ILE A CD1 
1469  N  N   . GLU A  180 ? 0.1253 0.1822 0.1502 0.0368  0.0222  0.0357  180 GLU A N   
1470  C  CA  . GLU A  180 ? 0.1427 0.2012 0.1299 0.0244  0.0329  0.0311  180 GLU A CA  
1471  C  C   . GLU A  180 ? 0.1330 0.1675 0.1447 0.0421  0.0208  0.0162  180 GLU A C   
1472  O  O   . GLU A  180 ? 0.1407 0.1937 0.1597 0.0460  0.0286  0.0133  180 GLU A O   
1473  C  CB  . GLU A  180 ? 0.1750 0.2698 0.1562 0.0527  0.0599  0.0019  180 GLU A CB  
1474  C  CG  . GLU A  180 ? 0.2150 0.2917 0.2258 0.0555  0.0672  -0.0071 180 GLU A CG  
1475  C  CD  . GLU A  180 ? 0.3016 0.3454 0.1637 0.1145  0.0637  0.0297  180 GLU A CD  
1476  O  OE1 . GLU A  180 ? 0.2958 0.2991 0.2132 0.0964  0.1028  0.0007  180 GLU A OE1 
1477  O  OE2 . GLU A  180 ? 0.3176 0.3684 0.1908 0.1146  0.0931  0.0021  180 GLU A OE2 
1478  N  N   . GLU A  181 ? 0.1339 0.1766 0.1436 0.0414  0.0361  0.0489  181 GLU A N   
1479  C  CA  . GLU A  181 ? 0.1243 0.1763 0.1714 0.0342  0.0208  0.0570  181 GLU A CA  
1480  C  C   . GLU A  181 ? 0.1254 0.1658 0.1425 0.0485  0.0557  0.0619  181 GLU A C   
1481  O  O   . GLU A  181 ? 0.1389 0.1786 0.1841 0.0478  0.0335  0.0597  181 GLU A O   
1482  C  CB  . GLU A  181 ? 0.1475 0.2353 0.1538 0.0736  0.0244  0.0570  181 GLU A CB  
1483  C  CG  . GLU A  181 ? 0.1452 0.2357 0.1993 0.0646  -0.0074 0.0538  181 GLU A CG  
1484  C  CD  . GLU A  181 ? 0.1863 0.2443 0.2035 0.0549  0.0063  0.0138  181 GLU A CD  
1485  O  OE1 . GLU A  181 ? 0.2240 0.2840 0.1772 0.0619  -0.0006 0.0244  181 GLU A OE1 
1486  O  OE2 . GLU A  181 ? 0.1816 0.3066 0.2615 0.0826  -0.0074 0.0852  181 GLU A OE2 
1487  N  N   . LEU A  182 ? 0.1165 0.1717 0.1268 0.0592  0.0082  0.0353  182 LEU A N   
1488  C  CA  . LEU A  182 ? 0.1125 0.1538 0.1161 0.0362  0.0107  0.0452  182 LEU A CA  
1489  C  C   . LEU A  182 ? 0.1240 0.1462 0.1222 0.0324  0.0063  0.0476  182 LEU A C   
1490  O  O   . LEU A  182 ? 0.1243 0.1629 0.1184 0.0195  0.0135  0.0255  182 LEU A O   
1491  C  CB  . LEU A  182 ? 0.1238 0.1656 0.1015 0.0388  0.0216  0.0357  182 LEU A CB  
1492  C  CG  . LEU A  182 ? 0.1289 0.1453 0.1109 0.0305  0.0133  0.0266  182 LEU A CG  
1493  C  CD1 . LEU A  182 ? 0.1365 0.1708 0.1507 0.0094  0.0012  0.0196  182 LEU A CD1 
1494  C  CD2 . LEU A  182 ? 0.1536 0.1861 0.1155 0.0214  0.0186  0.0322  182 LEU A CD2 
1495  N  N   . LEU A  183 ? 0.1473 0.1500 0.1206 0.0240  0.0217  0.0035  183 LEU A N   
1496  C  CA  . LEU A  183 ? 0.1359 0.1326 0.1256 0.0335  0.0252  0.0195  183 LEU A CA  
1497  C  C   . LEU A  183 ? 0.1386 0.1484 0.1357 0.0320  0.0217  0.0264  183 LEU A C   
1498  O  O   . LEU A  183 ? 0.1561 0.1513 0.1527 0.0359  0.0126  0.0261  183 LEU A O   
1499  C  CB  . LEU A  183 ? 0.1768 0.1513 0.1199 -0.0017 0.0412  0.0192  183 LEU A CB  
1500  C  CG  . LEU A  183 ? 0.1714 0.1867 0.1297 0.0062  0.0368  0.0100  183 LEU A CG  
1501  C  CD1 . LEU A  183 ? 0.2202 0.2475 0.1806 -0.0373 0.0784  0.0194  183 LEU A CD1 
1502  C  CD2 . LEU A  183 ? 0.1841 0.1457 0.1649 0.0197  0.0178  0.0167  183 LEU A CD2 
1503  N  N   . PRO A  184 ? 0.1436 0.1367 0.1287 0.0476  0.0240  0.0132  184 PRO A N   
1504  C  CA  . PRO A  184 ? 0.1680 0.1378 0.1588 0.0313  0.0159  0.0192  184 PRO A CA  
1505  C  C   . PRO A  184 ? 0.2269 0.1562 0.1884 0.0555  0.0491  0.0571  184 PRO A C   
1506  O  O   . PRO A  184 ? 0.2459 0.1599 0.1886 0.0579  0.0715  0.0182  184 PRO A O   
1507  C  CB  . PRO A  184 ? 0.1856 0.1554 0.1991 0.0388  0.0038  0.0658  184 PRO A CB  
1508  C  CG  . PRO A  184 ? 0.1553 0.1903 0.1608 0.0035  0.0051  0.0584  184 PRO A CG  
1509  C  CD  . PRO A  184 ? 0.1513 0.1626 0.1307 0.0516  0.0103  0.0304  184 PRO A CD  
1510  N  N   . GLU A  185 ? 0.2935 0.1233 0.1948 0.0467  0.0428  0.0243  185 GLU A N   
1511  C  CA  . GLU A  185 ? 0.2890 0.1533 0.2023 0.0351  0.0259  -0.0017 185 GLU A CA  
1512  C  C   . GLU A  185 ? 0.2784 0.1829 0.1987 0.0656  0.0755  0.0361  185 GLU A C   
1513  O  O   . GLU A  185 ? 0.2275 0.1576 0.2481 0.0405  0.0340  -0.0068 185 GLU A O   
1514  C  CB  . GLU A  185 ? 0.3876 0.1551 0.2341 0.0148  0.0216  0.0245  185 GLU A CB  
1515  C  CG  . GLU A  185 ? 0.4587 0.2406 0.2653 0.1001  0.0132  0.0410  185 GLU A CG  
1516  C  CD  . GLU A  185 ? 0.5227 0.5160 0.4119 0.2617  -0.0333 -0.1199 185 GLU A CD  
1517  O  OE1 . GLU A  185 ? 0.8197 0.4832 0.3048 0.2795  0.0719  -0.0568 185 GLU A OE1 
1518  O  OE2 . GLU A  185 ? 0.5496 0.8245 0.4282 0.0759  0.0122  -0.1269 185 GLU A OE2 
1519  N  N   . ARG A  186 ? 0.2413 0.1414 0.2285 0.0568  0.0417  -0.0155 186 ARG A N   
1520  C  CA  . ARG A  186 ? 0.2518 0.1863 0.2197 0.0357  0.0712  -0.0156 186 ARG A CA  
1521  C  C   . ARG A  186 ? 0.1669 0.1896 0.2449 0.0405  0.0434  -0.0066 186 ARG A C   
1522  O  O   . ARG A  186 ? 0.1786 0.1928 0.2096 0.0328  0.0430  -0.0146 186 ARG A O   
1523  C  CB  . ARG A  186 ? 0.2998 0.1732 0.3508 0.0399  0.0403  -0.0051 186 ARG A CB  
1524  C  CG  . ARG A  186 ? 0.4230 0.1850 0.3422 0.0606  -0.0041 0.0120  186 ARG A CG  
1525  C  CD  . ARG A  186 ? 0.4446 0.2044 0.4374 -0.0115 0.0595  -0.0275 186 ARG A CD  
1526  N  NE  . ARG A  186 ? 0.5058 0.1638 0.3661 -0.0331 0.0333  0.0342  186 ARG A NE  
1527  C  CZ  . ARG A  186 ? 0.5170 0.1921 0.4266 0.0592  0.2384  -0.0877 186 ARG A CZ  
1528  N  NH1 . ARG A  186 ? 0.5722 0.2867 0.5932 0.0109  0.0935  0.0571  186 ARG A NH1 
1529  N  NH2 . ARG A  186 ? 0.4963 0.2430 0.6973 0.0118  0.2518  -0.0676 186 ARG A NH2 
1530  N  N   . THR A  187 ? 0.1739 0.1737 0.1702 0.0305  0.0463  -0.0307 187 THR A N   
1531  C  CA  . THR A  187 ? 0.1660 0.1798 0.1951 0.0351  0.0491  -0.0183 187 THR A CA  
1532  C  C   . THR A  187 ? 0.1665 0.2305 0.1827 0.0217  0.0601  -0.0373 187 THR A C   
1533  O  O   . THR A  187 ? 0.2005 0.2190 0.1509 0.0154  0.0500  -0.0174 187 THR A O   
1534  C  CB  . THR A  187 ? 0.1569 0.2030 0.1651 0.0074  0.0511  -0.0178 187 THR A CB  
1535  O  OG1 . THR A  187 ? 0.1861 0.2249 0.2707 0.0472  0.0375  -0.0603 187 THR A OG1 
1536  C  CG2 . THR A  187 ? 0.2129 0.1976 0.1605 0.0092  0.0241  -0.0251 187 THR A CG2 
1537  N  N   . ALA A  188 ? 0.1924 0.2344 0.1822 0.0447  0.0520  -0.0397 188 ALA A N   
1538  C  CA  . ALA A  188 ? 0.1888 0.2511 0.1680 0.0900  0.0272  -0.0637 188 ALA A CA  
1539  C  C   . ALA A  188 ? 0.1856 0.1944 0.1538 0.0239  0.0278  -0.0621 188 ALA A C   
1540  O  O   . ALA A  188 ? 0.1755 0.2267 0.1535 0.0178  0.0419  -0.0370 188 ALA A O   
1541  C  CB  . ALA A  188 ? 0.2640 0.2953 0.2366 0.1010  0.0099  -0.1256 188 ALA A CB  
1542  N  N   . GLU A  189 ? 0.1659 0.1675 0.1799 0.0219  0.0474  -0.0577 189 GLU A N   
1543  C  CA  . GLU A  189 ? 0.1666 0.1457 0.1775 0.0313  0.0588  -0.0201 189 GLU A CA  
1544  C  C   . GLU A  189 ? 0.1651 0.1366 0.1270 0.0157  0.0428  -0.0120 189 GLU A C   
1545  O  O   . GLU A  189 ? 0.1518 0.1353 0.1254 0.0197  0.0406  -0.0048 189 GLU A O   
1546  C  CB  . GLU A  189 ? 0.2011 0.1335 0.2108 -0.0027 0.0500  -0.0013 189 GLU A CB  
1547  C  CG  . GLU A  189 ? 0.2565 0.1694 0.2921 0.0049  0.0816  -0.0538 189 GLU A CG  
1548  C  CD  . GLU A  189 ? 0.4485 0.1770 0.3124 -0.0764 0.1729  -0.0901 189 GLU A CD  
1549  O  OE1 . GLU A  189 ? 0.3244 0.1859 0.2761 0.0001  0.0794  -0.0122 189 GLU A OE1 
1550  O  OE2 . GLU A  189 ? 0.4630 0.2384 0.5483 0.0754  0.0405  -0.1171 189 GLU A OE2 
1551  N  N   . TYR A  190 ? 0.1495 0.1292 0.1202 -0.0071 0.0294  -0.0038 190 TYR A N   
1552  C  CA  . TYR A  190 ? 0.1332 0.1040 0.1096 -0.0074 0.0207  -0.0129 190 TYR A CA  
1553  C  C   . TYR A  190 ? 0.1493 0.1543 0.0958 -0.0193 0.0434  0.0001  190 TYR A C   
1554  O  O   . TYR A  190 ? 0.1705 0.1502 0.1028 -0.0133 0.0262  -0.0037 190 TYR A O   
1555  C  CB  . TYR A  190 ? 0.1493 0.1425 0.1073 -0.0074 0.0485  -0.0074 190 TYR A CB  
1556  C  CG  . TYR A  190 ? 0.1574 0.1623 0.1033 -0.0054 0.0434  -0.0182 190 TYR A CG  
1557  C  CD1 . TYR A  190 ? 0.1921 0.1640 0.1154 -0.0505 0.0593  -0.0203 190 TYR A CD1 
1558  C  CD2 . TYR A  190 ? 0.1427 0.1825 0.1568 -0.0111 0.0560  -0.0187 190 TYR A CD2 
1559  C  CE1 . TYR A  190 ? 0.1739 0.1723 0.1377 -0.0359 0.0626  -0.0276 190 TYR A CE1 
1560  C  CE2 . TYR A  190 ? 0.1617 0.1987 0.1466 -0.0027 0.0729  -0.0275 190 TYR A CE2 
1561  C  CZ  . TYR A  190 ? 0.1825 0.1901 0.1386 -0.0244 0.0731  -0.0337 190 TYR A CZ  
1562  O  OH  . TYR A  190 ? 0.2208 0.2062 0.1639 -0.0456 0.1067  -0.0476 190 TYR A OH  
1563  N  N   . TYR A  191 ? 0.1263 0.1391 0.1084 -0.0051 0.0359  0.0070  191 TYR A N   
1564  C  CA  . TYR A  191 ? 0.1281 0.1299 0.1170 -0.0044 0.0357  0.0186  191 TYR A CA  
1565  C  C   . TYR A  191 ? 0.1326 0.1434 0.0843 0.0066  0.0135  0.0062  191 TYR A C   
1566  O  O   . TYR A  191 ? 0.1438 0.1827 0.0834 -0.0203 0.0167  0.0207  191 TYR A O   
1567  C  CB  . TYR A  191 ? 0.1376 0.1400 0.1174 -0.0174 0.0172  0.0062  191 TYR A CB  
1568  C  CG  . TYR A  191 ? 0.1429 0.1658 0.1109 -0.0285 0.0293  0.0109  191 TYR A CG  
1569  C  CD1 . TYR A  191 ? 0.1428 0.1668 0.1308 -0.0236 0.0140  0.0010  191 TYR A CD1 
1570  C  CD2 . TYR A  191 ? 0.1453 0.1310 0.1199 0.0182  0.0359  0.0089  191 TYR A CD2 
1571  C  CE1 . TYR A  191 ? 0.1552 0.1662 0.1585 -0.0165 0.0270  0.0120  191 TYR A CE1 
1572  C  CE2 . TYR A  191 ? 0.1380 0.1623 0.1430 -0.0006 0.0392  0.0275  191 TYR A CE2 
1573  C  CZ  . TYR A  191 ? 0.1556 0.1502 0.1535 -0.0208 0.0430  0.0048  191 TYR A CZ  
1574  O  OH  . TYR A  191 ? 0.1641 0.1845 0.1933 -0.0305 0.0276  0.0397  191 TYR A OH  
1575  N  N   . ARG A  192 ? 0.1425 0.1498 0.1057 0.0000  0.0127  0.0280  192 ARG A N   
1576  C  CA  . ARG A  192 ? 0.1305 0.1444 0.1116 -0.0118 0.0197  0.0175  192 ARG A CA  
1577  C  C   . ARG A  192 ? 0.1567 0.1447 0.1019 -0.0137 0.0241  0.0221  192 ARG A C   
1578  O  O   . ARG A  192 ? 0.1644 0.1859 0.1091 -0.0276 0.0015  0.0137  192 ARG A O   
1579  C  CB  . ARG A  192 ? 0.1473 0.1619 0.1283 -0.0062 0.0313  0.0141  192 ARG A CB  
1580  C  CG  . ARG A  192 ? 0.1759 0.1863 0.1222 -0.0447 0.0149  0.0179  192 ARG A CG  
1581  C  CD  . ARG A  192 ? 0.1775 0.1919 0.1190 -0.0263 0.0270  0.0234  192 ARG A CD  
1582  N  NE  . ARG A  192 ? 0.1524 0.2513 0.1364 -0.0480 0.0392  -0.0008 192 ARG A NE  
1583  C  CZ  . ARG A  192 ? 0.1553 0.2178 0.1206 -0.0307 0.0333  -0.0068 192 ARG A CZ  
1584  N  NH1 . ARG A  192 ? 0.1620 0.2481 0.1454 -0.0295 0.0500  -0.0147 192 ARG A NH1 
1585  N  NH2 . ARG A  192 ? 0.1484 0.2109 0.1800 -0.0227 0.0340  0.0071  192 ARG A NH2 
1586  N  N   . TYR A  193 ? 0.1272 0.1453 0.1035 -0.0219 0.0189  0.0296  193 TYR A N   
1587  C  CA  . TYR A  193 ? 0.1416 0.1615 0.0987 -0.0082 0.0035  0.0253  193 TYR A CA  
1588  C  C   . TYR A  193 ? 0.1212 0.1673 0.1118 -0.0241 0.0326  0.0252  193 TYR A C   
1589  O  O   . TYR A  193 ? 0.1285 0.1766 0.1165 -0.0154 0.0094  0.0408  193 TYR A O   
1590  C  CB  . TYR A  193 ? 0.1271 0.1588 0.1292 0.0114  0.0003  0.0063  193 TYR A CB  
1591  C  CG  . TYR A  193 ? 0.0953 0.1721 0.1097 -0.0109 0.0201  0.0359  193 TYR A CG  
1592  C  CD1 . TYR A  193 ? 0.1124 0.1484 0.1003 -0.0261 0.0142  0.0219  193 TYR A CD1 
1593  C  CD2 . TYR A  193 ? 0.1116 0.1743 0.1208 -0.0129 -0.0052 0.0573  193 TYR A CD2 
1594  C  CE1 . TYR A  193 ? 0.0869 0.1378 0.1200 -0.0031 0.0054  0.0137  193 TYR A CE1 
1595  C  CE2 . TYR A  193 ? 0.1102 0.1833 0.1184 -0.0186 0.0076  0.0599  193 TYR A CE2 
1596  C  CZ  . TYR A  193 ? 0.0942 0.1488 0.0965 -0.0147 0.0137  0.0302  193 TYR A CZ  
1597  O  OH  . TYR A  193 ? 0.1042 0.1023 0.1213 -0.0100 0.0113  0.0276  193 TYR A OH  
1598  N  N   . ARG A  194 ? 0.1650 0.1562 0.1030 -0.0098 0.0121  0.0317  194 ARG A N   
1599  C  CA  . ARG A  194 ? 0.1605 0.1495 0.1006 -0.0186 0.0318  0.0454  194 ARG A CA  
1600  C  C   . ARG A  194 ? 0.1459 0.1894 0.0912 -0.0107 -0.0010 0.0627  194 ARG A C   
1601  O  O   . ARG A  194 ? 0.1550 0.1816 0.1299 -0.0122 -0.0136 0.0498  194 ARG A O   
1602  C  CB  . ARG A  194 ? 0.2730 0.1703 0.1348 0.0046  0.0834  0.0584  194 ARG A CB  
1603  C  CG  . ARG A  194 ? 0.2989 0.2495 0.1385 -0.0060 0.0755  0.0663  194 ARG A CG  
1604  C  CD  . ARG A  194 ? 0.3650 0.6269 0.3066 0.0120  0.0189  -0.0799 194 ARG A CD  
1605  N  NE  . ARG A  194 ? 0.4088 0.6683 0.6802 -0.1788 0.2358  -0.0736 194 ARG A NE  
1606  C  CZ  . ARG A  194 ? 0.4370 0.4104 0.5950 -0.1129 0.2644  0.0737  194 ARG A CZ  
1607  N  NH1 . ARG A  194 ? 0.6054 0.4837 0.8374 -0.1181 0.3253  -0.1680 194 ARG A NH1 
1608  N  NH2 . ARG A  194 ? 0.6191 0.8320 0.4216 0.0841  0.3237  0.0116  194 ARG A NH2 
1609  N  N   . GLY A  195 ? 0.1260 0.1247 0.1018 -0.0065 0.0204  0.0377  195 GLY A N   
1610  C  CA  . GLY A  195 ? 0.1005 0.1608 0.1242 -0.0012 0.0181  0.0366  195 GLY A CA  
1611  C  C   . GLY A  195 ? 0.0888 0.1368 0.1328 -0.0154 0.0099  0.0494  195 GLY A C   
1612  O  O   . GLY A  195 ? 0.1003 0.1509 0.1437 -0.0089 0.0221  0.0688  195 GLY A O   
1613  N  N   . SER A  196 ? 0.0863 0.1213 0.1190 -0.0100 0.0129  0.0410  196 SER A N   
1614  C  CA  . SER A  196 ? 0.1005 0.1344 0.1301 -0.0137 0.0041  0.0443  196 SER A CA  
1615  C  C   . SER A  196 ? 0.0881 0.1212 0.1450 -0.0008 0.0115  0.0472  196 SER A C   
1616  O  O   . SER A  196 ? 0.0976 0.1188 0.1511 -0.0048 0.0115  0.0564  196 SER A O   
1617  C  CB  . SER A  196 ? 0.0836 0.1500 0.1384 -0.0017 -0.0017 0.0710  196 SER A CB  
1618  O  OG  . SER A  196 ? 0.0813 0.1191 0.1529 -0.0153 0.0063  0.0496  196 SER A OG  
1619  N  N   . LEU A  197 ? 0.1009 0.1326 0.1285 -0.0171 -0.0098 0.0518  197 LEU A N   
1620  C  CA  . LEU A  197 ? 0.0802 0.1159 0.1524 -0.0015 -0.0118 0.0373  197 LEU A CA  
1621  C  C   . LEU A  197 ? 0.0834 0.1046 0.1508 -0.0098 -0.0109 0.0410  197 LEU A C   
1622  O  O   . LEU A  197 ? 0.0899 0.1225 0.1337 -0.0137 -0.0031 0.0408  197 LEU A O   
1623  C  CB  . LEU A  197 ? 0.1170 0.1230 0.1779 -0.0313 0.0136  0.0368  197 LEU A CB  
1624  C  CG  . LEU A  197 ? 0.1308 0.1387 0.2630 -0.0416 -0.0198 0.0692  197 LEU A CG  
1625  C  CD1 . LEU A  197 ? 0.1762 0.2159 0.3262 -0.0222 0.0215  0.1150  197 LEU A CD1 
1626  C  CD2 . LEU A  197 ? 0.1854 0.2793 0.3346 -0.1106 -0.0006 -0.0253 197 LEU A CD2 
1627  N  N   . THR A  198 ? 0.0878 0.1163 0.1475 -0.0054 -0.0041 0.0405  198 THR A N   
1628  C  CA  . THR A  198 ? 0.0827 0.0982 0.1570 -0.0093 0.0225  0.0370  198 THR A CA  
1629  C  C   . THR A  198 ? 0.0974 0.0973 0.1502 -0.0038 -0.0094 0.0595  198 THR A C   
1630  O  O   . THR A  198 ? 0.0926 0.1176 0.1432 0.0026  0.0028  0.0287  198 THR A O   
1631  C  CB  . THR A  198 ? 0.1137 0.1005 0.1306 -0.0108 0.0020  0.0171  198 THR A CB  
1632  O  OG1 . THR A  198 ? 0.0850 0.1152 0.1347 -0.0035 0.0049  0.0355  198 THR A OG1 
1633  C  CG2 . THR A  198 ? 0.1296 0.0909 0.1246 -0.0197 0.0184  0.0228  198 THR A CG2 
1634  N  N   . THR A  199 ? 0.1454 0.1125 0.1344 -0.0303 -0.0125 0.0379  199 THR A N   
1635  C  CA  . THR A  199 ? 0.1967 0.1111 0.1459 -0.0303 -0.0097 0.0297  199 THR A CA  
1636  C  C   . THR A  199 ? 0.1427 0.1057 0.1632 -0.0287 -0.0163 0.0306  199 THR A C   
1637  O  O   . THR A  199 ? 0.1437 0.1254 0.1667 -0.0082 0.0017  0.0553  199 THR A O   
1638  C  CB  . THR A  199 ? 0.2316 0.1921 0.1540 0.0015  -0.0430 0.0675  199 THR A CB  
1639  O  OG1 . THR A  199 ? 0.1639 0.3544 0.2725 -0.0722 -0.0546 0.1551  199 THR A OG1 
1640  C  CG2 . THR A  199 ? 0.2809 0.1130 0.1899 -0.0234 -0.0483 0.0447  199 THR A CG2 
1641  N  N   . PRO A  200 ? 0.1249 0.1154 0.1659 -0.0383 -0.0266 0.0342  200 PRO A N   
1642  C  CA  . PRO A  200 ? 0.1265 0.1100 0.1741 -0.0274 -0.0005 0.0313  200 PRO A CA  
1643  C  C   . PRO A  200 ? 0.1387 0.0985 0.2030 -0.0282 -0.0295 0.0520  200 PRO A C   
1644  O  O   . PRO A  200 ? 0.1416 0.1480 0.2326 -0.0207 -0.0467 0.0658  200 PRO A O   
1645  C  CB  . PRO A  200 ? 0.1474 0.1407 0.1714 -0.0227 -0.0065 0.0379  200 PRO A CB  
1646  C  CG  . PRO A  200 ? 0.1391 0.1441 0.1879 -0.0303 -0.0007 0.0120  200 PRO A CG  
1647  C  CD  . PRO A  200 ? 0.1499 0.1418 0.1838 -0.0186 -0.0052 0.0230  200 PRO A CD  
1648  N  N   . PRO A  201 ? 0.1215 0.1143 0.2025 -0.0313 -0.0274 0.0564  201 PRO A N   
1649  C  CA  . PRO A  201 ? 0.1190 0.1142 0.1938 -0.0167 -0.0093 0.0627  201 PRO A CA  
1650  C  C   . PRO A  201 ? 0.1305 0.1008 0.1809 -0.0306 -0.0137 0.0529  201 PRO A C   
1651  O  O   . PRO A  201 ? 0.1242 0.1152 0.2210 -0.0206 -0.0030 0.0724  201 PRO A O   
1652  C  CB  . PRO A  201 ? 0.1261 0.1161 0.2809 -0.0463 -0.0164 0.0720  201 PRO A CB  
1653  C  CG  . PRO A  201 ? 0.1595 0.1938 0.2933 -0.0741 -0.0401 0.1010  201 PRO A CG  
1654  C  CD  . PRO A  201 ? 0.1045 0.1398 0.2818 -0.0247 -0.0211 0.0518  201 PRO A CD  
1655  N  N   . CYS A  202 ? 0.1023 0.1061 0.1899 -0.0086 -0.0068 0.0439  202 CYS A N   
1656  C  CA  . CYS A  202 ? 0.0891 0.1384 0.1504 -0.0049 0.0008  0.0408  202 CYS A CA  
1657  C  C   . CYS A  202 ? 0.0847 0.1055 0.1676 0.0049  0.0000  0.0329  202 CYS A C   
1658  O  O   . CYS A  202 ? 0.1040 0.1199 0.1599 -0.0164 0.0024  0.0549  202 CYS A O   
1659  C  CB  . CYS A  202 ? 0.0978 0.1337 0.1576 -0.0005 0.0041  0.0480  202 CYS A CB  
1660  S  SG  . CYS A  202 ? 0.1055 0.1208 0.1705 -0.0130 -0.0017 0.0452  202 CYS A SG  
1661  N  N   . ASN A  203 ? 0.0920 0.1263 0.1726 -0.0160 0.0131  0.0626  203 ASN A N   
1662  C  CA  . ASN A  203 ? 0.1136 0.1414 0.1972 -0.0280 0.0147  0.0771  203 ASN A CA  
1663  C  C   . ASN A  203 ? 0.1093 0.1229 0.1904 -0.0344 0.0274  0.0645  203 ASN A C   
1664  O  O   . ASN A  203 ? 0.0969 0.1235 0.1680 -0.0186 0.0154  0.0548  203 ASN A O   
1665  C  CB  . ASN A  203 ? 0.1107 0.1614 0.2454 -0.0417 0.0121  0.0412  203 ASN A CB  
1666  C  CG  . ASN A  203 ? 0.1511 0.2062 0.2309 -0.0828 0.0032  0.0953  203 ASN A CG  
1667  O  OD1 . ASN A  203 ? 0.1726 0.1653 0.2624 -0.0359 -0.0001 0.0255  203 ASN A OD1 
1668  N  ND2 . ASN A  203 ? 0.2183 0.1795 0.3332 -0.0529 0.0120  0.0780  203 ASN A ND2 
1669  N  N   . PRO A  204 ? 0.1042 0.1371 0.1777 -0.0196 0.0193  0.0597  204 PRO A N   
1670  C  CA  . PRO A  204 ? 0.1102 0.1520 0.1797 -0.0088 0.0080  0.0741  204 PRO A CA  
1671  C  C   . PRO A  204 ? 0.1091 0.1446 0.1595 -0.0285 0.0124  0.0702  204 PRO A C   
1672  O  O   . PRO A  204 ? 0.1540 0.2100 0.1533 -0.0021 0.0149  0.0703  204 PRO A O   
1673  C  CB  . PRO A  204 ? 0.1272 0.1784 0.1791 -0.0085 -0.0077 0.0983  204 PRO A CB  
1674  C  CG  . PRO A  204 ? 0.1529 0.1991 0.2157 0.0185  0.0176  0.0957  204 PRO A CG  
1675  C  CD  . PRO A  204 ? 0.1775 0.1430 0.2039 -0.0059 -0.0102 0.0953  204 PRO A CD  
1676  N  N   . THR A  205 ? 0.0970 0.1545 0.1948 -0.0118 0.0020  0.0762  205 THR A N   
1677  C  CA  . THR A  205 ? 0.0818 0.1827 0.1947 -0.0114 0.0144  0.0790  205 THR A CA  
1678  C  C   . THR A  205 ? 0.0942 0.1865 0.1701 -0.0166 0.0055  0.0706  205 THR A C   
1679  O  O   . THR A  205 ? 0.0951 0.1920 0.2019 -0.0173 0.0216  0.0890  205 THR A O   
1680  C  CB  . THR A  205 ? 0.1188 0.1650 0.2203 -0.0273 0.0147  0.0983  205 THR A CB  
1681  O  OG1 . THR A  205 ? 0.1299 0.1671 0.2090 -0.0265 0.0102  0.0715  205 THR A OG1 
1682  C  CG2 . THR A  205 ? 0.1353 0.1660 0.2973 -0.0168 0.0094  0.0891  205 THR A CG2 
1683  N  N   . VAL A  206 ? 0.1042 0.1439 0.1567 -0.0048 0.0247  0.0623  206 VAL A N   
1684  C  CA  . VAL A  206 ? 0.1080 0.1414 0.1473 -0.0015 0.0186  0.0559  206 VAL A CA  
1685  C  C   . VAL A  206 ? 0.1084 0.1504 0.1401 -0.0148 0.0160  0.0640  206 VAL A C   
1686  O  O   . VAL A  206 ? 0.1085 0.1671 0.1676 -0.0026 -0.0057 0.0487  206 VAL A O   
1687  C  CB  . VAL A  206 ? 0.1125 0.1357 0.1502 -0.0110 0.0291  0.0656  206 VAL A CB  
1688  C  CG1 . VAL A  206 ? 0.0953 0.1692 0.1511 -0.0130 0.0148  0.0697  206 VAL A CG1 
1689  C  CG2 . VAL A  206 ? 0.1143 0.1398 0.1644 -0.0271 0.0179  0.0288  206 VAL A CG2 
1690  N  N   . LEU A  207 ? 0.1100 0.1396 0.1448 -0.0175 0.0265  0.0740  207 LEU A N   
1691  C  CA  . LEU A  207 ? 0.1234 0.1535 0.1434 -0.0109 0.0461  0.0500  207 LEU A CA  
1692  C  C   . LEU A  207 ? 0.1080 0.1398 0.0983 0.0000  0.0255  0.0229  207 LEU A C   
1693  O  O   . LEU A  207 ? 0.1075 0.1523 0.1212 -0.0109 0.0062  0.0370  207 LEU A O   
1694  C  CB  . LEU A  207 ? 0.1675 0.1951 0.1376 0.0087  0.0498  0.0516  207 LEU A CB  
1695  C  CG  . LEU A  207 ? 0.2402 0.2440 0.1633 0.0496  0.0179  0.0088  207 LEU A CG  
1696  C  CD1 . LEU A  207 ? 0.2908 0.3440 0.2044 0.0507  -0.0132 0.0362  207 LEU A CD1 
1697  C  CD2 . LEU A  207 ? 0.1509 0.3621 0.4900 0.0195  0.0379  -0.0062 207 LEU A CD2 
1698  N  N   . TRP A  208 ? 0.1062 0.1272 0.1036 -0.0098 0.0186  0.0320  208 TRP A N   
1699  C  CA  . TRP A  208 ? 0.0906 0.1125 0.1168 0.0027  0.0087  0.0359  208 TRP A CA  
1700  C  C   . TRP A  208 ? 0.1154 0.1145 0.0863 -0.0063 0.0271  0.0203  208 TRP A C   
1701  O  O   . TRP A  208 ? 0.1181 0.1576 0.1012 -0.0046 0.0148  0.0179  208 TRP A O   
1702  C  CB  . TRP A  208 ? 0.0931 0.1033 0.1409 -0.0013 0.0210  0.0423  208 TRP A CB  
1703  C  CG  . TRP A  208 ? 0.0836 0.1337 0.1213 0.0099  0.0092  0.0355  208 TRP A CG  
1704  C  CD1 . TRP A  208 ? 0.1021 0.1490 0.1102 0.0091  0.0211  0.0485  208 TRP A CD1 
1705  C  CD2 . TRP A  208 ? 0.0775 0.1235 0.1182 -0.0137 0.0137  0.0381  208 TRP A CD2 
1706  N  NE1 . TRP A  208 ? 0.1040 0.1461 0.1222 -0.0007 0.0160  0.0579  208 TRP A NE1 
1707  C  CE2 . TRP A  208 ? 0.0757 0.1204 0.1147 -0.0107 0.0189  0.0350  208 TRP A CE2 
1708  C  CE3 . TRP A  208 ? 0.0803 0.1412 0.1030 -0.0057 0.0199  0.0472  208 TRP A CE3 
1709  C  CZ2 . TRP A  208 ? 0.0822 0.1420 0.1200 -0.0102 0.0155  0.0414  208 TRP A CZ2 
1710  C  CZ3 . TRP A  208 ? 0.1046 0.1127 0.1154 -0.0006 0.0184  0.0241  208 TRP A CZ3 
1711  C  CH2 . TRP A  208 ? 0.1032 0.1254 0.1115 -0.0205 0.0175  0.0372  208 TRP A CH2 
1712  N  N   . THR A  209 ? 0.0854 0.1215 0.0991 -0.0001 0.0162  0.0196  209 THR A N   
1713  C  CA  . THR A  209 ? 0.1055 0.1188 0.1001 -0.0007 0.0361  0.0144  209 THR A CA  
1714  C  C   . THR A  209 ? 0.1055 0.1179 0.0885 0.0019  0.0197  0.0126  209 THR A C   
1715  O  O   . THR A  209 ? 0.1278 0.1516 0.0965 -0.0252 0.0148  0.0179  209 THR A O   
1716  C  CB  . THR A  209 ? 0.0962 0.1378 0.1116 -0.0026 0.0207  0.0164  209 THR A CB  
1717  O  OG1 . THR A  209 ? 0.1208 0.1787 0.1133 0.0026  0.0436  0.0190  209 THR A OG1 
1718  C  CG2 . THR A  209 ? 0.1109 0.1276 0.1506 0.0129  0.0302  -0.0028 209 THR A CG2 
1719  N  N   . VAL A  210 ? 0.0892 0.1288 0.0908 -0.0068 0.0280  0.0250  210 VAL A N   
1720  C  CA  . VAL A  210 ? 0.0926 0.1186 0.0865 0.0037  0.0242  0.0137  210 VAL A CA  
1721  C  C   . VAL A  210 ? 0.0996 0.1105 0.0964 -0.0003 0.0200  0.0127  210 VAL A C   
1722  O  O   . VAL A  210 ? 0.1274 0.1386 0.0816 -0.0006 0.0302  0.0003  210 VAL A O   
1723  C  CB  . VAL A  210 ? 0.1000 0.1150 0.1231 -0.0008 0.0254  0.0221  210 VAL A CB  
1724  C  CG1 . VAL A  210 ? 0.1127 0.1437 0.1028 -0.0006 0.0454  0.0010  210 VAL A CG1 
1725  C  CG2 . VAL A  210 ? 0.1116 0.1188 0.1385 0.0043  0.0038  0.0140  210 VAL A CG2 
1726  N  N   . PHE A  211 ? 0.1003 0.1073 0.1015 0.0073  0.0167  0.0163  211 PHE A N   
1727  C  CA  . PHE A  211 ? 0.1249 0.1120 0.1005 0.0103  0.0262  0.0099  211 PHE A CA  
1728  C  C   . PHE A  211 ? 0.1141 0.1204 0.1168 -0.0015 0.0337  0.0118  211 PHE A C   
1729  O  O   . PHE A  211 ? 0.1240 0.1208 0.1138 -0.0052 0.0215  0.0021  211 PHE A O   
1730  C  CB  . PHE A  211 ? 0.1208 0.1337 0.0954 0.0243  0.0242  0.0167  211 PHE A CB  
1731  C  CG  . PHE A  211 ? 0.1093 0.1378 0.1161 0.0099  0.0220  0.0007  211 PHE A CG  
1732  C  CD1 . PHE A  211 ? 0.1143 0.1481 0.1385 0.0204  0.0342  0.0152  211 PHE A CD1 
1733  C  CD2 . PHE A  211 ? 0.1249 0.1107 0.1314 0.0126  0.0035  0.0221  211 PHE A CD2 
1734  C  CE1 . PHE A  211 ? 0.1134 0.1913 0.1709 0.0071  0.0133  0.0222  211 PHE A CE1 
1735  C  CE2 . PHE A  211 ? 0.1330 0.1200 0.1328 0.0031  0.0054  0.0223  211 PHE A CE2 
1736  C  CZ  . PHE A  211 ? 0.1213 0.1868 0.1477 0.0197  0.0182  0.0251  211 PHE A CZ  
1737  N  N   . ARG A  212 ? 0.1326 0.1163 0.1120 -0.0024 0.0244  0.0001  212 ARG A N   
1738  C  CA  . ARG A  212 ? 0.1296 0.1023 0.1254 -0.0057 0.0248  -0.0031 212 ARG A CA  
1739  C  C   . ARG A  212 ? 0.1359 0.1184 0.1140 -0.0111 0.0419  -0.0046 212 ARG A C   
1740  O  O   . ARG A  212 ? 0.1502 0.1369 0.1455 -0.0142 0.0458  0.0074  212 ARG A O   
1741  C  CB  . ARG A  212 ? 0.1653 0.1378 0.1010 -0.0254 0.0225  -0.0122 212 ARG A CB  
1742  C  CG  . ARG A  212 ? 0.1933 0.1675 0.1502 -0.0542 0.0081  -0.0209 212 ARG A CG  
1743  C  CD  . ARG A  212 ? 0.2409 0.1888 0.1969 -0.0712 0.0612  -0.0670 212 ARG A CD  
1744  N  NE  . ARG A  212 ? 0.3398 0.3077 0.2481 -0.1733 0.0520  -0.1040 212 ARG A NE  
1745  C  CZ  . ARG A  212 ? 0.5566 0.3093 0.3064 -0.2185 0.1050  -0.0738 212 ARG A CZ  
1746  N  NH1 . ARG A  212 ? 0.4887 0.2524 0.3190 -0.1058 0.0627  0.0296  212 ARG A NH1 
1747  N  NH2 . ARG A  212 ? 0.5537 0.3136 0.5885 -0.2274 0.1552  -0.1341 212 ARG A NH2 
1748  N  N   . ASN A  213 ? 0.1605 0.1061 0.1106 0.0013  0.0198  0.0113  213 ASN A N   
1749  C  CA  . ASN A  213 ? 0.1994 0.1006 0.1307 0.0149  0.0183  0.0086  213 ASN A CA  
1750  C  C   . ASN A  213 ? 0.1435 0.1109 0.1268 0.0012  0.0287  0.0133  213 ASN A C   
1751  O  O   . ASN A  213 ? 0.1464 0.1138 0.1213 -0.0021 0.0206  0.0121  213 ASN A O   
1752  C  CB  . ASN A  213 ? 0.2177 0.0985 0.1482 0.0252  0.0408  0.0181  213 ASN A CB  
1753  C  CG  . ASN A  213 ? 0.2165 0.1324 0.2100 0.0104  0.0597  -0.0215 213 ASN A CG  
1754  O  OD1 . ASN A  213 ? 0.2976 0.1689 0.2380 -0.0035 0.1061  -0.0427 213 ASN A OD1 
1755  N  ND2 . ASN A  213 ? 0.2276 0.1347 0.1985 -0.0005 0.0649  -0.0485 213 ASN A ND2 
1756  N  N   . PRO A  214 ? 0.1493 0.1114 0.1203 0.0023  0.0333  0.0097  214 PRO A N   
1757  C  CA  . PRO A  214 ? 0.1444 0.1155 0.1233 0.0300  0.0251  0.0087  214 PRO A CA  
1758  C  C   . PRO A  214 ? 0.1268 0.1107 0.1222 0.0215  0.0366  0.0070  214 PRO A C   
1759  O  O   . PRO A  214 ? 0.1741 0.1310 0.1435 0.0395  0.0282  0.0237  214 PRO A O   
1760  C  CB  . PRO A  214 ? 0.1333 0.1263 0.1766 0.0094  0.0287  0.0218  214 PRO A CB  
1761  C  CG  . PRO A  214 ? 0.1791 0.1631 0.1611 -0.0211 0.0425  -0.0096 214 PRO A CG  
1762  C  CD  . PRO A  214 ? 0.1736 0.1443 0.1924 -0.0340 0.0886  0.0043  214 PRO A CD  
1763  N  N   . VAL A  215 ? 0.1493 0.1191 0.1050 0.0102  0.0287  0.0119  215 VAL A N   
1764  C  CA  . VAL A  215 ? 0.1502 0.1263 0.1073 0.0311  0.0326  0.0335  215 VAL A CA  
1765  C  C   . VAL A  215 ? 0.1253 0.1218 0.1355 0.0326  0.0328  0.0401  215 VAL A C   
1766  O  O   . VAL A  215 ? 0.1247 0.1450 0.1456 0.0353  0.0362  0.0496  215 VAL A O   
1767  C  CB  . VAL A  215 ? 0.1362 0.1333 0.1341 0.0346  0.0307  0.0322  215 VAL A CB  
1768  C  CG1 . VAL A  215 ? 0.1435 0.1499 0.1373 0.0322  0.0397  0.0421  215 VAL A CG1 
1769  C  CG2 . VAL A  215 ? 0.1572 0.1221 0.1369 0.0200  0.0162  0.0353  215 VAL A CG2 
1770  N  N   A GLN A  216 ? 0.1127 0.1513 0.1263 0.0251  0.0331  0.0443  216 GLN A N   
1771  N  N   B GLN A  216 ? 0.1545 0.0809 0.1471 0.0430  0.0553  0.0441  216 GLN A N   
1772  C  CA  A GLN A  216 ? 0.1364 0.1371 0.1222 -0.0098 0.0324  0.0614  216 GLN A CA  
1773  C  CA  B GLN A  216 ? 0.1240 0.1240 0.1457 0.0303  0.0513  0.0368  216 GLN A CA  
1774  C  C   A GLN A  216 ? 0.1294 0.1718 0.1030 0.0273  0.0476  0.0562  216 GLN A C   
1775  C  C   B GLN A  216 ? 0.1177 0.1638 0.1341 0.0377  0.0509  0.0511  216 GLN A C   
1776  O  O   A GLN A  216 ? 0.1358 0.1583 0.1599 -0.0082 0.0372  0.0153  216 GLN A O   
1777  O  O   B GLN A  216 ? 0.1206 0.1374 0.1272 0.0361  0.0244  0.0176  216 GLN A O   
1778  C  CB  A GLN A  216 ? 0.2091 0.1249 0.2093 -0.0482 -0.0284 0.0322  216 GLN A CB  
1779  C  CB  B GLN A  216 ? 0.1750 0.1420 0.1118 -0.0017 0.0808  0.0632  216 GLN A CB  
1780  C  CG  A GLN A  216 ? 0.2461 0.1463 0.1910 -0.0716 -0.0197 0.0187  216 GLN A CG  
1781  C  CG  B GLN A  216 ? 0.1948 0.1407 0.1448 0.0296  0.0324  0.0511  216 GLN A CG  
1782  C  CD  A GLN A  216 ? 0.3192 0.1317 0.1298 -0.0399 0.0194  0.0188  216 GLN A CD  
1783  C  CD  B GLN A  216 ? 0.1969 0.1136 0.1838 0.0373  0.0489  0.0421  216 GLN A CD  
1784  O  OE1 A GLN A  216 ? 0.2635 0.1632 0.2395 0.0276  0.0306  0.0828  216 GLN A OE1 
1785  O  OE1 B GLN A  216 ? 0.2222 0.1782 0.1942 0.0715  0.0500  0.0284  216 GLN A OE1 
1786  N  NE2 A GLN A  216 ? 0.4514 0.2461 0.2371 -0.1571 -0.0313 0.0860  216 GLN A NE2 
1787  N  NE2 B GLN A  216 ? 0.2881 0.1441 0.2479 0.0197  -0.0293 0.0745  216 GLN A NE2 
1788  N  N   . ILE A  217 ? 0.1580 0.1541 0.1164 0.0381  0.0544  0.0452  217 ILE A N   
1789  C  CA  . ILE A  217 ? 0.1726 0.1718 0.1041 0.0405  0.0595  0.0557  217 ILE A CA  
1790  C  C   . ILE A  217 ? 0.1468 0.1675 0.1508 0.0551  0.0467  0.0715  217 ILE A C   
1791  O  O   . ILE A  217 ? 0.1475 0.1762 0.1396 0.0425  0.0566  0.0566  217 ILE A O   
1792  C  CB  . ILE A  217 ? 0.1335 0.1694 0.1344 0.0251  0.0344  0.0597  217 ILE A CB  
1793  C  CG1 . ILE A  217 ? 0.1385 0.1461 0.1261 0.0297  0.0406  0.0513  217 ILE A CG1 
1794  C  CG2 . ILE A  217 ? 0.1879 0.1506 0.1425 0.0538  0.0671  0.0608  217 ILE A CG2 
1795  C  CD1 . ILE A  217 ? 0.1540 0.1764 0.1064 0.0377  0.0372  0.0421  217 ILE A CD1 
1796  N  N   . SER A  218 ? 0.1633 0.1596 0.1206 0.0283  0.0483  0.0575  218 SER A N   
1797  C  CA  . SER A  218 ? 0.1465 0.2039 0.1396 0.0263  0.0531  0.0756  218 SER A CA  
1798  C  C   . SER A  218 ? 0.1814 0.1669 0.1215 0.0234  0.0630  0.0509  218 SER A C   
1799  O  O   . SER A  218 ? 0.1452 0.1621 0.1377 0.0237  0.0483  0.0529  218 SER A O   
1800  C  CB  . SER A  218 ? 0.2154 0.1975 0.1525 0.0222  0.0348  0.0850  218 SER A CB  
1801  O  OG  . SER A  218 ? 0.2222 0.1953 0.1371 0.0671  0.0507  0.0614  218 SER A OG  
1802  N  N   A GLN A  219 ? 0.2118 0.1746 0.1732 0.0414  0.1037  0.0701  219 GLN A N   
1803  N  N   B GLN A  219 ? 0.2132 0.1745 0.1707 0.0403  0.1026  0.0728  219 GLN A N   
1804  C  CA  A GLN A  219 ? 0.1678 0.1761 0.1748 0.0190  0.0788  0.0557  219 GLN A CA  
1805  C  CA  B GLN A  219 ? 0.1725 0.1781 0.1967 0.0285  0.0665  0.0428  219 GLN A CA  
1806  C  C   A GLN A  219 ? 0.1509 0.2109 0.1680 0.0282  0.0671  0.0579  219 GLN A C   
1807  C  C   B GLN A  219 ? 0.1504 0.2116 0.1678 0.0275  0.0650  0.0581  219 GLN A C   
1808  O  O   A GLN A  219 ? 0.1493 0.1890 0.1481 0.0166  0.0544  0.0346  219 GLN A O   
1809  O  O   B GLN A  219 ? 0.1495 0.1887 0.1484 0.0129  0.0562  0.0340  219 GLN A O   
1810  C  CB  A GLN A  219 ? 0.2275 0.2398 0.2086 -0.0260 0.1746  0.0010  219 GLN A CB  
1811  C  CB  B GLN A  219 ? 0.2305 0.2240 0.2795 -0.0813 0.1141  -0.0052 219 GLN A CB  
1812  C  CG  A GLN A  219 ? 0.3337 0.2897 0.3036 0.0747  0.1553  0.0825  219 GLN A CG  
1813  C  CG  B GLN A  219 ? 0.1439 0.3625 0.4555 -0.0544 0.1492  0.0141  219 GLN A CG  
1814  C  CD  A GLN A  219 ? 0.3941 0.3111 0.3497 0.0794  0.2397  0.1450  219 GLN A CD  
1815  C  CD  B GLN A  219 ? 0.4612 0.2833 0.4214 0.0500  0.0494  0.2144  219 GLN A CD  
1816  O  OE1 A GLN A  219 ? 0.4192 0.4237 0.5710 -0.0329 0.1561  0.2757  219 GLN A OE1 
1817  O  OE1 B GLN A  219 ? 0.4036 0.5731 0.7006 -0.0667 0.2026  0.4199  219 GLN A OE1 
1818  N  NE2 A GLN A  219 ? 0.8106 0.2865 0.3558 0.1849  0.2131  0.1168  219 GLN A NE2 
1819  N  NE2 B GLN A  219 ? 0.4029 0.2354 0.0872 0.2187  0.1234  0.0732  219 GLN A NE2 
1820  N  N   . GLU A  220 ? 0.1667 0.2046 0.1351 0.0253  0.0571  0.0606  220 GLU A N   
1821  C  CA  . GLU A  220 ? 0.2064 0.1929 0.1423 0.0260  0.0324  0.0628  220 GLU A CA  
1822  C  C   . GLU A  220 ? 0.1782 0.2063 0.1100 0.0208  0.0318  0.0542  220 GLU A C   
1823  O  O   . GLU A  220 ? 0.1793 0.2048 0.1152 0.0229  0.0397  0.0401  220 GLU A O   
1824  C  CB  . GLU A  220 ? 0.2608 0.3425 0.1330 0.0913  0.0680  0.1359  220 GLU A CB  
1825  C  CG  . GLU A  220 ? 0.3091 0.2863 0.1811 0.0728  0.0894  0.1058  220 GLU A CG  
1826  C  CD  . GLU A  220 ? 0.5205 0.3603 0.1852 0.0303  0.1027  0.1474  220 GLU A CD  
1827  O  OE1 . GLU A  220 ? 0.3082 0.2858 0.2272 0.0546  0.0640  0.1163  220 GLU A OE1 
1828  O  OE2 . GLU A  220 ? 0.4526 0.3752 0.3061 0.0918  0.1423  0.1312  220 GLU A OE2 
1829  N  N   . GLN A  221 ? 0.1471 0.2016 0.1134 0.0384  0.0368  0.0417  221 GLN A N   
1830  C  CA  . GLN A  221 ? 0.1623 0.1705 0.1062 0.0377  0.0379  0.0410  221 GLN A CA  
1831  C  C   . GLN A  221 ? 0.1421 0.1863 0.1158 0.0115  0.0432  0.0377  221 GLN A C   
1832  O  O   . GLN A  221 ? 0.1475 0.1840 0.1085 0.0192  0.0187  0.0357  221 GLN A O   
1833  C  CB  . GLN A  221 ? 0.1475 0.1990 0.1017 0.0533  0.0373  0.0329  221 GLN A CB  
1834  C  CG  . GLN A  221 ? 0.1685 0.2253 0.1362 0.0657  0.0456  0.0553  221 GLN A CG  
1835  C  CD  . GLN A  221 ? 0.1629 0.2231 0.1010 0.0410  0.0264  0.0516  221 GLN A CD  
1836  O  OE1 . GLN A  221 ? 0.1531 0.2098 0.1228 0.0603  0.0315  0.0505  221 GLN A OE1 
1837  N  NE2 . GLN A  221 ? 0.1668 0.2120 0.1590 0.0337  0.0410  0.0456  221 GLN A NE2 
1838  N  N   . LEU A  222 ? 0.1296 0.1823 0.1121 0.0198  0.0463  0.0450  222 LEU A N   
1839  C  CA  . LEU A  222 ? 0.1518 0.1743 0.1075 0.0231  0.0288  0.0375  222 LEU A CA  
1840  C  C   . LEU A  222 ? 0.1086 0.1863 0.1143 0.0170  0.0275  0.0379  222 LEU A C   
1841  O  O   . LEU A  222 ? 0.1351 0.1759 0.1082 0.0249  0.0260  0.0198  222 LEU A O   
1842  C  CB  . LEU A  222 ? 0.1522 0.1504 0.1106 0.0153  0.0346  0.0472  222 LEU A CB  
1843  C  CG  . LEU A  222 ? 0.1301 0.1535 0.1222 0.0048  0.0230  0.0196  222 LEU A CG  
1844  C  CD1 . LEU A  222 ? 0.1635 0.1407 0.1199 0.0104  0.0200  0.0310  222 LEU A CD1 
1845  C  CD2 . LEU A  222 ? 0.1441 0.2267 0.1307 -0.0129 0.0350  0.0469  222 LEU A CD2 
1846  N  N   . LEU A  223 ? 0.1482 0.1942 0.1001 0.0313  0.0417  0.0232  223 LEU A N   
1847  C  CA  . LEU A  223 ? 0.1622 0.1730 0.1094 0.0035  0.0383  0.0318  223 LEU A CA  
1848  C  C   . LEU A  223 ? 0.1768 0.1730 0.0978 0.0092  0.0346  0.0129  223 LEU A C   
1849  O  O   . LEU A  223 ? 0.1814 0.1723 0.1190 0.0052  0.0339  0.0071  223 LEU A O   
1850  C  CB  . LEU A  223 ? 0.1660 0.2179 0.1103 0.0359  0.0465  0.0474  223 LEU A CB  
1851  C  CG  . LEU A  223 ? 0.1953 0.2424 0.1310 0.0507  0.0478  0.0307  223 LEU A CG  
1852  C  CD1 . LEU A  223 ? 0.1748 0.2421 0.1975 0.0652  0.0905  0.0649  223 LEU A CD1 
1853  C  CD2 . LEU A  223 ? 0.2427 0.2996 0.1671 0.0445  0.0984  0.0890  223 LEU A CD2 
1854  N  N   . ALA A  224 ? 0.1331 0.2364 0.1070 0.0078  0.0120  0.0151  224 ALA A N   
1855  C  CA  . ALA A  224 ? 0.1775 0.1982 0.1484 0.0136  0.0052  0.0166  224 ALA A CA  
1856  C  C   . ALA A  224 ? 0.1579 0.2003 0.1430 -0.0115 -0.0044 0.0131  224 ALA A C   
1857  O  O   . ALA A  224 ? 0.1804 0.2117 0.1553 -0.0140 0.0159  -0.0131 224 ALA A O   
1858  C  CB  . ALA A  224 ? 0.1960 0.2290 0.1474 0.0337  -0.0226 0.0273  224 ALA A CB  
1859  N  N   . LEU A  225 ? 0.1553 0.1906 0.1226 0.0091  0.0125  0.0120  225 LEU A N   
1860  C  CA  . LEU A  225 ? 0.1380 0.1791 0.1432 -0.0003 0.0185  0.0225  225 LEU A CA  
1861  C  C   . LEU A  225 ? 0.1446 0.1610 0.1587 -0.0021 0.0513  0.0168  225 LEU A C   
1862  O  O   . LEU A  225 ? 0.1604 0.1682 0.1969 0.0017  0.0337  -0.0148 225 LEU A O   
1863  C  CB  . LEU A  225 ? 0.1480 0.1775 0.1042 0.0152  0.0164  0.0110  225 LEU A CB  
1864  C  CG  . LEU A  225 ? 0.1448 0.1662 0.1416 0.0102  0.0229  0.0542  225 LEU A CG  
1865  C  CD1 . LEU A  225 ? 0.1482 0.1793 0.2190 -0.0076 0.0184  0.0540  225 LEU A CD1 
1866  C  CD2 . LEU A  225 ? 0.1980 0.1809 0.1112 0.0313  0.0322  0.0176  225 LEU A CD2 
1867  N  N   . GLU A  226 ? 0.1313 0.1511 0.1240 0.0046  0.0184  0.0130  226 GLU A N   
1868  C  CA  . GLU A  226 ? 0.1430 0.1608 0.1349 -0.0019 0.0324  0.0008  226 GLU A CA  
1869  C  C   . GLU A  226 ? 0.1747 0.1597 0.1410 0.0152  0.0088  0.0241  226 GLU A C   
1870  O  O   . GLU A  226 ? 0.2003 0.1787 0.1743 0.0329  -0.0063 -0.0233 226 GLU A O   
1871  C  CB  . GLU A  226 ? 0.1315 0.1641 0.1127 0.0071  0.0300  0.0030  226 GLU A CB  
1872  C  CG  . GLU A  226 ? 0.1401 0.1689 0.1280 -0.0065 0.0329  0.0193  226 GLU A CG  
1873  C  CD  . GLU A  226 ? 0.1267 0.1867 0.1021 0.0021  0.0245  0.0187  226 GLU A CD  
1874  O  OE1 . GLU A  226 ? 0.1513 0.2099 0.1055 -0.0153 0.0357  0.0392  226 GLU A OE1 
1875  O  OE2 . GLU A  226 ? 0.1572 0.1793 0.1137 -0.0192 0.0244  0.0348  226 GLU A OE2 
1876  N  N   . THR A  227 ? 0.1595 0.1881 0.1193 -0.0052 0.0243  0.0046  227 THR A N   
1877  C  CA  . THR A  227 ? 0.2336 0.1723 0.1068 -0.0171 0.0355  -0.0142 227 THR A CA  
1878  C  C   . THR A  227 ? 0.1935 0.2375 0.1086 -0.0105 0.0071  -0.0077 227 THR A C   
1879  O  O   . THR A  227 ? 0.2552 0.3212 0.1386 -0.0705 0.0628  -0.0668 227 THR A O   
1880  C  CB  . THR A  227 ? 0.2011 0.1842 0.1585 0.0170  0.0535  -0.0013 227 THR A CB  
1881  O  OG1 . THR A  227 ? 0.2055 0.2343 0.1272 0.0030  0.0516  -0.0017 227 THR A OG1 
1882  C  CG2 . THR A  227 ? 0.2583 0.2167 0.1826 -0.0502 0.0684  -0.0216 227 THR A CG2 
1883  N  N   . ALA A  228 ? 0.1899 0.2111 0.1332 -0.0087 0.0223  0.0153  228 ALA A N   
1884  C  CA  . ALA A  228 ? 0.2098 0.2073 0.1484 -0.0472 0.0031  -0.0091 228 ALA A CA  
1885  C  C   . ALA A  228 ? 0.1876 0.2318 0.1305 -0.0146 -0.0003 -0.0351 228 ALA A C   
1886  O  O   . ALA A  228 ? 0.2117 0.2398 0.1608 -0.0082 -0.0203 -0.0212 228 ALA A O   
1887  C  CB  . ALA A  228 ? 0.1773 0.2276 0.2885 -0.0013 -0.0063 -0.0410 228 ALA A CB  
1888  N  N   . LEU A  229 ? 0.1888 0.1673 0.1351 -0.0062 0.0131  -0.0210 229 LEU A N   
1889  C  CA  . LEU A  229 ? 0.1888 0.1863 0.1481 0.0156  0.0110  -0.0168 229 LEU A CA  
1890  C  C   . LEU A  229 ? 0.1611 0.2142 0.1356 -0.0054 0.0147  -0.0571 229 LEU A C   
1891  O  O   . LEU A  229 ? 0.1489 0.1960 0.1678 -0.0192 0.0020  -0.0275 229 LEU A O   
1892  C  CB  . LEU A  229 ? 0.1895 0.1932 0.1622 0.0082  0.0131  0.0068  229 LEU A CB  
1893  C  CG  . LEU A  229 ? 0.1504 0.2380 0.1513 0.0220  0.0324  -0.0241 229 LEU A CG  
1894  C  CD1 . LEU A  229 ? 0.1940 0.3388 0.1615 0.0546  0.0335  0.0222  229 LEU A CD1 
1895  C  CD2 . LEU A  229 ? 0.1678 0.2768 0.2371 -0.0104 -0.0107 -0.0244 229 LEU A CD2 
1896  N  N   . TYR A  230 ? 0.1789 0.1982 0.1859 -0.0083 0.0021  -0.0722 230 TYR A N   
1897  C  CA  . TYR A  230 ? 0.2211 0.1675 0.1685 -0.0019 0.0234  -0.0533 230 TYR A CA  
1898  C  C   . TYR A  230 ? 0.1752 0.2054 0.1874 -0.0241 0.0195  -0.0423 230 TYR A C   
1899  O  O   . TYR A  230 ? 0.1712 0.2321 0.1982 -0.0043 0.0287  -0.0383 230 TYR A O   
1900  C  CB  . TYR A  230 ? 0.2089 0.1984 0.1782 -0.0028 0.0208  -0.0573 230 TYR A CB  
1901  C  CG  . TYR A  230 ? 0.2073 0.2921 0.1793 0.0276  0.0194  -0.0225 230 TYR A CG  
1902  C  CD1 . TYR A  230 ? 0.3722 0.3298 0.2081 0.0614  0.0333  0.0216  230 TYR A CD1 
1903  C  CD2 . TYR A  230 ? 0.2154 0.3795 0.3427 0.0581  0.0767  0.0939  230 TYR A CD2 
1904  C  CE1 . TYR A  230 ? 0.4271 0.4490 0.2852 0.0529  0.1159  0.0790  230 TYR A CE1 
1905  C  CE2 . TYR A  230 ? 0.3018 0.4047 0.3382 0.0758  0.1324  0.0337  230 TYR A CE2 
1906  C  CZ  . TYR A  230 ? 0.2804 0.4609 0.5152 -0.0226 0.1367  0.2423  230 TYR A CZ  
1907  O  OH  . TYR A  230 ? 0.5261 0.6855 0.3849 0.0375  0.0976  0.2829  230 TYR A OH  
1908  N  N   A CYS A  231 ? 0.2217 0.2284 0.1226 0.0250  0.0231  -0.0794 231 CYS A N   
1909  N  N   B CYS A  231 ? 0.2527 0.2387 0.2075 0.0003  -0.0048 -0.0057 231 CYS A N   
1910  C  CA  A CYS A  231 ? 0.2309 0.2833 0.1046 0.0489  -0.0098 -0.0627 231 CYS A CA  
1911  C  CA  B CYS A  231 ? 0.3264 0.1915 0.2284 -0.0250 0.0289  -0.0430 231 CYS A CA  
1912  C  C   A CYS A  231 ? 0.1698 0.2098 0.1985 0.0706  0.0432  -0.0236 231 CYS A C   
1913  C  C   B CYS A  231 ? 0.2545 0.2158 0.1886 -0.0164 -0.0152 -0.0703 231 CYS A C   
1914  O  O   A CYS A  231 ? 0.1990 0.2389 0.1578 0.0375  -0.0151 -0.0313 231 CYS A O   
1915  O  O   B CYS A  231 ? 0.2296 0.2303 0.2732 0.0318  -0.0392 -0.0377 231 CYS A O   
1916  C  CB  A CYS A  231 ? 0.2215 0.2436 0.0838 0.0333  0.0000  -0.0707 231 CYS A CB  
1917  C  CB  B CYS A  231 ? 0.2813 0.4144 0.2125 -0.0313 0.1090  -0.1733 231 CYS A CB  
1918  S  SG  A CYS A  231 ? 0.2468 0.1874 0.1644 -0.0093 -0.0439 -0.0062 231 CYS A SG  
1919  S  SG  B CYS A  231 ? 0.2637 0.4411 0.3398 0.0960  0.0248  0.0100  231 CYS A SG  
1920  N  N   . THR A  232 ? 0.2239 0.2418 0.1826 0.0432  -0.0057 -0.0834 232 THR A N   
1921  C  CA  . THR A  232 ? 0.2633 0.2344 0.1741 0.0379  0.0273  -0.0590 232 THR A CA  
1922  C  C   . THR A  232 ? 0.2680 0.1966 0.1705 -0.0103 0.0086  -0.0322 232 THR A C   
1923  O  O   . THR A  232 ? 0.2511 0.2363 0.1924 0.0222  0.0120  -0.0357 232 THR A O   
1924  C  CB  . THR A  232 ? 0.2655 0.2402 0.1669 0.0293  -0.0148 -0.0706 232 THR A CB  
1925  O  OG1 . THR A  232 ? 0.3034 0.2213 0.2210 0.0324  0.0482  -0.0416 232 THR A OG1 
1926  C  CG2 . THR A  232 ? 0.2779 0.2908 0.2424 0.0878  -0.0021 -0.0619 232 THR A CG2 
1927  N  N   . HIS A  233 ? 0.2556 0.2125 0.2212 -0.0254 0.0186  -0.0264 233 HIS A N   
1928  C  CA  . HIS A  233 ? 0.3183 0.2064 0.1856 -0.0458 -0.0199 0.0271  233 HIS A CA  
1929  C  C   . HIS A  233 ? 0.3318 0.1438 0.2063 -0.0110 0.0130  -0.0308 233 HIS A C   
1930  O  O   . HIS A  233 ? 0.2852 0.2090 0.1836 0.0097  0.0283  -0.0217 233 HIS A O   
1931  C  CB  . HIS A  233 ? 0.3734 0.2008 0.3072 -0.0204 -0.0636 0.0560  233 HIS A CB  
1932  C  CG  . HIS A  233 ? 0.5697 0.2048 0.3537 -0.0847 0.0068  0.0109  233 HIS A CG  
1933  N  ND1 . HIS A  233 ? 0.6308 0.4025 0.4000 -0.0804 -0.0732 0.0943  233 HIS A ND1 
1934  C  CD2 . HIS A  233 ? 0.5382 0.3716 0.4429 -0.0076 -0.0023 0.0940  233 HIS A CD2 
1935  C  CE1 . HIS A  233 ? 0.7986 0.5141 0.4961 -0.1211 0.0601  0.1867  233 HIS A CE1 
1936  N  NE2 . HIS A  233 ? 0.7488 0.3434 0.3894 -0.1984 0.0715  0.0842  233 HIS A NE2 
1937  N  N   . MET A  234 ? 0.2937 0.2488 0.2060 -0.0006 -0.0148 -0.0427 234 MET A N   
1938  C  CA  . MET A  234 ? 0.3436 0.2291 0.1843 0.0162  -0.0124 -0.0291 234 MET A CA  
1939  C  C   . MET A  234 ? 0.2703 0.2228 0.2323 -0.0219 -0.0098 -0.0608 234 MET A C   
1940  O  O   . MET A  234 ? 0.3643 0.2806 0.2285 0.0175  0.0601  -0.0518 234 MET A O   
1941  C  CB  . MET A  234 ? 0.3486 0.2296 0.2235 0.0115  0.0364  -0.0439 234 MET A CB  
1942  C  CG  . MET A  234 ? 0.2628 0.4370 0.2044 -0.0775 -0.0068 -0.0087 234 MET A CG  
1943  S  SD  . MET A  234 ? 0.3248 0.6625 0.3136 0.0130  -0.0738 -0.0412 234 MET A SD  
1944  C  CE  . MET A  234 ? 0.4289 0.9455 0.5293 -0.2508 -0.1176 -0.1574 234 MET A CE  
1945  N  N   A ASP A  235 ? 0.3873 0.2100 0.1705 0.0020  0.0093  -0.0778 235 ASP A N   
1946  N  N   B ASP A  235 ? 0.3864 0.2273 0.2272 -0.0162 0.0171  -0.0423 235 ASP A N   
1947  C  CA  A ASP A  235 ? 0.4630 0.1962 0.2429 0.0533  -0.0066 -0.0772 235 ASP A CA  
1948  C  CA  B ASP A  235 ? 0.4486 0.2809 0.2229 -0.0140 0.0627  -0.0377 235 ASP A CA  
1949  C  C   A ASP A  235 ? 0.4827 0.1592 0.2035 0.0939  0.0024  -0.0335 235 ASP A C   
1950  C  C   B ASP A  235 ? 0.4586 0.3185 0.3147 0.0280  0.0115  -0.1333 235 ASP A C   
1951  O  O   A ASP A  235 ? 0.4379 0.1870 0.2317 0.1019  0.0640  0.0037  235 ASP A O   
1952  O  O   B ASP A  235 ? 0.5399 0.3045 0.2919 -0.0634 0.0873  -0.1718 235 ASP A O   
1953  C  CB  A ASP A  235 ? 0.5810 0.1845 0.2942 0.0274  -0.0593 -0.1150 235 ASP A CB  
1954  C  CB  B ASP A  235 ? 0.3032 0.5871 0.4413 -0.0710 -0.0182 -0.0822 235 ASP A CB  
1955  C  CG  A ASP A  235 ? 0.6624 0.2626 0.3695 -0.0350 -0.0692 -0.0712 235 ASP A CG  
1956  C  CG  B ASP A  235 ? 0.3089 0.4564 0.3713 -0.0384 -0.0003 -0.1764 235 ASP A CG  
1957  O  OD1 A ASP A  235 ? 0.7109 0.1935 0.3815 -0.1448 -0.1230 0.0640  235 ASP A OD1 
1958  O  OD1 B ASP A  235 ? 0.4022 0.5123 0.3601 -0.2045 0.1787  -0.2310 235 ASP A OD1 
1959  O  OD2 A ASP A  235 ? 0.7283 0.2148 0.5278 -0.0272 -0.0439 0.0000  235 ASP A OD2 
1960  O  OD2 B ASP A  235 ? 0.4047 0.5184 0.4500 -0.1423 0.0068  -0.0772 235 ASP A OD2 
1961  N  N   . ASP A  236 ? 0.4595 0.2253 0.2174 0.0680  0.0113  -0.0419 236 ASP A N   
1962  C  CA  . ASP A  236 ? 0.4041 0.2115 0.2725 0.0480  0.0335  -0.0603 236 ASP A CA  
1963  C  C   . ASP A  236 ? 0.4135 0.2037 0.2666 0.0623  -0.0038 -0.0160 236 ASP A C   
1964  O  O   . ASP A  236 ? 0.3932 0.2036 0.2775 0.0608  0.0953  -0.0044 236 ASP A O   
1965  C  CB  . ASP A  236 ? 0.3673 0.2151 0.2023 0.0544  0.0428  -0.0160 236 ASP A CB  
1966  C  CG  . ASP A  236 ? 0.4907 0.2476 0.2278 0.1190  0.0635  0.0253  236 ASP A CG  
1967  O  OD1 . ASP A  236 ? 0.4226 0.4018 0.2413 0.1080  0.0307  -0.0289 236 ASP A OD1 
1968  O  OD2 . ASP A  236 ? 0.4523 0.3177 0.2477 0.0891  0.0617  0.0423  236 ASP A OD2 
1969  N  N   . PRO A  237 ? 0.5360 0.1978 0.2667 0.0507  0.1026  -0.0546 237 PRO A N   
1970  C  CA  . PRO A  237 ? 0.5738 0.2159 0.2621 0.1492  0.1347  0.0197  237 PRO A CA  
1971  C  C   . PRO A  237 ? 0.6309 0.3075 0.3609 0.1089  0.1802  -0.0603 237 PRO A C   
1972  O  O   . PRO A  237 ? 0.5059 0.2689 0.3750 0.1722  0.1368  -0.0361 237 PRO A O   
1973  C  CB  . PRO A  237 ? 0.5450 0.2249 0.3429 0.1243  0.1243  -0.0593 237 PRO A CB  
1974  C  CG  . PRO A  237 ? 0.7296 0.2649 0.4032 0.1869  0.2342  0.0153  237 PRO A CG  
1975  C  CD  . PRO A  237 ? 0.5690 0.1951 0.3544 0.1372  0.0454  0.0015  237 PRO A CD  
1976  N  N   . SER A  238 ? 0.3711 0.2849 0.3327 0.1488  0.0294  -0.0441 238 SER A N   
1977  C  CA  . SER A  238 ? 0.4408 0.2944 0.3962 0.1655  0.0068  -0.0778 238 SER A CA  
1978  C  C   . SER A  238 ? 0.3420 0.2833 0.2558 0.0816  0.0175  -0.0582 238 SER A C   
1979  O  O   . SER A  238 ? 0.3840 0.3355 0.2763 0.1221  0.0015  -0.0041 238 SER A O   
1980  C  CB  . SER A  238 ? 0.4300 0.3330 0.3458 0.1492  0.0094  -0.0531 238 SER A CB  
1981  O  OG  . SER A  238 ? 0.6348 0.5533 0.5903 0.3201  0.1257  -0.0456 238 SER A OG  
1982  N  N   . PRO A  239 ? 0.3415 0.2263 0.3596 0.0794  0.0760  -0.0553 239 PRO A N   
1983  C  CA  . PRO A  239 ? 0.2660 0.2500 0.2723 0.0434  0.0432  -0.1101 239 PRO A CA  
1984  C  C   . PRO A  239 ? 0.2554 0.3327 0.3591 0.0286  0.0494  -0.1489 239 PRO A C   
1985  O  O   . PRO A  239 ? 0.2294 0.3842 0.4174 0.0476  0.0551  -0.1275 239 PRO A O   
1986  C  CB  . PRO A  239 ? 0.2761 0.3258 0.3163 0.0970  0.0252  -0.1115 239 PRO A CB  
1987  C  CG  . PRO A  239 ? 0.4891 0.2816 0.3729 0.1383  0.1040  -0.0794 239 PRO A CG  
1988  C  CD  . PRO A  239 ? 0.3495 0.2678 0.3107 0.0888  0.0674  -0.0359 239 PRO A CD  
1989  N  N   . ARG A  240 ? 0.2278 0.2558 0.2922 0.0320  0.0480  -0.1136 240 ARG A N   
1990  C  CA  . ARG A  240 ? 0.2535 0.2849 0.3255 0.0458  0.0204  -0.1607 240 ARG A CA  
1991  C  C   . ARG A  240 ? 0.2233 0.2730 0.2743 0.0340  0.0789  -0.0912 240 ARG A C   
1992  O  O   . ARG A  240 ? 0.2393 0.2497 0.2276 0.0097  0.0465  -0.0768 240 ARG A O   
1993  C  CB  . ARG A  240 ? 0.3607 0.4268 0.3930 0.1449  -0.1118 -0.0969 240 ARG A CB  
1994  C  CG  . ARG A  240 ? 0.5116 0.6805 0.2795 0.3025  -0.0019 -0.0943 240 ARG A CG  
1995  C  CD  . ARG A  240 ? 0.8123 1.0091 0.3122 -0.1158 -0.2171 0.0491  240 ARG A CD  
1996  N  NE  . ARG A  240 ? 0.8062 0.4515 0.4154 0.2214  0.1072  -0.0110 240 ARG A NE  
1997  C  CZ  . ARG A  240 ? 0.8643 0.4536 0.2078 0.2290  0.0549  -0.0055 240 ARG A CZ  
1998  N  NH1 . ARG A  240 ? 0.4975 0.3504 0.4045 0.1211  -0.1080 -0.0416 240 ARG A NH1 
1999  N  NH2 . ARG A  240 ? 0.5832 0.7950 0.5196 0.1230  0.2294  0.2527  240 ARG A NH2 
2000  N  N   . GLU A  241 ? 0.2037 0.2524 0.3185 0.0182  0.0516  -0.1168 241 GLU A N   
2001  C  CA  . GLU A  241 ? 0.2150 0.2693 0.2545 0.0239  0.0175  -0.1220 241 GLU A CA  
2002  C  C   . GLU A  241 ? 0.1362 0.2605 0.2233 0.0126  0.0021  -0.0582 241 GLU A C   
2003  O  O   . GLU A  241 ? 0.2068 0.2863 0.2800 0.0667  -0.0146 -0.1162 241 GLU A O   
2004  C  CB  . GLU A  241 ? 0.2240 0.3655 0.3878 -0.0654 0.1254  -0.1026 241 GLU A CB  
2005  C  CG  . GLU A  241 ? 0.2834 0.5295 0.3905 -0.0619 0.1335  -0.1238 241 GLU A CG  
2006  C  CD  . GLU A  241 ? 0.4410 0.8233 0.3077 -0.3115 0.2283  -0.2179 241 GLU A CD  
2007  O  OE1 . GLU A  241 ? 0.6473 0.7055 0.4889 -0.1794 0.1055  -0.3330 241 GLU A OE1 
2008  O  OE2 . GLU A  241 ? 0.6607 0.5588 0.3104 -0.1570 0.1291  -0.0781 241 GLU A OE2 
2009  N  N   . MET A  242 ? 0.1560 0.1958 0.1842 -0.0031 0.0221  -0.0454 242 MET A N   
2010  C  CA  . MET A  242 ? 0.1628 0.1484 0.1791 0.0248  0.0034  -0.0329 242 MET A CA  
2011  C  C   . MET A  242 ? 0.1314 0.1536 0.1509 0.0074  0.0104  -0.0283 242 MET A C   
2012  O  O   . MET A  242 ? 0.1656 0.1513 0.1456 0.0252  0.0020  -0.0156 242 MET A O   
2013  C  CB  . MET A  242 ? 0.1630 0.1865 0.1468 -0.0057 0.0298  -0.0108 242 MET A CB  
2014  C  CG  . MET A  242 ? 0.2039 0.1535 0.1342 -0.0383 -0.0146 -0.0024 242 MET A CG  
2015  S  SD  . MET A  242 ? 0.1886 0.1951 0.1457 -0.0168 0.0188  -0.0251 242 MET A SD  
2016  C  CE  . MET A  242 ? 0.1996 0.1941 0.2133 -0.0533 0.0276  -0.0270 242 MET A CE  
2017  N  N   . ILE A  243 ? 0.1346 0.1651 0.1272 -0.0048 0.0096  -0.0207 243 ILE A N   
2018  C  CA  . ILE A  243 ? 0.1142 0.1725 0.1129 -0.0066 0.0194  -0.0109 243 ILE A CA  
2019  C  C   . ILE A  243 ? 0.0992 0.1520 0.1366 -0.0007 0.0205  0.0153  243 ILE A C   
2020  O  O   . ILE A  243 ? 0.1380 0.1292 0.1249 -0.0027 0.0335  -0.0020 243 ILE A O   
2021  C  CB  . ILE A  243 ? 0.1536 0.1874 0.1279 0.0252  0.0317  0.0211  243 ILE A CB  
2022  C  CG1 . ILE A  243 ? 0.1712 0.2413 0.1845 0.0176  0.0640  -0.0184 243 ILE A CG1 
2023  C  CG2 . ILE A  243 ? 0.1858 0.2702 0.1376 -0.0197 0.0104  0.0373  243 ILE A CG2 
2024  C  CD1 . ILE A  243 ? 0.1926 0.2303 0.2097 0.0417  0.0833  0.0414  243 ILE A CD1 
2025  N  N   . ASN A  244 ? 0.1141 0.1281 0.1062 -0.0137 0.0183  0.0127  244 ASN A N   
2026  C  CA  . ASN A  244 ? 0.1023 0.1209 0.1181 -0.0049 0.0277  0.0093  244 ASN A CA  
2027  C  C   . ASN A  244 ? 0.1177 0.1342 0.1073 -0.0174 0.0010  0.0185  244 ASN A C   
2028  O  O   . ASN A  244 ? 0.1018 0.1367 0.1337 0.0104  0.0182  0.0231  244 ASN A O   
2029  C  CB  . ASN A  244 ? 0.1061 0.1563 0.1465 0.0165  0.0269  0.0170  244 ASN A CB  
2030  C  CG  . ASN A  244 ? 0.1109 0.1538 0.1448 0.0285  0.0256  0.0350  244 ASN A CG  
2031  O  OD1 . ASN A  244 ? 0.1296 0.1775 0.1711 0.0147  0.0489  0.0310  244 ASN A OD1 
2032  N  ND2 . ASN A  244 ? 0.1459 0.2133 0.1732 0.0331  0.0445  -0.0063 244 ASN A ND2 
2033  N  N   . ASN A  245 ? 0.1042 0.1093 0.1145 -0.0041 0.0264  0.0098  245 ASN A N   
2034  C  CA  . ASN A  245 ? 0.1127 0.1165 0.1181 -0.0031 0.0218  0.0179  245 ASN A CA  
2035  C  C   . ASN A  245 ? 0.1086 0.0836 0.1181 0.0006  0.0173  0.0217  245 ASN A C   
2036  O  O   . ASN A  245 ? 0.0841 0.1461 0.1150 -0.0024 0.0109  -0.0040 245 ASN A O   
2037  C  CB  . ASN A  245 ? 0.1323 0.0908 0.1368 0.0065  0.0153  -0.0074 245 ASN A CB  
2038  C  CG  . ASN A  245 ? 0.1229 0.0958 0.1105 0.0021  0.0186  -0.0012 245 ASN A CG  
2039  O  OD1 . ASN A  245 ? 0.1149 0.1044 0.1520 0.0087  0.0096  0.0060  245 ASN A OD1 
2040  N  ND2 . ASN A  245 ? 0.1085 0.1242 0.2057 -0.0021 0.0015  0.0104  245 ASN A ND2 
2041  N  N   . PHE A  246 ? 0.0865 0.1154 0.1146 0.0007  0.0160  0.0226  246 PHE A N   
2042  C  CA  . PHE A  246 ? 0.1109 0.1145 0.1134 0.0251  0.0118  0.0085  246 PHE A CA  
2043  C  C   . PHE A  246 ? 0.0931 0.0978 0.1089 0.0122  0.0080  0.0207  246 PHE A C   
2044  O  O   . PHE A  246 ? 0.0947 0.1118 0.1279 0.0107  0.0173  0.0227  246 PHE A O   
2045  C  CB  . PHE A  246 ? 0.1182 0.0989 0.1322 0.0041  0.0284  0.0342  246 PHE A CB  
2046  C  CG  . PHE A  246 ? 0.1326 0.0856 0.1127 0.0094  0.0034  0.0164  246 PHE A CG  
2047  C  CD1 . PHE A  246 ? 0.1058 0.1129 0.1197 0.0054  0.0071  0.0131  246 PHE A CD1 
2048  C  CD2 . PHE A  246 ? 0.1387 0.1009 0.1500 -0.0098 -0.0037 0.0221  246 PHE A CD2 
2049  C  CE1 . PHE A  246 ? 0.1220 0.0878 0.1622 -0.0055 -0.0003 0.0068  246 PHE A CE1 
2050  C  CE2 . PHE A  246 ? 0.1181 0.1371 0.1786 -0.0119 -0.0261 0.0498  246 PHE A CE2 
2051  C  CZ  . PHE A  246 ? 0.1163 0.1142 0.2020 -0.0113 -0.0193 0.0381  246 PHE A CZ  
2052  N  N   . ARG A  247 ? 0.1046 0.0935 0.0973 -0.0015 0.0060  0.0285  247 ARG A N   
2053  C  CA  . ARG A  247 ? 0.0982 0.0877 0.1100 -0.0082 0.0083  0.0275  247 ARG A CA  
2054  C  C   . ARG A  247 ? 0.0994 0.0848 0.1042 0.0026  0.0118  0.0167  247 ARG A C   
2055  O  O   . ARG A  247 ? 0.0989 0.0940 0.1173 -0.0082 0.0124  0.0099  247 ARG A O   
2056  C  CB  . ARG A  247 ? 0.0890 0.1143 0.1026 -0.0046 0.0078  0.0348  247 ARG A CB  
2057  C  CG  . ARG A  247 ? 0.1014 0.1068 0.1091 -0.0073 0.0104  0.0384  247 ARG A CG  
2058  C  CD  . ARG A  247 ? 0.1046 0.0811 0.1249 -0.0019 0.0049  0.0299  247 ARG A CD  
2059  N  NE  . ARG A  247 ? 0.1082 0.0890 0.1274 -0.0068 0.0070  0.0362  247 ARG A NE  
2060  C  CZ  . ARG A  247 ? 0.1023 0.0965 0.1294 -0.0062 0.0229  0.0313  247 ARG A CZ  
2061  N  NH1 . ARG A  247 ? 0.1061 0.0965 0.1360 -0.0218 0.0156  0.0342  247 ARG A NH1 
2062  N  NH2 . ARG A  247 ? 0.0996 0.0874 0.1659 -0.0130 -0.0076 0.0351  247 ARG A NH2 
2063  N  N   . GLN A  248 ? 0.0942 0.0890 0.1142 -0.0001 0.0131  0.0291  248 GLN A N   
2064  C  CA  . GLN A  248 ? 0.0820 0.0888 0.1269 0.0091  0.0136  0.0274  248 GLN A CA  
2065  C  C   . GLN A  248 ? 0.0942 0.0746 0.1137 0.0000  0.0207  0.0239  248 GLN A C   
2066  O  O   . GLN A  248 ? 0.0976 0.0917 0.1096 -0.0081 0.0197  0.0234  248 GLN A O   
2067  C  CB  . GLN A  248 ? 0.1018 0.0881 0.1125 0.0153  0.0148  0.0366  248 GLN A CB  
2068  C  CG  . GLN A  248 ? 0.0996 0.0952 0.1224 -0.0006 0.0206  0.0186  248 GLN A CG  
2069  C  CD  . GLN A  248 ? 0.0784 0.1360 0.1202 -0.0052 0.0227  0.0353  248 GLN A CD  
2070  O  OE1 . GLN A  248 ? 0.1222 0.1039 0.1495 -0.0070 0.0031  0.0326  248 GLN A OE1 
2071  N  NE2 . GLN A  248 ? 0.1088 0.1200 0.1529 -0.0230 0.0026  0.0379  248 GLN A NE2 
2072  N  N   . VAL A  249 ? 0.0901 0.0820 0.1106 0.0074  0.0091  0.0210  249 VAL A N   
2073  C  CA  . VAL A  249 ? 0.1044 0.1003 0.0994 0.0052  0.0098  0.0144  249 VAL A CA  
2074  C  C   . VAL A  249 ? 0.0784 0.0897 0.1222 0.0027  0.0001  0.0164  249 VAL A C   
2075  O  O   . VAL A  249 ? 0.0873 0.0970 0.1299 0.0043  0.0085  0.0249  249 VAL A O   
2076  C  CB  . VAL A  249 ? 0.1306 0.0825 0.1384 0.0071  -0.0052 0.0229  249 VAL A CB  
2077  C  CG1 . VAL A  249 ? 0.1570 0.1021 0.1508 0.0324  0.0087  0.0313  249 VAL A CG1 
2078  C  CG2 . VAL A  249 ? 0.1425 0.1247 0.1639 -0.0126 -0.0046 0.0419  249 VAL A CG2 
2079  N  N   . GLN A  250 ? 0.0957 0.0883 0.1221 -0.0144 0.0080  0.0255  250 GLN A N   
2080  C  CA  . GLN A  250 ? 0.1061 0.0931 0.1156 -0.0001 0.0066  0.0193  250 GLN A CA  
2081  C  C   . GLN A  250 ? 0.1143 0.1030 0.1254 -0.0205 0.0013  0.0196  250 GLN A C   
2082  O  O   . GLN A  250 ? 0.1750 0.1165 0.1326 -0.0144 0.0024  0.0020  250 GLN A O   
2083  C  CB  . GLN A  250 ? 0.0903 0.1242 0.1186 0.0020  0.0129  0.0326  250 GLN A CB  
2084  C  CG  . GLN A  250 ? 0.1005 0.0991 0.1356 0.0049  0.0132  0.0285  250 GLN A CG  
2085  C  CD  . GLN A  250 ? 0.0800 0.0930 0.1287 0.0035  0.0040  0.0304  250 GLN A CD  
2086  O  OE1 . GLN A  250 ? 0.1093 0.0960 0.1466 0.0098  0.0122  0.0438  250 GLN A OE1 
2087  N  NE2 . GLN A  250 ? 0.1005 0.0982 0.1283 -0.0125 0.0015  0.0175  250 GLN A NE2 
2088  N  N   . LYS A  251 ? 0.0960 0.1682 0.1154 -0.0043 0.0144  0.0164  251 LYS A N   
2089  C  CA  . LYS A  251 ? 0.0996 0.2090 0.0998 -0.0250 0.0126  0.0287  251 LYS A CA  
2090  C  C   . LYS A  251 ? 0.1080 0.1482 0.1253 -0.0132 0.0144  0.0275  251 LYS A C   
2091  O  O   . LYS A  251 ? 0.1221 0.1655 0.1389 -0.0081 0.0200  0.0310  251 LYS A O   
2092  C  CB  . LYS A  251 ? 0.0838 0.2678 0.1152 0.0109  0.0220  0.0337  251 LYS A CB  
2093  C  CG  . LYS A  251 ? 0.0966 0.3118 0.1403 0.0377  0.0392  0.0154  251 LYS A CG  
2094  C  CD  . LYS A  251 ? 0.1141 0.3133 0.1368 0.0487  0.0428  0.0394  251 LYS A CD  
2095  C  CE  . LYS A  251 ? 0.0912 0.1489 0.1077 0.0001  0.0175  0.0194  251 LYS A CE  
2096  N  NZ  . LYS A  251 ? 0.0838 0.1194 0.1215 -0.0035 0.0151  0.0241  251 LYS A NZ  
2097  N  N   . PHE A  252 ? 0.1475 0.1842 0.1385 -0.0066 0.0012  0.0187  252 PHE A N   
2098  C  CA  . PHE A  252 ? 0.1692 0.2093 0.1274 0.0285  0.0241  0.0120  252 PHE A CA  
2099  C  C   . PHE A  252 ? 0.1592 0.2554 0.2114 -0.0141 0.0149  0.0126  252 PHE A C   
2100  O  O   . PHE A  252 ? 0.3240 0.2894 0.2319 -0.0522 -0.0328 0.0114  252 PHE A O   
2101  C  CB  . PHE A  252 ? 0.2017 0.1877 0.1719 0.0399  0.0476  0.0372  252 PHE A CB  
2102  C  CG  . PHE A  252 ? 0.1971 0.2335 0.1375 0.0571  0.0017  0.0109  252 PHE A CG  
2103  C  CD1 . PHE A  252 ? 0.1802 0.2829 0.1382 0.0390  0.0070  0.0623  252 PHE A CD1 
2104  C  CD2 . PHE A  252 ? 0.2334 0.2384 0.1962 0.0293  0.0474  -0.0063 252 PHE A CD2 
2105  C  CE1 . PHE A  252 ? 0.1928 0.2725 0.1926 0.0597  -0.0162 0.0370  252 PHE A CE1 
2106  C  CE2 . PHE A  252 ? 0.2239 0.2188 0.2055 0.0449  0.0527  0.0109  252 PHE A CE2 
2107  C  CZ  . PHE A  252 ? 0.2140 0.2445 0.2030 0.0392  0.0434  0.0597  252 PHE A CZ  
2108  N  N   . ASP A  253 ? 0.2691 0.3984 0.2012 0.0276  -0.0395 0.0269  253 ASP A N   
2109  C  CA  . ASP A  253 ? 0.2906 0.4501 0.1601 0.0456  -0.0450 -0.0200 253 ASP A CA  
2110  C  C   . ASP A  253 ? 0.2003 0.3883 0.2266 0.0472  -0.0305 -0.0439 253 ASP A C   
2111  O  O   . ASP A  253 ? 0.2637 0.3689 0.2535 0.0000  -0.0264 -0.0675 253 ASP A O   
2112  C  CB  . ASP A  253 ? 0.4095 0.5231 0.2398 0.1700  -0.1062 -0.0315 253 ASP A CB  
2113  C  CG  . ASP A  253 ? 0.5271 0.7767 0.4972 0.0430  -0.2040 0.0057  253 ASP A CG  
2114  O  OD1 . ASP A  253 ? 0.3815 0.7778 0.4061 0.1568  -0.0641 0.0489  253 ASP A OD1 
2115  O  OD2 . ASP A  253 ? 0.6245 0.7329 0.2696 0.2824  -0.0397 -0.0939 253 ASP A OD2 
2116  N  N   A GLU A  254 ? 0.2662 0.3745 0.1554 0.0740  -0.0564 -0.0322 254 GLU A N   
2117  N  N   B GLU A  254 ? 0.3111 0.4219 0.1987 0.0293  -0.0232 -0.0844 254 GLU A N   
2118  C  CA  A GLU A  254 ? 0.1899 0.3820 0.1939 0.0641  -0.0189 0.0154  254 GLU A CA  
2119  C  CA  B GLU A  254 ? 0.1941 0.4068 0.2219 -0.0104 -0.0115 -0.0436 254 GLU A CA  
2120  C  C   A GLU A  254 ? 0.1917 0.3759 0.2831 0.0498  -0.0172 0.0674  254 GLU A C   
2121  C  C   B GLU A  254 ? 0.1994 0.3639 0.2815 0.0186  -0.0054 0.0738  254 GLU A C   
2122  O  O   A GLU A  254 ? 0.2337 0.3382 0.2472 0.0414  -0.0137 0.0456  254 GLU A O   
2123  O  O   B GLU A  254 ? 0.3693 0.4253 0.3046 -0.0826 0.0653  0.0285  254 GLU A O   
2124  C  CB  A GLU A  254 ? 0.2272 0.4000 0.1890 0.0672  0.0008  0.0570  254 GLU A CB  
2125  C  CB  B GLU A  254 ? 0.2294 0.4147 0.2450 -0.0395 -0.0219 0.0030  254 GLU A CB  
2126  C  CG  A GLU A  254 ? 0.2163 0.5101 0.1342 0.0886  0.0432  0.0895  254 GLU A CG  
2127  C  CG  B GLU A  254 ? 0.2520 0.4925 0.4242 0.0007  -0.0961 -0.0031 254 GLU A CG  
2128  C  CD  A GLU A  254 ? 0.1328 0.5705 0.2423 0.0983  0.0355  0.1527  254 GLU A CD  
2129  C  CD  B GLU A  254 ? 0.6054 0.4153 0.2184 -0.0531 0.0219  0.1404  254 GLU A CD  
2130  O  OE1 A GLU A  254 ? 0.6247 0.5343 0.3325 -0.0346 -0.0864 -0.0936 254 GLU A OE1 
2131  O  OE1 B GLU A  254 ? 0.8891 0.3027 0.3991 0.1537  0.0425  0.0076  254 GLU A OE1 
2132  O  OE2 A GLU A  254 ? 0.2154 0.7627 0.2350 0.1291  -0.0270 -0.1108 254 GLU A OE2 
2133  O  OE2 B GLU A  254 ? 0.4837 0.6279 0.2809 -0.0896 0.1054  -0.0222 254 GLU A OE2 
2134  N  N   . ARG A  255 ? 0.2493 0.3440 0.2264 -0.0003 -0.0285 0.0361  255 ARG A N   
2135  C  CA  . ARG A  255 ? 0.2299 0.3075 0.2579 0.0017  -0.0467 0.0269  255 ARG A CA  
2136  C  C   . ARG A  255 ? 0.2389 0.3084 0.1676 0.0524  0.0263  -0.0001 255 ARG A C   
2137  O  O   . ARG A  255 ? 0.2003 0.3522 0.2276 0.0445  0.0049  0.0054  255 ARG A O   
2138  C  CB  . ARG A  255 ? 0.2105 0.2842 0.2273 0.0228  -0.0318 0.0113  255 ARG A CB  
2139  C  CG  . ARG A  255 ? 0.2768 0.3305 0.1980 0.0507  -0.0003 0.0040  255 ARG A CG  
2140  C  CD  . ARG A  255 ? 0.2463 0.2576 0.3441 0.0243  -0.1208 -0.0200 255 ARG A CD  
2141  N  NE  . ARG A  255 ? 0.2334 0.3704 0.2057 -0.0688 -0.0483 0.1072  255 ARG A NE  
2142  C  CZ  . ARG A  255 ? 0.2639 0.2662 0.2305 -0.0696 -0.0606 0.0520  255 ARG A CZ  
2143  N  NH1 . ARG A  255 ? 0.2885 0.2472 0.2834 -0.0043 -0.0685 -0.0092 255 ARG A NH1 
2144  N  NH2 . ARG A  255 ? 0.1888 0.3023 0.1811 -0.0054 -0.0566 0.0125  255 ARG A NH2 
2145  N  N   . LEU A  256 ? 0.2039 0.3635 0.2289 0.0313  0.0055  0.0956  256 LEU A N   
2146  C  CA  . LEU A  256 ? 0.2626 0.3510 0.1773 0.0996  0.0027  0.0515  256 LEU A CA  
2147  C  C   . LEU A  256 ? 0.2190 0.2786 0.2027 0.0263  0.0098  0.0419  256 LEU A C   
2148  O  O   . LEU A  256 ? 0.2741 0.2734 0.2046 0.0649  -0.0040 0.0251  256 LEU A O   
2149  C  CB  . LEU A  256 ? 0.2949 0.3549 0.1500 0.0450  0.0005  0.0116  256 LEU A CB  
2150  C  CG  . LEU A  256 ? 0.4482 0.4293 0.1892 0.0586  -0.0900 -0.0170 256 LEU A CG  
2151  C  CD1 . LEU A  256 ? 0.5816 0.3659 0.1623 0.0203  -0.0315 -0.0027 256 LEU A CD1 
2152  C  CD2 . LEU A  256 ? 0.4596 0.4318 0.3659 0.0612  -0.1360 0.0179  256 LEU A CD2 
2153  N  N   . VAL A  257 ? 0.1915 0.3233 0.1757 0.0131  -0.0052 0.0392  257 VAL A N   
2154  C  CA  . VAL A  257 ? 0.1714 0.2574 0.1721 0.0041  0.0031  0.0005  257 VAL A CA  
2155  C  C   . VAL A  257 ? 0.1951 0.2459 0.1436 -0.0082 0.0390  -0.0232 257 VAL A C   
2156  O  O   . VAL A  257 ? 0.2057 0.2637 0.1800 -0.0299 0.0017  -0.0531 257 VAL A O   
2157  C  CB  . VAL A  257 ? 0.1764 0.2725 0.1432 0.0094  0.0166  0.0008  257 VAL A CB  
2158  C  CG1 . VAL A  257 ? 0.2048 0.2238 0.1756 0.0298  0.0017  -0.0103 257 VAL A CG1 
2159  C  CG2 . VAL A  257 ? 0.1987 0.2186 0.2377 0.0113  0.0232  0.0377  257 VAL A CG2 
2160  N  N   . TYR A  258 ? 0.1802 0.2233 0.1423 -0.0111 0.0184  0.0300  258 TYR A N   
2161  C  CA  . TYR A  258 ? 0.2348 0.2220 0.1286 0.0046  0.0208  0.0131  258 TYR A CA  
2162  C  C   . TYR A  258 ? 0.2001 0.2125 0.1172 -0.0445 -0.0049 -0.0006 258 TYR A C   
2163  O  O   . TYR A  258 ? 0.2608 0.1942 0.1335 -0.0093 -0.0317 -0.0160 258 TYR A O   
2164  C  CB  . TYR A  258 ? 0.2391 0.2937 0.1380 -0.0277 0.0094  0.0458  258 TYR A CB  
2165  C  CG  . TYR A  258 ? 0.2396 0.2736 0.1730 -0.0077 0.0417  0.0173  258 TYR A CG  
2166  C  CD1 . TYR A  258 ? 0.2782 0.3589 0.1500 -0.0302 -0.0214 0.0359  258 TYR A CD1 
2167  C  CD2 . TYR A  258 ? 0.2924 0.2773 0.1556 0.0043  0.0137  0.0284  258 TYR A CD2 
2168  C  CE1 . TYR A  258 ? 0.3345 0.3783 0.2646 -0.0157 0.0208  0.1026  258 TYR A CE1 
2169  C  CE2 . TYR A  258 ? 0.3131 0.3400 0.2124 0.0006  -0.0085 0.0850  258 TYR A CE2 
2170  C  CZ  . TYR A  258 ? 0.2831 0.3600 0.2138 -0.0258 -0.0280 0.1186  258 TYR A CZ  
2171  O  OH  . TYR A  258 ? 0.4031 0.4986 0.2605 0.0104  -0.0432 0.1861  258 TYR A OH  
2172  N  N   . THR A  259 ? 0.2337 0.1897 0.1260 -0.0392 0.0020  -0.0087 259 THR A N   
2173  C  CA  . THR A  259 ? 0.2109 0.2020 0.0989 -0.0372 0.0041  -0.0271 259 THR A CA  
2174  C  C   . THR A  259 ? 0.2127 0.1511 0.1102 -0.0346 0.0450  -0.0015 259 THR A C   
2175  O  O   . THR A  259 ? 0.2585 0.2041 0.1055 -0.0390 0.0414  -0.0329 259 THR A O   
2176  C  CB  . THR A  259 ? 0.2021 0.2106 0.1350 -0.0375 0.0130  0.0006  259 THR A CB  
2177  O  OG1 . THR A  259 ? 0.2782 0.2644 0.1520 -0.0904 0.0136  -0.0184 259 THR A OG1 
2178  C  CG2 . THR A  259 ? 0.2023 0.2592 0.1562 -0.0178 0.0310  0.0274  259 THR A CG2 
2179  N  N   . SER A  260 ? 0.2291 0.1483 0.1048 0.0012  0.0256  -0.0186 260 SER A N   
2180  C  CA  . SER A  260 ? 0.2461 0.1924 0.1242 0.0120  0.0485  -0.0443 260 SER A CA  
2181  C  C   . SER A  260 ? 0.2658 0.1897 0.1272 0.0233  0.0527  -0.0465 260 SER A C   
2182  O  O   . SER A  260 ? 0.2793 0.1926 0.2755 0.0232  0.0421  -0.0926 260 SER A O   
2183  C  CB  . SER A  260 ? 0.2102 0.1966 0.1377 -0.0308 0.0710  -0.0317 260 SER A CB  
2184  O  OG  . SER A  260 ? 0.1948 0.2176 0.1102 -0.0070 0.0516  -0.0461 260 SER A OG  
2185  N  N   . PHE A  261 ? 0.2635 0.1910 0.1560 -0.0331 0.0175  -0.0405 261 PHE A N   
2186  C  CA  . PHE A  261 ? 0.3425 0.1811 0.1887 -0.0702 0.0151  -0.0295 261 PHE A CA  
2187  C  C   . PHE A  261 ? 0.3000 0.1879 0.2556 -0.0938 0.0063  -0.0068 261 PHE A C   
2188  O  O   . PHE A  261 ? 0.3846 0.2414 0.2206 -0.0463 -0.0416 -0.0157 261 PHE A O   
2189  C  CB  . PHE A  261 ? 0.2786 0.2020 0.2035 -0.0522 0.0272  -0.0100 261 PHE A CB  
2190  C  CG  . PHE A  261 ? 0.2892 0.2547 0.1376 -0.0693 0.0476  -0.0214 261 PHE A CG  
2191  C  CD1 . PHE A  261 ? 0.3097 0.2240 0.2583 -0.0460 -0.0351 0.0171  261 PHE A CD1 
2192  C  CD2 . PHE A  261 ? 0.2626 0.2107 0.1064 -0.0307 0.0298  0.0031  261 PHE A CD2 
2193  C  CE1 . PHE A  261 ? 0.2766 0.3111 0.3068 -0.0776 0.0035  -0.0329 261 PHE A CE1 
2194  C  CE2 . PHE A  261 ? 0.2822 0.2231 0.1167 -0.0274 0.0518  0.0226  261 PHE A CE2 
2195  C  CZ  . PHE A  261 ? 0.2989 0.2362 0.1854 -0.0198 0.0408  0.0122  261 PHE A CZ  
2196  N  N   . SER A  262 ? 0.6926 0.2379 0.2206 -0.2047 -0.0362 -0.0200 262 SER A N   
2197  C  CA  . SER A  262 ? 0.8428 0.3835 0.3528 -0.2809 -0.2254 0.0423  262 SER A CA  
2198  C  C   . SER A  262 ? 0.6991 0.4239 0.6952 -0.3050 -0.2833 0.1574  262 SER A C   
2199  O  O   . SER A  262 ? 0.7817 0.5489 0.9416 0.0852  -0.0100 0.0746  262 SER A O   
2200  C  CB  . SER A  262 ? 1.1448 0.3537 0.5796 -0.0750 0.1342  0.0109  262 SER A CB  
2201  O  OG  . SER A  262 ? 1.5053 0.4612 0.3000 0.0658  -0.0223 -0.0063 262 SER A OG  
2202  N  N   . GLN A  263 ? 0.9796 0.3601 0.4138 -0.0979 -0.0504 0.1327  263 GLN A N   
2203  C  CA  . GLN A  263 ? 1.1153 0.3865 0.5390 0.2808  0.3916  0.2057  263 GLN A CA  
2204  C  C   . GLN A  263 ? 1.3047 0.5557 0.5317 0.0802  0.5547  0.1035  263 GLN A C   
2205  O  O   . GLN A  263 ? 3.1912 0.9910 2.3522 0.7344  2.6149  0.7746  263 GLN A O   
2206  C  CB  . GLN A  263 ? 0.8600 0.6675 0.7511 0.1955  0.4316  0.4602  263 GLN A CB  
2207  C  CG  . GLN A  263 ? 1.2891 0.1610 1.0329 -0.1486 0.1569  -0.1004 263 GLN A CG  
2208  C  CD  . GLN A  263 ? 0.3251 0.3095 0.5436 -0.0803 -0.0454 -0.0927 263 GLN A CD  
2209  O  OE1 . GLN A  263 ? 0.3635 0.5515 0.4219 -0.1410 -0.0798 -0.0487 263 GLN A OE1 
2210  N  NE2 . GLN A  263 ? 0.3163 0.1777 0.2795 -0.0870 0.0450  -0.0076 263 GLN A NE2 
2211  N  N   . LYS B  3   ? 5.7638 0.1103 5.6360 0.5990  0.6014  -0.0522 3   LYS B N   
2212  C  CA  . LYS B  3   ? 0.7832 0.2809 0.9915 -0.2398 -0.4248 0.4316  3   LYS B CA  
2213  C  C   . LYS B  3   ? 0.7149 0.1423 0.2838 -0.0076 0.0551  0.1342  3   LYS B C   
2214  O  O   . LYS B  3   ? 0.5101 0.2912 0.2393 -0.0590 0.0672  0.0866  3   LYS B O   
2215  C  CB  . LYS B  3   ? 0.5357 0.2597 0.8525 -0.0865 -0.1613 0.0648  3   LYS B CB  
2216  C  CG  . LYS B  3   ? 0.4126 0.2364 0.6947 -0.1472 0.0137  0.0114  3   LYS B CG  
2217  C  CD  . LYS B  3   ? 1.0154 0.3474 0.6506 -0.2049 0.0494  0.3353  3   LYS B CD  
2218  C  CE  . LYS B  3   ? 1.0806 0.7886 1.0504 -0.2687 -0.2662 0.1173  3   LYS B CE  
2219  N  NZ  . LYS B  3   ? 1.5965 0.1197 1.5221 0.2355  0.1560  0.0700  3   LYS B NZ  
2220  N  N   . TRP B  4   ? 0.3257 0.1145 0.1982 -0.0013 -0.0003 0.0419  4   TRP B N   
2221  C  CA  . TRP B  4   ? 0.2046 0.1041 0.1836 -0.0059 -0.0024 0.0414  4   TRP B CA  
2222  C  C   . TRP B  4   ? 0.1843 0.1158 0.1725 -0.0217 -0.0317 0.0370  4   TRP B C   
2223  O  O   . TRP B  4   ? 0.1775 0.1489 0.1639 -0.0070 -0.0142 0.0328  4   TRP B O   
2224  C  CB  . TRP B  4   ? 0.1818 0.1274 0.1844 0.0000  0.0000  0.0255  4   TRP B CB  
2225  C  CG  . TRP B  4   ? 0.1696 0.1125 0.1536 0.0071  -0.0107 0.0269  4   TRP B CG  
2226  C  CD1 . TRP B  4   ? 0.2023 0.1340 0.1696 0.0297  0.0167  0.0003  4   TRP B CD1 
2227  C  CD2 . TRP B  4   ? 0.1534 0.1086 0.1430 -0.0001 -0.0337 0.0214  4   TRP B CD2 
2228  N  NE1 . TRP B  4   ? 0.1680 0.1362 0.1723 0.0408  -0.0088 0.0233  4   TRP B NE1 
2229  C  CE2 . TRP B  4   ? 0.1495 0.1398 0.1369 0.0082  -0.0153 0.0164  4   TRP B CE2 
2230  C  CE3 . TRP B  4   ? 0.1884 0.0882 0.1572 -0.0055 -0.0252 0.0034  4   TRP B CE3 
2231  C  CZ2 . TRP B  4   ? 0.2039 0.1571 0.1412 -0.0172 -0.0320 0.0485  4   TRP B CZ2 
2232  C  CZ3 . TRP B  4   ? 0.1626 0.1482 0.1404 -0.0370 -0.0318 0.0197  4   TRP B CZ3 
2233  C  CH2 . TRP B  4   ? 0.1714 0.1605 0.1359 -0.0434 -0.0329 0.0206  4   TRP B CH2 
2234  N  N   . THR B  5   ? 0.1712 0.1102 0.1685 -0.0226 -0.0003 0.0421  5   THR B N   
2235  C  CA  . THR B  5   ? 0.1929 0.0920 0.1671 -0.0131 0.0119  0.0276  5   THR B CA  
2236  C  C   . THR B  5   ? 0.1470 0.1231 0.1407 -0.0254 0.0102  0.0206  5   THR B C   
2237  O  O   . THR B  5   ? 0.1628 0.1123 0.1319 -0.0403 0.0140  0.0261  5   THR B O   
2238  C  CB  . THR B  5   ? 0.1800 0.1491 0.1668 -0.0286 0.0179  0.0522  5   THR B CB  
2239  O  OG1 . THR B  5   ? 0.1868 0.1714 0.1967 -0.0156 0.0329  0.0653  5   THR B OG1 
2240  C  CG2 . THR B  5   ? 0.3149 0.1393 0.1308 -0.0494 -0.0082 0.0483  5   THR B CG2 
2241  N  N   . TYR B  6   ? 0.1703 0.1190 0.1319 -0.0401 0.0238  0.0318  6   TYR B N   
2242  C  CA  . TYR B  6   ? 0.1720 0.1003 0.1911 -0.0234 0.0248  0.0634  6   TYR B CA  
2243  C  C   . TYR B  6   ? 0.2082 0.1037 0.1561 -0.0203 0.0505  0.0252  6   TYR B C   
2244  O  O   . TYR B  6   ? 0.1874 0.1274 0.1551 -0.0280 0.0136  0.0208  6   TYR B O   
2245  C  CB  . TYR B  6   ? 0.1738 0.1287 0.1759 -0.0483 0.0494  0.0491  6   TYR B CB  
2246  C  CG  . TYR B  6   ? 0.1653 0.0864 0.1407 -0.0471 0.0271  0.0147  6   TYR B CG  
2247  C  CD1 . TYR B  6   ? 0.1782 0.0746 0.1253 -0.0195 0.0234  0.0049  6   TYR B CD1 
2248  C  CD2 . TYR B  6   ? 0.1547 0.0764 0.1492 -0.0212 0.0381  0.0147  6   TYR B CD2 
2249  C  CE1 . TYR B  6   ? 0.2113 0.0725 0.1355 0.0119  0.0500  0.0152  6   TYR B CE1 
2250  C  CE2 . TYR B  6   ? 0.1551 0.0798 0.1299 0.0000  0.0370  0.0115  6   TYR B CE2 
2251  C  CZ  . TYR B  6   ? 0.1565 0.0676 0.1405 0.0170  0.0285  0.0125  6   TYR B CZ  
2252  O  OH  . TYR B  6   ? 0.1796 0.1306 0.1378 0.0436  0.0527  0.0073  6   TYR B OH  
2253  N  N   . PHE B  7   ? 0.1725 0.1771 0.1457 -0.0392 0.0339  0.0487  7   PHE B N   
2254  C  CA  . PHE B  7   ? 0.1653 0.2109 0.2026 -0.0373 0.0434  0.0223  7   PHE B CA  
2255  C  C   . PHE B  7   ? 0.1847 0.2424 0.2341 -0.0284 0.0509  0.0878  7   PHE B C   
2256  O  O   . PHE B  7   ? 0.2025 0.1951 0.2531 -0.0408 0.0092  0.0636  7   PHE B O   
2257  C  CB  . PHE B  7   ? 0.2536 0.3023 0.2100 -0.0310 0.0285  0.0419  7   PHE B CB  
2258  C  CG  . PHE B  7   ? 0.3617 0.2246 0.2881 -0.0877 0.0873  -0.0195 7   PHE B CG  
2259  C  CD1 . PHE B  7   ? 0.3043 0.4201 0.3495 0.0201  0.1147  -0.0275 7   PHE B CD1 
2260  C  CD2 . PHE B  7   ? 0.5497 0.4565 0.2379 0.0681  0.1704  0.0540  7   PHE B CD2 
2261  C  CE1 . PHE B  7   ? 0.3869 0.3310 0.4361 -0.0140 0.2071  -0.0659 7   PHE B CE1 
2262  C  CE2 . PHE B  7   ? 0.6434 0.6151 0.4038 -0.0210 0.3467  0.0791  7   PHE B CE2 
2263  C  CZ  . PHE B  7   ? 0.7125 0.5758 0.6262 -0.0299 0.3488  0.0856  7   PHE B CZ  
2264  N  N   . GLY B  8   ? 0.1842 0.2786 0.2305 -0.0524 0.0452  0.0593  8   GLY B N   
2265  C  CA  . GLY B  8   ? 0.2377 0.2309 0.2296 -0.0427 0.0357  0.0261  8   GLY B CA  
2266  C  C   . GLY B  8   ? 0.1655 0.2335 0.2133 -0.0288 0.0399  0.0505  8   GLY B C   
2267  O  O   . GLY B  8   ? 0.1729 0.2373 0.1877 -0.0515 -0.0035 0.0588  8   GLY B O   
2268  N  N   A PRO B  9   ? 0.2294 0.2190 0.2012 -0.0342 -0.0138 0.0662  9   PRO B N   
2269  N  N   B PRO B  9   ? 0.1611 0.2610 0.2404 -0.1036 0.0110  0.0709  9   PRO B N   
2270  C  CA  A PRO B  9   ? 0.2257 0.2197 0.1858 -0.0364 0.0060  0.0595  9   PRO B CA  
2271  C  CA  B PRO B  9   ? 0.2657 0.1967 0.2520 -0.1013 0.0467  0.0483  9   PRO B CA  
2272  C  C   A PRO B  9   ? 0.1938 0.2222 0.1827 -0.0274 -0.0138 0.0675  9   PRO B C   
2273  C  C   B PRO B  9   ? 0.2052 0.2705 0.2251 -0.0795 -0.0098 0.0917  9   PRO B C   
2274  O  O   A PRO B  9   ? 0.1799 0.1572 0.1941 -0.0601 -0.0241 0.0747  9   PRO B O   
2275  O  O   B PRO B  9   ? 0.2657 0.2255 0.2689 -0.0582 -0.0524 0.0899  9   PRO B O   
2276  C  CB  A PRO B  9   ? 0.2601 0.2212 0.2030 -0.0838 -0.0427 0.0754  9   PRO B CB  
2277  C  CB  B PRO B  9   ? 0.2253 0.3151 0.2583 -0.1242 0.0204  0.1323  9   PRO B CB  
2278  C  CG  A PRO B  9   ? 0.3045 0.2167 0.2933 -0.0234 0.0692  0.1292  9   PRO B CG  
2279  C  CG  B PRO B  9   ? 0.3018 0.3431 0.2579 -0.1071 -0.0120 0.1638  9   PRO B CG  
2280  C  CD  A PRO B  9   ? 0.2359 0.2361 0.2671 -0.0414 0.0808  0.1368  9   PRO B CD  
2281  C  CD  B PRO B  9   ? 0.2287 0.3450 0.2673 -0.0342 0.1118  0.1221  9   PRO B CD  
2282  N  N   . ASP B  10  ? 0.2041 0.2030 0.2118 -0.0482 0.0065  0.1125  10  ASP B N   
2283  C  CA  . ASP B  10  ? 0.1935 0.0886 0.2129 -0.0308 -0.0127 0.0487  10  ASP B CA  
2284  C  C   . ASP B  10  ? 0.1592 0.0971 0.1780 -0.0276 -0.0140 0.0355  10  ASP B C   
2285  O  O   . ASP B  10  ? 0.1479 0.1200 0.1975 -0.0228 -0.0315 0.0485  10  ASP B O   
2286  C  CB  . ASP B  10  ? 0.2565 0.1447 0.2069 -0.0417 -0.0428 0.0876  10  ASP B CB  
2287  C  CG  . ASP B  10  ? 0.3285 0.1509 0.2540 -0.0449 -0.0131 0.0873  10  ASP B CG  
2288  O  OD1 . ASP B  10  ? 0.4329 0.1547 0.2872 -0.1150 -0.0366 0.0631  10  ASP B OD1 
2289  O  OD2 . ASP B  10  ? 0.4850 0.2256 0.2728 -0.0816 -0.0584 0.1248  10  ASP B OD2 
2290  N  N   . GLY B  11  ? 0.1662 0.1136 0.1878 -0.0392 -0.0109 0.0557  11  GLY B N   
2291  C  CA  . GLY B  11  ? 0.1371 0.1120 0.1611 -0.0329 0.0077  0.0476  11  GLY B CA  
2292  C  C   . GLY B  11  ? 0.1155 0.0830 0.1644 -0.0230 -0.0212 0.0417  11  GLY B C   
2293  O  O   . GLY B  11  ? 0.1322 0.0811 0.1565 -0.0143 -0.0170 0.0441  11  GLY B O   
2294  N  N   . GLU B  12  ? 0.1172 0.0800 0.1347 -0.0110 0.0059  0.0335  12  GLU B N   
2295  C  CA  . GLU B  12  ? 0.1112 0.0715 0.1404 -0.0133 -0.0021 0.0307  12  GLU B CA  
2296  C  C   . GLU B  12  ? 0.1017 0.0654 0.1597 -0.0062 -0.0048 0.0282  12  GLU B C   
2297  O  O   . GLU B  12  ? 0.1049 0.0843 0.1576 -0.0212 -0.0013 0.0131  12  GLU B O   
2298  C  CB  . GLU B  12  ? 0.0983 0.0712 0.1588 -0.0098 0.0023  0.0306  12  GLU B CB  
2299  C  CG  . GLU B  12  ? 0.1075 0.0723 0.1457 -0.0060 0.0190  0.0176  12  GLU B CG  
2300  C  CD  . GLU B  12  ? 0.0962 0.0881 0.1267 -0.0186 0.0073  0.0234  12  GLU B CD  
2301  O  OE1 . GLU B  12  ? 0.1082 0.0829 0.1290 -0.0089 0.0089  0.0236  12  GLU B OE1 
2302  O  OE2 . GLU B  12  ? 0.1439 0.0922 0.1281 -0.0252 0.0027  0.0233  12  GLU B OE2 
2303  N  N   . ASN B  13  ? 0.0942 0.0748 0.1509 -0.0114 0.0013  0.0405  13  ASN B N   
2304  C  CA  . ASN B  13  ? 0.0891 0.0653 0.1798 -0.0157 0.0035  0.0108  13  ASN B CA  
2305  C  C   . ASN B  13  ? 0.1018 0.0757 0.1646 -0.0179 -0.0098 0.0326  13  ASN B C   
2306  O  O   . ASN B  13  ? 0.1362 0.0732 0.1793 -0.0192 -0.0249 0.0280  13  ASN B O   
2307  C  CB  . ASN B  13  ? 0.0920 0.0696 0.1836 0.0006  -0.0031 0.0333  13  ASN B CB  
2308  C  CG  . ASN B  13  ? 0.0987 0.0778 0.1586 -0.0137 0.0074  0.0277  13  ASN B CG  
2309  O  OD1 . ASN B  13  ? 0.0973 0.0697 0.1766 -0.0024 0.0107  0.0339  13  ASN B OD1 
2310  N  ND2 . ASN B  13  ? 0.0931 0.0987 0.1705 0.0019  0.0141  0.0350  13  ASN B ND2 
2311  N  N   . SER B  14  ? 0.1001 0.0630 0.1680 0.0015  0.0083  0.0460  14  SER B N   
2312  C  CA  . SER B  14  ? 0.1184 0.0639 0.2032 -0.0063 0.0023  0.0425  14  SER B CA  
2313  C  C   . SER B  14  ? 0.1123 0.0694 0.1371 -0.0089 0.0073  0.0167  14  SER B C   
2314  O  O   . SER B  14  ? 0.1296 0.0635 0.1799 -0.0146 0.0000  0.0214  14  SER B O   
2315  C  CB  . SER B  14  ? 0.1185 0.1132 0.1863 -0.0114 0.0245  0.0680  14  SER B CB  
2316  O  OG  . SER B  14  ? 0.1243 0.1105 0.2084 -0.0052 0.0225  0.0527  14  SER B OG  
2317  N  N   . TRP B  15  ? 0.1019 0.0737 0.1484 -0.0142 0.0043  0.0299  15  TRP B N   
2318  C  CA  . TRP B  15  ? 0.1050 0.0757 0.1644 -0.0088 -0.0088 0.0221  15  TRP B CA  
2319  C  C   . TRP B  15  ? 0.1012 0.0888 0.1592 -0.0131 -0.0020 0.0073  15  TRP B C   
2320  O  O   . TRP B  15  ? 0.1252 0.0802 0.1730 -0.0017 0.0173  0.0082  15  TRP B O   
2321  C  CB  . TRP B  15  ? 0.1231 0.0750 0.1412 -0.0322 -0.0057 0.0152  15  TRP B CB  
2322  C  CG  . TRP B  15  ? 0.1059 0.0821 0.1324 -0.0076 -0.0015 0.0162  15  TRP B CG  
2323  C  CD1 . TRP B  15  ? 0.1193 0.0969 0.1395 0.0043  -0.0164 0.0203  15  TRP B CD1 
2324  C  CD2 . TRP B  15  ? 0.0960 0.0635 0.1515 -0.0041 0.0070  0.0240  15  TRP B CD2 
2325  N  NE1 . TRP B  15  ? 0.1094 0.0843 0.1420 -0.0052 -0.0078 0.0209  15  TRP B NE1 
2326  C  CE2 . TRP B  15  ? 0.1019 0.0838 0.1561 0.0041  -0.0055 0.0182  15  TRP B CE2 
2327  C  CE3 . TRP B  15  ? 0.1172 0.0649 0.1358 0.0001  0.0091  0.0175  15  TRP B CE3 
2328  C  CZ2 . TRP B  15  ? 0.1057 0.0798 0.1714 0.0017  -0.0160 0.0498  15  TRP B CZ2 
2329  C  CZ3 . TRP B  15  ? 0.1001 0.0834 0.1461 -0.0044 -0.0087 0.0350  15  TRP B CZ3 
2330  C  CH2 . TRP B  15  ? 0.1306 0.0839 0.1268 0.0098  -0.0156 0.0252  15  TRP B CH2 
2331  N  N   . SER B  16  ? 0.1283 0.0899 0.1517 -0.0294 0.0013  -0.0051 16  SER B N   
2332  C  CA  . SER B  16  ? 0.1457 0.0803 0.1577 -0.0260 -0.0116 0.0190  16  SER B CA  
2333  C  C   . SER B  16  ? 0.1396 0.0780 0.1696 0.0017  -0.0038 0.0137  16  SER B C   
2334  O  O   . SER B  16  ? 0.1624 0.0869 0.2041 -0.0155 0.0021  0.0032  16  SER B O   
2335  C  CB  . SER B  16  ? 0.1727 0.0845 0.2328 -0.0294 -0.0116 0.0650  16  SER B CB  
2336  O  OG  . SER B  16  ? 0.2158 0.1477 0.2308 -0.0144 -0.0172 0.0086  16  SER B OG  
2337  N  N   . LYS B  17  ? 0.1304 0.0857 0.1800 -0.0297 0.0048  0.0242  17  LYS B N   
2338  C  CA  . LYS B  17  ? 0.1468 0.0748 0.1784 -0.0230 -0.0083 0.0190  17  LYS B CA  
2339  C  C   . LYS B  17  ? 0.1387 0.0948 0.2061 -0.0161 0.0137  0.0223  17  LYS B C   
2340  O  O   . LYS B  17  ? 0.1698 0.0820 0.2953 -0.0234 0.0132  -0.0078 17  LYS B O   
2341  C  CB  . LYS B  17  ? 0.1328 0.0839 0.2233 -0.0184 0.0335  0.0059  17  LYS B CB  
2342  C  CG  . LYS B  17  ? 0.1225 0.0948 0.2298 -0.0148 0.0076  0.0377  17  LYS B CG  
2343  C  CD  . LYS B  17  ? 0.1547 0.0631 0.2154 -0.0129 0.0262  0.0181  17  LYS B CD  
2344  C  CE  . LYS B  17  ? 0.1347 0.0732 0.2161 -0.0277 0.0172  0.0142  17  LYS B CE  
2345  N  NZ  . LYS B  17  ? 0.1556 0.1064 0.2005 -0.0249 0.0240  0.0055  17  LYS B NZ  
2346  N  N   . LYS B  18  ? 0.1538 0.0881 0.2021 -0.0054 0.0091  0.0098  18  LYS B N   
2347  C  CA  . LYS B  18  ? 0.1559 0.0773 0.2272 -0.0012 0.0220  0.0308  18  LYS B CA  
2348  C  C   . LYS B  18  ? 0.1581 0.0850 0.2063 0.0142  0.0216  0.0452  18  LYS B C   
2349  O  O   . LYS B  18  ? 0.1730 0.0820 0.3154 0.0140  0.0340  0.0458  18  LYS B O   
2350  C  CB  . LYS B  18  ? 0.1675 0.1870 0.2284 -0.0294 -0.0078 0.0615  18  LYS B CB  
2351  C  CG  . LYS B  18  ? 0.2341 0.3210 0.2673 -0.0970 0.0080  0.0557  18  LYS B CG  
2352  C  CD  . LYS B  18  ? 0.3206 0.4909 0.2440 -0.1121 -0.0355 0.1616  18  LYS B CD  
2353  N  N   . TYR B  19  ? 0.1481 0.0769 0.1881 -0.0071 0.0146  0.0252  19  TYR B N   
2354  C  CA  . TYR B  19  ? 0.1525 0.0848 0.1664 -0.0040 0.0104  0.0080  19  TYR B CA  
2355  C  C   . TYR B  19  ? 0.1450 0.0939 0.1604 -0.0176 0.0173  0.0092  19  TYR B C   
2356  O  O   . TYR B  19  ? 0.1368 0.0903 0.1926 0.0024  0.0109  0.0157  19  TYR B O   
2357  C  CB  . TYR B  19  ? 0.1520 0.0957 0.1884 -0.0154 -0.0035 0.0159  19  TYR B CB  
2358  C  CG  . TYR B  19  ? 0.1470 0.0879 0.1881 -0.0026 -0.0043 0.0215  19  TYR B CG  
2359  C  CD1 . TYR B  19  ? 0.1802 0.1045 0.2463 0.0258  -0.0137 0.0179  19  TYR B CD1 
2360  C  CD2 . TYR B  19  ? 0.1542 0.0868 0.1863 -0.0118 -0.0024 0.0182  19  TYR B CD2 
2361  C  CE1 . TYR B  19  ? 0.2284 0.1240 0.2721 0.0255  -0.0339 0.0414  19  TYR B CE1 
2362  C  CE2 . TYR B  19  ? 0.1965 0.1176 0.2271 -0.0263 -0.0298 0.0216  19  TYR B CE2 
2363  C  CZ  . TYR B  19  ? 0.2380 0.1728 0.2450 0.0296  -0.0439 0.0434  19  TYR B CZ  
2364  O  OH  . TYR B  19  ? 0.3416 0.2032 0.2474 0.0759  -0.0886 0.0159  19  TYR B OH  
2365  N  N   . PRO B  20  ? 0.1859 0.0962 0.1727 -0.0102 0.0000  0.0020  20  PRO B N   
2366  C  CA  . PRO B  20  ? 0.2179 0.1026 0.1978 -0.0445 -0.0211 -0.0030 20  PRO B CA  
2367  C  C   . PRO B  20  ? 0.1698 0.1010 0.1673 -0.0185 -0.0216 -0.0065 20  PRO B C   
2368  O  O   . PRO B  20  ? 0.1696 0.0983 0.2012 -0.0151 -0.0197 -0.0193 20  PRO B O   
2369  C  CB  . PRO B  20  ? 0.3292 0.1088 0.2879 -0.0546 -0.0238 -0.0333 20  PRO B CB  
2370  C  CG  . PRO B  20  ? 0.3508 0.1535 0.2820 0.0331  -0.0538 -0.0533 20  PRO B CG  
2371  C  CD  . PRO B  20  ? 0.2287 0.0906 0.2278 -0.0189 -0.0017 -0.0155 20  PRO B CD  
2372  N  N   . SER B  21  ? 0.1689 0.0927 0.1464 -0.0006 -0.0085 -0.0111 21  SER B N   
2373  C  CA  . SER B  21  ? 0.1756 0.0730 0.1629 -0.0062 -0.0041 -0.0068 21  SER B CA  
2374  C  C   . SER B  21  ? 0.1283 0.0702 0.1341 0.0074  -0.0189 -0.0003 21  SER B C   
2375  O  O   . SER B  21  ? 0.1568 0.0931 0.1533 0.0007  -0.0167 0.0063  21  SER B O   
2376  C  CB  . SER B  21  ? 0.1624 0.0793 0.2008 0.0089  0.0167  -0.0263 21  SER B CB  
2377  O  OG  . SER B  21  ? 0.2138 0.1281 0.2142 0.0265  0.0054  -0.0395 21  SER B OG  
2378  N  N   . CYS B  22  ? 0.1317 0.0918 0.1441 -0.0049 -0.0035 -0.0063 22  CYS B N   
2379  C  CA  . CYS B  22  ? 0.1249 0.0863 0.1720 0.0163  0.0015  -0.0296 22  CYS B CA  
2380  C  C   . CYS B  22  ? 0.1299 0.0755 0.1897 -0.0183 -0.0104 0.0108  22  CYS B C   
2381  O  O   . CYS B  22  ? 0.1378 0.0913 0.1779 0.0048  -0.0161 -0.0001 22  CYS B O   
2382  C  CB  . CYS B  22  ? 0.1304 0.1075 0.1403 -0.0054 -0.0046 0.0008  22  CYS B CB  
2383  S  SG  . CYS B  22  ? 0.1466 0.0874 0.1596 0.0076  -0.0012 0.0132  22  CYS B SG  
2384  N  N   . GLY B  23  ? 0.1288 0.1028 0.1924 0.0031  -0.0307 -0.0118 23  GLY B N   
2385  C  CA  . GLY B  23  ? 0.1414 0.1287 0.1877 0.0217  -0.0212 -0.0104 23  GLY B CA  
2386  C  C   . GLY B  23  ? 0.1734 0.0913 0.1892 -0.0187 -0.0522 0.0024  23  GLY B C   
2387  O  O   . GLY B  23  ? 0.1796 0.1461 0.2017 -0.0142 -0.0568 -0.0010 23  GLY B O   
2388  N  N   . GLY B  24  ? 0.1802 0.1304 0.1793 -0.0220 -0.0350 -0.0049 24  GLY B N   
2389  C  CA  . GLY B  24  ? 0.2208 0.1482 0.1750 -0.0507 -0.0368 0.0119  24  GLY B CA  
2390  C  C   . GLY B  24  ? 0.2958 0.1441 0.1669 -0.0786 -0.0590 -0.0286 24  GLY B C   
2391  O  O   . GLY B  24  ? 0.3208 0.1452 0.1811 -0.0505 -0.0741 0.0217  24  GLY B O   
2392  N  N   . LEU B  25  ? 0.3127 0.1964 0.1608 -0.1044 -0.0606 0.0197  25  LEU B N   
2393  C  CA  . LEU B  25  ? 0.3242 0.2133 0.1822 -0.1298 -0.0460 0.0311  25  LEU B CA  
2394  C  C   . LEU B  25  ? 0.3120 0.1685 0.1653 -0.0772 -0.0478 0.0041  25  LEU B C   
2395  O  O   . LEU B  25  ? 0.2799 0.1353 0.1489 -0.0434 -0.0110 -0.0207 25  LEU B O   
2396  C  CB  . LEU B  25  ? 0.7272 0.3328 0.1475 -0.2892 -0.0668 0.0250  25  LEU B CB  
2397  C  CG  . LEU B  25  ? 0.6481 0.2998 0.2010 -0.2106 -0.1108 0.0357  25  LEU B CG  
2398  C  CD1 . LEU B  25  ? 0.9534 0.4429 0.1770 -0.3097 -0.0412 0.0216  25  LEU B CD1 
2399  C  CD2 . LEU B  25  ? 0.5177 0.3991 0.3230 -0.1541 -0.2230 0.0714  25  LEU B CD2 
2400  N  N   . LEU B  26  ? 0.2540 0.1739 0.1427 -0.0535 -0.0320 0.0350  26  LEU B N   
2401  C  CA  . LEU B  26  ? 0.2500 0.1322 0.1559 -0.0454 -0.0157 0.0063  26  LEU B CA  
2402  C  C   . LEU B  26  ? 0.1789 0.1256 0.1315 -0.0023 -0.0131 0.0188  26  LEU B C   
2403  O  O   . LEU B  26  ? 0.1660 0.1671 0.1331 -0.0115 0.0088  0.0052  26  LEU B O   
2404  C  CB  . LEU B  26  ? 0.3147 0.1868 0.1337 -0.0146 0.0405  -0.0240 26  LEU B CB  
2405  C  CG  . LEU B  26  ? 0.4162 0.3163 0.1676 0.0307  0.1120  0.0408  26  LEU B CG  
2406  C  CD1 . LEU B  26  ? 0.5433 0.5070 0.2364 0.1011  0.1648  -0.0414 26  LEU B CD1 
2407  C  CD2 . LEU B  26  ? 0.5115 0.2493 0.1924 -0.0483 0.0342  0.0842  26  LEU B CD2 
2408  N  N   . GLN B  27  ? 0.1447 0.1233 0.1511 -0.0252 -0.0133 0.0057  27  GLN B N   
2409  C  CA  . GLN B  27  ? 0.1146 0.1010 0.1268 -0.0068 -0.0160 0.0109  27  GLN B CA  
2410  C  C   . GLN B  27  ? 0.1290 0.0852 0.1188 -0.0017 -0.0098 0.0175  27  GLN B C   
2411  O  O   . GLN B  27  ? 0.1509 0.0942 0.1549 0.0046  -0.0236 0.0217  27  GLN B O   
2412  C  CB  . GLN B  27  ? 0.1231 0.0935 0.1678 -0.0102 -0.0034 0.0031  27  GLN B CB  
2413  C  CG  . GLN B  27  ? 0.1253 0.0890 0.1800 -0.0140 -0.0233 0.0070  27  GLN B CG  
2414  C  CD  . GLN B  27  ? 0.1197 0.0852 0.1484 -0.0178 -0.0057 0.0028  27  GLN B CD  
2415  O  OE1 . GLN B  27  ? 0.1471 0.0843 0.1428 -0.0012 -0.0093 0.0063  27  GLN B OE1 
2416  N  NE2 . GLN B  27  ? 0.1513 0.0824 0.1409 -0.0185 -0.0062 -0.0010 27  GLN B NE2 
2417  N  N   . SER B  28  ? 0.1028 0.0863 0.1052 -0.0008 0.0146  -0.0008 28  SER B N   
2418  C  CA  . SER B  28  ? 0.0939 0.0660 0.1014 0.0057  0.0015  0.0129  28  SER B CA  
2419  C  C   . SER B  28  ? 0.0775 0.0794 0.1080 -0.0122 0.0165  0.0259  28  SER B C   
2420  O  O   . SER B  28  ? 0.0890 0.0721 0.1288 -0.0020 0.0142  0.0243  28  SER B O   
2421  C  CB  . SER B  28  ? 0.0865 0.0985 0.0942 0.0098  0.0206  0.0114  28  SER B CB  
2422  O  OG  . SER B  28  ? 0.1111 0.0900 0.0976 0.0097  0.0146  0.0057  28  SER B OG  
2423  N  N   . PRO B  29  ? 0.0839 0.0644 0.1111 0.0049  0.0135  0.0197  29  PRO B N   
2424  C  CA  . PRO B  29  ? 0.0832 0.0658 0.1048 0.0003  0.0116  0.0226  29  PRO B CA  
2425  C  C   . PRO B  29  ? 0.0766 0.0732 0.0904 0.0020  0.0132  0.0059  29  PRO B C   
2426  O  O   . PRO B  29  ? 0.0755 0.0850 0.1086 0.0007  0.0043  0.0214  29  PRO B O   
2427  C  CB  . PRO B  29  ? 0.1012 0.0768 0.0982 -0.0131 0.0333  0.0142  29  PRO B CB  
2428  C  CG  . PRO B  29  ? 0.0940 0.0728 0.1231 -0.0021 0.0223  0.0144  29  PRO B CG  
2429  C  CD  . PRO B  29  ? 0.0904 0.0776 0.1137 -0.0068 0.0231  0.0111  29  PRO B CD  
2430  N  N   . ILE B  30  ? 0.0827 0.0845 0.1107 0.0060  0.0179  0.0299  30  ILE B N   
2431  C  CA  . ILE B  30  ? 0.0680 0.0909 0.1037 -0.0035 0.0201  0.0324  30  ILE B CA  
2432  C  C   . ILE B  30  ? 0.0710 0.0903 0.1174 -0.0005 0.0284  0.0313  30  ILE B C   
2433  O  O   . ILE B  30  ? 0.0897 0.0848 0.1274 0.0068  0.0210  0.0245  30  ILE B O   
2434  C  CB  . ILE B  30  ? 0.0983 0.0998 0.1091 -0.0040 0.0108  0.0258  30  ILE B CB  
2435  C  CG1 . ILE B  30  ? 0.1017 0.1414 0.0987 0.0205  0.0308  0.0428  30  ILE B CG1 
2436  C  CG2 . ILE B  30  ? 0.1835 0.1040 0.1280 0.0099  0.0181  0.0177  30  ILE B CG2 
2437  C  CD1 . ILE B  30  ? 0.1124 0.1924 0.1164 0.0189  0.0337  0.0401  30  ILE B CD1 
2438  N  N   . ASP B  31  ? 0.0872 0.0870 0.1143 0.0104  0.0232  0.0292  31  ASP B N   
2439  C  CA  . ASP B  31  ? 0.0883 0.0917 0.1285 0.0094  0.0267  0.0427  31  ASP B CA  
2440  C  C   . ASP B  31  ? 0.0927 0.1057 0.1141 -0.0013 0.0063  0.0350  31  ASP B C   
2441  O  O   . ASP B  31  ? 0.1276 0.1324 0.1296 -0.0256 0.0006  0.0441  31  ASP B O   
2442  C  CB  . ASP B  31  ? 0.0945 0.0985 0.1651 0.0193  0.0348  0.0469  31  ASP B CB  
2443  C  CG  . ASP B  31  ? 0.1344 0.1310 0.1303 0.0329  0.0074  0.0250  31  ASP B CG  
2444  O  OD1 . ASP B  31  ? 0.1231 0.1134 0.1842 0.0245  -0.0031 0.0379  31  ASP B OD1 
2445  O  OD2 . ASP B  31  ? 0.2066 0.1344 0.1527 0.0342  0.0089  0.0324  31  ASP B OD2 
2446  N  N   . LEU B  32  ? 0.1014 0.1015 0.1367 -0.0093 0.0164  0.0379  32  LEU B N   
2447  C  CA  . LEU B  32  ? 0.1159 0.1270 0.1335 -0.0114 0.0148  0.0612  32  LEU B CA  
2448  C  C   . LEU B  32  ? 0.1057 0.1279 0.1473 -0.0390 0.0021  0.0434  32  LEU B C   
2449  O  O   . LEU B  32  ? 0.1872 0.1179 0.1617 -0.0196 -0.0251 0.0406  32  LEU B O   
2450  C  CB  . LEU B  32  ? 0.1342 0.1391 0.1283 -0.0218 0.0186  0.0458  32  LEU B CB  
2451  C  CG  . LEU B  32  ? 0.1059 0.1416 0.1410 -0.0231 0.0260  0.0474  32  LEU B CG  
2452  C  CD1 . LEU B  32  ? 0.0890 0.2072 0.1981 -0.0179 0.0176  0.0421  32  LEU B CD1 
2453  C  CD2 . LEU B  32  ? 0.1763 0.2226 0.1592 -0.0165 0.0406  0.0115  32  LEU B CD2 
2454  N  N   . HIS B  33  ? 0.1258 0.1324 0.1402 -0.0236 0.0043  0.0590  33  HIS B N   
2455  C  CA  . HIS B  33  ? 0.1315 0.1597 0.1382 -0.0088 0.0010  0.0763  33  HIS B CA  
2456  C  C   . HIS B  33  ? 0.1290 0.1404 0.1488 -0.0322 -0.0097 0.0439  33  HIS B C   
2457  O  O   . HIS B  33  ? 0.1184 0.1551 0.1520 -0.0206 0.0115  0.0619  33  HIS B O   
2458  C  CB  . HIS B  33  ? 0.1265 0.2048 0.1346 -0.0265 0.0177  0.0443  33  HIS B CB  
2459  C  CG  . HIS B  33  ? 0.1177 0.1736 0.1468 -0.0307 0.0129  0.0776  33  HIS B CG  
2460  N  ND1 . HIS B  33  ? 0.2019 0.2084 0.1811 -0.0947 -0.0518 0.1105  33  HIS B ND1 
2461  C  CD2 . HIS B  33  ? 0.1322 0.2000 0.1423 -0.0096 0.0142  0.0776  33  HIS B CD2 
2462  C  CE1 . HIS B  33  ? 0.2344 0.2199 0.2050 -0.0612 -0.0797 0.0997  33  HIS B CE1 
2463  N  NE2 . HIS B  33  ? 0.1405 0.1994 0.1701 -0.0190 -0.0041 0.0697  33  HIS B NE2 
2464  N  N   . SER B  34  ? 0.1335 0.1416 0.1658 -0.0098 -0.0019 0.0680  34  SER B N   
2465  C  CA  . SER B  34  ? 0.1278 0.1899 0.1887 -0.0296 -0.0278 0.1004  34  SER B CA  
2466  C  C   . SER B  34  ? 0.1280 0.2222 0.1209 -0.0287 0.0144  0.0873  34  SER B C   
2467  O  O   . SER B  34  ? 0.1421 0.2179 0.1753 -0.0188 0.0265  0.1001  34  SER B O   
2468  C  CB  . SER B  34  ? 0.2522 0.2362 0.2402 0.0247  0.0083  0.1640  34  SER B CB  
2469  O  OG  . SER B  34  ? 0.2833 0.2617 0.2440 0.0355  0.0283  0.0619  34  SER B OG  
2470  N  N   . ASP B  35  ? 0.1055 0.2238 0.1332 -0.0165 0.0124  0.0537  35  ASP B N   
2471  C  CA  . ASP B  35  ? 0.1118 0.2337 0.1260 0.0031  0.0068  0.0659  35  ASP B CA  
2472  C  C   . ASP B  35  ? 0.1437 0.2623 0.1391 -0.0046 0.0168  0.0454  35  ASP B C   
2473  O  O   . ASP B  35  ? 0.1610 0.3160 0.1351 0.0300  0.0156  0.0206  35  ASP B O   
2474  C  CB  . ASP B  35  ? 0.1094 0.2472 0.1674 0.0030  0.0248  0.0680  35  ASP B CB  
2475  C  CG  . ASP B  35  ? 0.1453 0.2452 0.1429 -0.0195 -0.0032 0.0728  35  ASP B CG  
2476  O  OD1 . ASP B  35  ? 0.1401 0.2486 0.1597 0.0199  0.0181  0.0328  35  ASP B OD1 
2477  O  OD2 . ASP B  35  ? 0.1403 0.2790 0.1754 -0.0015 0.0135  0.0872  35  ASP B OD2 
2478  N  N   . ILE B  36  ? 0.1024 0.2054 0.1586 -0.0120 0.0189  0.0601  36  ILE B N   
2479  C  CA  . ILE B  36  ? 0.1106 0.2440 0.1246 -0.0148 0.0217  0.0366  36  ILE B CA  
2480  C  C   . ILE B  36  ? 0.1258 0.2249 0.1439 -0.0220 -0.0060 0.0644  36  ILE B C   
2481  O  O   . ILE B  36  ? 0.1402 0.2186 0.1687 0.0159  0.0108  0.0288  36  ILE B O   
2482  C  CB  . ILE B  36  ? 0.1412 0.2533 0.1775 -0.0186 0.0320  0.0604  36  ILE B CB  
2483  C  CG1 . ILE B  36  ? 0.3540 0.1694 0.1247 -0.0003 0.0500  0.0623  36  ILE B CG1 
2484  C  CG2 . ILE B  36  ? 0.1705 0.2958 0.2086 -0.0373 0.0324  0.0267  36  ILE B CG2 
2485  C  CD1 . ILE B  36  ? 0.3077 0.4002 0.2800 0.1055  0.0035  0.0456  36  ILE B CD1 
2486  N  N   . LEU B  37  ? 0.1052 0.2048 0.1288 -0.0280 0.0172  0.0671  37  LEU B N   
2487  C  CA  . LEU B  37  ? 0.1098 0.2108 0.1276 -0.0052 0.0126  0.0549  37  LEU B CA  
2488  C  C   . LEU B  37  ? 0.1229 0.2016 0.1326 0.0000  0.0040  0.1008  37  LEU B C   
2489  O  O   . LEU B  37  ? 0.1373 0.2985 0.1678 0.0359  0.0285  0.1459  37  LEU B O   
2490  C  CB  . LEU B  37  ? 0.1116 0.1809 0.1730 -0.0082 0.0044  0.0571  37  LEU B CB  
2491  C  CG  . LEU B  37  ? 0.1111 0.2310 0.1622 0.0129  0.0195  0.0348  37  LEU B CG  
2492  C  CD1 . LEU B  37  ? 0.1712 0.1875 0.2800 0.0256  -0.0307 0.0044  37  LEU B CD1 
2493  C  CD2 . LEU B  37  ? 0.1728 0.1881 0.1525 0.0008  0.0070  0.0472  37  LEU B CD2 
2494  N  N   . GLN B  38  ? 0.1100 0.2269 0.1395 0.0080  0.0311  0.0771  38  GLN B N   
2495  C  CA  . GLN B  38  ? 0.1371 0.2754 0.0967 0.0074  0.0242  0.0560  38  GLN B CA  
2496  C  C   . GLN B  38  ? 0.1301 0.2422 0.0949 0.0129  0.0313  0.0658  38  GLN B C   
2497  O  O   . GLN B  38  ? 0.1418 0.2303 0.1041 0.0078  0.0167  0.0833  38  GLN B O   
2498  C  CB  . GLN B  38  ? 0.1369 0.3921 0.1124 -0.0124 0.0060  0.0137  38  GLN B CB  
2499  C  CG  . GLN B  38  ? 0.2310 0.5216 0.1296 -0.0307 0.0003  0.0428  38  GLN B CG  
2500  C  CD  . GLN B  38  ? 0.3174 0.5831 0.1544 0.0287  -0.0656 0.0109  38  GLN B CD  
2501  O  OE1 . GLN B  38  ? 0.3835 0.8467 0.2289 0.0000  -0.0463 -0.0851 38  GLN B OE1 
2502  N  NE2 . GLN B  38  ? 0.4126 0.5034 0.3125 0.0728  -0.0659 0.0724  38  GLN B NE2 
2503  N  N   . TYR B  39  ? 0.1308 0.2014 0.1353 0.0294  0.0452  0.0854  39  TYR B N   
2504  C  CA  . TYR B  39  ? 0.1360 0.1734 0.1070 0.0252  0.0553  0.0662  39  TYR B CA  
2505  C  C   . TYR B  39  ? 0.1436 0.1985 0.0794 0.0361  0.0299  0.0685  39  TYR B C   
2506  O  O   . TYR B  39  ? 0.1592 0.2078 0.0879 0.0392  0.0216  0.0427  39  TYR B O   
2507  C  CB  . TYR B  39  ? 0.1874 0.1605 0.1752 0.0265  0.0617  0.0987  39  TYR B CB  
2508  C  CG  . TYR B  39  ? 0.2036 0.1290 0.1418 0.0287  0.0678  0.0568  39  TYR B CG  
2509  C  CD1 . TYR B  39  ? 0.1826 0.1766 0.1581 0.0335  0.0527  0.0674  39  TYR B CD1 
2510  C  CD2 . TYR B  39  ? 0.2190 0.1401 0.1430 0.0024  0.0520  0.0808  39  TYR B CD2 
2511  C  CE1 . TYR B  39  ? 0.2215 0.1747 0.1416 -0.0028 0.0571  0.0612  39  TYR B CE1 
2512  C  CE2 . TYR B  39  ? 0.2037 0.1860 0.1368 0.0054  0.0494  0.0722  39  TYR B CE2 
2513  C  CZ  . TYR B  39  ? 0.1915 0.2073 0.1432 0.0035  0.0252  0.0771  39  TYR B CZ  
2514  O  OH  . TYR B  39  ? 0.2334 0.2129 0.1992 -0.0179 0.0706  0.0694  39  TYR B OH  
2515  N  N   . ASP B  40  ? 0.1461 0.1586 0.0886 0.0269  0.0364  0.0355  40  ASP B N   
2516  C  CA  . ASP B  40  ? 0.1541 0.1928 0.1057 0.0542  0.0329  0.0271  40  ASP B CA  
2517  C  C   . ASP B  40  ? 0.1577 0.1650 0.0940 0.0225  0.0239  0.0379  40  ASP B C   
2518  O  O   . ASP B  40  ? 0.1272 0.1983 0.1052 0.0234  0.0348  0.0320  40  ASP B O   
2519  C  CB  . ASP B  40  ? 0.1799 0.1664 0.1253 0.0434  0.0322  0.0372  40  ASP B CB  
2520  C  CG  . ASP B  40  ? 0.1984 0.1922 0.1605 0.0353  0.0403  0.0173  40  ASP B CG  
2521  O  OD1 . ASP B  40  ? 0.2170 0.2538 0.1495 0.0342  0.0476  -0.0204 40  ASP B OD1 
2522  O  OD2 . ASP B  40  ? 0.3021 0.2190 0.3258 0.0306  0.0780  -0.0434 40  ASP B OD2 
2523  N  N   . ALA B  41  ? 0.1500 0.1946 0.1262 0.0232  0.0608  0.0482  41  ALA B N   
2524  C  CA  . ALA B  41  ? 0.1840 0.2007 0.1386 0.0170  0.0729  0.0434  41  ALA B CA  
2525  C  C   . ALA B  41  ? 0.1421 0.2105 0.1450 0.0188  0.0908  0.0289  41  ALA B C   
2526  O  O   . ALA B  41  ? 0.1757 0.2542 0.1642 0.0144  0.0813  0.0386  41  ALA B O   
2527  C  CB  . ALA B  41  ? 0.2324 0.2012 0.1351 -0.0125 0.0619  0.0621  41  ALA B CB  
2528  N  N   A SER B  42  ? 0.2084 0.2154 0.1003 0.0421  0.0610  0.0031  42  SER B N   
2529  N  N   B SER B  42  ? 0.1700 0.2154 0.1376 0.0366  0.0635  0.0197  42  SER B N   
2530  C  CA  A SER B  42  ? 0.2082 0.2233 0.1526 0.0507  0.0329  -0.0188 42  SER B CA  
2531  C  CA  B SER B  42  ? 0.1993 0.2285 0.1080 0.0672  0.0927  0.0052  42  SER B CA  
2532  C  C   A SER B  42  ? 0.1640 0.1917 0.1515 0.0531  0.0401  0.0020  42  SER B C   
2533  C  C   B SER B  42  ? 0.1787 0.1791 0.1310 0.0300  0.0807  0.0487  42  SER B C   
2534  O  O   A SER B  42  ? 0.1592 0.2402 0.1975 0.0432  0.0127  -0.0116 42  SER B O   
2535  O  O   B SER B  42  ? 0.1632 0.1535 0.1511 0.0144  0.0381  -0.0015 42  SER B O   
2536  C  CB  A SER B  42  ? 0.3483 0.3291 0.1109 -0.0454 0.0107  -0.0408 42  SER B CB  
2537  C  CB  B SER B  42  ? 0.2073 0.2533 0.2185 0.1313  0.0663  -0.0560 42  SER B CB  
2538  O  OG  A SER B  42  ? 0.2635 0.2287 0.2354 0.0307  0.0313  -0.0714 42  SER B OG  
2539  O  OG  B SER B  42  ? 0.2709 0.2930 0.1870 0.0657  0.0458  -0.0738 42  SER B OG  
2540  N  N   . LEU B  43  ? 0.1649 0.2003 0.1136 0.0236  0.0535  0.0277  43  LEU B N   
2541  C  CA  . LEU B  43  ? 0.1547 0.2001 0.1303 0.0120  0.0308  0.0566  43  LEU B CA  
2542  C  C   . LEU B  43  ? 0.1421 0.1808 0.1685 0.0296  0.0471  0.0702  43  LEU B C   
2543  O  O   . LEU B  43  ? 0.1635 0.1984 0.1753 0.0124  0.0151  0.0511  43  LEU B O   
2544  C  CB  . LEU B  43  ? 0.1457 0.1802 0.1062 0.0027  0.0406  0.0230  43  LEU B CB  
2545  C  CG  . LEU B  43  ? 0.1473 0.1374 0.1156 0.0044  0.0115  0.0337  43  LEU B CG  
2546  C  CD1 . LEU B  43  ? 0.1748 0.1911 0.1109 0.0219  0.0248  0.0212  43  LEU B CD1 
2547  C  CD2 . LEU B  43  ? 0.2020 0.1621 0.1396 -0.0043 0.0103  0.0412  43  LEU B CD2 
2548  N  N   . THR B  44  ? 0.1281 0.2381 0.1793 0.0237  0.0719  0.0798  44  THR B N   
2549  C  CA  . THR B  44  ? 0.1597 0.2687 0.1739 0.0164  0.0724  0.0898  44  THR B CA  
2550  C  C   . THR B  44  ? 0.1059 0.2538 0.2266 0.0162  0.0675  0.1132  44  THR B C   
2551  O  O   . THR B  44  ? 0.1185 0.2190 0.2050 0.0165  0.0432  0.0777  44  THR B O   
2552  C  CB  . THR B  44  ? 0.1872 0.4065 0.2082 0.0129  0.1061  0.1331  44  THR B CB  
2553  O  OG1 . THR B  44  ? 0.2174 0.4266 0.3014 0.1250  0.1360  0.1356  44  THR B OG1 
2554  C  CG2 . THR B  44  ? 0.1624 0.5447 0.2583 0.0249  0.0974  0.1995  44  THR B CG2 
2555  N  N   . PRO B  45  ? 0.1400 0.2879 0.2014 -0.0096 0.0292  0.1280  45  PRO B N   
2556  C  CA  . PRO B  45  ? 0.1347 0.2470 0.1903 0.0307  0.0122  0.0712  45  PRO B CA  
2557  C  C   . PRO B  45  ? 0.0694 0.2989 0.1974 0.0164  0.0505  0.0935  45  PRO B C   
2558  O  O   . PRO B  45  ? 0.1256 0.3709 0.2375 0.0662  0.0866  0.1512  45  PRO B O   
2559  C  CB  . PRO B  45  ? 0.2185 0.2127 0.2906 -0.0608 0.0052  0.0878  45  PRO B CB  
2560  C  CG  . PRO B  45  ? 0.1773 0.2712 0.3151 -0.0104 -0.0038 0.1181  45  PRO B CG  
2561  C  CD  . PRO B  45  ? 0.2020 0.3580 0.2370 -0.0899 0.0310  0.1409  45  PRO B CD  
2562  N  N   . LEU B  46  ? 0.1163 0.2407 0.1552 0.0124  0.0259  0.0531  46  LEU B N   
2563  C  CA  . LEU B  46  ? 0.1123 0.2418 0.1696 0.0144  0.0046  0.0870  46  LEU B CA  
2564  C  C   . LEU B  46  ? 0.1416 0.1897 0.1721 0.0126  0.0243  0.0948  46  LEU B C   
2565  O  O   . LEU B  46  ? 0.1073 0.2073 0.2406 0.0031  0.0173  0.0741  46  LEU B O   
2566  C  CB  . LEU B  46  ? 0.0960 0.2217 0.2201 -0.0082 0.0242  0.0527  46  LEU B CB  
2567  C  CG  . LEU B  46  ? 0.1154 0.2397 0.2509 0.0147  0.0344  0.0118  46  LEU B CG  
2568  C  CD1 . LEU B  46  ? 0.1463 0.2791 0.2718 -0.0156 0.0608  0.0355  46  LEU B CD1 
2569  C  CD2 . LEU B  46  ? 0.1473 0.3594 0.2804 0.0178  0.0073  -0.0674 46  LEU B CD2 
2570  N  N   . GLU B  47  ? 0.1328 0.2175 0.1410 0.0210  0.0126  0.0690  47  GLU B N   
2571  C  CA  . GLU B  47  ? 0.1292 0.2786 0.1556 -0.0171 0.0131  0.1130  47  GLU B CA  
2572  C  C   . GLU B  47  ? 0.1353 0.1883 0.1468 0.0000  0.0066  0.0608  47  GLU B C   
2573  O  O   . GLU B  47  ? 0.1947 0.1976 0.1579 0.0070  0.0384  0.0449  47  GLU B O   
2574  C  CB  . GLU B  47  ? 0.1256 0.3147 0.2236 -0.0001 0.0320  0.1295  47  GLU B CB  
2575  C  CG  . GLU B  47  ? 0.1638 0.3591 0.2594 -0.0164 0.0826  0.1655  47  GLU B CG  
2576  C  CD  . GLU B  47  ? 0.2570 0.4867 0.2377 -0.0292 0.0975  0.1894  47  GLU B CD  
2577  O  OE1 . GLU B  47  ? 0.4029 1.0375 0.3287 -0.1467 0.0830  0.0038  47  GLU B OE1 
2578  O  OE2 . GLU B  47  ? 0.2125 0.8305 0.6067 0.0452  0.1136  0.1403  47  GLU B OE2 
2579  N  N   . PHE B  48  ? 0.1154 0.1917 0.1599 0.0093  0.0114  0.0719  48  PHE B N   
2580  C  CA  . PHE B  48  ? 0.1321 0.1770 0.1351 0.0096  0.0104  0.0509  48  PHE B CA  
2581  C  C   . PHE B  48  ? 0.1159 0.1658 0.1768 0.0119  0.0153  0.0513  48  PHE B C   
2582  O  O   . PHE B  48  ? 0.1732 0.2050 0.2552 -0.0073 -0.0285 0.0549  48  PHE B O   
2583  C  CB  . PHE B  48  ? 0.1669 0.1947 0.1699 0.0430  0.0419  0.0631  48  PHE B CB  
2584  C  CG  . PHE B  48  ? 0.1687 0.2118 0.1305 0.0153  0.0438  0.0555  48  PHE B CG  
2585  C  CD1 . PHE B  48  ? 0.1310 0.1980 0.1574 0.0076  0.0564  0.0557  48  PHE B CD1 
2586  C  CD2 . PHE B  48  ? 0.2011 0.1826 0.1716 0.0333  0.0445  0.0689  48  PHE B CD2 
2587  C  CE1 . PHE B  48  ? 0.1193 0.2145 0.1887 0.0203  0.0694  0.0747  48  PHE B CE1 
2588  C  CE2 . PHE B  48  ? 0.1601 0.2400 0.2037 0.0277  0.0505  0.0834  48  PHE B CE2 
2589  C  CZ  . PHE B  48  ? 0.1342 0.2481 0.1861 0.0293  0.0800  0.1106  48  PHE B CZ  
2590  N  N   . GLN B  49  ? 0.1238 0.1838 0.1623 0.0212  0.0355  0.0568  49  GLN B N   
2591  C  CA  . GLN B  49  ? 0.1204 0.1953 0.1615 0.0270  0.0496  0.0593  49  GLN B CA  
2592  C  C   . GLN B  49  ? 0.0992 0.1791 0.1480 0.0148  0.0364  0.0441  49  GLN B C   
2593  O  O   . GLN B  49  ? 0.1021 0.1870 0.1523 0.0054  0.0272  0.0386  49  GLN B O   
2594  C  CB  . GLN B  49  ? 0.1659 0.2515 0.1534 0.0560  0.0593  0.0597  49  GLN B CB  
2595  C  CG  . GLN B  49  ? 0.1635 0.2847 0.1949 0.0148  0.0970  0.1055  49  GLN B CG  
2596  C  CD  . GLN B  49  ? 0.1145 0.3276 0.1362 -0.0093 0.0109  0.1349  49  GLN B CD  
2597  O  OE1 . GLN B  49  ? 0.1608 0.3524 0.4131 0.0403  0.0597  0.2477  49  GLN B OE1 
2598  N  NE2 . GLN B  49  ? 0.1100 0.3695 0.3583 0.0383  0.0432  0.1780  49  GLN B NE2 
2599  N  N   . GLY B  50  ? 0.1062 0.2300 0.1534 0.0132  0.0348  0.0584  50  GLY B N   
2600  C  CA  . GLY B  50  ? 0.1010 0.2235 0.1714 0.0174  0.0397  0.0417  50  GLY B CA  
2601  C  C   . GLY B  50  ? 0.0804 0.2325 0.1262 0.0185  0.0125  0.0627  50  GLY B C   
2602  O  O   . GLY B  50  ? 0.1030 0.2037 0.1829 0.0370  0.0274  0.0614  50  GLY B O   
2603  N  N   . TYR B  51  ? 0.0958 0.1892 0.1243 0.0008  0.0214  0.0392  51  TYR B N   
2604  C  CA  . TYR B  51  ? 0.0723 0.1556 0.1455 -0.0153 0.0216  0.0337  51  TYR B CA  
2605  C  C   . TYR B  51  ? 0.0892 0.1525 0.1369 0.0023  -0.0015 0.0454  51  TYR B C   
2606  O  O   . TYR B  51  ? 0.0924 0.1563 0.1477 -0.0037 0.0102  0.0368  51  TYR B O   
2607  C  CB  . TYR B  51  ? 0.0834 0.1396 0.1412 -0.0153 0.0068  0.0379  51  TYR B CB  
2608  C  CG  . TYR B  51  ? 0.0954 0.1319 0.1125 -0.0194 0.0220  0.0460  51  TYR B CG  
2609  C  CD1 . TYR B  51  ? 0.1032 0.1436 0.1121 -0.0006 0.0081  0.0275  51  TYR B CD1 
2610  C  CD2 . TYR B  51  ? 0.0790 0.1362 0.1240 -0.0115 0.0197  0.0632  51  TYR B CD2 
2611  C  CE1 . TYR B  51  ? 0.1161 0.1493 0.1003 0.0168  0.0277  0.0264  51  TYR B CE1 
2612  C  CE2 . TYR B  51  ? 0.1044 0.1202 0.1228 -0.0065 0.0186  0.0228  51  TYR B CE2 
2613  C  CZ  . TYR B  51  ? 0.1003 0.1488 0.1177 0.0065  0.0100  0.0098  51  TYR B CZ  
2614  O  OH  . TYR B  51  ? 0.1179 0.1425 0.1411 0.0199  -0.0129 0.0124  51  TYR B OH  
2615  N  N   . ASN B  52  ? 0.0939 0.1734 0.1579 -0.0239 -0.0076 0.0533  52  ASN B N   
2616  C  CA  . ASN B  52  ? 0.1005 0.2055 0.1646 -0.0410 -0.0335 0.0608  52  ASN B CA  
2617  C  C   . ASN B  52  ? 0.0910 0.2172 0.1484 -0.0104 0.0171  0.0425  52  ASN B C   
2618  O  O   . ASN B  52  ? 0.0861 0.3043 0.2486 -0.0038 0.0102  0.1246  52  ASN B O   
2619  C  CB  . ASN B  52  ? 0.1276 0.1969 0.2321 -0.0538 -0.0223 0.0727  52  ASN B CB  
2620  C  CG  . ASN B  52  ? 0.1567 0.2398 0.2585 -0.0692 -0.0372 0.0443  52  ASN B CG  
2621  O  OD1 . ASN B  52  ? 0.3490 0.4397 0.2343 -0.2487 -0.0719 0.0927  52  ASN B OD1 
2622  N  ND2 . ASN B  52  ? 0.1567 0.2703 0.3429 -0.0579 0.0120  -0.0059 52  ASN B ND2 
2623  N  N   . LEU B  53  ? 0.0924 0.1905 0.1393 -0.0087 -0.0012 0.0394  53  LEU B N   
2624  C  CA  . LEU B  53  ? 0.1179 0.1820 0.1337 -0.0054 -0.0081 0.0348  53  LEU B CA  
2625  C  C   . LEU B  53  ? 0.0930 0.1939 0.1535 -0.0164 0.0010  0.0164  53  LEU B C   
2626  O  O   . LEU B  53  ? 0.1328 0.2091 0.1633 -0.0113 -0.0163 0.0211  53  LEU B O   
2627  C  CB  . LEU B  53  ? 0.1228 0.1535 0.1709 -0.0118 -0.0196 0.0419  53  LEU B CB  
2628  C  CG  . LEU B  53  ? 0.1215 0.1735 0.2014 -0.0261 -0.0300 0.0544  53  LEU B CG  
2629  C  CD1 . LEU B  53  ? 0.1558 0.1748 0.2682 -0.0362 -0.0445 0.0810  53  LEU B CD1 
2630  C  CD2 . LEU B  53  ? 0.2402 0.2231 0.2032 -0.0135 -0.0474 0.0113  53  LEU B CD2 
2631  N  N   . SER B  54  ? 0.0922 0.2334 0.1466 -0.0026 0.0010  0.0579  54  SER B N   
2632  C  CA  . SER B  54  ? 0.1163 0.2858 0.1617 -0.0297 -0.0125 0.0811  54  SER B CA  
2633  C  C   . SER B  54  ? 0.0827 0.2463 0.1826 -0.0273 -0.0013 0.0672  54  SER B C   
2634  O  O   . SER B  54  ? 0.1106 0.2141 0.1493 -0.0092 0.0000  0.0346  54  SER B O   
2635  C  CB  . SER B  54  ? 0.0942 0.4566 0.1495 0.0315  -0.0205 0.0926  54  SER B CB  
2636  O  OG  . SER B  54  ? 0.1226 0.3971 0.1490 -0.0248 0.0104  0.0819  54  SER B OG  
2637  N  N   . ALA B  55  ? 0.2061 0.1958 0.1833 -0.0729 -0.0553 0.0945  55  ALA B N   
2638  C  CA  . ALA B  55  ? 0.2157 0.2105 0.2007 -0.0571 -0.0537 0.0636  55  ALA B CA  
2639  C  C   . ALA B  55  ? 0.1504 0.2021 0.1667 -0.0403 -0.0183 0.0509  55  ALA B C   
2640  O  O   . ALA B  55  ? 0.1939 0.2551 0.1796 -0.0026 0.0165  0.0256  55  ALA B O   
2641  C  CB  . ALA B  55  ? 0.3628 0.2312 0.2953 -0.0258 -0.1395 0.0170  55  ALA B CB  
2642  N  N   . ASN B  56  ? 0.1253 0.2249 0.1782 -0.0432 -0.0305 0.0447  56  ASN B N   
2643  C  CA  . ASN B  56  ? 0.1337 0.2454 0.1637 -0.0087 -0.0013 0.0417  56  ASN B CA  
2644  C  C   . ASN B  56  ? 0.1360 0.2052 0.1235 0.0052  0.0232  0.0395  56  ASN B C   
2645  O  O   . ASN B  56  ? 0.1863 0.2490 0.2122 -0.0094 -0.0274 0.0842  56  ASN B O   
2646  C  CB  . ASN B  56  ? 0.1089 0.3210 0.1852 -0.0337 -0.0185 0.0601  56  ASN B CB  
2647  C  CG  . ASN B  56  ? 0.1225 0.3946 0.3260 -0.0575 0.0000  -0.0195 56  ASN B CG  
2648  O  OD1 . ASN B  56  ? 0.2352 0.3246 0.2939 -0.0491 -0.0340 0.0408  56  ASN B OD1 
2649  N  ND2 . ASN B  56  ? 0.1858 0.3946 0.4113 -0.0824 0.0478  0.0441  56  ASN B ND2 
2650  N  N   . LYS B  57  ? 0.1129 0.1956 0.1698 0.0060  0.0152  0.0337  57  LYS B N   
2651  C  CA  . LYS B  57  ? 0.1251 0.1881 0.1613 0.0231  0.0125  0.0439  57  LYS B CA  
2652  C  C   . LYS B  57  ? 0.1211 0.1678 0.1586 0.0267  -0.0076 0.0625  57  LYS B C   
2653  O  O   . LYS B  57  ? 0.1163 0.1800 0.1694 0.0240  0.0120  0.0590  57  LYS B O   
2654  C  CB  . LYS B  57  ? 0.1439 0.2284 0.1838 0.0181  0.0593  0.0300  57  LYS B CB  
2655  C  CG  . LYS B  57  ? 0.1867 0.3772 0.2068 0.0644  0.0811  0.0408  57  LYS B CG  
2656  C  CD  . LYS B  57  ? 0.3409 0.5200 0.2671 0.1636  0.0974  -0.0131 57  LYS B CD  
2657  C  CE  . LYS B  57  ? 0.6499 0.5939 0.4738 0.1150  0.0496  -0.2872 57  LYS B CE  
2658  N  NZ  . LYS B  57  ? 0.2152 0.6141 0.5307 0.0089  0.0958  -0.1585 57  LYS B NZ  
2659  N  N   . GLN B  58  ? 0.1249 0.1941 0.1696 -0.0078 -0.0108 0.0333  58  GLN B N   
2660  C  CA  . GLN B  58  ? 0.1116 0.2359 0.1509 -0.0262 -0.0142 0.0500  58  GLN B CA  
2661  C  C   . GLN B  58  ? 0.1410 0.1644 0.1577 0.0120  -0.0049 0.0392  58  GLN B C   
2662  O  O   . GLN B  58  ? 0.1360 0.1644 0.2091 0.0104  -0.0122 0.0383  58  GLN B O   
2663  C  CB  . GLN B  58  ? 0.1948 0.3201 0.1387 -0.0088 -0.0231 0.0436  58  GLN B CB  
2664  C  CG  . GLN B  58  ? 0.3434 0.2260 0.2558 0.0276  0.0599  0.0806  58  GLN B CG  
2665  C  CD  . GLN B  58  ? 0.3560 0.3824 0.2529 0.0815  -0.0242 0.0562  58  GLN B CD  
2666  O  OE1 . GLN B  58  ? 0.2635 0.4014 0.2908 -0.0091 -0.0684 0.0668  58  GLN B OE1 
2667  N  NE2 . GLN B  58  ? 0.3982 0.4092 0.2547 0.1061  0.0483  0.1262  58  GLN B NE2 
2668  N  N   . PHE B  59  ? 0.1216 0.1759 0.1351 -0.0200 -0.0218 0.0628  59  PHE B N   
2669  C  CA  . PHE B  59  ? 0.1292 0.1502 0.1055 -0.0105 0.0030  0.0373  59  PHE B CA  
2670  C  C   . PHE B  59  ? 0.1177 0.1509 0.1057 -0.0104 -0.0146 0.0348  59  PHE B C   
2671  O  O   . PHE B  59  ? 0.1319 0.1757 0.1014 -0.0283 0.0003  0.0289  59  PHE B O   
2672  C  CB  . PHE B  59  ? 0.1292 0.1678 0.1184 -0.0114 0.0034  0.0644  59  PHE B CB  
2673  C  CG  . PHE B  59  ? 0.1111 0.1629 0.1176 0.0049  0.0093  0.0467  59  PHE B CG  
2674  C  CD1 . PHE B  59  ? 0.1064 0.1455 0.1604 0.0071  -0.0034 0.0698  59  PHE B CD1 
2675  C  CD2 . PHE B  59  ? 0.1448 0.1772 0.1133 0.0210  0.0028  0.0392  59  PHE B CD2 
2676  C  CE1 . PHE B  59  ? 0.1328 0.1759 0.1624 0.0220  0.0153  0.0658  59  PHE B CE1 
2677  C  CE2 . PHE B  59  ? 0.1314 0.2044 0.1376 0.0272  0.0115  0.0317  59  PHE B CE2 
2678  C  CZ  . PHE B  59  ? 0.1466 0.2172 0.1576 0.0273  -0.0080 0.0520  59  PHE B CZ  
2679  N  N   . LEU B  60  ? 0.1111 0.1502 0.1416 -0.0120 -0.0103 0.0438  60  LEU B N   
2680  C  CA  . LEU B  60  ? 0.1281 0.1432 0.1407 -0.0359 -0.0175 0.0373  60  LEU B CA  
2681  C  C   . LEU B  60  ? 0.1299 0.1357 0.1023 -0.0089 0.0000  0.0428  60  LEU B C   
2682  O  O   . LEU B  60  ? 0.1414 0.2023 0.0958 -0.0049 -0.0078 0.0491  60  LEU B O   
2683  C  CB  . LEU B  60  ? 0.1716 0.1620 0.1899 -0.0362 -0.0159 0.0653  60  LEU B CB  
2684  C  CG  . LEU B  60  ? 0.2515 0.1605 0.2585 -0.0082 0.0467  0.0860  60  LEU B CG  
2685  C  CD1 . LEU B  60  ? 0.2337 0.2994 0.2903 -0.0013 0.0461  0.1339  60  LEU B CD1 
2686  C  CD2 . LEU B  60  ? 0.3386 0.2345 0.3210 -0.1063 0.0172  0.0518  60  LEU B CD2 
2687  N  N   . LEU B  61  ? 0.1019 0.2174 0.0940 -0.0295 -0.0024 0.0348  61  LEU B N   
2688  C  CA  . LEU B  61  ? 0.1140 0.2001 0.0988 -0.0277 0.0131  0.0531  61  LEU B CA  
2689  C  C   . LEU B  61  ? 0.1513 0.2123 0.0821 -0.0416 -0.0118 0.0502  61  LEU B C   
2690  O  O   . LEU B  61  ? 0.1754 0.2664 0.1027 -0.0641 -0.0195 0.0817  61  LEU B O   
2691  C  CB  . LEU B  61  ? 0.1508 0.2434 0.0970 -0.0285 0.0153  0.0118  61  LEU B CB  
2692  C  CG  . LEU B  61  ? 0.1800 0.2037 0.0938 -0.0399 0.0196  -0.0034 61  LEU B CG  
2693  C  CD1 . LEU B  61  ? 0.1926 0.2508 0.1277 0.0115  0.0236  0.0137  61  LEU B CD1 
2694  C  CD2 . LEU B  61  ? 0.2255 0.2599 0.1066 -0.0560 0.0284  -0.0186 61  LEU B CD2 
2695  N  N   . THR B  62  ? 0.1353 0.2438 0.0970 -0.0557 0.0008  0.0562  62  THR B N   
2696  C  CA  . THR B  62  ? 0.1430 0.2962 0.1387 -0.0905 0.0003  0.0952  62  THR B CA  
2697  C  C   . THR B  62  ? 0.1619 0.2958 0.0994 -0.1127 0.0043  0.0732  62  THR B C   
2698  O  O   . THR B  62  ? 0.1423 0.4338 0.1280 -0.0824 -0.0007 0.1137  62  THR B O   
2699  C  CB  . THR B  62  ? 0.2637 0.2994 0.3892 -0.1377 0.0542  0.0654  62  THR B CB  
2700  O  OG1 . THR B  62  ? 0.3059 0.3174 0.2113 -0.0842 0.0120  0.0152  62  THR B OG1 
2701  C  CG2 . THR B  62  ? 0.4591 0.2151 0.4293 -0.1216 0.1020  0.0194  62  THR B CG2 
2702  N  N   . ASN B  63  ? 0.1391 0.4095 0.1173 -0.1191 0.0107  0.0873  63  ASN B N   
2703  C  CA  . ASN B  63  ? 0.1816 0.3027 0.1102 -0.0812 0.0348  0.0324  63  ASN B CA  
2704  C  C   . ASN B  63  ? 0.2987 0.1542 0.1416 -0.0247 0.0841  -0.0472 63  ASN B C   
2705  O  O   . ASN B  63  ? 0.1671 0.1463 0.2673 -0.0337 0.0148  0.0055  63  ASN B O   
2706  C  CB  . ASN B  63  ? 0.1793 0.3362 0.0922 -0.1026 0.0024  0.0732  63  ASN B CB  
2707  C  CG  . ASN B  63  ? 0.1689 0.2696 0.1179 -0.1046 -0.0175 0.1151  63  ASN B CG  
2708  O  OD1 . ASN B  63  ? 0.1951 0.2991 0.1167 -0.0961 0.0035  0.0657  63  ASN B OD1 
2709  N  ND2 . ASN B  63  ? 0.2761 0.2910 0.1014 -0.0785 0.0249  0.0923  63  ASN B ND2 
2710  N  N   . ASN B  64  ? 0.1773 0.3043 0.1364 -0.0432 0.0375  -0.0163 64  ASN B N   
2711  C  CA  . ASN B  64  ? 0.2486 0.1804 0.2348 -0.0313 0.1536  -0.0304 64  ASN B CA  
2712  C  C   . ASN B  64  ? 0.2294 0.1586 0.1134 0.0152  0.0186  0.0165  64  ASN B C   
2713  O  O   . ASN B  64  ? 0.1976 0.1896 0.1782 -0.0063 0.0000  -0.0104 64  ASN B O   
2714  C  CB  . ASN B  64  ? 0.2354 0.1965 0.1826 0.0373  0.0601  0.0021  64  ASN B CB  
2715  C  CG  . ASN B  64  ? 0.2275 0.1791 0.1556 0.0085  0.0339  -0.0137 64  ASN B CG  
2716  O  OD1 . ASN B  64  ? 0.2125 0.1523 0.1563 0.0076  0.0370  0.0082  64  ASN B OD1 
2717  N  ND2 . ASN B  64  ? 0.2578 0.3422 0.2170 0.0507  0.0837  0.0093  64  ASN B ND2 
2718  N  N   . GLY B  65  ? 0.1953 0.2971 0.1303 -0.0529 0.0780  -0.0026 65  GLY B N   
2719  C  CA  . GLY B  65  ? 0.1727 0.2581 0.1613 -0.0066 0.0777  0.0147  65  GLY B CA  
2720  C  C   . GLY B  65  ? 0.1902 0.2102 0.1428 -0.0130 0.0794  -0.0057 65  GLY B C   
2721  O  O   . GLY B  65  ? 0.1921 0.2309 0.1847 -0.0144 0.0781  0.0178  65  GLY B O   
2722  N  N   . HIS B  66  ? 0.1985 0.1717 0.1823 0.0258  0.0725  0.0305  66  HIS B N   
2723  C  CA  . HIS B  66  ? 0.2274 0.1526 0.1775 0.0167  -0.0143 -0.0068 66  HIS B CA  
2724  C  C   . HIS B  66  ? 0.1425 0.1770 0.1603 0.0008  0.0533  0.0421  66  HIS B C   
2725  O  O   . HIS B  66  ? 0.1870 0.1170 0.1899 0.0153  0.0425  0.0227  66  HIS B O   
2726  C  CB  . HIS B  66  ? 0.2867 0.1502 0.1738 0.0162  -0.0049 0.0207  66  HIS B CB  
2727  C  CG  . HIS B  66  ? 0.2560 0.1554 0.1560 0.0013  -0.0304 0.0159  66  HIS B CG  
2728  N  ND1 . HIS B  66  ? 0.2291 0.2193 0.2316 -0.0441 -0.0055 0.0291  66  HIS B ND1 
2729  C  CD2 . HIS B  66  ? 0.2605 0.1956 0.1515 0.0586  -0.0405 0.0243  66  HIS B CD2 
2730  C  CE1 . HIS B  66  ? 0.1922 0.1702 0.1597 -0.0175 -0.0040 0.0487  66  HIS B CE1 
2731  N  NE2 . HIS B  66  ? 0.2606 0.2463 0.1985 -0.0707 0.0043  0.0326  66  HIS B NE2 
2732  N  N   A SER B  67  ? 0.1818 0.1281 0.1493 0.0086  0.0296  0.0115  67  SER B N   
2733  N  N   B SER B  67  ? 0.1829 0.1269 0.1497 0.0097  0.0288  0.0080  67  SER B N   
2734  C  CA  A SER B  67  ? 0.1752 0.1796 0.1290 -0.0055 0.0324  0.0137  67  SER B CA  
2735  C  CA  B SER B  67  ? 0.1735 0.1789 0.1342 -0.0023 0.0307  0.0203  67  SER B CA  
2736  C  C   A SER B  67  ? 0.2443 0.1082 0.1215 -0.0271 0.0154  0.0289  67  SER B C   
2737  C  C   B SER B  67  ? 0.2517 0.1115 0.1234 -0.0271 0.0121  0.0263  67  SER B C   
2738  O  O   A SER B  67  ? 0.1822 0.1529 0.1360 0.0078  0.0373  0.0214  67  SER B O   
2739  O  O   B SER B  67  ? 0.1897 0.1562 0.1720 0.0215  0.0137  0.0244  67  SER B O   
2740  C  CB  A SER B  67  ? 0.1980 0.1504 0.1130 -0.0200 0.0240  0.0159  67  SER B CB  
2741  C  CB  B SER B  67  ? 0.2114 0.1901 0.1271 0.0062  0.0104  0.0153  67  SER B CB  
2742  O  OG  A SER B  67  ? 0.0836 0.0960 0.0628 0.0141  0.0370  0.0335  67  SER B OG  
2743  O  OG  B SER B  67  ? 0.1680 0.1613 0.1446 0.0092  0.0250  0.0000  67  SER B OG  
2744  N  N   A VAL B  68  ? 0.1577 0.1412 0.1680 0.0006  0.0397  0.0410  68  VAL B N   
2745  N  N   B VAL B  68  ? 0.1605 0.1387 0.1750 -0.0032 0.0395  0.0299  68  VAL B N   
2746  C  CA  A VAL B  68  ? 0.1529 0.3265 0.1094 -0.0043 0.0299  -0.0087 68  VAL B CA  
2747  C  CA  B VAL B  68  ? 0.1597 0.2639 0.1048 -0.0057 0.0355  -0.0041 68  VAL B CA  
2748  C  C   A VAL B  68  ? 0.1222 0.3991 0.0869 -0.0267 0.0296  0.0329  68  VAL B C   
2749  C  C   B VAL B  68  ? 0.0913 0.3802 0.0960 -0.0208 0.0315  0.0340  68  VAL B C   
2750  O  O   A VAL B  68  ? 0.1339 0.3292 0.1075 -0.0108 0.0162  -0.0322 68  VAL B O   
2751  O  O   B VAL B  68  ? 0.1283 0.3244 0.0985 -0.0231 0.0342  -0.0447 68  VAL B O   
2752  C  CB  A VAL B  68  ? 0.1732 0.3192 0.0952 0.0326  0.0604  -0.0093 68  VAL B CB  
2753  C  CB  B VAL B  68  ? 0.2079 0.2763 0.1195 0.0214  0.0436  -0.0017 68  VAL B CB  
2754  C  CG1 A VAL B  68  ? 0.2324 0.2370 0.1502 0.0203  0.0344  -0.0187 68  VAL B CG1 
2755  C  CG1 B VAL B  68  ? 0.2343 0.1972 0.1401 0.0322  0.0183  -0.0251 68  VAL B CG1 
2756  C  CG2 A VAL B  68  ? 0.1773 0.4050 0.1484 0.0060  0.0155  0.0333  68  VAL B CG2 
2757  C  CG2 B VAL B  68  ? 0.1957 0.3998 0.1351 -0.0170 0.0258  0.0718  68  VAL B CG2 
2758  N  N   . LYS B  69  ? 0.1281 0.3332 0.0876 -0.0456 0.0102  0.0804  69  LYS B N   
2759  C  CA  . LYS B  69  ? 0.1062 0.1935 0.0868 -0.0335 0.0142  0.0414  69  LYS B CA  
2760  C  C   . LYS B  69  ? 0.1209 0.1750 0.0660 -0.0126 0.0026  0.0403  69  LYS B C   
2761  O  O   . LYS B  69  ? 0.1204 0.2560 0.1075 -0.0307 -0.0066 0.0861  69  LYS B O   
2762  C  CB  . LYS B  69  ? 0.1806 0.1599 0.1935 -0.0456 -0.0337 0.0370  69  LYS B CB  
2763  C  CG  . LYS B  69  ? 0.2235 0.1953 0.3021 -0.0287 -0.0520 0.0375  69  LYS B CG  
2764  C  CD  . LYS B  69  ? 0.2635 0.1614 0.4036 -0.0057 -0.0412 -0.0205 69  LYS B CD  
2765  C  CE  . LYS B  69  ? 0.2728 0.2578 0.4619 0.0270  -0.0027 0.0586  69  LYS B CE  
2766  N  NZ  . LYS B  69  ? 0.3747 0.2416 0.4327 0.0493  -0.0078 -0.0012 69  LYS B NZ  
2767  N  N   . LEU B  70  ? 0.0967 0.1341 0.0754 -0.0081 0.0198  0.0087  70  LEU B N   
2768  C  CA  . LEU B  70  ? 0.0926 0.1224 0.0757 0.0017  0.0146  0.0027  70  LEU B CA  
2769  C  C   . LEU B  70  ? 0.1190 0.1080 0.0773 -0.0003 0.0131  0.0215  70  LEU B C   
2770  O  O   . LEU B  70  ? 0.1128 0.1109 0.0719 0.0114  0.0221  0.0230  70  LEU B O   
2771  C  CB  . LEU B  70  ? 0.1010 0.1073 0.1237 -0.0007 0.0176  0.0137  70  LEU B CB  
2772  C  CG  . LEU B  70  ? 0.1134 0.1197 0.1000 -0.0007 0.0060  0.0127  70  LEU B CG  
2773  C  CD1 . LEU B  70  ? 0.1247 0.1926 0.1181 -0.0186 -0.0220 0.0120  70  LEU B CD1 
2774  C  CD2 . LEU B  70  ? 0.1495 0.1132 0.1721 -0.0251 0.0214  0.0046  70  LEU B CD2 
2775  N  N   . ASN B  71  ? 0.1167 0.1048 0.0910 0.0096  0.0153  0.0245  71  ASN B N   
2776  C  CA  . ASN B  71  ? 0.1500 0.1147 0.1057 0.0204  0.0265  0.0300  71  ASN B CA  
2777  C  C   . ASN B  71  ? 0.1143 0.1572 0.0960 0.0333  0.0065  0.0241  71  ASN B C   
2778  O  O   . ASN B  71  ? 0.1265 0.2294 0.1023 -0.0087 0.0055  0.0261  71  ASN B O   
2779  C  CB  . ASN B  71  ? 0.1671 0.1466 0.1527 0.0439  0.0533  0.0610  71  ASN B CB  
2780  C  CG  . ASN B  71  ? 0.2157 0.1743 0.1536 0.0328  0.0540  0.0513  71  ASN B CG  
2781  O  OD1 . ASN B  71  ? 0.2228 0.1831 0.2865 -0.0313 0.0812  0.0209  71  ASN B OD1 
2782  N  ND2 . ASN B  71  ? 0.4020 0.1745 0.2847 0.0639  0.0806  0.0666  71  ASN B ND2 
2783  N  N   . LEU B  72  ? 0.1261 0.1268 0.1040 0.0189  0.0153  0.0179  72  LEU B N   
2784  C  CA  . LEU B  72  ? 0.0897 0.1283 0.1226 0.0197  0.0127  0.0127  72  LEU B CA  
2785  C  C   . LEU B  72  ? 0.1181 0.1237 0.1125 0.0218  0.0096  0.0219  72  LEU B C   
2786  O  O   . LEU B  72  ? 0.1353 0.1328 0.1563 0.0108  0.0408  -0.0008 72  LEU B O   
2787  C  CB  . LEU B  72  ? 0.1097 0.1039 0.1376 0.0252  0.0159  0.0308  72  LEU B CB  
2788  C  CG  . LEU B  72  ? 0.1012 0.1111 0.1097 0.0136  0.0133  0.0163  72  LEU B CG  
2789  C  CD1 . LEU B  72  ? 0.0953 0.1231 0.1186 0.0247  0.0190  0.0296  72  LEU B CD1 
2790  C  CD2 . LEU B  72  ? 0.1244 0.1231 0.1215 0.0055  0.0120  0.0019  72  LEU B CD2 
2791  N  N   . PRO B  73  ? 0.1146 0.1274 0.1326 0.0344  0.0153  0.0147  73  PRO B N   
2792  C  CA  . PRO B  73  ? 0.1170 0.1524 0.1445 0.0333  0.0296  0.0273  73  PRO B CA  
2793  C  C   . PRO B  73  ? 0.1468 0.1728 0.1342 0.0329  0.0269  -0.0063 73  PRO B C   
2794  O  O   . PRO B  73  ? 0.1326 0.2213 0.1419 0.0121  0.0262  0.0342  73  PRO B O   
2795  C  CB  . PRO B  73  ? 0.1462 0.1635 0.1611 0.0222  0.0172  0.0104  73  PRO B CB  
2796  C  CG  . PRO B  73  ? 0.1027 0.1601 0.1781 0.0215  0.0296  0.0141  73  PRO B CG  
2797  C  CD  . PRO B  73  ? 0.1134 0.1493 0.1535 0.0121  0.0120  -0.0007 73  PRO B CD  
2798  N  N   . SER B  74  ? 0.2266 0.1833 0.1750 0.0190  0.0886  -0.0087 74  SER B N   
2799  C  CA  . SER B  74  ? 0.2226 0.1675 0.1826 0.0104  0.0688  0.0178  74  SER B CA  
2800  C  C   . SER B  74  ? 0.1604 0.1960 0.1786 0.0208  0.0648  0.0119  74  SER B C   
2801  O  O   . SER B  74  ? 0.1935 0.2754 0.1601 0.0073  0.0781  -0.0089 74  SER B O   
2802  C  CB  . SER B  74  ? 0.2969 0.1755 0.2712 0.0219  0.0938  0.0057  74  SER B CB  
2803  O  OG  . SER B  74  ? 0.3494 0.2254 0.3034 0.0903  0.0935  -0.0177 74  SER B OG  
2804  N  N   . ASP B  75  ? 0.1356 0.2070 0.2170 0.0329  0.0626  0.0436  75  ASP B N   
2805  C  CA  . ASP B  75  ? 0.1335 0.2314 0.2363 0.0584  0.0627  0.0895  75  ASP B CA  
2806  C  C   . ASP B  75  ? 0.1371 0.1890 0.2108 0.0465  0.0653  0.0504  75  ASP B C   
2807  O  O   . ASP B  75  ? 0.1590 0.2495 0.2474 0.0348  0.0885  0.0681  75  ASP B O   
2808  C  CB  . ASP B  75  ? 0.1629 0.2414 0.2842 0.0597  0.0329  0.0291  75  ASP B CB  
2809  C  CG  . ASP B  75  ? 0.2228 0.6894 0.3177 0.0520  -0.0621 -0.0244 75  ASP B CG  
2810  O  OD1 . ASP B  75  ? 0.3589 0.5177 0.4334 -0.0825 0.1271  0.0794  75  ASP B OD1 
2811  O  OD2 . ASP B  75  ? 0.1824 1.0527 0.8984 0.0548  -0.1569 -0.0908 75  ASP B OD2 
2812  N  N   . MET B  76  ? 0.1091 0.1890 0.1538 0.0461  0.0355  0.0355  76  MET B N   
2813  C  CA  . MET B  76  ? 0.0876 0.1912 0.1392 0.0231  0.0390  0.0161  76  MET B CA  
2814  C  C   . MET B  76  ? 0.0829 0.1800 0.1353 0.0328  0.0313  0.0436  76  MET B C   
2815  O  O   . MET B  76  ? 0.1204 0.1720 0.1477 0.0183  0.0395  0.0203  76  MET B O   
2816  C  CB  . MET B  76  ? 0.1516 0.1529 0.1256 0.0251  0.0428  0.0283  76  MET B CB  
2817  C  CG  . MET B  76  ? 0.1077 0.1757 0.1653 0.0242  0.0428  0.0441  76  MET B CG  
2818  S  SD  . MET B  76  ? 0.1365 0.1784 0.1283 0.0073  0.0364  0.0153  76  MET B SD  
2819  C  CE  . MET B  76  ? 0.1272 0.1226 0.1407 0.0057  0.0221  0.0189  76  MET B CE  
2820  N  N   . HIS B  77  ? 0.0901 0.1956 0.1283 0.0397  0.0313  0.0296  77  HIS B N   
2821  C  CA  . HIS B  77  ? 0.1206 0.1845 0.1279 0.0425  0.0309  0.0172  77  HIS B CA  
2822  C  C   . HIS B  77  ? 0.1082 0.1709 0.1052 0.0230  0.0329  0.0342  77  HIS B C   
2823  O  O   . HIS B  77  ? 0.1243 0.1858 0.1380 0.0126  0.0329  0.0227  77  HIS B O   
2824  C  CB  . HIS B  77  ? 0.1225 0.2233 0.1872 0.0628  0.0645  0.0049  77  HIS B CB  
2825  C  CG  . HIS B  77  ? 0.1444 0.2928 0.1597 0.0247  0.0697  -0.0230 77  HIS B CG  
2826  N  ND1 . HIS B  77  ? 0.1215 0.4079 0.2415 0.0641  0.0802  0.0441  77  HIS B ND1 
2827  C  CD2 . HIS B  77  ? 0.2010 0.2651 0.1581 0.0103  0.0872  -0.0052 77  HIS B CD2 
2828  C  CE1 . HIS B  77  ? 0.1357 0.3573 0.2755 0.0518  0.0727  0.0183  77  HIS B CE1 
2829  N  NE2 . HIS B  77  ? 0.1541 0.3693 0.2820 0.0520  0.0608  -0.0111 77  HIS B NE2 
2830  N  N   . ILE B  78  ? 0.1439 0.2005 0.1033 0.0482  0.0317  0.0299  78  ILE B N   
2831  C  CA  . ILE B  78  ? 0.1489 0.2037 0.1045 0.0351  0.0340  0.0696  78  ILE B CA  
2832  C  C   . ILE B  78  ? 0.1621 0.1684 0.1221 0.0612  0.0104  0.0359  78  ILE B C   
2833  O  O   . ILE B  78  ? 0.1960 0.2078 0.1301 0.0476  0.0339  0.0289  78  ILE B O   
2834  C  CB  . ILE B  78  ? 0.1542 0.2655 0.1270 0.0868  0.0397  0.0724  78  ILE B CB  
2835  C  CG1 . ILE B  78  ? 0.1782 0.3664 0.1437 0.0715  0.0816  0.0768  78  ILE B CG1 
2836  C  CG2 . ILE B  78  ? 0.2102 0.2946 0.1711 0.0934  0.0582  0.0773  78  ILE B CG2 
2837  C  CD1 . ILE B  78  ? 0.1306 0.2518 0.2267 0.0390  0.0595  0.0687  78  ILE B CD1 
2838  N  N   . GLN B  79  ? 0.1687 0.2014 0.1164 0.0454  0.0403  0.0500  79  GLN B N   
2839  C  CA  . GLN B  79  ? 0.2089 0.2438 0.1362 0.0707  0.0746  0.0654  79  GLN B CA  
2840  C  C   . GLN B  79  ? 0.2205 0.2400 0.1475 0.0678  0.0711  0.0850  79  GLN B C   
2841  O  O   . GLN B  79  ? 0.2402 0.2409 0.1640 0.0544  0.0373  0.0643  79  GLN B O   
2842  C  CB  . GLN B  79  ? 0.1992 0.2964 0.2467 0.0170  0.1168  0.0568  79  GLN B CB  
2843  C  CG  . GLN B  79  ? 0.2100 0.5572 0.3003 -0.0476 0.0864  0.1588  79  GLN B CG  
2844  C  CD  . GLN B  79  ? 0.2890 0.9919 0.2885 0.0923  0.1571  0.0252  79  GLN B CD  
2845  O  OE1 . GLN B  79  ? 0.6055 0.9308 0.4196 0.2926  0.2955  0.1178  79  GLN B OE1 
2846  N  NE2 . GLN B  79  ? 0.8163 1.0922 0.3023 -0.3316 0.0564  0.1174  79  GLN B NE2 
2847  N  N   . GLY B  80  ? 0.2050 0.2782 0.1405 0.0493  0.0570  0.0697  80  GLY B N   
2848  C  CA  . GLY B  80  ? 0.2845 0.3007 0.1292 0.0265  0.0104  0.0593  80  GLY B CA  
2849  C  C   . GLY B  80  ? 0.2522 0.2323 0.1766 0.0703  0.0194  0.0617  80  GLY B C   
2850  O  O   . GLY B  80  ? 0.2019 0.3722 0.2319 0.0465  0.0320  0.1261  80  GLY B O   
2851  N  N   . LEU B  81  ? 0.2134 0.2274 0.1466 0.0443  0.0351  0.0207  81  LEU B N   
2852  C  CA  . LEU B  81  ? 0.2393 0.2393 0.1486 0.0710  0.0239  0.0214  81  LEU B CA  
2853  C  C   . LEU B  81  ? 0.2160 0.3519 0.1387 0.1035  0.0000  0.0052  81  LEU B C   
2854  O  O   . LEU B  81  ? 0.2547 0.2711 0.1648 0.0882  0.0423  -0.0027 81  LEU B O   
2855  C  CB  . LEU B  81  ? 0.1908 0.3237 0.1917 0.0874  0.0800  0.0538  81  LEU B CB  
2856  C  CG  . LEU B  81  ? 0.2605 0.2346 0.1840 0.1116  0.0394  0.0520  81  LEU B CG  
2857  C  CD1 . LEU B  81  ? 0.2642 0.2055 0.2235 0.1059  0.0714  0.0640  81  LEU B CD1 
2858  C  CD2 . LEU B  81  ? 0.2168 0.2689 0.3206 0.1018  0.0465  0.1057  81  LEU B CD2 
2859  N  N   . GLN B  82  ? 0.2921 0.3034 0.1676 0.0829  -0.0405 -0.0208 82  GLN B N   
2860  C  CA  . GLN B  82  ? 0.3925 0.3407 0.1383 0.1307  -0.0211 -0.0086 82  GLN B CA  
2861  C  C   . GLN B  82  ? 0.3819 0.4119 0.1106 0.1791  0.0000  -0.0143 82  GLN B C   
2862  O  O   . GLN B  82  ? 0.4853 0.4357 0.1249 0.2187  0.0551  -0.0031 82  GLN B O   
2863  C  CB  . GLN B  82  ? 0.4302 0.4816 0.2795 0.2049  -0.1535 -0.1322 82  GLN B CB  
2864  C  CG  . GLN B  82  ? 0.6790 0.6327 0.5408 0.2435  -0.2930 -0.1388 82  GLN B CG  
2865  C  CD  . GLN B  82  ? 0.3080 0.5554 1.1940 -0.0432 -0.2777 -0.2126 82  GLN B CD  
2866  O  OE1 . GLN B  82  ? 1.0142 0.8306 2.6658 0.0878  0.8147  0.1625  82  GLN B OE1 
2867  N  NE2 . GLN B  82  ? 0.5299 0.8370 0.6758 0.0803  0.1524  -0.2536 82  GLN B NE2 
2868  N  N   . SER B  83  ? 0.3059 0.3382 0.1168 0.1303  0.0423  0.0017  83  SER B N   
2869  C  CA  . SER B  83  ? 0.2118 0.2741 0.1322 0.0839  0.0111  -0.0154 83  SER B CA  
2870  C  C   . SER B  83  ? 0.2202 0.2709 0.1046 0.0794  0.0502  0.0000  83  SER B C   
2871  O  O   . SER B  83  ? 0.2025 0.2615 0.1231 0.0767  0.0403  -0.0059 83  SER B O   
2872  C  CB  . SER B  83  ? 0.3027 0.2980 0.1941 0.0803  0.0125  -0.0825 83  SER B CB  
2873  O  OG  . SER B  83  ? 0.3540 0.3531 0.2100 0.0636  -0.0370 -0.0899 83  SER B OG  
2874  N  N   A ARG B  84  ? 0.2037 0.2563 0.0978 0.0652  0.0653  -0.0071 84  ARG B N   
2875  N  N   B ARG B  84  ? 0.2055 0.2572 0.0992 0.0676  0.0636  -0.0083 84  ARG B N   
2876  C  CA  A ARG B  84  ? 0.1630 0.2964 0.1127 0.0318  0.0586  -0.0082 84  ARG B CA  
2877  C  CA  B ARG B  84  ? 0.1624 0.3043 0.1127 0.0292  0.0586  -0.0076 84  ARG B CA  
2878  C  C   A ARG B  84  ? 0.1696 0.1987 0.0838 0.0364  0.0362  0.0028  84  ARG B C   
2879  C  C   B ARG B  84  ? 0.1712 0.1999 0.0838 0.0359  0.0375  0.0027  84  ARG B C   
2880  O  O   A ARG B  84  ? 0.1872 0.1935 0.1416 0.0544  0.0434  -0.0274 84  ARG B O   
2881  O  O   B ARG B  84  ? 0.1870 0.1990 0.1461 0.0560  0.0480  -0.0337 84  ARG B O   
2882  C  CB  A ARG B  84  ? 0.1841 0.3282 0.1403 0.0764  0.0571  -0.0100 84  ARG B CB  
2883  C  CB  B ARG B  84  ? 0.1875 0.3305 0.1450 0.0732  0.0520  -0.0165 84  ARG B CB  
2884  C  CG  A ARG B  84  ? 0.1642 0.2800 0.1465 0.0667  0.0370  0.0183  84  ARG B CG  
2885  C  CG  B ARG B  84  ? 0.1693 0.2833 0.1468 0.0665  0.0447  0.0142  84  ARG B CG  
2886  C  CD  A ARG B  84  ? 0.1542 0.3156 0.1464 0.0423  0.0487  0.0476  84  ARG B CD  
2887  C  CD  B ARG B  84  ? 0.1807 0.3436 0.2291 0.0856  0.0399  0.0060  84  ARG B CD  
2888  N  NE  A ARG B  84  ? 0.1720 0.2454 0.1281 0.1368  0.0830  0.0595  84  ARG B NE  
2889  N  NE  B ARG B  84  ? 0.2921 0.4190 0.2759 -0.0049 0.0756  0.0073  84  ARG B NE  
2890  C  CZ  A ARG B  84  ? 0.1915 0.4097 0.1233 0.1591  0.0800  0.0375  84  ARG B CZ  
2891  C  CZ  B ARG B  84  ? 0.2355 0.5442 0.2563 0.0060  0.1287  0.0201  84  ARG B CZ  
2892  N  NH1 A ARG B  84  ? 0.2032 0.5724 0.1100 0.1525  0.0930  -0.0375 84  ARG B NH1 
2893  N  NH1 B ARG B  84  ? 0.2888 0.6534 0.3885 0.0917  -0.0015 0.0588  84  ARG B NH1 
2894  N  NH2 A ARG B  84  ? 0.2773 0.4590 0.1018 0.1641  0.0399  -0.0083 84  ARG B NH2 
2895  N  NH2 B ARG B  84  ? 0.2337 0.5389 0.3337 -0.0581 0.0860  0.1136  84  ARG B NH2 
2896  N  N   . TYR B  85  ? 0.1635 0.2166 0.0719 0.0584  0.0377  -0.0046 85  TYR B N   
2897  C  CA  . TYR B  85  ? 0.1711 0.1841 0.0759 0.0702  0.0461  0.0160  85  TYR B CA  
2898  C  C   . TYR B  85  ? 0.1317 0.1493 0.1145 0.0223  0.0474  -0.0115 85  TYR B C   
2899  O  O   . TYR B  85  ? 0.1766 0.1642 0.1290 0.0222  0.0294  0.0170  85  TYR B O   
2900  C  CB  . TYR B  85  ? 0.1515 0.1881 0.1000 0.0509  0.0205  0.0040  85  TYR B CB  
2901  C  CG  . TYR B  85  ? 0.1351 0.1856 0.1014 0.0546  0.0296  -0.0176 85  TYR B CG  
2902  C  CD1 . TYR B  85  ? 0.1777 0.2239 0.1127 0.0672  0.0270  0.0013  85  TYR B CD1 
2903  C  CD2 . TYR B  85  ? 0.1473 0.1554 0.1407 0.0555  0.0346  -0.0198 85  TYR B CD2 
2904  C  CE1 . TYR B  85  ? 0.1744 0.2400 0.1254 0.0329  0.0153  0.0142  85  TYR B CE1 
2905  C  CE2 . TYR B  85  ? 0.1879 0.1727 0.1188 0.0753  0.0212  -0.0377 85  TYR B CE2 
2906  C  CZ  . TYR B  85  ? 0.1788 0.2120 0.1254 0.0500  0.0142  -0.0317 85  TYR B CZ  
2907  O  OH  . TYR B  85  ? 0.1964 0.2935 0.1477 0.0318  0.0013  -0.0240 85  TYR B OH  
2908  N  N   . SER B  86  ? 0.1290 0.1775 0.1032 0.0507  0.0375  0.0218  86  SER B N   
2909  C  CA  . SER B  86  ? 0.1382 0.1712 0.0906 0.0619  0.0296  0.0071  86  SER B CA  
2910  C  C   . SER B  86  ? 0.1079 0.1269 0.0912 0.0351  0.0179  0.0089  86  SER B C   
2911  O  O   . SER B  86  ? 0.1091 0.1290 0.1165 0.0381  0.0259  -0.0034 86  SER B O   
2912  C  CB  . SER B  86  ? 0.1394 0.2043 0.1238 0.0870  0.0447  0.0000  86  SER B CB  
2913  O  OG  . SER B  86  ? 0.1457 0.2687 0.1513 0.0742  0.0571  -0.0161 86  SER B OG  
2914  N  N   . ALA B  87  ? 0.1030 0.1622 0.0953 0.0299  0.0231  0.0052  87  ALA B N   
2915  C  CA  . ALA B  87  ? 0.1125 0.1314 0.0935 0.0252  0.0379  0.0091  87  ALA B CA  
2916  C  C   . ALA B  87  ? 0.1222 0.1365 0.0897 0.0414  0.0344  0.0109  87  ALA B C   
2917  O  O   . ALA B  87  ? 0.1076 0.1656 0.1174 0.0373  0.0305  0.0244  87  ALA B O   
2918  C  CB  . ALA B  87  ? 0.1500 0.1499 0.1254 -0.0041 0.0386  0.0041  87  ALA B CB  
2919  N  N   . THR B  88  ? 0.1136 0.1140 0.0847 0.0296  0.0416  0.0082  88  THR B N   
2920  C  CA  . THR B  88  ? 0.1443 0.1107 0.0824 0.0197  0.0311  0.0038  88  THR B CA  
2921  C  C   . THR B  88  ? 0.1107 0.0942 0.0845 0.0227  0.0248  0.0133  88  THR B C   
2922  O  O   . THR B  88  ? 0.1130 0.0978 0.0987 0.0311  0.0264  0.0092  88  THR B O   
2923  C  CB  . THR B  88  ? 0.1800 0.1115 0.1341 0.0131  0.0452  0.0077  88  THR B CB  
2924  O  OG1 . THR B  88  ? 0.3309 0.1154 0.1579 0.0136  0.0178  0.0043  88  THR B OG1 
2925  C  CG2 . THR B  88  ? 0.1524 0.1340 0.1692 0.0181  0.0318  -0.0379 88  THR B CG2 
2926  N  N   . GLN B  89  ? 0.1001 0.0863 0.0885 0.0225  0.0304  0.0017  89  GLN B N   
2927  C  CA  . GLN B  89  ? 0.0964 0.0894 0.0804 0.0315  0.0286  0.0109  89  GLN B CA  
2928  C  C   . GLN B  89  ? 0.0757 0.0766 0.0847 0.0197  0.0259  0.0076  89  GLN B C   
2929  O  O   . GLN B  89  ? 0.1062 0.0980 0.0763 0.0285  0.0160  0.0148  89  GLN B O   
2930  C  CB  . GLN B  89  ? 0.1107 0.0854 0.1057 0.0051  0.0274  0.0089  89  GLN B CB  
2931  C  CG  . GLN B  89  ? 0.1176 0.0956 0.1296 0.0000  0.0207  -0.0076 89  GLN B CG  
2932  C  CD  . GLN B  89  ? 0.1184 0.1067 0.1267 0.0104  0.0038  0.0232  89  GLN B CD  
2933  O  OE1 . GLN B  89  ? 0.1039 0.1026 0.1292 0.0198  0.0278  0.0041  89  GLN B OE1 
2934  N  NE2 . GLN B  89  ? 0.1326 0.1209 0.2640 0.0017  -0.0124 0.0096  89  GLN B NE2 
2935  N  N   . LEU B  90  ? 0.0793 0.0873 0.0788 0.0156  0.0244  0.0000  90  LEU B N   
2936  C  CA  . LEU B  90  ? 0.0791 0.0732 0.0794 0.0127  0.0322  0.0071  90  LEU B CA  
2937  C  C   . LEU B  90  ? 0.0806 0.0909 0.0672 0.0159  0.0219  0.0088  90  LEU B C   
2938  O  O   . LEU B  90  ? 0.0954 0.0852 0.0850 0.0131  0.0251  0.0229  90  LEU B O   
2939  C  CB  . LEU B  90  ? 0.0945 0.0791 0.0824 0.0017  0.0209  0.0091  90  LEU B CB  
2940  C  CG  . LEU B  90  ? 0.1044 0.0917 0.0942 -0.0070 0.0116  0.0225  90  LEU B CG  
2941  C  CD1 . LEU B  90  ? 0.1130 0.0906 0.1046 0.0118  0.0136  -0.0012 90  LEU B CD1 
2942  C  CD2 . LEU B  90  ? 0.1133 0.1109 0.1256 -0.0071 0.0098  0.0197  90  LEU B CD2 
2943  N  N   . HIS B  91  ? 0.0744 0.0820 0.0780 0.0088  0.0322  0.0087  91  HIS B N   
2944  C  CA  . HIS B  91  ? 0.0847 0.0712 0.0820 0.0136  0.0397  0.0230  91  HIS B CA  
2945  C  C   . HIS B  91  ? 0.0861 0.0663 0.0748 0.0098  0.0278  0.0131  91  HIS B C   
2946  O  O   . HIS B  91  ? 0.0940 0.0746 0.0692 0.0132  0.0282  0.0177  91  HIS B O   
2947  C  CB  . HIS B  91  ? 0.0903 0.0866 0.0883 0.0092  0.0329  0.0215  91  HIS B CB  
2948  C  CG  . HIS B  91  ? 0.0830 0.0800 0.0784 0.0040  0.0254  0.0100  91  HIS B CG  
2949  N  ND1 . HIS B  91  ? 0.0976 0.0741 0.0886 0.0091  0.0288  0.0098  91  HIS B ND1 
2950  C  CD2 . HIS B  91  ? 0.0897 0.0724 0.0688 -0.0086 0.0228  0.0104  91  HIS B CD2 
2951  C  CE1 . HIS B  91  ? 0.0784 0.0730 0.1138 0.0087  0.0252  0.0108  91  HIS B CE1 
2952  N  NE2 . HIS B  91  ? 0.0701 0.0781 0.0785 0.0082  0.0087  0.0023  91  HIS B NE2 
2953  N  N   . LEU B  92  ? 0.0863 0.0818 0.0815 0.0197  0.0355  0.0159  92  LEU B N   
2954  C  CA  . LEU B  92  ? 0.0824 0.0662 0.0976 0.0146  0.0384  0.0005  92  LEU B CA  
2955  C  C   . LEU B  92  ? 0.0895 0.0782 0.0608 0.0116  0.0357  0.0125  92  LEU B C   
2956  O  O   . LEU B  92  ? 0.0940 0.0820 0.0872 0.0057  0.0359  0.0184  92  LEU B O   
2957  C  CB  . LEU B  92  ? 0.1136 0.1111 0.1048 -0.0104 0.0474  -0.0153 92  LEU B CB  
2958  C  CG  . LEU B  92  ? 0.1100 0.1333 0.1006 -0.0066 0.0261  -0.0216 92  LEU B CG  
2959  C  CD1 . LEU B  92  ? 0.1599 0.1511 0.1642 0.0147  0.0000  -0.0155 92  LEU B CD1 
2960  C  CD2 . LEU B  92  ? 0.1518 0.1252 0.1890 -0.0273 0.0129  0.0384  92  LEU B CD2 
2961  N  N   . HIS B  93  ? 0.0728 0.0822 0.0750 0.0131  0.0274  0.0040  93  HIS B N   
2962  C  CA  . HIS B  93  ? 0.0751 0.0707 0.0863 0.0125  0.0326  0.0070  93  HIS B CA  
2963  C  C   . HIS B  93  ? 0.0933 0.0712 0.0739 0.0096  0.0441  0.0113  93  HIS B C   
2964  O  O   . HIS B  93  ? 0.1041 0.0662 0.0815 0.0049  0.0454  0.0121  93  HIS B O   
2965  C  CB  . HIS B  93  ? 0.0812 0.0680 0.0939 0.0115  0.0296  0.0040  93  HIS B CB  
2966  C  CG  . HIS B  93  ? 0.0790 0.0714 0.0848 0.0071  0.0260  0.0103  93  HIS B CG  
2967  N  ND1 . HIS B  93  ? 0.0942 0.0755 0.0931 0.0081  0.0410  0.0129  93  HIS B ND1 
2968  C  CD2 . HIS B  93  ? 0.0822 0.0918 0.0794 0.0177  0.0307  0.0052  93  HIS B CD2 
2969  C  CE1 . HIS B  93  ? 0.0897 0.0851 0.0773 0.0082  0.0417  0.0187  93  HIS B CE1 
2970  N  NE2 . HIS B  93  ? 0.0833 0.0703 0.0827 -0.0006 0.0259  0.0186  93  HIS B NE2 
2971  N  N   . TRP B  94  ? 0.0847 0.0759 0.0877 0.0060  0.0416  0.0055  94  TRP B N   
2972  C  CA  . TRP B  94  ? 0.1023 0.0657 0.0906 0.0178  0.0625  0.0126  94  TRP B CA  
2973  C  C   . TRP B  94  ? 0.1149 0.0781 0.0890 0.0080  0.0476  0.0254  94  TRP B C   
2974  O  O   . TRP B  94  ? 0.0979 0.0836 0.0978 0.0092  0.0568  0.0154  94  TRP B O   
2975  C  CB  . TRP B  94  ? 0.1179 0.0924 0.0909 -0.0003 0.0423  0.0247  94  TRP B CB  
2976  C  CG  . TRP B  94  ? 0.1045 0.0897 0.0784 0.0038  0.0474  0.0114  94  TRP B CG  
2977  C  CD1 . TRP B  94  ? 0.1536 0.1028 0.0807 0.0234  0.0678  0.0185  94  TRP B CD1 
2978  C  CD2 . TRP B  94  ? 0.1174 0.0938 0.0723 0.0005  0.0364  0.0028  94  TRP B CD2 
2979  N  NE1 . TRP B  94  ? 0.1304 0.0921 0.1036 0.0182  0.0628  0.0212  94  TRP B NE1 
2980  C  CE2 . TRP B  94  ? 0.1274 0.1005 0.0803 0.0214  0.0487  0.0104  94  TRP B CE2 
2981  C  CE3 . TRP B  94  ? 0.1174 0.0991 0.0700 0.0081  0.0410  0.0080  94  TRP B CE3 
2982  C  CZ2 . TRP B  94  ? 0.1387 0.0985 0.0954 0.0164  0.0428  0.0131  94  TRP B CZ2 
2983  C  CZ3 . TRP B  94  ? 0.1321 0.1015 0.0964 0.0005  0.0317  0.0166  94  TRP B CZ3 
2984  C  CH2 . TRP B  94  ? 0.1360 0.1010 0.0974 0.0141  0.0467  0.0088  94  TRP B CH2 
2985  N  N   . GLY B  95  ? 0.1195 0.0807 0.0944 0.0152  0.0630  0.0127  95  GLY B N   
2986  C  CA  . GLY B  95  ? 0.1364 0.1014 0.1123 0.0200  0.0807  0.0340  95  GLY B CA  
2987  C  C   . GLY B  95  ? 0.1149 0.1067 0.0978 0.0219  0.0671  0.0159  95  GLY B C   
2988  O  O   . GLY B  95  ? 0.1308 0.0992 0.1077 0.0111  0.0623  0.0165  95  GLY B O   
2989  N  N   . ASN B  96  ? 0.1437 0.0989 0.1059 0.0049  0.0781  0.0060  96  ASN B N   
2990  C  CA  . ASN B  96  ? 0.1953 0.1342 0.0903 0.0299  0.0749  0.0080  96  ASN B CA  
2991  C  C   . ASN B  96  ? 0.1527 0.1693 0.1091 0.0368  0.0934  0.0115  96  ASN B C   
2992  O  O   . ASN B  96  ? 0.1692 0.1429 0.1150 0.0297  0.0837  -0.0017 96  ASN B O   
2993  C  CB  . ASN B  96  ? 0.2041 0.1387 0.1811 0.0082  0.1196  0.0452  96  ASN B CB  
2994  C  CG  . ASN B  96  ? 0.1834 0.1499 0.2709 -0.0154 0.1614  -0.0115 96  ASN B CG  
2995  O  OD1 . ASN B  96  ? 0.2388 0.2211 0.4013 -0.0430 0.2397  -0.1162 96  ASN B OD1 
2996  N  ND2 . ASN B  96  ? 0.1434 0.1894 0.3176 0.0217  0.0877  -0.0310 96  ASN B ND2 
2997  N  N   . PRO B  97  ? 0.1913 0.1834 0.1125 0.0566  0.0817  -0.0027 97  PRO B N   
2998  C  CA  . PRO B  97  ? 0.1999 0.2463 0.1206 0.0632  0.0509  -0.0432 97  PRO B CA  
2999  C  C   . PRO B  97  ? 0.1678 0.1856 0.1332 0.0031  0.0829  0.0032  97  PRO B C   
3000  O  O   . PRO B  97  ? 0.2246 0.2131 0.1712 -0.0186 0.0839  0.0175  97  PRO B O   
3001  C  CB  . PRO B  97  ? 0.2017 0.3894 0.1143 0.1650  0.0300  -0.0291 97  PRO B CB  
3002  C  CG  . PRO B  97  ? 0.2269 0.3095 0.1402 0.1133  0.0494  -0.0096 97  PRO B CG  
3003  C  CD  . PRO B  97  ? 0.2502 0.2633 0.1176 0.0843  0.0675  0.0263  97  PRO B CD  
3004  N  N   . ASN B  98  ? 0.1454 0.1723 0.1240 0.0264  0.0700  -0.0043 98  ASN B N   
3005  C  CA  . ASN B  98  ? 0.1572 0.2434 0.1307 0.0274  0.0797  0.0241  98  ASN B CA  
3006  C  C   . ASN B  98  ? 0.2043 0.2856 0.1562 0.0702  0.0715  0.0247  98  ASN B C   
3007  O  O   . ASN B  98  ? 0.2714 0.3912 0.2330 0.1798  0.1103  0.0362  98  ASN B O   
3008  C  CB  . ASN B  98  ? 0.1721 0.2456 0.1328 0.0218  0.0546  0.0309  98  ASN B CB  
3009  C  CG  . ASN B  98  ? 0.1588 0.2032 0.1364 0.0237  0.0680  0.0318  98  ASN B CG  
3010  O  OD1 . ASN B  98  ? 0.2570 0.1746 0.1471 0.0513  0.0776  0.0306  98  ASN B OD1 
3011  N  ND2 . ASN B  98  ? 0.2579 0.1896 0.1814 0.0082  0.1054  0.0313  98  ASN B ND2 
3012  N  N   . ASP B  99  ? 0.2037 0.1990 0.1242 0.0214  0.0800  0.0434  99  ASP B N   
3013  C  CA  . ASP B  99  ? 0.1587 0.2766 0.1376 0.0412  0.0653  0.0518  99  ASP B CA  
3014  C  C   . ASP B  99  ? 0.1400 0.1536 0.1791 0.0254  0.0555  -0.0006 99  ASP B C   
3015  O  O   . ASP B  99  ? 0.1620 0.1412 0.1486 0.0026  0.0373  0.0333  99  ASP B O   
3016  C  CB  . ASP B  99  ? 0.1450 0.3319 0.2142 0.0143  0.0461  0.0502  99  ASP B CB  
3017  C  CG  . ASP B  99  ? 0.1356 0.5277 0.2939 0.0126  0.0310  0.1127  99  ASP B CG  
3018  O  OD1 . ASP B  99  ? 0.2901 0.6128 0.2594 0.0317  0.0635  0.1872  99  ASP B OD1 
3019  O  OD2 . ASP B  99  ? 0.4742 0.8177 0.4399 -0.0250 -0.2231 -0.0183 99  ASP B OD2 
3020  N  N   . PRO B  100 ? 0.1590 0.1364 0.1261 0.0293  0.0491  0.0054  100 PRO B N   
3021  C  CA  . PRO B  100 ? 0.1465 0.1655 0.1347 -0.0096 0.0590  -0.0019 100 PRO B CA  
3022  C  C   . PRO B  100 ? 0.1493 0.1174 0.1395 0.0017  0.0824  0.0143  100 PRO B C   
3023  O  O   . PRO B  100 ? 0.1949 0.1386 0.1590 -0.0252 0.1054  -0.0087 100 PRO B O   
3024  C  CB  . PRO B  100 ? 0.2095 0.1457 0.1799 -0.0059 0.0247  -0.0078 100 PRO B CB  
3025  C  CG  . PRO B  100 ? 0.2411 0.1626 0.2332 0.0181  0.0882  -0.0340 100 PRO B CG  
3026  C  CD  . PRO B  100 ? 0.2406 0.1357 0.1849 0.0381  0.0680  -0.0230 100 PRO B CD  
3027  N  N   . HIS B  101 ? 0.1455 0.1448 0.1483 0.0108  0.0388  -0.0012 101 HIS B N   
3028  C  CA  . HIS B  101 ? 0.1626 0.1254 0.1699 0.0161  0.0573  -0.0132 101 HIS B CA  
3029  C  C   . HIS B  101 ? 0.1089 0.1164 0.2341 -0.0337 0.0780  -0.0111 101 HIS B C   
3030  O  O   . HIS B  101 ? 0.1409 0.2172 0.2957 0.0046  0.0339  -0.0225 101 HIS B O   
3031  C  CB  . HIS B  101 ? 0.1668 0.1676 0.1815 0.0197  0.0377  0.0351  101 HIS B CB  
3032  C  CG  . HIS B  101 ? 0.1920 0.1432 0.3226 0.0209  0.0037  0.0416  101 HIS B CG  
3033  N  ND1 . HIS B  101 ? 0.2714 0.1805 0.4627 0.0772  0.0652  0.0843  101 HIS B ND1 
3034  C  CD2 . HIS B  101 ? 0.2549 0.1653 0.2849 0.0696  0.0346  -0.0046 101 HIS B CD2 
3035  C  CE1 . HIS B  101 ? 0.2425 0.1448 0.4817 0.0474  0.1023  0.0498  101 HIS B CE1 
3036  N  NE2 . HIS B  101 ? 0.2556 0.1762 0.4147 0.0441  0.0351  -0.0003 101 HIS B NE2 
3037  N  N   . GLY B  102 ? 0.1228 0.0856 0.1316 0.0035  0.0542  0.0149  102 GLY B N   
3038  C  CA  . GLY B  102 ? 0.1324 0.0851 0.1118 0.0028  0.0467  0.0027  102 GLY B CA  
3039  C  C   . GLY B  102 ? 0.1127 0.0854 0.1234 -0.0070 0.0335  0.0208  102 GLY B C   
3040  O  O   . GLY B  102 ? 0.1231 0.0917 0.1261 -0.0035 0.0306  0.0280  102 GLY B O   
3041  N  N   . SER B  103 ? 0.0917 0.0940 0.1019 0.0008  0.0346  0.0171  103 SER B N   
3042  C  CA  . SER B  103 ? 0.1023 0.0918 0.1014 0.0086  0.0403  0.0197  103 SER B CA  
3043  C  C   . SER B  103 ? 0.0848 0.0800 0.1058 0.0151  0.0320  0.0175  103 SER B C   
3044  O  O   . SER B  103 ? 0.0861 0.1259 0.1421 -0.0052 0.0432  -0.0060 103 SER B O   
3045  C  CB  . SER B  103 ? 0.1028 0.0820 0.1055 0.0094  0.0285  0.0265  103 SER B CB  
3046  O  OG  . SER B  103 ? 0.1084 0.0772 0.1143 0.0110  0.0208  0.0174  103 SER B OG  
3047  N  N   . GLU B  104 ? 0.0996 0.0703 0.0897 0.0048  0.0247  0.0132  104 GLU B N   
3048  C  CA  . GLU B  104 ? 0.0935 0.0698 0.1098 0.0116  0.0105  0.0166  104 GLU B CA  
3049  C  C   . GLU B  104 ? 0.0701 0.0841 0.0899 0.0077  0.0218  0.0082  104 GLU B C   
3050  O  O   . GLU B  104 ? 0.0818 0.0707 0.1222 0.0038  0.0165  0.0152  104 GLU B O   
3051  C  CB  . GLU B  104 ? 0.0931 0.0803 0.1033 0.0148  0.0256  0.0221  104 GLU B CB  
3052  C  CG  . GLU B  104 ? 0.1224 0.0606 0.0948 0.0194  0.0238  0.0245  104 GLU B CG  
3053  C  CD  . GLU B  104 ? 0.0734 0.0971 0.0961 0.0037  0.0204  0.0170  104 GLU B CD  
3054  O  OE1 . GLU B  104 ? 0.0881 0.0920 0.1168 0.0001  0.0302  -0.0008 104 GLU B OE1 
3055  O  OE2 . GLU B  104 ? 0.0816 0.0872 0.1459 0.0044  0.0253  0.0206  104 GLU B OE2 
3056  N  N   . HIS B  105 ? 0.0865 0.0777 0.0974 0.0175  0.0254  0.0253  105 HIS B N   
3057  C  CA  . HIS B  105 ? 0.0913 0.0739 0.1014 0.0065  0.0209  0.0149  105 HIS B CA  
3058  C  C   . HIS B  105 ? 0.0899 0.0610 0.0952 -0.0008 0.0140  0.0094  105 HIS B C   
3059  O  O   . HIS B  105 ? 0.1167 0.0847 0.0951 0.0131  0.0105  0.0078  105 HIS B O   
3060  C  CB  . HIS B  105 ? 0.0942 0.0739 0.0958 0.0057  0.0296  0.0105  105 HIS B CB  
3061  C  CG  . HIS B  105 ? 0.0825 0.0782 0.0856 0.0049  0.0179  0.0165  105 HIS B CG  
3062  N  ND1 . HIS B  105 ? 0.0931 0.0788 0.1041 0.0071  0.0153  0.0170  105 HIS B ND1 
3063  C  CD2 . HIS B  105 ? 0.0821 0.0856 0.0906 0.0017  0.0274  0.0184  105 HIS B CD2 
3064  C  CE1 . HIS B  105 ? 0.0949 0.1037 0.0948 -0.0068 0.0149  0.0012  105 HIS B CE1 
3065  N  NE2 . HIS B  105 ? 0.0750 0.0979 0.1036 0.0013  0.0182  0.0032  105 HIS B NE2 
3066  N  N   . THR B  106 ? 0.0895 0.0885 0.1080 0.0087  0.0108  0.0252  106 THR B N   
3067  C  CA  . THR B  106 ? 0.0958 0.0734 0.1518 0.0175  0.0166  0.0137  106 THR B CA  
3068  C  C   . THR B  106 ? 0.1073 0.0829 0.1165 0.0098  -0.0021 0.0126  106 THR B C   
3069  O  O   . THR B  106 ? 0.1200 0.0895 0.1217 0.0093  0.0013  0.0239  106 THR B O   
3070  C  CB  . THR B  106 ? 0.0927 0.1168 0.1392 0.0109  0.0195  0.0104  106 THR B CB  
3071  O  OG1 . THR B  106 ? 0.1100 0.1053 0.1560 0.0228  0.0143  0.0043  106 THR B OG1 
3072  C  CG2 . THR B  106 ? 0.1147 0.1118 0.1779 -0.0126 0.0362  0.0317  106 THR B CG2 
3073  N  N   . VAL B  107 ? 0.1228 0.0703 0.1597 0.0165  -0.0074 0.0313  107 VAL B N   
3074  C  CA  . VAL B  107 ? 0.1310 0.0890 0.1808 -0.0037 -0.0240 0.0513  107 VAL B CA  
3075  C  C   . VAL B  107 ? 0.1285 0.0649 0.2125 -0.0115 -0.0250 0.0086  107 VAL B C   
3076  O  O   . VAL B  107 ? 0.1599 0.0904 0.2263 0.0236  -0.0527 0.0121  107 VAL B O   
3077  C  CB  . VAL B  107 ? 0.1088 0.1134 0.2108 0.0020  -0.0281 0.0432  107 VAL B CB  
3078  C  CG1 . VAL B  107 ? 0.1499 0.1523 0.2183 -0.0104 -0.0021 0.0744  107 VAL B CG1 
3079  C  CG2 . VAL B  107 ? 0.1091 0.1392 0.2386 0.0005  -0.0102 0.0533  107 VAL B CG2 
3080  N  N   . SER B  108 ? 0.1278 0.0960 0.1944 0.0071  -0.0182 0.0461  108 SER B N   
3081  C  CA  . SER B  108 ? 0.1389 0.1014 0.2048 0.0250  -0.0137 0.0340  108 SER B CA  
3082  C  C   . SER B  108 ? 0.1217 0.1230 0.2143 0.0489  -0.0170 0.0204  108 SER B C   
3083  O  O   . SER B  108 ? 0.1543 0.1172 0.2459 0.0430  -0.0164 0.0054  108 SER B O   
3084  C  CB  . SER B  108 ? 0.1886 0.1120 0.2838 0.0217  -0.0207 0.0854  108 SER B CB  
3085  O  OG  . SER B  108 ? 0.2601 0.1484 0.2693 -0.0037 -0.0206 0.1124  108 SER B OG  
3086  N  N   . GLY B  109 ? 0.1350 0.1208 0.1784 0.0230  -0.0034 0.0359  109 GLY B N   
3087  C  CA  . GLY B  109 ? 0.1271 0.1660 0.1726 0.0406  -0.0003 0.0276  109 GLY B CA  
3088  C  C   . GLY B  109 ? 0.1373 0.2829 0.1962 0.0824  0.0200  0.0038  109 GLY B C   
3089  O  O   . GLY B  109 ? 0.2122 0.4142 0.1841 0.0998  0.0373  0.0401  109 GLY B O   
3090  N  N   . GLN B  110 ? 0.1757 0.1726 0.2030 0.0913  -0.0285 -0.0375 110 GLN B N   
3091  C  CA  . GLN B  110 ? 0.2099 0.2064 0.2316 0.1002  -0.0718 -0.0568 110 GLN B CA  
3092  C  C   . GLN B  110 ? 0.1218 0.1755 0.1921 0.0410  0.0051  0.0163  110 GLN B C   
3093  O  O   . GLN B  110 ? 0.1217 0.0988 0.1635 0.0049  0.0174  0.0211  110 GLN B O   
3094  C  CB  . GLN B  110 ? 0.3140 0.1878 0.2782 0.1005  -0.1052 -0.0505 110 GLN B CB  
3095  C  CG  . GLN B  110 ? 0.2233 0.1392 0.3447 0.0335  -0.0265 -0.0085 110 GLN B CG  
3096  C  CD  . GLN B  110 ? 0.2303 0.2427 0.3693 0.0723  0.0035  -0.0074 110 GLN B CD  
3097  O  OE1 . GLN B  110 ? 0.5770 0.3758 0.4183 0.1724  0.0311  -0.1040 110 GLN B OE1 
3098  N  NE2 . GLN B  110 ? 0.3406 0.3362 0.5310 0.1154  -0.0922 0.0254  110 GLN B NE2 
3099  N  N   . HIS B  111 ? 0.1017 0.1998 0.1962 0.0417  0.0375  -0.0055 111 HIS B N   
3100  C  CA  . HIS B  111 ? 0.1055 0.1410 0.1588 -0.0048 0.0379  0.0245  111 HIS B CA  
3101  C  C   . HIS B  111 ? 0.1120 0.1421 0.1538 0.0259  0.0115  -0.0135 111 HIS B C   
3102  O  O   . HIS B  111 ? 0.1578 0.1879 0.4070 0.0812  -0.0478 -0.0974 111 HIS B O   
3103  C  CB  . HIS B  111 ? 0.1851 0.1544 0.2206 -0.0357 0.0798  0.0206  111 HIS B CB  
3104  C  CG  . HIS B  111 ? 0.1118 0.1272 0.2179 0.0187  0.0778  0.0551  111 HIS B CG  
3105  N  ND1 . HIS B  111 ? 0.1850 0.1744 0.2096 0.0606  0.0678  0.0234  111 HIS B ND1 
3106  C  CD2 . HIS B  111 ? 0.1421 0.1554 0.2806 -0.0031 0.0410  -0.0208 111 HIS B CD2 
3107  C  CE1 . HIS B  111 ? 0.1738 0.1802 0.2220 0.0041  0.0820  0.0020  111 HIS B CE1 
3108  N  NE2 . HIS B  111 ? 0.1856 0.1924 0.3248 -0.0041 0.1158  -0.0557 111 HIS B NE2 
3109  N  N   . PHE B  112 ? 0.1091 0.0933 0.1188 0.0223  0.0289  0.0267  112 PHE B N   
3110  C  CA  . PHE B  112 ? 0.1012 0.0945 0.1184 0.0062  0.0288  0.0151  112 PHE B CA  
3111  C  C   . PHE B  112 ? 0.0954 0.0716 0.1265 0.0163  0.0441  0.0074  112 PHE B C   
3112  O  O   . PHE B  112 ? 0.1269 0.0988 0.1270 -0.0019 0.0388  0.0237  112 PHE B O   
3113  C  CB  . PHE B  112 ? 0.1199 0.0996 0.1326 0.0154  0.0496  0.0384  112 PHE B CB  
3114  C  CG  . PHE B  112 ? 0.1170 0.1504 0.1656 0.0299  0.0560  0.0628  112 PHE B CG  
3115  C  CD1 . PHE B  112 ? 0.1890 0.2231 0.1515 0.0542  0.0480  0.0741  112 PHE B CD1 
3116  C  CD2 . PHE B  112 ? 0.2305 0.1301 0.2181 0.0122  0.0869  0.0593  112 PHE B CD2 
3117  C  CE1 . PHE B  112 ? 0.2188 0.3989 0.1863 0.0960  0.0851  0.1710  112 PHE B CE1 
3118  C  CE2 . PHE B  112 ? 0.2678 0.1797 0.2838 0.0527  0.1430  0.1174  112 PHE B CE2 
3119  C  CZ  . PHE B  112 ? 0.3030 0.3488 0.2782 0.0923  0.1486  0.1957  112 PHE B CZ  
3120  N  N   . ALA B  113 ? 0.1041 0.0834 0.1121 0.0188  0.0368  0.0063  113 ALA B N   
3121  C  CA  . ALA B  113 ? 0.1233 0.0822 0.1163 0.0198  0.0522  0.0038  113 ALA B CA  
3122  C  C   . ALA B  113 ? 0.0994 0.0777 0.0854 -0.0015 0.0447  0.0068  113 ALA B C   
3123  O  O   . ALA B  113 ? 0.1159 0.0852 0.0929 0.0046  0.0478  0.0109  113 ALA B O   
3124  C  CB  . ALA B  113 ? 0.1577 0.0957 0.1200 0.0060  0.0388  -0.0151 113 ALA B CB  
3125  N  N   . ALA B  114 ? 0.1064 0.0605 0.0927 0.0120  0.0408  0.0074  114 ALA B N   
3126  C  CA  . ALA B  114 ? 0.0895 0.0768 0.0877 0.0097  0.0454  0.0057  114 ALA B CA  
3127  C  C   . ALA B  114 ? 0.0773 0.0741 0.0809 0.0060  0.0260  0.0152  114 ALA B C   
3128  O  O   . ALA B  114 ? 0.0913 0.0669 0.0790 0.0013  0.0277  0.0120  114 ALA B O   
3129  C  CB  . ALA B  114 ? 0.1111 0.0971 0.0791 0.0247  0.0259  0.0152  114 ALA B CB  
3130  N  N   . GLU B  115 ? 0.0822 0.0698 0.0852 0.0083  0.0373  0.0104  115 GLU B N   
3131  C  CA  . GLU B  115 ? 0.0798 0.0736 0.0863 0.0105  0.0445  0.0089  115 GLU B CA  
3132  C  C   . GLU B  115 ? 0.0908 0.0753 0.0642 0.0065  0.0223  0.0162  115 GLU B C   
3133  O  O   . GLU B  115 ? 0.0859 0.0843 0.0899 0.0140  0.0450  0.0315  115 GLU B O   
3134  C  CB  . GLU B  115 ? 0.0815 0.0809 0.0904 -0.0046 0.0384  0.0054  115 GLU B CB  
3135  C  CG  . GLU B  115 ? 0.0781 0.0922 0.0741 0.0052  0.0210  0.0081  115 GLU B CG  
3136  C  CD  . GLU B  115 ? 0.0904 0.0768 0.0797 0.0031  0.0255  0.0115  115 GLU B CD  
3137  O  OE1 . GLU B  115 ? 0.0723 0.0929 0.1010 0.0027  0.0204  0.0088  115 GLU B OE1 
3138  O  OE2 . GLU B  115 ? 0.0848 0.0933 0.0883 0.0109  0.0179  0.0146  115 GLU B OE2 
3139  N  N   . LEU B  116 ? 0.0751 0.0654 0.0694 0.0082  0.0307  0.0065  116 LEU B N   
3140  C  CA  . LEU B  116 ? 0.0653 0.0746 0.0784 0.0068  0.0264  -0.0003 116 LEU B CA  
3141  C  C   . LEU B  116 ? 0.0543 0.0645 0.0606 0.0098  0.0242  0.0129  116 LEU B C   
3142  O  O   . LEU B  116 ? 0.0841 0.0640 0.0723 0.0026  0.0280  0.0234  116 LEU B O   
3143  C  CB  . LEU B  116 ? 0.0750 0.0818 0.1035 0.0037  0.0138  0.0088  116 LEU B CB  
3144  C  CG  . LEU B  116 ? 0.0829 0.0892 0.1136 -0.0001 0.0120  0.0046  116 LEU B CG  
3145  C  CD1 . LEU B  116 ? 0.0899 0.1079 0.1315 0.0054  0.0133  0.0335  116 LEU B CD1 
3146  C  CD2 . LEU B  116 ? 0.0874 0.1109 0.1348 -0.0104 0.0263  0.0054  116 LEU B CD2 
3147  N  N   . HIS B  117 ? 0.0777 0.0568 0.0658 0.0103  0.0271  0.0119  117 HIS B N   
3148  C  CA  . HIS B  117 ? 0.0615 0.0672 0.0746 0.0041  0.0216  -0.0003 117 HIS B CA  
3149  C  C   . HIS B  117 ? 0.0669 0.0640 0.0683 0.0091  0.0263  0.0179  117 HIS B C   
3150  O  O   . HIS B  117 ? 0.0876 0.0802 0.0716 0.0174  0.0274  0.0175  117 HIS B O   
3151  C  CB  . HIS B  117 ? 0.0718 0.0685 0.0861 0.0024  0.0261  0.0015  117 HIS B CB  
3152  C  CG  . HIS B  117 ? 0.0680 0.0705 0.0737 -0.0027 0.0342  0.0092  117 HIS B CG  
3153  N  ND1 . HIS B  117 ? 0.0721 0.0753 0.0658 -0.0055 0.0226  0.0082  117 HIS B ND1 
3154  C  CD2 . HIS B  117 ? 0.0809 0.0683 0.0741 -0.0026 0.0215  0.0052  117 HIS B CD2 
3155  C  CE1 . HIS B  117 ? 0.0804 0.0802 0.0836 0.0082  0.0178  0.0154  117 HIS B CE1 
3156  N  NE2 . HIS B  117 ? 0.0714 0.0794 0.0868 0.0024  0.0203  0.0116  117 HIS B NE2 
3157  N  N   . ILE B  118 ? 0.0694 0.0712 0.0741 0.0044  0.0348  0.0149  118 ILE B N   
3158  C  CA  . ILE B  118 ? 0.0672 0.0859 0.0933 0.0133  0.0187  0.0060  118 ILE B CA  
3159  C  C   . ILE B  118 ? 0.0741 0.0931 0.0741 0.0258  0.0166  0.0119  118 ILE B C   
3160  O  O   . ILE B  118 ? 0.0951 0.1079 0.0710 0.0249  0.0275  0.0147  118 ILE B O   
3161  C  CB  . ILE B  118 ? 0.0776 0.1100 0.0716 0.0024  0.0181  0.0226  118 ILE B CB  
3162  C  CG1 . ILE B  118 ? 0.1041 0.0991 0.0836 -0.0062 0.0256  -0.0059 118 ILE B CG1 
3163  C  CG2 . ILE B  118 ? 0.0706 0.1626 0.0976 0.0194  0.0178  0.0187  118 ILE B CG2 
3164  C  CD1 . ILE B  118 ? 0.1226 0.1434 0.1294 -0.0366 0.0423  0.0281  118 ILE B CD1 
3165  N  N   . VAL B  119 ? 0.0922 0.0816 0.0958 0.0291  0.0261  -0.0026 119 VAL B N   
3166  C  CA  . VAL B  119 ? 0.1037 0.0864 0.1120 0.0218  0.0313  0.0052  119 VAL B CA  
3167  C  C   . VAL B  119 ? 0.0960 0.1058 0.0940 0.0203  0.0215  -0.0162 119 VAL B C   
3168  O  O   . VAL B  119 ? 0.0960 0.1326 0.0996 0.0381  0.0244  0.0070  119 VAL B O   
3169  C  CB  . VAL B  119 ? 0.1285 0.0906 0.0996 0.0219  0.0403  0.0234  119 VAL B CB  
3170  C  CG1 . VAL B  119 ? 0.1385 0.1082 0.1243 0.0088  0.0244  -0.0107 119 VAL B CG1 
3171  C  CG2 . VAL B  119 ? 0.1155 0.1392 0.1242 0.0320  0.0689  0.0300  119 VAL B CG2 
3172  N  N   . HIS B  120 ? 0.0985 0.0873 0.0983 0.0250  0.0315  -0.0065 120 HIS B N   
3173  C  CA  . HIS B  120 ? 0.1159 0.0998 0.1021 0.0263  0.0461  -0.0174 120 HIS B CA  
3174  C  C   . HIS B  120 ? 0.1240 0.1089 0.1048 0.0469  0.0204  -0.0023 120 HIS B C   
3175  O  O   . HIS B  120 ? 0.1298 0.1098 0.0944 0.0379  0.0209  -0.0160 120 HIS B O   
3176  C  CB  . HIS B  120 ? 0.1195 0.1288 0.0952 0.0113  0.0243  0.0035  120 HIS B CB  
3177  C  CG  . HIS B  120 ? 0.1080 0.1066 0.0901 0.0255  0.0337  0.0060  120 HIS B CG  
3178  N  ND1 . HIS B  120 ? 0.0958 0.1285 0.0953 0.0211  0.0408  0.0000  120 HIS B ND1 
3179  C  CD2 . HIS B  120 ? 0.0971 0.1237 0.1086 0.0098  0.0229  0.0277  120 HIS B CD2 
3180  C  CE1 . HIS B  120 ? 0.1001 0.1174 0.1048 -0.0074 0.0394  0.0291  120 HIS B CE1 
3181  N  NE2 . HIS B  120 ? 0.0992 0.1188 0.1199 0.0115  0.0361  0.0196  120 HIS B NE2 
3182  N  N   . TYR B  121 ? 0.1217 0.1208 0.1283 0.0368  0.0381  -0.0261 121 TYR B N   
3183  C  CA  . TYR B  121 ? 0.1360 0.1260 0.1450 0.0342  0.0292  -0.0463 121 TYR B CA  
3184  C  C   . TYR B  121 ? 0.1244 0.1330 0.1376 0.0592  0.0175  -0.0392 121 TYR B C   
3185  O  O   . TYR B  121 ? 0.1231 0.1710 0.1188 0.0549  0.0331  -0.0173 121 TYR B O   
3186  C  CB  . TYR B  121 ? 0.1894 0.1579 0.1660 0.0658  0.0333  -0.0126 121 TYR B CB  
3187  C  CG  . TYR B  121 ? 0.1868 0.1454 0.1465 0.0754  0.0306  -0.0098 121 TYR B CG  
3188  C  CD1 . TYR B  121 ? 0.1777 0.1757 0.1472 0.0608  0.0379  0.0127  121 TYR B CD1 
3189  C  CD2 . TYR B  121 ? 0.2133 0.2030 0.1791 0.1055  0.0549  -0.0054 121 TYR B CD2 
3190  C  CE1 . TYR B  121 ? 0.2318 0.1978 0.1638 0.0860  0.0303  0.0463  121 TYR B CE1 
3191  C  CE2 . TYR B  121 ? 0.2669 0.2402 0.1717 0.1676  0.0939  0.0571  121 TYR B CE2 
3192  C  CZ  . TYR B  121 ? 0.2581 0.2431 0.1854 0.1150  0.0656  0.0824  121 TYR B CZ  
3193  O  OH  . TYR B  121 ? 0.2824 0.3901 0.3704 0.1887  0.0738  0.1776  121 TYR B OH  
3194  N  N   . ASN B  122 ? 0.1653 0.1702 0.1439 0.0688  0.0292  -0.0741 122 ASN B N   
3195  C  CA  . ASN B  122 ? 0.1583 0.1870 0.1224 0.0822  0.0070  -0.0511 122 ASN B CA  
3196  C  C   . ASN B  122 ? 0.1299 0.1938 0.1237 0.0588  0.0318  -0.0357 122 ASN B C   
3197  O  O   . ASN B  122 ? 0.1895 0.1876 0.1538 0.0799  0.0211  -0.0370 122 ASN B O   
3198  C  CB  . ASN B  122 ? 0.1807 0.2113 0.1475 0.0732  -0.0071 -0.0527 122 ASN B CB  
3199  C  CG  . ASN B  122 ? 0.2364 0.2019 0.1441 0.0776  -0.0261 -0.0599 122 ASN B CG  
3200  O  OD1 . ASN B  122 ? 0.2176 0.2438 0.1184 0.0890  0.0255  -0.0355 122 ASN B OD1 
3201  N  ND2 . ASN B  122 ? 0.3842 0.2156 0.1624 0.0573  -0.0733 -0.0165 122 ASN B ND2 
3202  N  N   . SER B  123 ? 0.1362 0.2213 0.1324 0.0706  0.0281  -0.0397 123 SER B N   
3203  C  CA  . SER B  123 ? 0.1313 0.2732 0.1386 0.0926  0.0248  -0.0593 123 SER B CA  
3204  C  C   . SER B  123 ? 0.1967 0.2506 0.1340 0.1164  0.0285  -0.0308 123 SER B C   
3205  O  O   . SER B  123 ? 0.2201 0.2791 0.1559 0.1377  0.0502  -0.0133 123 SER B O   
3206  C  CB  . SER B  123 ? 0.2158 0.2405 0.1125 0.0961  0.0046  -0.0326 123 SER B CB  
3207  O  OG  . SER B  123 ? 0.1674 0.2614 0.1545 0.0674  0.0176  -0.0421 123 SER B OG  
3208  N  N   . ASP B  124 ? 0.1910 0.3151 0.1143 0.1194  0.0450  -0.0272 124 ASP B N   
3209  C  CA  . ASP B  124 ? 0.2653 0.2583 0.1337 0.1014  0.0693  -0.0263 124 ASP B CA  
3210  C  C   . ASP B  124 ? 0.2682 0.2626 0.1102 0.0965  0.0474  -0.0476 124 ASP B C   
3211  O  O   . ASP B  124 ? 0.2451 0.2675 0.2082 0.1077  0.0586  -0.0599 124 ASP B O   
3212  C  CB  . ASP B  124 ? 0.2662 0.3246 0.1375 0.1173  0.0710  -0.0049 124 ASP B CB  
3213  C  CG  . ASP B  124 ? 0.3036 0.3265 0.1454 0.1203  0.0577  -0.0586 124 ASP B CG  
3214  O  OD1 . ASP B  124 ? 0.2845 0.4219 0.1374 0.0434  0.0740  -0.0340 124 ASP B OD1 
3215  O  OD2 . ASP B  124 ? 0.3240 0.3246 0.1498 0.1370  0.0984  -0.0219 124 ASP B OD2 
3216  N  N   . LEU B  125 ? 0.2407 0.2630 0.1238 0.0912  0.0259  -0.0505 125 LEU B N   
3217  C  CA  . LEU B  125 ? 0.2490 0.2486 0.1017 0.0737  0.0351  -0.0505 125 LEU B CA  
3218  C  C   . LEU B  125 ? 0.2662 0.2500 0.1380 0.1041  0.0584  -0.0311 125 LEU B C   
3219  O  O   . LEU B  125 ? 0.3923 0.2429 0.1805 0.1287  0.0226  -0.0921 125 LEU B O   
3220  C  CB  . LEU B  125 ? 0.2551 0.2597 0.1711 0.0873  0.0269  -0.0277 125 LEU B CB  
3221  C  CG  . LEU B  125 ? 0.3440 0.3019 0.1538 0.0790  0.0265  -0.0197 125 LEU B CG  
3222  C  CD1 . LEU B  125 ? 0.3720 0.2779 0.1858 0.0621  -0.0373 -0.0788 125 LEU B CD1 
3223  C  CD2 . LEU B  125 ? 0.4063 0.2870 0.1756 0.0868  0.0339  -0.0776 125 LEU B CD2 
3224  N  N   . TYR B  126 ? 0.2451 0.2003 0.1213 0.0922  0.0425  -0.0121 126 TYR B N   
3225  C  CA  . TYR B  126 ? 0.2822 0.1999 0.1322 0.1052  0.0361  0.0081  126 TYR B CA  
3226  C  C   . TYR B  126 ? 0.3016 0.2222 0.1228 0.1190  0.0324  0.0099  126 TYR B C   
3227  O  O   . TYR B  126 ? 0.2603 0.2660 0.1642 0.1203  0.0221  0.0010  126 TYR B O   
3228  C  CB  . TYR B  126 ? 0.2522 0.2294 0.1678 0.0921  0.0237  -0.0230 126 TYR B CB  
3229  C  CG  . TYR B  126 ? 0.2637 0.2084 0.1942 0.0868  0.0187  -0.0333 126 TYR B CG  
3230  C  CD1 . TYR B  126 ? 0.3124 0.2470 0.2958 0.0926  -0.0076 -0.0847 126 TYR B CD1 
3231  C  CD2 . TYR B  126 ? 0.2509 0.2440 0.1590 0.0812  0.0359  -0.0287 126 TYR B CD2 
3232  C  CE1 . TYR B  126 ? 0.3393 0.3379 0.3125 0.1475  -0.0461 -0.1449 126 TYR B CE1 
3233  C  CE2 . TYR B  126 ? 0.2709 0.2842 0.1759 0.1324  0.0151  -0.0443 126 TYR B CE2 
3234  C  CZ  . TYR B  126 ? 0.2919 0.3476 0.2179 0.1015  -0.0187 -0.0825 126 TYR B CZ  
3235  O  OH  . TYR B  126 ? 0.3012 0.4406 0.2470 0.1259  -0.0120 -0.1252 126 TYR B OH  
3236  N  N   . PRO B  127 ? 0.3833 0.2718 0.1572 0.1829  0.0487  0.0452  127 PRO B N   
3237  C  CA  . PRO B  127 ? 0.3790 0.3382 0.1635 0.2063  0.0166  0.0485  127 PRO B CA  
3238  C  C   . PRO B  127 ? 0.2531 0.3497 0.1787 0.1090  0.0239  0.0200  127 PRO B C   
3239  O  O   . PRO B  127 ? 0.2917 0.4576 0.1897 0.0864  0.0017  0.0848  127 PRO B O   
3240  C  CB  . PRO B  127 ? 0.4591 0.3172 0.2237 0.2073  -0.0218 0.0086  127 PRO B CB  
3241  C  CG  . PRO B  127 ? 0.5906 0.2917 0.3097 0.1547  -0.0245 0.0515  127 PRO B CG  
3242  C  CD  . PRO B  127 ? 0.4656 0.2029 0.2766 0.1738  0.0710  0.0450  127 PRO B CD  
3243  N  N   . ASP B  128 ? 0.2651 0.2533 0.1984 0.1102  0.0458  0.0266  128 ASP B N   
3244  C  CA  . ASP B  128 ? 0.2066 0.2874 0.1432 0.0271  0.0179  0.0265  128 ASP B CA  
3245  C  C   . ASP B  128 ? 0.2211 0.2443 0.1405 0.0379  0.0300  -0.0137 128 ASP B C   
3246  O  O   . ASP B  128 ? 0.2565 0.2161 0.1896 0.0649  0.0115  -0.0357 128 ASP B O   
3247  C  CB  . ASP B  128 ? 0.2544 0.2646 0.2540 0.0178  -0.0034 0.0788  128 ASP B CB  
3248  C  CG  . ASP B  128 ? 0.3226 0.1984 0.2755 0.0590  0.0274  0.0032  128 ASP B CG  
3249  O  OD1 . ASP B  128 ? 0.4095 0.4936 0.4830 0.1282  -0.0076 -0.2109 128 ASP B OD1 
3250  O  OD2 . ASP B  128 ? 0.3093 0.4311 0.4041 -0.0403 0.0531  0.0043  128 ASP B OD2 
3251  N  N   . ALA B  129 ? 0.2203 0.2181 0.1860 0.0212  0.0476  -0.0052 129 ALA B N   
3252  C  CA  . ALA B  129 ? 0.2231 0.1865 0.1827 0.0156  0.0355  -0.0518 129 ALA B CA  
3253  C  C   . ALA B  129 ? 0.2222 0.1295 0.2010 0.0249  0.0496  -0.0710 129 ALA B C   
3254  O  O   . ALA B  129 ? 0.2342 0.1560 0.2319 0.0170  0.0351  -0.0491 129 ALA B O   
3255  C  CB  . ALA B  129 ? 0.2563 0.2008 0.1805 -0.0006 0.0645  -0.0697 129 ALA B CB  
3256  N  N   A SER B  130 ? 0.2838 0.1626 0.2380 0.0068  0.0478  -0.0458 130 SER B N   
3257  N  N   B SER B  130 ? 0.2890 0.1691 0.2402 0.0003  0.0458  -0.0399 130 SER B N   
3258  C  CA  A SER B  130 ? 0.2748 0.1225 0.2973 0.0190  0.0335  -0.0474 130 SER B CA  
3259  C  CA  B SER B  130 ? 0.2734 0.1990 0.2989 -0.0126 0.0305  0.0026  130 SER B CA  
3260  C  C   A SER B  130 ? 0.2493 0.1816 0.2944 0.0724  -0.0120 -0.0702 130 SER B C   
3261  C  C   B SER B  130 ? 0.2238 0.2203 0.3043 0.0211  -0.0082 -0.0297 130 SER B C   
3262  O  O   A SER B  130 ? 0.2849 0.1975 0.3804 0.0344  -0.0254 -0.1155 130 SER B O   
3263  O  O   B SER B  130 ? 0.2355 0.1057 0.3754 0.0057  -0.0306 0.0262  130 SER B O   
3264  C  CB  A SER B  130 ? 0.3641 0.1465 0.2389 -0.0173 0.0055  -0.0597 130 SER B CB  
3265  C  CB  B SER B  130 ? 0.3407 0.3098 0.2377 -0.0746 0.0412  0.0700  130 SER B CB  
3266  O  OG  A SER B  130 ? 0.3788 0.1376 0.4834 -0.0364 0.0035  0.0264  130 SER B OG  
3267  O  OG  B SER B  130 ? 0.5842 0.3556 0.2323 -0.1037 0.0241  0.0672  130 SER B OG  
3268  N  N   . THR B  131 ? 0.3352 0.1457 0.3407 0.0038  0.0584  -0.0627 131 THR B N   
3269  C  CA  . THR B  131 ? 0.3357 0.1414 0.3481 0.0368  0.0427  -0.0671 131 THR B CA  
3270  C  C   . THR B  131 ? 0.2258 0.2247 0.3233 0.0028  -0.0013 -0.0943 131 THR B C   
3271  O  O   . THR B  131 ? 0.3057 0.2467 0.3319 0.0138  -0.0144 -0.1563 131 THR B O   
3272  C  CB  . THR B  131 ? 0.3808 0.2125 0.3007 0.1448  0.0118  -0.0747 131 THR B CB  
3273  O  OG1 . THR B  131 ? 0.4043 0.2355 0.3729 0.1424  -0.0122 -0.0742 131 THR B OG1 
3274  C  CG2 . THR B  131 ? 0.5040 0.3612 0.3978 0.1739  -0.0102 -0.2263 131 THR B CG2 
3275  N  N   . ALA B  132 ? 0.2240 0.1800 0.2745 0.0355  0.0229  -0.1172 132 ALA B N   
3276  C  CA  . ALA B  132 ? 0.2280 0.2138 0.2328 0.0656  0.0157  -0.0829 132 ALA B CA  
3277  C  C   . ALA B  132 ? 0.2190 0.2145 0.2205 0.0399  0.0296  -0.1328 132 ALA B C   
3278  O  O   . ALA B  132 ? 0.2179 0.2057 0.2653 0.0427  0.0013  -0.0714 132 ALA B O   
3279  C  CB  . ALA B  132 ? 0.1811 0.2190 0.2125 0.0242  0.0329  -0.0540 132 ALA B CB  
3280  N  N   . SER B  133 ? 0.2087 0.2066 0.2556 0.0146  0.0350  -0.0799 133 SER B N   
3281  C  CA  . SER B  133 ? 0.1993 0.1808 0.2481 0.0296  0.0220  -0.0913 133 SER B CA  
3282  C  C   . SER B  133 ? 0.2282 0.1133 0.3109 0.0222  0.0068  -0.0160 133 SER B C   
3283  O  O   . SER B  133 ? 0.2245 0.1596 0.3418 0.0546  0.0285  0.0449  133 SER B O   
3284  C  CB  . SER B  133 ? 0.2436 0.2204 0.2896 -0.0350 0.0866  -0.0480 133 SER B CB  
3285  O  OG  . SER B  133 ? 0.2770 0.2197 0.2892 -0.0129 0.0399  -0.0062 133 SER B OG  
3286  N  N   A ASN B  134 ? 0.3289 0.1709 0.3138 0.0384  -0.0538 -0.1027 134 ASN B N   
3287  N  N   B ASN B  134 ? 0.3052 0.1342 0.3073 0.0425  -0.0883 -0.0630 134 ASN B N   
3288  C  CA  A ASN B  134 ? 0.3693 0.1052 0.3993 0.0482  -0.1283 -0.0259 134 ASN B CA  
3289  C  CA  B ASN B  134 ? 0.3526 0.2211 0.4372 -0.0718 -0.0698 -0.1076 134 ASN B CA  
3290  C  C   A ASN B  134 ? 0.3373 0.1094 0.4744 0.0930  -0.0019 -0.1391 134 ASN B C   
3291  C  C   B ASN B  134 ? 0.2585 0.2906 0.4095 -0.0430 -0.0355 -0.2073 134 ASN B C   
3292  O  O   A ASN B  134 ? 0.4032 0.2982 0.5800 0.0293  -0.1187 -0.1432 134 ASN B O   
3293  O  O   B ASN B  134 ? 0.3628 0.2289 0.4235 -0.0087 -0.0929 -0.1982 134 ASN B O   
3294  C  CB  A ASN B  134 ? 0.4943 0.2946 0.6532 -0.1261 0.0559  -0.1617 134 ASN B CB  
3295  C  CB  B ASN B  134 ? 0.6320 0.2723 0.6843 -0.2834 -0.1552 -0.1559 134 ASN B CB  
3296  C  CG  A ASN B  134 ? 0.8729 0.2210 0.7261 -0.1190 0.2446  0.1280  134 ASN B CG  
3297  C  CG  B ASN B  134 ? 1.0867 0.2247 0.9588 0.0362  0.0588  -0.1969 134 ASN B CG  
3298  O  OD1 A ASN B  134 ? 1.3882 0.3124 1.3408 0.1411  -0.3454 -0.3490 134 ASN B OD1 
3299  O  OD1 B ASN B  134 ? 1.4901 0.1547 1.3481 -0.0608 -0.2216 -0.0812 134 ASN B OD1 
3300  N  ND2 A ASN B  134 ? 0.4921 0.3242 0.4731 -0.0942 0.3305  -0.0684 134 ASN B ND2 
3301  N  ND2 B ASN B  134 ? 0.8148 0.1317 0.9255 -0.0688 -0.0088 -0.0516 134 ASN B ND2 
3302  N  N   A LYS B  135 ? 0.2658 0.2691 0.3149 0.0741  0.0445  -0.1275 135 LYS B N   
3303  N  N   B LYS B  135 ? 0.2639 0.2709 0.3149 0.0652  0.0443  -0.1288 135 LYS B N   
3304  C  CA  A LYS B  135 ? 0.3657 0.2754 0.2928 0.0298  0.0282  -0.1437 135 LYS B CA  
3305  C  CA  B LYS B  135 ? 0.3659 0.2867 0.3005 0.0286  0.0293  -0.1345 135 LYS B CA  
3306  C  C   A LYS B  135 ? 0.4160 0.3395 0.2447 0.0577  -0.0026 -0.1050 135 LYS B C   
3307  C  C   B LYS B  135 ? 0.4183 0.3409 0.2490 0.0531  -0.0088 -0.1022 135 LYS B C   
3308  O  O   A LYS B  135 ? 0.2267 0.3059 0.2470 0.0406  -0.0311 -0.0873 135 LYS B O   
3309  O  O   B LYS B  135 ? 0.2344 0.3100 0.2492 0.0370  -0.0306 -0.0824 135 LYS B O   
3310  C  CB  A LYS B  135 ? 0.3772 0.2138 0.3630 0.0346  0.1218  -0.0535 135 LYS B CB  
3311  C  CG  A LYS B  135 ? 0.3864 0.3255 0.4259 0.1351  0.0513  -0.0166 135 LYS B CG  
3312  N  N   . SER B  136 ? 0.6312 0.4672 0.3303 -0.1358 -0.1956 -0.0306 136 SER B N   
3313  C  CA  . SER B  136 ? 0.3616 0.4888 0.2100 -0.0877 -0.0483 -0.0359 136 SER B CA  
3314  C  C   . SER B  136 ? 0.3310 0.4029 0.2373 0.0186  -0.0159 -0.1431 136 SER B C   
3315  O  O   . SER B  136 ? 0.2915 0.3131 0.1680 -0.0204 0.0253  -0.0474 136 SER B O   
3316  N  N   . GLU B  137 ? 0.2951 0.3440 0.1917 0.0397  -0.0502 -0.0109 137 GLU B N   
3317  C  CA  . GLU B  137 ? 0.3402 0.2703 0.2476 0.0657  -0.0775 -0.0494 137 GLU B CA  
3318  C  C   . GLU B  137 ? 0.2632 0.2472 0.2141 0.0181  -0.0342 -0.0273 137 GLU B C   
3319  O  O   . GLU B  137 ? 0.2373 0.2775 0.2293 0.0205  -0.0252 0.0066  137 GLU B O   
3320  C  CB  . GLU B  137 ? 0.3831 0.5052 0.3199 -0.0052 -0.0978 0.1562  137 GLU B CB  
3321  C  CG  . GLU B  137 ? 0.4986 0.6855 0.4742 0.0156  -0.1133 0.3043  137 GLU B CG  
3322  C  CD  . GLU B  137 ? 0.7860 0.7628 0.5350 -0.0865 -0.2345 0.4912  137 GLU B CD  
3323  O  OE1 . GLU B  137 ? 0.6245 1.2472 0.7996 -0.0303 -0.4090 0.1438  137 GLU B OE1 
3324  O  OE2 . GLU B  137 ? 0.9067 0.4665 0.4616 0.1274  -0.2748 0.0057  137 GLU B OE2 
3325  N  N   . GLY B  138 ? 0.2334 0.2217 0.1906 -0.0013 -0.0375 -0.0465 138 GLY B N   
3326  C  CA  . GLY B  138 ? 0.1712 0.2224 0.1511 0.0406  0.0065  -0.0586 138 GLY B CA  
3327  C  C   . GLY B  138 ? 0.1211 0.1737 0.1703 0.0423  0.0208  -0.0617 138 GLY B C   
3328  O  O   . GLY B  138 ? 0.1414 0.2089 0.1784 0.0680  0.0217  -0.0803 138 GLY B O   
3329  N  N   . LEU B  139 ? 0.1448 0.1132 0.1441 0.0320  0.0200  -0.0342 139 LEU B N   
3330  C  CA  . LEU B  139 ? 0.1498 0.1308 0.1161 0.0322  0.0255  -0.0023 139 LEU B CA  
3331  C  C   . LEU B  139 ? 0.1220 0.1317 0.0897 0.0381  0.0223  -0.0186 139 LEU B C   
3332  O  O   . LEU B  139 ? 0.1240 0.1527 0.1167 0.0199  0.0063  -0.0232 139 LEU B O   
3333  C  CB  . LEU B  139 ? 0.1468 0.1204 0.1357 0.0168  0.0326  0.0119  139 LEU B CB  
3334  C  CG  . LEU B  139 ? 0.1502 0.1323 0.1668 0.0272  0.0571  -0.0043 139 LEU B CG  
3335  C  CD1 . LEU B  139 ? 0.1659 0.1326 0.1975 0.0153  0.0615  0.0124  139 LEU B CD1 
3336  C  CD2 . LEU B  139 ? 0.1371 0.1581 0.1583 0.0333  0.0212  0.0078  139 LEU B CD2 
3337  N  N   . ALA B  140 ? 0.1335 0.1242 0.0997 0.0452  0.0248  -0.0174 140 ALA B N   
3338  C  CA  . ALA B  140 ? 0.1335 0.1138 0.0942 0.0348  0.0183  -0.0129 140 ALA B CA  
3339  C  C   . ALA B  140 ? 0.1030 0.1234 0.0927 0.0331  0.0322  -0.0049 140 ALA B C   
3340  O  O   . ALA B  140 ? 0.1127 0.1258 0.1053 0.0406  0.0137  -0.0111 140 ALA B O   
3341  C  CB  . ALA B  140 ? 0.1244 0.1604 0.0985 0.0276  0.0430  -0.0059 140 ALA B CB  
3342  N  N   . VAL B  141 ? 0.1109 0.0821 0.0834 0.0181  0.0329  0.0034  141 VAL B N   
3343  C  CA  . VAL B  141 ? 0.1040 0.0764 0.0790 0.0207  0.0353  0.0027  141 VAL B CA  
3344  C  C   . VAL B  141 ? 0.0833 0.0895 0.0617 0.0230  0.0288  0.0109  141 VAL B C   
3345  O  O   . VAL B  141 ? 0.0973 0.1030 0.0734 0.0228  0.0141  0.0068  141 VAL B O   
3346  C  CB  . VAL B  141 ? 0.0944 0.1133 0.0909 0.0197  0.0342  0.0086  141 VAL B CB  
3347  C  CG1 . VAL B  141 ? 0.0856 0.1732 0.0707 0.0046  0.0379  0.0091  141 VAL B CG1 
3348  C  CG2 . VAL B  141 ? 0.1085 0.1124 0.1238 0.0046  0.0179  0.0337  141 VAL B CG2 
3349  N  N   . LEU B  142 ? 0.0816 0.0843 0.0622 0.0157  0.0326  0.0100  142 LEU B N   
3350  C  CA  . LEU B  142 ? 0.0865 0.0861 0.0750 0.0219  0.0226  0.0038  142 LEU B CA  
3351  C  C   . LEU B  142 ? 0.0931 0.0755 0.0562 0.0046  0.0164  0.0159  142 LEU B C   
3352  O  O   . LEU B  142 ? 0.1116 0.1012 0.0644 0.0278  0.0270  0.0226  142 LEU B O   
3353  C  CB  . LEU B  142 ? 0.0829 0.1179 0.0877 0.0010  0.0313  0.0115  142 LEU B CB  
3354  C  CG  . LEU B  142 ? 0.0936 0.1441 0.0879 0.0096  0.0278  0.0280  142 LEU B CG  
3355  C  CD1 . LEU B  142 ? 0.0956 0.1520 0.1412 0.0141  0.0229  0.0258  142 LEU B CD1 
3356  C  CD2 . LEU B  142 ? 0.0976 0.1852 0.0901 0.0207  0.0388  0.0368  142 LEU B CD2 
3357  N  N   . ALA B  143 ? 0.0852 0.0757 0.0784 0.0131  0.0348  0.0110  143 ALA B N   
3358  C  CA  . ALA B  143 ? 0.0869 0.0678 0.0764 0.0151  0.0353  0.0038  143 ALA B CA  
3359  C  C   . ALA B  143 ? 0.0712 0.0706 0.0730 0.0037  0.0252  0.0196  143 ALA B C   
3360  O  O   . ALA B  143 ? 0.1028 0.0825 0.0669 0.0032  0.0258  0.0205  143 ALA B O   
3361  C  CB  . ALA B  143 ? 0.0815 0.0809 0.0966 -0.0001 0.0114  0.0147  143 ALA B CB  
3362  N  N   . VAL B  144 ? 0.0845 0.0705 0.0626 0.0003  0.0219  0.0081  144 VAL B N   
3363  C  CA  . VAL B  144 ? 0.0952 0.0676 0.0707 0.0043  0.0292  0.0015  144 VAL B CA  
3364  C  C   . VAL B  144 ? 0.0904 0.0618 0.0815 -0.0091 0.0296  0.0078  144 VAL B C   
3365  O  O   . VAL B  144 ? 0.0952 0.0755 0.0825 0.0013  0.0381  0.0174  144 VAL B O   
3366  C  CB  . VAL B  144 ? 0.0915 0.0913 0.0915 0.0000  0.0266  0.0190  144 VAL B CB  
3367  C  CG1 . VAL B  144 ? 0.1277 0.0809 0.1086 -0.0020 0.0208  -0.0035 144 VAL B CG1 
3368  C  CG2 . VAL B  144 ? 0.1206 0.0987 0.0985 0.0132  0.0395  0.0144  144 VAL B CG2 
3369  N  N   . LEU B  145 ? 0.0861 0.0710 0.0918 0.0015  0.0274  0.0137  145 LEU B N   
3370  C  CA  . LEU B  145 ? 0.0807 0.0879 0.0906 0.0015  0.0283  -0.0010 145 LEU B CA  
3371  C  C   . LEU B  145 ? 0.0970 0.0623 0.0843 0.0049  0.0241  0.0093  145 LEU B C   
3372  O  O   . LEU B  145 ? 0.1023 0.0888 0.0961 -0.0197 0.0256  0.0026  145 LEU B O   
3373  C  CB  . LEU B  145 ? 0.1015 0.0861 0.1005 0.0148  0.0113  -0.0008 145 LEU B CB  
3374  C  CG  . LEU B  145 ? 0.1206 0.1176 0.1102 0.0259  -0.0027 -0.0043 145 LEU B CG  
3375  C  CD1 . LEU B  145 ? 0.1590 0.1744 0.1115 0.0329  -0.0138 0.0120  145 LEU B CD1 
3376  C  CD2 . LEU B  145 ? 0.1660 0.1315 0.1802 -0.0264 -0.0458 0.0028  145 LEU B CD2 
3377  N  N   . ILE B  146 ? 0.0973 0.0873 0.0784 0.0027  0.0318  0.0046  146 ILE B N   
3378  C  CA  . ILE B  146 ? 0.1033 0.0848 0.0856 0.0027  0.0138  -0.0017 146 ILE B CA  
3379  C  C   . ILE B  146 ? 0.0952 0.0827 0.0873 -0.0054 0.0200  -0.0026 146 ILE B C   
3380  O  O   . ILE B  146 ? 0.1089 0.0775 0.1194 0.0049  0.0456  -0.0052 146 ILE B O   
3381  C  CB  . ILE B  146 ? 0.1158 0.0804 0.0863 0.0096  0.0241  0.0000  146 ILE B CB  
3382  C  CG1 . ILE B  146 ? 0.1105 0.0807 0.1154 0.0187  0.0228  0.0000  146 ILE B CG1 
3383  C  CG2 . ILE B  146 ? 0.1335 0.0921 0.0956 0.0094  0.0071  -0.0219 146 ILE B CG2 
3384  C  CD1 . ILE B  146 ? 0.1252 0.0771 0.1233 0.0118  0.0230  0.0155  146 ILE B CD1 
3385  N  N   . GLU B  147 ? 0.1254 0.0721 0.1120 0.0066  0.0148  -0.0111 147 GLU B N   
3386  C  CA  . GLU B  147 ? 0.1398 0.0954 0.1191 0.0287  0.0044  -0.0215 147 GLU B CA  
3387  C  C   . GLU B  147 ? 0.1006 0.0625 0.1328 0.0023  0.0252  -0.0182 147 GLU B C   
3388  O  O   . GLU B  147 ? 0.1079 0.0985 0.1405 0.0059  0.0215  -0.0186 147 GLU B O   
3389  C  CB  . GLU B  147 ? 0.2522 0.1168 0.2201 0.0900  -0.0028 -0.0189 147 GLU B CB  
3390  C  CG  . GLU B  147 ? 0.2799 0.2603 0.2127 0.0379  -0.0005 0.0164  147 GLU B CG  
3391  C  CD  . GLU B  147 ? 0.4343 0.2838 0.2486 0.1500  -0.0287 0.0216  147 GLU B CD  
3392  O  OE1 . GLU B  147 ? 0.3576 0.3370 0.2689 0.1675  0.0071  0.1024  147 GLU B OE1 
3393  O  OE2 . GLU B  147 ? 0.6901 0.2786 0.4018 0.1853  -0.2921 -0.1307 147 GLU B OE2 
3394  N  N   . MET B  148 ? 0.1143 0.0838 0.1118 -0.0023 0.0296  -0.0115 148 MET B N   
3395  C  CA  . MET B  148 ? 0.1066 0.0771 0.1299 0.0007  0.0242  -0.0147 148 MET B CA  
3396  C  C   . MET B  148 ? 0.1040 0.0732 0.1405 0.0200  0.0156  -0.0098 148 MET B C   
3397  O  O   . MET B  148 ? 0.1394 0.0766 0.1800 0.0179  -0.0253 -0.0076 148 MET B O   
3398  C  CB  . MET B  148 ? 0.1181 0.1222 0.1365 -0.0013 0.0412  -0.0344 148 MET B CB  
3399  C  CG  . MET B  148 ? 0.1787 0.1222 0.1326 -0.0273 0.0524  -0.0074 148 MET B CG  
3400  S  SD  . MET B  148 ? 0.1899 0.1436 0.2008 -0.0071 0.0710  -0.0394 148 MET B SD  
3401  C  CE  . MET B  148 ? 0.2254 0.1536 0.1965 -0.0167 0.0751  -0.0441 148 MET B CE  
3402  N  N   . GLY B  149 ? 0.1121 0.0806 0.1410 0.0049  0.0164  -0.0221 149 GLY B N   
3403  C  CA  . GLY B  149 ? 0.1127 0.0804 0.1718 0.0034  -0.0116 -0.0218 149 GLY B CA  
3404  C  C   . GLY B  149 ? 0.1254 0.0678 0.1292 0.0146  0.0153  -0.0226 149 GLY B C   
3405  O  O   . GLY B  149 ? 0.1295 0.0754 0.1407 0.0100  0.0107  -0.0255 149 GLY B O   
3406  N  N   . SER B  150 ? 0.1200 0.0768 0.1581 0.0000  -0.0003 -0.0141 150 SER B N   
3407  C  CA  . SER B  150 ? 0.1217 0.0687 0.1567 0.0082  -0.0008 -0.0012 150 SER B CA  
3408  C  C   . SER B  150 ? 0.1432 0.0710 0.1475 0.0007  -0.0065 -0.0252 150 SER B C   
3409  O  O   . SER B  150 ? 0.1590 0.0825 0.1500 0.0065  -0.0026 -0.0288 150 SER B O   
3410  C  CB  . SER B  150 ? 0.1378 0.0578 0.1881 0.0000  0.0113  0.0035  150 SER B CB  
3411  O  OG  . SER B  150 ? 0.1305 0.0667 0.1923 0.0049  0.0041  0.0102  150 SER B OG  
3412  N  N   . PHE B  151 ? 0.1647 0.0614 0.1626 0.0104  -0.0271 -0.0194 151 PHE B N   
3413  C  CA  . PHE B  151 ? 0.1533 0.0813 0.1330 0.0057  -0.0137 -0.0192 151 PHE B CA  
3414  C  C   . PHE B  151 ? 0.1511 0.0676 0.1595 -0.0043 -0.0054 -0.0100 151 PHE B C   
3415  O  O   . PHE B  151 ? 0.1763 0.0657 0.2012 -0.0171 0.0076  -0.0163 151 PHE B O   
3416  C  CB  . PHE B  151 ? 0.1700 0.0784 0.1727 0.0089  -0.0366 -0.0282 151 PHE B CB  
3417  C  CG  . PHE B  151 ? 0.1886 0.0865 0.1405 0.0104  -0.0275 -0.0335 151 PHE B CG  
3418  C  CD1 . PHE B  151 ? 0.2177 0.0750 0.1689 0.0094  -0.0414 -0.0251 151 PHE B CD1 
3419  C  CD2 . PHE B  151 ? 0.1703 0.1484 0.1590 0.0140  -0.0200 -0.0096 151 PHE B CD2 
3420  C  CE1 . PHE B  151 ? 0.2360 0.0938 0.1727 0.0200  -0.0648 -0.0320 151 PHE B CE1 
3421  C  CE2 . PHE B  151 ? 0.2142 0.1272 0.1847 0.0204  -0.0434 -0.0362 151 PHE B CE2 
3422  C  CZ  . PHE B  151 ? 0.2201 0.1154 0.1754 0.0254  -0.0697 -0.0560 151 PHE B CZ  
3423  N  N   . ASN B  152 ? 0.1475 0.0671 0.1277 0.0034  -0.0028 -0.0083 152 ASN B N   
3424  C  CA  . ASN B  152 ? 0.1222 0.0712 0.1475 -0.0054 -0.0057 -0.0153 152 ASN B CA  
3425  C  C   . ASN B  152 ? 0.1359 0.0709 0.1416 -0.0030 -0.0020 -0.0215 152 ASN B C   
3426  O  O   . ASN B  152 ? 0.1242 0.0778 0.1395 -0.0005 0.0013  -0.0142 152 ASN B O   
3427  C  CB  . ASN B  152 ? 0.1298 0.0824 0.1283 -0.0048 -0.0020 -0.0107 152 ASN B CB  
3428  C  CG  . ASN B  152 ? 0.1344 0.0768 0.1340 0.0070  0.0012  0.0000  152 ASN B CG  
3429  O  OD1 . ASN B  152 ? 0.1378 0.1152 0.1322 0.0097  0.0015  -0.0010 152 ASN B OD1 
3430  N  ND2 . ASN B  152 ? 0.1328 0.0983 0.1127 -0.0087 0.0093  0.0026  152 ASN B ND2 
3431  N  N   . PRO B  153 ? 0.1283 0.0766 0.1703 -0.0100 -0.0236 -0.0005 153 PRO B N   
3432  C  CA  . PRO B  153 ? 0.1341 0.1141 0.2045 -0.0125 -0.0388 -0.0255 153 PRO B CA  
3433  C  C   . PRO B  153 ? 0.1091 0.1228 0.1524 -0.0098 -0.0248 -0.0017 153 PRO B C   
3434  O  O   . PRO B  153 ? 0.1888 0.1213 0.1387 0.0178  -0.0111 0.0024  153 PRO B O   
3435  C  CB  . PRO B  153 ? 0.1550 0.1387 0.2597 -0.0230 -0.0423 -0.0313 153 PRO B CB  
3436  C  CG  . PRO B  153 ? 0.1844 0.1238 0.4077 -0.0366 -0.0935 0.0390  153 PRO B CG  
3437  C  CD  . PRO B  153 ? 0.1553 0.0899 0.2587 -0.0230 -0.0359 -0.0115 153 PRO B CD  
3438  N  N   . SER B  154 ? 0.1229 0.1073 0.1583 -0.0066 -0.0065 -0.0013 154 SER B N   
3439  C  CA  . SER B  154 ? 0.1256 0.1283 0.1450 -0.0013 0.0089  0.0024  154 SER B CA  
3440  C  C   . SER B  154 ? 0.1173 0.0987 0.1358 0.0135  -0.0021 -0.0054 154 SER B C   
3441  O  O   . SER B  154 ? 0.1348 0.1017 0.1396 0.0142  0.0054  -0.0086 154 SER B O   
3442  C  CB  . SER B  154 ? 0.1599 0.1500 0.1502 -0.0395 0.0353  0.0175  154 SER B CB  
3443  O  OG  . SER B  154 ? 0.2293 0.2138 0.2240 -0.0944 0.0636  -0.0092 154 SER B OG  
3444  N  N   . TYR B  155 ? 0.1036 0.0868 0.1301 0.0052  0.0057  -0.0074 155 TYR B N   
3445  C  CA  . TYR B  155 ? 0.1100 0.0961 0.1127 -0.0104 0.0034  -0.0043 155 TYR B CA  
3446  C  C   . TYR B  155 ? 0.1197 0.0777 0.1145 0.0074  0.0055  -0.0149 155 TYR B C   
3447  O  O   . TYR B  155 ? 0.1446 0.0791 0.1128 -0.0008 0.0076  -0.0109 155 TYR B O   
3448  C  CB  . TYR B  155 ? 0.1125 0.0836 0.1249 -0.0017 0.0109  -0.0049 155 TYR B CB  
3449  C  CG  . TYR B  155 ? 0.0996 0.0741 0.1028 0.0130  0.0161  -0.0126 155 TYR B CG  
3450  C  CD1 . TYR B  155 ? 0.1129 0.0854 0.1213 0.0129  0.0207  0.0027  155 TYR B CD1 
3451  C  CD2 . TYR B  155 ? 0.1190 0.0742 0.1317 0.0148  0.0133  -0.0097 155 TYR B CD2 
3452  C  CE1 . TYR B  155 ? 0.1066 0.0877 0.1142 0.0052  0.0126  -0.0082 155 TYR B CE1 
3453  C  CE2 . TYR B  155 ? 0.1094 0.1163 0.1188 0.0057  0.0114  0.0023  155 TYR B CE2 
3454  C  CZ  . TYR B  155 ? 0.1102 0.0797 0.1138 0.0156  0.0059  -0.0127 155 TYR B CZ  
3455  O  OH  . TYR B  155 ? 0.1050 0.0952 0.1253 0.0015  0.0013  -0.0068 155 TYR B OH  
3456  N  N   . ASP B  156 ? 0.1269 0.0885 0.1097 0.0015  0.0019  -0.0102 156 ASP B N   
3457  C  CA  . ASP B  156 ? 0.1491 0.0926 0.1163 0.0054  0.0093  -0.0263 156 ASP B CA  
3458  C  C   . ASP B  156 ? 0.1347 0.1045 0.1436 -0.0307 0.0081  0.0120  156 ASP B C   
3459  O  O   . ASP B  156 ? 0.1757 0.1155 0.1253 -0.0104 -0.0063 0.0055  156 ASP B O   
3460  C  CB  . ASP B  156 ? 0.2314 0.1088 0.1364 -0.0037 0.0131  -0.0322 156 ASP B CB  
3461  C  CG  . ASP B  156 ? 0.2057 0.1091 0.1407 0.0170  -0.0313 0.0113  156 ASP B CG  
3462  O  OD1 . ASP B  156 ? 0.2034 0.1093 0.1186 0.0370  0.0093  0.0001  156 ASP B OD1 
3463  O  OD2 . ASP B  156 ? 0.3070 0.2014 0.1542 -0.0113 -0.0710 -0.0032 156 ASP B OD2 
3464  N  N   . LYS B  157 ? 0.1351 0.1014 0.1337 0.0006  -0.0071 -0.0155 157 LYS B N   
3465  C  CA  . LYS B  157 ? 0.1524 0.1021 0.1696 0.0182  0.0082  -0.0043 157 LYS B CA  
3466  C  C   . LYS B  157 ? 0.1513 0.0961 0.1319 0.0226  0.0001  -0.0024 157 LYS B C   
3467  O  O   . LYS B  157 ? 0.1843 0.1367 0.2066 0.0217  -0.0340 0.0252  157 LYS B O   
3468  C  CB  . LYS B  157 ? 0.1351 0.1212 0.1802 0.0364  0.0051  0.0109  157 LYS B CB  
3469  C  CG  . LYS B  157 ? 0.1617 0.1286 0.2524 0.0015  0.0331  0.0113  157 LYS B CG  
3470  C  CD  . LYS B  157 ? 0.1942 0.2109 0.2278 0.0027  0.0350  -0.0636 157 LYS B CD  
3471  C  CE  . LYS B  157 ? 0.1955 0.2536 0.2937 -0.0820 0.0636  -0.0529 157 LYS B CE  
3472  N  NZ  . LYS B  157 ? 0.2400 0.2644 0.2703 -0.0287 0.0308  -0.0318 157 LYS B NZ  
3473  N  N   . ILE B  158 ? 0.1525 0.0992 0.1249 -0.0015 -0.0044 0.0024  158 ILE B N   
3474  C  CA  . ILE B  158 ? 0.1847 0.1018 0.1225 -0.0221 0.0113  -0.0132 158 ILE B CA  
3475  C  C   . ILE B  158 ? 0.1590 0.0958 0.1315 -0.0237 -0.0010 0.0124  158 ILE B C   
3476  O  O   . ILE B  158 ? 0.1887 0.1048 0.1313 -0.0153 0.0026  0.0161  158 ILE B O   
3477  C  CB  . ILE B  158 ? 0.2149 0.0998 0.1364 -0.0206 0.0034  -0.0209 158 ILE B CB  
3478  C  CG1 . ILE B  158 ? 0.2721 0.1368 0.1389 -0.0241 0.0353  -0.0416 158 ILE B CG1 
3479  C  CG2 . ILE B  158 ? 0.2233 0.0988 0.1662 -0.0331 -0.0196 -0.0049 158 ILE B CG2 
3480  C  CD1 . ILE B  158 ? 0.2892 0.1940 0.1568 -0.0326 0.0166  -0.0120 158 ILE B CD1 
3481  N  N   . PHE B  159 ? 0.1932 0.0956 0.1321 -0.0034 0.0263  -0.0118 159 PHE B N   
3482  C  CA  . PHE B  159 ? 0.2023 0.1317 0.1412 -0.0340 0.0463  -0.0270 159 PHE B CA  
3483  C  C   . PHE B  159 ? 0.2168 0.1495 0.1500 -0.0326 0.0625  -0.0171 159 PHE B C   
3484  O  O   . PHE B  159 ? 0.2865 0.2237 0.1759 -0.0852 0.0833  0.0087  159 PHE B O   
3485  C  CB  . PHE B  159 ? 0.1737 0.1400 0.1668 -0.0104 0.0516  -0.0715 159 PHE B CB  
3486  C  CG  . PHE B  159 ? 0.1569 0.1170 0.1673 -0.0203 0.0586  -0.0454 159 PHE B CG  
3487  C  CD1 . PHE B  159 ? 0.1748 0.1461 0.1933 -0.0193 0.0094  -0.0720 159 PHE B CD1 
3488  C  CD2 . PHE B  159 ? 0.2185 0.1203 0.1836 0.0263  0.0747  -0.0286 159 PHE B CD2 
3489  C  CE1 . PHE B  159 ? 0.1698 0.1562 0.1856 -0.0254 0.0052  -0.0403 159 PHE B CE1 
3490  C  CE2 . PHE B  159 ? 0.1657 0.2012 0.1520 -0.0023 0.0665  -0.0093 159 PHE B CE2 
3491  C  CZ  . PHE B  159 ? 0.1525 0.1747 0.1847 -0.0089 0.0524  -0.0186 159 PHE B CZ  
3492  N  N   . SER B  160 ? 0.2833 0.1592 0.1111 -0.0657 0.0171  -0.0133 160 SER B N   
3493  C  CA  . SER B  160 ? 0.3499 0.2305 0.1254 -0.0920 -0.0070 0.0055  160 SER B CA  
3494  C  C   . SER B  160 ? 0.2953 0.2055 0.1233 -0.0763 0.0126  0.0252  160 SER B C   
3495  O  O   . SER B  160 ? 0.3600 0.2815 0.1271 -0.0648 -0.0311 0.0254  160 SER B O   
3496  C  CB  . SER B  160 ? 0.3688 0.2402 0.1281 -0.1027 -0.0375 0.0197  160 SER B CB  
3497  O  OG  . SER B  160 ? 0.3000 0.3107 0.1269 -0.1128 -0.0205 0.0097  160 SER B OG  
3498  N  N   . HIS B  161 ? 0.3048 0.1718 0.1278 -0.1023 -0.0119 0.0298  161 HIS B N   
3499  C  CA  . HIS B  161 ? 0.2430 0.1915 0.1687 -0.0676 -0.0370 0.0584  161 HIS B CA  
3500  C  C   . HIS B  161 ? 0.3343 0.2314 0.1971 -0.1432 -0.0392 0.0908  161 HIS B C   
3501  O  O   . HIS B  161 ? 0.3691 0.2050 0.1960 -0.1234 -0.0603 0.0916  161 HIS B O   
3502  C  CB  . HIS B  161 ? 0.3113 0.1874 0.1450 -0.0030 -0.0628 0.0254  161 HIS B CB  
3503  C  CG  . HIS B  161 ? 0.3646 0.1448 0.1745 -0.0425 -0.0848 -0.0041 161 HIS B CG  
3504  N  ND1 . HIS B  161 ? 0.2666 0.2377 0.1678 -0.0197 -0.0357 0.0302  161 HIS B ND1 
3505  C  CD2 . HIS B  161 ? 0.3161 0.1533 0.2266 -0.0006 -0.0103 -0.0060 161 HIS B CD2 
3506  C  CE1 . HIS B  161 ? 0.3098 0.1852 0.1969 -0.0184 -0.0485 -0.0105 161 HIS B CE1 
3507  N  NE2 . HIS B  161 ? 0.3212 0.1696 0.1996 -0.0178 -0.0122 -0.0066 161 HIS B NE2 
3508  N  N   . LEU B  162 ? 0.3535 0.2129 0.2926 -0.1453 -0.0738 0.0797  162 LEU B N   
3509  C  CA  . LEU B  162 ? 0.3610 0.4379 0.2287 -0.2027 -0.0284 0.1295  162 LEU B CA  
3510  C  C   . LEU B  162 ? 0.4569 0.4090 0.1721 -0.2777 -0.0987 0.1304  162 LEU B C   
3511  O  O   . LEU B  162 ? 0.5864 0.2727 0.2640 -0.2374 -0.0639 0.1005  162 LEU B O   
3512  C  CB  . LEU B  162 ? 0.4325 0.4402 0.2901 -0.2289 -0.1397 0.1634  162 LEU B CB  
3513  C  CG  . LEU B  162 ? 0.3115 0.4604 0.2599 -0.1384 -0.1005 0.1779  162 LEU B CG  
3514  C  CD1 . LEU B  162 ? 0.2206 0.8180 0.3892 -0.0864 -0.0483 0.3799  162 LEU B CD1 
3515  C  CD2 . LEU B  162 ? 0.2685 0.3932 0.3224 -0.1243 -0.0662 0.1280  162 LEU B CD2 
3516  N  N   . GLN B  163 ? 0.6445 0.2745 0.2061 -0.1611 -0.1208 0.0945  163 GLN B N   
3517  C  CA  . GLN B  163 ? 0.4544 0.3441 0.2456 -0.1389 -0.0666 0.1112  163 GLN B CA  
3518  C  C   . GLN B  163 ? 0.7691 0.1601 0.3479 -0.0625 -0.0601 -0.0513 163 GLN B C   
3519  O  O   . GLN B  163 ? 0.4104 0.6628 0.4963 -0.0957 -0.1323 0.3456  163 GLN B O   
3520  C  CB  . GLN B  163 ? 0.5598 0.3851 0.2547 -0.1138 -0.0737 0.1389  163 GLN B CB  
3521  C  CG  . GLN B  163 ? 0.4839 0.5310 0.6539 -0.0639 -0.1520 0.4336  163 GLN B CG  
3522  C  CD  . GLN B  163 ? 0.4400 0.4510 0.6614 0.1606  -0.0538 -0.3348 163 GLN B CD  
3523  O  OE1 . GLN B  163 ? 0.5504 0.4325 0.7444 0.0807  -0.0439 0.2991  163 GLN B OE1 
3524  N  NE2 . GLN B  163 ? 0.6176 0.2163 0.3876 -0.0311 0.0024  -0.0331 163 GLN B NE2 
3525  N  N   . HIS B  164 ? 0.6999 0.4129 0.2133 -0.2833 -0.0864 -0.1019 164 HIS B N   
3526  C  CA  . HIS B  164 ? 0.4081 0.5350 0.1055 -0.2601 -0.1271 0.0851  164 HIS B CA  
3527  C  C   . HIS B  164 ? 0.2658 0.3801 0.1586 -0.1528 -0.0658 0.1411  164 HIS B C   
3528  O  O   . HIS B  164 ? 0.2192 0.4517 0.2284 -0.0785 -0.0447 0.1852  164 HIS B O   
3529  C  CB  . HIS B  164 ? 0.4086 0.4251 0.3357 -0.2187 -0.1941 0.1456  164 HIS B CB  
3530  C  CG  . HIS B  164 ? 0.7023 0.4681 0.2509 -0.2495 -0.3287 0.1216  164 HIS B CG  
3531  N  ND1 . HIS B  164 ? 0.3477 0.2791 0.3883 -0.0441 -0.1324 0.0296  164 HIS B ND1 
3532  C  CD2 . HIS B  164 ? 0.4616 0.2089 0.3186 0.0557  -0.1439 -0.0136 164 HIS B CD2 
3533  C  CE1 . HIS B  164 ? 0.4504 0.4203 0.3864 -0.0715 -0.2572 -0.0909 164 HIS B CE1 
3534  N  NE2 . HIS B  164 ? 0.5139 0.3443 0.4320 0.0879  -0.0961 -0.1172 164 HIS B NE2 
3535  N  N   . VAL B  165 ? 0.2416 0.2344 0.1316 -0.0948 -0.0472 0.0683  165 VAL B N   
3536  C  CA  . VAL B  165 ? 0.1847 0.1671 0.1527 -0.0362 0.0076  0.0403  165 VAL B CA  
3537  C  C   . VAL B  165 ? 0.1728 0.1249 0.1238 -0.0392 0.0251  0.0538  165 VAL B C   
3538  O  O   . VAL B  165 ? 0.1631 0.2088 0.1251 -0.0502 0.0183  0.0537  165 VAL B O   
3539  C  CB  . VAL B  165 ? 0.2237 0.2485 0.1292 -0.0728 0.0164  0.0324  165 VAL B CB  
3540  C  CG1 . VAL B  165 ? 0.1832 0.2736 0.2267 -0.0931 0.0193  0.0217  165 VAL B CG1 
3541  C  CG2 . VAL B  165 ? 0.2298 0.2953 0.1473 -0.0573 -0.0137 0.1243  165 VAL B CG2 
3542  N  N   A LYS B  166 ? 0.2481 0.1125 0.1622 -0.0362 0.0776  0.0351  166 LYS B N   
3543  N  N   B LYS B  166 ? 0.1560 0.1407 0.1215 0.0035  0.0122  0.0392  166 LYS B N   
3544  C  CA  A LYS B  166 ? 0.2583 0.1714 0.0562 -0.0027 0.0310  0.0439  166 LYS B CA  
3545  C  CA  B LYS B  166 ? 0.1448 0.0728 0.1374 -0.0071 0.0168  0.0449  166 LYS B CA  
3546  C  C   A LYS B  166 ? 0.2431 0.1549 0.0579 0.0335  0.0373  0.0584  166 LYS B C   
3547  C  C   B LYS B  166 ? 0.1522 0.0991 0.1335 -0.0211 0.0366  0.0311  166 LYS B C   
3548  O  O   A LYS B  166 ? 0.2472 0.0803 0.1145 -0.0189 0.0162  0.0608  166 LYS B O   
3549  O  O   B LYS B  166 ? 0.1319 0.1260 0.1202 0.0021  0.0399  -0.0154 166 LYS B O   
3550  C  CB  A LYS B  166 ? 0.3228 0.1497 0.0795 0.0339  0.0445  -0.0003 166 LYS B CB  
3551  C  CB  B LYS B  166 ? 0.1495 0.1351 0.1387 -0.0086 -0.0113 -0.0049 166 LYS B CB  
3552  C  CG  A LYS B  166 ? 0.2682 0.1723 0.1446 0.0472  0.0043  -0.0048 166 LYS B CG  
3553  C  CG  B LYS B  166 ? 0.1676 0.1091 0.1375 -0.0035 0.0218  -0.0031 166 LYS B CG  
3554  C  CD  A LYS B  166 ? 0.3783 0.1335 0.1617 0.0511  0.0305  0.0031  166 LYS B CD  
3555  C  CD  B LYS B  166 ? 0.2036 0.1901 0.1380 -0.0120 0.0081  0.0040  166 LYS B CD  
3556  C  CE  A LYS B  166 ? 0.4002 0.3199 0.1349 0.1379  -0.0346 -0.1042 166 LYS B CE  
3557  C  CE  B LYS B  166 ? 0.3698 0.1506 0.4041 0.0295  -0.1055 0.0175  166 LYS B CE  
3558  N  NZ  A LYS B  166 ? 0.3231 0.3353 0.1587 -0.1618 0.0136  0.0601  166 LYS B NZ  
3559  N  NZ  B LYS B  166 ? 0.3540 0.1811 0.2998 0.1058  0.0199  -0.0229 166 LYS B NZ  
3560  N  N   . TYR B  167 ? 0.1809 0.1100 0.1152 0.0129  0.0640  0.0284  167 TYR B N   
3561  C  CA  . TYR B  167 ? 0.2059 0.0879 0.1080 -0.0216 0.0881  0.0181  167 TYR B CA  
3562  C  C   . TYR B  167 ? 0.1558 0.1319 0.0944 -0.0083 0.0397  0.0189  167 TYR B C   
3563  O  O   . TYR B  167 ? 0.1630 0.1436 0.1112 -0.0041 0.0687  0.0136  167 TYR B O   
3564  C  CB  . TYR B  167 ? 0.2226 0.1145 0.1085 0.0065  0.0737  0.0170  167 TYR B CB  
3565  C  CG  . TYR B  167 ? 0.2256 0.0856 0.1603 -0.0024 0.0957  0.0331  167 TYR B CG  
3566  C  CD1 . TYR B  167 ? 0.2874 0.1150 0.2370 0.0320  0.1828  0.0553  167 TYR B CD1 
3567  C  CD2 . TYR B  167 ? 0.2748 0.1385 0.1272 0.0034  0.0617  0.0010  167 TYR B CD2 
3568  C  CE1 . TYR B  167 ? 0.3274 0.1317 0.1064 0.0000  0.0498  0.0130  167 TYR B CE1 
3569  C  CE2 . TYR B  167 ? 0.1967 0.1888 0.1569 -0.0028 0.0386  -0.0060 167 TYR B CE2 
3570  C  CZ  . TYR B  167 ? 0.2181 0.1520 0.1538 0.0222  0.1045  0.0080  167 TYR B CZ  
3571  O  OH  . TYR B  167 ? 0.2549 0.2476 0.1875 -0.0010 0.0913  -0.0785 167 TYR B OH  
3572  N  N   . LYS B  168 ? 0.1797 0.1504 0.1021 -0.0178 0.0582  -0.0065 168 LYS B N   
3573  C  CA  . LYS B  168 ? 0.1683 0.2149 0.1619 -0.0493 0.0698  -0.0538 168 LYS B CA  
3574  C  C   . LYS B  168 ? 0.1984 0.2170 0.1500 -0.0329 0.0821  -0.0652 168 LYS B C   
3575  O  O   . LYS B  168 ? 0.1984 0.1838 0.2060 -0.0007 0.0719  -0.0443 168 LYS B O   
3576  C  CB  . LYS B  168 ? 0.1920 0.2113 0.1488 -0.0560 0.0465  -0.0604 168 LYS B CB  
3577  C  CG  . LYS B  168 ? 0.2140 0.3050 0.2310 -0.0872 0.1039  -0.1640 168 LYS B CG  
3578  C  CD  . LYS B  168 ? 0.2048 0.4264 0.3257 -0.0964 0.0680  -0.1948 168 LYS B CD  
3579  C  CE  . LYS B  168 ? 0.2885 0.5113 0.6245 -0.0879 0.0456  -0.4032 168 LYS B CE  
3580  N  NZ  . LYS B  168 ? 0.2824 0.7536 0.6618 -0.1375 0.0830  -0.4909 168 LYS B NZ  
3581  N  N   . GLY B  169 ? 0.1520 0.3082 0.2066 -0.0716 0.0900  -0.1427 169 GLY B N   
3582  C  CA  . GLY B  169 ? 0.1687 0.2987 0.3637 -0.0715 0.0923  -0.1923 169 GLY B CA  
3583  C  C   . GLY B  169 ? 0.1425 0.2761 0.3440 -0.0344 0.0672  -0.1711 169 GLY B C   
3584  O  O   . GLY B  169 ? 0.1872 0.3395 0.5213 0.0015  0.0588  -0.2347 169 GLY B O   
3585  N  N   . GLN B  170 ? 0.1735 0.1732 0.1820 -0.0342 0.0604  -0.0303 170 GLN B N   
3586  C  CA  . GLN B  170 ? 0.1845 0.1563 0.1545 -0.0215 0.0185  0.0164  170 GLN B CA  
3587  C  C   . GLN B  170 ? 0.1518 0.2075 0.1324 -0.0055 0.0333  0.0259  170 GLN B C   
3588  O  O   . GLN B  170 ? 0.1635 0.2601 0.1322 -0.0436 0.0200  0.0313  170 GLN B O   
3589  C  CB  . GLN B  170 ? 0.1872 0.1486 0.1242 -0.0126 0.0311  0.0152  170 GLN B CB  
3590  C  CG  . GLN B  170 ? 0.2263 0.1867 0.1506 0.0297  0.0544  0.0577  170 GLN B CG  
3591  C  CD  . GLN B  170 ? 0.3228 0.2345 0.1288 0.0553  0.0610  0.0606  170 GLN B CD  
3592  O  OE1 . GLN B  170 ? 0.2937 0.2199 0.1193 0.0241  0.0329  0.0366  170 GLN B OE1 
3593  N  NE2 . GLN B  170 ? 0.3862 0.3359 0.1843 0.1557  0.0520  0.1130  170 GLN B NE2 
3594  N  N   . GLU B  171 ? 0.1490 0.1951 0.1615 0.0043  0.0254  0.0693  171 GLU B N   
3595  C  CA  . GLU B  171 ? 0.1705 0.2071 0.1308 -0.0432 0.0260  0.0518  171 GLU B CA  
3596  C  C   . GLU B  171 ? 0.1662 0.2689 0.1330 -0.0604 -0.0197 0.0778  171 GLU B C   
3597  O  O   . GLU B  171 ? 0.2052 0.3273 0.1506 -0.0715 -0.0410 0.1169  171 GLU B O   
3598  C  CB  . GLU B  171 ? 0.1939 0.2466 0.2395 -0.0019 0.0798  0.0288  171 GLU B CB  
3599  C  CG  . GLU B  171 ? 0.3327 0.1965 0.3562 -0.0526 0.1097  -0.0416 171 GLU B CG  
3600  C  CD  . GLU B  171 ? 0.5037 0.2293 0.6255 -0.0439 0.2230  -0.0811 171 GLU B CD  
3601  O  OE1 . GLU B  171 ? 0.6158 0.5328 0.9694 0.2775  0.2118  0.0518  171 GLU B OE1 
3602  O  OE2 . GLU B  171 ? 0.8941 0.2518 0.5465 0.0886  0.0991  -0.0456 171 GLU B OE2 
3603  N  N   . ALA B  172 ? 0.1683 0.2827 0.1265 -0.0828 -0.0092 0.0846  172 ALA B N   
3604  C  CA  . ALA B  172 ? 0.1348 0.3127 0.1272 -0.0522 -0.0116 0.0527  172 ALA B CA  
3605  C  C   . ALA B  172 ? 0.1723 0.2222 0.0874 -0.0443 -0.0116 0.0626  172 ALA B C   
3606  O  O   . ALA B  172 ? 0.1671 0.3461 0.1015 -0.0694 -0.0028 0.0485  172 ALA B O   
3607  C  CB  . ALA B  172 ? 0.1746 0.3312 0.1495 -0.0685 0.0137  -0.0041 172 ALA B CB  
3608  N  N   . PHE B  173 ? 0.1702 0.2436 0.1208 -0.0421 -0.0214 0.0417  173 PHE B N   
3609  C  CA  . PHE B  173 ? 0.1703 0.1872 0.1421 -0.0304 0.0003  0.0287  173 PHE B CA  
3610  C  C   . PHE B  173 ? 0.2050 0.1736 0.1193 -0.0348 -0.0183 0.0076  173 PHE B C   
3611  O  O   . PHE B  173 ? 0.3343 0.2567 0.1088 -0.0697 -0.0136 0.0065  173 PHE B O   
3612  C  CB  . PHE B  173 ? 0.1777 0.2671 0.2517 -0.0535 -0.0441 0.0516  173 PHE B CB  
3613  C  CG  . PHE B  173 ? 0.1922 0.2547 0.2416 -0.0715 -0.0549 0.0983  173 PHE B CG  
3614  C  CD1 . PHE B  173 ? 0.1832 0.2348 0.3036 -0.0071 -0.0496 0.0604  173 PHE B CD1 
3615  C  CD2 . PHE B  173 ? 0.3307 0.3186 0.3120 -0.0756 -0.1146 0.1386  173 PHE B CD2 
3616  C  CE1 . PHE B  173 ? 0.2506 0.2405 0.4709 0.0815  0.0031  0.0825  173 PHE B CE1 
3617  C  CE2 . PHE B  173 ? 0.4734 0.3517 0.5314 0.0339  0.0164  0.0844  173 PHE B CE2 
3618  C  CZ  . PHE B  173 ? 0.3452 0.2461 0.5799 0.0767  -0.0942 0.1342  173 PHE B CZ  
3619  N  N   . VAL B  174 ? 0.1565 0.1820 0.1213 -0.0362 0.0005  0.0254  174 VAL B N   
3620  C  CA  . VAL B  174 ? 0.1429 0.1599 0.1310 -0.0015 0.0210  -0.0109 174 VAL B CA  
3621  C  C   . VAL B  174 ? 0.1518 0.1551 0.1285 -0.0046 0.0131  0.0133  174 VAL B C   
3622  O  O   . VAL B  174 ? 0.1314 0.1771 0.1290 -0.0194 0.0140  0.0060  174 VAL B O   
3623  C  CB  . VAL B  174 ? 0.1242 0.2107 0.1310 -0.0170 0.0183  0.0236  174 VAL B CB  
3624  C  CG1 . VAL B  174 ? 0.1755 0.1585 0.1800 -0.0082 0.0146  -0.0024 174 VAL B CG1 
3625  C  CG2 . VAL B  174 ? 0.1301 0.2560 0.1626 -0.0333 0.0313  -0.0091 174 VAL B CG2 
3626  N  N   . PRO B  175 ? 0.1132 0.1475 0.1414 -0.0035 -0.0017 0.0241  175 PRO B N   
3627  C  CA  . PRO B  175 ? 0.1048 0.1668 0.1532 -0.0307 -0.0184 0.0546  175 PRO B CA  
3628  C  C   . PRO B  175 ? 0.1059 0.1470 0.1590 -0.0105 0.0094  0.0527  175 PRO B C   
3629  O  O   . PRO B  175 ? 0.1154 0.1818 0.1527 0.0024  0.0068  0.0379  175 PRO B O   
3630  C  CB  . PRO B  175 ? 0.1513 0.1498 0.2001 -0.0233 -0.0377 0.0183  175 PRO B CB  
3631  C  CG  . PRO B  175 ? 0.1580 0.2460 0.2018 -0.0627 -0.0362 0.0560  175 PRO B CG  
3632  C  CD  . PRO B  175 ? 0.1347 0.2016 0.1350 -0.0006 -0.0040 -0.0027 175 PRO B CD  
3633  N  N   . GLY B  176 ? 0.1120 0.1626 0.1574 -0.0155 0.0076  0.0599  176 GLY B N   
3634  C  CA  . GLY B  176 ? 0.1468 0.1605 0.1439 -0.0082 0.0230  0.0408  176 GLY B CA  
3635  C  C   . GLY B  176 ? 0.1176 0.1615 0.1520 -0.0027 0.0020  0.0310  176 GLY B C   
3636  O  O   . GLY B  176 ? 0.1185 0.1983 0.1523 -0.0206 -0.0041 0.0274  176 GLY B O   
3637  N  N   . PHE B  177 ? 0.1048 0.1416 0.1596 -0.0192 -0.0080 0.0388  177 PHE B N   
3638  C  CA  . PHE B  177 ? 0.1457 0.1369 0.1525 -0.0222 -0.0187 0.0335  177 PHE B CA  
3639  C  C   . PHE B  177 ? 0.1125 0.1462 0.1447 -0.0227 -0.0135 0.0092  177 PHE B C   
3640  O  O   . PHE B  177 ? 0.1238 0.1416 0.1572 -0.0085 -0.0283 0.0183  177 PHE B O   
3641  C  CB  . PHE B  177 ? 0.1513 0.1502 0.1509 -0.0162 -0.0142 0.0024  177 PHE B CB  
3642  C  CG  . PHE B  177 ? 0.1179 0.1726 0.1344 0.0181  -0.0048 -0.0085 177 PHE B CG  
3643  C  CD1 . PHE B  177 ? 0.1224 0.1726 0.1553 0.0043  0.0205  0.0049  177 PHE B CD1 
3644  C  CD2 . PHE B  177 ? 0.1475 0.1996 0.1626 0.0377  -0.0203 -0.0291 177 PHE B CD2 
3645  C  CE1 . PHE B  177 ? 0.1190 0.1835 0.1585 0.0261  0.0218  0.0038  177 PHE B CE1 
3646  C  CE2 . PHE B  177 ? 0.1308 0.2312 0.1240 0.0348  0.0099  -0.0003 177 PHE B CE2 
3647  C  CZ  . PHE B  177 ? 0.1115 0.2624 0.1631 0.0384  0.0242  0.0159  177 PHE B CZ  
3648  N  N   . ASN B  178 ? 0.1641 0.1425 0.1777 -0.0228 -0.0296 0.0571  178 ASN B N   
3649  C  CA  . ASN B  178 ? 0.1472 0.1405 0.1750 -0.0434 -0.0040 0.0416  178 ASN B CA  
3650  C  C   . ASN B  178 ? 0.1269 0.0969 0.1626 -0.0195 0.0003  0.0306  178 ASN B C   
3651  O  O   . ASN B  178 ? 0.1459 0.1109 0.1614 -0.0207 -0.0238 0.0155  178 ASN B O   
3652  C  CB  . ASN B  178 ? 0.1651 0.1703 0.2053 -0.0728 -0.0417 0.0636  178 ASN B CB  
3653  C  CG  . ASN B  178 ? 0.1348 0.1858 0.1932 -0.0395 0.0287  0.0555  178 ASN B CG  
3654  O  OD1 . ASN B  178 ? 0.1396 0.1689 0.1917 -0.0240 0.0043  0.0595  178 ASN B OD1 
3655  N  ND2 . ASN B  178 ? 0.2005 0.1730 0.2497 -0.0511 0.0390  0.0417  178 ASN B ND2 
3656  N  N   . ILE B  179 ? 0.0926 0.1140 0.1707 -0.0171 -0.0063 0.0307  179 ILE B N   
3657  C  CA  . ILE B  179 ? 0.0922 0.1140 0.1410 -0.0137 0.0015  0.0148  179 ILE B CA  
3658  C  C   . ILE B  179 ? 0.1193 0.0970 0.1274 -0.0049 0.0113  0.0082  179 ILE B C   
3659  O  O   . ILE B  179 ? 0.1039 0.1164 0.1323 0.0074  0.0165  0.0105  179 ILE B O   
3660  C  CB  . ILE B  179 ? 0.0992 0.1164 0.1350 -0.0020 0.0225  0.0164  179 ILE B CB  
3661  C  CG1 . ILE B  179 ? 0.1100 0.1475 0.1423 -0.0003 0.0285  0.0331  179 ILE B CG1 
3662  C  CG2 . ILE B  179 ? 0.0827 0.1313 0.1549 -0.0076 0.0218  -0.0021 179 ILE B CG2 
3663  C  CD1 . ILE B  179 ? 0.1518 0.1387 0.1231 0.0177  0.0241  0.0136  179 ILE B CD1 
3664  N  N   . GLU B  180 ? 0.0987 0.1247 0.1340 -0.0028 0.0206  0.0311  180 GLU B N   
3665  C  CA  . GLU B  180 ? 0.1313 0.1247 0.1448 0.0116  0.0258  0.0383  180 GLU B CA  
3666  C  C   . GLU B  180 ? 0.1295 0.1265 0.1405 0.0070  0.0230  0.0339  180 GLU B C   
3667  O  O   . GLU B  180 ? 0.1186 0.1278 0.1743 -0.0006 0.0288  0.0666  180 GLU B O   
3668  C  CB  . GLU B  180 ? 0.1459 0.2025 0.1547 0.0077  0.0560  0.0443  180 GLU B CB  
3669  C  CG  . GLU B  180 ? 0.1993 0.2405 0.2754 0.0326  0.0688  0.1412  180 GLU B CG  
3670  C  CD  . GLU B  180 ? 0.2552 0.2472 0.2479 -0.0003 0.0636  0.0712  180 GLU B CD  
3671  O  OE1 . GLU B  180 ? 0.2536 0.4205 0.1978 -0.0019 0.0868  0.1304  180 GLU B OE1 
3672  O  OE2 . GLU B  180 ? 0.2791 0.3679 0.2800 -0.0573 0.0943  0.1058  180 GLU B OE2 
3673  N  N   . GLU B  181 ? 0.1130 0.1145 0.1529 -0.0184 0.0234  0.0113  181 GLU B N   
3674  C  CA  . GLU B  181 ? 0.1254 0.1244 0.1518 -0.0151 0.0406  0.0160  181 GLU B CA  
3675  C  C   . GLU B  181 ? 0.1111 0.1164 0.1341 -0.0070 0.0142  0.0104  181 GLU B C   
3676  O  O   . GLU B  181 ? 0.1290 0.1044 0.2093 0.0041  0.0223  -0.0070 181 GLU B O   
3677  C  CB  . GLU B  181 ? 0.1285 0.1856 0.1917 -0.0296 -0.0035 -0.0222 181 GLU B CB  
3678  C  CG  . GLU B  181 ? 0.1448 0.2236 0.2874 -0.0302 0.0031  -0.0769 181 GLU B CG  
3679  C  CD  . GLU B  181 ? 0.1536 0.2964 0.2685 -0.0680 0.0171  -0.0315 181 GLU B CD  
3680  O  OE1 . GLU B  181 ? 0.1827 0.4332 0.2549 -0.0524 0.0162  -0.0060 181 GLU B OE1 
3681  O  OE2 . GLU B  181 ? 0.1789 0.3068 0.2536 -0.0689 -0.0003 -0.0143 181 GLU B OE2 
3682  N  N   . LEU B  182 ? 0.0960 0.0921 0.1279 -0.0021 0.0159  0.0142  182 LEU B N   
3683  C  CA  . LEU B  182 ? 0.0985 0.0957 0.1295 -0.0038 0.0068  0.0236  182 LEU B CA  
3684  C  C   . LEU B  182 ? 0.1073 0.1001 0.1073 -0.0049 0.0087  0.0136  182 LEU B C   
3685  O  O   . LEU B  182 ? 0.1008 0.1136 0.1280 0.0013  0.0172  0.0155  182 LEU B O   
3686  C  CB  . LEU B  182 ? 0.1050 0.1052 0.1100 0.0003  0.0131  0.0201  182 LEU B CB  
3687  C  CG  . LEU B  182 ? 0.1036 0.0921 0.1161 -0.0012 0.0109  0.0105  182 LEU B CG  
3688  C  CD1 . LEU B  182 ? 0.1290 0.0992 0.1208 0.0007  0.0071  0.0077  182 LEU B CD1 
3689  C  CD2 . LEU B  182 ? 0.1143 0.1193 0.1103 0.0088  0.0186  0.0062  182 LEU B CD2 
3690  N  N   . LEU B  183 ? 0.1033 0.1398 0.1237 0.0024  0.0162  0.0326  183 LEU B N   
3691  C  CA  . LEU B  183 ? 0.1265 0.1129 0.1082 -0.0082 0.0102  0.0250  183 LEU B CA  
3692  C  C   . LEU B  183 ? 0.0991 0.1249 0.1259 -0.0181 0.0181  0.0258  183 LEU B C   
3693  O  O   . LEU B  183 ? 0.1244 0.1414 0.1606 -0.0133 -0.0003 0.0215  183 LEU B O   
3694  C  CB  . LEU B  183 ? 0.1294 0.1438 0.1181 0.0135  0.0274  0.0219  183 LEU B CB  
3695  C  CG  . LEU B  183 ? 0.1590 0.1445 0.1307 0.0085  0.0282  0.0297  183 LEU B CG  
3696  C  CD1 . LEU B  183 ? 0.2420 0.1802 0.1597 0.0653  0.0866  0.0546  183 LEU B CD1 
3697  C  CD2 . LEU B  183 ? 0.1550 0.1393 0.2109 0.0068  -0.0063 -0.0032 183 LEU B CD2 
3698  N  N   . PRO B  184 ? 0.1006 0.1073 0.1274 -0.0044 0.0255  0.0351  184 PRO B N   
3699  C  CA  . PRO B  184 ? 0.1217 0.1080 0.1647 -0.0241 0.0219  0.0126  184 PRO B CA  
3700  C  C   . PRO B  184 ? 0.2084 0.1066 0.1630 -0.0500 0.0340  0.0049  184 PRO B C   
3701  O  O   . PRO B  184 ? 0.2160 0.1359 0.2090 -0.0456 0.0820  0.0048  184 PRO B O   
3702  C  CB  . PRO B  184 ? 0.1623 0.1626 0.1668 0.0288  -0.0287 -0.0071 184 PRO B CB  
3703  C  CG  . PRO B  184 ? 0.1623 0.1425 0.1445 0.0373  -0.0153 -0.0149 184 PRO B CG  
3704  C  CD  . PRO B  184 ? 0.1211 0.1235 0.1058 -0.0161 0.0052  0.0206  184 PRO B CD  
3705  N  N   A GLU B  185 ? 0.2185 0.1152 0.1746 -0.0298 0.0203  0.0052  185 GLU B N   
3706  N  N   B GLU B  185 ? 0.2199 0.1161 0.1764 -0.0286 0.0198  0.0043  185 GLU B N   
3707  C  CA  A GLU B  185 ? 0.2779 0.0891 0.1905 -0.0443 0.0452  -0.0063 185 GLU B CA  
3708  C  CA  B GLU B  185 ? 0.2800 0.0940 0.1932 -0.0465 0.0364  -0.0030 185 GLU B CA  
3709  C  C   A GLU B  185 ? 0.1885 0.1149 0.1998 -0.0432 0.0000  0.0253  185 GLU B C   
3710  C  C   B GLU B  185 ? 0.1941 0.1195 0.2002 -0.0388 0.0024  0.0277  185 GLU B C   
3711  O  O   A GLU B  185 ? 0.1962 0.1644 0.1938 -0.0626 -0.0162 0.0864  185 GLU B O   
3712  O  O   B GLU B  185 ? 0.1982 0.1734 0.1967 -0.0529 -0.0093 0.0785  185 GLU B O   
3713  C  CB  A GLU B  185 ? 0.3513 0.1517 0.1626 0.0524  0.0148  0.0046  185 GLU B CB  
3714  C  CB  B GLU B  185 ? 0.3447 0.1526 0.1818 0.0406  0.0538  0.0000  185 GLU B CB  
3715  C  CG  A GLU B  185 ? 0.5636 0.1888 0.2017 -0.0206 0.0746  -0.0533 185 GLU B CG  
3716  C  CG  B GLU B  185 ? 0.5349 0.2116 0.1750 -0.1155 0.0859  0.0253  185 GLU B CG  
3717  C  CD  A GLU B  185 ? 0.5077 0.1330 0.5274 -0.1250 0.1137  0.1240  185 GLU B CD  
3718  C  CD  B GLU B  185 ? 0.5372 0.3395 0.5515 -0.1761 0.1004  -0.0353 185 GLU B CD  
3719  O  OE1 A GLU B  185 ? 0.7979 0.2439 0.4878 0.1643  0.1439  0.1228  185 GLU B OE1 
3720  O  OE1 B GLU B  185 ? 0.7785 0.3770 0.3388 -0.1727 0.2644  -0.0230 185 GLU B OE1 
3721  O  OE2 A GLU B  185 ? 1.7625 0.7132 4.3470 0.5935  -2.0099 -1.4299 185 GLU B OE2 
3722  O  OE2 B GLU B  185 ? 0.1657 0.5364 1.8837 0.0675  0.0810  0.3248  185 GLU B OE2 
3723  N  N   . ARG B  186 ? 0.1835 0.1346 0.1804 -0.0487 0.0189  0.0328  186 ARG B N   
3724  C  CA  . ARG B  186 ? 0.2381 0.1233 0.1664 -0.0228 0.0024  0.0388  186 ARG B CA  
3725  C  C   . ARG B  186 ? 0.1692 0.1473 0.1924 -0.0175 0.0248  0.0333  186 ARG B C   
3726  O  O   . ARG B  186 ? 0.1651 0.1786 0.1762 -0.0109 0.0414  0.0362  186 ARG B O   
3727  C  CB  . ARG B  186 ? 0.2386 0.1428 0.2323 -0.0155 0.0038  0.0584  186 ARG B CB  
3728  C  CG  . ARG B  186 ? 0.5069 0.1238 0.3127 -0.0562 -0.0737 0.1001  186 ARG B CG  
3729  C  CD  . ARG B  186 ? 0.3790 0.1923 0.3019 -0.0657 0.0062  0.0309  186 ARG B CD  
3730  N  NE  . ARG B  186 ? 0.3607 0.3596 0.3700 -0.0326 -0.0118 0.2006  186 ARG B NE  
3731  C  CZ  . ARG B  186 ? 0.3553 0.2434 0.5618 -0.0141 0.1101  0.1667  186 ARG B CZ  
3732  N  NH1 . ARG B  186 ? 0.9521 0.1644 0.3693 -0.1474 -0.0966 0.0023  186 ARG B NH1 
3733  N  NH2 . ARG B  186 ? 0.5004 0.2007 0.7741 -0.0384 0.3528  -0.0507 186 ARG B NH2 
3734  N  N   . THR B  187 ? 0.1315 0.1359 0.1680 -0.0192 0.0324  0.0581  187 THR B N   
3735  C  CA  . THR B  187 ? 0.1112 0.1353 0.1441 -0.0073 0.0212  0.0579  187 THR B CA  
3736  C  C   . THR B  187 ? 0.1349 0.1324 0.1450 0.0023  0.0292  0.0502  187 THR B C   
3737  O  O   . THR B  187 ? 0.1531 0.1446 0.1288 -0.0148 0.0405  0.0461  187 THR B O   
3738  C  CB  . THR B  187 ? 0.1344 0.1581 0.1252 -0.0103 0.0305  0.0500  187 THR B CB  
3739  O  OG1 . THR B  187 ? 0.1304 0.2235 0.1992 -0.0068 0.0100  0.0680  187 THR B OG1 
3740  C  CG2 . THR B  187 ? 0.2023 0.2106 0.1407 0.0228  0.0272  0.0384  187 THR B CG2 
3741  N  N   . ALA B  188 ? 0.1430 0.2023 0.1389 -0.0529 0.0219  0.0723  188 ALA B N   
3742  C  CA  . ALA B  188 ? 0.1154 0.2327 0.1313 -0.0386 0.0273  0.0820  188 ALA B CA  
3743  C  C   . ALA B  188 ? 0.1118 0.1535 0.1272 -0.0285 0.0277  0.0527  188 ALA B C   
3744  O  O   . ALA B  188 ? 0.1127 0.1680 0.1448 -0.0087 0.0317  0.0428  188 ALA B O   
3745  C  CB  . ALA B  188 ? 0.1738 0.2906 0.1475 -0.0952 0.0107  0.0939  188 ALA B CB  
3746  N  N   A GLU B  189 ? 0.1089 0.1483 0.1517 -0.0410 0.0406  0.0782  189 GLU B N   
3747  N  N   B GLU B  189 ? 0.1385 0.1409 0.1272 -0.0026 0.0201  0.0269  189 GLU B N   
3748  C  CA  A GLU B  189 ? 0.1244 0.1308 0.1068 -0.0208 0.0057  0.0586  189 GLU B CA  
3749  C  CA  B GLU B  189 ? 0.1062 0.1172 0.1404 -0.0196 0.0584  0.0148  189 GLU B CA  
3750  C  C   A GLU B  189 ? 0.0944 0.1155 0.0949 0.0010  0.0252  0.0436  189 GLU B C   
3751  C  C   B GLU B  189 ? 0.0931 0.1097 0.1263 -0.0017 0.0428  0.0258  189 GLU B C   
3752  O  O   A GLU B  189 ? 0.1012 0.1159 0.0857 0.0038  0.0505  0.0346  189 GLU B O   
3753  O  O   B GLU B  189 ? 0.1185 0.0913 0.1258 -0.0006 0.0175  0.0281  189 GLU B O   
3754  C  CB  A GLU B  189 ? 0.0957 0.1335 0.1547 -0.0136 0.0093  0.0584  189 GLU B CB  
3755  C  CB  B GLU B  189 ? 0.2415 0.0696 0.2055 -0.0218 0.0434  0.0250  189 GLU B CB  
3756  C  CG  A GLU B  189 ? 0.2224 0.1107 0.1324 -0.0326 0.0034  0.0421  189 GLU B CG  
3757  C  CG  B GLU B  189 ? 0.2436 0.1111 0.2658 -0.0458 0.0529  0.0452  189 GLU B CG  
3758  C  CD  A GLU B  189 ? 0.3267 0.0912 0.2702 -0.0306 0.0026  0.0406  189 GLU B CD  
3759  C  CD  B GLU B  189 ? 0.2301 0.1553 0.2025 0.0131  -0.0099 0.0848  189 GLU B CD  
3760  O  OE1 A GLU B  189 ? 0.3495 0.1127 0.2337 0.0281  -0.0121 0.0581  189 GLU B OE1 
3761  O  OE1 B GLU B  189 ? 0.2456 0.1641 0.2271 0.0254  0.0980  0.0313  189 GLU B OE1 
3762  O  OE2 A GLU B  189 ? 0.3118 0.0885 0.4792 -0.0142 0.1005  0.0619  189 GLU B OE2 
3763  O  OE2 B GLU B  189 ? 0.2520 0.2930 0.2389 -0.0099 -0.0355 0.1554  189 GLU B OE2 
3764  N  N   . TYR B  190 ? 0.0940 0.1229 0.1028 -0.0115 0.0173  0.0370  190 TYR B N   
3765  C  CA  . TYR B  190 ? 0.1045 0.0998 0.1023 -0.0023 0.0171  0.0370  190 TYR B CA  
3766  C  C   . TYR B  190 ? 0.1014 0.1120 0.0872 0.0048  0.0223  0.0258  190 TYR B C   
3767  O  O   . TYR B  190 ? 0.1190 0.1143 0.0908 0.0040  0.0259  0.0372  190 TYR B O   
3768  C  CB  . TYR B  190 ? 0.0985 0.1238 0.0978 0.0142  0.0309  0.0425  190 TYR B CB  
3769  C  CG  . TYR B  190 ? 0.0962 0.1199 0.0956 0.0164  0.0255  0.0493  190 TYR B CG  
3770  C  CD1 . TYR B  190 ? 0.1150 0.1328 0.0727 0.0082  0.0233  0.0388  190 TYR B CD1 
3771  C  CD2 . TYR B  190 ? 0.1017 0.1285 0.1254 0.0163  0.0307  0.0337  190 TYR B CD2 
3772  C  CE1 . TYR B  190 ? 0.1036 0.1565 0.0773 0.0110  0.0295  0.0430  190 TYR B CE1 
3773  C  CE2 . TYR B  190 ? 0.1220 0.1509 0.1008 -0.0006 0.0428  0.0379  190 TYR B CE2 
3774  C  CZ  . TYR B  190 ? 0.1163 0.1409 0.0988 0.0240  0.0370  0.0529  190 TYR B CZ  
3775  O  OH  . TYR B  190 ? 0.1459 0.1668 0.1116 0.0250  0.0636  0.0428  190 TYR B OH  
3776  N  N   . TYR B  191 ? 0.0899 0.0976 0.0917 0.0005  0.0287  0.0238  191 TYR B N   
3777  C  CA  . TYR B  191 ? 0.1039 0.0976 0.0839 -0.0003 0.0340  0.0259  191 TYR B CA  
3778  C  C   . TYR B  191 ? 0.0949 0.1080 0.0798 0.0068  0.0122  0.0353  191 TYR B C   
3779  O  O   . TYR B  191 ? 0.1411 0.1215 0.0829 0.0272  0.0094  0.0295  191 TYR B O   
3780  C  CB  . TYR B  191 ? 0.1057 0.1073 0.0890 0.0080  0.0303  0.0194  191 TYR B CB  
3781  C  CG  . TYR B  191 ? 0.1079 0.1062 0.0956 -0.0003 0.0329  0.0408  191 TYR B CG  
3782  C  CD1 . TYR B  191 ? 0.1001 0.1172 0.1238 0.0086  0.0412  0.0482  191 TYR B CD1 
3783  C  CD2 . TYR B  191 ? 0.0940 0.1156 0.1005 0.0017  0.0399  0.0233  191 TYR B CD2 
3784  C  CE1 . TYR B  191 ? 0.1141 0.1172 0.1401 0.0149  0.0414  0.0505  191 TYR B CE1 
3785  C  CE2 . TYR B  191 ? 0.1204 0.1032 0.1461 0.0057  0.0601  0.0359  191 TYR B CE2 
3786  C  CZ  . TYR B  191 ? 0.1158 0.1141 0.1393 0.0043  0.0557  0.0313  191 TYR B CZ  
3787  O  OH  . TYR B  191 ? 0.1470 0.1416 0.2001 0.0184  0.0505  -0.0062 191 TYR B OH  
3788  N  N   . ARG B  192 ? 0.1049 0.1041 0.0897 0.0028  0.0252  0.0166  192 ARG B N   
3789  C  CA  . ARG B  192 ? 0.1308 0.1123 0.0639 0.0038  0.0189  0.0197  192 ARG B CA  
3790  C  C   . ARG B  192 ? 0.1155 0.1128 0.0888 0.0197  0.0122  0.0118  192 ARG B C   
3791  O  O   . ARG B  192 ? 0.1262 0.1319 0.0951 0.0092  0.0068  0.0253  192 ARG B O   
3792  C  CB  . ARG B  192 ? 0.1277 0.1256 0.1105 0.0228  0.0406  0.0237  192 ARG B CB  
3793  C  CG  . ARG B  192 ? 0.1398 0.1509 0.1163 0.0337  0.0201  0.0183  192 ARG B CG  
3794  C  CD  . ARG B  192 ? 0.1728 0.1727 0.1097 0.0344  0.0373  0.0254  192 ARG B CD  
3795  N  NE  . ARG B  192 ? 0.1465 0.1842 0.1040 0.0428  0.0353  0.0333  192 ARG B NE  
3796  C  CZ  . ARG B  192 ? 0.1268 0.1696 0.0989 0.0373  0.0417  0.0373  192 ARG B CZ  
3797  N  NH1 . ARG B  192 ? 0.1574 0.1795 0.1150 0.0296  0.0535  0.0421  192 ARG B NH1 
3798  N  NH2 . ARG B  192 ? 0.1506 0.1875 0.1427 0.0405  0.0318  0.0318  192 ARG B NH2 
3799  N  N   . TYR B  193 ? 0.1295 0.1184 0.0908 -0.0003 0.0208  0.0127  193 TYR B N   
3800  C  CA  . TYR B  193 ? 0.1277 0.1159 0.1084 -0.0027 0.0121  0.0248  193 TYR B CA  
3801  C  C   . TYR B  193 ? 0.1405 0.1179 0.0906 0.0000  0.0172  -0.0017 193 TYR B C   
3802  O  O   . TYR B  193 ? 0.1251 0.1206 0.0944 0.0114  0.0115  0.0063  193 TYR B O   
3803  C  CB  . TYR B  193 ? 0.1168 0.1527 0.1138 0.0023  -0.0032 0.0447  193 TYR B CB  
3804  C  CG  . TYR B  193 ? 0.1052 0.1203 0.1053 0.0100  0.0017  0.0339  193 TYR B CG  
3805  C  CD1 . TYR B  193 ? 0.1010 0.1190 0.1006 0.0165  0.0248  0.0262  193 TYR B CD1 
3806  C  CD2 . TYR B  193 ? 0.1102 0.1124 0.1055 0.0131  0.0171  0.0186  193 TYR B CD2 
3807  C  CE1 . TYR B  193 ? 0.0863 0.0965 0.1050 0.0146  0.0159  0.0230  193 TYR B CE1 
3808  C  CE2 . TYR B  193 ? 0.1086 0.0891 0.0976 0.0077  0.0096  0.0063  193 TYR B CE2 
3809  C  CZ  . TYR B  193 ? 0.0877 0.0988 0.0949 0.0049  0.0258  0.0144  193 TYR B CZ  
3810  O  OH  . TYR B  193 ? 0.1039 0.1012 0.1109 0.0057  0.0293  0.0104  193 TYR B OH  
3811  N  N   . ARG B  194 ? 0.1951 0.1197 0.1084 -0.0026 0.0000  -0.0092 194 ARG B N   
3812  C  CA  . ARG B  194 ? 0.1913 0.1068 0.1097 -0.0120 0.0175  -0.0082 194 ARG B CA  
3813  C  C   . ARG B  194 ? 0.1536 0.1167 0.1195 0.0092  -0.0155 -0.0071 194 ARG B C   
3814  O  O   . ARG B  194 ? 0.1708 0.1414 0.1342 0.0020  -0.0291 0.0129  194 ARG B O   
3815  C  CB  . ARG B  194 ? 0.3310 0.1491 0.1240 -0.0292 0.0469  -0.0232 194 ARG B CB  
3816  C  CG  . ARG B  194 ? 0.4047 0.3183 0.1380 -0.0423 0.1074  -0.0182 194 ARG B CG  
3817  C  CD  . ARG B  194 ? 0.4318 0.5699 0.1644 -0.1321 0.1441  -0.0652 194 ARG B CD  
3818  N  NE  . ARG B  194 ? 0.4207 0.7577 0.6856 -0.1527 0.1370  -0.1030 194 ARG B NE  
3819  C  CZ  . ARG B  194 ? 0.6449 0.7366 0.3188 -0.1363 0.1351  -0.2142 194 ARG B CZ  
3820  N  NH1 . ARG B  194 ? 0.8953 0.8213 0.6669 0.0094  0.5033  0.1036  194 ARG B NH1 
3821  N  NH2 . ARG B  194 ? 0.2389 0.7980 0.9861 0.1019  -0.1150 0.0859  194 ARG B NH2 
3822  N  N   . GLY B  195 ? 0.1572 0.0979 0.1028 0.0063  -0.0065 -0.0121 195 GLY B N   
3823  C  CA  . GLY B  195 ? 0.1308 0.1204 0.1217 -0.0098 0.0164  0.0170  195 GLY B CA  
3824  C  C   . GLY B  195 ? 0.1125 0.1021 0.1093 0.0094  -0.0006 -0.0196 195 GLY B C   
3825  O  O   . GLY B  195 ? 0.1423 0.1195 0.1141 0.0040  0.0215  -0.0124 195 GLY B O   
3826  N  N   . SER B  196 ? 0.1125 0.1014 0.0971 -0.0017 0.0096  0.0017  196 SER B N   
3827  C  CA  . SER B  196 ? 0.1375 0.0886 0.1204 -0.0087 0.0034  0.0068  196 SER B CA  
3828  C  C   . SER B  196 ? 0.1073 0.0741 0.1154 0.0010  0.0114  -0.0060 196 SER B C   
3829  O  O   . SER B  196 ? 0.1150 0.0728 0.1163 0.0023  0.0183  -0.0086 196 SER B O   
3830  C  CB  . SER B  196 ? 0.1378 0.0851 0.1228 -0.0062 0.0126  -0.0230 196 SER B CB  
3831  O  OG  . SER B  196 ? 0.1197 0.0678 0.1398 0.0043  0.0093  -0.0063 196 SER B OG  
3832  N  N   . LEU B  197 ? 0.1252 0.0763 0.1048 0.0137  0.0098  0.0006  197 LEU B N   
3833  C  CA  . LEU B  197 ? 0.1066 0.0888 0.0996 0.0260  0.0182  -0.0017 197 LEU B CA  
3834  C  C   . LEU B  197 ? 0.0970 0.0730 0.1188 -0.0006 0.0035  0.0031  197 LEU B C   
3835  O  O   . LEU B  197 ? 0.1059 0.0926 0.1270 -0.0020 0.0027  -0.0013 197 LEU B O   
3836  C  CB  . LEU B  197 ? 0.1080 0.0933 0.1274 0.0208  0.0093  0.0035  197 LEU B CB  
3837  C  CG  . LEU B  197 ? 0.1398 0.1429 0.1676 0.0346  0.0081  0.0331  197 LEU B CG  
3838  C  CD1 . LEU B  197 ? 0.1781 0.1269 0.3580 0.0423  0.0099  0.0599  197 LEU B CD1 
3839  C  CD2 . LEU B  197 ? 0.1666 0.1684 0.2275 0.0248  0.0245  0.0227  197 LEU B CD2 
3840  N  N   . THR B  198 ? 0.1073 0.0751 0.1080 0.0204  0.0068  -0.0074 198 THR B N   
3841  C  CA  . THR B  198 ? 0.0895 0.0734 0.1206 0.0015  0.0212  0.0157  198 THR B CA  
3842  C  C   . THR B  198 ? 0.0985 0.0878 0.1103 -0.0070 0.0116  0.0037  198 THR B C   
3843  O  O   . THR B  198 ? 0.0958 0.0872 0.1290 -0.0140 0.0204  0.0121  198 THR B O   
3844  C  CB  . THR B  198 ? 0.0942 0.0766 0.1243 -0.0060 0.0149  0.0273  198 THR B CB  
3845  O  OG1 . THR B  198 ? 0.0786 0.0759 0.1136 0.0087  0.0221  0.0098  198 THR B OG1 
3846  C  CG2 . THR B  198 ? 0.1116 0.0804 0.1143 0.0126  0.0355  0.0205  198 THR B CG2 
3847  N  N   . THR B  199 ? 0.1344 0.0775 0.1252 0.0083  0.0007  0.0198  199 THR B N   
3848  C  CA  . THR B  199 ? 0.1879 0.0696 0.1018 0.0120  -0.0054 0.0154  199 THR B CA  
3849  C  C   . THR B  199 ? 0.1385 0.0815 0.1213 0.0131  -0.0038 0.0076  199 THR B C   
3850  O  O   . THR B  199 ? 0.1463 0.0886 0.1179 -0.0044 0.0068  -0.0020 199 THR B O   
3851  C  CB  . THR B  199 ? 0.2345 0.1152 0.1811 0.0306  -0.0498 0.0105  199 THR B CB  
3852  O  OG1 . THR B  199 ? 0.2026 0.1931 0.1982 0.0244  -0.0496 -0.0088 199 THR B OG1 
3853  C  CG2 . THR B  199 ? 0.3140 0.0988 0.1466 0.0013  -0.0285 -0.0262 199 THR B CG2 
3854  N  N   . PRO B  200 ? 0.1403 0.0806 0.1249 0.0052  0.0006  0.0199  200 PRO B N   
3855  C  CA  . PRO B  200 ? 0.1290 0.0658 0.1471 0.0071  -0.0103 0.0167  200 PRO B CA  
3856  C  C   . PRO B  200 ? 0.1330 0.0965 0.1404 0.0007  -0.0135 0.0225  200 PRO B C   
3857  O  O   . PRO B  200 ? 0.1328 0.1057 0.1696 0.0077  -0.0181 0.0256  200 PRO B O   
3858  C  CB  . PRO B  200 ? 0.1482 0.0829 0.1775 -0.0074 0.0082  0.0110  200 PRO B CB  
3859  C  CG  . PRO B  200 ? 0.1454 0.1094 0.1459 0.0005  -0.0062 0.0037  200 PRO B CG  
3860  C  CD  . PRO B  200 ? 0.1387 0.1040 0.1226 0.0100  0.0188  0.0153  200 PRO B CD  
3861  N  N   A PRO B  201 ? 0.1520 0.0906 0.1628 0.0148  -0.0111 0.0068  201 PRO B N   
3862  N  N   B PRO B  201 ? 0.1111 0.0978 0.1393 0.0120  0.0026  0.0249  201 PRO B N   
3863  C  CA  A PRO B  201 ? 0.1818 0.0838 0.1536 0.0524  -0.0346 -0.0136 201 PRO B CA  
3864  C  CA  B PRO B  201 ? 0.1224 0.0892 0.1419 0.0080  0.0087  -0.0010 201 PRO B CA  
3865  C  C   A PRO B  201 ? 0.1586 0.0829 0.1353 -0.0048 0.0171  -0.0046 201 PRO B C   
3866  C  C   B PRO B  201 ? 0.1256 0.0908 0.1348 -0.0308 -0.0081 0.0000  201 PRO B C   
3867  O  O   A PRO B  201 ? 0.1233 0.0877 0.1578 0.0001  0.0303  -0.0151 201 PRO B O   
3868  O  O   B PRO B  201 ? 0.1278 0.0929 0.0926 -0.0192 0.0209  -0.0133 201 PRO B O   
3869  C  CB  A PRO B  201 ? 0.1705 0.0958 0.2569 0.0219  0.0626  -0.0340 201 PRO B CB  
3870  C  CB  B PRO B  201 ? 0.1193 0.0881 0.1750 0.0083  0.0137  0.0098  201 PRO B CB  
3871  C  CG  A PRO B  201 ? 0.1919 0.2357 0.2527 0.0759  0.0065  -0.1099 201 PRO B CG  
3872  C  CG  B PRO B  201 ? 0.1097 0.0755 0.1701 0.0193  0.0200  -0.0149 201 PRO B CG  
3873  C  CD  A PRO B  201 ? 0.1782 0.1290 0.2330 0.0526  0.0206  0.0223  201 PRO B CD  
3874  C  CD  B PRO B  201 ? 0.1181 0.1100 0.1409 0.0324  0.0116  -0.0019 201 PRO B CD  
3875  N  N   . CYS B  202 ? 0.1213 0.0732 0.1671 0.0019  -0.0030 0.0046  202 CYS B N   
3876  C  CA  . CYS B  202 ? 0.1360 0.1075 0.1238 -0.0043 -0.0097 -0.0024 202 CYS B CA  
3877  C  C   . CYS B  202 ? 0.1375 0.0702 0.1283 0.0027  -0.0141 -0.0010 202 CYS B C   
3878  O  O   . CYS B  202 ? 0.1475 0.0976 0.1279 0.0052  -0.0024 -0.0030 202 CYS B O   
3879  C  CB  . CYS B  202 ? 0.1416 0.1222 0.1414 0.0003  -0.0111 0.0003  202 CYS B CB  
3880  S  SG  . CYS B  202 ? 0.1233 0.0938 0.1428 0.0007  0.0008  0.0032  202 CYS B SG  
3881  N  N   . ASN B  203 ? 0.1518 0.0936 0.1290 0.0216  0.0152  -0.0129 203 ASN B N   
3882  C  CA  . ASN B  203 ? 0.1599 0.1143 0.1490 0.0012  0.0019  -0.0024 203 ASN B CA  
3883  C  C   . ASN B  203 ? 0.1576 0.0912 0.1319 0.0188  0.0020  -0.0192 203 ASN B C   
3884  O  O   . ASN B  203 ? 0.1642 0.0931 0.1161 0.0104  0.0115  -0.0230 203 ASN B O   
3885  C  CB  . ASN B  203 ? 0.1768 0.1277 0.1687 0.0428  0.0211  -0.0148 203 ASN B CB  
3886  C  CG  . ASN B  203 ? 0.2296 0.1037 0.2691 0.0597  0.0270  0.0071  203 ASN B CG  
3887  O  OD1 . ASN B  203 ? 0.2978 0.2150 0.3486 0.0353  0.0236  0.0961  203 ASN B OD1 
3888  N  ND2 . ASN B  203 ? 0.2975 0.2242 0.3174 0.1401  0.0920  0.0595  203 ASN B ND2 
3889  N  N   . PRO B  204 ? 0.1842 0.1028 0.1349 0.0010  -0.0124 -0.0287 204 PRO B N   
3890  C  CA  . PRO B  204 ? 0.1581 0.1199 0.1177 0.0037  -0.0028 -0.0142 204 PRO B CA  
3891  C  C   . PRO B  204 ? 0.1829 0.1059 0.1376 -0.0121 -0.0074 -0.0335 204 PRO B C   
3892  O  O   . PRO B  204 ? 0.2299 0.1817 0.1222 -0.0208 0.0263  -0.0373 204 PRO B O   
3893  C  CB  . PRO B  204 ? 0.1711 0.1457 0.1905 -0.0390 -0.0164 -0.0282 204 PRO B CB  
3894  C  CG  . PRO B  204 ? 0.2310 0.1456 0.1536 -0.0272 -0.0403 -0.0264 204 PRO B CG  
3895  C  CD  . PRO B  204 ? 0.2114 0.1296 0.1398 -0.0296 0.0012  -0.0395 204 PRO B CD  
3896  N  N   . THR B  205 ? 0.1493 0.0998 0.1513 0.0083  0.0038  -0.0320 205 THR B N   
3897  C  CA  . THR B  205 ? 0.1608 0.1141 0.1694 0.0165  0.0177  -0.0381 205 THR B CA  
3898  C  C   . THR B  205 ? 0.1362 0.1328 0.1333 0.0237  0.0399  -0.0276 205 THR B C   
3899  O  O   . THR B  205 ? 0.1464 0.1482 0.1832 0.0315  0.0406  -0.0377 205 THR B O   
3900  C  CB  . THR B  205 ? 0.1876 0.1256 0.1820 0.0124  -0.0023 -0.0193 205 THR B CB  
3901  O  OG1 . THR B  205 ? 0.2120 0.1249 0.1777 0.0244  -0.0092 -0.0272 205 THR B OG1 
3902  C  CG2 . THR B  205 ? 0.2181 0.1290 0.2472 0.0126  -0.0038 -0.0498 205 THR B CG2 
3903  N  N   . VAL B  206 ? 0.1382 0.0978 0.1159 0.0121  0.0242  -0.0285 206 VAL B N   
3904  C  CA  . VAL B  206 ? 0.1252 0.1222 0.1168 0.0160  0.0320  -0.0206 206 VAL B CA  
3905  C  C   . VAL B  206 ? 0.1170 0.1387 0.1019 0.0131  0.0149  -0.0113 206 VAL B C   
3906  O  O   . VAL B  206 ? 0.1288 0.1365 0.1453 0.0088  -0.0003 0.0066  206 VAL B O   
3907  C  CB  . VAL B  206 ? 0.1499 0.1077 0.1129 0.0048  0.0408  -0.0137 206 VAL B CB  
3908  C  CG1 . VAL B  206 ? 0.1226 0.1107 0.1188 0.0015  0.0237  -0.0187 206 VAL B CG1 
3909  C  CG2 . VAL B  206 ? 0.1703 0.1133 0.1100 0.0297  0.0410  -0.0049 206 VAL B CG2 
3910  N  N   . LEU B  207 ? 0.1344 0.0951 0.1066 0.0017  0.0384  -0.0162 207 LEU B N   
3911  C  CA  . LEU B  207 ? 0.1333 0.1154 0.0939 0.0129  0.0326  -0.0043 207 LEU B CA  
3912  C  C   . LEU B  207 ? 0.1033 0.0994 0.0863 0.0098  0.0146  0.0068  207 LEU B C   
3913  O  O   . LEU B  207 ? 0.1023 0.1154 0.0935 0.0189  0.0126  -0.0003 207 LEU B O   
3914  C  CB  . LEU B  207 ? 0.1845 0.1710 0.0922 0.0097  0.0619  -0.0192 207 LEU B CB  
3915  C  CG  . LEU B  207 ? 0.3147 0.1768 0.1674 -0.0249 0.0575  0.0127  207 LEU B CG  
3916  C  CD1 . LEU B  207 ? 0.4266 0.3251 0.1773 -0.0024 -0.0221 0.0617  207 LEU B CD1 
3917  C  CD2 . LEU B  207 ? 0.3046 0.6463 0.2037 0.0142  0.1570  0.1717  207 LEU B CD2 
3918  N  N   . TRP B  208 ? 0.1080 0.0994 0.0958 0.0083  0.0116  0.0229  208 TRP B N   
3919  C  CA  . TRP B  208 ? 0.0969 0.0969 0.0886 0.0086  0.0148  0.0013  208 TRP B CA  
3920  C  C   . TRP B  208 ? 0.1133 0.0983 0.0764 0.0153  0.0076  0.0076  208 TRP B C   
3921  O  O   . TRP B  208 ? 0.1308 0.1125 0.0775 0.0104  0.0078  0.0164  208 TRP B O   
3922  C  CB  . TRP B  208 ? 0.0886 0.1194 0.0958 0.0052  0.0232  0.0099  208 TRP B CB  
3923  C  CG  . TRP B  208 ? 0.0803 0.1055 0.0952 0.0007  0.0189  -0.0038 208 TRP B CG  
3924  C  CD1 . TRP B  208 ? 0.0872 0.1328 0.0863 -0.0076 0.0200  0.0109  208 TRP B CD1 
3925  C  CD2 . TRP B  208 ? 0.0922 0.0890 0.0841 0.0007  0.0252  -0.0059 208 TRP B CD2 
3926  N  NE1 . TRP B  208 ? 0.0915 0.1067 0.1000 0.0081  0.0313  0.0000  208 TRP B NE1 
3927  C  CE2 . TRP B  208 ? 0.0838 0.0794 0.0912 0.0062  0.0193  -0.0105 208 TRP B CE2 
3928  C  CE3 . TRP B  208 ? 0.0897 0.0924 0.1010 0.0098  0.0104  -0.0057 208 TRP B CE3 
3929  C  CZ2 . TRP B  208 ? 0.1055 0.0848 0.0922 0.0100  0.0375  -0.0041 208 TRP B CZ2 
3930  C  CZ3 . TRP B  208 ? 0.1084 0.0798 0.0982 0.0148  0.0176  0.0020  208 TRP B CZ3 
3931  C  CH2 . TRP B  208 ? 0.1167 0.0917 0.0899 0.0063  0.0262  -0.0141 208 TRP B CH2 
3932  N  N   . THR B  209 ? 0.0967 0.0863 0.0847 0.0082  0.0296  0.0148  209 THR B N   
3933  C  CA  . THR B  209 ? 0.1070 0.0948 0.0736 0.0003  0.0190  0.0093  209 THR B CA  
3934  C  C   . THR B  209 ? 0.0908 0.1006 0.0657 0.0096  0.0228  0.0373  209 THR B C   
3935  O  O   . THR B  209 ? 0.1310 0.1147 0.0623 0.0379  0.0142  0.0275  209 THR B O   
3936  C  CB  . THR B  209 ? 0.1003 0.1079 0.0969 0.0104  0.0377  0.0167  209 THR B CB  
3937  O  OG1 . THR B  209 ? 0.1127 0.1271 0.0863 0.0223  0.0427  0.0221  209 THR B OG1 
3938  C  CG2 . THR B  209 ? 0.1283 0.1073 0.1032 0.0054  0.0148  0.0234  209 THR B CG2 
3939  N  N   . VAL B  210 ? 0.0890 0.0784 0.0863 0.0119  0.0174  0.0233  210 VAL B N   
3940  C  CA  . VAL B  210 ? 0.0872 0.0757 0.0845 0.0089  0.0311  0.0162  210 VAL B CA  
3941  C  C   . VAL B  210 ? 0.0859 0.0798 0.0816 0.0081  0.0275  0.0269  210 VAL B C   
3942  O  O   . VAL B  210 ? 0.1054 0.0948 0.0757 0.0035  0.0219  0.0249  210 VAL B O   
3943  C  CB  . VAL B  210 ? 0.0985 0.0996 0.0915 -0.0003 0.0195  0.0226  210 VAL B CB  
3944  C  CG1 . VAL B  210 ? 0.0908 0.1168 0.1008 0.0144  0.0403  0.0136  210 VAL B CG1 
3945  C  CG2 . VAL B  210 ? 0.1006 0.1190 0.1039 -0.0074 0.0225  0.0237  210 VAL B CG2 
3946  N  N   . PHE B  211 ? 0.0938 0.0802 0.0822 0.0066  0.0230  0.0182  211 PHE B N   
3947  C  CA  . PHE B  211 ? 0.0891 0.0701 0.1130 -0.0032 0.0138  0.0149  211 PHE B CA  
3948  C  C   . PHE B  211 ? 0.1039 0.0813 0.0883 0.0020  0.0280  0.0211  211 PHE B C   
3949  O  O   . PHE B  211 ? 0.1077 0.0992 0.1045 0.0071  0.0383  0.0318  211 PHE B O   
3950  C  CB  . PHE B  211 ? 0.0996 0.1077 0.1008 -0.0017 0.0227  0.0302  211 PHE B CB  
3951  C  CG  . PHE B  211 ? 0.0772 0.1027 0.0967 -0.0124 0.0110  0.0188  211 PHE B CG  
3952  C  CD1 . PHE B  211 ? 0.0956 0.1308 0.1190 -0.0120 0.0333  0.0299  211 PHE B CD1 
3953  C  CD2 . PHE B  211 ? 0.1237 0.1053 0.1093 -0.0071 -0.0024 0.0298  211 PHE B CD2 
3954  C  CE1 . PHE B  211 ? 0.0878 0.1542 0.1444 0.0023  0.0353  0.0467  211 PHE B CE1 
3955  C  CE2 . PHE B  211 ? 0.0918 0.1046 0.1666 -0.0143 0.0083  0.0469  211 PHE B CE2 
3956  C  CZ  . PHE B  211 ? 0.1048 0.1394 0.1692 -0.0068 0.0322  0.0353  211 PHE B CZ  
3957  N  N   . ARG B  212 ? 0.1040 0.0948 0.1003 0.0071  0.0178  0.0412  212 ARG B N   
3958  C  CA  . ARG B  212 ? 0.1262 0.0956 0.1032 0.0149  0.0138  0.0342  212 ARG B CA  
3959  C  C   . ARG B  212 ? 0.1216 0.1017 0.1107 -0.0043 0.0318  0.0303  212 ARG B C   
3960  O  O   . ARG B  212 ? 0.1335 0.1235 0.1288 0.0161  0.0390  0.0265  212 ARG B O   
3961  C  CB  . ARG B  212 ? 0.1446 0.1046 0.1082 0.0109  0.0142  0.0493  212 ARG B CB  
3962  C  CG  . ARG B  212 ? 0.1809 0.1190 0.1185 0.0392  0.0155  0.0522  212 ARG B CG  
3963  C  CD  . ARG B  212 ? 0.2017 0.1143 0.1536 0.0399  0.0263  0.0557  212 ARG B CD  
3964  N  NE  . ARG B  212 ? 0.2242 0.1689 0.1649 0.0776  0.0351  0.0688  212 ARG B NE  
3965  C  CZ  . ARG B  212 ? 0.2894 0.1747 0.1619 0.0925  0.0111  0.0465  212 ARG B CZ  
3966  N  NH1 . ARG B  212 ? 0.3142 0.1811 0.2095 0.0434  0.0644  0.0776  212 ARG B NH1 
3967  N  NH2 . ARG B  212 ? 0.3655 0.2409 0.2348 0.1497  0.0281  0.0786  212 ARG B NH2 
3968  N  N   . ASN B  213 ? 0.1310 0.0830 0.1075 -0.0046 0.0057  0.0286  213 ASN B N   
3969  C  CA  . ASN B  213 ? 0.1524 0.0965 0.1014 -0.0071 0.0076  0.0329  213 ASN B CA  
3970  C  C   . ASN B  213 ? 0.1186 0.0940 0.1048 -0.0065 0.0163  0.0258  213 ASN B C   
3971  O  O   . ASN B  213 ? 0.1596 0.0845 0.1199 0.0141  0.0274  0.0293  213 ASN B O   
3972  C  CB  . ASN B  213 ? 0.1973 0.0926 0.1289 -0.0395 0.0052  0.0399  213 ASN B CB  
3973  C  CG  . ASN B  213 ? 0.2045 0.1149 0.2206 -0.0274 -0.0221 0.0751  213 ASN B CG  
3974  O  OD1 . ASN B  213 ? 0.2809 0.2109 0.3023 0.0074  0.0262  0.1701  213 ASN B OD1 
3975  N  ND2 . ASN B  213 ? 0.3736 0.1847 0.2524 -0.0364 0.0776  0.1431  213 ASN B ND2 
3976  N  N   . PRO B  214 ? 0.1315 0.0947 0.1080 0.0259  0.0210  0.0188  214 PRO B N   
3977  C  CA  . PRO B  214 ? 0.1075 0.0976 0.1156 0.0087  0.0294  0.0178  214 PRO B CA  
3978  C  C   . PRO B  214 ? 0.1075 0.0947 0.1106 -0.0027 0.0146  0.0291  214 PRO B C   
3979  O  O   . PRO B  214 ? 0.1375 0.1006 0.1351 -0.0264 0.0060  0.0230  214 PRO B O   
3980  C  CB  . PRO B  214 ? 0.1188 0.1436 0.1265 0.0219  0.0196  0.0034  214 PRO B CB  
3981  C  CG  . PRO B  214 ? 0.1865 0.1623 0.1772 0.0282  0.0522  0.0269  214 PRO B CG  
3982  C  CD  . PRO B  214 ? 0.1680 0.1253 0.1484 0.0460  0.0221  0.0172  214 PRO B CD  
3983  N  N   . VAL B  215 ? 0.1050 0.1012 0.1024 -0.0034 0.0120  0.0186  215 VAL B N   
3984  C  CA  . VAL B  215 ? 0.1027 0.0807 0.1073 -0.0041 0.0010  0.0048  215 VAL B CA  
3985  C  C   . VAL B  215 ? 0.1091 0.0644 0.1158 -0.0015 0.0082  0.0110  215 VAL B C   
3986  O  O   . VAL B  215 ? 0.1057 0.1026 0.1247 -0.0129 0.0175  -0.0098 215 VAL B O   
3987  C  CB  . VAL B  215 ? 0.1032 0.0953 0.1206 0.0071  0.0310  0.0184  215 VAL B CB  
3988  C  CG1 . VAL B  215 ? 0.1231 0.1435 0.1394 -0.0174 0.0449  -0.0006 215 VAL B CG1 
3989  C  CG2 . VAL B  215 ? 0.1251 0.0820 0.1265 0.0054  0.0109  0.0013  215 VAL B CG2 
3990  N  N   . GLN B  216 ? 0.1247 0.0599 0.1073 0.0063  0.0138  0.0071  216 GLN B N   
3991  C  CA  . GLN B  216 ? 0.1317 0.0811 0.0948 0.0043  0.0074  0.0046  216 GLN B CA  
3992  C  C   . GLN B  216 ? 0.1077 0.0813 0.1103 -0.0049 0.0065  -0.0155 216 GLN B C   
3993  O  O   . GLN B  216 ? 0.1167 0.1102 0.1215 0.0015  0.0063  0.0026  216 GLN B O   
3994  C  CB  . GLN B  216 ? 0.1588 0.0838 0.1362 0.0231  0.0100  -0.0138 216 GLN B CB  
3995  C  CG  . GLN B  216 ? 0.1729 0.1037 0.1395 0.0104  0.0125  0.0182  216 GLN B CG  
3996  C  CD  . GLN B  216 ? 0.1875 0.1140 0.1498 0.0178  0.0060  0.0247  216 GLN B CD  
3997  O  OE1 . GLN B  216 ? 0.1782 0.1244 0.1617 0.0071  -0.0017 0.0313  216 GLN B OE1 
3998  N  NE2 . GLN B  216 ? 0.3420 0.1757 0.1996 0.0649  -0.0834 -0.0333 216 GLN B NE2 
3999  N  N   . ILE B  217 ? 0.1369 0.0665 0.0903 0.0057  0.0204  -0.0103 217 ILE B N   
4000  C  CA  . ILE B  217 ? 0.1324 0.0715 0.0953 0.0034  0.0129  -0.0098 217 ILE B CA  
4001  C  C   . ILE B  217 ? 0.1348 0.0544 0.0969 0.0046  0.0131  -0.0031 217 ILE B C   
4002  O  O   . ILE B  217 ? 0.1371 0.0723 0.1106 0.0120  0.0099  -0.0054 217 ILE B O   
4003  C  CB  . ILE B  217 ? 0.1287 0.0642 0.1114 0.0104  0.0168  -0.0210 217 ILE B CB  
4004  C  CG1 . ILE B  217 ? 0.1340 0.0733 0.1109 -0.0068 0.0289  -0.0003 217 ILE B CG1 
4005  C  CG2 . ILE B  217 ? 0.1337 0.0784 0.1246 -0.0028 0.0231  -0.0154 217 ILE B CG2 
4006  C  CD1 . ILE B  217 ? 0.1799 0.0809 0.1231 -0.0361 0.0296  -0.0038 217 ILE B CD1 
4007  N  N   . SER B  218 ? 0.1346 0.0605 0.1023 0.0010  0.0116  -0.0118 218 SER B N   
4008  C  CA  . SER B  218 ? 0.1430 0.0698 0.1018 -0.0003 0.0164  -0.0294 218 SER B CA  
4009  C  C   . SER B  218 ? 0.1421 0.0806 0.1064 0.0259  0.0193  -0.0057 218 SER B C   
4010  O  O   . SER B  218 ? 0.1728 0.0742 0.1124 0.0126  0.0271  0.0092  218 SER B O   
4011  C  CB  . SER B  218 ? 0.1626 0.0824 0.1106 0.0236  -0.0048 -0.0258 218 SER B CB  
4012  O  OG  . SER B  218 ? 0.1831 0.1032 0.1097 0.0223  0.0077  -0.0140 218 SER B OG  
4013  N  N   . GLN B  219 ? 0.1412 0.1136 0.1319 0.0223  0.0309  -0.0143 219 GLN B N   
4014  C  CA  . GLN B  219 ? 0.1624 0.1142 0.1347 0.0239  0.0350  0.0120  219 GLN B CA  
4015  C  C   . GLN B  219 ? 0.1890 0.1067 0.1055 0.0178  0.0364  -0.0087 219 GLN B C   
4016  O  O   . GLN B  219 ? 0.1887 0.1018 0.1222 0.0149  0.0320  -0.0087 219 GLN B O   
4017  C  CB  . GLN B  219 ? 0.2443 0.1875 0.1976 0.1112  0.1464  0.0498  219 GLN B CB  
4018  C  CG  . GLN B  219 ? 0.2768 0.3190 0.2878 0.1058  0.1381  0.0778  219 GLN B CG  
4019  C  CD  . GLN B  219 ? 0.3291 0.3713 0.3930 0.1098  0.1878  0.0964  219 GLN B CD  
4020  O  OE1 . GLN B  219 ? 0.4305 0.4674 0.3849 -0.0276 0.1720  0.1000  219 GLN B OE1 
4021  N  NE2 . GLN B  219 ? 0.3853 0.4679 0.4899 0.1406  0.0898  -0.0820 219 GLN B NE2 
4022  N  N   . GLU B  220 ? 0.2059 0.1152 0.0958 0.0324  0.0533  -0.0127 220 GLU B N   
4023  C  CA  . GLU B  220 ? 0.2308 0.1114 0.1430 0.0190  0.0233  -0.0068 220 GLU B CA  
4024  C  C   . GLU B  220 ? 0.1772 0.1172 0.1079 0.0186  0.0120  -0.0171 220 GLU B C   
4025  O  O   . GLU B  220 ? 0.2069 0.1137 0.1064 0.0233  0.0318  -0.0006 220 GLU B O   
4026  C  CB  . GLU B  220 ? 0.2481 0.1902 0.1243 0.0077  0.0005  -0.0632 220 GLU B CB  
4027  C  CG  . GLU B  220 ? 0.2948 0.1712 0.1310 0.0505  -0.0074 -0.0417 220 GLU B CG  
4028  C  CD  . GLU B  220 ? 0.3431 0.1888 0.1465 0.0088  0.0406  -0.0478 220 GLU B CD  
4029  O  OE1 . GLU B  220 ? 0.2931 0.1484 0.1777 -0.0295 0.0500  -0.0487 220 GLU B OE1 
4030  O  OE2 . GLU B  220 ? 0.5181 0.1944 0.2723 0.0494  0.1071  -0.0527 220 GLU B OE2 
4031  N  N   . GLN B  221 ? 0.1641 0.1224 0.0924 0.0172  0.0192  -0.0175 221 GLN B N   
4032  C  CA  . GLN B  221 ? 0.1705 0.0996 0.0942 0.0177  0.0359  0.0043  221 GLN B CA  
4033  C  C   . GLN B  221 ? 0.1486 0.0873 0.1109 0.0087  0.0381  -0.0185 221 GLN B C   
4034  O  O   . GLN B  221 ? 0.1779 0.0809 0.1185 0.0066  0.0540  -0.0027 221 GLN B O   
4035  C  CB  . GLN B  221 ? 0.1655 0.0854 0.0998 0.0068  0.0197  0.0148  221 GLN B CB  
4036  C  CG  . GLN B  221 ? 0.1463 0.0870 0.1098 0.0186  0.0161  -0.0035 221 GLN B CG  
4037  C  CD  . GLN B  221 ? 0.1488 0.0590 0.0997 0.0065  0.0092  -0.0102 221 GLN B CD  
4038  O  OE1 . GLN B  221 ? 0.1369 0.0742 0.1204 0.0082  0.0055  -0.0060 221 GLN B OE1 
4039  N  NE2 . GLN B  221 ? 0.1491 0.0842 0.1234 0.0263  0.0032  -0.0103 221 GLN B NE2 
4040  N  N   . LEU B  222 ? 0.1265 0.1052 0.1105 0.0038  0.0412  -0.0026 222 LEU B N   
4041  C  CA  . LEU B  222 ? 0.1299 0.0915 0.1317 0.0127  0.0421  0.0027  222 LEU B CA  
4042  C  C   . LEU B  222 ? 0.1454 0.0901 0.1276 0.0152  0.0604  -0.0052 222 LEU B C   
4043  O  O   . LEU B  222 ? 0.1587 0.0888 0.1218 0.0078  0.0476  0.0028  222 LEU B O   
4044  C  CB  . LEU B  222 ? 0.1795 0.0998 0.1268 0.0148  0.0392  -0.0034 222 LEU B CB  
4045  C  CG  . LEU B  222 ? 0.1705 0.1045 0.1136 0.0060  0.0276  -0.0057 222 LEU B CG  
4046  C  CD1 . LEU B  222 ? 0.1967 0.1077 0.1082 -0.0030 0.0273  0.0110  222 LEU B CD1 
4047  C  CD2 . LEU B  222 ? 0.1703 0.1197 0.1292 -0.0089 0.0193  -0.0241 222 LEU B CD2 
4048  N  N   . LEU B  223 ? 0.1662 0.1177 0.1005 0.0119  0.0463  0.0098  223 LEU B N   
4049  C  CA  . LEU B  223 ? 0.2210 0.1170 0.1134 0.0394  0.0780  0.0311  223 LEU B CA  
4050  C  C   . LEU B  223 ? 0.1957 0.1224 0.1079 0.0031  0.0355  0.0121  223 LEU B C   
4051  O  O   . LEU B  223 ? 0.2199 0.1062 0.1453 0.0151  0.0533  0.0324  223 LEU B O   
4052  C  CB  . LEU B  223 ? 0.2536 0.1324 0.1116 0.0375  0.0763  0.0093  223 LEU B CB  
4053  C  CG  . LEU B  223 ? 0.2552 0.1583 0.1450 0.0258  0.1013  0.0280  223 LEU B CG  
4054  C  CD1 . LEU B  223 ? 0.2345 0.2053 0.2439 0.0172  0.1120  0.0129  223 LEU B CD1 
4055  C  CD2 . LEU B  223 ? 0.3528 0.2117 0.1492 0.0348  0.1231  -0.0333 223 LEU B CD2 
4056  N  N   . ALA B  224 ? 0.2032 0.1287 0.1286 0.0082  0.0346  0.0000  224 ALA B N   
4057  C  CA  . ALA B  224 ? 0.1863 0.1366 0.1306 0.0148  0.0241  0.0237  224 ALA B CA  
4058  C  C   . ALA B  224 ? 0.1772 0.1394 0.1393 -0.0010 0.0562  0.0379  224 ALA B C   
4059  O  O   . ALA B  224 ? 0.2249 0.1298 0.1608 0.0331  0.0751  0.0383  224 ALA B O   
4060  C  CB  . ALA B  224 ? 0.1926 0.1868 0.1815 -0.0015 0.0183  0.0509  224 ALA B CB  
4061  N  N   . LEU B  225 ? 0.1655 0.1362 0.1429 0.0222  0.0504  0.0161  225 LEU B N   
4062  C  CA  . LEU B  225 ? 0.1669 0.1094 0.1434 0.0133  0.0908  0.0188  225 LEU B CA  
4063  C  C   . LEU B  225 ? 0.1626 0.1046 0.1587 0.0183  0.0881  -0.0006 225 LEU B C   
4064  O  O   . LEU B  225 ? 0.1885 0.0881 0.1958 0.0283  0.0881  0.0228  225 LEU B O   
4065  C  CB  . LEU B  225 ? 0.1597 0.1106 0.1150 0.0060  0.0491  0.0148  225 LEU B CB  
4066  C  CG  . LEU B  225 ? 0.1335 0.1513 0.1400 -0.0005 0.0322  0.0138  225 LEU B CG  
4067  C  CD1 . LEU B  225 ? 0.1444 0.1420 0.1554 0.0263  0.0271  -0.0262 225 LEU B CD1 
4068  C  CD2 . LEU B  225 ? 0.1745 0.1378 0.1152 -0.0019 0.0432  0.0102  225 LEU B CD2 
4069  N  N   . GLU B  226 ? 0.1561 0.1010 0.1137 0.0093  0.0659  0.0059  226 GLU B N   
4070  C  CA  . GLU B  226 ? 0.1606 0.0980 0.1398 -0.0077 0.0653  0.0188  226 GLU B CA  
4071  C  C   . GLU B  226 ? 0.1414 0.0942 0.1224 0.0007  0.0527  0.0297  226 GLU B C   
4072  O  O   . GLU B  226 ? 0.2086 0.1639 0.1450 -0.0405 0.0564  0.0390  226 GLU B O   
4073  C  CB  . GLU B  226 ? 0.1741 0.1059 0.1158 0.0182  0.0740  0.0313  226 GLU B CB  
4074  C  CG  . GLU B  226 ? 0.1919 0.1107 0.1145 0.0104  0.0540  0.0086  226 GLU B CG  
4075  C  CD  . GLU B  226 ? 0.1844 0.1296 0.1084 0.0252  0.0621  0.0035  226 GLU B CD  
4076  O  OE1 . GLU B  226 ? 0.2154 0.1502 0.1177 0.0465  0.0904  0.0125  226 GLU B OE1 
4077  O  OE2 . GLU B  226 ? 0.2416 0.1190 0.1159 0.0087  0.0562  0.0071  226 GLU B OE2 
4078  N  N   . THR B  227 ? 0.1617 0.1222 0.1256 0.0381  0.0546  0.0295  227 THR B N   
4079  C  CA  . THR B  227 ? 0.2082 0.1561 0.1185 0.0445  0.0644  0.0423  227 THR B CA  
4080  C  C   . THR B  227 ? 0.2131 0.1082 0.1673 0.0199  0.0449  0.0362  227 THR B C   
4081  O  O   . THR B  227 ? 0.3939 0.1684 0.1324 0.0641  0.0469  0.0524  227 THR B O   
4082  C  CB  . THR B  227 ? 0.2050 0.1884 0.1185 0.0326  0.0544  0.0149  227 THR B CB  
4083  O  OG1 . THR B  227 ? 0.2005 0.1432 0.1529 0.0286  0.0592  0.0209  227 THR B OG1 
4084  C  CG2 . THR B  227 ? 0.1813 0.1818 0.1581 0.0222  0.0636  0.0162  227 THR B CG2 
4085  N  N   . ALA B  228 ? 0.1913 0.1230 0.1650 0.0340  0.0055  0.0017  228 ALA B N   
4086  C  CA  . ALA B  228 ? 0.2901 0.1088 0.2497 0.0599  -0.0582 -0.0019 228 ALA B CA  
4087  C  C   . ALA B  228 ? 0.3253 0.1005 0.1809 0.0724  -0.0450 0.0098  228 ALA B C   
4088  O  O   . ALA B  228 ? 0.5446 0.1308 0.2226 0.1014  -0.1479 0.0094  228 ALA B O   
4089  C  CB  . ALA B  228 ? 0.1987 0.2035 0.5009 0.0728  -0.0379 0.0114  228 ALA B CB  
4090  N  N   . LEU B  229 ? 0.2319 0.0824 0.1368 -0.0003 0.0267  0.0368  229 LEU B N   
4091  C  CA  . LEU B  229 ? 0.1824 0.0944 0.1268 0.0000  0.0285  0.0247  229 LEU B CA  
4092  C  C   . LEU B  229 ? 0.1850 0.1012 0.1145 0.0119  0.0461  0.0333  229 LEU B C   
4093  O  O   . LEU B  229 ? 0.1770 0.1096 0.1357 0.0118  0.0595  0.0432  229 LEU B O   
4094  C  CB  . LEU B  229 ? 0.1571 0.1599 0.1319 -0.0185 0.0318  0.0357  229 LEU B CB  
4095  C  CG  . LEU B  229 ? 0.1865 0.1215 0.1398 -0.0315 0.0308  0.0241  229 LEU B CG  
4096  C  CD1 . LEU B  229 ? 0.1766 0.2050 0.1480 -0.0472 0.0520  0.0362  229 LEU B CD1 
4097  C  CD2 . LEU B  229 ? 0.1734 0.3064 0.2592 -0.0463 -0.0225 0.1923  229 LEU B CD2 
4098  N  N   . TYR B  230 ? 0.1949 0.0921 0.1550 -0.0098 0.0590  0.0597  230 TYR B N   
4099  C  CA  . TYR B  230 ? 0.2239 0.0873 0.1629 -0.0148 0.0397  0.0670  230 TYR B CA  
4100  C  C   . TYR B  230 ? 0.1669 0.1238 0.1696 -0.0177 0.0208  0.0643  230 TYR B C   
4101  O  O   . TYR B  230 ? 0.1811 0.1304 0.1789 0.0015  0.0538  0.0308  230 TYR B O   
4102  C  CB  . TYR B  230 ? 0.2280 0.0931 0.1504 -0.0078 0.0659  0.0456  230 TYR B CB  
4103  C  CG  . TYR B  230 ? 0.2043 0.0859 0.1495 0.0024  0.0285  0.0397  230 TYR B CG  
4104  C  CD1 . TYR B  230 ? 0.2935 0.1317 0.1571 -0.0273 0.0244  0.0597  230 TYR B CD1 
4105  C  CD2 . TYR B  230 ? 0.2213 0.2542 0.1080 0.0219  0.0599  0.0542  230 TYR B CD2 
4106  C  CE1 . TYR B  230 ? 0.3882 0.1362 0.1680 0.0083  -0.0121 0.0264  230 TYR B CE1 
4107  C  CE2 . TYR B  230 ? 0.3799 0.3048 0.0778 0.0803  0.0386  0.0284  230 TYR B CE2 
4108  C  CZ  . TYR B  230 ? 0.3892 0.2333 0.1316 0.0958  0.0260  0.0131  230 TYR B CZ  
4109  O  OH  . TYR B  230 ? 0.6262 0.2257 0.1699 0.1792  0.0555  0.0155  230 TYR B OH  
4110  N  N   . CYS B  231 ? 0.1757 0.1883 0.1211 0.0099  0.0590  0.0685  231 CYS B N   
4111  C  CA  . CYS B  231 ? 0.1525 0.1738 0.1254 -0.0038 0.0562  0.0577  231 CYS B CA  
4112  C  C   . CYS B  231 ? 0.1964 0.1642 0.1254 -0.0054 0.0659  0.0355  231 CYS B C   
4113  O  O   . CYS B  231 ? 0.2283 0.1814 0.1170 -0.0100 0.0788  0.0274  231 CYS B O   
4114  C  CB  . CYS B  231 ? 0.2183 0.2197 0.1639 -0.0175 0.0229  0.0998  231 CYS B CB  
4115  S  SG  . CYS B  231 ? 0.2299 0.2057 0.2082 -0.0126 0.0351  0.0788  231 CYS B SG  
4116  N  N   . THR B  232 ? 0.2134 0.1439 0.1326 -0.0160 0.0577  0.0675  232 THR B N   
4117  C  CA  . THR B  232 ? 0.1933 0.1197 0.1188 -0.0078 0.0750  0.0247  232 THR B CA  
4118  C  C   . THR B  232 ? 0.1721 0.1421 0.1260 0.0000  0.0671  0.0322  232 THR B C   
4119  O  O   . THR B  232 ? 0.1550 0.1533 0.1773 0.0093  0.0864  0.0381  232 THR B O   
4120  C  CB  . THR B  232 ? 0.1829 0.1224 0.1228 0.0203  0.0710  0.0263  232 THR B CB  
4121  O  OG1 . THR B  232 ? 0.1804 0.1229 0.1439 0.0105  0.0810  0.0328  232 THR B OG1 
4122  C  CG2 . THR B  232 ? 0.2073 0.1745 0.1667 0.0333  0.0675  0.0285  232 THR B CG2 
4123  N  N   . HIS B  233 ? 0.1965 0.1337 0.1605 0.0263  0.1032  0.0403  233 HIS B N   
4124  C  CA  . HIS B  233 ? 0.1933 0.1335 0.1597 0.0302  0.0873  0.0232  233 HIS B CA  
4125  C  C   . HIS B  233 ? 0.1669 0.1010 0.1515 0.0120  0.0790  0.0292  233 HIS B C   
4126  O  O   . HIS B  233 ? 0.1793 0.1249 0.1780 0.0129  0.0839  0.0606  233 HIS B O   
4127  C  CB  . HIS B  233 ? 0.2450 0.1362 0.2342 0.0333  0.0807  0.0156  233 HIS B CB  
4128  C  CG  . HIS B  233 ? 0.2197 0.1477 0.3756 -0.0160 0.0982  -0.0842 233 HIS B CG  
4129  N  ND1 . HIS B  233 ? 0.2759 0.4176 0.4995 -0.0469 0.0626  -0.2096 233 HIS B ND1 
4130  C  CD2 . HIS B  233 ? 0.2782 0.1702 0.4113 0.0144  0.1512  -0.0927 233 HIS B CD2 
4131  C  CE1 . HIS B  233 ? 0.3560 0.3882 0.6093 -0.0575 0.1647  -0.2461 233 HIS B CE1 
4132  N  NE2 . HIS B  233 ? 0.3454 0.2685 0.4099 -0.0107 0.1644  -0.1484 233 HIS B NE2 
4133  N  N   A MET B  234 ? 0.1714 0.1111 0.1631 0.0083  0.0738  0.0584  234 MET B N   
4134  N  N   B MET B  234 ? 0.1827 0.1468 0.1477 0.0300  0.0807  0.0274  234 MET B N   
4135  C  CA  A MET B  234 ? 0.1798 0.1281 0.1818 0.0205  0.0688  0.0229  234 MET B CA  
4136  C  CA  B MET B  234 ? 0.1745 0.1391 0.1464 0.0003  0.0903  0.0355  234 MET B CA  
4137  C  C   A MET B  234 ? 0.1969 0.1147 0.1344 0.0054  0.0524  -0.0068 234 MET B C   
4138  C  C   B MET B  234 ? 0.1928 0.1235 0.0833 -0.0164 0.0707  0.0111  234 MET B C   
4139  O  O   A MET B  234 ? 0.1307 0.1036 0.1268 0.0073  0.0048  -0.0063 234 MET B O   
4140  O  O   B MET B  234 ? 0.1292 0.1784 0.1084 -0.0020 0.0406  0.0001  234 MET B O   
4141  C  CB  A MET B  234 ? 0.1933 0.0944 0.1858 0.0303  0.0262  0.0278  234 MET B CB  
4142  C  CB  B MET B  234 ? 0.1506 0.2687 0.1396 -0.0750 0.0886  -0.0027 234 MET B CB  
4143  C  CG  A MET B  234 ? 0.2325 0.2818 0.1597 -0.0256 -0.0118 0.0732  234 MET B CG  
4144  C  CG  B MET B  234 ? 0.2089 0.1844 0.2029 0.0052  0.1101  -0.0662 234 MET B CG  
4145  S  SD  A MET B  234 ? 0.1723 0.3122 0.1763 0.0313  0.0794  0.0083  234 MET B SD  
4146  S  SD  B MET B  234 ? 0.2610 0.2343 0.2651 0.0060  -0.0335 0.0162  234 MET B SD  
4147  C  CE  A MET B  234 ? 0.2039 0.4074 0.0741 -0.0032 0.0493  -0.0024 234 MET B CE  
4148  C  CE  B MET B  234 ? 0.1976 0.3684 0.3366 0.1422  0.1309  -0.0500 234 MET B CE  
4149  N  N   A ASP B  235 ? 0.1420 0.1107 0.1464 0.0054  0.0474  0.0277  235 ASP B N   
4150  N  N   B ASP B  235 ? 0.2585 0.1168 0.1071 -0.0324 0.0406  0.0441  235 ASP B N   
4151  C  CA  A ASP B  235 ? 0.2165 0.0821 0.1881 -0.0155 0.0653  0.0441  235 ASP B CA  
4152  C  CA  B ASP B  235 ? 0.2245 0.1887 0.1167 -0.0463 0.0381  0.0667  235 ASP B CA  
4153  C  C   A ASP B  235 ? 0.2314 0.1170 0.0991 -0.0315 0.0582  0.0120  235 ASP B C   
4154  C  C   B ASP B  235 ? 0.2244 0.1120 0.1407 -0.0353 0.0289  0.0274  235 ASP B C   
4155  O  O   A ASP B  235 ? 0.2592 0.0969 0.1520 -0.0516 0.0711  0.0250  235 ASP B O   
4156  O  O   B ASP B  235 ? 0.2500 0.1272 0.1349 -0.0549 0.0126  0.0476  235 ASP B O   
4157  C  CB  A ASP B  235 ? 0.2490 0.1346 0.1576 0.0132  -0.0198 0.0828  235 ASP B CB  
4158  C  CB  B ASP B  235 ? 0.3334 0.1865 0.1759 -0.0259 0.0608  0.1154  235 ASP B CB  
4159  C  CG  A ASP B  235 ? 0.2411 0.0821 0.2944 0.0471  -0.0474 -0.0060 235 ASP B CG  
4160  C  CG  B ASP B  235 ? 0.4536 0.3045 0.2793 0.0294  -0.0758 0.1360  235 ASP B CG  
4161  O  OD1 A ASP B  235 ? 0.3470 0.1285 0.2497 0.0644  0.0383  -0.0640 235 ASP B OD1 
4162  O  OD1 B ASP B  235 ? 0.5257 0.2601 0.3874 0.0903  -0.0065 0.1344  235 ASP B OD1 
4163  O  OD2 A ASP B  235 ? 0.4205 0.1263 0.4777 0.1045  0.0628  0.1027  235 ASP B OD2 
4164  O  OD2 B ASP B  235 ? 0.3736 0.4255 0.5133 0.1290  -0.1427 0.1620  235 ASP B OD2 
4165  N  N   . ASP B  236 ? 0.1991 0.1491 0.1296 -0.0046 0.0436  0.0243  236 ASP B N   
4166  C  CA  . ASP B  236 ? 0.1833 0.1321 0.1259 -0.0035 0.0410  0.0306  236 ASP B CA  
4167  C  C   . ASP B  236 ? 0.2055 0.0789 0.1314 -0.0087 0.0485  0.0333  236 ASP B C   
4168  O  O   . ASP B  236 ? 0.1856 0.1033 0.1459 -0.0215 0.0383  0.0094  236 ASP B O   
4169  C  CB  . ASP B  236 ? 0.2289 0.1761 0.1211 -0.0226 0.0500  0.0436  236 ASP B CB  
4170  C  CG  . ASP B  236 ? 0.2467 0.1571 0.1429 -0.0379 0.0788  0.0093  236 ASP B CG  
4171  O  OD1 . ASP B  236 ? 0.2696 0.1685 0.1350 -0.0392 0.0439  -0.0233 236 ASP B OD1 
4172  O  OD2 . ASP B  236 ? 0.3080 0.2391 0.1577 -0.0445 0.0834  -0.0082 236 ASP B OD2 
4173  N  N   . PRO B  237 ? 0.2287 0.1001 0.1421 -0.0221 0.0562  0.0299  237 PRO B N   
4174  C  CA  . PRO B  237 ? 0.2025 0.1159 0.1585 -0.0157 0.0627  0.0410  237 PRO B CA  
4175  C  C   . PRO B  237 ? 0.1872 0.1292 0.1328 -0.0230 0.0520  0.0275  237 PRO B C   
4176  O  O   . PRO B  237 ? 0.1942 0.1527 0.1350 -0.0148 0.0553  0.0357  237 PRO B O   
4177  C  CB  . PRO B  237 ? 0.2592 0.1041 0.1894 -0.0241 0.0584  0.0384  237 PRO B CB  
4178  C  CG  . PRO B  237 ? 0.2716 0.1204 0.2764 -0.0267 0.1194  0.0098  237 PRO B CG  
4179  C  CD  . PRO B  237 ? 0.2318 0.0866 0.1762 -0.0436 0.0582  0.0113  237 PRO B CD  
4180  N  N   A SER B  238 ? 0.1969 0.1228 0.1212 -0.0516 0.0575  0.0219  238 SER B N   
4181  N  N   B SER B  238 ? 0.2154 0.0737 0.1220 -0.0471 0.0276  0.0151  238 SER B N   
4182  C  CA  A SER B  238 ? 0.2213 0.1202 0.1330 -0.0465 0.0315  0.0350  238 SER B CA  
4183  C  CA  B SER B  238 ? 0.1917 0.1032 0.1127 -0.0266 0.0337  0.0255  238 SER B CA  
4184  C  C   A SER B  238 ? 0.1799 0.0989 0.1243 -0.0239 0.0511  0.0119  238 SER B C   
4185  C  C   B SER B  238 ? 0.1852 0.0834 0.0958 -0.0164 0.0304  0.0226  238 SER B C   
4186  O  O   A SER B  238 ? 0.1693 0.1403 0.1211 0.0245  0.0329  0.0364  238 SER B O   
4187  O  O   B SER B  238 ? 0.1668 0.1147 0.0863 -0.0138 0.0186  0.0102  238 SER B O   
4188  C  CB  A SER B  238 ? 0.3120 0.1374 0.1985 -0.1335 0.0026  0.0667  238 SER B CB  
4189  C  CB  B SER B  238 ? 0.1797 0.2109 0.1702 -0.0826 -0.0046 0.0548  238 SER B CB  
4190  O  OG  A SER B  238 ? 0.3743 0.3079 0.2730 -0.1178 -0.0283 0.1374  238 SER B OG  
4191  O  OG  B SER B  238 ? 0.2772 0.2438 0.1319 -0.1527 0.0020  0.0383  238 SER B OG  
4192  N  N   . PRO B  239 ? 0.1974 0.0985 0.1049 -0.0287 0.0489  0.0138  239 PRO B N   
4193  C  CA  . PRO B  239 ? 0.1906 0.1137 0.1335 -0.0390 0.0540  0.0384  239 PRO B CA  
4194  C  C   . PRO B  239 ? 0.1529 0.1168 0.1335 0.0017  0.0590  0.0288  239 PRO B C   
4195  O  O   . PRO B  239 ? 0.1739 0.1271 0.1614 0.0062  0.0617  0.0439  239 PRO B O   
4196  C  CB  . PRO B  239 ? 0.2167 0.1407 0.1502 -0.0692 0.0452  0.0041  239 PRO B CB  
4197  C  CG  . PRO B  239 ? 0.3127 0.1747 0.1371 -0.1301 0.0662  -0.0093 239 PRO B CG  
4198  C  CD  . PRO B  239 ? 0.2050 0.1269 0.1021 -0.0288 0.0496  -0.0132 239 PRO B CD  
4199  N  N   . ARG B  240 ? 0.1633 0.1333 0.1357 -0.0107 0.0623  0.0529  240 ARG B N   
4200  C  CA  . ARG B  240 ? 0.1764 0.1448 0.1601 -0.0218 0.0298  0.0617  240 ARG B CA  
4201  C  C   . ARG B  240 ? 0.1579 0.1347 0.1459 -0.0068 0.0537  0.0693  240 ARG B C   
4202  O  O   . ARG B  240 ? 0.1653 0.1435 0.1630 -0.0052 0.0483  0.0617  240 ARG B O   
4203  C  CB  . ARG B  240 ? 0.1701 0.1520 0.1759 -0.0085 0.0065  0.0522  240 ARG B CB  
4204  C  CG  . ARG B  240 ? 0.2222 0.2490 0.1789 -0.0852 0.0296  0.0242  240 ARG B CG  
4205  C  CD  . ARG B  240 ? 0.1804 0.2206 0.2174 -0.0177 0.0089  0.0031  240 ARG B CD  
4206  N  NE  . ARG B  240 ? 0.2572 0.2705 0.2373 0.0120  0.0795  0.0758  240 ARG B NE  
4207  C  CZ  . ARG B  240 ? 0.1926 0.2323 0.2477 -0.0013 0.0428  0.0344  240 ARG B CZ  
4208  N  NH1 . ARG B  240 ? 0.2443 0.2052 0.2237 -0.0261 0.0381  0.0320  240 ARG B NH1 
4209  N  NH2 . ARG B  240 ? 0.2606 0.2684 0.3388 0.0386  0.0857  0.0285  240 ARG B NH2 
4210  N  N   . GLU B  241 ? 0.1883 0.1186 0.1615 0.0049  0.0560  0.0627  241 GLU B N   
4211  C  CA  . GLU B  241 ? 0.2337 0.1172 0.1371 -0.0142 0.0482  0.0516  241 GLU B CA  
4212  C  C   . GLU B  241 ? 0.1817 0.1259 0.1368 0.0032  0.0487  0.0511  241 GLU B C   
4213  O  O   . GLU B  241 ? 0.1867 0.1342 0.1596 -0.0239 0.0443  0.0577  241 GLU B O   
4214  C  CB  . GLU B  241 ? 0.2734 0.1186 0.1719 0.0107  0.0932  0.0667  241 GLU B CB  
4215  C  CG  . GLU B  241 ? 0.3106 0.1590 0.1297 0.0329  0.0662  0.0661  241 GLU B CG  
4216  C  CD  . GLU B  241 ? 0.3221 0.2691 0.2484 0.0953  0.0458  0.0337  241 GLU B CD  
4217  O  OE1 . GLU B  241 ? 0.4002 0.5331 0.2723 0.1753  -0.0132 -0.0564 241 GLU B OE1 
4218  O  OE2 . GLU B  241 ? 0.3368 0.4586 0.3555 0.1615  -0.0405 -0.1411 241 GLU B OE2 
4219  N  N   . MET B  242 ? 0.1653 0.1246 0.1310 0.0035  0.0436  0.0693  242 MET B N   
4220  C  CA  . MET B  242 ? 0.1879 0.1206 0.1507 -0.0030 0.0340  0.0725  242 MET B CA  
4221  C  C   . MET B  242 ? 0.1597 0.1154 0.1030 0.0081  0.0584  0.0421  242 MET B C   
4222  O  O   . MET B  242 ? 0.1655 0.1150 0.1231 -0.0098 0.0507  0.0454  242 MET B O   
4223  C  CB  . MET B  242 ? 0.1556 0.1240 0.1340 0.0126  0.0498  0.0529  242 MET B CB  
4224  C  CG  . MET B  242 ? 0.1756 0.1473 0.1233 0.0030  0.0063  0.0370  242 MET B CG  
4225  S  SD  . MET B  242 ? 0.1692 0.1262 0.1450 -0.0013 0.0443  0.0434  242 MET B SD  
4226  C  CE  . MET B  242 ? 0.2168 0.1010 0.2244 -0.0087 0.0307  0.0524  242 MET B CE  
4227  N  N   . ILE B  243 ? 0.1657 0.0979 0.1094 0.0160  0.0584  0.0399  243 ILE B N   
4228  C  CA  . ILE B  243 ? 0.1412 0.1015 0.1089 0.0212  0.0405  0.0357  243 ILE B CA  
4229  C  C   . ILE B  243 ? 0.1073 0.0924 0.1341 0.0073  0.0579  0.0353  243 ILE B C   
4230  O  O   . ILE B  243 ? 0.1299 0.1048 0.1337 0.0068  0.0746  0.0291  243 ILE B O   
4231  C  CB  . ILE B  243 ? 0.1587 0.1427 0.1159 0.0083  0.0678  0.0276  243 ILE B CB  
4232  C  CG1 . ILE B  243 ? 0.2238 0.1477 0.1657 -0.0296 0.1230  0.0146  243 ILE B CG1 
4233  C  CG2 . ILE B  243 ? 0.2524 0.1590 0.1015 0.0255  0.0256  0.0176  243 ILE B CG2 
4234  C  CD1 . ILE B  243 ? 0.2120 0.2156 0.1676 0.0019  0.1194  0.0263  243 ILE B CD1 
4235  N  N   . ASN B  244 ? 0.1044 0.1080 0.1064 0.0222  0.0480  0.0331  244 ASN B N   
4236  C  CA  . ASN B  244 ? 0.0909 0.0821 0.1297 0.0153  0.0631  0.0253  244 ASN B CA  
4237  C  C   . ASN B  244 ? 0.0973 0.0881 0.1089 -0.0006 0.0474  0.0326  244 ASN B C   
4238  O  O   . ASN B  244 ? 0.0885 0.1088 0.1402 0.0021  0.0373  0.0188  244 ASN B O   
4239  C  CB  . ASN B  244 ? 0.0872 0.1190 0.1933 0.0241  0.0724  0.0263  244 ASN B CB  
4240  C  CG  . ASN B  244 ? 0.0924 0.1450 0.2333 0.0127  0.0782  -0.0102 244 ASN B CG  
4241  O  OD1 . ASN B  244 ? 0.1247 0.1511 0.2197 0.0197  0.0746  0.0054  244 ASN B OD1 
4242  N  ND2 . ASN B  244 ? 0.1745 0.1947 0.2748 0.0209  0.1720  -0.0104 244 ASN B ND2 
4243  N  N   . ASN B  245 ? 0.0901 0.0892 0.0967 0.0102  0.0571  0.0320  245 ASN B N   
4244  C  CA  . ASN B  245 ? 0.0888 0.0870 0.0910 0.0118  0.0405  0.0174  245 ASN B CA  
4245  C  C   . ASN B  245 ? 0.0798 0.0790 0.0863 0.0054  0.0399  0.0131  245 ASN B C   
4246  O  O   . ASN B  245 ? 0.0856 0.1429 0.1098 0.0137  0.0463  0.0370  245 ASN B O   
4247  C  CB  . ASN B  245 ? 0.1170 0.0802 0.0964 -0.0049 0.0353  0.0335  245 ASN B CB  
4248  C  CG  . ASN B  245 ? 0.1032 0.0791 0.0863 0.0046  0.0248  0.0291  245 ASN B CG  
4249  O  OD1 . ASN B  245 ? 0.1076 0.0778 0.1533 -0.0076 0.0359  0.0432  245 ASN B OD1 
4250  N  ND2 . ASN B  245 ? 0.1023 0.1159 0.1513 0.0097  0.0070  -0.0124 245 ASN B ND2 
4251  N  N   . PHE B  246 ? 0.0751 0.0877 0.1048 -0.0041 0.0249  0.0251  246 PHE B N   
4252  C  CA  . PHE B  246 ? 0.1001 0.0788 0.0985 -0.0210 0.0247  0.0237  246 PHE B CA  
4253  C  C   . PHE B  246 ? 0.0892 0.0748 0.1173 0.0005  0.0226  0.0253  246 PHE B C   
4254  O  O   . PHE B  246 ? 0.0705 0.0994 0.1238 -0.0073 0.0244  0.0243  246 PHE B O   
4255  C  CB  . PHE B  246 ? 0.1127 0.0654 0.1154 -0.0041 0.0447  0.0129  246 PHE B CB  
4256  C  CG  . PHE B  246 ? 0.0996 0.0675 0.1301 -0.0071 0.0231  0.0281  246 PHE B CG  
4257  C  CD1 . PHE B  246 ? 0.1256 0.0733 0.1387 -0.0030 0.0496  0.0233  246 PHE B CD1 
4258  C  CD2 . PHE B  246 ? 0.1351 0.0881 0.1303 -0.0031 0.0196  0.0197  246 PHE B CD2 
4259  C  CE1 . PHE B  246 ? 0.1159 0.0649 0.1592 -0.0043 0.0300  0.0130  246 PHE B CE1 
4260  C  CE2 . PHE B  246 ? 0.1235 0.1088 0.1535 0.0108  0.0024  0.0000  246 PHE B CE2 
4261  C  CZ  . PHE B  246 ? 0.1332 0.1421 0.1353 -0.0176 0.0204  0.0210  246 PHE B CZ  
4262  N  N   . ARG B  247 ? 0.0883 0.0707 0.0996 -0.0062 0.0151  0.0249  247 ARG B N   
4263  C  CA  . ARG B  247 ? 0.0895 0.0745 0.1062 -0.0065 0.0215  0.0185  247 ARG B CA  
4264  C  C   . ARG B  247 ? 0.0952 0.0674 0.0904 -0.0049 0.0137  0.0240  247 ARG B C   
4265  O  O   . ARG B  247 ? 0.0881 0.0656 0.1306 0.0000  0.0230  0.0247  247 ARG B O   
4266  C  CB  . ARG B  247 ? 0.0879 0.1012 0.1036 -0.0155 0.0207  0.0120  247 ARG B CB  
4267  C  CG  . ARG B  247 ? 0.0933 0.0714 0.1163 -0.0057 0.0157  0.0060  247 ARG B CG  
4268  C  CD  . ARG B  247 ? 0.0992 0.0707 0.1182 -0.0021 0.0132  0.0098  247 ARG B CD  
4269  N  NE  . ARG B  247 ? 0.1109 0.0798 0.1085 0.0012  -0.0063 0.0087  247 ARG B NE  
4270  C  CZ  . ARG B  247 ? 0.1044 0.0520 0.1012 -0.0020 -0.0020 0.0118  247 ARG B CZ  
4271  N  NH1 . ARG B  247 ? 0.1143 0.0917 0.1468 0.0043  0.0203  0.0189  247 ARG B NH1 
4272  N  NH2 . ARG B  247 ? 0.1242 0.0660 0.1395 -0.0104 -0.0052 0.0083  247 ARG B NH2 
4273  N  N   . GLN B  248 ? 0.0876 0.0813 0.1000 0.0012  0.0168  0.0157  248 GLN B N   
4274  C  CA  . GLN B  248 ? 0.0703 0.1003 0.1032 0.0005  0.0159  0.0361  248 GLN B CA  
4275  C  C   . GLN B  248 ? 0.0843 0.0705 0.1100 -0.0088 0.0049  0.0168  248 GLN B C   
4276  O  O   . GLN B  248 ? 0.1008 0.0748 0.1107 -0.0024 0.0210  0.0227  248 GLN B O   
4277  C  CB  . GLN B  248 ? 0.0843 0.0848 0.1124 -0.0051 0.0286  0.0234  248 GLN B CB  
4278  C  CG  . GLN B  248 ? 0.1003 0.0888 0.1073 -0.0035 0.0322  0.0164  248 GLN B CG  
4279  C  CD  . GLN B  248 ? 0.0856 0.1058 0.0962 -0.0048 0.0210  0.0298  248 GLN B CD  
4280  O  OE1 . GLN B  248 ? 0.1039 0.0944 0.1159 0.0052  0.0131  0.0153  248 GLN B OE1 
4281  N  NE2 . GLN B  248 ? 0.1058 0.1188 0.1244 0.0250  0.0034  0.0251  248 GLN B NE2 
4282  N  N   . VAL B  249 ? 0.0827 0.0899 0.0913 -0.0115 0.0182  0.0306  249 VAL B N   
4283  C  CA  . VAL B  249 ? 0.1052 0.0762 0.0994 -0.0037 0.0082  0.0251  249 VAL B CA  
4284  C  C   . VAL B  249 ? 0.0897 0.0755 0.1085 -0.0057 0.0110  0.0296  249 VAL B C   
4285  O  O   . VAL B  249 ? 0.0917 0.0917 0.1297 -0.0040 0.0148  0.0234  249 VAL B O   
4286  C  CB  . VAL B  249 ? 0.1125 0.0775 0.1306 -0.0089 0.0049  0.0297  249 VAL B CB  
4287  C  CG1 . VAL B  249 ? 0.1195 0.0960 0.1411 -0.0258 0.0103  0.0261  249 VAL B CG1 
4288  C  CG2 . VAL B  249 ? 0.1292 0.0746 0.1786 0.0129  -0.0087 0.0267  249 VAL B CG2 
4289  N  N   . GLN B  250 ? 0.0989 0.0838 0.1077 -0.0091 0.0094  0.0188  250 GLN B N   
4290  C  CA  . GLN B  250 ? 0.1068 0.0906 0.1023 0.0115  0.0043  0.0136  250 GLN B CA  
4291  C  C   . GLN B  250 ? 0.1035 0.1026 0.1027 -0.0073 0.0164  0.0320  250 GLN B C   
4292  O  O   . GLN B  250 ? 0.1552 0.0951 0.1366 -0.0207 0.0098  0.0351  250 GLN B O   
4293  C  CB  . GLN B  250 ? 0.1084 0.0917 0.1163 0.0017  0.0185  0.0089  250 GLN B CB  
4294  C  CG  . GLN B  250 ? 0.0985 0.0766 0.1513 -0.0063 -0.0027 0.0339  250 GLN B CG  
4295  C  CD  . GLN B  250 ? 0.0942 0.0755 0.1441 -0.0007 0.0030  0.0088  250 GLN B CD  
4296  O  OE1 . GLN B  250 ? 0.1184 0.0945 0.1423 -0.0153 0.0129  0.0125  250 GLN B OE1 
4297  N  NE2 . GLN B  250 ? 0.1093 0.0784 0.1456 0.0044  0.0154  0.0252  250 GLN B NE2 
4298  N  N   . LYS B  251 ? 0.1009 0.1315 0.1150 0.0104  0.0003  0.0172  251 LYS B N   
4299  C  CA  . LYS B  251 ? 0.1168 0.1405 0.1121 0.0109  0.0074  0.0089  251 LYS B CA  
4300  C  C   . LYS B  251 ? 0.1216 0.1387 0.1231 0.0165  0.0157  0.0219  251 LYS B C   
4301  O  O   . LYS B  251 ? 0.1330 0.1299 0.1391 0.0116  0.0170  0.0294  251 LYS B O   
4302  C  CB  . LYS B  251 ? 0.1055 0.1825 0.1418 -0.0108 0.0086  0.0000  251 LYS B CB  
4303  C  CG  . LYS B  251 ? 0.1402 0.2770 0.1500 0.0450  0.0487  0.0078  251 LYS B CG  
4304  C  CD  . LYS B  251 ? 0.1174 0.3980 0.1509 0.0698  0.0256  0.0441  251 LYS B CD  
4305  C  CE  . LYS B  251 ? 0.1179 0.2321 0.1289 0.0223  0.0034  0.0156  251 LYS B CE  
4306  N  NZ  . LYS B  251 ? 0.1226 0.1400 0.1102 0.0046  0.0052  0.0219  251 LYS B NZ  
4307  N  N   . PHE B  252 ? 0.1317 0.1622 0.1242 0.0080  0.0082  0.0300  252 PHE B N   
4308  C  CA  . PHE B  252 ? 0.1567 0.1552 0.1520 -0.0125 0.0306  0.0582  252 PHE B CA  
4309  C  C   . PHE B  252 ? 0.2427 0.3222 0.2782 -0.0425 0.0425  0.1820  252 PHE B C   
4310  O  O   . PHE B  252 ? 0.2917 0.4268 0.2590 -0.0434 0.0533  0.1638  252 PHE B O   
4311  C  CB  . PHE B  252 ? 0.2276 0.1949 0.2000 -0.0529 0.0830  -0.0131 252 PHE B CB  
4312  C  CG  . PHE B  252 ? 0.1844 0.2606 0.1532 -0.0878 0.0126  0.0215  252 PHE B CG  
4313  C  CD1 . PHE B  252 ? 0.1752 0.3186 0.1678 -0.0294 -0.0308 0.0057  252 PHE B CD1 
4314  C  CD2 . PHE B  252 ? 0.2266 0.2922 0.1917 -0.1033 -0.0012 0.0326  252 PHE B CD2 
4315  C  CE1 . PHE B  252 ? 0.1752 0.4253 0.2319 -0.0939 -0.0296 0.0632  252 PHE B CE1 
4316  C  CE2 . PHE B  252 ? 0.2154 0.3752 0.2113 -0.1466 -0.0046 0.0746  252 PHE B CE2 
4317  C  CZ  . PHE B  252 ? 0.2556 0.4074 0.2184 -0.0987 -0.0116 0.0614  252 PHE B CZ  
4318  N  N   . ASP B  253 ? 0.4788 0.6589 0.2102 0.0065  -0.0307 -0.1828 253 ASP B N   
4319  C  CA  . ASP B  253 ? 0.5174 0.6431 0.3332 -0.1190 -0.0820 -0.2080 253 ASP B CA  
4320  C  C   . ASP B  253 ? 0.5562 0.9860 0.3341 -0.2863 0.0430  -0.2405 253 ASP B C   
4321  O  O   . ASP B  253 ? 0.5224 1.0806 0.2897 -0.2646 0.0120  -0.0964 253 ASP B O   
4322  C  CB  . ASP B  253 ? 0.4557 1.0292 0.2190 -0.1494 0.0910  -0.0847 253 ASP B CB  
4323  C  CG  . ASP B  253 ? 1.0565 1.2384 1.0549 -0.1022 0.0936  -0.0518 253 ASP B CG  
4324  O  OD1 . ASP B  253 ? 1.0536 1.2575 1.0197 0.1693  0.0988  -0.1391 253 ASP B OD1 
4325  O  OD2 . ASP B  253 ? 1.3739 1.8938 1.1933 -0.1259 -0.2328 0.0255  253 ASP B OD2 
4326  N  N   . GLU B  254 ? 0.7114 0.9707 0.4079 -0.4537 -0.0241 -0.2031 254 GLU B N   
4327  C  CA  . GLU B  254 ? 0.6493 1.1532 0.6590 -0.4153 -0.0478 -0.3294 254 GLU B CA  
4328  C  C   . GLU B  254 ? 0.5643 1.1151 0.7005 -0.3634 -0.0386 -0.1123 254 GLU B C   
4329  O  O   . GLU B  254 ? 0.9326 0.9301 0.7383 -0.2883 -0.0020 0.3188  254 GLU B O   
4330  N  N   . ARG B  255 ? 0.5065 0.5940 0.7014 -0.3339 0.0059  0.0513  255 ARG B N   
4331  C  CA  . ARG B  255 ? 0.3889 0.2585 0.2879 0.0221  -0.0987 -0.0555 255 ARG B CA  
4332  C  C   . ARG B  255 ? 0.2982 0.3429 0.5152 -0.0063 0.0494  -0.0842 255 ARG B C   
4333  O  O   . ARG B  255 ? 0.2605 0.3165 0.4219 -0.0384 -0.0307 -0.0970 255 ARG B O   
4334  C  CB  . ARG B  255 ? 0.4302 0.3237 0.2960 -0.0160 -0.0019 0.0656  255 ARG B CB  
4335  C  CG  . ARG B  255 ? 0.3145 0.3501 0.2213 -0.0263 0.0041  0.0864  255 ARG B CG  
4336  C  CD  . ARG B  255 ? 0.3526 0.3722 0.2016 0.0597  -0.0724 0.0271  255 ARG B CD  
4337  N  NE  . ARG B  255 ? 0.7746 0.6287 0.3506 0.2615  0.2208  0.1674  255 ARG B NE  
4338  C  CZ  . ARG B  255 ? 0.2253 0.4716 0.3657 0.0606  -0.0408 -0.0157 255 ARG B CZ  
4339  N  NH1 . ARG B  255 ? 0.2594 0.1660 0.2476 -0.0020 -0.0777 0.0260  255 ARG B NH1 
4340  N  NH2 . ARG B  255 ? 0.2477 0.2190 0.1772 0.1319  -0.0417 -0.0005 255 ARG B NH2 
4341  N  N   . LEU B  256 ? 0.3088 0.4541 0.3404 -0.0584 -0.0142 -0.1368 256 LEU B N   
4342  C  CA  . LEU B  256 ? 0.1942 0.3186 0.3231 0.0671  -0.0361 -0.0357 256 LEU B CA  
4343  C  C   . LEU B  256 ? 0.2975 0.2542 0.1953 -0.0771 -0.0784 0.0296  256 LEU B C   
4344  O  O   . LEU B  256 ? 0.3409 0.2197 0.2594 -0.0816 -0.0745 -0.0020 256 LEU B O   
4345  C  CB  . LEU B  256 ? 0.3912 0.3944 0.3767 0.0416  -0.1283 -0.0533 256 LEU B CB  
4346  C  CG  . LEU B  256 ? 0.4724 0.1962 0.3858 0.1133  -0.1881 -0.0164 256 LEU B CG  
4347  C  CD1 . LEU B  256 ? 0.5487 0.3379 0.4946 -0.0781 -0.2236 -0.0082 256 LEU B CD1 
4348  C  CD2 . LEU B  256 ? 0.4433 0.4643 0.2265 0.2245  -0.1270 0.0483  256 LEU B CD2 
4349  N  N   . VAL B  257 ? 0.1772 0.2254 0.1504 -0.0535 -0.0276 0.0676  257 VAL B N   
4350  C  CA  . VAL B  257 ? 0.1453 0.1660 0.1129 -0.0333 -0.0093 0.0423  257 VAL B CA  
4351  C  C   . VAL B  257 ? 0.1235 0.1540 0.1023 -0.0089 -0.0065 0.0511  257 VAL B C   
4352  O  O   . VAL B  257 ? 0.1398 0.1833 0.1520 0.0160  0.0193  0.0839  257 VAL B O   
4353  C  CB  . VAL B  257 ? 0.1186 0.1674 0.1493 -0.0020 0.0295  0.0610  257 VAL B CB  
4354  C  CG1 . VAL B  257 ? 0.1294 0.2020 0.1441 0.0046  0.0082  0.0353  257 VAL B CG1 
4355  C  CG2 . VAL B  257 ? 0.1495 0.1800 0.1757 -0.0302 0.0359  0.0698  257 VAL B CG2 
4356  N  N   . TYR B  258 ? 0.1116 0.1624 0.1068 -0.0109 0.0137  0.0340  258 TYR B N   
4357  C  CA  . TYR B  258 ? 0.1332 0.1692 0.1082 -0.0054 0.0251  0.0395  258 TYR B CA  
4358  C  C   . TYR B  258 ? 0.1254 0.1560 0.0929 0.0071  0.0178  0.0533  258 TYR B C   
4359  O  O   . TYR B  258 ? 0.1637 0.1594 0.1127 -0.0148 -0.0161 0.0631  258 TYR B O   
4360  C  CB  . TYR B  258 ? 0.1592 0.2393 0.1109 0.0149  0.0240  0.0116  258 TYR B CB  
4361  C  CG  . TYR B  258 ? 0.2026 0.2425 0.1383 0.0160  0.0247  0.0296  258 TYR B CG  
4362  C  CD1 . TYR B  258 ? 0.2867 0.2903 0.1243 -0.0144 -0.0292 0.0278  258 TYR B CD1 
4363  C  CD2 . TYR B  258 ? 0.2651 0.2001 0.1923 0.0068  -0.0414 0.0109  258 TYR B CD2 
4364  C  CE1 . TYR B  258 ? 0.3321 0.2894 0.2003 -0.0073 -0.0087 -0.0635 258 TYR B CE1 
4365  C  CE2 . TYR B  258 ? 0.3068 0.3043 0.1746 -0.0551 -0.0283 0.0034  258 TYR B CE2 
4366  C  CZ  . TYR B  258 ? 0.3666 0.2890 0.1716 -0.0299 -0.0781 -0.0313 258 TYR B CZ  
4367  O  OH  . TYR B  258 ? 0.4780 0.3416 0.2847 -0.0715 -0.1255 -0.0676 258 TYR B OH  
4368  N  N   . THR B  259 ? 0.1314 0.1283 0.1006 -0.0017 0.0277  0.0348  259 THR B N   
4369  C  CA  . THR B  259 ? 0.1174 0.1385 0.1010 0.0000  0.0313  0.0465  259 THR B CA  
4370  C  C   . THR B  259 ? 0.1154 0.1450 0.0850 0.0074  0.0282  0.0447  259 THR B C   
4371  O  O   . THR B  259 ? 0.1242 0.1978 0.0848 0.0115  0.0250  0.0553  259 THR B O   
4372  C  CB  . THR B  259 ? 0.1197 0.1646 0.1062 0.0142  0.0449  0.0597  259 THR B CB  
4373  O  OG1 . THR B  259 ? 0.1233 0.1863 0.1524 0.0410  0.0384  0.0807  259 THR B OG1 
4374  C  CG2 . THR B  259 ? 0.1156 0.2132 0.1323 0.0129  0.0617  0.0559  259 THR B CG2 
4375  N  N   . SER B  260 ? 0.1055 0.1509 0.0873 0.0129  0.0320  0.0355  260 SER B N   
4376  C  CA  . SER B  260 ? 0.0958 0.1486 0.1498 0.0098  0.0333  0.0529  260 SER B CA  
4377  C  C   . SER B  260 ? 0.1044 0.1606 0.1263 0.0000  0.0320  0.0463  260 SER B C   
4378  O  O   . SER B  260 ? 0.1556 0.2009 0.1901 -0.0082 0.0577  0.0820  260 SER B O   
4379  C  CB  . SER B  260 ? 0.1000 0.1832 0.1046 0.0071  0.0388  0.0324  260 SER B CB  
4380  O  OG  . SER B  260 ? 0.1132 0.1637 0.1055 0.0000  0.0458  0.0469  260 SER B OG  
4381  N  N   . PHE B  261 ? 0.1367 0.1317 0.1136 0.0124  0.0368  0.0461  261 PHE B N   
4382  C  CA  . PHE B  261 ? 0.1279 0.1495 0.1401 0.0225  0.0247  0.0397  261 PHE B CA  
4383  C  C   . PHE B  261 ? 0.1529 0.1502 0.1396 0.0125  0.0285  0.0711  261 PHE B C   
4384  O  O   . PHE B  261 ? 0.1586 0.1430 0.1583 -0.0017 0.0318  0.0763  261 PHE B O   
4385  C  CB  . PHE B  261 ? 0.1574 0.1580 0.1314 -0.0137 0.0394  0.0516  261 PHE B CB  
4386  C  CG  . PHE B  261 ? 0.1543 0.1204 0.1529 -0.0147 0.0297  0.0590  261 PHE B CG  
4387  C  CD1 . PHE B  261 ? 0.1797 0.1220 0.1132 0.0031  0.0293  0.0375  261 PHE B CD1 
4388  C  CD2 . PHE B  261 ? 0.1777 0.2000 0.1368 0.0337  0.0562  0.0531  261 PHE B CD2 
4389  C  CE1 . PHE B  261 ? 0.1838 0.1579 0.1150 0.0044  0.0348  0.0340  261 PHE B CE1 
4390  C  CE2 . PHE B  261 ? 0.1818 0.2231 0.1163 0.0300  0.0366  0.0527  261 PHE B CE2 
4391  C  CZ  . PHE B  261 ? 0.1635 0.1987 0.1391 -0.0093 0.0189  0.0516  261 PHE B CZ  
4392  N  N   . SER B  262 ? 0.2486 0.1443 0.1727 -0.0302 -0.0013 0.0819  262 SER B N   
4393  C  CA  . SER B  262 ? 0.2788 0.1944 0.1714 0.0017  0.0110  0.0559  262 SER B CA  
4394  C  C   . SER B  262 ? 0.4194 0.3495 0.2885 0.0242  0.1111  -0.1587 262 SER B C   
4395  O  O   . SER B  262 ? 0.8222 0.1911 0.2856 -0.1212 -0.2081 0.0788  262 SER B O   
4396  C  CB  . SER B  262 ? 0.2436 0.5092 0.5692 -0.0113 -0.0489 0.4578  262 SER B CB  
4397  O  OG  . SER B  262 ? 0.7299 0.3312 0.5594 -0.2012 -0.1673 0.1484  262 SER B OG  
4398  N  N   . GLN B  263 ? 0.4183 0.4931 0.3176 0.3063  -0.1429 -0.1323 263 GLN B N   
4399  C  CA  . GLN B  263 ? 0.6836 0.4178 0.3495 0.2404  0.1229  0.0223  263 GLN B CA  
4400  C  C   . GLN B  263 ? 0.6003 0.6927 0.7174 0.2282  -0.2364 0.1567  263 GLN B C   
4401  O  O   . GLN B  263 ? 0.5036 0.7477 0.7680 0.1890  0.1525  0.4086  263 GLN B O   
4402  C  CB  . GLN B  263 ? 0.6819 0.6252 0.6075 0.1208  0.1451  0.2129  263 GLN B CB  
4403  C  CG  . GLN B  263 ? 0.8668 1.1952 0.8439 -0.1354 0.1846  0.3291  263 GLN B CG  
4404  C  CD  . GLN B  263 ? 1.8963 0.6294 1.1848 0.4523  -0.2480 0.1776  263 GLN B CD  
4405  O  OE1 . GLN B  263 ? 0.4386 0.8730 0.5052 -0.0306 0.1110  -0.1562 263 GLN B OE1 
4406  N  NE2 . GLN B  263 ? 3.9871 1.1773 0.6407 -1.9970 1.3619  -0.5403 263 GLN B NE2 
4407  O  OXT . GLN B  263 ? 0.4316 0.2362 0.2095 0.0060  0.0390  0.0608  263 GLN B OXT 
4408  N  N   . SER C  2   ? 1.0331 1.0130 0.4426 0.0560  -0.3107 -0.2768 2   SER C N   
4409  C  CA  . SER C  2   ? 0.9121 0.7807 0.9247 -0.1272 -0.0573 -0.0741 2   SER C CA  
4410  C  C   . SER C  2   ? 0.7099 1.0226 0.4658 -0.1904 0.0108  -0.3950 2   SER C C   
4411  O  O   . SER C  2   ? 0.6086 0.6453 0.2802 -0.0125 0.0097  -0.1682 2   SER C O   
4412  C  CB  . SER C  2   ? 1.2659 1.7587 0.6405 0.1917  -0.4264 -0.3558 2   SER C CB  
4413  O  OG  . SER C  2   ? 0.9186 1.6569 0.8025 0.0077  -0.5580 -0.3555 2   SER C OG  
4414  N  N   . LYS C  3   ? 0.8791 0.7692 0.6622 -0.3679 0.0148  -0.4063 3   LYS C N   
4415  C  CA  . LYS C  3   ? 0.8877 0.4260 0.8271 -0.2660 0.0615  -0.3341 3   LYS C CA  
4416  C  C   . LYS C  3   ? 0.5015 0.4027 0.8292 0.0454  0.0995  -0.4208 3   LYS C C   
4417  O  O   . LYS C  3   ? 0.6920 0.6484 0.6754 -0.1036 0.1805  -0.3903 3   LYS C O   
4418  C  CB  . LYS C  3   ? 0.8612 0.6212 0.5665 -0.2088 0.2544  -0.4041 3   LYS C CB  
4419  N  N   . TRP C  4   ? 0.4092 0.3036 0.1838 -0.0630 -0.0164 -0.1199 4   TRP C N   
4420  C  CA  . TRP C  4   ? 0.3337 0.2406 0.1744 -0.0780 0.0259  -0.0820 4   TRP C CA  
4421  C  C   . TRP C  4   ? 0.2935 0.2513 0.1477 -0.0390 -0.0012 -0.1076 4   TRP C C   
4422  O  O   . TRP C  4   ? 0.3436 0.3300 0.1583 -0.0324 -0.0153 -0.1242 4   TRP C O   
4423  C  CB  . TRP C  4   ? 0.2797 0.2169 0.1454 -0.0588 0.0089  -0.0493 4   TRP C CB  
4424  C  CG  . TRP C  4   ? 0.2465 0.2075 0.1491 -0.0659 0.0003  -0.0405 4   TRP C CG  
4425  C  CD1 . TRP C  4   ? 0.2820 0.2046 0.1717 -0.0878 0.0348  -0.0392 4   TRP C CD1 
4426  C  CD2 . TRP C  4   ? 0.2479 0.2046 0.1299 -0.0549 -0.0238 -0.0403 4   TRP C CD2 
4427  N  NE1 . TRP C  4   ? 0.2741 0.2458 0.1644 -0.0718 0.0092  -0.0778 4   TRP C NE1 
4428  C  CE2 . TRP C  4   ? 0.2863 0.2649 0.1233 -0.0635 -0.0270 -0.0676 4   TRP C CE2 
4429  C  CE3 . TRP C  4   ? 0.2395 0.1877 0.1290 -0.0386 0.0074  -0.0645 4   TRP C CE3 
4430  C  CZ2 . TRP C  4   ? 0.2732 0.2657 0.1471 -0.0258 -0.0140 -0.0684 4   TRP C CZ2 
4431  C  CZ3 . TRP C  4   ? 0.2712 0.2117 0.1100 -0.0017 0.0060  -0.0665 4   TRP C CZ3 
4432  C  CH2 . TRP C  4   ? 0.2804 0.2423 0.1356 0.0032  0.0216  -0.0854 4   TRP C CH2 
4433  N  N   . THR C  5   ? 0.2910 0.2172 0.1606 -0.0443 0.0271  -0.0907 5   THR C N   
4434  C  CA  . THR C  5   ? 0.3068 0.2245 0.1141 0.0070  0.0037  -0.0535 5   THR C CA  
4435  C  C   . THR C  5   ? 0.2287 0.2290 0.1315 -0.0070 0.0476  -0.0573 5   THR C C   
4436  O  O   . THR C  5   ? 0.2632 0.2520 0.1184 -0.0060 0.0188  -0.0489 5   THR C O   
4437  C  CB  . THR C  5   ? 0.3925 0.3840 0.1863 0.0000  0.0302  -0.1808 5   THR C CB  
4438  O  OG1 . THR C  5   ? 0.3380 0.3244 0.2008 -0.0390 0.0496  -0.1115 5   THR C OG1 
4439  C  CG2 . THR C  5   ? 0.3792 0.3476 0.2030 -0.0153 0.0542  -0.1263 5   THR C CG2 
4440  N  N   . TYR C  6   ? 0.3790 0.2346 0.1186 -0.0274 0.0278  -0.0544 6   TYR C N   
4441  C  CA  . TYR C  6   ? 0.4223 0.2335 0.1324 -0.0604 0.0368  -0.0661 6   TYR C CA  
4442  C  C   . TYR C  6   ? 0.3808 0.2391 0.1908 0.0124  0.0087  -0.0306 6   TYR C C   
4443  O  O   . TYR C  6   ? 0.4334 0.3063 0.1364 -0.0662 -0.0068 -0.0350 6   TYR C O   
4444  C  CB  . TYR C  6   ? 0.3621 0.2486 0.1669 -0.0793 0.1076  -0.0397 6   TYR C CB  
4445  C  CG  . TYR C  6   ? 0.3400 0.2409 0.1299 -0.0854 0.0780  -0.0728 6   TYR C CG  
4446  C  CD1 . TYR C  6   ? 0.3499 0.1996 0.1082 -0.0815 0.0449  -0.0272 6   TYR C CD1 
4447  C  CD2 . TYR C  6   ? 0.2806 0.1791 0.1287 -0.0137 0.0405  -0.0326 6   TYR C CD2 
4448  C  CE1 . TYR C  6   ? 0.3012 0.2666 0.1080 -0.0839 0.0248  -0.0166 6   TYR C CE1 
4449  C  CE2 . TYR C  6   ? 0.2438 0.2021 0.1188 -0.0406 0.0353  -0.0185 6   TYR C CE2 
4450  C  CZ  . TYR C  6   ? 0.2560 0.2409 0.1114 -0.0926 0.0020  -0.0256 6   TYR C CZ  
4451  O  OH  . TYR C  6   ? 0.2490 0.3070 0.1244 -0.1077 0.0010  0.0040  6   TYR C OH  
4452  N  N   . PHE C  7   ? 0.5371 0.3736 0.3036 -0.0469 0.2193  -0.1683 7   PHE C N   
4453  C  CA  . PHE C  7   ? 0.4708 0.6869 0.4185 -0.1353 0.1791  -0.2338 7   PHE C CA  
4454  C  C   . PHE C  7   ? 0.8621 0.5126 0.7519 -0.1202 0.3677  -0.2027 7   PHE C C   
4455  O  O   . PHE C  7   ? 0.5875 0.6571 0.5618 -0.2414 0.3616  -0.3596 7   PHE C O   
4456  C  CB  . PHE C  7   ? 0.9159 1.1432 0.5042 -0.0431 0.6509  0.0265  7   PHE C CB  
4457  N  N   . GLY C  8   ? 0.4982 1.0235 0.3546 -0.2849 -0.0485 -0.0500 8   GLY C N   
4458  C  CA  . GLY C  8   ? 0.3670 0.9408 0.2745 -0.2250 -0.0175 -0.1215 8   GLY C CA  
4459  C  C   . GLY C  8   ? 0.7310 0.6800 0.3540 -0.1513 0.0144  -0.1680 8   GLY C C   
4460  O  O   . GLY C  8   ? 1.2379 1.2525 0.4291 -0.4124 0.1455  -0.3632 8   GLY C O   
4461  N  N   . PRO C  9   ? 0.6161 0.6516 0.4551 0.2002  -0.0162 -0.3556 9   PRO C N   
4462  C  CA  . PRO C  9   ? 0.3589 0.4604 0.5555 0.1074  0.1206  -0.2542 9   PRO C CA  
4463  C  C   . PRO C  9   ? 0.2842 0.3556 0.5058 0.0456  0.0489  -0.1647 9   PRO C C   
4464  O  O   . PRO C  9   ? 0.4004 0.3433 0.4532 0.0390  0.0248  -0.2044 9   PRO C O   
4465  C  CB  . PRO C  9   ? 0.7091 0.4740 0.9443 0.1636  0.1612  -0.3510 9   PRO C CB  
4466  C  CG  . PRO C  9   ? 0.5737 0.8504 0.7167 0.1815  -0.1865 -0.1790 9   PRO C CG  
4467  C  CD  . PRO C  9   ? 0.4020 0.7103 0.4172 0.1005  0.0137  -0.3210 9   PRO C CD  
4468  N  N   . ASP C  10  ? 0.3695 0.3336 0.3050 0.0527  0.0377  -0.1720 10  ASP C N   
4469  C  CA  . ASP C  10  ? 0.3046 0.3106 0.3659 0.0439  0.0167  -0.1976 10  ASP C CA  
4470  C  C   . ASP C  10  ? 0.3646 0.1730 0.2962 -0.0529 0.0348  -0.1387 10  ASP C C   
4471  O  O   . ASP C  10  ? 0.3181 0.3095 0.2502 0.0549  -0.0626 -0.1801 10  ASP C O   
4472  C  CB  . ASP C  10  ? 0.4643 0.3106 0.4523 0.0211  -0.0886 -0.2524 10  ASP C CB  
4473  C  CG  . ASP C  10  ? 0.5850 0.2346 1.2503 0.0066  -0.0144 -0.1106 10  ASP C CG  
4474  O  OD1 . ASP C  10  ? 0.5938 0.3122 0.4680 -0.0498 0.0671  -0.1862 10  ASP C OD1 
4475  O  OD2 . ASP C  10  ? 0.9926 0.7907 3.5148 0.3388  -1.0211 -1.5230 10  ASP C OD2 
4476  N  N   . GLY C  11  ? 0.2964 0.2391 0.2384 -0.0198 0.0193  -0.0988 11  GLY C N   
4477  C  CA  . GLY C  11  ? 0.2804 0.2240 0.1567 0.0194  -0.0144 -0.0604 11  GLY C CA  
4478  C  C   . GLY C  11  ? 0.2299 0.1461 0.1556 -0.0088 -0.0015 -0.0388 11  GLY C C   
4479  O  O   . GLY C  11  ? 0.2102 0.1419 0.1824 -0.0060 0.0012  -0.0685 11  GLY C O   
4480  N  N   . GLU C  12  ? 0.1854 0.1665 0.1495 -0.0186 0.0120  -0.0478 12  GLU C N   
4481  C  CA  . GLU C  12  ? 0.1571 0.1254 0.1340 -0.0031 0.0049  -0.0259 12  GLU C CA  
4482  C  C   . GLU C  12  ? 0.1622 0.0996 0.1526 -0.0085 0.0140  -0.0238 12  GLU C C   
4483  O  O   . GLU C  12  ? 0.1486 0.1244 0.1420 -0.0151 0.0138  -0.0080 12  GLU C O   
4484  C  CB  . GLU C  12  ? 0.1508 0.1283 0.1480 -0.0260 -0.0044 -0.0147 12  GLU C CB  
4485  C  CG  . GLU C  12  ? 0.1624 0.0994 0.1462 -0.0132 0.0271  -0.0355 12  GLU C CG  
4486  C  CD  . GLU C  12  ? 0.1743 0.1165 0.1080 -0.0163 0.0109  -0.0244 12  GLU C CD  
4487  O  OE1 . GLU C  12  ? 0.1696 0.1109 0.1085 -0.0148 0.0243  -0.0132 12  GLU C OE1 
4488  O  OE2 . GLU C  12  ? 0.2442 0.1421 0.1075 -0.0265 0.0015  -0.0216 12  GLU C OE2 
4489  N  N   . ASN C  13  ? 0.1689 0.0842 0.1395 -0.0098 0.0111  -0.0121 13  ASN C N   
4490  C  CA  . ASN C  13  ? 0.1374 0.0850 0.1353 -0.0062 0.0068  0.0020  13  ASN C CA  
4491  C  C   . ASN C  13  ? 0.1649 0.0966 0.1283 -0.0078 0.0159  -0.0324 13  ASN C C   
4492  O  O   . ASN C  13  ? 0.1559 0.0899 0.1689 -0.0065 0.0142  -0.0168 13  ASN C O   
4493  C  CB  . ASN C  13  ? 0.1294 0.0890 0.1632 -0.0103 0.0310  -0.0206 13  ASN C CB  
4494  C  CG  . ASN C  13  ? 0.1337 0.0830 0.1272 0.0082  0.0175  -0.0082 13  ASN C CG  
4495  O  OD1 . ASN C  13  ? 0.1410 0.0815 0.1799 -0.0104 0.0283  -0.0206 13  ASN C OD1 
4496  N  ND2 . ASN C  13  ? 0.1396 0.1141 0.1194 -0.0129 0.0223  -0.0126 13  ASN C ND2 
4497  N  N   A SER C  14  ? 0.1620 0.1046 0.1533 -0.0165 0.0348  -0.0516 14  SER C N   
4498  N  N   B SER C  14  ? 0.1517 0.0732 0.1762 -0.0280 0.0348  -0.0337 14  SER C N   
4499  C  CA  A SER C  14  ? 0.1678 0.0910 0.1748 0.0060  0.0579  -0.0785 14  SER C CA  
4500  C  CA  B SER C  14  ? 0.1933 0.0806 0.1680 -0.0487 0.0324  -0.0239 14  SER C CA  
4501  C  C   A SER C  14  ? 0.1524 0.1049 0.1587 -0.0177 0.0205  -0.0175 14  SER C C   
4502  C  C   B SER C  14  ? 0.1775 0.0924 0.1339 -0.0289 0.0182  -0.0675 14  SER C C   
4503  O  O   A SER C  14  ? 0.1712 0.0901 0.1299 -0.0423 0.0010  -0.0348 14  SER C O   
4504  O  O   B SER C  14  ? 0.1863 0.1053 0.1342 -0.0564 -0.0043 -0.0458 14  SER C O   
4505  C  CB  A SER C  14  ? 0.1829 0.1666 0.1177 0.0051  0.0267  -0.0302 14  SER C CB  
4506  C  CB  B SER C  14  ? 0.2081 0.0931 0.2319 -0.0436 0.0781  -0.0509 14  SER C CB  
4507  O  OG  A SER C  14  ? 0.1687 0.1710 0.1928 -0.0261 0.0870  -0.0675 14  SER C OG  
4508  O  OG  B SER C  14  ? 0.3664 0.1565 0.2222 -0.0119 0.0170  -0.0608 14  SER C OG  
4509  N  N   . TRP C  15  ? 0.1500 0.1271 0.1310 -0.0125 0.0261  -0.0423 15  TRP C N   
4510  C  CA  . TRP C  15  ? 0.1653 0.1033 0.1371 -0.0212 0.0104  -0.0286 15  TRP C CA  
4511  C  C   . TRP C  15  ? 0.1750 0.0895 0.1367 -0.0287 0.0526  -0.0423 15  TRP C C   
4512  O  O   . TRP C  15  ? 0.1691 0.1057 0.1477 -0.0357 0.0294  -0.0157 15  TRP C O   
4513  C  CB  . TRP C  15  ? 0.1761 0.1319 0.1281 -0.0317 0.0531  -0.0109 15  TRP C CB  
4514  C  CG  . TRP C  15  ? 0.1658 0.1158 0.1324 -0.0295 0.0283  -0.0353 15  TRP C CG  
4515  C  CD1 . TRP C  15  ? 0.1883 0.1218 0.1217 -0.0342 0.0203  -0.0115 15  TRP C CD1 
4516  C  CD2 . TRP C  15  ? 0.1611 0.1181 0.1167 -0.0243 0.0049  -0.0244 15  TRP C CD2 
4517  N  NE1 . TRP C  15  ? 0.1816 0.1272 0.1222 -0.0278 0.0126  -0.0500 15  TRP C NE1 
4518  C  CE2 . TRP C  15  ? 0.1403 0.1093 0.1511 -0.0157 0.0057  -0.0307 15  TRP C CE2 
4519  C  CE3 . TRP C  15  ? 0.1728 0.0890 0.1660 -0.0206 0.0196  -0.0465 15  TRP C CE3 
4520  C  CZ2 . TRP C  15  ? 0.1596 0.1317 0.1486 -0.0215 -0.0104 -0.0386 15  TRP C CZ2 
4521  C  CZ3 . TRP C  15  ? 0.1676 0.1156 0.1114 -0.0375 0.0043  -0.0350 15  TRP C CZ3 
4522  C  CH2 . TRP C  15  ? 0.1753 0.1216 0.1400 -0.0344 -0.0089 -0.0160 15  TRP C CH2 
4523  N  N   . SER C  16  ? 0.1750 0.0734 0.1339 -0.0160 0.0313  -0.0286 16  SER C N   
4524  C  CA  . SER C  16  ? 0.1638 0.0951 0.1199 -0.0147 0.0197  -0.0265 16  SER C CA  
4525  C  C   . SER C  16  ? 0.1875 0.0881 0.1165 -0.0296 0.0153  -0.0144 16  SER C C   
4526  O  O   . SER C  16  ? 0.1875 0.0939 0.1547 -0.0237 0.0270  -0.0082 16  SER C O   
4527  C  CB  . SER C  16  ? 0.1543 0.0942 0.1680 -0.0252 0.0249  -0.0280 16  SER C CB  
4528  O  OG  . SER C  16  ? 0.1771 0.1015 0.1793 -0.0244 0.0204  -0.0137 16  SER C OG  
4529  N  N   A LYS C  17  ? 0.1949 0.0979 0.1563 -0.0165 0.0094  -0.0575 17  LYS C N   
4530  N  N   B LYS C  17  ? 0.1748 0.0623 0.1666 0.0003  0.0412  -0.0049 17  LYS C N   
4531  C  CA  A LYS C  17  ? 0.1703 0.1163 0.1807 -0.0098 0.0120  -0.0619 17  LYS C CA  
4532  C  CA  B LYS C  17  ? 0.1872 0.0724 0.1689 -0.0218 0.0487  -0.0271 17  LYS C CA  
4533  C  C   A LYS C  17  ? 0.1755 0.0639 0.1836 -0.0035 0.0138  -0.0266 17  LYS C C   
4534  C  C   B LYS C  17  ? 0.2100 0.0775 0.1536 -0.0318 -0.0031 -0.0274 17  LYS C C   
4535  O  O   A LYS C  17  ? 0.1881 0.0982 0.2264 -0.0148 0.0184  0.0105  17  LYS C O   
4536  O  O   B LYS C  17  ? 0.2266 0.0766 0.2587 -0.0564 -0.0164 0.0088  17  LYS C O   
4537  C  CB  A LYS C  17  ? 0.2328 0.0630 0.2470 0.0149  0.0505  -0.0627 17  LYS C CB  
4538  C  CB  B LYS C  17  ? 0.1938 0.0845 0.1978 -0.0533 0.0706  -0.0253 17  LYS C CB  
4539  C  CG  A LYS C  17  ? 0.2488 0.2883 0.2093 -0.0560 0.0750  -0.1155 17  LYS C CG  
4540  C  CG  B LYS C  17  ? 0.2224 0.1838 0.2581 -0.0706 0.0511  -0.0571 17  LYS C CG  
4541  C  CD  A LYS C  17  ? 0.2693 0.2664 0.1680 0.0252  0.0021  -0.0984 17  LYS C CD  
4542  C  CD  B LYS C  17  ? 0.1998 0.1578 0.2739 -0.0908 0.0627  -0.0242 17  LYS C CD  
4543  C  CE  A LYS C  17  ? 0.3158 0.1725 0.2165 -0.0001 0.0494  -0.0852 17  LYS C CE  
4544  C  CE  B LYS C  17  ? 0.2120 0.1793 0.1892 -0.0164 0.0280  -0.0734 17  LYS C CE  
4545  N  NZ  A LYS C  17  ? 0.2398 0.1542 0.2030 0.0154  0.0474  -0.0286 17  LYS C NZ  
4546  N  NZ  B LYS C  17  ? 0.2131 0.2269 0.1768 0.0384  0.0278  -0.0115 17  LYS C NZ  
4547  N  N   A LYS C  18  ? 0.1863 0.0872 0.1590 -0.0260 0.0116  -0.0277 18  LYS C N   
4548  N  N   B LYS C  18  ? 0.1874 0.0895 0.1606 -0.0245 0.0120  -0.0283 18  LYS C N   
4549  C  CA  A LYS C  18  ? 0.1754 0.1288 0.1680 -0.0212 0.0066  -0.0428 18  LYS C CA  
4550  C  CA  B LYS C  18  ? 0.1768 0.1286 0.1687 -0.0197 0.0068  -0.0368 18  LYS C CA  
4551  C  C   A LYS C  18  ? 0.2050 0.1308 0.1588 -0.0593 0.0535  -0.0491 18  LYS C C   
4552  C  C   B LYS C  18  ? 0.2060 0.1308 0.1620 -0.0599 0.0538  -0.0487 18  LYS C C   
4553  O  O   A LYS C  18  ? 0.2404 0.1213 0.2825 -0.0786 0.1052  -0.0808 18  LYS C O   
4554  O  O   B LYS C  18  ? 0.2405 0.1247 0.2829 -0.0776 0.1054  -0.0833 18  LYS C O   
4555  C  CB  A LYS C  18  ? 0.2363 0.1647 0.1872 0.0057  0.0131  -0.0419 18  LYS C CB  
4556  C  CB  B LYS C  18  ? 0.2337 0.1615 0.1820 0.0092  0.0138  -0.0443 18  LYS C CB  
4557  C  CG  A LYS C  18  ? 0.2163 0.1888 0.3860 -0.0480 -0.0088 -0.1835 18  LYS C CG  
4558  C  CG  B LYS C  18  ? 0.2397 0.1953 0.3598 -0.0186 -0.0184 -0.1049 18  LYS C CG  
4559  C  CD  A LYS C  18  ? 0.3088 0.2687 0.4893 0.1868  -0.0595 -0.1375 18  LYS C CD  
4560  C  CD  B LYS C  18  ? 0.3679 0.2258 0.4059 0.0206  -0.0631 -0.1296 18  LYS C CD  
4561  C  CE  A LYS C  18  ? 0.4862 0.4408 0.2648 0.0333  -0.1247 0.0204  18  LYS C CE  
4562  C  CE  B LYS C  18  ? 0.4266 0.1619 0.4598 -0.0300 -0.1913 0.0126  18  LYS C CE  
4563  N  NZ  A LYS C  18  ? 0.4770 0.3506 0.5195 0.2705  0.0553  0.0397  18  LYS C NZ  
4564  N  NZ  B LYS C  18  ? 0.5927 0.3722 0.4612 0.1172  -0.0588 -0.1289 18  LYS C NZ  
4565  N  N   . TYR C  19  ? 0.1818 0.1045 0.1416 -0.0261 0.0305  -0.0357 19  TYR C N   
4566  C  CA  . TYR C  19  ? 0.1558 0.1030 0.1586 -0.0249 0.0208  -0.0157 19  TYR C CA  
4567  C  C   . TYR C  19  ? 0.1308 0.1018 0.1423 -0.0063 0.0163  -0.0170 19  TYR C C   
4568  O  O   . TYR C  19  ? 0.1750 0.1048 0.1404 -0.0300 0.0315  -0.0298 19  TYR C O   
4569  C  CB  . TYR C  19  ? 0.1850 0.1000 0.1547 -0.0362 0.0162  -0.0260 19  TYR C CB  
4570  C  CG  . TYR C  19  ? 0.2055 0.1106 0.1612 -0.0221 -0.0003 -0.0364 19  TYR C CG  
4571  C  CD1 . TYR C  19  ? 0.1931 0.1168 0.2053 -0.0315 -0.0205 -0.0121 19  TYR C CD1 
4572  C  CD2 . TYR C  19  ? 0.2027 0.1179 0.1565 -0.0149 0.0110  -0.0511 19  TYR C CD2 
4573  C  CE1 . TYR C  19  ? 0.2217 0.1560 0.2240 -0.0474 0.0023  -0.0773 19  TYR C CE1 
4574  C  CE2 . TYR C  19  ? 0.2709 0.1289 0.1811 -0.0522 -0.0190 -0.0271 19  TYR C CE2 
4575  C  CZ  . TYR C  19  ? 0.3063 0.1403 0.1797 -0.0612 -0.0286 -0.0635 19  TYR C CZ  
4576  O  OH  . TYR C  19  ? 0.3851 0.2014 0.2229 -0.0060 -0.0903 -0.0716 19  TYR C OH  
4577  N  N   A PRO C  20  ? 0.1673 0.0698 0.1720 -0.0126 0.0188  -0.0125 20  PRO C N   
4578  N  N   B PRO C  20  ? 0.1687 0.0906 0.1608 -0.0267 0.0505  -0.0131 20  PRO C N   
4579  C  CA  A PRO C  20  ? 0.1518 0.1017 0.1603 -0.0013 0.0215  -0.0263 20  PRO C CA  
4580  C  CA  B PRO C  20  ? 0.1854 0.0935 0.1860 -0.0006 0.0121  -0.0110 20  PRO C CA  
4581  C  C   A PRO C  20  ? 0.1477 0.0791 0.1595 -0.0308 0.0251  -0.0003 20  PRO C C   
4582  C  C   B PRO C  20  ? 0.1556 0.1057 0.1526 -0.0116 0.0417  -0.0048 20  PRO C C   
4583  O  O   A PRO C  20  ? 0.1744 0.0811 0.1822 -0.0522 0.0208  -0.0074 20  PRO C O   
4584  O  O   B PRO C  20  ? 0.1335 0.1120 0.1170 0.0192  0.0340  0.0199  20  PRO C O   
4585  C  CB  A PRO C  20  ? 0.2125 0.0739 0.1791 0.0024  0.0427  -0.0227 20  PRO C CB  
4586  C  CB  B PRO C  20  ? 0.1957 0.0886 0.2117 -0.0211 0.0829  -0.0197 20  PRO C CB  
4587  C  CG  A PRO C  20  ? 0.1667 0.1292 0.1694 -0.0243 0.0049  -0.0220 20  PRO C CG  
4588  C  CG  B PRO C  20  ? 0.2100 0.1156 0.2197 -0.0031 0.0392  0.0408  20  PRO C CG  
4589  C  CD  A PRO C  20  ? 0.1554 0.0818 0.1466 -0.0166 0.0383  -0.0142 20  PRO C CD  
4590  C  CD  B PRO C  20  ? 0.1921 0.0547 0.2169 -0.0077 0.0219  0.0065  20  PRO C CD  
4591  N  N   . SER C  21  ? 0.1527 0.0892 0.1411 -0.0193 0.0276  -0.0048 21  SER C N   
4592  C  CA  . SER C  21  ? 0.1310 0.0892 0.1710 -0.0200 0.0392  -0.0218 21  SER C CA  
4593  C  C   . SER C  21  ? 0.1340 0.0906 0.1107 -0.0107 0.0216  -0.0094 21  SER C C   
4594  O  O   . SER C  21  ? 0.1365 0.0949 0.1313 -0.0127 0.0209  -0.0188 21  SER C O   
4595  C  CB  . SER C  21  ? 0.1536 0.1055 0.1502 -0.0188 0.0414  0.0006  21  SER C CB  
4596  O  OG  . SER C  21  ? 0.1533 0.1274 0.1781 -0.0324 0.0463  -0.0093 21  SER C OG  
4597  N  N   . CYS C  22  ? 0.1348 0.1163 0.1195 -0.0294 0.0307  -0.0083 22  CYS C N   
4598  C  CA  . CYS C  22  ? 0.1364 0.1163 0.1143 -0.0270 0.0329  -0.0046 22  CYS C CA  
4599  C  C   . CYS C  22  ? 0.1145 0.1084 0.1554 -0.0131 0.0304  -0.0148 22  CYS C C   
4600  O  O   . CYS C  22  ? 0.1445 0.0935 0.1392 -0.0261 0.0274  -0.0008 22  CYS C O   
4601  C  CB  . CYS C  22  ? 0.1493 0.1242 0.1193 -0.0226 0.0546  -0.0173 22  CYS C CB  
4602  S  SG  . CYS C  22  ? 0.1653 0.1123 0.1222 -0.0259 0.0256  -0.0296 22  CYS C SG  
4603  N  N   . GLY C  23  ? 0.1488 0.1032 0.1270 -0.0076 0.0186  -0.0024 23  GLY C N   
4604  C  CA  . GLY C  23  ? 0.1481 0.1283 0.1286 -0.0310 0.0282  -0.0031 23  GLY C CA  
4605  C  C   . GLY C  23  ? 0.1477 0.0750 0.1502 -0.0120 0.0200  0.0146  23  GLY C C   
4606  O  O   . GLY C  23  ? 0.1380 0.1247 0.1414 -0.0015 0.0175  0.0032  23  GLY C O   
4607  N  N   . GLY C  24  ? 0.1362 0.1263 0.1444 -0.0052 0.0267  0.0065  24  GLY C N   
4608  C  CA  . GLY C  24  ? 0.1793 0.1270 0.1258 -0.0108 0.0344  0.0000  24  GLY C CA  
4609  C  C   . GLY C  24  ? 0.1759 0.0926 0.1292 -0.0007 -0.0015 0.0205  24  GLY C C   
4610  O  O   . GLY C  24  ? 0.1926 0.1152 0.1418 -0.0322 0.0046  0.0259  24  GLY C O   
4611  N  N   . LEU C  25  ? 0.2061 0.1061 0.1287 0.0043  0.0124  0.0000  25  LEU C N   
4612  C  CA  . LEU C  25  ? 0.2294 0.1071 0.1438 0.0186  0.0013  0.0006  25  LEU C CA  
4613  C  C   . LEU C  25  ? 0.1718 0.0909 0.1152 -0.0103 0.0043  -0.0059 25  LEU C C   
4614  O  O   . LEU C  25  ? 0.1872 0.1070 0.1112 -0.0085 0.0225  -0.0015 25  LEU C O   
4615  C  CB  . LEU C  25  ? 0.2998 0.1526 0.1222 0.0303  0.0310  0.0233  25  LEU C CB  
4616  C  CG  . LEU C  25  ? 0.3346 0.1935 0.1498 0.0340  -0.0245 0.0339  25  LEU C CG  
4617  C  CD1 . LEU C  25  ? 0.5144 0.2205 0.1579 -0.0052 0.0219  0.0675  25  LEU C CD1 
4618  C  CD2 . LEU C  25  ? 0.4359 0.2206 0.3357 -0.0181 -0.1912 0.1216  25  LEU C CD2 
4619  N  N   . LEU C  26  ? 0.2280 0.0940 0.1084 -0.0110 -0.0059 0.0028  26  LEU C N   
4620  C  CA  . LEU C  26  ? 0.1863 0.1046 0.1064 0.0052  0.0043  0.0000  26  LEU C CA  
4621  C  C   . LEU C  26  ? 0.1395 0.0949 0.1023 -0.0185 0.0019  -0.0082 26  LEU C C   
4622  O  O   . LEU C  26  ? 0.1621 0.1545 0.1000 0.0206  0.0239  -0.0156 26  LEU C O   
4623  C  CB  . LEU C  26  ? 0.1965 0.1335 0.1365 -0.0149 0.0368  -0.0032 26  LEU C CB  
4624  C  CG  . LEU C  26  ? 0.2705 0.3718 0.1492 -0.0269 0.0405  -0.1108 26  LEU C CG  
4625  C  CD1 . LEU C  26  ? 0.2445 0.4120 0.2632 -0.0537 0.1140  -0.1504 26  LEU C CD1 
4626  C  CD2 . LEU C  26  ? 0.3583 0.2984 0.1039 -0.0907 0.0586  -0.0627 26  LEU C CD2 
4627  N  N   . GLN C  27  ? 0.1540 0.0901 0.0965 -0.0228 0.0131  0.0068  27  GLN C N   
4628  C  CA  . GLN C  27  ? 0.1411 0.0732 0.0886 -0.0032 0.0104  0.0065  27  GLN C CA  
4629  C  C   . GLN C  27  ? 0.1499 0.0816 0.0908 -0.0163 -0.0080 0.0038  27  GLN C C   
4630  O  O   . GLN C  27  ? 0.1946 0.0992 0.1123 -0.0383 -0.0416 0.0113  27  GLN C O   
4631  C  CB  . GLN C  27  ? 0.1234 0.0768 0.1203 -0.0107 0.0041  -0.0019 27  GLN C CB  
4632  C  CG  . GLN C  27  ? 0.1283 0.0915 0.1193 -0.0190 0.0086  0.0120  27  GLN C CG  
4633  C  CD  . GLN C  27  ? 0.1299 0.0815 0.0971 -0.0023 0.0219  0.0013  27  GLN C CD  
4634  O  OE1 . GLN C  27  ? 0.1446 0.0961 0.1042 -0.0263 0.0232  -0.0041 27  GLN C OE1 
4635  N  NE2 . GLN C  27  ? 0.1308 0.0904 0.1071 -0.0126 0.0214  -0.0087 27  GLN C NE2 
4636  N  N   . SER C  28  ? 0.1044 0.1010 0.0702 -0.0087 0.0142  0.0065  28  SER C N   
4637  C  CA  . SER C  28  ? 0.1154 0.0960 0.0768 0.0008  0.0171  0.0008  28  SER C CA  
4638  C  C   . SER C  28  ? 0.0998 0.0908 0.0929 0.0020  0.0152  -0.0074 28  SER C C   
4639  O  O   . SER C  28  ? 0.1317 0.0931 0.0895 -0.0010 0.0192  -0.0126 28  SER C O   
4640  C  CB  . SER C  28  ? 0.1136 0.1127 0.0732 0.0030  0.0153  -0.0099 28  SER C CB  
4641  O  OG  . SER C  28  ? 0.1208 0.1127 0.0687 -0.0037 0.0167  -0.0103 28  SER C OG  
4642  N  N   . PRO C  29  ? 0.1094 0.0832 0.0696 -0.0065 0.0131  -0.0118 29  PRO C N   
4643  C  CA  . PRO C  29  ? 0.1145 0.0864 0.0748 -0.0093 0.0035  -0.0092 29  PRO C CA  
4644  C  C   . PRO C  29  ? 0.1112 0.0915 0.0605 0.0007  0.0221  0.0054  29  PRO C C   
4645  O  O   . PRO C  29  ? 0.1106 0.0931 0.0804 0.0023  0.0034  -0.0131 29  PRO C O   
4646  C  CB  . PRO C  29  ? 0.1297 0.1190 0.0697 -0.0065 0.0115  0.0021  29  PRO C CB  
4647  C  CG  . PRO C  29  ? 0.1457 0.0987 0.0794 -0.0043 0.0114  -0.0115 29  PRO C CG  
4648  C  CD  . PRO C  29  ? 0.1307 0.0979 0.0617 -0.0127 0.0181  -0.0020 29  PRO C CD  
4649  N  N   . ILE C  30  ? 0.1123 0.0886 0.0857 0.0059  0.0043  -0.0020 30  ILE C N   
4650  C  CA  . ILE C  30  ? 0.1019 0.1080 0.0793 -0.0140 0.0059  -0.0052 30  ILE C CA  
4651  C  C   . ILE C  30  ? 0.1073 0.0834 0.0974 -0.0049 0.0127  -0.0089 30  ILE C C   
4652  O  O   . ILE C  30  ? 0.1149 0.1014 0.0956 -0.0010 0.0152  -0.0041 30  ILE C O   
4653  C  CB  . ILE C  30  ? 0.1197 0.0863 0.0784 0.0055  0.0086  -0.0007 30  ILE C CB  
4654  C  CG1 . ILE C  30  ? 0.1299 0.1158 0.0757 0.0057  0.0054  -0.0003 30  ILE C CG1 
4655  C  CG2 . ILE C  30  ? 0.1784 0.1048 0.0978 -0.0068 0.0178  0.0046  30  ILE C CG2 
4656  C  CD1 . ILE C  30  ? 0.1513 0.1416 0.0721 0.0054  0.0104  -0.0132 30  ILE C CD1 
4657  N  N   . ASP C  31  ? 0.1125 0.0818 0.1066 -0.0131 0.0073  -0.0055 31  ASP C N   
4658  C  CA  . ASP C  31  ? 0.1228 0.0882 0.1091 -0.0148 0.0040  -0.0007 31  ASP C CA  
4659  C  C   . ASP C  31  ? 0.1349 0.0798 0.0924 -0.0253 -0.0052 0.0031  31  ASP C C   
4660  O  O   . ASP C  31  ? 0.2117 0.1053 0.0987 0.0121  0.0126  0.0068  31  ASP C O   
4661  C  CB  . ASP C  31  ? 0.1111 0.1091 0.1410 -0.0152 0.0037  0.0013  31  ASP C CB  
4662  C  CG  . ASP C  31  ? 0.1357 0.1374 0.1130 -0.0285 0.0043  0.0126  31  ASP C CG  
4663  O  OD1 . ASP C  31  ? 0.1523 0.1107 0.1315 -0.0210 0.0044  -0.0013 31  ASP C OD1 
4664  O  OD2 . ASP C  31  ? 0.2284 0.1535 0.1705 -0.0850 -0.0443 0.0410  31  ASP C OD2 
4665  N  N   . LEU C  32  ? 0.1444 0.0962 0.1028 0.0142  0.0154  0.0083  32  LEU C N   
4666  C  CA  . LEU C  32  ? 0.1504 0.1212 0.1050 0.0100  0.0344  -0.0087 32  LEU C CA  
4667  C  C   . LEU C  32  ? 0.1502 0.1540 0.1243 0.0107  0.0366  -0.0245 32  LEU C C   
4668  O  O   . LEU C  32  ? 0.1913 0.1265 0.1396 -0.0131 0.0302  -0.0060 32  LEU C O   
4669  C  CB  . LEU C  32  ? 0.1587 0.1066 0.1242 0.0141  0.0271  -0.0146 32  LEU C CB  
4670  C  CG  . LEU C  32  ? 0.1324 0.1191 0.1150 0.0043  0.0348  0.0104  32  LEU C CG  
4671  C  CD1 . LEU C  32  ? 0.1605 0.1542 0.1542 0.0263  0.0141  0.0037  32  LEU C CD1 
4672  C  CD2 . LEU C  32  ? 0.1811 0.1721 0.1292 -0.0210 0.0403  0.0120  32  LEU C CD2 
4673  N  N   . HIS C  33  ? 0.1964 0.2063 0.1270 -0.0500 -0.0003 0.0116  33  HIS C N   
4674  C  CA  . HIS C  33  ? 0.1872 0.2429 0.2003 -0.0824 0.0219  -0.0425 33  HIS C CA  
4675  C  C   . HIS C  33  ? 0.1971 0.1893 0.1969 -0.0553 0.0083  0.0074  33  HIS C C   
4676  O  O   . HIS C  33  ? 0.1840 0.1572 0.1932 -0.0538 0.0337  -0.0110 33  HIS C O   
4677  C  CB  . HIS C  33  ? 0.2201 0.2581 0.1843 -0.0392 0.0066  -0.0007 33  HIS C CB  
4678  C  CG  . HIS C  33  ? 0.1982 0.3019 0.1621 0.0151  0.0054  -0.0430 33  HIS C CG  
4679  N  ND1 . HIS C  33  ? 0.2145 0.4343 0.2205 -0.0017 -0.0366 -0.0658 33  HIS C ND1 
4680  C  CD2 . HIS C  33  ? 0.2215 0.3411 0.2010 0.0662  0.0114  -0.0535 33  HIS C CD2 
4681  C  CE1 . HIS C  33  ? 0.2096 0.4397 0.2091 -0.0445 0.0027  -0.0170 33  HIS C CE1 
4682  N  NE2 . HIS C  33  ? 0.2332 0.3454 0.2090 0.0487  -0.0044 -0.0366 33  HIS C NE2 
4683  N  N   . SER C  34  ? 0.3072 0.2082 0.1702 -0.1146 0.0214  0.0091  34  SER C N   
4684  C  CA  . SER C  34  ? 0.2574 0.2075 0.2143 -0.0631 0.0229  0.0017  34  SER C CA  
4685  C  C   . SER C  34  ? 0.2434 0.1829 0.1859 -0.0582 -0.0125 -0.0247 34  SER C C   
4686  O  O   . SER C  34  ? 0.2852 0.2217 0.2132 -0.0553 0.0197  -0.0627 34  SER C O   
4687  C  CB  . SER C  34  ? 0.5245 0.2098 0.3995 -0.1317 0.0500  0.0381  34  SER C CB  
4688  O  OG  . SER C  34  ? 0.5333 0.2384 0.7555 -0.1031 0.0430  0.0962  34  SER C OG  
4689  N  N   . ASP C  35  ? 0.2183 0.2157 0.2079 -0.0623 0.0130  -0.0181 35  ASP C N   
4690  C  CA  . ASP C  35  ? 0.2208 0.3199 0.2143 -0.0612 -0.0109 -0.0280 35  ASP C CA  
4691  C  C   . ASP C  35  ? 0.1741 0.2614 0.1867 -0.0375 -0.0250 -0.0531 35  ASP C C   
4692  O  O   . ASP C  35  ? 0.2734 0.3779 0.1973 -0.0289 -0.0689 -0.0754 35  ASP C O   
4693  C  CB  . ASP C  35  ? 0.1565 0.5383 0.4314 -0.0979 0.0461  -0.0623 35  ASP C CB  
4694  C  CG  . ASP C  35  ? 0.3555 0.5494 0.7095 -0.1784 0.1085  -0.1404 35  ASP C CG  
4695  O  OD1 . ASP C  35  ? 0.6327 0.6286 0.7714 -0.0949 -0.2146 -0.2159 35  ASP C OD1 
4696  O  OD2 . ASP C  35  ? 0.2849 1.1588 0.9657 0.0157  -0.0888 0.0153  35  ASP C OD2 
4697  N  N   . ILE C  36  ? 0.1392 0.1897 0.1890 -0.0093 -0.0037 -0.0412 36  ILE C N   
4698  C  CA  . ILE C  36  ? 0.1350 0.2041 0.1570 -0.0153 0.0129  -0.0243 36  ILE C CA  
4699  C  C   . ILE C  36  ? 0.1502 0.1532 0.1550 -0.0228 -0.0038 -0.0379 36  ILE C C   
4700  O  O   . ILE C  36  ? 0.1523 0.1746 0.1773 0.0044  0.0037  -0.0115 36  ILE C O   
4701  C  CB  . ILE C  36  ? 0.1571 0.1992 0.1597 0.0109  0.0252  -0.0194 36  ILE C CB  
4702  C  CG1 . ILE C  36  ? 0.3005 0.1619 0.1403 -0.0331 0.0527  -0.0021 36  ILE C CG1 
4703  C  CG2 . ILE C  36  ? 0.2450 0.2646 0.2323 0.1020  0.0165  0.0148  36  ILE C CG2 
4704  C  CD1 . ILE C  36  ? 0.2233 0.1705 0.2363 -0.0020 0.0509  -0.0259 36  ILE C CD1 
4705  N  N   . LEU C  37  ? 0.1457 0.1809 0.1502 -0.0020 0.0175  -0.0421 37  LEU C N   
4706  C  CA  . LEU C  37  ? 0.1583 0.1497 0.1613 0.0124  0.0182  -0.0211 37  LEU C CA  
4707  C  C   . LEU C  37  ? 0.1631 0.1459 0.1518 -0.0001 0.0032  -0.0410 37  LEU C C   
4708  O  O   . LEU C  37  ? 0.1779 0.2231 0.2195 -0.0245 0.0199  -0.0983 37  LEU C O   
4709  C  CB  . LEU C  37  ? 0.2107 0.1500 0.1915 -0.0289 0.0226  -0.0286 37  LEU C CB  
4710  C  CG  . LEU C  37  ? 0.2345 0.1761 0.1698 0.0054  0.0038  -0.0167 37  LEU C CG  
4711  C  CD1 . LEU C  37  ? 0.2309 0.2012 0.2109 -0.0027 -0.0059 0.0031  37  LEU C CD1 
4712  C  CD2 . LEU C  37  ? 0.1793 0.1895 0.1723 0.0049  0.0263  -0.0122 37  LEU C CD2 
4713  N  N   . GLN C  38  ? 0.1457 0.1392 0.1500 0.0041  0.0148  -0.0329 38  GLN C N   
4714  C  CA  . GLN C  38  ? 0.1707 0.1088 0.1373 0.0114  0.0109  -0.0399 38  GLN C CA  
4715  C  C   . GLN C  38  ? 0.1784 0.1306 0.1200 0.0171  -0.0102 -0.0381 38  GLN C C   
4716  O  O   . GLN C  38  ? 0.1757 0.1287 0.1326 0.0144  -0.0054 -0.0221 38  GLN C O   
4717  C  CB  . GLN C  38  ? 0.2321 0.1344 0.1378 0.0214  0.0138  -0.0274 38  GLN C CB  
4718  C  CG  . GLN C  38  ? 0.2998 0.1888 0.1186 0.0403  -0.0066 -0.0452 38  GLN C CG  
4719  C  CD  . GLN C  38  ? 0.3499 0.2081 0.1475 0.0295  0.0020  -0.0494 38  GLN C CD  
4720  O  OE1 . GLN C  38  ? 0.4400 0.2775 0.2829 0.0454  -0.0452 -0.0121 38  GLN C OE1 
4721  N  NE2 . GLN C  38  ? 0.3921 0.2433 0.1739 -0.0237 0.0307  -0.0368 38  GLN C NE2 
4722  N  N   . TYR C  39  ? 0.1951 0.1263 0.1414 0.0166  0.0100  -0.0250 39  TYR C N   
4723  C  CA  . TYR C  39  ? 0.2008 0.1118 0.1744 0.0136  0.0114  -0.0155 39  TYR C CA  
4724  C  C   . TYR C  39  ? 0.1772 0.1118 0.1286 0.0315  0.0108  -0.0094 39  TYR C C   
4725  O  O   . TYR C  39  ? 0.2197 0.1493 0.1365 0.0315  0.0121  -0.0264 39  TYR C O   
4726  C  CB  . TYR C  39  ? 0.2321 0.1127 0.1993 0.0469  0.0093  -0.0450 39  TYR C CB  
4727  C  CG  . TYR C  39  ? 0.2231 0.1286 0.1773 0.0291  -0.0130 -0.0126 39  TYR C CG  
4728  C  CD1 . TYR C  39  ? 0.2522 0.1437 0.1802 0.0746  0.0165  -0.0097 39  TYR C CD1 
4729  C  CD2 . TYR C  39  ? 0.2247 0.1818 0.2305 0.0335  0.0206  -0.0693 39  TYR C CD2 
4730  C  CE1 . TYR C  39  ? 0.2646 0.1673 0.2231 0.1216  0.0243  -0.0144 39  TYR C CE1 
4731  C  CE2 . TYR C  39  ? 0.2540 0.2251 0.2750 0.0913  -0.0114 -0.0738 39  TYR C CE2 
4732  C  CZ  . TYR C  39  ? 0.3125 0.2678 0.2185 0.1532  0.0059  -0.0627 39  TYR C CZ  
4733  O  OH  . TYR C  39  ? 0.2730 0.3143 0.3014 0.1626  0.0164  -0.0419 39  TYR C OH  
4734  N  N   . ASP C  40  ? 0.1793 0.1572 0.1337 0.0273  0.0305  -0.0148 40  ASP C N   
4735  C  CA  . ASP C  40  ? 0.1527 0.1687 0.1717 0.0498  0.0551  0.0126  40  ASP C CA  
4736  C  C   . ASP C  40  ? 0.1847 0.2030 0.1181 0.0476  0.0109  0.0113  40  ASP C C   
4737  O  O   . ASP C  40  ? 0.1924 0.2093 0.1222 0.0734  0.0318  0.0070  40  ASP C O   
4738  C  CB  . ASP C  40  ? 0.1779 0.1759 0.1917 0.0417  0.0604  0.0375  40  ASP C CB  
4739  C  CG  . ASP C  40  ? 0.2009 0.1685 0.2594 0.0674  0.0785  0.0760  40  ASP C CG  
4740  O  OD1 . ASP C  40  ? 0.1951 0.2210 0.1883 0.0577  0.0573  0.0678  40  ASP C OD1 
4741  O  OD2 . ASP C  40  ? 0.2951 0.2107 0.2443 -0.0114 0.1018  0.0085  40  ASP C OD2 
4742  N  N   . ALA C  41  ? 0.1994 0.2425 0.1330 0.0652  0.0516  -0.0107 41  ALA C N   
4743  C  CA  . ALA C  41  ? 0.1942 0.2459 0.1339 0.0555  0.0439  -0.0302 41  ALA C CA  
4744  C  C   . ALA C  41  ? 0.1781 0.2199 0.1773 0.0680  0.0676  -0.0006 41  ALA C C   
4745  O  O   . ALA C  41  ? 0.2151 0.2813 0.1536 0.0961  0.0692  0.0120  41  ALA C O   
4746  C  CB  . ALA C  41  ? 0.2224 0.3465 0.1587 0.0564  0.0364  -0.0772 41  ALA C CB  
4747  N  N   . SER C  42  ? 0.1944 0.2326 0.1021 0.0564  0.0375  0.0208  42  SER C N   
4748  C  CA  . SER C  42  ? 0.1730 0.2341 0.1432 0.0221  0.0153  0.0348  42  SER C CA  
4749  C  C   . SER C  42  ? 0.1491 0.2454 0.1509 0.0331  0.0120  0.0529  42  SER C C   
4750  O  O   . SER C  42  ? 0.1667 0.2872 0.1473 0.0463  0.0527  0.0097  42  SER C O   
4751  C  CB  . SER C  42  ? 0.2323 0.2296 0.1844 0.0318  0.0549  0.0423  42  SER C CB  
4752  O  OG  . SER C  42  ? 0.2010 0.2418 0.2293 0.0487  0.0619  0.0505  42  SER C OG  
4753  N  N   . LEU C  43  ? 0.1883 0.1964 0.1375 0.0498  0.0573  0.0057  43  LEU C N   
4754  C  CA  . LEU C  43  ? 0.1784 0.2055 0.1179 0.0505  0.0557  0.0187  43  LEU C CA  
4755  C  C   . LEU C  43  ? 0.1419 0.2439 0.1547 0.0315  0.0425  0.0174  43  LEU C C   
4756  O  O   . LEU C  43  ? 0.1928 0.2343 0.1726 0.0709  0.0641  0.0436  43  LEU C O   
4757  C  CB  . LEU C  43  ? 0.1534 0.2016 0.1321 0.0509  0.0384  0.0001  43  LEU C CB  
4758  C  CG  . LEU C  43  ? 0.1545 0.1454 0.1486 0.0111  0.0306  0.0057  43  LEU C CG  
4759  C  CD1 . LEU C  43  ? 0.1789 0.1912 0.1216 0.0527  0.0544  -0.0003 43  LEU C CD1 
4760  C  CD2 . LEU C  43  ? 0.1850 0.1928 0.1596 -0.0172 0.0381  -0.0162 43  LEU C CD2 
4761  N  N   . THR C  44  ? 0.1619 0.2283 0.1820 0.0454  0.0278  0.0214  44  THR C N   
4762  C  CA  . THR C  44  ? 0.1971 0.2917 0.1333 0.0817  0.0222  0.0399  44  THR C CA  
4763  C  C   . THR C  44  ? 0.1698 0.2626 0.1849 0.0595  0.0077  0.0174  44  THR C C   
4764  O  O   . THR C  44  ? 0.1865 0.2556 0.1845 0.0710  0.0335  -0.0006 44  THR C O   
4765  C  CB  . THR C  44  ? 0.1805 0.3598 0.2093 0.0659  0.0674  0.0248  44  THR C CB  
4766  O  OG1 . THR C  44  ? 0.2020 0.3616 0.2910 0.0505  0.0844  0.0944  44  THR C OG1 
4767  C  CG2 . THR C  44  ? 0.3167 0.4474 0.1649 0.1454  0.0986  0.0487  44  THR C CG2 
4768  N  N   . PRO C  45  ? 0.1924 0.2973 0.1930 0.1098  0.0190  -0.0041 45  PRO C N   
4769  C  CA  . PRO C  45  ? 0.2054 0.2987 0.1644 0.0824  0.0267  0.0289  45  PRO C CA  
4770  C  C   . PRO C  45  ? 0.2221 0.2833 0.2172 0.0709  0.0401  0.0379  45  PRO C C   
4771  O  O   . PRO C  45  ? 0.2034 0.3835 0.2811 0.0586  0.0742  -0.0208 45  PRO C O   
4772  C  CB  . PRO C  45  ? 0.2603 0.3061 0.3055 0.0680  0.0270  0.0923  45  PRO C CB  
4773  C  CG  . PRO C  45  ? 0.3384 0.2728 0.3418 0.0939  0.0121  0.0895  45  PRO C CG  
4774  C  CD  . PRO C  45  ? 0.2779 0.3167 0.2375 0.1504  0.0259  0.0111  45  PRO C CD  
4775  N  N   . LEU C  46  ? 0.1669 0.2955 0.2075 0.0485  0.0204  0.0126  46  LEU C N   
4776  C  CA  . LEU C  46  ? 0.2030 0.2743 0.2188 0.0474  0.0130  0.0383  46  LEU C CA  
4777  C  C   . LEU C  46  ? 0.2005 0.2433 0.3285 0.0694  -0.0513 -0.0209 46  LEU C C   
4778  O  O   . LEU C  46  ? 0.2176 0.2931 0.3492 0.0529  -0.0628 0.0297  46  LEU C O   
4779  C  CB  . LEU C  46  ? 0.1723 0.3149 0.2307 0.0621  -0.0152 0.0188  46  LEU C CB  
4780  C  CG  . LEU C  46  ? 0.2197 0.2624 0.3003 0.0504  -0.0082 0.0903  46  LEU C CG  
4781  C  CD1 . LEU C  46  ? 0.1687 0.3113 0.3413 0.0612  -0.0166 -0.0094 46  LEU C CD1 
4782  C  CD2 . LEU C  46  ? 0.2800 0.3470 0.2414 0.0449  0.0007  0.0599  46  LEU C CD2 
4783  N  N   . GLU C  47  ? 0.1967 0.3197 0.2946 0.0671  0.0135  -0.0291 47  GLU C N   
4784  C  CA  . GLU C  47  ? 0.1860 0.3016 0.3980 0.1002  -0.0149 0.0575  47  GLU C CA  
4785  C  C   . GLU C  47  ? 0.2014 0.3124 0.3772 0.0595  -0.0310 0.0772  47  GLU C C   
4786  O  O   . GLU C  47  ? 0.2800 0.2725 0.2982 0.0368  -0.0361 0.0386  47  GLU C O   
4787  C  CB  . GLU C  47  ? 0.3122 0.5041 0.4424 0.1430  0.0948  0.0289  47  GLU C CB  
4788  C  CG  . GLU C  47  ? 0.3183 0.6348 0.5892 0.2088  0.1228  -0.1523 47  GLU C CG  
4789  C  CD  . GLU C  47  ? 0.6406 0.6589 0.8985 -0.1254 0.3098  -0.2149 47  GLU C CD  
4790  O  OE1 . GLU C  47  ? 0.6604 0.7641 1.1218 0.4659  0.0759  -0.2162 47  GLU C OE1 
4791  O  OE2 . GLU C  47  ? 0.9395 0.7554 0.8687 -0.1262 0.4201  0.2230  47  GLU C OE2 
4792  N  N   . PHE C  48  ? 0.1565 0.1806 0.3292 0.0366  -0.0489 0.0021  48  PHE C N   
4793  C  CA  . PHE C  48  ? 0.1933 0.2077 0.3890 0.0109  -0.0195 0.0044  48  PHE C CA  
4794  C  C   . PHE C  48  ? 0.1712 0.2257 0.3551 0.0060  -0.0469 0.0725  48  PHE C C   
4795  O  O   . PHE C  48  ? 0.3034 0.2935 0.4401 0.0710  -0.0891 0.0860  48  PHE C O   
4796  C  CB  . PHE C  48  ? 0.2215 0.2549 0.3429 -0.0068 -0.0408 0.1099  48  PHE C CB  
4797  C  CG  . PHE C  48  ? 0.2585 0.3192 0.2436 -0.0350 -0.0274 0.0749  48  PHE C CG  
4798  C  CD1 . PHE C  48  ? 0.2233 0.3494 0.1928 0.0417  0.0054  0.0093  48  PHE C CD1 
4799  C  CD2 . PHE C  48  ? 0.2230 0.2728 0.2601 0.0057  -0.0245 0.0637  48  PHE C CD2 
4800  C  CE1 . PHE C  48  ? 0.2230 0.3986 0.2328 -0.0122 0.0076  0.0377  48  PHE C CE1 
4801  C  CE2 . PHE C  48  ? 0.2011 0.4439 0.2193 -0.0283 0.0364  0.0549  48  PHE C CE2 
4802  C  CZ  . PHE C  48  ? 0.1405 0.4174 0.2472 0.0098  0.0582  -0.0252 48  PHE C CZ  
4803  N  N   . GLN C  49  ? 0.1932 0.2666 0.2707 0.0331  -0.0648 0.0595  49  GLN C N   
4804  C  CA  . GLN C  49  ? 0.1748 0.4144 0.3535 -0.0026 -0.0414 0.1169  49  GLN C CA  
4805  C  C   . GLN C  49  ? 0.2486 0.3975 0.2987 0.1004  -0.0241 0.0709  49  GLN C C   
4806  O  O   . GLN C  49  ? 0.1516 0.3533 0.3222 0.0160  -0.0562 0.0755  49  GLN C O   
4807  C  CB  . GLN C  49  ? 0.2294 0.5044 0.2504 0.0615  0.0111  0.0054  49  GLN C CB  
4808  C  CG  . GLN C  49  ? 0.2768 0.4411 0.3797 0.0342  0.1297  -0.0548 49  GLN C CG  
4809  C  CD  . GLN C  49  ? 0.5741 0.4144 0.8526 0.1594  0.1155  -0.2570 49  GLN C CD  
4810  O  OE1 . GLN C  49  ? 0.7950 0.8069 0.7466 -0.1984 0.1331  -0.3513 49  GLN C OE1 
4811  N  NE2 . GLN C  49  ? 0.6262 0.6017 0.6541 0.2284  0.0636  -0.3039 49  GLN C NE2 
4812  N  N   . GLY C  50  ? 0.1800 0.3465 0.3635 0.0218  -0.0674 0.0604  50  GLY C N   
4813  C  CA  . GLY C  50  ? 0.1402 0.6261 0.3027 0.0320  -0.0425 -0.0010 50  GLY C CA  
4814  C  C   . GLY C  50  ? 0.1213 0.2739 0.2601 0.0449  -0.0443 -0.0299 50  GLY C C   
4815  O  O   . GLY C  50  ? 0.1859 0.3736 0.4241 0.0038  -0.0251 -0.0945 50  GLY C O   
4816  N  N   . TYR C  51  ? 0.1301 0.4383 0.4151 0.0414  -0.0538 0.1048  51  TYR C N   
4817  C  CA  . TYR C  51  ? 0.1394 0.3086 0.3659 0.0109  -0.0732 0.0879  51  TYR C CA  
4818  C  C   . TYR C  51  ? 0.2375 0.4832 0.2890 0.1494  -0.1448 -0.0467 51  TYR C C   
4819  O  O   . TYR C  51  ? 0.2892 0.2169 0.2987 0.0187  -0.0974 0.0124  51  TYR C O   
4820  C  CB  . TYR C  51  ? 0.2603 0.2348 0.2689 0.0054  -0.1032 0.0244  51  TYR C CB  
4821  C  CG  . TYR C  51  ? 0.1660 0.3045 0.3531 0.0302  -0.0520 0.1156  51  TYR C CG  
4822  C  CD1 . TYR C  51  ? 0.2184 0.1944 0.2460 0.0375  -0.0753 0.0010  51  TYR C CD1 
4823  C  CD2 . TYR C  51  ? 0.1795 0.2249 0.2151 0.0154  -0.0370 0.0124  51  TYR C CD2 
4824  C  CE1 . TYR C  51  ? 0.1554 0.2215 0.3248 -0.0008 -0.0637 0.0715  51  TYR C CE1 
4825  C  CE2 . TYR C  51  ? 0.1621 0.3154 0.2987 0.0513  -0.0136 0.1266  51  TYR C CE2 
4826  C  CZ  . TYR C  51  ? 0.1590 0.2628 0.2384 0.0038  -0.0606 0.0614  51  TYR C CZ  
4827  O  OH  . TYR C  51  ? 0.1502 0.2736 0.2876 -0.0107 -0.0571 0.1106  51  TYR C OH  
4828  N  N   . ASN C  52  ? 0.2158 0.2951 0.4050 0.0511  -0.1622 -0.0542 52  ASN C N   
4829  C  CA  . ASN C  52  ? 0.3456 0.2108 0.4357 0.0989  -0.1995 -0.0593 52  ASN C CA  
4830  C  C   . ASN C  52  ? 0.3467 0.2224 0.4210 0.1177  -0.1562 -0.1298 52  ASN C C   
4831  O  O   . ASN C  52  ? 0.3000 0.5685 0.5813 0.0824  -0.1960 -0.1676 52  ASN C O   
4832  C  CB  . ASN C  52  ? 0.5644 0.3228 0.4460 0.2883  -0.1615 -0.1018 52  ASN C CB  
4833  C  CG  . ASN C  52  ? 0.3756 0.7380 0.3935 0.2480  -0.1615 -0.0130 52  ASN C CG  
4834  O  OD1 . ASN C  52  ? 0.4792 0.3614 0.4128 0.1653  -0.2099 -0.0811 52  ASN C OD1 
4835  N  ND2 . ASN C  52  ? 1.0249 0.4548 0.4845 0.3165  -0.1835 0.0807  52  ASN C ND2 
4836  N  N   . LEU C  53  ? 0.4210 0.2642 0.3754 0.1421  -0.2393 -0.0971 53  LEU C N   
4837  C  CA  . LEU C  53  ? 0.4232 0.2513 0.3328 0.0737  -0.1023 -0.0553 53  LEU C CA  
4838  C  C   . LEU C  53  ? 0.6173 0.3321 0.4011 0.0859  -0.2874 -0.1070 53  LEU C C   
4839  O  O   . LEU C  53  ? 0.7353 0.4752 0.7728 -0.0362 -0.5070 0.2107  53  LEU C O   
4840  C  CB  . LEU C  53  ? 0.3154 0.3106 0.3113 0.0800  -0.1000 -0.0010 53  LEU C CB  
4841  C  CG  . LEU C  53  ? 0.2678 0.2739 0.2125 0.0439  -0.0445 0.0006  53  LEU C CG  
4842  C  CD1 . LEU C  53  ? 0.2517 0.2825 0.1852 0.0280  0.0195  -0.0273 53  LEU C CD1 
4843  C  CD2 . LEU C  53  ? 0.3688 0.3752 0.2942 -0.0019 -0.0346 0.0879  53  LEU C CD2 
4844  N  N   . SER C  54  ? 0.4501 0.5396 0.2696 0.1824  -0.0803 -0.0348 54  SER C N   
4845  C  CA  . SER C  54  ? 0.5472 0.7321 0.1587 0.1519  -0.1278 -0.1272 54  SER C CA  
4846  C  C   . SER C  54  ? 0.7595 1.1301 0.1211 0.0794  -0.0763 0.0854  54  SER C C   
4847  O  O   . SER C  54  ? 0.6043 1.5650 1.1984 0.1837  -0.3704 -0.2391 54  SER C O   
4848  C  CB  . SER C  54  ? 0.6179 0.7813 0.4541 0.1027  0.0948  -0.1750 54  SER C CB  
4849  O  OG  . SER C  54  ? 0.4329 1.1957 0.4950 -0.0932 0.1666  -0.1721 54  SER C OG  
4850  N  N   . ALA C  55  ? 1.0658 0.8022 0.5661 0.2043  -0.1564 -0.0163 55  ALA C N   
4851  C  CA  . ALA C  55  ? 1.3444 0.4190 0.4390 0.0230  -0.3643 -0.0612 55  ALA C CA  
4852  C  C   . ALA C  55  ? 0.9936 0.9059 1.2845 -0.1010 -0.5274 -0.4648 55  ALA C C   
4853  O  O   . ALA C  55  ? 2.6040 2.3987 0.3547 0.5304  0.0841  0.1621  55  ALA C O   
4854  C  CB  . ALA C  55  ? 0.9491 0.5146 0.4867 0.2958  -0.2949 -0.1172 55  ALA C CB  
4855  N  N   . ASN C  56  ? 0.7641 0.5333 0.4128 0.2518  -0.3486 -0.2108 56  ASN C N   
4856  C  CA  . ASN C  56  ? 0.4483 0.8763 1.2058 0.1247  -0.6241 -0.4063 56  ASN C CA  
4857  C  C   . ASN C  56  ? 0.8702 1.0269 0.7870 0.1862  -0.6017 -0.3971 56  ASN C C   
4858  O  O   . ASN C  56  ? 0.9440 2.2911 4.1135 1.0781  -1.3260 -2.4254 56  ASN C O   
4859  N  N   . LYS C  57  ? 0.3930 0.6902 0.6963 0.1966  -0.3476 -0.3468 57  LYS C N   
4860  C  CA  . LYS C  57  ? 0.5245 1.0240 0.6268 0.3230  0.0013  -0.1428 57  LYS C CA  
4861  C  C   . LYS C  57  ? 0.3251 0.2337 0.3596 0.0388  -0.1897 -0.0680 57  LYS C C   
4862  O  O   . LYS C  57  ? 0.4307 0.3560 0.5838 -0.0401 -0.3431 0.0227  57  LYS C O   
4863  C  CB  . LYS C  57  ? 0.5498 0.6154 0.5825 -0.0601 -0.0953 -0.4384 57  LYS C CB  
4864  C  CG  . LYS C  57  ? 0.2703 1.2323 0.8647 -0.1893 0.0759  0.0731  57  LYS C CG  
4865  N  N   . GLN C  58  ? 0.3576 0.3420 0.4666 0.1202  -0.2360 -0.0522 58  GLN C N   
4866  C  CA  . GLN C  58  ? 0.3806 0.4659 0.3089 0.0953  -0.1885 -0.0197 58  GLN C CA  
4867  C  C   . GLN C  58  ? 0.4711 0.4248 0.3646 -0.1155 -0.2791 -0.0189 58  GLN C C   
4868  O  O   . GLN C  58  ? 0.2518 0.4181 0.4147 0.0803  -0.1103 -0.0199 58  GLN C O   
4869  C  CB  . GLN C  58  ? 0.6983 0.5522 0.4178 -0.0932 -0.2154 -0.2137 58  GLN C CB  
4870  C  CG  . GLN C  58  ? 0.3984 0.4483 0.2109 0.0260  -0.1137 -0.0737 58  GLN C CG  
4871  C  CD  . GLN C  58  ? 0.6912 0.3088 0.1944 0.1011  -0.0239 -0.0463 58  GLN C CD  
4872  O  OE1 . GLN C  58  ? 1.1132 0.4162 0.3190 -0.1410 -0.1552 0.0214  58  GLN C OE1 
4873  N  NE2 . GLN C  58  ? 0.3068 0.3889 0.3416 -0.1002 -0.0966 0.0013  58  GLN C NE2 
4874  N  N   . PHE C  59  ? 0.4359 0.3393 0.2165 0.0700  -0.1378 -0.1225 59  PHE C N   
4875  C  CA  . PHE C  59  ? 0.3382 0.4350 0.2278 0.0579  -0.1797 -0.1775 59  PHE C CA  
4876  C  C   . PHE C  59  ? 0.2536 0.2856 0.3021 0.0104  -0.1613 0.0054  59  PHE C C   
4877  O  O   . PHE C  59  ? 0.3353 0.3325 0.2509 0.0342  -0.0766 -0.0577 59  PHE C O   
4878  C  CB  . PHE C  59  ? 0.3529 0.3224 0.2363 0.1040  -0.1345 -0.1002 59  PHE C CB  
4879  C  CG  . PHE C  59  ? 0.4597 0.3982 0.2433 0.2311  -0.1502 -0.1861 59  PHE C CG  
4880  C  CD1 . PHE C  59  ? 0.2260 0.5322 0.3179 0.0264  -0.0939 -0.1997 59  PHE C CD1 
4881  C  CD2 . PHE C  59  ? 0.2639 0.3267 0.5886 0.1613  -0.1077 -0.1027 59  PHE C CD2 
4882  C  CE1 . PHE C  59  ? 0.3350 0.3617 0.2827 0.1761  -0.0784 -0.1068 59  PHE C CE1 
4883  C  CE2 . PHE C  59  ? 0.2824 0.3912 0.3524 0.1416  -0.1865 -0.1802 59  PHE C CE2 
4884  C  CZ  . PHE C  59  ? 0.2271 0.2845 0.6036 0.0198  -0.0416 -0.0206 59  PHE C CZ  
4885  N  N   A LEU C  60  ? 0.1592 0.2246 0.2822 0.0652  -0.1324 -0.0860 60  LEU C N   
4886  N  N   B LEU C  60  ? 0.3876 0.3526 0.2205 0.0099  -0.1835 0.0630  60  LEU C N   
4887  C  CA  A LEU C  60  ? 0.2167 0.1800 0.2549 0.0282  -0.0513 -0.0153 60  LEU C CA  
4888  C  CA  B LEU C  60  ? 0.2671 0.4641 0.1258 -0.0733 -0.0815 0.0070  60  LEU C CA  
4889  C  C   A LEU C  60  ? 0.2090 0.1753 0.1971 0.0623  -0.0975 -0.0116 60  LEU C C   
4890  C  C   B LEU C  60  ? 0.3222 0.7217 0.1872 -0.1729 -0.0666 -0.1796 60  LEU C C   
4891  O  O   A LEU C  60  ? 0.1829 0.1412 0.1567 0.0595  -0.0538 -0.0449 60  LEU C O   
4892  O  O   B LEU C  60  ? 0.1633 0.6790 0.1509 0.0111  -0.0454 -0.1532 60  LEU C O   
4893  C  CB  A LEU C  60  ? 0.1827 0.2075 0.1951 -0.0013 -0.0513 -0.0082 60  LEU C CB  
4894  C  CB  B LEU C  60  ? 0.3959 0.3546 0.2606 -0.0408 0.0274  -0.0715 60  LEU C CB  
4895  C  CG  A LEU C  60  ? 0.1940 0.2422 0.1545 -0.0302 0.0187  -0.0076 60  LEU C CG  
4896  C  CG  B LEU C  60  ? 0.1671 0.3120 0.3032 -0.0509 -0.0582 -0.0661 60  LEU C CG  
4897  C  CD1 A LEU C  60  ? 0.3440 0.2134 0.1623 0.0052  -0.0471 0.0187  60  LEU C CD1 
4898  C  CD1 B LEU C  60  ? 0.2411 0.3246 0.2985 -0.0588 -0.0065 -0.1699 60  LEU C CD1 
4899  C  CD2 A LEU C  60  ? 0.1974 0.2700 0.1623 -0.0384 0.0104  0.0164  60  LEU C CD2 
4900  C  CD2 B LEU C  60  ? 0.3686 0.2021 0.4702 0.0099  0.0538  -0.1059 60  LEU C CD2 
4901  N  N   A LEU C  61  ? 0.2942 0.1188 0.1845 0.0074  -0.0729 0.0048  61  LEU C N   
4902  N  N   B LEU C  61  ? 0.3702 0.9966 0.1233 -0.2488 -0.0093 -0.0949 61  LEU C N   
4903  C  CA  A LEU C  61  ? 0.2786 0.1583 0.0843 0.0126  -0.0348 -0.0653 61  LEU C CA  
4904  C  CA  B LEU C  61  ? 0.4341 0.5527 0.2531 -0.2000 0.0291  -0.1172 61  LEU C CA  
4905  C  C   A LEU C  61  ? 0.3564 0.1349 0.2023 0.0066  -0.0891 -0.1089 61  LEU C C   
4906  C  C   B LEU C  61  ? 0.2362 0.5891 0.1365 -0.0838 0.0071  -0.0043 61  LEU C C   
4907  O  O   A LEU C  61  ? 0.2642 0.1692 0.1446 0.0322  -0.0846 -0.0690 61  LEU C O   
4908  O  O   B LEU C  61  ? 0.4442 0.7156 0.1409 -0.3395 0.0956  -0.1546 61  LEU C O   
4909  C  CB  A LEU C  61  ? 0.1885 0.2666 0.1692 0.1169  0.0232  0.0373  61  LEU C CB  
4910  C  CB  B LEU C  61  ? 0.1981 0.6380 0.1629 -0.1263 -0.0755 -0.1675 61  LEU C CB  
4911  C  CG  A LEU C  61  ? 0.2522 0.2935 0.0631 0.0265  0.0333  -0.0091 61  LEU C CG  
4912  C  CG  B LEU C  61  ? 0.3686 0.5655 0.1405 -0.0795 0.1106  -0.1375 61  LEU C CG  
4913  C  CD1 A LEU C  61  ? 0.3104 0.1430 0.1533 -0.0929 -0.0553 -0.0204 61  LEU C CD1 
4914  C  CD1 B LEU C  61  ? 0.2348 0.5151 0.1213 -0.0098 -0.0010 -0.0821 61  LEU C CD1 
4915  C  CD2 A LEU C  61  ? 0.4558 0.1023 0.2445 -0.0044 -0.0697 0.0760  61  LEU C CD2 
4916  C  CD2 B LEU C  61  ? 0.2583 0.5784 0.2797 0.1300  -0.0861 -0.0366 61  LEU C CD2 
4917  N  N   . THR C  62  ? 0.2910 0.2183 0.1147 -0.0410 -0.0394 -0.0320 62  THR C N   
4918  C  CA  . THR C  62  ? 0.2998 0.2062 0.1870 0.0052  -0.0241 -0.0248 62  THR C CA  
4919  C  C   . THR C  62  ? 0.3160 0.2538 0.1454 -0.0313 -0.0220 -0.0218 62  THR C C   
4920  O  O   . THR C  62  ? 0.3075 0.2867 0.1619 -0.0195 -0.0419 -0.0584 62  THR C O   
4921  C  CB  . THR C  62  ? 0.2989 0.2127 0.2212 -0.0102 0.0041  -0.0471 62  THR C CB  
4922  O  OG1 . THR C  62  ? 0.3106 0.2836 0.2230 0.0013  -0.0493 -0.0593 62  THR C OG1 
4923  C  CG2 . THR C  62  ? 0.4284 0.2872 0.3456 0.0575  -0.0052 -0.1326 62  THR C CG2 
4924  N  N   . ASN C  63  ? 0.3131 0.4058 0.0900 -0.1180 0.0057  -0.0472 63  ASN C N   
4925  C  CA  . ASN C  63  ? 0.3005 0.2386 0.1340 -0.0041 -0.0628 -0.0020 63  ASN C CA  
4926  C  C   . ASN C  63  ? 0.3853 0.1931 0.1326 0.0340  -0.0111 -0.0540 63  ASN C C   
4927  O  O   . ASN C  63  ? 0.3276 0.2425 0.1495 0.0281  -0.0196 -0.0307 63  ASN C O   
4928  C  CB  . ASN C  63  ? 0.3152 0.3009 0.0976 0.0370  -0.0509 -0.0639 63  ASN C CB  
4929  C  CG  . ASN C  63  ? 0.2452 0.2727 0.2858 -0.0361 -0.0709 0.0820  63  ASN C CG  
4930  O  OD1 . ASN C  63  ? 0.3768 0.2768 0.1504 -0.0187 -0.0239 -0.0068 63  ASN C OD1 
4931  N  ND2 . ASN C  63  ? 0.3517 0.3745 0.1120 -0.1030 -0.0082 -0.0197 63  ASN C ND2 
4932  N  N   . ASN C  64  ? 0.4458 0.2132 0.1170 -0.0812 -0.0549 -0.0054 64  ASN C N   
4933  C  CA  . ASN C  64  ? 0.3661 0.2727 0.1154 -0.0649 -0.0406 0.0122  64  ASN C CA  
4934  C  C   . ASN C  64  ? 0.3052 0.1820 0.2154 -0.0024 -0.1097 -0.0142 64  ASN C C   
4935  O  O   . ASN C  64  ? 0.4257 0.2364 0.2010 -0.0066 -0.0096 0.0015  64  ASN C O   
4936  C  CB  . ASN C  64  ? 0.3427 0.3233 0.1612 -0.0939 -0.0161 -0.0024 64  ASN C CB  
4937  C  CG  . ASN C  64  ? 0.3952 0.4133 0.0906 -0.1453 -0.0141 -0.0256 64  ASN C CG  
4938  O  OD1 . ASN C  64  ? 0.4384 0.4896 0.1213 -0.2287 0.0019  -0.0570 64  ASN C OD1 
4939  N  ND2 . ASN C  64  ? 0.4063 0.5593 0.1540 -0.2069 0.0732  -0.0930 64  ASN C ND2 
4940  N  N   . GLY C  65  ? 0.4183 0.3777 0.1489 -0.1396 -0.0344 -0.0649 65  GLY C N   
4941  C  CA  . GLY C  65  ? 0.5056 0.2637 0.2016 -0.1001 -0.0445 -0.0419 65  GLY C CA  
4942  C  C   . GLY C  65  ? 0.2883 0.3702 0.1653 -0.0621 0.0034  -0.0617 65  GLY C C   
4943  O  O   . GLY C  65  ? 0.3452 0.5842 0.2694 -0.1313 0.0054  -0.1385 65  GLY C O   
4944  N  N   . HIS C  66  ? 0.3727 0.3610 0.1199 -0.1578 0.0232  -0.0480 66  HIS C N   
4945  C  CA  . HIS C  66  ? 0.4169 0.2691 0.1395 -0.0961 -0.0526 0.0066  66  HIS C CA  
4946  C  C   . HIS C  66  ? 0.3143 0.2264 0.1538 -0.0788 -0.0344 0.0092  66  HIS C C   
4947  O  O   . HIS C  66  ? 0.3136 0.3276 0.2791 -0.1283 -0.0110 0.0154  66  HIS C O   
4948  C  CB  . HIS C  66  ? 0.3018 0.2684 0.1079 -0.1199 0.0093  -0.0416 66  HIS C CB  
4949  C  CG  . HIS C  66  ? 0.3953 0.2321 0.1585 -0.1158 -0.0086 -0.0635 66  HIS C CG  
4950  N  ND1 . HIS C  66  ? 0.3481 0.2843 0.2436 -0.1042 -0.0542 -0.0625 66  HIS C ND1 
4951  C  CD2 . HIS C  66  ? 0.3693 0.2623 0.1188 -0.0434 0.0013  -0.0105 66  HIS C CD2 
4952  C  CE1 . HIS C  66  ? 0.3258 0.2813 0.2138 -0.0754 0.0073  -0.0688 66  HIS C CE1 
4953  N  NE2 . HIS C  66  ? 0.3425 0.3264 0.2233 -0.0876 -0.0032 -0.0125 66  HIS C NE2 
4954  N  N   . SER C  67  ? 0.3702 0.2536 0.1459 -0.0608 -0.0281 -0.0307 67  SER C N   
4955  C  CA  . SER C  67  ? 0.3023 0.2583 0.0825 -0.0628 -0.0288 -0.0171 67  SER C CA  
4956  C  C   . SER C  67  ? 0.3515 0.2416 0.1507 -0.0763 0.0288  -0.0285 67  SER C C   
4957  O  O   . SER C  67  ? 0.3404 0.2838 0.1547 -0.1160 -0.0399 -0.0206 67  SER C O   
4958  C  CB  . SER C  67  ? 0.4715 0.2614 0.1574 0.0295  -0.0054 -0.0775 67  SER C CB  
4959  O  OG  . SER C  67  ? 0.3366 0.4228 0.1404 -0.0643 -0.0764 -0.0715 67  SER C OG  
4960  N  N   . VAL C  68  ? 0.2617 0.2511 0.1049 -0.0324 -0.0351 -0.0066 68  VAL C N   
4961  C  CA  . VAL C  68  ? 0.3134 0.3914 0.1030 -0.1561 -0.0425 -0.0059 68  VAL C CA  
4962  C  C   . VAL C  68  ? 0.4083 0.4456 0.0630 -0.1230 -0.0344 -0.0089 68  VAL C C   
4963  O  O   . VAL C  68  ? 0.2851 0.3811 0.1026 -0.0877 -0.0291 0.0103  68  VAL C O   
4964  C  CB  . VAL C  68  ? 0.3542 0.3336 0.1513 -0.0551 -0.0693 -0.0060 68  VAL C CB  
4965  C  CG1 . VAL C  68  ? 0.4086 0.2447 0.1350 0.0458  0.0214  -0.0001 68  VAL C CG1 
4966  C  CG2 . VAL C  68  ? 0.3824 0.5493 0.1658 -0.1668 -0.0856 0.0688  68  VAL C CG2 
4967  N  N   . LYS C  69  ? 0.3510 0.3183 0.1439 -0.0625 -0.0103 -0.0348 69  LYS C N   
4968  C  CA  . LYS C  69  ? 0.2556 0.2245 0.1712 -0.0185 -0.0487 -0.0038 69  LYS C CA  
4969  C  C   . LYS C  69  ? 0.3294 0.2515 0.1482 0.0209  -0.0819 0.0076  69  LYS C C   
4970  O  O   . LYS C  69  ? 0.3512 0.2786 0.1583 -0.0114 -0.0734 -0.0377 69  LYS C O   
4971  C  CB  . LYS C  69  ? 0.3799 0.2781 0.1377 -0.0986 -0.0223 0.0164  69  LYS C CB  
4972  C  CG  . LYS C  69  ? 0.3718 0.2908 0.1852 -0.0526 -0.1203 -0.0214 69  LYS C CG  
4973  C  CD  . LYS C  69  ? 0.4154 0.2689 0.2075 -0.0281 -0.0166 0.0245  69  LYS C CD  
4974  C  CE  . LYS C  69  ? 0.4652 0.3600 0.2375 -0.0715 -0.0918 0.0465  69  LYS C CE  
4975  N  NZ  . LYS C  69  ? 0.3637 0.2962 0.2881 -0.0287 0.0612  0.0155  69  LYS C NZ  
4976  N  N   . LEU C  70  ? 0.1926 0.2325 0.1626 -0.0187 -0.0640 -0.0276 70  LEU C N   
4977  C  CA  . LEU C  70  ? 0.2179 0.2522 0.1341 0.0401  -0.0273 -0.0148 70  LEU C CA  
4978  C  C   . LEU C  70  ? 0.2427 0.3298 0.1286 -0.0769 -0.0601 -0.0020 70  LEU C C   
4979  O  O   . LEU C  70  ? 0.2382 0.3143 0.1340 -0.0577 -0.0472 -0.0093 70  LEU C O   
4980  C  CB  . LEU C  70  ? 0.2117 0.1924 0.1904 0.0353  -0.0834 -0.0461 70  LEU C CB  
4981  C  CG  . LEU C  70  ? 0.3075 0.2310 0.2217 0.0782  -0.0668 0.0124  70  LEU C CG  
4982  C  CD1 . LEU C  70  ? 0.3905 0.2992 0.2858 0.0542  -0.2269 -0.0509 70  LEU C CD1 
4983  C  CD2 . LEU C  70  ? 0.2603 0.2278 0.1714 0.0964  -0.1186 -0.0709 70  LEU C CD2 
4984  N  N   . ASN C  71  ? 0.1955 0.2957 0.1531 -0.0362 -0.0480 -0.0155 71  ASN C N   
4985  C  CA  . ASN C  71  ? 0.3280 0.1813 0.2109 -0.0320 -0.0263 -0.0507 71  ASN C CA  
4986  C  C   . ASN C  71  ? 0.2337 0.1875 0.1656 -0.0231 -0.0987 -0.0274 71  ASN C C   
4987  O  O   . ASN C  71  ? 0.3869 0.3422 0.1949 -0.0146 -0.0844 0.0203  71  ASN C O   
4988  C  CB  . ASN C  71  ? 0.2219 0.2366 0.1773 -0.0355 -0.0394 -0.0377 71  ASN C CB  
4989  C  CG  . ASN C  71  ? 0.2698 0.2549 0.3249 -0.0226 -0.0485 -0.0599 71  ASN C CG  
4990  O  OD1 . ASN C  71  ? 0.3276 0.1865 0.2423 -0.0031 -0.0693 -0.0130 71  ASN C OD1 
4991  N  ND2 . ASN C  71  ? 0.2678 0.2599 0.3032 -0.0403 -0.0551 -0.0122 71  ASN C ND2 
4992  N  N   . LEU C  72  ? 0.2452 0.2388 0.1691 -0.0166 -0.0527 -0.0076 72  LEU C N   
4993  C  CA  . LEU C  72  ? 0.2396 0.1576 0.2342 0.0282  -0.0949 -0.0132 72  LEU C CA  
4994  C  C   . LEU C  72  ? 0.2077 0.2454 0.2635 -0.0197 -0.0898 0.0208  72  LEU C C   
4995  O  O   . LEU C  72  ? 0.2364 0.3240 0.1782 -0.0161 -0.0445 0.0192  72  LEU C O   
4996  C  CB  . LEU C  72  ? 0.2433 0.2985 0.1877 -0.0350 -0.1289 0.0340  72  LEU C CB  
4997  C  CG  . LEU C  72  ? 0.3005 0.3231 0.1795 -0.0873 -0.0987 0.0588  72  LEU C CG  
4998  C  CD1 . LEU C  72  ? 0.1834 0.4454 0.1726 -0.0483 -0.0732 0.0124  72  LEU C CD1 
4999  C  CD2 . LEU C  72  ? 0.2398 0.3855 0.2585 -0.0434 -0.0619 0.0727  72  LEU C CD2 
5000  N  N   . PRO C  73  ? 0.3052 0.2431 0.2158 0.0304  -0.0331 0.0230  73  PRO C N   
5001  C  CA  . PRO C  73  ? 0.2217 0.3941 0.2318 -0.0430 -0.0816 0.0423  73  PRO C CA  
5002  C  C   . PRO C  73  ? 0.1914 0.4641 0.2551 -0.0443 -0.0903 0.0458  73  PRO C C   
5003  O  O   . PRO C  73  ? 0.2711 0.3725 0.2251 -0.0003 -0.0595 0.0373  73  PRO C O   
5004  C  CB  . PRO C  73  ? 0.2860 0.3535 0.2561 -0.0494 -0.1102 0.0513  73  PRO C CB  
5005  C  CG  . PRO C  73  ? 0.2567 0.2518 0.3276 -0.0087 -0.1033 -0.0149 73  PRO C CG  
5006  C  CD  . PRO C  73  ? 0.2125 0.1944 0.3883 0.0207  -0.0668 -0.0082 73  PRO C CD  
5007  N  N   . SER C  74  ? 0.2924 0.5616 0.3718 -0.0196 -0.0640 0.2090  74  SER C N   
5008  C  CA  . SER C  74  ? 0.2229 0.4101 0.3853 -0.0206 -0.0692 0.1406  74  SER C CA  
5009  C  C   . SER C  74  ? 0.2518 0.5669 0.2330 -0.0759 -0.1098 0.0480  74  SER C C   
5010  O  O   . SER C  74  ? 0.2897 0.7106 0.2475 -0.0392 -0.1074 0.0368  74  SER C O   
5011  C  CB  . SER C  74  ? 0.3237 0.4735 0.4578 -0.0320 -0.0732 0.2301  74  SER C CB  
5012  O  OG  . SER C  74  ? 0.2524 0.7894 0.4906 -0.0228 -0.0599 0.1266  74  SER C OG  
5013  N  N   . ASP C  75  ? 0.2500 0.4451 0.3675 -0.1084 -0.1253 -0.0006 75  ASP C N   
5014  C  CA  . ASP C  75  ? 0.2908 0.3382 0.4708 0.0679  -0.1697 0.0124  75  ASP C CA  
5015  C  C   . ASP C  75  ? 0.3792 0.4657 0.3916 -0.0049 0.0575  0.1256  75  ASP C C   
5016  O  O   . ASP C  75  ? 0.1274 0.7006 0.3714 0.0458  -0.0635 -0.1015 75  ASP C O   
5017  C  CB  . ASP C  75  ? 0.3804 0.3102 0.2883 0.0370  -0.1006 0.0217  75  ASP C CB  
5018  C  CG  . ASP C  75  ? 0.1777 0.3984 0.3073 -0.0178 0.0671  -0.0178 75  ASP C CG  
5019  O  OD1 . ASP C  75  ? 0.3996 0.6542 0.3186 0.0842  0.0676  -0.1098 75  ASP C OD1 
5020  O  OD2 . ASP C  75  ? 0.4253 0.4590 0.6977 0.0351  -0.0241 0.0917  75  ASP C OD2 
5021  N  N   . MET C  76  ? 0.2319 0.2624 0.2680 0.0027  -0.0870 0.0074  76  MET C N   
5022  C  CA  . MET C  76  ? 0.2915 0.2872 0.1809 -0.0250 -0.0750 -0.0020 76  MET C CA  
5023  C  C   . MET C  76  ? 0.1744 0.3499 0.1982 0.0060  -0.0445 0.0262  76  MET C C   
5024  O  O   . MET C  76  ? 0.1515 0.3894 0.2179 0.0292  -0.0313 0.0154  76  MET C O   
5025  C  CB  . MET C  76  ? 0.2377 0.2628 0.2617 -0.0183 -0.0289 -0.0089 76  MET C CB  
5026  C  CG  . MET C  76  ? 0.2612 0.2612 0.2540 -0.0627 0.0461  -0.0017 76  MET C CG  
5027  S  SD  . MET C  76  ? 0.1910 0.3328 0.3113 -0.0031 0.0203  0.0292  76  MET C SD  
5028  C  CE  . MET C  76  ? 0.1574 0.3652 0.2687 0.0206  0.0124  0.0467  76  MET C CE  
5029  N  N   . HIS C  77  ? 0.1098 0.3607 0.2197 -0.0436 -0.0458 0.0419  77  HIS C N   
5030  C  CA  . HIS C  77  ? 0.1405 0.3736 0.2272 -0.0154 -0.0339 0.0157  77  HIS C CA  
5031  C  C   . HIS C  77  ? 0.1656 0.3402 0.1949 0.0146  -0.0357 0.0259  77  HIS C C   
5032  O  O   . HIS C  77  ? 0.1438 0.3481 0.2389 0.0229  -0.0245 0.0718  77  HIS C O   
5033  C  CB  . HIS C  77  ? 0.1134 0.4092 0.2664 -0.0299 0.0049  -0.0059 77  HIS C CB  
5034  C  CG  . HIS C  77  ? 0.1741 0.3713 0.1844 -0.0003 -0.0148 0.0156  77  HIS C CG  
5035  N  ND1 . HIS C  77  ? 0.1612 0.4450 0.2420 -0.0281 -0.0089 -0.0149 77  HIS C ND1 
5036  C  CD2 . HIS C  77  ? 0.1885 0.2644 0.2540 -0.0364 -0.0063 0.0000  77  HIS C CD2 
5037  C  CE1 . HIS C  77  ? 0.1259 0.3662 0.3571 0.0223  -0.0143 0.0942  77  HIS C CE1 
5038  N  NE2 . HIS C  77  ? 0.1258 0.4839 0.3826 -0.0573 0.0100  0.0342  77  HIS C NE2 
5039  N  N   . ILE C  78  ? 0.1725 0.2793 0.2203 -0.0010 -0.0538 0.0163  78  ILE C N   
5040  C  CA  . ILE C  78  ? 0.1836 0.2060 0.2079 -0.0020 -0.0028 0.0216  78  ILE C CA  
5041  C  C   . ILE C  78  ? 0.1583 0.2904 0.2485 0.0040  -0.0274 0.0436  78  ILE C C   
5042  O  O   . ILE C  78  ? 0.1967 0.2761 0.2317 -0.0370 0.0186  0.0074  78  ILE C O   
5043  C  CB  . ILE C  78  ? 0.1581 0.3203 0.1759 -0.0201 -0.0119 0.0027  78  ILE C CB  
5044  C  CG1 . ILE C  78  ? 0.1739 0.3758 0.1992 -0.0511 0.0230  0.0052  78  ILE C CG1 
5045  C  CG2 . ILE C  78  ? 0.2224 0.3061 0.2231 -0.0122 0.0102  -0.0110 78  ILE C CG2 
5046  C  CD1 . ILE C  78  ? 0.2027 0.2601 0.2111 -0.0046 0.0193  -0.0197 78  ILE C CD1 
5047  N  N   . GLN C  79  ? 0.1953 0.3314 0.2415 0.0303  0.0173  0.0060  79  GLN C N   
5048  C  CA  . GLN C  79  ? 0.2526 0.2967 0.3221 0.0795  0.0237  -0.0808 79  GLN C CA  
5049  C  C   . GLN C  79  ? 0.2397 0.2818 0.2779 0.0419  0.0529  0.0043  79  GLN C C   
5050  O  O   . GLN C  79  ? 0.2518 0.3379 0.3305 0.0520  0.0005  0.0627  79  GLN C O   
5051  C  CB  . GLN C  79  ? 0.2412 0.4185 0.4959 0.0835  0.0397  -0.0676 79  GLN C CB  
5052  N  N   . GLY C  80  ? 0.2793 0.3833 0.2472 -0.0284 0.0812  -0.0013 80  GLY C N   
5053  C  CA  . GLY C  80  ? 0.2019 0.4773 0.3147 0.0127  0.0588  -0.0456 80  GLY C CA  
5054  C  C   . GLY C  80  ? 0.3082 0.4305 0.1836 0.0449  0.0935  -0.0810 80  GLY C C   
5055  O  O   . GLY C  80  ? 0.2806 0.4234 0.2745 -0.0115 0.0644  -0.1185 80  GLY C O   
5056  N  N   . LEU C  81  ? 0.2470 0.2946 0.2161 -0.0302 0.0546  -0.0121 81  LEU C N   
5057  C  CA  . LEU C  81  ? 0.2372 0.3025 0.1942 -0.0307 0.0546  -0.0174 81  LEU C CA  
5058  C  C   . LEU C  81  ? 0.2552 0.2784 0.1674 0.0043  0.0540  -0.0555 81  LEU C C   
5059  O  O   . LEU C  81  ? 0.2712 0.3607 0.2518 -0.0019 0.1000  -0.0392 81  LEU C O   
5060  C  CB  . LEU C  81  ? 0.2486 0.2466 0.1590 -0.0772 0.0458  -0.0129 81  LEU C CB  
5061  C  CG  . LEU C  81  ? 0.2264 0.2391 0.2055 -0.0719 0.0302  0.0210  81  LEU C CG  
5062  C  CD1 . LEU C  81  ? 0.2867 0.2969 0.1948 -0.0724 0.0753  -0.0211 81  LEU C CD1 
5063  C  CD2 . LEU C  81  ? 0.2406 0.1967 0.3102 -0.0362 -0.0008 -0.0351 81  LEU C CD2 
5064  N  N   . GLN C  82  ? 0.2899 0.3249 0.1382 0.0126  0.0162  -0.0003 82  GLN C N   
5065  C  CA  . GLN C  82  ? 0.3607 0.3088 0.2393 0.0135  0.1008  0.0013  82  GLN C CA  
5066  C  C   . GLN C  82  ? 0.3145 0.3459 0.1473 0.0154  0.0560  0.0277  82  GLN C C   
5067  O  O   . GLN C  82  ? 0.5137 0.3474 0.2125 -0.0423 0.1459  -0.0065 82  GLN C O   
5068  C  CB  . GLN C  82  ? 0.4550 0.4192 0.2728 0.1645  0.1143  0.0847  82  GLN C CB  
5069  N  N   . SER C  83  ? 0.2202 0.2649 0.1805 -0.0133 0.0615  0.0000  83  SER C N   
5070  C  CA  . SER C  83  ? 0.2097 0.2612 0.1642 -0.0121 0.0254  0.0126  83  SER C CA  
5071  C  C   . SER C  83  ? 0.1692 0.2230 0.1908 -0.0362 0.0406  -0.0271 83  SER C C   
5072  O  O   . SER C  83  ? 0.1430 0.2044 0.1847 -0.0220 0.0197  0.0015  83  SER C O   
5073  C  CB  . SER C  83  ? 0.2529 0.2741 0.2284 0.0242  0.0185  0.0041  83  SER C CB  
5074  O  OG  . SER C  83  ? 0.3623 0.3294 0.2287 0.0286  0.0637  0.0419  83  SER C OG  
5075  N  N   . ARG C  84  ? 0.1701 0.2055 0.1797 -0.0237 0.0328  -0.0130 84  ARG C N   
5076  C  CA  . ARG C  84  ? 0.1265 0.1978 0.2276 -0.0197 0.0240  -0.0017 84  ARG C CA  
5077  C  C   . ARG C  84  ? 0.1181 0.2096 0.1824 0.0017  0.0005  0.0226  84  ARG C C   
5078  O  O   . ARG C  84  ? 0.1094 0.2355 0.2108 -0.0126 0.0186  0.0232  84  ARG C O   
5079  C  CB  . ARG C  84  ? 0.1188 0.2928 0.2644 -0.0355 0.0208  -0.0057 84  ARG C CB  
5080  C  CG  . ARG C  84  ? 0.1138 0.2384 0.2896 -0.0182 -0.0041 0.0006  84  ARG C CG  
5081  C  CD  . ARG C  84  ? 0.0961 0.2642 0.3664 -0.0165 0.0120  -0.0017 84  ARG C CD  
5082  N  NE  . ARG C  84  ? 0.1267 0.2748 0.2912 0.0245  0.0196  0.0303  84  ARG C NE  
5083  C  CZ  . ARG C  84  ? 0.1165 0.3598 0.2511 0.0168  0.0340  0.0193  84  ARG C CZ  
5084  N  NH1 . ARG C  84  ? 0.1585 0.3876 0.3346 0.0292  -0.0003 -0.0142 84  ARG C NH1 
5085  N  NH2 . ARG C  84  ? 0.1448 0.3201 0.3562 0.0474  0.0478  0.0771  84  ARG C NH2 
5086  N  N   . TYR C  85  ? 0.1154 0.2630 0.1709 -0.0138 -0.0031 0.0125  85  TYR C N   
5087  C  CA  . TYR C  85  ? 0.1127 0.2615 0.1553 -0.0216 -0.0052 0.0068  85  TYR C CA  
5088  C  C   . TYR C  85  ? 0.1261 0.2788 0.1466 -0.0074 0.0129  0.0239  85  TYR C C   
5089  O  O   . TYR C  85  ? 0.1700 0.2689 0.2066 -0.0171 -0.0496 0.0502  85  TYR C O   
5090  C  CB  . TYR C  85  ? 0.1132 0.3248 0.1317 -0.0381 -0.0007 0.0087  85  TYR C CB  
5091  C  CG  . TYR C  85  ? 0.1125 0.2157 0.1285 -0.0419 0.0091  -0.0038 85  TYR C CG  
5092  C  CD1 . TYR C  85  ? 0.1246 0.2231 0.1463 -0.0293 0.0242  -0.0178 85  TYR C CD1 
5093  C  CD2 . TYR C  85  ? 0.0958 0.2084 0.1734 -0.0192 0.0063  -0.0208 85  TYR C CD2 
5094  C  CE1 . TYR C  85  ? 0.1190 0.2124 0.1563 -0.0428 0.0248  -0.0008 85  TYR C CE1 
5095  C  CE2 . TYR C  85  ? 0.1195 0.2305 0.1405 -0.0060 0.0138  -0.0068 85  TYR C CE2 
5096  C  CZ  . TYR C  85  ? 0.1228 0.2152 0.1438 -0.0275 0.0173  -0.0183 85  TYR C CZ  
5097  O  OH  . TYR C  85  ? 0.1960 0.2549 0.1418 -0.0098 -0.0153 0.0207  85  TYR C OH  
5098  N  N   . SER C  86  ? 0.1215 0.2723 0.1712 -0.0188 -0.0166 0.0118  86  SER C N   
5099  C  CA  . SER C  86  ? 0.1163 0.3057 0.1814 -0.0269 -0.0441 -0.0127 86  SER C CA  
5100  C  C   . SER C  86  ? 0.1635 0.2021 0.1759 0.0164  -0.0219 -0.0028 86  SER C C   
5101  O  O   . SER C  86  ? 0.1414 0.2414 0.1867 -0.0329 -0.0267 0.0196  86  SER C O   
5102  C  CB  . SER C  86  ? 0.1332 0.3874 0.2389 -0.0825 -0.0159 0.0109  86  SER C CB  
5103  O  OG  . SER C  86  ? 0.1253 0.4049 0.2479 -0.0445 -0.0010 0.0394  86  SER C OG  
5104  N  N   . ALA C  87  ? 0.1269 0.3355 0.1904 -0.0412 -0.0228 0.0326  87  ALA C N   
5105  C  CA  . ALA C  87  ? 0.1360 0.1962 0.2129 -0.0003 -0.0164 0.0037  87  ALA C CA  
5106  C  C   . ALA C  87  ? 0.1870 0.2705 0.1791 0.0253  -0.0671 -0.0684 87  ALA C C   
5107  O  O   . ALA C  87  ? 0.1813 0.2705 0.2075 -0.0419 -0.0240 -0.0344 87  ALA C O   
5108  C  CB  . ALA C  87  ? 0.2134 0.3470 0.2005 -0.0214 -0.0368 0.0648  87  ALA C CB  
5109  N  N   . THR C  88  ? 0.1554 0.1766 0.2170 -0.0087 -0.0126 0.0186  88  THR C N   
5110  C  CA  . THR C  88  ? 0.1815 0.2197 0.2161 -0.0250 -0.0346 -0.0185 88  THR C CA  
5111  C  C   . THR C  88  ? 0.1789 0.1956 0.1617 -0.0220 -0.0540 -0.0007 88  THR C C   
5112  O  O   . THR C  88  ? 0.1976 0.2382 0.1852 -0.0527 -0.0604 0.0034  88  THR C O   
5113  C  CB  . THR C  88  ? 0.1870 0.1868 0.2027 -0.0271 0.0152  -0.0043 88  THR C CB  
5114  O  OG1 . THR C  88  ? 0.2495 0.2687 0.1759 -0.0449 -0.0149 -0.0471 88  THR C OG1 
5115  C  CG2 . THR C  88  ? 0.1782 0.2335 0.1827 -0.0447 -0.0035 0.0024  88  THR C CG2 
5116  N  N   . GLN C  89  ? 0.1890 0.2949 0.1247 -0.0573 -0.0142 -0.0044 89  GLN C N   
5117  C  CA  . GLN C  89  ? 0.1660 0.2388 0.1687 -0.0351 -0.0640 0.0049  89  GLN C CA  
5118  C  C   . GLN C  89  ? 0.2070 0.2824 0.1254 -0.0584 -0.0392 -0.0219 89  GLN C C   
5119  O  O   . GLN C  89  ? 0.1632 0.2878 0.1084 -0.0399 -0.0240 -0.0133 89  GLN C O   
5120  C  CB  . GLN C  89  ? 0.2278 0.2319 0.2310 0.0240  -0.0060 0.0296  89  GLN C CB  
5121  C  CG  . GLN C  89  ? 0.2142 0.3327 0.1619 -0.0494 -0.0216 -0.0156 89  GLN C CG  
5122  C  CD  . GLN C  89  ? 0.2109 0.2696 0.1170 -0.0900 -0.0020 -0.0256 89  GLN C CD  
5123  O  OE1 . GLN C  89  ? 0.2342 0.3533 0.1768 -0.1125 -0.0277 0.0410  89  GLN C OE1 
5124  N  NE2 . GLN C  89  ? 0.4393 0.5044 0.1416 0.0759  -0.0175 -0.1058 89  GLN C NE2 
5125  N  N   . LEU C  90  ? 0.1714 0.3380 0.1238 -0.0527 -0.0518 0.0177  90  LEU C N   
5126  C  CA  . LEU C  90  ? 0.1500 0.2409 0.1631 -0.0206 -0.0209 0.0310  90  LEU C CA  
5127  C  C   . LEU C  90  ? 0.2063 0.2513 0.1027 -0.0302 -0.0447 0.0425  90  LEU C C   
5128  O  O   . LEU C  90  ? 0.2290 0.3109 0.1050 -0.0728 -0.0401 0.0178  90  LEU C O   
5129  C  CB  . LEU C  90  ? 0.1599 0.2466 0.1023 0.0010  -0.0230 0.0031  90  LEU C CB  
5130  C  CG  . LEU C  90  ? 0.2696 0.1793 0.1597 0.0046  -0.0709 0.0223  90  LEU C CG  
5131  C  CD1 . LEU C  90  ? 0.2590 0.3837 0.1164 -0.0423 -0.0662 0.0714  90  LEU C CD1 
5132  C  CD2 . LEU C  90  ? 0.2955 0.1861 0.1517 0.0144  -0.1124 0.0160  90  LEU C CD2 
5133  N  N   . HIS C  91  ? 0.1718 0.3431 0.1028 -0.0540 -0.0131 -0.0083 91  HIS C N   
5134  C  CA  . HIS C  91  ? 0.1721 0.2721 0.0663 -0.0575 -0.0176 -0.0063 91  HIS C CA  
5135  C  C   . HIS C  91  ? 0.2361 0.3249 0.0459 -0.0983 -0.0103 0.0304  91  HIS C C   
5136  O  O   . HIS C  91  ? 0.1966 0.3413 0.0820 -0.0582 -0.0243 0.0046  91  HIS C O   
5137  C  CB  . HIS C  91  ? 0.2090 0.2745 0.0935 -0.0450 -0.0269 0.0377  91  HIS C CB  
5138  C  CG  . HIS C  91  ? 0.2043 0.2901 0.0811 -0.0819 -0.0207 -0.0006 91  HIS C CG  
5139  N  ND1 . HIS C  91  ? 0.2360 0.2554 0.0728 -0.0701 0.0000  0.0157  91  HIS C ND1 
5140  C  CD2 . HIS C  91  ? 0.1791 0.2499 0.0741 -0.0414 -0.0261 0.0035  91  HIS C CD2 
5141  C  CE1 . HIS C  91  ? 0.1881 0.2305 0.1018 -0.0625 -0.0063 0.0020  91  HIS C CE1 
5142  N  NE2 . HIS C  91  ? 0.1826 0.2402 0.0706 -0.0329 -0.0265 -0.0062 91  HIS C NE2 
5143  N  N   . LEU C  92  ? 0.1674 0.3176 0.0843 -0.0478 -0.0303 0.0216  92  LEU C N   
5144  C  CA  . LEU C  92  ? 0.2069 0.3149 0.0863 -0.0632 -0.0163 0.0277  92  LEU C CA  
5145  C  C   . LEU C  92  ? 0.1621 0.2736 0.0781 -0.0511 0.0074  0.0315  92  LEU C C   
5146  O  O   . LEU C  92  ? 0.2224 0.3055 0.1005 -0.0649 -0.0073 -0.0035 92  LEU C O   
5147  C  CB  . LEU C  92  ? 0.1999 0.4068 0.1662 -0.0265 -0.0093 0.1010  92  LEU C CB  
5148  C  CG  . LEU C  92  ? 0.2432 0.3492 0.1337 -0.0164 -0.0100 0.1076  92  LEU C CG  
5149  C  CD1 . LEU C  92  ? 0.2648 0.5687 0.1847 -0.0469 -0.0480 0.0546  92  LEU C CD1 
5150  C  CD2 . LEU C  92  ? 0.2064 0.3316 0.2538 0.0024  0.0098  0.0049  92  LEU C CD2 
5151  N  N   . HIS C  93  ? 0.2017 0.2926 0.0571 -0.0685 0.0031  -0.0017 93  HIS C N   
5152  C  CA  . HIS C  93  ? 0.1791 0.2955 0.0733 -0.0630 0.0083  0.0281  93  HIS C CA  
5153  C  C   . HIS C  93  ? 0.1935 0.2492 0.0560 -0.0394 -0.0155 0.0133  93  HIS C C   
5154  O  O   . HIS C  93  ? 0.2071 0.2867 0.0728 -0.0640 0.0027  0.0143  93  HIS C O   
5155  C  CB  . HIS C  93  ? 0.1802 0.2545 0.0683 -0.0593 -0.0048 0.0300  93  HIS C CB  
5156  C  CG  . HIS C  93  ? 0.1509 0.2359 0.0599 -0.0340 -0.0043 0.0137  93  HIS C CG  
5157  N  ND1 . HIS C  93  ? 0.1897 0.2424 0.0897 -0.0469 0.0098  -0.0024 93  HIS C ND1 
5158  C  CD2 . HIS C  93  ? 0.1721 0.2127 0.0577 -0.0333 -0.0174 -0.0021 93  HIS C CD2 
5159  C  CE1 . HIS C  93  ? 0.1694 0.2332 0.0730 -0.0518 0.0157  -0.0285 93  HIS C CE1 
5160  N  NE2 . HIS C  93  ? 0.1782 0.2118 0.0678 -0.0454 0.0052  -0.0010 93  HIS C NE2 
5161  N  N   . TRP C  94  ? 0.1779 0.2468 0.0696 -0.0456 -0.0076 0.0166  94  TRP C N   
5162  C  CA  . TRP C  94  ? 0.1850 0.2660 0.0994 -0.0384 -0.0103 0.0346  94  TRP C CA  
5163  C  C   . TRP C  94  ? 0.2452 0.2917 0.0681 -0.0362 -0.0055 0.0403  94  TRP C C   
5164  O  O   . TRP C  94  ? 0.1674 0.2759 0.0778 -0.0395 0.0244  -0.0003 94  TRP C O   
5165  C  CB  . TRP C  94  ? 0.2700 0.3219 0.0790 -0.0802 -0.0250 0.0566  94  TRP C CB  
5166  C  CG  . TRP C  94  ? 0.2418 0.3768 0.0538 -0.0758 0.0037  0.0263  94  TRP C CG  
5167  C  CD1 . TRP C  94  ? 0.2319 0.3655 0.0839 -0.0322 -0.0094 -0.0091 94  TRP C CD1 
5168  C  CD2 . TRP C  94  ? 0.2802 0.4083 0.0544 -0.1298 -0.0315 0.0410  94  TRP C CD2 
5169  N  NE1 . TRP C  94  ? 0.2511 0.4167 0.0656 -0.0947 0.0001  0.0176  94  TRP C NE1 
5170  C  CE2 . TRP C  94  ? 0.2888 0.4212 0.0395 -0.1090 0.0031  0.0306  94  TRP C CE2 
5171  C  CE3 . TRP C  94  ? 0.2678 0.3531 0.0618 -0.0807 -0.0186 0.0408  94  TRP C CE3 
5172  C  CZ2 . TRP C  94  ? 0.2477 0.4343 0.1080 -0.0878 -0.0372 0.0115  94  TRP C CZ2 
5173  C  CZ3 . TRP C  94  ? 0.1958 0.4385 0.1206 -0.1008 -0.0515 0.0538  94  TRP C CZ3 
5174  C  CH2 . TRP C  94  ? 0.2599 0.4255 0.1106 -0.1162 -0.0284 0.0480  94  TRP C CH2 
5175  N  N   . GLY C  95  ? 0.1739 0.2509 0.0909 -0.0329 0.0211  0.0172  95  GLY C N   
5176  C  CA  . GLY C  95  ? 0.1920 0.2834 0.0847 -0.0017 0.0267  -0.0098 95  GLY C CA  
5177  C  C   . GLY C  95  ? 0.1908 0.2955 0.0834 -0.0456 0.0163  0.0000  95  GLY C C   
5178  O  O   . GLY C  95  ? 0.2508 0.3167 0.0780 -0.0745 0.0238  0.0006  95  GLY C O   
5179  N  N   . ASN C  96  ? 0.2759 0.2958 0.0883 -0.0438 0.0405  0.0110  96  ASN C N   
5180  C  CA  . ASN C  96  ? 0.2732 0.3454 0.0809 -0.0617 0.0564  0.0154  96  ASN C CA  
5181  C  C   . ASN C  96  ? 0.2407 0.3458 0.0872 -0.0483 0.0175  -0.0052 96  ASN C C   
5182  O  O   . ASN C  96  ? 0.2784 0.2912 0.0952 -0.0701 0.0252  0.0209  96  ASN C O   
5183  C  CB  . ASN C  96  ? 0.3030 0.3670 0.1161 -0.0693 0.0456  -0.0109 96  ASN C CB  
5184  C  CG  . ASN C  96  ? 0.2716 0.4217 0.1761 -0.0270 0.1150  0.0081  96  ASN C CG  
5185  O  OD1 . ASN C  96  ? 0.3777 0.3903 0.2655 -0.0315 0.1932  0.0261  96  ASN C OD1 
5186  N  ND2 . ASN C  96  ? 0.3698 0.3298 0.1935 -0.0099 0.0965  -0.0381 96  ASN C ND2 
5187  N  N   . PRO C  97  ? 0.3131 0.4314 0.0921 -0.1137 0.0240  0.0165  97  PRO C N   
5188  C  CA  . PRO C  97  ? 0.2984 0.4727 0.1307 -0.0784 0.0247  0.0513  97  PRO C CA  
5189  C  C   . PRO C  97  ? 0.3129 0.3296 0.1141 -0.0882 0.0636  -0.0010 97  PRO C C   
5190  O  O   . PRO C  97  ? 0.3222 0.3551 0.1588 -0.0553 0.0298  0.0612  97  PRO C O   
5191  C  CB  . PRO C  97  ? 0.4113 0.5357 0.1216 -0.1415 -0.0093 0.1027  97  PRO C CB  
5192  C  CG  . PRO C  97  ? 0.3890 0.4645 0.1075 -0.1251 -0.0104 0.0432  97  PRO C CG  
5193  C  CD  . PRO C  97  ? 0.3677 0.4375 0.0772 -0.1328 0.0144  0.0165  97  PRO C CD  
5194  N  N   . ASN C  98  ? 0.2504 0.4025 0.1249 -0.0573 0.0754  0.0149  98  ASN C N   
5195  C  CA  . ASN C  98  ? 0.2712 0.4670 0.1473 -0.0571 0.0813  -0.0529 98  ASN C CA  
5196  C  C   . ASN C  98  ? 0.2840 0.3404 0.1272 -0.0299 0.0515  0.0238  98  ASN C C   
5197  O  O   . ASN C  98  ? 0.2536 0.4857 0.1617 -0.1032 0.0643  -0.0148 98  ASN C O   
5198  C  CB  . ASN C  98  ? 0.2494 0.4591 0.2120 -0.0362 0.0952  -0.0728 98  ASN C CB  
5199  C  CG  . ASN C  98  ? 0.6353 0.6683 0.3019 0.0724  0.0472  -0.1788 98  ASN C CG  
5200  O  OD1 . ASN C  98  ? 0.5958 0.8730 0.2060 -0.1630 0.2106  -0.0460 98  ASN C OD1 
5201  N  ND2 . ASN C  98  ? 0.9900 0.7968 0.5335 -0.0342 0.1071  -0.3120 98  ASN C ND2 
5202  N  N   . ASP C  99  ? 0.2737 0.3860 0.1127 -0.0593 0.0513  0.0031  99  ASP C N   
5203  C  CA  . ASP C  99  ? 0.2379 0.3244 0.1102 -0.0186 0.0289  -0.0181 99  ASP C CA  
5204  C  C   . ASP C  99  ? 0.2149 0.2725 0.1127 -0.0542 0.0253  0.0168  99  ASP C C   
5205  O  O   . ASP C  99  ? 0.2960 0.3106 0.1061 -0.0582 0.0284  0.0318  99  ASP C O   
5206  C  CB  . ASP C  99  ? 0.2369 0.3098 0.1315 -0.0059 0.0406  -0.0223 99  ASP C CB  
5207  C  CG  . ASP C  99  ? 0.2933 0.3402 0.1235 -0.0065 0.0690  0.0114  99  ASP C CG  
5208  O  OD1 . ASP C  99  ? 0.4314 0.3296 0.1353 -0.0131 0.0054  -0.0197 99  ASP C OD1 
5209  O  OD2 . ASP C  99  ? 0.3977 0.2919 0.2199 0.0715  -0.0379 -0.0546 99  ASP C OD2 
5210  N  N   . PRO C  100 ? 0.2727 0.2725 0.1030 -0.0430 0.0425  0.0229  100 PRO C N   
5211  C  CA  . PRO C  100 ? 0.2748 0.3971 0.1112 -0.0406 0.0245  0.0675  100 PRO C CA  
5212  C  C   . PRO C  100 ? 0.2357 0.2702 0.1331 -0.0423 0.0675  0.0498  100 PRO C C   
5213  O  O   . PRO C  100 ? 0.2463 0.3177 0.1337 -0.0222 0.0406  0.0834  100 PRO C O   
5214  C  CB  . PRO C  100 ? 0.2354 0.3434 0.1474 -0.0662 0.0425  0.0662  100 PRO C CB  
5215  C  CG  . PRO C  100 ? 0.2761 0.3264 0.2059 -0.0392 0.0114  0.1229  100 PRO C CG  
5216  C  CD  . PRO C  100 ? 0.2705 0.2946 0.0863 -0.0461 0.0438  0.0401  100 PRO C CD  
5217  N  N   . HIS C  101 ? 0.2194 0.2312 0.1076 -0.0586 0.0170  0.0274  101 HIS C N   
5218  C  CA  . HIS C  101 ? 0.2142 0.2829 0.0864 -0.0526 0.0318  0.0264  101 HIS C CA  
5219  C  C   . HIS C  101 ? 0.2057 0.3285 0.1125 -0.0515 0.0249  0.0698  101 HIS C C   
5220  O  O   . HIS C  101 ? 0.2231 0.2499 0.2303 -0.0476 -0.0164 0.0469  101 HIS C O   
5221  C  CB  . HIS C  101 ? 0.2720 0.3273 0.1027 -0.1248 0.0425  0.0186  101 HIS C CB  
5222  C  CG  . HIS C  101 ? 0.2727 0.2879 0.1389 -0.0800 0.0500  0.0146  101 HIS C CG  
5223  N  ND1 . HIS C  101 ? 0.2558 0.2766 0.2167 -0.0656 0.0719  0.0023  101 HIS C ND1 
5224  C  CD2 . HIS C  101 ? 0.2754 0.2879 0.1676 -0.0366 0.0772  0.0644  101 HIS C CD2 
5225  C  CE1 . HIS C  101 ? 0.2477 0.2698 0.2642 -0.0361 0.0522  0.0031  101 HIS C CE1 
5226  N  NE2 . HIS C  101 ? 0.2985 0.2425 0.1502 -0.0228 0.0856  0.0538  101 HIS C NE2 
5227  N  N   . GLY C  102 ? 0.1802 0.2544 0.0915 -0.0335 0.0241  0.0178  102 GLY C N   
5228  C  CA  . GLY C  102 ? 0.2187 0.2061 0.0836 -0.0109 0.0489  0.0059  102 GLY C CA  
5229  C  C   . GLY C  102 ? 0.1554 0.2104 0.0648 -0.0076 0.0120  0.0172  102 GLY C C   
5230  O  O   . GLY C  102 ? 0.1924 0.2199 0.1019 -0.0276 0.0359  0.0167  102 GLY C O   
5231  N  N   . SER C  103 ? 0.1615 0.2172 0.0701 -0.0003 0.0137  0.0172  103 SER C N   
5232  C  CA  . SER C  103 ? 0.1920 0.2188 0.0553 -0.0217 0.0156  0.0377  103 SER C CA  
5233  C  C   . SER C  103 ? 0.1660 0.1757 0.0644 -0.0368 0.0114  0.0201  103 SER C C   
5234  O  O   . SER C  103 ? 0.1568 0.1912 0.0982 -0.0173 0.0278  0.0544  103 SER C O   
5235  C  CB  . SER C  103 ? 0.1753 0.1603 0.1120 -0.0206 -0.0017 0.0331  103 SER C CB  
5236  O  OG  . SER C  103 ? 0.1583 0.1779 0.0834 -0.0144 0.0148  0.0298  103 SER C OG  
5237  N  N   . GLU C  104 ? 0.1385 0.1509 0.0692 -0.0182 0.0155  0.0241  104 GLU C N   
5238  C  CA  . GLU C  104 ? 0.1532 0.1298 0.0744 -0.0185 -0.0111 0.0153  104 GLU C CA  
5239  C  C   . GLU C  104 ? 0.1310 0.1159 0.0746 -0.0028 0.0160  0.0135  104 GLU C C   
5240  O  O   . GLU C  104 ? 0.1247 0.1229 0.0790 0.0066  0.0099  0.0003  104 GLU C O   
5241  C  CB  . GLU C  104 ? 0.1658 0.1687 0.0721 -0.0467 -0.0115 0.0093  104 GLU C CB  
5242  C  CG  . GLU C  104 ? 0.1712 0.1897 0.0856 -0.0582 0.0115  -0.0049 104 GLU C CG  
5243  C  CD  . GLU C  104 ? 0.1369 0.1709 0.0836 -0.0434 0.0062  -0.0043 104 GLU C CD  
5244  O  OE1 . GLU C  104 ? 0.1579 0.1375 0.0960 -0.0184 0.0104  0.0087  104 GLU C OE1 
5245  O  OE2 . GLU C  104 ? 0.1509 0.1748 0.1243 -0.0142 0.0239  -0.0087 104 GLU C OE2 
5246  N  N   . HIS C  105 ? 0.1143 0.1272 0.0773 -0.0046 0.0186  0.0081  105 HIS C N   
5247  C  CA  . HIS C  105 ? 0.1238 0.1124 0.0596 -0.0144 0.0110  0.0034  105 HIS C CA  
5248  C  C   . HIS C  105 ? 0.1225 0.1098 0.0736 -0.0010 0.0131  0.0185  105 HIS C C   
5249  O  O   . HIS C  105 ? 0.1545 0.1515 0.0815 -0.0055 0.0086  0.0350  105 HIS C O   
5250  C  CB  . HIS C  105 ? 0.0969 0.1199 0.1181 -0.0074 0.0130  0.0190  105 HIS C CB  
5251  C  CG  . HIS C  105 ? 0.1123 0.1077 0.0815 0.0035  0.0203  0.0024  105 HIS C CG  
5252  N  ND1 . HIS C  105 ? 0.1098 0.1301 0.0988 -0.0168 0.0190  0.0003  105 HIS C ND1 
5253  C  CD2 . HIS C  105 ? 0.1037 0.1084 0.0931 -0.0060 0.0189  0.0252  105 HIS C CD2 
5254  C  CE1 . HIS C  105 ? 0.1412 0.1359 0.0724 -0.0060 0.0129  0.0063  105 HIS C CE1 
5255  N  NE2 . HIS C  105 ? 0.1143 0.1242 0.0841 0.0010  0.0109  0.0147  105 HIS C NE2 
5256  N  N   . THR C  106 ? 0.1199 0.1008 0.0802 -0.0001 0.0104  0.0121  106 THR C N   
5257  C  CA  . THR C  106 ? 0.1290 0.1003 0.1050 -0.0088 0.0295  0.0199  106 THR C CA  
5258  C  C   . THR C  106 ? 0.1234 0.1125 0.0803 -0.0035 0.0168  0.0104  106 THR C C   
5259  O  O   . THR C  106 ? 0.1335 0.1003 0.0967 0.0048  0.0174  0.0146  106 THR C O   
5260  C  CB  . THR C  106 ? 0.1222 0.1502 0.0910 0.0035  0.0284  0.0186  106 THR C CB  
5261  O  OG1 . THR C  106 ? 0.1173 0.1091 0.1152 0.0065  0.0157  0.0165  106 THR C OG1 
5262  C  CG2 . THR C  106 ? 0.1454 0.1712 0.1161 0.0282  0.0439  0.0141  106 THR C CG2 
5263  N  N   . VAL C  107 ? 0.1395 0.0992 0.1165 0.0031  0.0165  0.0076  107 VAL C N   
5264  C  CA  . VAL C  107 ? 0.1344 0.0958 0.1209 0.0060  0.0099  -0.0012 107 VAL C CA  
5265  C  C   . VAL C  107 ? 0.1321 0.0784 0.1335 0.0000  0.0195  0.0013  107 VAL C C   
5266  O  O   . VAL C  107 ? 0.1518 0.1107 0.1475 0.0005  0.0250  0.0252  107 VAL C O   
5267  C  CB  . VAL C  107 ? 0.1319 0.1152 0.1735 0.0148  0.0103  0.0057  107 VAL C CB  
5268  C  CG1 . VAL C  107 ? 0.1860 0.1116 0.2032 0.0273  0.0223  0.0023  107 VAL C CG1 
5269  C  CG2 . VAL C  107 ? 0.1281 0.1933 0.1718 0.0104  0.0196  0.0370  107 VAL C CG2 
5270  N  N   . SER C  108 ? 0.1335 0.1184 0.1360 -0.0017 0.0043  -0.0126 108 SER C N   
5271  C  CA  . SER C  108 ? 0.1574 0.1386 0.1416 -0.0205 0.0147  -0.0104 108 SER C CA  
5272  C  C   . SER C  108 ? 0.1400 0.1402 0.1149 -0.0170 0.0175  -0.0046 108 SER C C   
5273  O  O   . SER C  108 ? 0.1518 0.1353 0.1917 -0.0296 0.0326  0.0115  108 SER C O   
5274  C  CB  . SER C  108 ? 0.2005 0.1281 0.2151 -0.0020 0.0256  -0.0281 108 SER C CB  
5275  O  OG  . SER C  108 ? 0.2285 0.1748 0.3495 -0.0359 0.0940  -0.0461 108 SER C OG  
5276  N  N   . GLY C  109 ? 0.1326 0.1134 0.1380 -0.0007 0.0110  0.0017  109 GLY C N   
5277  C  CA  . GLY C  109 ? 0.1621 0.1407 0.1133 0.0071  0.0164  -0.0027 109 GLY C CA  
5278  C  C   . GLY C  109 ? 0.1316 0.1635 0.1448 0.0040  0.0285  0.0063  109 GLY C C   
5279  O  O   . GLY C  109 ? 0.1863 0.1714 0.1479 0.0260  0.0236  -0.0001 109 GLY C O   
5280  N  N   . GLN C  110 ? 0.1508 0.1256 0.1215 -0.0060 0.0189  0.0179  110 GLN C N   
5281  C  CA  . GLN C  110 ? 0.1823 0.1368 0.1371 -0.0065 0.0052  0.0265  110 GLN C CA  
5282  C  C   . GLN C  110 ? 0.1447 0.1439 0.1033 0.0043  0.0209  0.0333  110 GLN C C   
5283  O  O   . GLN C  110 ? 0.1474 0.1321 0.1140 0.0070  0.0315  0.0269  110 GLN C O   
5284  C  CB  . GLN C  110 ? 0.1894 0.1378 0.1741 -0.0124 -0.0082 0.0538  110 GLN C CB  
5285  C  CG  . GLN C  110 ? 0.1922 0.1299 0.2373 -0.0089 0.0088  0.0144  110 GLN C CG  
5286  C  CD  . GLN C  110 ? 0.2045 0.1563 0.2077 0.0310  0.0428  0.0240  110 GLN C CD  
5287  O  OE1 . GLN C  110 ? 0.2608 0.2251 0.2497 0.0189  0.0359  0.0557  110 GLN C OE1 
5288  N  NE2 . GLN C  110 ? 0.1705 0.1687 0.2023 -0.0083 0.0546  0.0529  110 GLN C NE2 
5289  N  N   . HIS C  111 ? 0.1531 0.1911 0.0918 -0.0003 0.0284  0.0331  111 HIS C N   
5290  C  CA  . HIS C  111 ? 0.1852 0.1753 0.1091 -0.0110 -0.0125 0.0340  111 HIS C CA  
5291  C  C   . HIS C  111 ? 0.1989 0.1915 0.1462 -0.0278 0.0030  0.0766  111 HIS C C   
5292  O  O   . HIS C  111 ? 0.2179 0.2626 0.2705 -0.0627 -0.0452 0.1534  111 HIS C O   
5293  C  CB  . HIS C  111 ? 0.2321 0.1976 0.1441 -0.0562 0.0485  0.0259  111 HIS C CB  
5294  C  CG  . HIS C  111 ? 0.1883 0.1787 0.1292 -0.0342 0.0351  -0.0017 111 HIS C CG  
5295  N  ND1 . HIS C  111 ? 0.1884 0.1905 0.1423 -0.0159 0.0527  -0.0362 111 HIS C ND1 
5296  C  CD2 . HIS C  111 ? 0.1671 0.1553 0.2424 0.0175  0.0538  -0.0258 111 HIS C CD2 
5297  C  CE1 . HIS C  111 ? 0.1746 0.1723 0.2246 0.0006  0.0817  -0.0190 111 HIS C CE1 
5298  N  NE2 . HIS C  111 ? 0.1962 0.1646 0.3276 0.0207  0.0838  -0.0035 111 HIS C NE2 
5299  N  N   . PHE C  112 ? 0.1838 0.1682 0.1100 -0.0116 0.0087  0.0472  112 PHE C N   
5300  C  CA  . PHE C  112 ? 0.2190 0.2159 0.0983 0.0124  0.0035  0.0632  112 PHE C CA  
5301  C  C   . PHE C  112 ? 0.2172 0.1958 0.1003 -0.0344 0.0041  0.0746  112 PHE C C   
5302  O  O   . PHE C  112 ? 0.2043 0.1951 0.1019 -0.0173 0.0027  0.0436  112 PHE C O   
5303  C  CB  . PHE C  112 ? 0.2053 0.2213 0.1301 -0.0081 0.0065  0.0631  112 PHE C CB  
5304  C  CG  . PHE C  112 ? 0.2057 0.2134 0.1556 -0.0232 0.0126  0.0337  112 PHE C CG  
5305  C  CD1 . PHE C  112 ? 0.2504 0.3097 0.1102 -0.0619 0.0077  0.0177  112 PHE C CD1 
5306  C  CD2 . PHE C  112 ? 0.2804 0.2271 0.2088 0.0270  0.1081  0.0542  112 PHE C CD2 
5307  C  CE1 . PHE C  112 ? 0.3343 0.3531 0.1876 -0.0785 0.0640  -0.0472 112 PHE C CE1 
5308  C  CE2 . PHE C  112 ? 0.2689 0.3023 0.3032 -0.0097 0.1500  -0.0447 112 PHE C CE2 
5309  C  CZ  . PHE C  112 ? 0.3921 0.3260 0.2725 -0.0740 0.1150  -0.0590 112 PHE C CZ  
5310  N  N   . ALA C  113 ? 0.1890 0.2678 0.0865 -0.0266 0.0013  0.0653  113 ALA C N   
5311  C  CA  . ALA C  113 ? 0.1976 0.2114 0.0809 -0.0088 0.0048  0.0518  113 ALA C CA  
5312  C  C   . ALA C  113 ? 0.1831 0.2633 0.1138 -0.0063 0.0020  0.0469  113 ALA C C   
5313  O  O   . ALA C  113 ? 0.2087 0.2709 0.0922 -0.0052 0.0226  0.0665  113 ALA C O   
5314  C  CB  . ALA C  113 ? 0.2377 0.2752 0.1274 -0.0118 -0.0469 0.0719  113 ALA C CB  
5315  N  N   . ALA C  114 ? 0.1883 0.2443 0.0926 -0.0188 0.0076  0.0639  114 ALA C N   
5316  C  CA  . ALA C  114 ? 0.2012 0.2552 0.0718 -0.0361 0.0041  0.0450  114 ALA C CA  
5317  C  C   . ALA C  114 ? 0.1946 0.2249 0.0535 -0.0030 -0.0023 0.0612  114 ALA C C   
5318  O  O   . ALA C  114 ? 0.1614 0.2439 0.1039 -0.0214 -0.0074 0.0509  114 ALA C O   
5319  C  CB  . ALA C  114 ? 0.2123 0.3244 0.0940 -0.0489 -0.0216 0.0447  114 ALA C CB  
5320  N  N   . GLU C  115 ? 0.1793 0.2518 0.0825 -0.0266 0.0129  0.0625  115 GLU C N   
5321  C  CA  . GLU C  115 ? 0.1623 0.2443 0.0751 -0.0286 -0.0082 0.0522  115 GLU C CA  
5322  C  C   . GLU C  115 ? 0.1563 0.2082 0.1256 -0.0109 -0.0263 0.0524  115 GLU C C   
5323  O  O   . GLU C  115 ? 0.1843 0.2309 0.1204 -0.0284 0.0017  0.0386  115 GLU C O   
5324  C  CB  . GLU C  115 ? 0.1527 0.2389 0.0780 -0.0017 0.0083  0.0472  115 GLU C CB  
5325  C  CG  . GLU C  115 ? 0.1396 0.2148 0.0710 0.0000  0.0038  0.0296  115 GLU C CG  
5326  C  CD  . GLU C  115 ? 0.1412 0.1768 0.0697 -0.0086 -0.0013 0.0057  115 GLU C CD  
5327  O  OE1 . GLU C  115 ? 0.1392 0.1714 0.0737 -0.0008 -0.0030 0.0060  115 GLU C OE1 
5328  O  OE2 . GLU C  115 ? 0.1367 0.1833 0.0786 -0.0131 0.0019  0.0250  115 GLU C OE2 
5329  N  N   . LEU C  116 ? 0.1396 0.2666 0.1037 -0.0115 -0.0162 0.0509  116 LEU C N   
5330  C  CA  . LEU C  116 ? 0.1395 0.3055 0.1001 -0.0261 -0.0296 0.0839  116 LEU C CA  
5331  C  C   . LEU C  116 ? 0.1435 0.2314 0.0597 0.0065  -0.0200 0.0295  116 LEU C C   
5332  O  O   . LEU C  116 ? 0.1447 0.2648 0.0983 -0.0138 -0.0153 0.0313  116 LEU C O   
5333  C  CB  . LEU C  116 ? 0.1754 0.3169 0.1140 0.0082  -0.0222 0.0478  116 LEU C CB  
5334  C  CG  . LEU C  116 ? 0.1782 0.2768 0.1965 0.0008  -0.0829 0.0559  116 LEU C CG  
5335  C  CD1 . LEU C  116 ? 0.3359 0.3668 0.1671 -0.0851 -0.0728 0.0778  116 LEU C CD1 
5336  C  CD2 . LEU C  116 ? 0.2768 0.2175 0.1990 -0.0237 0.0467  0.0339  116 LEU C CD2 
5337  N  N   . HIS C  117 ? 0.1583 0.2488 0.0847 -0.0544 -0.0076 0.0386  117 HIS C N   
5338  C  CA  . HIS C  117 ? 0.1556 0.2172 0.0807 -0.0311 -0.0126 0.0247  117 HIS C CA  
5339  C  C   . HIS C  117 ? 0.1635 0.2284 0.0897 -0.0489 -0.0185 0.0285  117 HIS C C   
5340  O  O   . HIS C  117 ? 0.1410 0.3003 0.0915 -0.0456 -0.0267 0.0126  117 HIS C O   
5341  C  CB  . HIS C  117 ? 0.1274 0.2333 0.1089 -0.0157 -0.0108 0.0281  117 HIS C CB  
5342  C  CG  . HIS C  117 ? 0.1168 0.2257 0.0829 -0.0030 -0.0012 0.0012  117 HIS C CG  
5343  N  ND1 . HIS C  117 ? 0.1653 0.1987 0.0538 -0.0401 0.0104  -0.0174 117 HIS C ND1 
5344  C  CD2 . HIS C  117 ? 0.1387 0.1935 0.0839 -0.0280 -0.0003 0.0020  117 HIS C CD2 
5345  C  CE1 . HIS C  117 ? 0.1553 0.1881 0.0703 -0.0309 -0.0103 -0.0060 117 HIS C CE1 
5346  N  NE2 . HIS C  117 ? 0.1342 0.1768 0.0710 -0.0087 0.0003  0.0076  117 HIS C NE2 
5347  N  N   . ILE C  118 ? 0.1150 0.2552 0.1050 -0.0088 -0.0129 0.0408  118 ILE C N   
5348  C  CA  . ILE C  118 ? 0.1328 0.2472 0.1567 -0.0181 -0.0377 0.0542  118 ILE C CA  
5349  C  C   . ILE C  118 ? 0.1193 0.2000 0.1023 -0.0097 0.0003  0.0317  118 ILE C C   
5350  O  O   . ILE C  118 ? 0.1452 0.2421 0.0958 -0.0377 -0.0147 0.0135  118 ILE C O   
5351  C  CB  . ILE C  118 ? 0.1653 0.2324 0.1364 -0.0242 -0.0370 0.0483  118 ILE C CB  
5352  C  CG1 . ILE C  118 ? 0.1990 0.1716 0.2328 -0.0120 -0.0571 0.0822  118 ILE C CG1 
5353  C  CG2 . ILE C  118 ? 0.1457 0.3574 0.1468 -0.0248 -0.0245 0.0335  118 ILE C CG2 
5354  C  CD1 . ILE C  118 ? 0.2989 0.1588 0.2141 -0.0110 -0.0335 0.0732  118 ILE C CD1 
5355  N  N   . VAL C  119 ? 0.1522 0.1894 0.1597 -0.0306 -0.0080 0.0208  119 VAL C N   
5356  C  CA  . VAL C  119 ? 0.1277 0.2025 0.1365 -0.0361 -0.0055 0.0311  119 VAL C CA  
5357  C  C   . VAL C  119 ? 0.1229 0.2682 0.1050 -0.0416 -0.0252 0.0115  119 VAL C C   
5358  O  O   . VAL C  119 ? 0.1326 0.2642 0.1441 -0.0357 -0.0252 0.0038  119 VAL C O   
5359  C  CB  . VAL C  119 ? 0.1401 0.2097 0.1373 -0.0516 0.0032  -0.0198 119 VAL C CB  
5360  C  CG1 . VAL C  119 ? 0.1569 0.2495 0.1316 -0.0454 -0.0049 0.0153  119 VAL C CG1 
5361  C  CG2 . VAL C  119 ? 0.1587 0.2460 0.1362 -0.0509 0.0133  -0.0204 119 VAL C CG2 
5362  N  N   . HIS C  120 ? 0.1355 0.2413 0.1093 -0.0337 -0.0017 0.0162  120 HIS C N   
5363  C  CA  . HIS C  120 ? 0.1050 0.2093 0.1471 -0.0242 -0.0062 -0.0144 120 HIS C CA  
5364  C  C   . HIS C  120 ? 0.1026 0.2667 0.1195 -0.0306 0.0188  -0.0221 120 HIS C C   
5365  O  O   . HIS C  120 ? 0.1188 0.1865 0.1486 -0.0286 0.0102  -0.0076 120 HIS C O   
5366  C  CB  . HIS C  120 ? 0.1333 0.2199 0.1324 -0.0167 -0.0078 0.0256  120 HIS C CB  
5367  C  CG  . HIS C  120 ? 0.1416 0.2097 0.1726 -0.0381 -0.0231 0.0278  120 HIS C CG  
5368  N  ND1 . HIS C  120 ? 0.1558 0.2276 0.1339 -0.0242 0.0108  0.0357  120 HIS C ND1 
5369  C  CD2 . HIS C  120 ? 0.1763 0.2372 0.1944 -0.0137 -0.0359 0.0586  120 HIS C CD2 
5370  C  CE1 . HIS C  120 ? 0.1518 0.2161 0.2063 0.0186  0.0280  0.0542  120 HIS C CE1 
5371  N  NE2 . HIS C  120 ? 0.1511 0.2335 0.1999 -0.0221 -0.0526 0.0606  120 HIS C NE2 
5372  N  N   . TYR C  121 ? 0.1003 0.2213 0.1611 -0.0187 0.0098  0.0081  121 TYR C N   
5373  C  CA  . TYR C  121 ? 0.1457 0.2158 0.1353 -0.0331 0.0152  -0.0052 121 TYR C CA  
5374  C  C   . TYR C  121 ? 0.1328 0.2095 0.1439 -0.0403 0.0060  -0.0026 121 TYR C C   
5375  O  O   . TYR C  121 ? 0.1308 0.2267 0.1653 -0.0186 0.0091  -0.0035 121 TYR C O   
5376  C  CB  . TYR C  121 ? 0.1301 0.2355 0.1714 -0.0425 0.0087  -0.0287 121 TYR C CB  
5377  C  CG  . TYR C  121 ? 0.1691 0.2445 0.1613 -0.0610 0.0027  -0.0469 121 TYR C CG  
5378  C  CD1 . TYR C  121 ? 0.1581 0.3052 0.1660 -0.0263 -0.0051 -0.0408 121 TYR C CD1 
5379  C  CD2 . TYR C  121 ? 0.1563 0.2333 0.1999 -0.0662 0.0010  -0.0243 121 TYR C CD2 
5380  C  CE1 . TYR C  121 ? 0.1958 0.3731 0.2626 -0.0929 -0.0206 -0.0593 121 TYR C CE1 
5381  C  CE2 . TYR C  121 ? 0.1587 0.2102 0.2527 -0.0529 -0.0214 -0.0397 121 TYR C CE2 
5382  C  CZ  . TYR C  121 ? 0.1696 0.2353 0.2939 -0.0340 -0.0654 -0.0186 121 TYR C CZ  
5383  O  OH  . TYR C  121 ? 0.1723 0.3070 0.3815 -0.0746 -0.0759 0.0107  121 TYR C OH  
5384  N  N   . ASN C  122 ? 0.1307 0.2572 0.1351 -0.0421 0.0153  0.0124  122 ASN C N   
5385  C  CA  . ASN C  122 ? 0.1066 0.2617 0.1395 -0.0425 0.0305  -0.0094 122 ASN C CA  
5386  C  C   . ASN C  122 ? 0.1206 0.2111 0.1833 -0.0308 0.0197  0.0070  122 ASN C C   
5387  O  O   . ASN C  122 ? 0.1256 0.2231 0.2309 -0.0342 0.0221  0.0083  122 ASN C O   
5388  C  CB  . ASN C  122 ? 0.1259 0.2531 0.1479 -0.0283 0.0120  -0.0003 122 ASN C CB  
5389  C  CG  . ASN C  122 ? 0.1421 0.2081 0.1823 -0.0121 0.0350  -0.0049 122 ASN C CG  
5390  O  OD1 . ASN C  122 ? 0.1462 0.2452 0.1892 0.0062  0.0516  0.0278  122 ASN C OD1 
5391  N  ND2 . ASN C  122 ? 0.1746 0.2400 0.1719 0.0001  0.0296  0.0052  122 ASN C ND2 
5392  N  N   . SER C  123 ? 0.1015 0.2549 0.1700 -0.0324 0.0215  0.0035  123 SER C N   
5393  C  CA  . SER C  123 ? 0.1165 0.2615 0.1893 -0.0339 0.0003  0.0048  123 SER C CA  
5394  C  C   . SER C  123 ? 0.1107 0.2204 0.2122 -0.0197 0.0164  -0.0154 123 SER C C   
5395  O  O   . SER C  123 ? 0.1350 0.2712 0.2448 -0.0619 0.0274  -0.0196 123 SER C O   
5396  C  CB  . SER C  123 ? 0.2087 0.2431 0.1615 -0.0068 0.0087  -0.0080 123 SER C CB  
5397  O  OG  . SER C  123 ? 0.1376 0.2691 0.2027 -0.0142 0.0149  -0.0043 123 SER C OG  
5398  N  N   . ASP C  124 ? 0.1235 0.2414 0.1717 -0.0214 0.0238  0.0137  124 ASP C N   
5399  C  CA  . ASP C  124 ? 0.1395 0.2348 0.1745 -0.0307 0.0247  0.0133  124 ASP C CA  
5400  C  C   . ASP C  124 ? 0.1574 0.2531 0.1978 -0.0184 0.0601  0.0253  124 ASP C C   
5401  O  O   . ASP C  124 ? 0.1884 0.2872 0.3005 0.0057  0.0965  0.0894  124 ASP C O   
5402  C  CB  . ASP C  124 ? 0.1414 0.2220 0.2003 -0.0287 0.0364  0.0174  124 ASP C CB  
5403  C  CG  . ASP C  124 ? 0.1535 0.2339 0.2136 -0.0390 0.0156  0.0133  124 ASP C CG  
5404  O  OD1 . ASP C  124 ? 0.1398 0.2303 0.2305 -0.0099 0.0087  -0.0071 124 ASP C OD1 
5405  O  OD2 . ASP C  124 ? 0.1525 0.2298 0.2617 -0.0406 0.0483  0.0137  124 ASP C OD2 
5406  N  N   . LEU C  125 ? 0.1360 0.2386 0.1805 -0.0313 0.0135  -0.0065 125 LEU C N   
5407  C  CA  . LEU C  125 ? 0.1635 0.2309 0.1817 -0.0012 0.0263  -0.0027 125 LEU C CA  
5408  C  C   . LEU C  125 ? 0.1701 0.2253 0.2107 -0.0630 0.0060  0.0020  125 LEU C C   
5409  O  O   . LEU C  125 ? 0.2409 0.1895 0.2630 -0.0340 0.0265  0.0092  125 LEU C O   
5410  C  CB  . LEU C  125 ? 0.1795 0.2266 0.1946 -0.0222 0.0337  0.0021  125 LEU C CB  
5411  C  CG  . LEU C  125 ? 0.1786 0.2458 0.1993 -0.0070 0.0329  -0.0206 125 LEU C CG  
5412  C  CD1 . LEU C  125 ? 0.1980 0.2389 0.2310 0.0115  -0.0285 0.0049  125 LEU C CD1 
5413  C  CD2 . LEU C  125 ? 0.2680 0.2642 0.2488 -0.0454 0.0745  0.0074  125 LEU C CD2 
5414  N  N   . TYR C  126 ? 0.1386 0.2430 0.1989 -0.0311 0.0419  -0.0089 126 TYR C N   
5415  C  CA  . TYR C  126 ? 0.1412 0.2129 0.2389 -0.0476 0.0469  -0.0339 126 TYR C CA  
5416  C  C   . TYR C  126 ? 0.1540 0.2431 0.2728 -0.0728 0.0337  -0.0167 126 TYR C C   
5417  O  O   . TYR C  126 ? 0.1955 0.2206 0.2276 -0.0471 -0.0017 -0.0120 126 TYR C O   
5418  C  CB  . TYR C  126 ? 0.1497 0.2522 0.2447 -0.0315 0.0527  0.0197  126 TYR C CB  
5419  C  CG  . TYR C  126 ? 0.1517 0.1811 0.2578 -0.0205 0.0221  0.0172  126 TYR C CG  
5420  C  CD1 . TYR C  126 ? 0.1897 0.2185 0.2463 -0.0188 -0.0040 0.0259  126 TYR C CD1 
5421  C  CD2 . TYR C  126 ? 0.1599 0.1784 0.2213 -0.0342 0.0513  -0.0212 126 TYR C CD2 
5422  C  CE1 . TYR C  126 ? 0.1854 0.2405 0.2488 -0.0604 -0.0015 0.0520  126 TYR C CE1 
5423  C  CE2 . TYR C  126 ? 0.1490 0.1861 0.2400 0.0094  0.0227  0.0335  126 TYR C CE2 
5424  C  CZ  . TYR C  126 ? 0.1350 0.1730 0.2906 -0.0065 0.0118  0.0368  126 TYR C CZ  
5425  O  OH  . TYR C  126 ? 0.1588 0.2587 0.2418 -0.0278 0.0107  0.0653  126 TYR C OH  
5426  N  N   . PRO C  127 ? 0.1908 0.2431 0.2359 -0.0967 0.0166  -0.0241 127 PRO C N   
5427  C  CA  . PRO C  127 ? 0.2337 0.3113 0.2077 -0.1204 0.0082  -0.0337 127 PRO C CA  
5428  C  C   . PRO C  127 ? 0.2044 0.2903 0.2244 -0.0806 -0.0070 -0.0284 127 PRO C C   
5429  O  O   . PRO C  127 ? 0.2314 0.3510 0.2741 -0.0790 -0.0228 -0.0259 127 PRO C O   
5430  C  CB  . PRO C  127 ? 0.2687 0.3305 0.4406 -0.0835 -0.0676 -0.1093 127 PRO C CB  
5431  C  CG  . PRO C  127 ? 0.3048 0.3208 0.3003 -0.1064 -0.0395 -0.0573 127 PRO C CG  
5432  C  CD  . PRO C  127 ? 0.2786 0.2211 0.2707 -0.0467 0.0035  -0.0408 127 PRO C CD  
5433  N  N   . ASP C  128 ? 0.2066 0.2603 0.1953 -0.0847 0.0135  -0.0329 128 ASP C N   
5434  C  CA  . ASP C  128 ? 0.2402 0.3316 0.2032 -0.0634 0.0274  -0.0891 128 ASP C CA  
5435  C  C   . ASP C  128 ? 0.1998 0.2483 0.2158 -0.0333 0.0305  -0.0107 128 ASP C C   
5436  O  O   . ASP C  128 ? 0.2005 0.2467 0.2233 -0.0286 -0.0013 -0.0156 128 ASP C O   
5437  C  CB  . ASP C  128 ? 0.3519 0.2409 0.2587 -0.1322 0.0071  -0.0592 128 ASP C CB  
5438  C  CG  . ASP C  128 ? 0.3551 0.3001 0.2319 -0.0491 0.0159  -0.1101 128 ASP C CG  
5439  O  OD1 . ASP C  128 ? 0.3747 0.2793 0.5758 -0.0549 -0.1282 -0.0013 128 ASP C OD1 
5440  O  OD2 . ASP C  128 ? 0.4508 0.2761 0.3682 -0.0373 -0.1212 -0.0714 128 ASP C OD2 
5441  N  N   . ALA C  129 ? 0.2527 0.2143 0.1856 -0.0401 0.0344  -0.0162 129 ALA C N   
5442  C  CA  . ALA C  129 ? 0.2245 0.2050 0.2079 -0.0375 0.0366  -0.0060 129 ALA C CA  
5443  C  C   . ALA C  129 ? 0.2660 0.3032 0.1985 -0.0031 0.0412  -0.0232 129 ALA C C   
5444  O  O   . ALA C  129 ? 0.2215 0.2714 0.2226 0.0010  0.0527  -0.0077 129 ALA C O   
5445  C  CB  . ALA C  129 ? 0.3018 0.2195 0.2299 -0.0533 0.0666  0.0021  129 ALA C CB  
5446  N  N   . SER C  130 ? 0.3429 0.2154 0.2287 -0.0118 0.0548  0.0113  130 SER C N   
5447  C  CA  . SER C  130 ? 0.3377 0.2292 0.3147 -0.0161 0.0979  -0.0579 130 SER C CA  
5448  C  C   . SER C  130 ? 0.2490 0.2091 0.3718 0.0659  0.0432  -0.0155 130 SER C C   
5449  O  O   . SER C  130 ? 0.2797 0.3431 0.3817 0.1054  0.1237  0.0489  130 SER C O   
5450  C  CB  . SER C  130 ? 0.5006 0.2249 0.4025 0.0697  -0.0789 -0.0738 130 SER C CB  
5451  O  OG  . SER C  130 ? 0.5009 0.6780 0.5123 -0.0395 -0.1451 -0.1216 130 SER C OG  
5452  N  N   . THR C  131 ? 0.2452 0.2217 0.2578 -0.0592 0.0073  -0.0329 131 THR C N   
5453  C  CA  . THR C  131 ? 0.2293 0.2181 0.2698 -0.0615 0.0489  -0.0441 131 THR C CA  
5454  C  C   . THR C  131 ? 0.1962 0.1757 0.2876 -0.0015 0.0476  -0.0370 131 THR C C   
5455  O  O   . THR C  131 ? 0.2145 0.1576 0.3030 -0.0241 0.0248  0.0080  131 THR C O   
5456  C  CB  . THR C  131 ? 0.2170 0.2109 0.2730 -0.0784 -0.0062 0.0017  131 THR C CB  
5457  O  OG1 . THR C  131 ? 0.2892 0.2342 0.3725 -0.1040 -0.0375 -0.0348 131 THR C OG1 
5458  C  CG2 . THR C  131 ? 0.2321 0.2427 0.2723 -0.0546 0.0617  0.0000  131 THR C CG2 
5459  N  N   . ALA C  132 ? 0.1802 0.1989 0.2397 -0.0478 0.0573  -0.0302 132 ALA C N   
5460  C  CA  . ALA C  132 ? 0.1523 0.1852 0.2118 -0.0362 0.0245  -0.0038 132 ALA C CA  
5461  C  C   . ALA C  132 ? 0.1493 0.1904 0.2301 -0.0491 0.0485  -0.0406 132 ALA C C   
5462  O  O   . ALA C  132 ? 0.1671 0.1854 0.1998 -0.0294 0.0366  -0.0311 132 ALA C O   
5463  C  CB  . ALA C  132 ? 0.1624 0.2000 0.1917 -0.0333 0.0346  -0.0013 132 ALA C CB  
5464  N  N   . SER C  133 ? 0.1633 0.1790 0.2348 -0.0476 0.0546  -0.0500 133 SER C N   
5465  C  CA  . SER C  133 ? 0.1504 0.2262 0.2136 -0.0293 0.0375  -0.0461 133 SER C CA  
5466  C  C   . SER C  133 ? 0.1680 0.1665 0.2161 -0.0403 0.0392  -0.0617 133 SER C C   
5467  O  O   . SER C  133 ? 0.1676 0.1920 0.2100 -0.0688 0.0505  -0.0566 133 SER C O   
5468  C  CB  . SER C  133 ? 0.2136 0.2389 0.2204 -0.0295 0.0759  -0.0264 133 SER C CB  
5469  O  OG  . SER C  133 ? 0.2088 0.2549 0.2522 -0.0450 0.0518  -0.0856 133 SER C OG  
5470  N  N   . ASN C  134 ? 0.1554 0.1416 0.2770 -0.0297 0.0318  -0.0494 134 ASN C N   
5471  C  CA  . ASN C  134 ? 0.1647 0.1730 0.2975 -0.0059 0.0140  -0.0439 134 ASN C CA  
5472  C  C   . ASN C  134 ? 0.2138 0.1420 0.2872 -0.0469 0.0555  0.0021  134 ASN C C   
5473  O  O   . ASN C  134 ? 0.2384 0.2087 0.3592 0.0020  0.0489  0.0427  134 ASN C O   
5474  C  CB  . ASN C  134 ? 0.2158 0.1432 0.3199 -0.0423 0.0859  -0.0489 134 ASN C CB  
5475  C  CG  . ASN C  134 ? 0.1813 0.1682 0.4641 -0.0160 0.0507  0.0065  134 ASN C CG  
5476  O  OD1 . ASN C  134 ? 0.1834 0.1674 0.5210 -0.0458 0.0658  -0.0763 134 ASN C OD1 
5477  N  ND2 . ASN C  134 ? 0.2233 0.1459 0.5490 -0.0335 0.0425  0.0040  134 ASN C ND2 
5478  N  N   . LYS C  135 ? 0.1701 0.1833 0.2736 -0.0498 0.0688  -0.0342 135 LYS C N   
5479  C  CA  . LYS C  135 ? 0.1567 0.2020 0.2741 -0.0313 0.0297  0.0046  135 LYS C CA  
5480  C  C   . LYS C  135 ? 0.1416 0.2053 0.2485 -0.0010 0.0436  0.0311  135 LYS C C   
5481  O  O   . LYS C  135 ? 0.1610 0.2140 0.2046 -0.0076 0.0425  0.0263  135 LYS C O   
5482  C  CB  . LYS C  135 ? 0.1854 0.2520 0.2958 -0.0625 0.0504  0.0445  135 LYS C CB  
5483  C  CG  . LYS C  135 ? 0.2293 0.2973 0.3612 -0.1350 0.0837  -0.0584 135 LYS C CG  
5484  C  CD  . LYS C  135 ? 0.2113 0.2818 0.3332 -0.0913 0.0328  0.0116  135 LYS C CD  
5485  C  CE  . LYS C  135 ? 0.2831 0.2284 0.4092 -0.0295 0.0100  0.0863  135 LYS C CE  
5486  N  NZ  . LYS C  135 ? 0.2808 0.1996 0.4469 -0.0219 0.0480  -0.0149 135 LYS C NZ  
5487  N  N   . SER C  136 ? 0.2387 0.2242 0.2280 0.0065  0.0658  -0.0104 136 SER C N   
5488  C  CA  . SER C  136 ? 0.2409 0.2163 0.1763 0.0696  0.0242  0.0273  136 SER C CA  
5489  C  C   . SER C  136 ? 0.1604 0.1775 0.1620 0.0043  0.0454  0.0142  136 SER C C   
5490  O  O   . SER C  136 ? 0.1793 0.1789 0.2014 -0.0130 0.0548  0.0266  136 SER C O   
5491  C  CB  . SER C  136 ? 0.3648 0.3222 0.1827 0.0996  0.0834  0.0485  136 SER C CB  
5492  O  OG  . SER C  136 ? 0.4444 0.3429 0.2522 0.1416  0.1076  0.0794  136 SER C OG  
5493  N  N   . GLU C  137 ? 0.1809 0.1827 0.1683 -0.0140 0.0351  0.0300  137 GLU C N   
5494  C  CA  . GLU C  137 ? 0.1744 0.2082 0.1445 -0.0359 0.0137  0.0183  137 GLU C CA  
5495  C  C   . GLU C  137 ? 0.1369 0.2167 0.1559 -0.0449 0.0239  0.0071  137 GLU C C   
5496  O  O   . GLU C  137 ? 0.1378 0.2470 0.1615 -0.0085 0.0065  0.0043  137 GLU C O   
5497  C  CB  . GLU C  137 ? 0.1860 0.1993 0.1624 0.0049  0.0194  0.0161  137 GLU C CB  
5498  C  CG  . GLU C  137 ? 0.2863 0.2885 0.1475 -0.0417 0.0142  0.0236  137 GLU C CG  
5499  C  CD  . GLU C  137 ? 0.3871 0.4548 0.2034 -0.0311 0.0579  -0.0590 137 GLU C CD  
5500  O  OE1 . GLU C  137 ? 0.4124 0.6783 0.3837 -0.1270 0.1375  -0.2238 137 GLU C OE1 
5501  O  OE2 . GLU C  137 ? 0.5354 0.7728 0.2461 -0.1457 0.0254  -0.1591 137 GLU C OE2 
5502  N  N   . GLY C  138 ? 0.1244 0.1872 0.1700 -0.0351 0.0163  0.0148  138 GLY C N   
5503  C  CA  . GLY C  138 ? 0.1631 0.2000 0.1832 -0.0403 0.0077  0.0105  138 GLY C CA  
5504  C  C   . GLY C  138 ? 0.1202 0.1468 0.1572 -0.0434 -0.0032 -0.0140 138 GLY C C   
5505  O  O   . GLY C  138 ? 0.1176 0.1935 0.1624 -0.0362 0.0024  -0.0125 138 GLY C O   
5506  N  N   . LEU C  139 ? 0.1263 0.1628 0.1276 -0.0397 0.0266  -0.0041 139 LEU C N   
5507  C  CA  . LEU C  139 ? 0.1224 0.1748 0.1224 -0.0251 0.0054  -0.0017 139 LEU C CA  
5508  C  C   . LEU C  139 ? 0.0931 0.1660 0.1371 -0.0244 0.0185  -0.0261 139 LEU C C   
5509  O  O   . LEU C  139 ? 0.1037 0.1793 0.1177 -0.0275 0.0026  -0.0034 139 LEU C O   
5510  C  CB  . LEU C  139 ? 0.1165 0.1763 0.1437 -0.0326 0.0265  -0.0215 139 LEU C CB  
5511  C  CG  . LEU C  139 ? 0.1208 0.1993 0.1632 -0.0320 0.0199  -0.0421 139 LEU C CG  
5512  C  CD1 . LEU C  139 ? 0.1455 0.1738 0.2055 -0.0340 0.0430  -0.0430 139 LEU C CD1 
5513  C  CD2 . LEU C  139 ? 0.1574 0.1942 0.1942 -0.0260 -0.0083 -0.0537 139 LEU C CD2 
5514  N  N   . ALA C  140 ? 0.0938 0.1890 0.1321 -0.0245 0.0091  0.0100  140 ALA C N   
5515  C  CA  . ALA C  140 ? 0.1177 0.1739 0.1186 -0.0252 0.0043  0.0154  140 ALA C CA  
5516  C  C   . ALA C  140 ? 0.1057 0.1707 0.1075 -0.0083 -0.0035 -0.0060 140 ALA C C   
5517  O  O   . ALA C  140 ? 0.1186 0.2364 0.1181 -0.0377 -0.0098 -0.0109 140 ALA C O   
5518  C  CB  . ALA C  140 ? 0.1218 0.1996 0.1156 0.0021  0.0060  -0.0081 140 ALA C CB  
5519  N  N   . VAL C  141 ? 0.1125 0.1766 0.0816 -0.0263 0.0071  0.0034  141 VAL C N   
5520  C  CA  . VAL C  141 ? 0.1167 0.1622 0.0912 -0.0059 -0.0041 0.0081  141 VAL C CA  
5521  C  C   . VAL C  141 ? 0.1249 0.1570 0.0900 -0.0010 0.0078  0.0162  141 VAL C C   
5522  O  O   . VAL C  141 ? 0.1304 0.1829 0.0936 -0.0154 -0.0135 0.0070  141 VAL C O   
5523  C  CB  . VAL C  141 ? 0.1089 0.1919 0.0876 -0.0146 -0.0026 -0.0074 141 VAL C CB  
5524  C  CG1 . VAL C  141 ? 0.1281 0.2041 0.0960 -0.0046 0.0103  0.0013  141 VAL C CG1 
5525  C  CG2 . VAL C  141 ? 0.1517 0.1829 0.1012 -0.0344 -0.0099 -0.0211 141 VAL C CG2 
5526  N  N   . LEU C  142 ? 0.1238 0.1705 0.1052 -0.0122 0.0120  0.0401  142 LEU C N   
5527  C  CA  . LEU C  142 ? 0.1256 0.2041 0.1039 0.0127  0.0006  0.0353  142 LEU C CA  
5528  C  C   . LEU C  142 ? 0.1335 0.2034 0.0734 -0.0120 -0.0113 0.0388  142 LEU C C   
5529  O  O   . LEU C  142 ? 0.1330 0.2402 0.1039 -0.0131 -0.0116 0.0181  142 LEU C O   
5530  C  CB  . LEU C  142 ? 0.1513 0.2301 0.1133 0.0342  -0.0035 0.0414  142 LEU C CB  
5531  C  CG  . LEU C  142 ? 0.1105 0.3167 0.1471 0.0240  0.0024  0.0434  142 LEU C CG  
5532  C  CD1 . LEU C  142 ? 0.1617 0.3346 0.1727 0.0209  -0.0421 0.0551  142 LEU C CD1 
5533  C  CD2 . LEU C  142 ? 0.1398 0.2558 0.1522 0.0097  0.0274  0.0206  142 LEU C CD2 
5534  N  N   . ALA C  143 ? 0.1359 0.1744 0.0908 -0.0111 0.0035  0.0361  143 ALA C N   
5535  C  CA  . ALA C  143 ? 0.1212 0.1965 0.0822 -0.0010 0.0063  0.0441  143 ALA C CA  
5536  C  C   . ALA C  143 ? 0.1259 0.2075 0.0746 0.0057  0.0048  0.0307  143 ALA C C   
5537  O  O   . ALA C  143 ? 0.1527 0.1725 0.1005 0.0109  0.0054  0.0480  143 ALA C O   
5538  C  CB  . ALA C  143 ? 0.1252 0.2089 0.0890 0.0166  0.0124  0.0049  143 ALA C CB  
5539  N  N   . VAL C  144 ? 0.1572 0.2201 0.0781 0.0195  -0.0068 0.0465  144 VAL C N   
5540  C  CA  . VAL C  144 ? 0.1377 0.1990 0.1351 0.0310  0.0035  0.0678  144 VAL C CA  
5541  C  C   . VAL C  144 ? 0.1373 0.2509 0.1310 0.0255  -0.0244 0.0427  144 VAL C C   
5542  O  O   . VAL C  144 ? 0.1899 0.2236 0.1172 0.0230  0.0172  0.0608  144 VAL C O   
5543  C  CB  . VAL C  144 ? 0.1435 0.2470 0.1632 -0.0046 -0.0296 0.0767  144 VAL C CB  
5544  C  CG1 . VAL C  144 ? 0.1951 0.3075 0.2008 0.0142  -0.0100 0.1310  144 VAL C CG1 
5545  C  CG2 . VAL C  144 ? 0.1425 0.2887 0.1942 0.0342  -0.0264 0.0837  144 VAL C CG2 
5546  N  N   . LEU C  145 ? 0.1738 0.2258 0.0956 0.0131  0.0157  0.0782  145 LEU C N   
5547  C  CA  . LEU C  145 ? 0.1843 0.2281 0.0802 0.0361  0.0236  0.0603  145 LEU C CA  
5548  C  C   . LEU C  145 ? 0.1534 0.2962 0.1155 0.0242  0.0055  0.0847  145 LEU C C   
5549  O  O   . LEU C  145 ? 0.2007 0.2734 0.1463 0.0604  0.0093  0.1023  145 LEU C O   
5550  C  CB  . LEU C  145 ? 0.1984 0.2163 0.1154 0.0063  -0.0102 0.0649  145 LEU C CB  
5551  C  CG  . LEU C  145 ? 0.1847 0.1935 0.1439 -0.0010 -0.0315 0.0581  145 LEU C CG  
5552  C  CD1 . LEU C  145 ? 0.1971 0.3122 0.1109 -0.0052 0.0099  0.0452  145 LEU C CD1 
5553  C  CD2 . LEU C  145 ? 0.2163 0.2034 0.1911 0.0193  -0.0130 0.0617  145 LEU C CD2 
5554  N  N   . ILE C  146 ? 0.1917 0.2050 0.1048 -0.0010 0.0220  0.0696  146 ILE C N   
5555  C  CA  . ILE C  146 ? 0.1919 0.2897 0.1215 0.0076  0.0122  0.0996  146 ILE C CA  
5556  C  C   . ILE C  146 ? 0.2253 0.2908 0.1608 -0.0098 -0.0071 0.1648  146 ILE C C   
5557  O  O   . ILE C  146 ? 0.1892 0.2470 0.1527 0.0015  0.0071  0.0944  146 ILE C O   
5558  C  CB  . ILE C  146 ? 0.2443 0.3655 0.1130 -0.0220 -0.0010 0.1199  146 ILE C CB  
5559  C  CG1 . ILE C  146 ? 0.2007 0.3206 0.1238 0.0041  -0.0037 0.0943  146 ILE C CG1 
5560  C  CG2 . ILE C  146 ? 0.2533 0.3700 0.1163 -0.0003 -0.0337 0.1137  146 ILE C CG2 
5561  C  CD1 . ILE C  146 ? 0.2481 0.3948 0.1243 -0.0593 -0.0423 0.0662  146 ILE C CD1 
5562  N  N   . GLU C  147 ? 0.1888 0.2847 0.1568 0.0300  0.0240  0.1298  147 GLU C N   
5563  C  CA  . GLU C  147 ? 0.2545 0.2572 0.1788 -0.0386 0.0142  0.1315  147 GLU C CA  
5564  C  C   . GLU C  147 ? 0.2669 0.2903 0.1818 0.0024  0.0262  0.1359  147 GLU C C   
5565  O  O   . GLU C  147 ? 0.2608 0.3768 0.1976 0.0296  0.0148  0.1684  147 GLU C O   
5566  C  CB  . GLU C  147 ? 0.2743 0.1994 0.2005 0.0185  0.0275  0.0794  147 GLU C CB  
5567  C  CG  . GLU C  147 ? 0.2734 0.2447 0.2558 0.0098  0.0175  0.1184  147 GLU C CG  
5568  C  CD  . GLU C  147 ? 0.2825 0.3321 0.3454 -0.0401 0.0432  0.0753  147 GLU C CD  
5569  O  OE1 . GLU C  147 ? 0.3853 0.3646 0.2788 -0.0632 0.0353  0.0745  147 GLU C OE1 
5570  O  OE2 . GLU C  147 ? 0.4264 0.3697 0.3395 0.0318  0.0419  0.0759  147 GLU C OE2 
5571  N  N   A MET C  148 ? 0.3386 0.3553 0.1980 -0.0370 0.0560  0.1993  148 MET C N   
5572  N  N   B MET C  148 ? 0.2046 0.3504 0.2342 0.0154  0.0261  0.1709  148 MET C N   
5573  C  CA  A MET C  148 ? 0.3835 0.3862 0.2054 0.0549  0.0485  0.2020  148 MET C CA  
5574  C  CA  B MET C  148 ? 0.1956 0.3768 0.2309 0.0133  0.0164  0.1757  148 MET C CA  
5575  C  C   A MET C  148 ? 0.4784 0.4250 0.2305 0.0593  -0.0423 0.1225  148 MET C C   
5576  C  C   B MET C  148 ? 0.2310 0.3415 0.3702 -0.0834 0.0111  0.2013  148 MET C C   
5577  O  O   A MET C  148 ? 0.4554 0.2664 0.2761 0.0693  0.0421  0.0982  148 MET C O   
5578  O  O   B MET C  148 ? 0.2754 0.3844 0.2418 -0.0254 -0.0182 0.1993  148 MET C O   
5579  C  CB  A MET C  148 ? 0.4203 0.6003 0.3522 0.0962  0.1085  0.2034  148 MET C CB  
5580  C  CB  B MET C  148 ? 0.2556 0.3851 0.1623 -0.0178 0.0408  0.1695  148 MET C CB  
5581  C  CG  A MET C  148 ? 0.4914 0.6154 0.2655 0.0088  0.0851  0.1815  148 MET C CG  
5582  C  CG  B MET C  148 ? 0.3666 0.4526 0.1632 0.0432  0.1063  0.1982  148 MET C CG  
5583  S  SD  A MET C  148 ? 0.4582 1.2359 0.3759 -0.1711 0.0680  0.1405  148 MET C SD  
5584  S  SD  B MET C  148 ? 0.6108 0.5167 0.4305 0.0443  0.0899  0.2467  148 MET C SD  
5585  C  CE  A MET C  148 ? 0.8427 0.9829 0.4047 -0.0617 -0.0100 0.0377  148 MET C CE  
5586  C  CE  B MET C  148 ? 0.4695 0.4097 0.4408 -0.0074 0.0337  0.2545  148 MET C CE  
5587  N  N   . GLY C  149 ? 0.3201 0.4989 0.3655 0.1077  0.0588  0.2628  149 GLY C N   
5588  C  CA  . GLY C  149 ? 0.3328 0.4219 0.2481 -0.0071 0.0019  0.1617  149 GLY C CA  
5589  C  C   . GLY C  149 ? 0.3296 0.3928 0.2691 0.0762  0.0244  0.1952  149 GLY C C   
5590  O  O   . GLY C  149 ? 0.4205 0.4679 0.2136 0.0657  0.0083  0.1950  149 GLY C O   
5591  N  N   . SER C  150 ? 0.3756 0.4949 0.2470 0.1080  0.0099  0.1248  150 SER C N   
5592  C  CA  . SER C  150 ? 0.3925 0.4056 0.2506 0.0843  -0.0366 0.0808  150 SER C CA  
5593  C  C   . SER C  150 ? 0.4223 0.4708 0.3483 0.0111  -0.0452 0.2065  150 SER C C   
5594  O  O   . SER C  150 ? 0.3165 0.5964 0.2415 0.0082  -0.0143 0.2408  150 SER C O   
5595  C  CB  . SER C  150 ? 0.3564 0.5454 0.6796 0.1560  -0.0412 -0.0377 150 SER C CB  
5596  O  OG  . SER C  150 ? 0.6287 0.5680 0.7699 0.1553  -0.0003 -0.1106 150 SER C OG  
5597  N  N   . PHE C  151 ? 0.3849 0.6197 0.2465 0.1878  0.0515  0.1997  151 PHE C N   
5598  C  CA  . PHE C  151 ? 0.3294 0.9696 0.6284 -0.0445 -0.0432 0.2865  151 PHE C CA  
5599  C  C   . PHE C  151 ? 0.3192 0.5654 0.3752 -0.0912 -0.0828 0.1606  151 PHE C C   
5600  O  O   . PHE C  151 ? 0.4129 0.7775 0.3619 0.0024  -0.0054 0.1863  151 PHE C O   
5601  C  CB  . PHE C  151 ? 2.0046 2.5497 2.3285 -1.2201 -1.6073 1.8947  151 PHE C CB  
5602  C  CG  . PHE C  151 ? 1.5690 1.7180 0.7953 -0.6075 0.0685  0.3310  151 PHE C CG  
5603  C  CD1 . PHE C  151 ? 2.1445 1.8123 0.3770 -0.2935 -0.0087 0.6812  151 PHE C CD1 
5604  C  CD2 . PHE C  151 ? 2.3413 3.0890 0.9923 -0.6262 0.4801  0.9508  151 PHE C CD2 
5605  C  CE1 . PHE C  151 ? 1.9522 2.2441 0.7275 -0.5792 -0.1609 0.8356  151 PHE C CE1 
5606  C  CE2 . PHE C  151 ? 3.0548 2.5146 0.5468 -0.5946 -0.1289 0.4814  151 PHE C CE2 
5607  C  CZ  . PHE C  151 ? 2.1844 3.2514 0.2469 0.3499  -0.2739 0.7250  151 PHE C CZ  
5608  N  N   . ASN C  152 ? 0.3131 0.5569 0.4172 -0.0243 -0.1000 0.3494  152 ASN C N   
5609  C  CA  . ASN C  152 ? 0.2912 0.5489 0.4189 -0.0507 -0.1234 0.3127  152 ASN C CA  
5610  C  C   . ASN C  152 ? 0.2463 0.5206 0.1362 0.0640  -0.0340 0.2145  152 ASN C C   
5611  O  O   . ASN C  152 ? 0.5133 0.4657 0.4500 -0.0615 -0.1511 0.2316  152 ASN C O   
5612  C  CB  . ASN C  152 ? 0.3188 0.5716 0.2596 0.1263  -0.0693 0.1674  152 ASN C CB  
5613  C  CG  . ASN C  152 ? 1.7075 0.9401 2.4230 0.7397  1.6708  1.2038  152 ASN C CG  
5614  O  OD1 . ASN C  152 ? 1.1869 2.8924 0.5100 1.2130  0.5133  1.1783  152 ASN C OD1 
5615  N  ND2 . ASN C  152 ? 0.4329 0.7856 2.6064 -0.0599 0.1270  0.7814  152 ASN C ND2 
5616  N  N   . PRO C  153 ? 0.3465 0.4476 0.3528 0.0515  -0.0784 0.1598  153 PRO C N   
5617  C  CA  . PRO C  153 ? 0.4443 0.3865 0.4480 0.0635  -0.2412 0.1216  153 PRO C CA  
5618  C  C   . PRO C  153 ? 0.3650 0.6438 0.2563 -0.0057 -0.0856 0.1387  153 PRO C C   
5619  O  O   . PRO C  153 ? 0.3506 0.6265 0.2802 -0.0714 -0.1098 0.2373  153 PRO C O   
5620  C  CB  . PRO C  153 ? 0.4120 0.5228 0.3185 0.0877  -0.1534 0.1250  153 PRO C CB  
5621  C  CG  . PRO C  153 ? 0.4286 0.7062 0.3402 0.0432  -0.1489 -0.0720 153 PRO C CG  
5622  C  CD  . PRO C  153 ? 0.3625 0.3544 0.2581 0.2440  0.0294  0.1260  153 PRO C CD  
5623  N  N   . SER C  154 ? 0.4604 0.6226 0.2829 0.0498  -0.1066 0.2809  154 SER C N   
5624  C  CA  . SER C  154 ? 0.6105 0.6309 0.0935 0.0207  0.0665  0.1916  154 SER C CA  
5625  C  C   . SER C  154 ? 0.4350 0.4533 0.2036 -0.1290 -0.1668 -0.0564 154 SER C C   
5626  O  O   . SER C  154 ? 0.4212 0.4738 0.2292 -0.0617 -0.1573 0.0961  154 SER C O   
5627  C  CB  . SER C  154 ? 0.6092 0.2996 0.2908 0.1111  0.0379  0.0012  154 SER C CB  
5628  O  OG  . SER C  154 ? 1.0168 0.2892 0.3224 0.2720  0.1062  0.0740  154 SER C OG  
5629  N  N   . TYR C  155 ? 0.3921 0.2357 0.2624 0.0126  -0.0825 0.1088  155 TYR C N   
5630  C  CA  . TYR C  155 ? 0.3862 0.3508 0.1747 0.0131  -0.0916 0.0974  155 TYR C CA  
5631  C  C   . TYR C  155 ? 0.2644 0.1972 0.1545 0.0035  -0.0557 0.0522  155 TYR C C   
5632  O  O   . TYR C  155 ? 0.3639 0.3447 0.2041 -0.0355 -0.0980 0.0680  155 TYR C O   
5633  C  CB  . TYR C  155 ? 0.3465 0.5666 0.1881 -0.0980 -0.1193 0.1640  155 TYR C CB  
5634  C  CG  . TYR C  155 ? 0.2626 0.4174 0.1802 -0.0038 0.0052  0.1036  155 TYR C CG  
5635  C  CD1 . TYR C  155 ? 0.2623 0.3749 0.1822 0.0023  -0.0456 0.1045  155 TYR C CD1 
5636  C  CD2 . TYR C  155 ? 0.3000 0.4077 0.1586 -0.0405 -0.0482 0.0815  155 TYR C CD2 
5637  C  CE1 . TYR C  155 ? 0.2590 0.3522 0.1876 -0.0020 -0.0152 0.1014  155 TYR C CE1 
5638  C  CE2 . TYR C  155 ? 0.2849 0.4343 0.1683 -0.0505 -0.0124 0.1155  155 TYR C CE2 
5639  C  CZ  . TYR C  155 ? 0.2176 0.3643 0.1732 -0.0203 -0.0731 0.1124  155 TYR C CZ  
5640  O  OH  . TYR C  155 ? 0.2346 0.3125 0.1806 -0.0115 -0.0502 0.1315  155 TYR C OH  
5641  N  N   . ASP C  156 ? 0.4104 0.4778 0.3091 -0.0395 -0.1006 0.2025  156 ASP C N   
5642  C  CA  . ASP C  156 ? 0.4749 0.6836 0.2050 -0.2608 -0.1782 0.2410  156 ASP C CA  
5643  C  C   . ASP C  156 ? 0.3804 0.3524 0.2818 -0.0837 -0.0273 -0.0003 156 ASP C C   
5644  O  O   . ASP C  156 ? 0.5618 0.3036 0.3061 -0.0174 -0.1632 0.0922  156 ASP C O   
5645  C  CB  . ASP C  156 ? 0.3424 0.7631 0.3343 0.0251  -0.1300 0.2966  156 ASP C CB  
5646  C  CG  . ASP C  156 ? 0.8404 0.8615 0.5554 -0.3061 0.2046  0.2213  156 ASP C CG  
5647  O  OD1 . ASP C  156 ? 1.0252 1.4622 0.3253 -0.1576 0.0522  0.6395  156 ASP C OD1 
5648  O  OD2 . ASP C  156 ? 0.6967 1.3632 0.8377 -0.1571 -0.4059 0.9147  156 ASP C OD2 
5649  N  N   . LYS C  157 ? 0.3449 0.6111 0.2587 -0.0562 -0.1224 0.1731  157 LYS C N   
5650  C  CA  . LYS C  157 ? 0.3619 0.3368 0.3106 0.1542  -0.1414 0.0763  157 LYS C CA  
5651  C  C   . LYS C  157 ? 0.4341 0.3582 0.4435 0.0370  -0.1049 0.2108  157 LYS C C   
5652  O  O   . LYS C  157 ? 0.5791 0.7516 0.5335 -0.2011 -0.2795 0.2581  157 LYS C O   
5653  C  CB  . LYS C  157 ? 0.3542 0.3490 0.3939 0.0768  -0.1562 -0.0903 157 LYS C CB  
5654  C  CG  . LYS C  157 ? 0.4565 0.3258 0.4318 0.1544  -0.0496 -0.0469 157 LYS C CG  
5655  C  CD  . LYS C  157 ? 0.5123 0.4824 0.3521 0.2458  -0.1785 -0.1435 157 LYS C CD  
5656  C  CE  . LYS C  157 ? 0.4366 0.4126 0.6991 0.0181  -0.1275 0.0575  157 LYS C CE  
5657  N  NZ  . LYS C  157 ? 0.4769 0.7860 0.4115 0.1218  -0.1715 0.2230  157 LYS C NZ  
5658  N  N   . ILE C  158 ? 0.4395 0.2206 0.2267 0.0641  -0.1220 0.0732  158 ILE C N   
5659  C  CA  . ILE C  158 ? 0.3213 0.2743 0.2427 0.0288  -0.0649 0.0922  158 ILE C CA  
5660  C  C   . ILE C  158 ? 0.4095 0.2402 0.2427 -0.0241 0.0127  0.0010  158 ILE C C   
5661  O  O   . ILE C  158 ? 0.4497 0.3837 0.2007 -0.0351 -0.1282 0.0844  158 ILE C O   
5662  C  CB  . ILE C  158 ? 0.4875 0.1976 0.1748 0.0333  -0.0793 0.0487  158 ILE C CB  
5663  C  CG1 . ILE C  158 ? 0.4644 0.6323 0.2804 -0.0359 -0.0555 0.0790  158 ILE C CG1 
5664  C  CG2 . ILE C  158 ? 0.4974 0.2576 0.1881 0.0696  -0.0762 0.0054  158 ILE C CG2 
5665  C  CD1 . ILE C  158 ? 0.7200 0.3697 0.1789 0.0885  -0.0149 0.0452  158 ILE C CD1 
5666  N  N   . PHE C  159 ? 0.4770 0.4519 0.1859 -0.1257 -0.0925 0.1436  159 PHE C N   
5667  C  CA  . PHE C  159 ? 0.3465 0.3194 0.2167 -0.0208 -0.1387 0.1031  159 PHE C CA  
5668  C  C   . PHE C  159 ? 0.3499 0.4946 0.2621 -0.0344 -0.1930 0.0192  159 PHE C C   
5669  O  O   . PHE C  159 ? 0.5508 0.3743 0.1962 -0.0190 -0.0627 0.0754  159 PHE C O   
5670  C  CB  . PHE C  159 ? 0.5619 0.3438 0.1289 -0.1594 -0.0899 0.0736  159 PHE C CB  
5671  C  CG  . PHE C  159 ? 0.2996 0.5295 0.1714 -0.0768 -0.0568 0.0917  159 PHE C CG  
5672  C  CD1 . PHE C  159 ? 0.4414 0.6427 0.1662 -0.0575 -0.1308 0.1174  159 PHE C CD1 
5673  C  CD2 . PHE C  159 ? 0.3102 0.4138 0.2276 -0.0900 -0.1119 0.0966  159 PHE C CD2 
5674  C  CE1 . PHE C  159 ? 0.3754 0.5350 0.1732 -0.1084 -0.0922 0.1133  159 PHE C CE1 
5675  C  CE2 . PHE C  159 ? 0.3677 0.5468 0.1711 -0.0259 -0.0723 0.0619  159 PHE C CE2 
5676  C  CZ  . PHE C  159 ? 0.2845 0.5056 0.1673 0.0031  -0.0873 0.0186  159 PHE C CZ  
5677  N  N   . SER C  160 ? 0.4712 0.2219 0.1998 -0.0071 -0.0895 0.0763  160 SER C N   
5678  C  CA  . SER C  160 ? 0.4419 0.3652 0.2235 0.0500  -0.1528 -0.1081 160 SER C CA  
5679  C  C   . SER C  160 ? 0.3558 0.4814 0.1841 -0.0214 -0.1367 0.0237  160 SER C C   
5680  O  O   . SER C  160 ? 0.5365 0.5809 0.2278 -0.0449 -0.2003 0.0403  160 SER C O   
5681  C  CB  . SER C  160 ? 0.5691 0.4936 0.1181 0.1083  -0.0135 0.1068  160 SER C CB  
5682  O  OG  . SER C  160 ? 0.4214 0.3671 0.2646 0.0882  -0.1000 0.0313  160 SER C OG  
5683  N  N   . HIS C  161 ? 0.4626 0.4336 0.1675 -0.0969 -0.1358 0.0153  161 HIS C N   
5684  C  CA  . HIS C  161 ? 0.5042 0.4990 0.1958 -0.0597 -0.0688 0.0601  161 HIS C CA  
5685  C  C   . HIS C  161 ? 0.4277 0.2973 0.1474 -0.0966 -0.0901 -0.0153 161 HIS C C   
5686  O  O   . HIS C  161 ? 0.4077 0.3258 0.1967 -0.0723 -0.0993 0.0244  161 HIS C O   
5687  C  CB  . HIS C  161 ? 0.3571 0.7809 0.2174 -0.0689 -0.1504 0.1379  161 HIS C CB  
5688  C  CG  . HIS C  161 ? 0.3609 0.7559 0.4504 -0.0720 -0.1651 0.0903  161 HIS C CG  
5689  N  ND1 . HIS C  161 ? 0.4223 0.8755 0.6596 -0.2831 -0.2363 0.2682  161 HIS C ND1 
5690  C  CD2 . HIS C  161 ? 0.4706 0.4891 0.3235 -0.1846 -0.1921 0.1604  161 HIS C CD2 
5691  C  CE1 . HIS C  161 ? 0.5971 0.9294 0.4147 -0.1569 -0.1534 0.3517  161 HIS C CE1 
5692  N  NE2 . HIS C  161 ? 0.5551 0.7045 0.7605 -0.1519 -0.3517 0.3443  161 HIS C NE2 
5693  N  N   . LEU C  162 ? 0.4226 0.4291 0.2867 -0.0839 -0.1722 0.1169  162 LEU C N   
5694  C  CA  . LEU C  162 ? 0.3655 0.4203 0.1515 -0.0776 -0.0573 0.0737  162 LEU C CA  
5695  C  C   . LEU C  162 ? 0.2617 0.2644 0.1592 -0.0346 -0.1062 0.0287  162 LEU C C   
5696  O  O   . LEU C  162 ? 0.3894 0.2576 0.1971 -0.0187 -0.1305 -0.0073 162 LEU C O   
5697  C  CB  . LEU C  162 ? 0.4047 0.5077 0.1748 -0.0114 -0.1700 -0.0353 162 LEU C CB  
5698  C  CG  . LEU C  162 ? 0.4451 0.2910 0.2721 -0.0315 -0.2142 0.0015  162 LEU C CG  
5699  C  CD1 . LEU C  162 ? 0.3404 0.5422 0.3664 -0.0096 -0.1752 -0.0666 162 LEU C CD1 
5700  C  CD2 . LEU C  162 ? 0.4223 0.6750 0.2624 0.0041  -0.1412 0.0800  162 LEU C CD2 
5701  N  N   . GLN C  163 ? 0.4212 0.4034 0.1615 -0.1599 -0.1319 0.0384  163 GLN C N   
5702  C  CA  . GLN C  163 ? 0.5562 0.4214 0.1265 -0.2265 -0.1068 0.0399  163 GLN C CA  
5703  C  C   . GLN C  163 ? 0.3955 0.2016 0.2336 -0.0100 -0.0425 -0.0192 163 GLN C C   
5704  O  O   . GLN C  163 ? 0.3747 0.4043 0.4009 0.1120  -0.0794 -0.1533 163 GLN C O   
5705  C  CB  . GLN C  163 ? 0.6096 0.3738 0.1531 -0.2101 -0.0750 0.0292  163 GLN C CB  
5706  C  CG  . GLN C  163 ? 0.7038 0.4812 0.6050 -0.3251 -0.0573 0.3039  163 GLN C CG  
5707  C  CD  . GLN C  163 ? 0.7035 0.6510 0.1342 -0.2933 0.0891  0.0006  163 GLN C CD  
5708  O  OE1 . GLN C  163 ? 0.4529 0.8187 0.1842 -0.1718 -0.0154 -0.0615 163 GLN C OE1 
5709  N  NE2 . GLN C  163 ? 0.6159 0.7986 0.5243 -0.0241 -0.3970 0.0060  163 GLN C NE2 
5710  N  N   . HIS C  164 ? 0.3887 0.2998 0.1852 -0.0697 -0.1435 0.0498  164 HIS C N   
5711  C  CA  . HIS C  164 ? 0.3255 0.2915 0.3910 -0.0166 -0.2322 0.0763  164 HIS C CA  
5712  C  C   . HIS C  164 ? 0.5892 0.3127 0.2273 -0.1712 -0.2283 0.0992  164 HIS C C   
5713  O  O   . HIS C  164 ? 0.4348 0.3468 0.3273 -0.1337 -0.1833 0.0298  164 HIS C O   
5714  C  CB  . HIS C  164 ? 0.3680 0.3463 0.1978 -0.0399 -0.0637 0.0043  164 HIS C CB  
5715  C  CG  . HIS C  164 ? 0.2879 0.3628 0.1608 -0.1098 -0.0709 0.0520  164 HIS C CG  
5716  N  ND1 . HIS C  164 ? 0.2709 0.2705 0.1892 -0.0132 -0.0406 0.0013  164 HIS C ND1 
5717  C  CD2 . HIS C  164 ? 0.1890 0.4000 0.2538 -0.0763 -0.0225 -0.0454 164 HIS C CD2 
5718  C  CE1 . HIS C  164 ? 0.1678 0.3709 0.2447 0.0353  0.0320  0.1186  164 HIS C CE1 
5719  N  NE2 . HIS C  164 ? 0.2698 0.3682 0.2874 0.0392  -0.0988 0.0243  164 HIS C NE2 
5720  N  N   . VAL C  165 ? 0.3201 0.3908 0.2608 -0.1036 -0.1538 0.0900  165 VAL C N   
5721  C  CA  . VAL C  165 ? 0.4147 0.3463 0.2343 -0.1797 -0.1396 0.1089  165 VAL C CA  
5722  C  C   . VAL C  165 ? 0.3901 0.3610 0.1817 -0.1481 -0.0771 0.0091  165 VAL C C   
5723  O  O   . VAL C  165 ? 0.3765 0.4368 0.1705 -0.1906 -0.0798 0.0723  165 VAL C O   
5724  C  CB  . VAL C  165 ? 0.3506 0.2303 0.2445 0.0203  -0.1068 0.0377  165 VAL C CB  
5725  C  CG1 . VAL C  165 ? 0.3621 0.2626 0.3626 -0.0286 -0.1526 0.1013  165 VAL C CG1 
5726  C  CG2 . VAL C  165 ? 0.5652 0.2305 0.1646 -0.0115 0.0870  0.0206  165 VAL C CG2 
5727  N  N   . LYS C  166 ? 0.4638 0.7777 0.1540 -0.3316 -0.0564 0.0895  166 LYS C N   
5728  C  CA  . LYS C  166 ? 0.3797 0.6701 0.1316 -0.1915 -0.0900 0.0791  166 LYS C CA  
5729  C  C   . LYS C  166 ? 0.3869 0.6157 0.2493 -0.2300 0.0043  0.0751  166 LYS C C   
5730  O  O   . LYS C  166 ? 0.3991 0.7501 0.1563 -0.2949 -0.0794 0.0703  166 LYS C O   
5731  C  CB  . LYS C  166 ? 0.5533 0.6129 0.1534 -0.2217 -0.0430 0.0768  166 LYS C CB  
5732  C  CG  . LYS C  166 ? 0.6065 0.5116 0.1725 -0.2930 0.0118  0.0372  166 LYS C CG  
5733  C  CD  . LYS C  166 ? 0.7159 0.7768 0.1554 -0.3546 -0.0256 0.0120  166 LYS C CD  
5734  C  CE  . LYS C  166 ? 0.8256 0.4694 0.2630 -0.1370 0.0035  0.0452  166 LYS C CE  
5735  N  NZ  . LYS C  166 ? 0.7401 0.4713 0.1694 0.0131  -0.0559 0.0597  166 LYS C NZ  
5736  N  N   . TYR C  167 ? 0.3059 0.4418 0.0888 -0.0904 -0.0043 0.0500  167 TYR C N   
5737  C  CA  . TYR C  167 ? 0.4383 0.4584 0.1838 -0.1350 -0.0399 0.0709  167 TYR C CA  
5738  C  C   . TYR C  167 ? 0.5083 0.3163 0.1420 -0.0250 -0.0353 0.0485  167 TYR C C   
5739  O  O   . TYR C  167 ? 0.4892 0.4375 0.1396 -0.1269 -0.0189 -0.0551 167 TYR C O   
5740  C  CB  . TYR C  167 ? 0.5537 0.8981 0.1247 -0.3283 0.0216  -0.0507 167 TYR C CB  
5741  C  CG  . TYR C  167 ? 0.5670 1.0364 0.1516 -0.3731 -0.1024 0.1172  167 TYR C CG  
5742  C  CD1 . TYR C  167 ? 0.6151 0.9355 0.0983 -0.3172 0.0698  -0.0012 167 TYR C CD1 
5743  C  CD2 . TYR C  167 ? 0.3167 1.2007 0.1709 -0.2124 -0.0258 0.0509  167 TYR C CD2 
5744  C  CE1 . TYR C  167 ? 0.6165 1.2338 0.3357 -0.0326 0.0860  0.4427  167 TYR C CE1 
5745  C  CE2 . TYR C  167 ? 0.5658 1.2619 0.1817 -0.0601 0.0829  0.1212  167 TYR C CE2 
5746  C  CZ  . TYR C  167 ? 0.6895 2.0104 0.5159 0.2102  0.2888  0.7037  167 TYR C CZ  
5747  O  OH  . TYR C  167 ? 1.0240 2.8663 3.0281 0.9506  1.4056  2.7142  167 TYR C OH  
5748  N  N   . LYS C  168 ? 0.3508 0.3822 0.1674 -0.1177 0.0000  0.0044  168 LYS C N   
5749  C  CA  . LYS C  168 ? 0.3476 0.2339 0.1642 -0.0414 -0.0170 -0.0216 168 LYS C CA  
5750  C  C   . LYS C  168 ? 0.3840 0.2628 0.1615 -0.0329 0.0063  -0.0733 168 LYS C C   
5751  O  O   . LYS C  168 ? 0.5655 0.4004 0.1736 -0.1639 0.0379  -0.1001 168 LYS C O   
5752  C  CB  . LYS C  168 ? 0.3648 0.2470 0.2565 -0.0173 0.0160  0.0296  168 LYS C CB  
5753  C  CG  . LYS C  168 ? 0.4251 0.2885 0.1665 -0.0445 0.0093  -0.0080 168 LYS C CG  
5754  C  CD  . LYS C  168 ? 0.4537 0.3314 0.2615 0.0632  -0.0074 -0.0172 168 LYS C CD  
5755  C  CE  . LYS C  168 ? 0.4781 0.3370 0.3337 0.0976  -0.0082 0.0828  168 LYS C CE  
5756  N  NZ  . LYS C  168 ? 0.5519 0.5200 0.4490 0.1817  -0.0141 0.0408  168 LYS C NZ  
5757  N  N   . GLY C  169 ? 0.3429 0.2675 0.1877 -0.0812 0.0458  -0.0626 169 GLY C N   
5758  C  CA  . GLY C  169 ? 0.3869 0.3278 0.2615 -0.1463 0.1019  -0.0408 169 GLY C CA  
5759  C  C   . GLY C  169 ? 0.4440 0.4862 0.1825 -0.1561 0.0542  0.0359  169 GLY C C   
5760  O  O   . GLY C  169 ? 0.4537 0.3233 0.2567 -0.1409 0.0715  -0.0260 169 GLY C O   
5761  N  N   . GLN C  170 ? 0.3910 0.2978 0.1824 -0.0245 0.0344  -0.0348 170 GLN C N   
5762  C  CA  . GLN C  170 ? 0.3307 0.3901 0.1906 -0.0942 0.0450  -0.0324 170 GLN C CA  
5763  C  C   . GLN C  170 ? 0.3540 0.3298 0.1818 -0.0962 -0.0601 -0.0483 170 GLN C C   
5764  O  O   . GLN C  170 ? 0.3883 0.2689 0.1518 -0.0760 -0.0166 -0.0274 170 GLN C O   
5765  C  CB  . GLN C  170 ? 0.3172 0.2879 0.2172 -0.0592 0.0305  -0.0687 170 GLN C CB  
5766  C  CG  . GLN C  170 ? 0.3043 0.4068 0.2524 -0.1448 0.1121  -0.0976 170 GLN C CG  
5767  C  CD  . GLN C  170 ? 0.4691 0.5626 0.6317 -0.3488 -0.0879 0.2657  170 GLN C CD  
5768  O  OE1 . GLN C  170 ? 0.4785 0.6672 0.0398 -0.2430 -0.0071 -0.0439 170 GLN C OE1 
5769  N  NE2 . GLN C  170 ? 0.7239 3.1642 3.4521 0.0914  -0.0694 -3.0185 170 GLN C NE2 
5770  N  N   . GLU C  171 ? 0.3375 0.3075 0.1592 -0.0759 -0.0074 -0.0480 171 GLU C N   
5771  C  CA  . GLU C  171 ? 0.3167 0.3050 0.1836 -0.0186 -0.0027 -0.0756 171 GLU C CA  
5772  C  C   . GLU C  171 ? 0.3865 0.3100 0.1389 -0.0854 -0.0350 -0.0397 171 GLU C C   
5773  O  O   . GLU C  171 ? 0.3569 0.4396 0.1601 -0.0901 -0.0226 -0.0843 171 GLU C O   
5774  C  CB  . GLU C  171 ? 0.4952 0.3463 0.2599 -0.0636 0.0700  0.0401  171 GLU C CB  
5775  C  CG  . GLU C  171 ? 0.3380 0.3862 0.3023 -0.0714 0.0798  0.0821  171 GLU C CG  
5776  C  CD  . GLU C  171 ? 0.3181 0.4778 0.6890 -0.0829 0.0612  0.2337  171 GLU C CD  
5777  O  OE1 . GLU C  171 ? 0.4501 0.6330 0.3749 -0.2806 -0.0288 0.1562  171 GLU C OE1 
5778  O  OE2 . GLU C  171 ? 0.6467 0.3179 0.3558 -0.0148 0.0923  -0.0181 171 GLU C OE2 
5779  N  N   . ALA C  172 ? 0.2671 0.3932 0.1412 -0.0603 -0.0226 -0.1334 172 ALA C N   
5780  C  CA  . ALA C  172 ? 0.2885 0.3892 0.3278 -0.1181 -0.0878 0.1284  172 ALA C CA  
5781  C  C   . ALA C  172 ? 0.5044 0.3476 0.2222 -0.0546 -0.2274 -0.0403 172 ALA C C   
5782  O  O   . ALA C  172 ? 0.5914 0.4619 0.2021 -0.0467 -0.2158 -0.0399 172 ALA C O   
5783  C  CB  . ALA C  172 ? 0.3844 0.4766 0.3273 -0.2386 -0.1108 0.1099  172 ALA C CB  
5784  N  N   . PHE C  173 ? 0.5174 0.4122 0.2987 0.0142  -0.2090 0.0377  173 PHE C N   
5785  C  CA  . PHE C  173 ? 0.8338 0.2208 0.5552 0.1017  0.0066  -0.2029 173 PHE C CA  
5786  C  C   . PHE C  173 ? 0.9193 0.3352 0.3091 -0.0278 -0.1596 0.0710  173 PHE C C   
5787  O  O   . PHE C  173 ? 0.4802 0.3380 0.2973 0.0394  -0.1571 0.0060  173 PHE C O   
5788  C  CB  . PHE C  173 ? 0.9176 0.4410 0.2319 0.0832  -0.1629 0.0263  173 PHE C CB  
5789  C  CG  . PHE C  173 ? 0.5159 0.4230 0.2053 0.0522  -0.1805 -0.0260 173 PHE C CG  
5790  C  CD1 . PHE C  173 ? 0.7554 0.5504 0.3100 -0.1251 -0.0693 -0.0949 173 PHE C CD1 
5791  C  CD2 . PHE C  173 ? 0.6707 0.5099 0.1937 -0.0546 -0.1881 -0.0220 173 PHE C CD2 
5792  C  CE1 . PHE C  173 ? 0.4194 0.7192 0.2951 -0.2619 -0.0026 -0.0737 173 PHE C CE1 
5793  C  CE2 . PHE C  173 ? 0.3129 0.4677 0.3946 0.1150  -0.0916 -0.1277 173 PHE C CE2 
5794  C  CZ  . PHE C  173 ? 0.5356 0.4601 0.2822 -0.1067 -0.0672 -0.0816 173 PHE C CZ  
5795  N  N   . VAL C  174 ? 0.6338 0.3219 0.4403 0.2053  -0.2834 -0.0983 174 VAL C N   
5796  C  CA  . VAL C  174 ? 0.6000 0.3145 0.4828 0.0010  -0.2727 0.0324  174 VAL C CA  
5797  C  C   . VAL C  174 ? 0.4361 0.5608 0.6772 0.0364  -0.3517 0.1074  174 VAL C C   
5798  O  O   . VAL C  174 ? 0.5670 0.2824 0.6352 0.0657  -0.4336 -0.0091 174 VAL C O   
5799  C  CB  . VAL C  174 ? 0.5626 0.3587 0.2861 0.1773  -0.2302 -0.0040 174 VAL C CB  
5800  C  CG1 . VAL C  174 ? 0.5846 0.3104 0.3016 0.0000  -0.2888 0.0315  174 VAL C CG1 
5801  C  CG2 . VAL C  174 ? 0.4882 0.3562 0.4271 0.0504  -0.0974 0.1264  174 VAL C CG2 
5802  N  N   . PRO C  175 ? 0.5568 0.3425 0.3910 0.0335  -0.2655 -0.1044 175 PRO C N   
5803  C  CA  . PRO C  175 ? 0.5184 0.4774 0.3686 0.0791  -0.2924 0.0707  175 PRO C CA  
5804  C  C   . PRO C  175 ? 0.5924 0.5385 0.4893 -0.3050 -0.3118 0.1041  175 PRO C C   
5805  O  O   . PRO C  175 ? 0.3777 0.4196 0.2899 -0.1259 -0.1203 0.1224  175 PRO C O   
5806  C  CB  . PRO C  175 ? 0.5662 0.4386 0.4383 -0.0362 -0.1333 0.1763  175 PRO C CB  
5807  C  CG  . PRO C  175 ? 0.4382 0.5453 0.6345 0.1332  -0.0993 0.2624  175 PRO C CG  
5808  C  CD  . PRO C  175 ? 0.6392 0.3526 0.3521 0.0887  -0.2520 -0.0507 175 PRO C CD  
5809  N  N   . GLY C  176 ? 0.6309 0.2398 0.3828 0.2065  -0.2953 -0.0491 176 GLY C N   
5810  C  CA  . GLY C  176 ? 0.4873 0.2917 0.5399 0.0800  -0.2662 -0.1942 176 GLY C CA  
5811  C  C   . GLY C  176 ? 0.5838 0.2039 0.8461 0.1425  -0.5105 -0.1052 176 GLY C C   
5812  O  O   . GLY C  176 ? 1.3145 2.5025 3.6735 -1.2028 -1.5793 2.3882  176 GLY C O   
5813  N  N   . PHE C  177 ? 0.4920 0.2088 0.3626 -0.0436 -0.1362 0.0093  177 PHE C N   
5814  C  CA  . PHE C  177 ? 0.4917 0.2296 0.3515 -0.0093 -0.3524 0.0038  177 PHE C CA  
5815  C  C   . PHE C  177 ? 0.5960 0.2414 0.3901 0.1862  -0.2484 -0.0542 177 PHE C C   
5816  O  O   . PHE C  177 ? 0.3874 0.2714 0.3109 0.1216  -0.1395 -0.0649 177 PHE C O   
5817  C  CB  . PHE C  177 ? 0.4891 0.2170 0.4465 0.0355  -0.2529 0.0559  177 PHE C CB  
5818  C  CG  . PHE C  177 ? 0.4020 0.3555 0.1684 0.1097  -0.0719 0.0304  177 PHE C CG  
5819  C  CD1 . PHE C  177 ? 0.4180 0.4406 0.2739 0.0966  -0.0339 -0.0324 177 PHE C CD1 
5820  C  CD2 . PHE C  177 ? 0.4469 0.6137 0.3125 -0.0010 -0.1489 0.0907  177 PHE C CD2 
5821  C  CE1 . PHE C  177 ? 0.4013 0.8234 0.3287 0.0127  -0.1138 0.0878  177 PHE C CE1 
5822  C  CE2 . PHE C  177 ? 0.3903 0.6079 0.1720 0.0104  -0.1015 0.1237  177 PHE C CE2 
5823  C  CZ  . PHE C  177 ? 0.3296 0.7182 0.1732 0.0089  -0.0432 0.0954  177 PHE C CZ  
5824  N  N   . ASN C  178 ? 0.4084 0.2657 0.3093 0.1107  -0.2027 -0.0522 178 ASN C N   
5825  C  CA  . ASN C  178 ? 0.3756 0.3361 0.3486 0.1863  -0.1503 0.0041  178 ASN C CA  
5826  C  C   . ASN C  178 ? 0.3492 0.2122 0.3012 0.1307  -0.1165 -0.0144 178 ASN C C   
5827  O  O   . ASN C  178 ? 0.3039 0.5781 0.3481 -0.0348 -0.1146 0.2518  178 ASN C O   
5828  C  CB  . ASN C  178 ? 0.2849 0.2786 0.4158 0.1272  -0.1112 0.0948  178 ASN C CB  
5829  C  CG  . ASN C  178 ? 0.3531 0.3212 0.4612 0.1208  -0.1841 0.0631  178 ASN C CG  
5830  O  OD1 . ASN C  178 ? 0.3747 0.3098 0.2772 0.1541  -0.0980 -0.0392 178 ASN C OD1 
5831  N  ND2 . ASN C  178 ? 0.2982 0.2748 0.4505 0.1743  -0.0335 0.0131  178 ASN C ND2 
5832  N  N   . ILE C  179 ? 0.2926 0.2289 0.2980 0.0630  -0.0934 0.0065  179 ILE C N   
5833  C  CA  . ILE C  179 ? 0.1868 0.2351 0.3616 0.0197  -0.0318 0.0656  179 ILE C CA  
5834  C  C   . ILE C  179 ? 0.2637 0.2490 0.1852 0.0037  0.0124  0.0266  179 ILE C C   
5835  O  O   . ILE C  179 ? 0.1975 0.3914 0.2433 0.0250  -0.0408 0.1380  179 ILE C O   
5836  C  CB  . ILE C  179 ? 0.2576 0.2585 0.2612 -0.0414 -0.0571 0.0318  179 ILE C CB  
5837  C  CG1 . ILE C  179 ? 0.2888 0.2662 0.2786 0.0271  -0.0502 -0.0724 179 ILE C CG1 
5838  C  CG2 . ILE C  179 ? 0.1999 0.3693 0.2976 0.0000  -0.0355 0.1299  179 ILE C CG2 
5839  C  CD1 . ILE C  179 ? 0.2772 0.2409 0.2788 -0.0118 -0.0452 -0.0724 179 ILE C CD1 
5840  N  N   . GLU C  180 ? 0.2797 0.1937 0.2271 0.0476  -0.0527 0.0177  180 GLU C N   
5841  C  CA  . GLU C  180 ? 0.2989 0.1714 0.2064 0.0474  -0.0480 0.0368  180 GLU C CA  
5842  C  C   . GLU C  180 ? 0.3639 0.1951 0.3571 0.1256  -0.0640 0.0886  180 GLU C C   
5843  O  O   . GLU C  180 ? 0.3095 0.4738 0.2407 -0.0071 -0.0671 0.1350  180 GLU C O   
5844  C  CB  . GLU C  180 ? 0.4065 0.3050 0.2337 0.0640  0.0141  0.0000  180 GLU C CB  
5845  C  CG  . GLU C  180 ? 0.3228 0.3508 0.3057 0.0812  0.0294  -0.0643 180 GLU C CG  
5846  C  CD  . GLU C  180 ? 0.4501 0.4967 0.2953 0.1375  0.0888  0.1014  180 GLU C CD  
5847  O  OE1 . GLU C  180 ? 0.4820 0.3185 0.4020 0.0425  -0.0185 -0.0855 180 GLU C OE1 
5848  O  OE2 . GLU C  180 ? 0.6646 0.4634 0.2793 0.2328  0.1325  0.0463  180 GLU C OE2 
5849  N  N   . GLU C  181 ? 0.2476 0.3968 0.3231 0.0966  -0.0353 0.2356  181 GLU C N   
5850  C  CA  . GLU C  181 ? 0.2969 0.3535 0.3282 0.0564  -0.0375 0.1915  181 GLU C CA  
5851  C  C   . GLU C  181 ? 0.2935 0.2007 0.3797 0.0377  0.0438  0.0131  181 GLU C C   
5852  O  O   . GLU C  181 ? 0.2228 0.4907 0.3355 -0.0291 -0.0727 0.2471  181 GLU C O   
5853  C  CB  . GLU C  181 ? 0.2470 0.8784 0.2874 0.0927  0.0031  0.2949  181 GLU C CB  
5854  C  CG  . GLU C  181 ? 0.2764 0.8460 0.6844 0.0286  0.0322  0.2676  181 GLU C CG  
5855  C  CD  . GLU C  181 ? 0.5798 1.0817 0.5218 0.0232  0.0709  0.2316  181 GLU C CD  
5856  O  OE1 . GLU C  181 ? 0.2912 0.8015 0.3959 0.0381  -0.0772 0.3287  181 GLU C OE1 
5857  O  OE2 . GLU C  181 ? 0.6022 0.8731 0.7635 -0.2063 -0.3995 0.5936  181 GLU C OE2 
5858  N  N   . LEU C  182 ? 0.2691 0.2624 0.2526 0.0276  -0.0780 0.0891  182 LEU C N   
5859  C  CA  . LEU C  182 ? 0.2603 0.2502 0.1572 0.0141  -0.0346 0.0445  182 LEU C CA  
5860  C  C   . LEU C  182 ? 0.2578 0.3215 0.1872 -0.0271 -0.0516 0.0996  182 LEU C C   
5861  O  O   . LEU C  182 ? 0.2333 0.3075 0.1896 0.0403  -0.0131 0.1010  182 LEU C O   
5862  C  CB  . LEU C  182 ? 0.2978 0.2492 0.2224 -0.0307 -0.1221 0.0667  182 LEU C CB  
5863  C  CG  . LEU C  182 ? 0.2946 0.2158 0.1516 0.0219  -0.0423 0.0156  182 LEU C CG  
5864  C  CD1 . LEU C  182 ? 0.3443 0.1806 0.2055 0.0245  -0.0211 0.0406  182 LEU C CD1 
5865  C  CD2 . LEU C  182 ? 0.3912 0.2948 0.1826 -0.0256 -0.0573 0.0206  182 LEU C CD2 
5866  N  N   . LEU C  183 ? 0.2296 0.3316 0.2245 0.0283  -0.0187 0.1460  183 LEU C N   
5867  C  CA  . LEU C  183 ? 0.2466 0.2818 0.2152 -0.0238 -0.0178 0.1045  183 LEU C CA  
5868  C  C   . LEU C  183 ? 0.1938 0.2233 0.2253 0.0575  -0.0212 0.0500  183 LEU C C   
5869  O  O   . LEU C  183 ? 0.2644 0.4318 0.2867 0.0496  -0.0869 0.1562  183 LEU C O   
5870  C  CB  . LEU C  183 ? 0.2477 0.1888 0.2606 0.0331  -0.0280 0.0553  183 LEU C CB  
5871  C  CG  . LEU C  183 ? 0.3337 0.2637 0.2118 -0.0115 0.0118  0.0848  183 LEU C CG  
5872  C  CD1 . LEU C  183 ? 0.2928 0.3486 0.2407 0.0641  0.0390  0.0864  183 LEU C CD1 
5873  C  CD2 . LEU C  183 ? 0.3386 0.4027 0.2187 0.0967  0.0031  0.1665  183 LEU C CD2 
5874  N  N   . PRO C  184 ? 0.1973 0.2721 0.2148 0.0068  0.0015  0.0885  184 PRO C N   
5875  C  CA  . PRO C  184 ? 0.2409 0.2089 0.2599 0.0494  -0.0291 0.0671  184 PRO C CA  
5876  C  C   . PRO C  184 ? 0.3702 0.1860 0.2030 0.0732  -0.0178 0.0610  184 PRO C C   
5877  O  O   . PRO C  184 ? 0.3560 0.3476 0.2772 0.0131  0.0829  0.0662  184 PRO C O   
5878  C  CB  . PRO C  184 ? 0.2737 0.2971 0.2802 0.0303  -0.0027 0.1526  184 PRO C CB  
5879  C  CG  . PRO C  184 ? 0.2797 0.2885 0.2626 -0.0326 -0.0041 0.1228  184 PRO C CG  
5880  C  CD  . PRO C  184 ? 0.2294 0.2351 0.1902 0.0313  -0.0346 0.0716  184 PRO C CD  
5881  N  N   . GLU C  185 ? 0.5242 0.1561 0.3388 0.0738  -0.0599 0.0458  185 GLU C N   
5882  C  CA  . GLU C  185 ? 0.6000 0.1154 0.3508 0.0219  -0.0942 0.0456  185 GLU C CA  
5883  C  C   . GLU C  185 ? 0.3255 0.2698 0.2536 0.0987  0.0148  0.0485  185 GLU C C   
5884  O  O   . GLU C  185 ? 0.3134 0.2533 0.3240 0.1062  0.0089  0.0872  185 GLU C O   
5885  C  CB  . GLU C  185 ? 0.7016 0.2308 0.3156 0.0443  0.1253  0.0856  185 GLU C CB  
5886  C  CG  . GLU C  185 ? 0.7092 0.4217 0.4651 0.1172  0.0908  0.2545  185 GLU C CG  
5887  C  CD  . GLU C  185 ? 0.9196 0.4698 0.5601 0.3768  0.1631  0.2642  185 GLU C CD  
5888  O  OE1 . GLU C  185 ? 0.6836 0.6744 0.4418 0.0105  -0.0729 0.1464  185 GLU C OE1 
5889  O  OE2 . GLU C  185 ? 1.2017 0.9275 0.4095 0.1180  0.0643  0.3404  185 GLU C OE2 
5890  N  N   . ARG C  186 ? 0.3465 0.2867 0.3156 0.1138  0.0562  0.1307  186 ARG C N   
5891  C  CA  . ARG C  186 ? 0.3592 0.2851 0.3300 -0.0184 0.0339  0.1585  186 ARG C CA  
5892  C  C   . ARG C  186 ? 0.2721 0.1685 0.2276 -0.0021 0.0193  0.0272  186 ARG C C   
5893  O  O   . ARG C  186 ? 0.2549 0.3183 0.2276 0.0908  0.0401  0.0914  186 ARG C O   
5894  C  CB  . ARG C  186 ? 0.2949 0.1838 0.5271 0.0168  0.0873  0.1242  186 ARG C CB  
5895  C  CG  . ARG C  186 ? 0.3264 0.2148 0.4972 0.0263  0.0065  0.1317  186 ARG C CG  
5896  C  CD  . ARG C  186 ? 0.4609 0.2039 0.5371 -0.0780 -0.0450 0.0806  186 ARG C CD  
5897  N  NE  . ARG C  186 ? 0.7118 0.2904 0.9315 -0.0905 0.1738  -0.1405 186 ARG C NE  
5898  C  CZ  . ARG C  186 ? 0.7520 0.4201 0.7742 -0.2114 0.1736  -0.1071 186 ARG C CZ  
5899  N  NH1 . ARG C  186 ? 1.1862 0.6279 0.8137 -0.5044 0.0631  -0.2166 186 ARG C NH1 
5900  N  NH2 . ARG C  186 ? 1.0044 0.2522 1.0003 0.0205  0.3907  -0.0241 186 ARG C NH2 
5901  N  N   . THR C  187 ? 0.2549 0.1802 0.2583 0.0227  0.0680  -0.0040 187 THR C N   
5902  C  CA  . THR C  187 ? 0.2603 0.1932 0.1840 0.0763  0.0727  0.0276  187 THR C CA  
5903  C  C   . THR C  187 ? 0.2477 0.3109 0.2211 0.1278  0.0969  0.0320  187 THR C C   
5904  O  O   . THR C  187 ? 0.2345 0.2919 0.2073 0.0970  0.0275  0.0351  187 THR C O   
5905  C  CB  . THR C  187 ? 0.2096 0.3194 0.2129 0.0467  0.0324  0.1014  187 THR C CB  
5906  O  OG1 . THR C  187 ? 0.2396 0.3856 0.2973 0.1084  -0.0105 0.0575  187 THR C OG1 
5907  C  CG2 . THR C  187 ? 0.2899 0.2398 0.2082 0.0172  0.0331  0.0535  187 THR C CG2 
5908  N  N   . ALA C  188 ? 0.2190 0.2709 0.1944 0.1083  0.0074  0.0485  188 ALA C N   
5909  C  CA  . ALA C  188 ? 0.2309 0.3167 0.1843 0.1520  0.0219  0.0566  188 ALA C CA  
5910  C  C   . ALA C  188 ? 0.1840 0.1806 0.1908 0.0696  0.0315  0.0546  188 ALA C C   
5911  O  O   . ALA C  188 ? 0.1967 0.1923 0.1813 0.0819  0.0148  0.0310  188 ALA C O   
5912  C  CB  . ALA C  188 ? 0.3368 0.2919 0.3039 0.1861  0.0222  0.0680  188 ALA C CB  
5913  N  N   . GLU C  189 ? 0.1966 0.2044 0.2124 0.0868  0.0516  0.0571  189 GLU C N   
5914  C  CA  . GLU C  189 ? 0.1971 0.1770 0.2193 0.0798  0.0760  0.0872  189 GLU C CA  
5915  C  C   . GLU C  189 ? 0.1876 0.2086 0.1712 0.0819  0.0807  0.0703  189 GLU C C   
5916  O  O   . GLU C  189 ? 0.1771 0.1629 0.1694 0.0515  0.0406  0.0535  189 GLU C O   
5917  C  CB  . GLU C  189 ? 0.2458 0.1432 0.3485 0.0511  0.0876  0.0852  189 GLU C CB  
5918  C  CG  . GLU C  189 ? 0.3537 0.1624 0.4153 0.0694  0.0626  0.0449  189 GLU C CG  
5919  C  CD  . GLU C  189 ? 0.6435 0.0888 0.5594 0.0997  0.2951  0.0777  189 GLU C CD  
5920  O  OE1 . GLU C  189 ? 0.3598 0.3684 0.4869 0.0857  0.1714  0.1541  189 GLU C OE1 
5921  O  OE2 . GLU C  189 ? 1.0523 0.2364 0.8241 -0.0822 0.4241  -0.0406 189 GLU C OE2 
5922  N  N   . TYR C  190 ? 0.1669 0.1305 0.1516 0.0441  0.0377  0.0288  190 TYR C N   
5923  C  CA  . TYR C  190 ? 0.1696 0.1333 0.1142 0.0364  0.0370  0.0216  190 TYR C CA  
5924  C  C   . TYR C  190 ? 0.1516 0.1283 0.0971 0.0120  0.0406  0.0216  190 TYR C C   
5925  O  O   . TYR C  190 ? 0.1795 0.1355 0.1297 0.0430  0.0384  0.0162  190 TYR C O   
5926  C  CB  . TYR C  190 ? 0.1550 0.1590 0.1174 0.0340  0.0351  0.0269  190 TYR C CB  
5927  C  CG  . TYR C  190 ? 0.1606 0.1412 0.1249 0.0302  0.0379  0.0226  190 TYR C CG  
5928  C  CD1 . TYR C  190 ? 0.1596 0.1237 0.1326 0.0275  0.0313  0.0015  190 TYR C CD1 
5929  C  CD2 . TYR C  190 ? 0.1534 0.2111 0.1484 0.0362  0.0353  0.0091  190 TYR C CD2 
5930  C  CE1 . TYR C  190 ? 0.1455 0.1544 0.1333 0.0344  0.0240  0.0001  190 TYR C CE1 
5931  C  CE2 . TYR C  190 ? 0.1493 0.1990 0.1389 0.0417  0.0328  0.0256  190 TYR C CE2 
5932  C  CZ  . TYR C  190 ? 0.1796 0.1639 0.1346 0.0326  0.0485  0.0087  190 TYR C CZ  
5933  O  OH  . TYR C  190 ? 0.1642 0.1996 0.1544 0.0434  0.0533  0.0217  190 TYR C OH  
5934  N  N   . TYR C  191 ? 0.1391 0.1111 0.1290 0.0250  0.0280  0.0185  191 TYR C N   
5935  C  CA  . TYR C  191 ? 0.1145 0.1098 0.1364 0.0271  0.0221  0.0278  191 TYR C CA  
5936  C  C   . TYR C  191 ? 0.1155 0.1116 0.1005 0.0146  0.0015  -0.0032 191 TYR C C   
5937  O  O   . TYR C  191 ? 0.1436 0.1416 0.0927 0.0065  0.0071  0.0052  191 TYR C O   
5938  C  CB  . TYR C  191 ? 0.1339 0.1089 0.1179 0.0048  0.0262  0.0190  191 TYR C CB  
5939  C  CG  . TYR C  191 ? 0.1545 0.1064 0.1295 0.0242  0.0304  -0.0043 191 TYR C CG  
5940  C  CD1 . TYR C  191 ? 0.1493 0.1294 0.1190 0.0103  0.0331  -0.0074 191 TYR C CD1 
5941  C  CD2 . TYR C  191 ? 0.1534 0.1195 0.1308 0.0304  0.0372  0.0297  191 TYR C CD2 
5942  C  CE1 . TYR C  191 ? 0.1728 0.1260 0.1389 0.0035  0.0406  -0.0008 191 TYR C CE1 
5943  C  CE2 . TYR C  191 ? 0.1407 0.1277 0.1826 0.0189  0.0244  0.0357  191 TYR C CE2 
5944  C  CZ  . TYR C  191 ? 0.1535 0.1127 0.1565 0.0034  0.0408  -0.0003 191 TYR C CZ  
5945  O  OH  . TYR C  191 ? 0.1932 0.1491 0.2163 -0.0277 0.0646  0.0163  191 TYR C OH  
5946  N  N   . ARG C  192 ? 0.1321 0.1118 0.1082 0.0187  0.0000  0.0152  192 ARG C N   
5947  C  CA  . ARG C  192 ? 0.1159 0.1116 0.0989 0.0102  0.0178  0.0006  192 ARG C CA  
5948  C  C   . ARG C  192 ? 0.1055 0.1070 0.0929 0.0021  0.0115  0.0113  192 ARG C C   
5949  O  O   . ARG C  192 ? 0.1319 0.1204 0.0897 -0.0010 0.0035  -0.0017 192 ARG C O   
5950  C  CB  . ARG C  192 ? 0.1179 0.1389 0.1247 0.0122  0.0259  -0.0129 192 ARG C CB  
5951  C  CG  . ARG C  192 ? 0.1508 0.1597 0.1118 -0.0163 0.0242  -0.0190 192 ARG C CG  
5952  C  CD  . ARG C  192 ? 0.1265 0.1570 0.1324 0.0049  0.0270  0.0013  192 ARG C CD  
5953  N  NE  . ARG C  192 ? 0.1439 0.1770 0.1195 0.0131  0.0412  -0.0159 192 ARG C NE  
5954  C  CZ  . ARG C  192 ? 0.1360 0.1757 0.1103 0.0057  0.0081  -0.0098 192 ARG C CZ  
5955  N  NH1 . ARG C  192 ? 0.1483 0.2213 0.1247 0.0012  0.0449  -0.0182 192 ARG C NH1 
5956  N  NH2 . ARG C  192 ? 0.1434 0.1872 0.1680 0.0038  0.0172  -0.0136 192 ARG C NH2 
5957  N  N   . TYR C  193 ? 0.1299 0.0878 0.0775 0.0048  0.0160  -0.0007 193 TYR C N   
5958  C  CA  . TYR C  193 ? 0.1091 0.0891 0.1112 0.0066  -0.0043 0.0023  193 TYR C CA  
5959  C  C   . TYR C  193 ? 0.0987 0.1195 0.0804 0.0049  0.0148  -0.0034 193 TYR C C   
5960  O  O   . TYR C  193 ? 0.1322 0.1066 0.0930 -0.0051 0.0019  0.0043  193 TYR C O   
5961  C  CB  . TYR C  193 ? 0.1124 0.1315 0.0777 -0.0013 0.0021  -0.0237 193 TYR C CB  
5962  C  CG  . TYR C  193 ? 0.0998 0.1041 0.0791 -0.0068 0.0051  -0.0006 193 TYR C CG  
5963  C  CD1 . TYR C  193 ? 0.1152 0.1165 0.0778 -0.0102 0.0116  0.0008  193 TYR C CD1 
5964  C  CD2 . TYR C  193 ? 0.1107 0.0983 0.0949 -0.0019 0.0054  -0.0078 193 TYR C CD2 
5965  C  CE1 . TYR C  193 ? 0.1202 0.0998 0.0876 -0.0111 0.0063  0.0060  193 TYR C CE1 
5966  C  CE2 . TYR C  193 ? 0.1103 0.1211 0.0852 0.0060  0.0024  -0.0071 193 TYR C CE2 
5967  C  CZ  . TYR C  193 ? 0.0918 0.1102 0.0878 0.0019  0.0175  -0.0171 193 TYR C CZ  
5968  O  OH  . TYR C  193 ? 0.1156 0.0904 0.0845 -0.0048 0.0214  -0.0057 193 TYR C OH  
5969  N  N   . ARG C  194 ? 0.1188 0.0942 0.0877 0.0031  0.0030  0.0012  194 ARG C N   
5970  C  CA  . ARG C  194 ? 0.1430 0.1073 0.0748 -0.0001 0.0282  -0.0087 194 ARG C CA  
5971  C  C   . ARG C  194 ? 0.1272 0.0859 0.0751 -0.0026 0.0017  0.0005  194 ARG C C   
5972  O  O   . ARG C  194 ? 0.1224 0.1127 0.1084 0.0049  -0.0133 -0.0082 194 ARG C O   
5973  C  CB  . ARG C  194 ? 0.2168 0.1240 0.0900 0.0028  0.0483  0.0107  194 ARG C CB  
5974  C  CG  . ARG C  194 ? 0.2664 0.1809 0.1498 0.0087  0.1001  0.0000  194 ARG C CG  
5975  C  CD  . ARG C  194 ? 0.4849 0.4960 0.3018 0.0832  0.2363  0.1538  194 ARG C CD  
5976  N  NE  . ARG C  194 ? 0.4704 0.8413 0.7504 0.0782  0.2624  -0.0544 194 ARG C NE  
5977  C  CZ  . ARG C  194 ? 0.6915 0.7955 0.8342 0.1280  0.1028  -0.6310 194 ARG C CZ  
5978  N  NH1 . ARG C  194 ? 0.3844 0.4992 0.2924 -0.1446 0.0976  -0.0935 194 ARG C NH1 
5979  N  NH2 . ARG C  194 ? 0.7382 0.8169 0.7587 0.2125  0.2164  -0.3921 194 ARG C NH2 
5980  N  N   . GLY C  195 ? 0.1172 0.1067 0.0750 -0.0019 0.0151  -0.0054 195 GLY C N   
5981  C  CA  . GLY C  195 ? 0.1107 0.1096 0.0947 -0.0028 0.0046  -0.0126 195 GLY C CA  
5982  C  C   . GLY C  195 ? 0.1247 0.0900 0.0895 -0.0104 0.0184  -0.0031 195 GLY C C   
5983  O  O   . GLY C  195 ? 0.1274 0.1161 0.0992 -0.0104 0.0221  -0.0129 195 GLY C O   
5984  N  N   . SER C  196 ? 0.1197 0.1009 0.0795 -0.0103 0.0174  -0.0114 196 SER C N   
5985  C  CA  . SER C  196 ? 0.1304 0.1046 0.1005 -0.0173 0.0119  -0.0241 196 SER C CA  
5986  C  C   . SER C  196 ? 0.1049 0.1109 0.1073 -0.0175 0.0288  -0.0146 196 SER C C   
5987  O  O   . SER C  196 ? 0.1256 0.1163 0.0961 -0.0116 0.0174  -0.0109 196 SER C O   
5988  C  CB  . SER C  196 ? 0.1216 0.1062 0.1085 -0.0104 0.0414  0.0059  196 SER C CB  
5989  O  OG  . SER C  196 ? 0.1290 0.0935 0.1010 -0.0049 0.0266  -0.0118 196 SER C OG  
5990  N  N   . LEU C  197 ? 0.1262 0.1247 0.0922 -0.0149 0.0034  -0.0221 197 LEU C N   
5991  C  CA  . LEU C  197 ? 0.1328 0.1328 0.0996 -0.0131 0.0115  -0.0388 197 LEU C CA  
5992  C  C   . LEU C  197 ? 0.1294 0.1155 0.0971 -0.0082 0.0038  -0.0196 197 LEU C C   
5993  O  O   . LEU C  197 ? 0.1342 0.1124 0.0966 -0.0105 0.0107  -0.0181 197 LEU C O   
5994  C  CB  . LEU C  197 ? 0.1464 0.1351 0.1310 -0.0329 0.0087  -0.0255 197 LEU C CB  
5995  C  CG  . LEU C  197 ? 0.1808 0.1554 0.1364 -0.0581 -0.0091 -0.0096 197 LEU C CG  
5996  C  CD1 . LEU C  197 ? 0.2136 0.1646 0.1523 -0.0175 0.0115  -0.0230 197 LEU C CD1 
5997  C  CD2 . LEU C  197 ? 0.1964 0.2449 0.2651 -0.0931 0.0135  -0.1133 197 LEU C CD2 
5998  N  N   . THR C  198 ? 0.1332 0.1341 0.1049 -0.0229 0.0065  -0.0143 198 THR C N   
5999  C  CA  . THR C  198 ? 0.1353 0.1177 0.1059 -0.0181 0.0217  -0.0049 198 THR C CA  
6000  C  C   . THR C  198 ? 0.1475 0.1237 0.1134 -0.0399 0.0085  -0.0225 198 THR C C   
6001  O  O   . THR C  198 ? 0.1490 0.1412 0.1136 -0.0269 0.0170  -0.0270 198 THR C O   
6002  C  CB  . THR C  198 ? 0.1482 0.1106 0.0782 -0.0057 0.0032  -0.0167 198 THR C CB  
6003  O  OG1 . THR C  198 ? 0.1435 0.1398 0.0806 -0.0265 0.0043  -0.0140 198 THR C OG1 
6004  C  CG2 . THR C  198 ? 0.1515 0.1319 0.0881 -0.0096 0.0238  -0.0121 198 THR C CG2 
6005  N  N   . THR C  199 ? 0.1606 0.1202 0.0994 -0.0366 0.0115  -0.0115 199 THR C N   
6006  C  CA  . THR C  199 ? 0.2039 0.1202 0.0930 -0.0115 0.0013  -0.0245 199 THR C CA  
6007  C  C   . THR C  199 ? 0.1457 0.1295 0.1125 -0.0293 0.0060  -0.0304 199 THR C C   
6008  O  O   . THR C  199 ? 0.1744 0.1490 0.0969 -0.0197 0.0218  -0.0115 199 THR C O   
6009  C  CB  . THR C  199 ? 0.2434 0.1391 0.1231 -0.0379 -0.0160 -0.0041 199 THR C CB  
6010  O  OG1 . THR C  199 ? 0.1949 0.2533 0.1579 -0.0368 -0.0085 0.0154  199 THR C OG1 
6011  C  CG2 . THR C  199 ? 0.2481 0.1658 0.1202 -0.0395 -0.0151 -0.0054 199 THR C CG2 
6012  N  N   . PRO C  200 ? 0.1506 0.1429 0.1046 -0.0287 0.0088  -0.0441 200 PRO C N   
6013  C  CA  . PRO C  200 ? 0.1520 0.1238 0.1565 -0.0368 0.0221  -0.0386 200 PRO C CA  
6014  C  C   . PRO C  200 ? 0.1814 0.1400 0.1213 -0.0447 -0.0129 -0.0408 200 PRO C C   
6015  O  O   . PRO C  200 ? 0.2002 0.1972 0.1484 -0.0489 0.0000  -0.0197 200 PRO C O   
6016  C  CB  . PRO C  200 ? 0.1611 0.1637 0.1382 -0.0250 0.0165  -0.0450 200 PRO C CB  
6017  C  CG  . PRO C  200 ? 0.1809 0.1699 0.1587 -0.0353 0.0375  -0.0483 200 PRO C CG  
6018  C  CD  . PRO C  200 ? 0.1698 0.1856 0.1041 -0.0282 0.0197  -0.0608 200 PRO C CD  
6019  N  N   . PRO C  201 ? 0.1632 0.1457 0.1482 -0.0425 0.0159  -0.0397 201 PRO C N   
6020  C  CA  . PRO C  201 ? 0.1646 0.1452 0.1247 -0.0505 0.0177  -0.0043 201 PRO C CA  
6021  C  C   . PRO C  201 ? 0.1506 0.1102 0.1228 -0.0262 0.0103  -0.0137 201 PRO C C   
6022  O  O   . PRO C  201 ? 0.1655 0.1046 0.1423 -0.0197 0.0296  -0.0115 201 PRO C O   
6023  C  CB  . PRO C  201 ? 0.1757 0.1434 0.1400 -0.0698 0.0256  -0.0392 201 PRO C CB  
6024  C  CG  . PRO C  201 ? 0.1797 0.1729 0.1744 -0.0617 0.0430  -0.0082 201 PRO C CG  
6025  C  CD  . PRO C  201 ? 0.1565 0.1508 0.2086 -0.0546 -0.0060 -0.0124 201 PRO C CD  
6026  N  N   . CYS C  202 ? 0.1244 0.1021 0.1407 -0.0229 0.0144  -0.0124 202 CYS C N   
6027  C  CA  . CYS C  202 ? 0.1143 0.1071 0.1182 -0.0170 0.0126  -0.0307 202 CYS C CA  
6028  C  C   . CYS C  202 ? 0.1185 0.1021 0.1335 -0.0194 0.0093  -0.0156 202 CYS C C   
6029  O  O   . CYS C  202 ? 0.1312 0.1109 0.1190 -0.0197 0.0125  -0.0074 202 CYS C O   
6030  C  CB  . CYS C  202 ? 0.1262 0.1006 0.1288 -0.0109 0.0274  -0.0119 202 CYS C CB  
6031  S  SG  . CYS C  202 ? 0.1459 0.1251 0.1143 -0.0197 0.0231  -0.0232 202 CYS C SG  
6032  N  N   . ASN C  203 ? 0.1215 0.1200 0.1246 -0.0278 0.0212  -0.0204 203 ASN C N   
6033  C  CA  . ASN C  203 ? 0.1305 0.1331 0.1369 -0.0410 0.0342  -0.0261 203 ASN C CA  
6034  C  C   . ASN C  203 ? 0.1156 0.1195 0.1253 -0.0241 0.0388  0.0070  203 ASN C C   
6035  O  O   . ASN C  203 ? 0.1337 0.1091 0.1012 -0.0199 0.0274  -0.0092 203 ASN C O   
6036  C  CB  . ASN C  203 ? 0.1337 0.1518 0.1933 -0.0586 0.0344  -0.0366 203 ASN C CB  
6037  C  CG  . ASN C  203 ? 0.1516 0.1585 0.1800 -0.0557 0.0403  -0.0199 203 ASN C CG  
6038  O  OD1 . ASN C  203 ? 0.1798 0.1446 0.1926 -0.0427 0.0278  -0.0401 203 ASN C OD1 
6039  N  ND2 . ASN C  203 ? 0.1942 0.1525 0.2206 -0.0542 0.0476  -0.0326 203 ASN C ND2 
6040  N  N   . PRO C  204 ? 0.1258 0.1091 0.1234 -0.0240 0.0359  -0.0031 204 PRO C N   
6041  C  CA  . PRO C  204 ? 0.1247 0.1276 0.1331 -0.0239 0.0322  -0.0240 204 PRO C CA  
6042  C  C   . PRO C  204 ? 0.1278 0.1145 0.1191 -0.0252 0.0205  -0.0113 204 PRO C C   
6043  O  O   . PRO C  204 ? 0.1597 0.1639 0.1146 -0.0013 0.0199  -0.0032 204 PRO C O   
6044  C  CB  . PRO C  204 ? 0.1601 0.1365 0.1457 0.0015  0.0129  0.0114  204 PRO C CB  
6045  C  CG  . PRO C  204 ? 0.1951 0.1394 0.1353 -0.0013 0.0250  0.0183  204 PRO C CG  
6046  C  CD  . PRO C  204 ? 0.1937 0.1048 0.1444 -0.0098 0.0175  0.0140  204 PRO C CD  
6047  N  N   . THR C  205 ? 0.1272 0.1188 0.1220 -0.0185 0.0211  0.0010  205 THR C N   
6048  C  CA  . THR C  205 ? 0.1194 0.1396 0.1414 -0.0126 0.0114  -0.0046 205 THR C CA  
6049  C  C   . THR C  205 ? 0.1141 0.1541 0.1258 -0.0350 0.0194  -0.0234 205 THR C C   
6050  O  O   . THR C  205 ? 0.1130 0.1660 0.1490 -0.0108 0.0189  -0.0140 205 THR C O   
6051  C  CB  . THR C  205 ? 0.1419 0.1387 0.1353 -0.0218 0.0366  -0.0192 205 THR C CB  
6052  O  OG1 . THR C  205 ? 0.1533 0.1402 0.1601 -0.0370 0.0226  -0.0143 205 THR C OG1 
6053  C  CG2 . THR C  205 ? 0.1513 0.1204 0.2052 -0.0196 0.0175  0.0024  205 THR C CG2 
6054  N  N   . VAL C  206 ? 0.1238 0.1089 0.1217 -0.0065 0.0221  0.0003  206 VAL C N   
6055  C  CA  . VAL C  206 ? 0.1246 0.1369 0.1096 -0.0137 -0.0015 0.0006  206 VAL C CA  
6056  C  C   . VAL C  206 ? 0.1152 0.1243 0.1008 -0.0024 0.0055  0.0055  206 VAL C C   
6057  O  O   . VAL C  206 ? 0.1143 0.1369 0.1281 -0.0086 -0.0104 -0.0010 206 VAL C O   
6058  C  CB  . VAL C  206 ? 0.1393 0.1215 0.0935 -0.0041 0.0137  0.0003  206 VAL C CB  
6059  C  CG1 . VAL C  206 ? 0.1202 0.1371 0.1001 -0.0172 0.0119  0.0012  206 VAL C CG1 
6060  C  CG2 . VAL C  206 ? 0.1547 0.1504 0.1242 -0.0229 0.0199  -0.0306 206 VAL C CG2 
6061  N  N   . LEU C  207 ? 0.1387 0.1140 0.0940 -0.0073 0.0098  0.0071  207 LEU C N   
6062  C  CA  . LEU C  207 ? 0.1310 0.1387 0.0976 0.0098  0.0148  -0.0077 207 LEU C CA  
6063  C  C   . LEU C  207 ? 0.1109 0.1209 0.0886 0.0000  0.0013  -0.0120 207 LEU C C   
6064  O  O   . LEU C  207 ? 0.1247 0.1289 0.0935 -0.0024 -0.0049 0.0030  207 LEU C O   
6065  C  CB  . LEU C  207 ? 0.1500 0.1615 0.1191 0.0073  0.0507  -0.0031 207 LEU C CB  
6066  C  CG  . LEU C  207 ? 0.2527 0.1612 0.1674 0.0478  0.0304  -0.0052 207 LEU C CG  
6067  C  CD1 . LEU C  207 ? 0.3673 0.2046 0.1957 -0.0055 -0.0395 -0.0584 207 LEU C CD1 
6068  C  CD2 . LEU C  207 ? 0.2949 0.4345 0.3314 0.0800  0.1653  -0.1246 207 LEU C CD2 
6069  N  N   . TRP C  208 ? 0.1118 0.1141 0.0885 0.0098  0.0087  -0.0080 208 TRP C N   
6070  C  CA  . TRP C  208 ? 0.1079 0.1249 0.0985 0.0015  0.0015  0.0114  208 TRP C CA  
6071  C  C   . TRP C  208 ? 0.1079 0.1140 0.0789 -0.0060 0.0093  0.0080  208 TRP C C   
6072  O  O   . TRP C  208 ? 0.1292 0.1292 0.0917 0.0135  0.0063  -0.0051 208 TRP C O   
6073  C  CB  . TRP C  208 ? 0.0949 0.1279 0.1071 0.0062  0.0103  -0.0133 208 TRP C CB  
6074  C  CG  . TRP C  208 ? 0.0966 0.1290 0.0705 -0.0024 0.0041  0.0219  208 TRP C CG  
6075  C  CD1 . TRP C  208 ? 0.1296 0.1218 0.0744 -0.0071 0.0035  0.0028  208 TRP C CD1 
6076  C  CD2 . TRP C  208 ? 0.0868 0.1263 0.0703 -0.0008 0.0098  0.0006  208 TRP C CD2 
6077  N  NE1 . TRP C  208 ? 0.1077 0.1145 0.0922 -0.0071 0.0166  0.0032  208 TRP C NE1 
6078  C  CE2 . TRP C  208 ? 0.1177 0.1307 0.0804 -0.0085 0.0070  0.0024  208 TRP C CE2 
6079  C  CE3 . TRP C  208 ? 0.1055 0.1489 0.0931 -0.0078 0.0010  0.0148  208 TRP C CE3 
6080  C  CZ2 . TRP C  208 ? 0.1331 0.1563 0.0824 -0.0099 0.0189  0.0010  208 TRP C CZ2 
6081  C  CZ3 . TRP C  208 ? 0.1520 0.1349 0.0989 -0.0198 0.0081  0.0035  208 TRP C CZ3 
6082  C  CH2 . TRP C  208 ? 0.1523 0.1405 0.1067 -0.0283 0.0136  0.0076  208 TRP C CH2 
6083  N  N   . THR C  209 ? 0.1206 0.1268 0.0891 0.0132  0.0110  0.0149  209 THR C N   
6084  C  CA  . THR C  209 ? 0.1147 0.1392 0.0890 0.0159  0.0143  0.0108  209 THR C CA  
6085  C  C   . THR C  209 ? 0.1369 0.1606 0.0768 0.0226  -0.0006 0.0197  209 THR C C   
6086  O  O   . THR C  209 ? 0.1482 0.1854 0.0852 0.0131  0.0028  0.0151  209 THR C O   
6087  C  CB  . THR C  209 ? 0.1235 0.1569 0.1118 0.0157  0.0155  0.0137  209 THR C CB  
6088  O  OG1 . THR C  209 ? 0.1142 0.1811 0.1164 0.0186  0.0225  0.0017  209 THR C OG1 
6089  C  CG2 . THR C  209 ? 0.1425 0.1605 0.1623 0.0362  0.0280  0.0315  209 THR C CG2 
6090  N  N   . VAL C  210 ? 0.1102 0.1475 0.0949 0.0220  0.0130  0.0248  210 VAL C N   
6091  C  CA  . VAL C  210 ? 0.1358 0.1459 0.0987 0.0351  0.0154  0.0384  210 VAL C CA  
6092  C  C   . VAL C  210 ? 0.1308 0.1597 0.0996 0.0130  0.0060  0.0236  210 VAL C C   
6093  O  O   . VAL C  210 ? 0.1463 0.1222 0.1137 0.0165  0.0172  0.0212  210 VAL C O   
6094  C  CB  . VAL C  210 ? 0.1265 0.1292 0.1091 0.0068  0.0071  0.0186  210 VAL C CB  
6095  C  CG1 . VAL C  210 ? 0.1702 0.1644 0.1061 0.0230  0.0133  0.0254  210 VAL C CG1 
6096  C  CG2 . VAL C  210 ? 0.1603 0.1409 0.0857 0.0296  0.0026  0.0232  210 VAL C CG2 
6097  N  N   . PHE C  211 ? 0.1279 0.1531 0.1195 0.0362  0.0068  0.0410  211 PHE C N   
6098  C  CA  . PHE C  211 ? 0.1561 0.1560 0.1450 0.0307  0.0077  0.0634  211 PHE C CA  
6099  C  C   . PHE C  211 ? 0.1484 0.1475 0.1418 0.0262  0.0335  0.0733  211 PHE C C   
6100  O  O   . PHE C  211 ? 0.1735 0.1683 0.1324 0.0439  0.0300  0.0401  211 PHE C O   
6101  C  CB  . PHE C  211 ? 0.1720 0.1850 0.1332 -0.0010 -0.0124 0.0544  211 PHE C CB  
6102  C  CG  . PHE C  211 ? 0.1314 0.1826 0.1782 0.0375  0.0010  0.0697  211 PHE C CG  
6103  C  CD1 . PHE C  211 ? 0.1328 0.2781 0.1711 0.0612  0.0135  0.0701  211 PHE C CD1 
6104  C  CD2 . PHE C  211 ? 0.1646 0.2321 0.1798 0.0027  -0.0362 0.0737  211 PHE C CD2 
6105  C  CE1 . PHE C  211 ? 0.1208 0.2615 0.2075 0.0668  0.0070  0.0493  211 PHE C CE1 
6106  C  CE2 . PHE C  211 ? 0.1416 0.1965 0.2206 0.0241  -0.0307 0.0535  211 PHE C CE2 
6107  C  CZ  . PHE C  211 ? 0.1775 0.2301 0.2685 0.0289  -0.0109 0.0662  211 PHE C CZ  
6108  N  N   . ARG C  212 ? 0.1958 0.1472 0.1450 0.0350  0.0377  0.0454  212 ARG C N   
6109  C  CA  . ARG C  212 ? 0.1872 0.1459 0.1463 0.0315  0.0289  0.0297  212 ARG C CA  
6110  C  C   . ARG C  212 ? 0.1851 0.1831 0.1549 0.0342  0.0406  0.0564  212 ARG C C   
6111  O  O   . ARG C  212 ? 0.2063 0.1709 0.2016 0.0264  0.0590  0.0520  212 ARG C O   
6112  C  CB  . ARG C  212 ? 0.2050 0.1335 0.1754 0.0109  0.0375  0.0267  212 ARG C CB  
6113  C  CG  . ARG C  212 ? 0.2921 0.1554 0.1709 -0.0359 0.0395  -0.0199 212 ARG C CG  
6114  C  CD  . ARG C  212 ? 0.3406 0.1976 0.2470 -0.0335 0.0961  -0.0292 212 ARG C CD  
6115  N  NE  . ARG C  212 ? 0.4318 0.2174 0.3194 -0.1253 0.1248  -0.0824 212 ARG C NE  
6116  C  CZ  . ARG C  212 ? 0.5778 0.2179 0.3434 -0.2125 0.1019  -0.0548 212 ARG C CZ  
6117  N  NH1 . ARG C  212 ? 0.7095 0.2766 0.3828 0.0040  0.1817  0.0329  212 ARG C NH1 
6118  N  NH2 . ARG C  212 ? 0.7225 0.2942 0.3134 -0.2206 0.0606  -0.0531 212 ARG C NH2 
6119  N  N   . ASN C  213 ? 0.1872 0.2028 0.1886 0.0233  0.0346  0.0961  213 ASN C N   
6120  C  CA  . ASN C  213 ? 0.2179 0.2023 0.1791 0.0342  0.0063  0.0974  213 ASN C CA  
6121  C  C   . ASN C  213 ? 0.2418 0.2127 0.1516 0.0469  0.0094  0.0984  213 ASN C C   
6122  O  O   . ASN C  213 ? 0.2190 0.2105 0.1917 0.0421  0.0370  0.0648  213 ASN C O   
6123  C  CB  . ASN C  213 ? 0.2752 0.2416 0.2257 0.0868  0.0577  0.0943  213 ASN C CB  
6124  C  CG  . ASN C  213 ? 0.3476 0.1304 0.3321 0.0511  0.0910  0.0917  213 ASN C CG  
6125  O  OD1 . ASN C  213 ? 0.3300 0.2606 0.3962 0.0296  0.0816  0.0346  213 ASN C OD1 
6126  N  ND2 . ASN C  213 ? 0.3253 0.2897 0.2800 0.0298  0.1165  0.0362  213 ASN C ND2 
6127  N  N   . PRO C  214 ? 0.2075 0.1960 0.2100 0.0339  0.0156  0.0891  214 PRO C N   
6128  C  CA  . PRO C  214 ? 0.2324 0.2734 0.1247 0.0940  0.0244  0.0865  214 PRO C CA  
6129  C  C   . PRO C  214 ? 0.1818 0.2351 0.2235 0.0250  0.0031  0.1008  214 PRO C C   
6130  O  O   . PRO C  214 ? 0.2985 0.2804 0.2161 0.0793  0.0362  0.1375  214 PRO C O   
6131  C  CB  . PRO C  214 ? 0.2393 0.2445 0.1906 0.0505  0.0406  0.0790  214 PRO C CB  
6132  C  CG  . PRO C  214 ? 0.2495 0.2336 0.2023 0.0043  0.0368  0.0723  214 PRO C CG  
6133  C  CD  . PRO C  214 ? 0.2195 0.2518 0.1919 -0.0151 0.0463  0.0603  214 PRO C CD  
6134  N  N   . VAL C  215 ? 0.2326 0.2705 0.1905 0.0195  -0.0031 0.1380  215 VAL C N   
6135  C  CA  . VAL C  215 ? 0.2833 0.3815 0.1446 0.0331  0.0088  0.1412  215 VAL C CA  
6136  C  C   . VAL C  215 ? 0.2450 0.4400 0.1885 0.0879  0.0103  0.1692  215 VAL C C   
6137  O  O   . VAL C  215 ? 0.2284 0.3905 0.2154 0.0544  0.0340  0.1860  215 VAL C O   
6138  C  CB  . VAL C  215 ? 0.2639 0.3702 0.1852 0.0648  -0.0553 0.1318  215 VAL C CB  
6139  C  CG1 . VAL C  215 ? 0.2892 0.3467 0.2154 0.0189  0.0172  0.1413  215 VAL C CG1 
6140  C  CG2 . VAL C  215 ? 0.2646 0.3219 0.2536 0.0672  -0.0263 0.1694  215 VAL C CG2 
6141  N  N   . GLN C  216 ? 0.2199 0.4345 0.2237 0.0414  0.0046  0.2047  216 GLN C N   
6142  C  CA  . GLN C  216 ? 0.3025 0.4357 0.1698 0.1088  0.0370  0.1915  216 GLN C CA  
6143  C  C   . GLN C  216 ? 0.2908 0.5088 0.2675 0.0502  0.0269  0.2296  216 GLN C C   
6144  O  O   . GLN C  216 ? 0.2960 0.5835 0.2100 0.1244  0.0351  0.2317  216 GLN C O   
6145  C  CB  . GLN C  216 ? 0.2915 0.4041 0.2619 0.0702  0.0421  0.2110  216 GLN C CB  
6146  C  CG  . GLN C  216 ? 0.2644 0.3504 0.5015 -0.0038 -0.0789 0.2372  216 GLN C CG  
6147  C  CD  . GLN C  216 ? 0.6998 0.3517 0.5264 -0.1027 -0.0259 0.2944  216 GLN C CD  
6148  O  OE1 . GLN C  216 ? 0.6460 0.6035 0.6273 -0.0997 -0.0285 0.2865  216 GLN C OE1 
6149  N  NE2 . GLN C  216 ? 0.7730 0.7447 0.3935 0.0491  -0.0491 0.2140  216 GLN C NE2 
6150  N  N   . ILE C  217 ? 0.2702 0.3971 0.1752 -0.0026 -0.0070 0.1806  217 ILE C N   
6151  C  CA  . ILE C  217 ? 0.2931 0.4244 0.1319 0.0000  0.0024  0.1532  217 ILE C CA  
6152  C  C   . ILE C  217 ? 0.3689 0.4058 0.2624 -0.0997 -0.0816 0.2145  217 ILE C C   
6153  O  O   . ILE C  217 ? 0.2529 0.5232 0.1980 -0.0147 -0.0076 0.1835  217 ILE C O   
6154  C  CB  . ILE C  217 ? 0.2648 0.4636 0.2413 -0.0208 -0.0340 0.1976  217 ILE C CB  
6155  C  CG1 . ILE C  217 ? 0.2157 0.4296 0.1234 -0.0522 0.0003  0.0850  217 ILE C CG1 
6156  C  CG2 . ILE C  217 ? 0.2763 0.4397 0.1962 -0.0702 -0.0324 0.1897  217 ILE C CG2 
6157  C  CD1 . ILE C  217 ? 0.2885 0.4320 0.1725 -0.1147 -0.0293 0.1385  217 ILE C CD1 
6158  N  N   . SER C  218 ? 0.3436 0.4806 0.1726 0.0280  0.0049  0.1805  218 SER C N   
6159  C  CA  . SER C  218 ? 0.3569 0.3761 0.1851 0.0151  -0.0015 0.1477  218 SER C CA  
6160  C  C   . SER C  218 ? 0.3752 0.4475 0.0894 0.0466  0.1216  0.1114  218 SER C C   
6161  O  O   . SER C  218 ? 0.3222 0.4788 0.2026 -0.0285 -0.0230 0.1507  218 SER C O   
6162  C  CB  . SER C  218 ? 0.3517 0.5261 0.2962 -0.0222 -0.0701 0.2389  218 SER C CB  
6163  O  OG  . SER C  218 ? 0.3449 0.6261 0.2366 0.0155  -0.0156 0.1972  218 SER C OG  
6164  N  N   . GLN C  219 ? 0.3567 0.4677 0.2138 0.0285  0.0452  0.1273  219 GLN C N   
6165  C  CA  . GLN C  219 ? 0.3321 0.4212 0.1826 -0.0076 0.0744  0.0984  219 GLN C CA  
6166  C  C   . GLN C  219 ? 0.3402 0.4882 0.1999 -0.0531 0.0414  0.1305  219 GLN C C   
6167  O  O   . GLN C  219 ? 0.2874 0.5121 0.1764 -0.0206 0.0108  0.1404  219 GLN C O   
6168  C  CB  . GLN C  219 ? 0.4099 0.4885 0.2570 -0.1528 0.0245  0.0859  219 GLN C CB  
6169  N  N   . GLU C  220 ? 0.4216 0.5047 0.1215 0.0643  0.0445  0.1132  220 GLU C N   
6170  C  CA  . GLU C  220 ? 0.4250 0.4977 0.1919 -0.0054 0.0346  0.1333  220 GLU C CA  
6171  C  C   . GLU C  220 ? 0.2409 0.4762 0.1777 0.0267  -0.0126 -0.0006 220 GLU C C   
6172  O  O   . GLU C  220 ? 0.3479 0.4435 0.0960 0.0284  0.0140  0.1039  220 GLU C O   
6173  C  CB  . GLU C  220 ? 0.5078 0.6460 0.1123 0.0399  0.0273  0.1652  220 GLU C CB  
6174  C  CG  . GLU C  220 ? 0.6036 0.5073 0.2048 -0.0102 0.0610  0.1168  220 GLU C CG  
6175  C  CD  . GLU C  220 ? 0.5404 0.5163 0.2732 -0.1692 0.1449  0.0500  220 GLU C CD  
6176  O  OE1 . GLU C  220 ? 0.8263 0.3720 0.3434 -0.0723 0.2610  -0.0010 220 GLU C OE1 
6177  O  OE2 . GLU C  220 ? 0.7166 0.4043 0.1750 -0.0908 0.0666  0.0901  220 GLU C OE2 
6178  N  N   . GLN C  221 ? 0.2901 0.4251 0.1455 -0.0227 -0.0230 0.0666  221 GLN C N   
6179  C  CA  . GLN C  221 ? 0.2370 0.4336 0.2070 0.0118  0.0003  0.1234  221 GLN C CA  
6180  C  C   . GLN C  221 ? 0.2273 0.5332 0.1504 0.0498  -0.0087 0.0741  221 GLN C C   
6181  O  O   . GLN C  221 ? 0.3258 0.5813 0.0924 -0.0097 -0.0494 0.1146  221 GLN C O   
6182  C  CB  . GLN C  221 ? 0.2759 0.5088 0.1468 0.0461  0.0007  0.1058  221 GLN C CB  
6183  C  CG  . GLN C  221 ? 0.2831 0.4745 0.2849 -0.0271 -0.0834 0.1861  221 GLN C CG  
6184  C  CD  . GLN C  221 ? 0.8402 0.7592 0.3438 0.1641  -0.0193 0.1027  221 GLN C CD  
6185  O  OE1 . GLN C  221 ? 0.3564 0.6118 0.1714 0.1023  0.0715  0.2214  221 GLN C OE1 
6186  N  NE2 . GLN C  221 ? 0.9673 1.2223 0.4845 -0.1588 0.1483  0.1370  221 GLN C NE2 
6187  N  N   . LEU C  222 ? 0.2662 0.5074 0.1630 -0.0384 0.0052  0.1666  222 LEU C N   
6188  C  CA  . LEU C  222 ? 0.2624 0.4363 0.1416 -0.0485 0.0080  0.1268  222 LEU C CA  
6189  C  C   . LEU C  222 ? 0.3158 0.6093 0.0992 -0.0864 0.0237  0.0236  222 LEU C C   
6190  O  O   . LEU C  222 ? 0.2524 0.6268 0.0900 -0.0873 -0.0289 0.1106  222 LEU C O   
6191  C  CB  . LEU C  222 ? 0.2759 0.5458 0.1312 -0.0193 -0.0001 0.0798  222 LEU C CB  
6192  C  CG  . LEU C  222 ? 0.2592 0.4729 0.1258 -0.0310 0.0082  0.1049  222 LEU C CG  
6193  C  CD1 . LEU C  222 ? 0.2384 0.4081 0.1246 -0.0201 -0.0182 0.0961  222 LEU C CD1 
6194  C  CD2 . LEU C  222 ? 0.2208 0.4454 0.1621 -0.0310 0.0362  0.1143  222 LEU C CD2 
6195  N  N   . LEU C  223 ? 0.3282 0.5715 0.1202 -0.0463 -0.0188 0.0948  223 LEU C N   
6196  C  CA  . LEU C  223 ? 0.2732 0.5206 0.0989 -0.0093 0.0255  0.0966  223 LEU C CA  
6197  C  C   . LEU C  223 ? 0.2829 0.4717 0.1308 0.0348  0.0621  0.1378  223 LEU C C   
6198  O  O   . LEU C  223 ? 0.3371 0.4460 0.0908 -0.0247 -0.0010 0.0553  223 LEU C O   
6199  C  CB  . LEU C  223 ? 0.3573 0.4801 0.0890 0.0421  0.0288  0.0701  223 LEU C CB  
6200  C  CG  . LEU C  223 ? 0.4810 0.3079 0.1890 0.0681  0.0882  0.0093  223 LEU C CG  
6201  C  CD1 . LEU C  223 ? 0.5030 0.4602 0.2380 0.1821  0.2791  0.1661  223 LEU C CD1 
6202  C  CD2 . LEU C  223 ? 0.4694 0.5850 0.1071 -0.0524 0.1229  0.1030  223 LEU C CD2 
6203  N  N   . ALA C  224 ? 0.3039 0.4056 0.1230 -0.0076 -0.0089 0.0612  224 ALA C N   
6204  C  CA  . ALA C  224 ? 0.3826 0.4386 0.1919 -0.0742 -0.0790 0.0693  224 ALA C CA  
6205  C  C   . ALA C  224 ? 0.3558 0.4954 0.1141 -0.0886 -0.0344 0.0688  224 ALA C C   
6206  O  O   . ALA C  224 ? 0.3404 0.5383 0.1258 -0.0663 -0.0377 0.0452  224 ALA C O   
6207  C  CB  . ALA C  224 ? 0.3465 0.4047 0.1423 -0.0390 -0.0551 0.0108  224 ALA C CB  
6208  N  N   . LEU C  225 ? 0.2824 0.5041 0.1459 -0.0634 0.0071  0.0870  225 LEU C N   
6209  C  CA  . LEU C  225 ? 0.2790 0.5246 0.1208 -0.0603 -0.0132 0.0995  225 LEU C CA  
6210  C  C   . LEU C  225 ? 0.2565 0.4271 0.1136 -0.0763 -0.0261 0.0582  225 LEU C C   
6211  O  O   . LEU C  225 ? 0.3001 0.4523 0.1405 -0.0825 -0.0200 0.0170  225 LEU C O   
6212  C  CB  . LEU C  225 ? 0.2542 0.4589 0.1161 -0.0105 -0.0119 0.0847  225 LEU C CB  
6213  C  CG  . LEU C  225 ? 0.2572 0.4917 0.1102 -0.0855 -0.0086 0.0724  225 LEU C CG  
6214  C  CD1 . LEU C  225 ? 0.2447 0.4562 0.1989 -0.1137 -0.0482 0.1107  225 LEU C CD1 
6215  C  CD2 . LEU C  225 ? 0.2596 0.5048 0.0964 -0.0233 -0.0120 0.0661  225 LEU C CD2 
6216  N  N   . GLU C  226 ? 0.2888 0.4625 0.0757 -0.1055 -0.0233 0.0173  226 GLU C N   
6217  C  CA  . GLU C  226 ? 0.3163 0.4079 0.1028 -0.0869 0.0152  0.0165  226 GLU C CA  
6218  C  C   . GLU C  226 ? 0.2852 0.4298 0.1238 -0.0811 0.0074  -0.0109 226 GLU C C   
6219  O  O   . GLU C  226 ? 0.2942 0.4314 0.1486 -0.0306 0.0057  -0.0239 226 GLU C O   
6220  C  CB  . GLU C  226 ? 0.3418 0.4433 0.0824 -0.1137 -0.0151 0.0357  226 GLU C CB  
6221  C  CG  . GLU C  226 ? 0.3124 0.4645 0.1003 -0.1019 0.0386  0.0355  226 GLU C CG  
6222  C  CD  . GLU C  226 ? 0.2569 0.3711 0.0657 -0.0186 0.0176  0.0469  226 GLU C CD  
6223  O  OE1 . GLU C  226 ? 0.3061 0.4625 0.0921 -0.1076 0.0119  0.0662  226 GLU C OE1 
6224  O  OE2 . GLU C  226 ? 0.2966 0.4363 0.0847 -0.0617 -0.0026 0.0516  226 GLU C OE2 
6225  N  N   . THR C  227 ? 0.3084 0.5159 0.0821 -0.0918 0.0043  0.0020  227 THR C N   
6226  C  CA  . THR C  227 ? 0.3794 0.5253 0.0863 -0.1482 0.0282  0.0318  227 THR C CA  
6227  C  C   . THR C  227 ? 0.3472 0.6863 0.1006 -0.1542 -0.0304 -0.0225 227 THR C C   
6228  O  O   . THR C  227 ? 0.4724 0.5910 0.1288 -0.2416 0.0384  -0.0458 227 THR C O   
6229  C  CB  . THR C  227 ? 0.3382 0.3124 0.1143 -0.0560 0.0229  0.0062  227 THR C CB  
6230  O  OG1 . THR C  227 ? 0.4246 0.4128 0.1155 0.0046  0.0331  0.0076  227 THR C OG1 
6231  C  CG2 . THR C  227 ? 0.3551 0.4620 0.1886 -0.0820 -0.0093 0.0243  227 THR C CG2 
6232  N  N   . ALA C  228 ? 0.3217 0.6725 0.1673 -0.1715 -0.0230 0.1169  228 ALA C N   
6233  C  CA  . ALA C  228 ? 0.4210 0.6402 0.1721 -0.2226 0.0417  -0.0200 228 ALA C CA  
6234  C  C   . ALA C  228 ? 0.4989 0.6816 0.2172 -0.0989 -0.0877 -0.0657 228 ALA C C   
6235  O  O   . ALA C  228 ? 0.5762 0.7526 0.1807 -0.3802 -0.0555 0.1102  228 ALA C O   
6236  C  CB  . ALA C  228 ? 0.3546 0.6223 0.3470 -0.1723 0.0152  0.1266  228 ALA C CB  
6237  N  N   . LEU C  229 ? 0.3819 0.6338 0.1054 -0.2754 -0.0051 0.0524  229 LEU C N   
6238  C  CA  . LEU C  229 ? 0.3643 0.6779 0.1430 -0.2511 -0.0771 0.0186  229 LEU C CA  
6239  C  C   . LEU C  229 ? 0.4160 0.4990 0.1357 -0.2610 -0.0379 0.0060  229 LEU C C   
6240  O  O   . LEU C  229 ? 0.3643 0.6288 0.1384 -0.2158 -0.0263 -0.0087 229 LEU C O   
6241  C  CB  . LEU C  229 ? 0.3546 0.6868 0.1405 -0.2377 -0.0679 0.1050  229 LEU C CB  
6242  C  CG  . LEU C  229 ? 0.2529 0.7294 0.1461 -0.1994 -0.0252 0.0777  229 LEU C CG  
6243  C  CD1 . LEU C  229 ? 0.3192 0.8784 0.1367 -0.0423 -0.0044 0.0714  229 LEU C CD1 
6244  C  CD2 . LEU C  229 ? 0.2336 0.4846 0.2637 -0.0776 -0.0703 0.0388  229 LEU C CD2 
6245  N  N   . TYR C  230 ? 0.5149 0.5733 0.2204 -0.2572 -0.0662 0.0131  230 TYR C N   
6246  C  CA  . TYR C  230 ? 0.5727 0.4475 0.2472 -0.2225 -0.0957 0.0165  230 TYR C CA  
6247  C  C   . TYR C  230 ? 0.4687 0.4760 0.2300 -0.2471 -0.0339 0.0122  230 TYR C C   
6248  O  O   . TYR C  230 ? 0.4953 0.5120 0.1251 -0.2167 -0.0054 -0.1005 230 TYR C O   
6249  C  CB  . TYR C  230 ? 0.4462 0.7300 0.1337 -0.2594 -0.0221 0.0247  230 TYR C CB  
6250  C  CG  . TYR C  230 ? 0.5097 0.5852 0.1194 -0.1142 0.0074  0.0427  230 TYR C CG  
6251  C  CD1 . TYR C  230 ? 0.6539 0.4414 0.1990 -0.0957 -0.0107 0.0782  230 TYR C CD1 
6252  C  CD2 . TYR C  230 ? 0.5478 0.7157 0.3009 -0.1636 0.0882  -0.0728 230 TYR C CD2 
6253  C  CE1 . TYR C  230 ? 0.7784 0.3217 0.3756 -0.0068 0.0969  0.1670  230 TYR C CE1 
6254  C  CE2 . TYR C  230 ? 0.7487 0.7736 0.3810 -0.1088 0.2125  0.0582  230 TYR C CE2 
6255  C  CZ  . TYR C  230 ? 0.4305 0.8240 0.7251 -0.3125 -0.0131 0.2569  230 TYR C CZ  
6256  O  OH  . TYR C  230 ? 0.8640 0.9017 0.5471 -0.1359 0.2752  0.1250  230 TYR C OH  
6257  N  N   A CYS C  231 ? 0.4537 0.5634 0.1455 -0.2216 0.0273  -0.0221 231 CYS C N   
6258  N  N   B CYS C  231 ? 0.4851 0.4601 0.2808 -0.2263 -0.0284 -0.0267 231 CYS C N   
6259  C  CA  A CYS C  231 ? 0.4803 0.4386 0.1215 -0.2275 -0.0243 -0.0458 231 CYS C CA  
6260  C  CA  B CYS C  231 ? 0.6108 0.3370 0.2307 -0.1213 0.0000  -0.0711 231 CYS C CA  
6261  C  C   A CYS C  231 ? 0.5461 0.4408 0.1617 -0.2136 -0.0063 -0.0568 231 CYS C C   
6262  C  C   B CYS C  231 ? 0.5213 0.3255 0.1844 -0.2046 -0.1005 -0.0263 231 CYS C C   
6263  O  O   A CYS C  231 ? 0.2838 0.3986 0.2725 -0.0666 0.0181  -0.1146 231 CYS C O   
6264  O  O   B CYS C  231 ? 0.2305 0.2669 0.1703 0.0294  -0.0054 -0.0057 231 CYS C O   
6265  C  CB  A CYS C  231 ? 0.4291 0.4691 0.2021 -0.0773 -0.0077 -0.1512 231 CYS C CB  
6266  C  CB  B CYS C  231 ? 0.4428 0.2275 0.2815 0.1071  0.0516  -0.1110 231 CYS C CB  
6267  S  SG  A CYS C  231 ? 0.5368 0.4528 0.1960 -0.1495 0.0307  -0.1106 231 CYS C SG  
6268  S  SG  B CYS C  231 ? 0.3666 0.5375 0.3386 -0.0956 -0.1026 0.0379  231 CYS C SG  
6269  N  N   . THR C  232 ? 0.4092 0.5120 0.1940 -0.1833 0.0013  -0.1292 232 THR C N   
6270  C  CA  . THR C  232 ? 0.6514 0.4479 0.1838 -0.2445 0.0381  -0.0164 232 THR C CA  
6271  C  C   . THR C  232 ? 0.5310 0.5063 0.2867 -0.2351 0.1259  -0.1152 232 THR C C   
6272  O  O   . THR C  232 ? 0.5012 0.6177 0.1158 -0.3240 0.0559  -0.1048 232 THR C O   
6273  C  CB  . THR C  232 ? 0.6495 0.6241 0.2569 -0.3817 0.1191  -0.0298 232 THR C CB  
6274  O  OG1 . THR C  232 ? 0.5782 0.6108 0.2439 -0.3221 0.1325  -0.1676 232 THR C OG1 
6275  C  CG2 . THR C  232 ? 0.5855 0.6991 0.2527 -0.1914 0.0577  -0.2312 232 THR C CG2 
6276  N  N   . HIS C  233 ? 0.6603 0.7364 0.3307 -0.4250 0.1876  -0.2404 233 HIS C N   
6277  C  CA  . HIS C  233 ? 0.4959 0.9685 0.5852 -0.3758 0.1307  -0.1997 233 HIS C CA  
6278  C  C   . HIS C  233 ? 1.4219 1.0647 0.5680 0.0282  0.0949  -0.3441 233 HIS C C   
6279  O  O   . HIS C  233 ? 1.5556 1.5575 0.2032 -0.5425 -0.1440 -0.2703 233 HIS C O   
6280  C  CB  . HIS C  233 ? 0.9527 0.9451 0.2522 -0.1978 0.0038  -0.1730 233 HIS C CB  
6281  C  CG  . HIS C  233 ? 0.9419 0.7828 0.6473 -0.4357 0.3542  -0.2964 233 HIS C CG  
6282  N  ND1 . HIS C  233 ? 0.9493 1.1342 1.1535 -0.1595 0.3152  -0.2709 233 HIS C ND1 
6283  C  CD2 . HIS C  233 ? 0.7113 0.7986 0.9300 -0.2226 0.0153  -0.4194 233 HIS C CD2 
6284  C  CE1 . HIS C  233 ? 0.9479 0.5726 1.0822 -0.1800 0.3380  -0.3185 233 HIS C CE1 
6285  N  NE2 . HIS C  233 ? 1.2273 0.7516 0.9789 -0.0807 0.2924  -0.4645 233 HIS C NE2 
6286  N  N   . MET C  234 ? 1.1449 1.2676 0.1216 -0.3388 0.3091  -0.2056 234 MET C N   
6287  C  CA  . MET C  234 ? 0.7408 1.2257 0.1463 -0.2034 -0.1380 -0.2552 234 MET C CA  
6288  C  C   . MET C  234 ? 0.7161 1.8911 0.2361 -0.2179 0.1661  -0.1580 234 MET C C   
6289  O  O   . MET C  234 ? 0.9201 2.2783 0.3601 -0.3648 0.1518  -0.1544 234 MET C O   
6290  C  CB  . MET C  234 ? 1.1813 1.6167 0.3989 0.0595  -0.0315 0.1030  234 MET C CB  
6291  C  CG  . MET C  234 ? 1.0465 1.7187 0.3413 -0.1597 0.0895  0.1441  234 MET C CG  
6292  S  SD  . MET C  234 ? 0.9072 2.9412 0.6917 -0.1917 -0.0672 -0.0626 234 MET C SD  
6293  C  CE  . MET C  234 ? 0.5939 2.6017 0.5928 0.1106  0.1798  0.1729  234 MET C CE  
6294  N  N   . ASP C  235 ? 1.7546 2.1771 0.7539 0.6797  -0.7217 -1.1810 235 ASP C N   
6295  C  CA  . ASP C  235 ? 0.6802 0.9750 0.7702 -0.0509 -0.2666 -0.2164 235 ASP C CA  
6296  C  C   . ASP C  235 ? 0.7031 0.9345 0.6866 -0.0606 -0.2540 -0.3235 235 ASP C C   
6297  O  O   . ASP C  235 ? 0.9634 0.6406 0.4221 -0.2669 -0.1189 -0.1803 235 ASP C O   
6298  N  N   . ASP C  236 ? 0.6893 0.6800 0.5386 -0.2806 0.0399  -0.3734 236 ASP C N   
6299  C  CA  . ASP C  236 ? 0.6086 0.8230 0.4781 -0.3127 0.0340  -0.3905 236 ASP C CA  
6300  C  C   . ASP C  236 ? 0.7752 0.6682 0.5498 -0.1930 0.0392  -0.1125 236 ASP C C   
6301  O  O   . ASP C  236 ? 0.8152 0.6301 0.2522 -0.1199 0.0269  -0.1225 236 ASP C O   
6302  C  CB  . ASP C  236 ? 0.5676 0.6610 0.3122 -0.2457 0.1333  -0.2495 236 ASP C CB  
6303  C  CG  . ASP C  236 ? 0.6225 0.6147 0.7703 -0.0226 0.2971  -0.3339 236 ASP C CG  
6304  O  OD1 . ASP C  236 ? 0.5382 0.9650 0.6184 0.1456  0.1237  -0.2648 236 ASP C OD1 
6305  O  OD2 . ASP C  236 ? 0.9297 0.6525 0.6766 -0.2125 0.3325  -0.2268 236 ASP C OD2 
6306  N  N   . PRO C  237 ? 0.7702 0.7171 0.4727 -0.2216 0.0425  -0.2673 237 PRO C N   
6307  C  CA  . PRO C  237 ? 0.7559 0.7936 0.4699 -0.1803 0.0509  -0.3375 237 PRO C CA  
6308  C  C   . PRO C  237 ? 0.7281 0.5835 0.2921 -0.1611 0.0467  -0.1008 237 PRO C C   
6309  O  O   . PRO C  237 ? 0.8317 0.7161 0.3673 -0.2181 0.1351  -0.0712 237 PRO C O   
6310  C  CB  . PRO C  237 ? 0.5633 0.7274 0.6032 -0.2788 0.0071  -0.3779 237 PRO C CB  
6311  C  CG  . PRO C  237 ? 0.8206 0.5260 0.6811 -0.1278 0.1186  -0.3785 237 PRO C CG  
6312  C  CD  . PRO C  237 ? 0.7232 0.6161 0.5580 -0.2082 0.1186  -0.2680 237 PRO C CD  
6313  N  N   . SER C  238 ? 0.7329 0.7062 0.2782 -0.2673 0.0860  -0.2296 238 SER C N   
6314  C  CA  . SER C  238 ? 0.6273 0.6560 0.4399 -0.0500 -0.1484 -0.1763 238 SER C CA  
6315  C  C   . SER C  238 ? 0.7081 0.7073 0.4938 -0.1233 -0.0318 -0.1702 238 SER C C   
6316  O  O   . SER C  238 ? 0.7724 0.5329 0.4583 -0.0912 -0.0315 -0.2161 238 SER C O   
6317  C  CB  . SER C  238 ? 0.9190 0.9052 0.4864 0.0640  -0.2703 -0.1102 238 SER C CB  
6318  O  OG  . SER C  238 ? 1.1497 0.9193 0.7674 0.4699  -0.1237 0.1931  238 SER C OG  
6319  N  N   . PRO C  239 ? 0.5313 0.5404 0.2768 -0.2036 0.0564  -0.1641 239 PRO C N   
6320  C  CA  . PRO C  239 ? 0.6000 0.5853 0.2260 -0.0974 -0.0401 -0.1480 239 PRO C CA  
6321  C  C   . PRO C  239 ? 0.3671 0.3810 0.2657 -0.0834 0.0474  -0.0566 239 PRO C C   
6322  O  O   . PRO C  239 ? 0.4615 0.5853 0.3630 -0.2424 0.1116  -0.1835 239 PRO C O   
6323  C  CB  . PRO C  239 ? 0.4572 0.6818 0.1739 -0.0678 0.0790  -0.0644 239 PRO C CB  
6324  C  CG  . PRO C  239 ? 0.5501 0.7754 0.3181 0.0295  0.2380  0.1414  239 PRO C CG  
6325  C  CD  . PRO C  239 ? 0.5770 0.6977 0.2569 -0.0939 0.0731  -0.1794 239 PRO C CD  
6326  N  N   . ARG C  240 ? 0.5327 0.3689 0.2287 -0.1378 0.0662  -0.0714 240 ARG C N   
6327  C  CA  . ARG C  240 ? 0.6694 0.5134 0.2748 -0.2125 -0.0310 -0.0904 240 ARG C CA  
6328  C  C   . ARG C  240 ? 0.4594 0.5821 0.2858 -0.2477 -0.0857 0.0195  240 ARG C C   
6329  O  O   . ARG C  240 ? 0.4505 0.4753 0.2145 -0.2045 0.0038  -0.0573 240 ARG C O   
6330  C  CB  . ARG C  240 ? 0.7906 0.3684 0.4361 -0.1500 -0.1779 -0.0785 240 ARG C CB  
6331  N  N   . GLU C  241 ? 0.4190 0.5088 0.1984 -0.1924 0.0771  -0.0113 241 GLU C N   
6332  C  CA  . GLU C  241 ? 0.4505 0.5101 0.1985 -0.1651 0.1055  -0.1500 241 GLU C CA  
6333  C  C   . GLU C  241 ? 0.3431 0.4598 0.1545 -0.1895 -0.0183 -0.0403 241 GLU C C   
6334  O  O   . GLU C  241 ? 0.3352 0.4614 0.2251 -0.0417 -0.0300 -0.1158 241 GLU C O   
6335  C  CB  . GLU C  241 ? 0.4356 0.3537 0.2407 -0.0094 0.1212  -0.0535 241 GLU C CB  
6336  C  CG  . GLU C  241 ? 0.4875 0.4357 0.3278 -0.0584 0.1704  0.0714  241 GLU C CG  
6337  C  CD  . GLU C  241 ? 0.7215 0.6406 0.3693 -0.3077 0.2912  -0.2373 241 GLU C CD  
6338  O  OE1 . GLU C  241 ? 0.7052 0.9839 0.3061 -0.1420 0.2100  0.0954  241 GLU C OE1 
6339  O  OE2 . GLU C  241 ? 0.7669 1.0153 0.6687 -0.0199 0.3048  0.2055  241 GLU C OE2 
6340  N  N   . MET C  242 ? 0.3438 0.4923 0.1290 -0.1715 -0.0102 -0.0926 242 MET C N   
6341  C  CA  . MET C  242 ? 0.3538 0.4435 0.1254 -0.1915 -0.0059 -0.0601 242 MET C CA  
6342  C  C   . MET C  242 ? 0.2915 0.3964 0.0803 -0.1318 0.0116  -0.0472 242 MET C C   
6343  O  O   . MET C  242 ? 0.3359 0.4487 0.1006 -0.1178 -0.0305 0.0037  242 MET C O   
6344  C  CB  . MET C  242 ? 0.3470 0.4860 0.1123 -0.1296 -0.0164 -0.0432 242 MET C CB  
6345  C  CG  . MET C  242 ? 0.3330 0.4561 0.1111 -0.1386 -0.0094 -0.0031 242 MET C CG  
6346  S  SD  . MET C  242 ? 0.3926 0.4665 0.1089 -0.1606 -0.0107 -0.0285 242 MET C SD  
6347  C  CE  . MET C  242 ? 0.3555 0.4551 0.1923 -0.2404 -0.0156 0.0013  242 MET C CE  
6348  N  N   . ILE C  243 ? 0.2888 0.3903 0.0689 -0.0916 0.0206  -0.0313 243 ILE C N   
6349  C  CA  . ILE C  243 ? 0.2463 0.3788 0.0733 -0.1028 0.0074  -0.0324 243 ILE C CA  
6350  C  C   . ILE C  243 ? 0.2314 0.3185 0.0917 -0.0775 0.0218  0.0157  243 ILE C C   
6351  O  O   . ILE C  243 ? 0.2560 0.3158 0.0797 -0.0652 0.0231  -0.0276 243 ILE C O   
6352  C  CB  . ILE C  243 ? 0.2980 0.3797 0.1138 -0.0636 0.0313  0.0228  243 ILE C CB  
6353  C  CG1 . ILE C  243 ? 0.2869 0.3946 0.1414 -0.0740 0.0340  0.0074  243 ILE C CG1 
6354  C  CG2 . ILE C  243 ? 0.2953 0.4187 0.1048 -0.0675 0.0165  0.0181  243 ILE C CG2 
6355  C  CD1 . ILE C  243 ? 0.3526 0.2660 0.1946 -0.0116 0.1200  0.0060  243 ILE C CD1 
6356  N  N   . ASN C  244 ? 0.2073 0.3188 0.0782 -0.0780 0.0087  -0.0270 244 ASN C N   
6357  C  CA  . ASN C  244 ? 0.2007 0.3118 0.0917 -0.0744 0.0081  0.0170  244 ASN C CA  
6358  C  C   . ASN C  244 ? 0.2072 0.2542 0.0820 -0.0366 0.0344  -0.0229 244 ASN C C   
6359  O  O   . ASN C  244 ? 0.2057 0.2486 0.0983 -0.0474 0.0199  -0.0216 244 ASN C O   
6360  C  CB  . ASN C  244 ? 0.1878 0.2653 0.1231 -0.0513 0.0126  0.0017  244 ASN C CB  
6361  C  CG  . ASN C  244 ? 0.2093 0.2994 0.1000 -0.0311 0.0454  0.0015  244 ASN C CG  
6362  O  OD1 . ASN C  244 ? 0.2736 0.3172 0.1723 -0.0715 0.0656  -0.0005 244 ASN C OD1 
6363  N  ND2 . ASN C  244 ? 0.2716 0.4402 0.1499 -0.0434 0.1022  -0.0049 244 ASN C ND2 
6364  N  N   . ASN C  245 ? 0.2117 0.2617 0.0540 -0.0485 0.0105  -0.0274 245 ASN C N   
6365  C  CA  . ASN C  245 ? 0.1805 0.2675 0.0750 -0.0592 0.0277  -0.0037 245 ASN C CA  
6366  C  C   . ASN C  245 ? 0.1703 0.2413 0.0803 -0.0282 0.0263  0.0065  245 ASN C C   
6367  O  O   . ASN C  245 ? 0.1630 0.2964 0.0944 -0.0478 0.0205  -0.0344 245 ASN C O   
6368  C  CB  . ASN C  245 ? 0.2055 0.3131 0.1146 -0.0736 0.0098  -0.0197 245 ASN C CB  
6369  C  CG  . ASN C  245 ? 0.2470 0.3675 0.0696 -0.0803 0.0041  -0.0335 245 ASN C CG  
6370  O  OD1 . ASN C  245 ? 0.2168 0.2892 0.1127 -0.0511 -0.0217 -0.0143 245 ASN C OD1 
6371  N  ND2 . ASN C  245 ? 0.2628 0.4081 0.1419 -0.1240 -0.0305 -0.0057 245 ASN C ND2 
6372  N  N   . PHE C  246 ? 0.1840 0.2215 0.0593 -0.0375 0.0094  -0.0043 246 PHE C N   
6373  C  CA  . PHE C  246 ? 0.1746 0.1976 0.0762 -0.0157 0.0168  -0.0166 246 PHE C CA  
6374  C  C   . PHE C  246 ? 0.1588 0.1932 0.0728 -0.0361 0.0200  -0.0178 246 PHE C C   
6375  O  O   . PHE C  246 ? 0.1714 0.1980 0.0772 -0.0197 0.0232  -0.0196 246 PHE C O   
6376  C  CB  . PHE C  246 ? 0.1691 0.1912 0.0958 -0.0068 0.0273  0.0065  246 PHE C CB  
6377  C  CG  . PHE C  246 ? 0.1572 0.1849 0.0931 -0.0080 0.0020  0.0007  246 PHE C CG  
6378  C  CD1 . PHE C  246 ? 0.1719 0.2217 0.0890 -0.0164 0.0200  0.0110  246 PHE C CD1 
6379  C  CD2 . PHE C  246 ? 0.1824 0.1735 0.0985 -0.0129 -0.0035 -0.0051 246 PHE C CD2 
6380  C  CE1 . PHE C  246 ? 0.2131 0.2027 0.1146 -0.0522 0.0113  0.0153  246 PHE C CE1 
6381  C  CE2 . PHE C  246 ? 0.1908 0.1662 0.1292 -0.0259 -0.0131 -0.0131 246 PHE C CE2 
6382  C  CZ  . PHE C  246 ? 0.2107 0.2123 0.1384 -0.0214 -0.0160 0.0110  246 PHE C CZ  
6383  N  N   . ARG C  247 ? 0.1468 0.1437 0.0719 -0.0241 0.0074  -0.0003 247 ARG C N   
6384  C  CA  . ARG C  247 ? 0.1256 0.1208 0.0811 -0.0048 0.0043  -0.0071 247 ARG C CA  
6385  C  C   . ARG C  247 ? 0.1623 0.1224 0.0702 -0.0152 0.0166  -0.0141 247 ARG C C   
6386  O  O   . ARG C  247 ? 0.1465 0.1195 0.0879 -0.0027 0.0124  -0.0010 247 ARG C O   
6387  C  CB  . ARG C  247 ? 0.1378 0.1188 0.0760 -0.0278 0.0183  -0.0063 247 ARG C CB  
6388  C  CG  . ARG C  247 ? 0.1585 0.1301 0.0715 -0.0108 0.0163  0.0006  247 ARG C CG  
6389  C  CD  . ARG C  247 ? 0.1826 0.0929 0.0653 -0.0140 0.0309  -0.0098 247 ARG C CD  
6390  N  NE  . ARG C  247 ? 0.1411 0.1005 0.0842 -0.0109 0.0114  -0.0074 247 ARG C NE  
6391  C  CZ  . ARG C  247 ? 0.1401 0.0861 0.0949 -0.0212 0.0176  -0.0174 247 ARG C CZ  
6392  N  NH1 . ARG C  247 ? 0.1497 0.1019 0.1121 -0.0170 0.0266  -0.0253 247 ARG C NH1 
6393  N  NH2 . ARG C  247 ? 0.1529 0.0836 0.1234 -0.0179 0.0037  -0.0083 247 ARG C NH2 
6394  N  N   . GLN C  248 ? 0.1371 0.1231 0.0685 -0.0077 0.0087  -0.0052 248 GLN C N   
6395  C  CA  . GLN C  248 ? 0.1254 0.1208 0.0802 -0.0153 0.0155  -0.0088 248 GLN C CA  
6396  C  C   . GLN C  248 ? 0.1315 0.1085 0.0804 -0.0063 0.0054  -0.0024 248 GLN C C   
6397  O  O   . GLN C  248 ? 0.1439 0.1097 0.0771 -0.0046 0.0164  -0.0034 248 GLN C O   
6398  C  CB  . GLN C  248 ? 0.1437 0.1256 0.0778 -0.0046 0.0177  0.0010  248 GLN C CB  
6399  C  CG  . GLN C  248 ? 0.1488 0.1188 0.0883 0.0065  0.0357  0.0130  248 GLN C CG  
6400  C  CD  . GLN C  248 ? 0.1376 0.1315 0.0870 0.0003  0.0048  -0.0040 248 GLN C CD  
6401  O  OE1 . GLN C  248 ? 0.1886 0.1671 0.1130 -0.0324 -0.0024 0.0286  248 GLN C OE1 
6402  N  NE2 . GLN C  248 ? 0.1806 0.1612 0.1044 -0.0218 0.0098  0.0027  248 GLN C NE2 
6403  N  N   . VAL C  249 ? 0.1247 0.0992 0.0882 0.0010  0.0147  -0.0005 249 VAL C N   
6404  C  CA  . VAL C  249 ? 0.1541 0.0899 0.0748 0.0026  -0.0028 0.0006  249 VAL C CA  
6405  C  C   . VAL C  249 ? 0.1233 0.0852 0.0841 0.0000  0.0023  -0.0068 249 VAL C C   
6406  O  O   . VAL C  249 ? 0.1221 0.0874 0.1012 0.0051  0.0192  -0.0059 249 VAL C O   
6407  C  CB  . VAL C  249 ? 0.1980 0.0727 0.1301 -0.0020 -0.0236 0.0071  249 VAL C CB  
6408  C  CG1 . VAL C  249 ? 0.2353 0.0798 0.1331 0.0298  -0.0185 0.0046  249 VAL C CG1 
6409  C  CG2 . VAL C  249 ? 0.2082 0.1238 0.1674 -0.0038 0.0340  -0.0313 249 VAL C CG2 
6410  N  N   . GLN C  250 ? 0.1328 0.0870 0.0732 -0.0082 0.0122  0.0012  250 GLN C N   
6411  C  CA  . GLN C  250 ? 0.1351 0.0897 0.0815 -0.0007 0.0071  0.0000  250 GLN C CA  
6412  C  C   . GLN C  250 ? 0.1226 0.0927 0.0890 0.0012  0.0151  -0.0109 250 GLN C C   
6413  O  O   . GLN C  250 ? 0.1586 0.0877 0.1193 0.0030  0.0060  -0.0179 250 GLN C O   
6414  C  CB  . GLN C  250 ? 0.1093 0.0974 0.1039 0.0031  0.0149  -0.0051 250 GLN C CB  
6415  C  CG  . GLN C  250 ? 0.1301 0.0836 0.1177 0.0000  -0.0073 -0.0093 250 GLN C CG  
6416  C  CD  . GLN C  250 ? 0.1136 0.0807 0.0944 -0.0085 0.0159  -0.0074 250 GLN C CD  
6417  O  OE1 . GLN C  250 ? 0.1441 0.0833 0.1055 0.0046  0.0270  0.0013  250 GLN C OE1 
6418  N  NE2 . GLN C  250 ? 0.1233 0.1116 0.0776 -0.0241 0.0089  -0.0098 250 GLN C NE2 
6419  N  N   . LYS C  251 ? 0.1075 0.1280 0.0832 -0.0017 0.0074  -0.0107 251 LYS C N   
6420  C  CA  . LYS C  251 ? 0.1163 0.1524 0.0692 -0.0043 0.0142  -0.0105 251 LYS C CA  
6421  C  C   . LYS C  251 ? 0.1015 0.0996 0.1111 -0.0041 0.0104  -0.0035 251 LYS C C   
6422  O  O   . LYS C  251 ? 0.1233 0.1224 0.1127 -0.0006 0.0295  -0.0147 251 LYS C O   
6423  C  CB  . LYS C  251 ? 0.1048 0.2215 0.0897 0.0306  0.0104  -0.0293 251 LYS C CB  
6424  C  CG  . LYS C  251 ? 0.1133 0.1800 0.1073 0.0456  0.0342  -0.0181 251 LYS C CG  
6425  C  CD  . LYS C  251 ? 0.1218 0.2249 0.0777 0.0296  0.0379  0.0078  251 LYS C CD  
6426  C  CE  . LYS C  251 ? 0.1046 0.1680 0.0872 0.0164  0.0204  -0.0098 251 LYS C CE  
6427  N  NZ  . LYS C  251 ? 0.1168 0.1062 0.0878 0.0010  0.0152  -0.0041 251 LYS C NZ  
6428  N  N   . PHE C  252 ? 0.1258 0.1145 0.1010 0.0057  0.0231  -0.0143 252 PHE C N   
6429  C  CA  . PHE C  252 ? 0.1405 0.1462 0.0803 0.0156  0.0397  -0.0153 252 PHE C CA  
6430  C  C   . PHE C  252 ? 0.1596 0.1448 0.1333 0.0093  0.0293  -0.0270 252 PHE C C   
6431  O  O   . PHE C  252 ? 0.2201 0.1721 0.1705 0.0060  0.0098  -0.0478 252 PHE C O   
6432  C  CB  . PHE C  252 ? 0.1558 0.1265 0.1159 0.0266  0.0361  0.0066  252 PHE C CB  
6433  C  CG  . PHE C  252 ? 0.1464 0.1411 0.0865 0.0143  0.0057  -0.0155 252 PHE C CG  
6434  C  CD1 . PHE C  252 ? 0.1511 0.1470 0.0836 0.0136  0.0138  0.0299  252 PHE C CD1 
6435  C  CD2 . PHE C  252 ? 0.1775 0.1402 0.1085 0.0329  0.0114  -0.0005 252 PHE C CD2 
6436  C  CE1 . PHE C  252 ? 0.1624 0.1683 0.1080 0.0408  0.0168  0.0100  252 PHE C CE1 
6437  C  CE2 . PHE C  252 ? 0.1888 0.1574 0.1265 0.0304  0.0384  -0.0259 252 PHE C CE2 
6438  C  CZ  . PHE C  252 ? 0.1759 0.1563 0.1001 0.0425  0.0370  0.0258  252 PHE C CZ  
6439  N  N   . ASP C  253 ? 0.1820 0.2481 0.1102 0.0164  0.0109  -0.0027 253 ASP C N   
6440  C  CA  . ASP C  253 ? 0.1858 0.3140 0.1105 0.0423  -0.0010 0.0007  253 ASP C CA  
6441  C  C   . ASP C  253 ? 0.1563 0.2154 0.1342 0.0176  -0.0006 -0.0108 253 ASP C C   
6442  O  O   . ASP C  253 ? 0.1872 0.1998 0.1674 0.0361  0.0077  -0.0136 253 ASP C O   
6443  C  CB  . ASP C  253 ? 0.2847 0.3779 0.1479 0.1526  -0.0238 -0.0626 253 ASP C CB  
6444  C  CG  . ASP C  253 ? 0.3379 0.5731 0.1106 0.1151  0.0584  -0.0641 253 ASP C CG  
6445  O  OD1 . ASP C  253 ? 0.2231 0.7400 0.4652 0.0306  -0.0297 0.0856  253 ASP C OD1 
6446  O  OD2 . ASP C  253 ? 0.5094 0.4709 0.1728 0.1299  -0.0151 -0.0157 253 ASP C OD2 
6447  N  N   . GLU C  254 ? 0.1579 0.2361 0.1172 0.0186  -0.0173 -0.0148 254 GLU C N   
6448  C  CA  . GLU C  254 ? 0.1621 0.2561 0.1206 0.0299  -0.0093 -0.0254 254 GLU C CA  
6449  C  C   . GLU C  254 ? 0.1723 0.2017 0.1495 0.0324  -0.0156 -0.0043 254 GLU C C   
6450  O  O   . GLU C  254 ? 0.2102 0.2757 0.1656 0.0289  0.0156  0.0412  254 GLU C O   
6451  C  CB  . GLU C  254 ? 0.2165 0.2851 0.1368 0.0320  -0.0146 0.0274  254 GLU C CB  
6452  C  CG  . GLU C  254 ? 0.2477 0.3700 0.2138 0.0348  -0.0285 -0.0051 254 GLU C CG  
6453  C  CD  . GLU C  254 ? 0.4031 0.3481 0.1655 0.0276  0.0436  0.0190  254 GLU C CD  
6454  O  OE1 . GLU C  254 ? 0.4587 0.6976 0.3526 0.0548  0.0142  -0.2290 254 GLU C OE1 
6455  O  OE2 . GLU C  254 ? 0.5705 0.7123 0.2901 -0.3120 0.0947  -0.0681 254 GLU C OE2 
6456  N  N   . ARG C  255 ? 0.1639 0.1547 0.1489 0.0304  -0.0035 -0.0052 255 ARG C N   
6457  C  CA  . ARG C  255 ? 0.1502 0.1551 0.1396 0.0094  -0.0263 -0.0043 255 ARG C CA  
6458  C  C   . ARG C  255 ? 0.1637 0.1624 0.1008 0.0088  -0.0068 -0.0144 255 ARG C C   
6459  O  O   . ARG C  255 ? 0.1547 0.1635 0.1752 0.0082  0.0074  -0.0020 255 ARG C O   
6460  C  CB  . ARG C  255 ? 0.1793 0.1439 0.1156 0.0124  -0.0172 -0.0096 255 ARG C CB  
6461  C  CG  . ARG C  255 ? 0.2158 0.1459 0.1371 -0.0060 -0.0209 -0.0071 255 ARG C CG  
6462  C  CD  . ARG C  255 ? 0.1735 0.1662 0.1441 0.0092  -0.0219 -0.0192 255 ARG C CD  
6463  N  NE  . ARG C  255 ? 0.1723 0.1678 0.1592 -0.0044 -0.0282 -0.0027 255 ARG C NE  
6464  C  CZ  . ARG C  255 ? 0.2048 0.1450 0.1375 -0.0472 0.0006  -0.0137 255 ARG C CZ  
6465  N  NH1 . ARG C  255 ? 0.2147 0.1295 0.1287 -0.0258 -0.0065 -0.0046 255 ARG C NH1 
6466  N  NH2 . ARG C  255 ? 0.1745 0.1854 0.1172 -0.0124 -0.0113 0.0088  255 ARG C NH2 
6467  N  N   . LEU C  256 ? 0.1529 0.1592 0.1475 0.0274  0.0062  -0.0087 256 LEU C N   
6468  C  CA  . LEU C  256 ? 0.1850 0.1481 0.1398 0.0549  -0.0293 -0.0377 256 LEU C CA  
6469  C  C   . LEU C  256 ? 0.1592 0.1421 0.1000 0.0219  0.0086  -0.0355 256 LEU C C   
6470  O  O   . LEU C  256 ? 0.1752 0.1427 0.1412 0.0269  -0.0082 -0.0077 256 LEU C O   
6471  C  CB  . LEU C  256 ? 0.2406 0.1951 0.1036 0.0456  -0.0285 -0.0386 256 LEU C CB  
6472  C  CG  . LEU C  256 ? 0.2640 0.2034 0.1436 0.0419  -0.0392 -0.0463 256 LEU C CG  
6473  C  CD1 . LEU C  256 ? 0.3273 0.3440 0.1185 0.1196  -0.0388 -0.1063 256 LEU C CD1 
6474  C  CD2 . LEU C  256 ? 0.3362 0.2395 0.2199 -0.0395 -0.0621 0.0089  256 LEU C CD2 
6475  N  N   . VAL C  257 ? 0.1653 0.1541 0.1147 0.0502  -0.0024 -0.0174 257 VAL C N   
6476  C  CA  . VAL C  257 ? 0.1588 0.1360 0.1054 0.0340  0.0063  -0.0281 257 VAL C CA  
6477  C  C   . VAL C  257 ? 0.1181 0.1274 0.1383 0.0131  -0.0024 -0.0315 257 VAL C C   
6478  O  O   . VAL C  257 ? 0.1484 0.1353 0.1633 0.0057  0.0003  -0.0498 257 VAL C O   
6479  C  CB  . VAL C  257 ? 0.1795 0.1540 0.1049 0.0478  0.0097  0.0046  257 VAL C CB  
6480  C  CG1 . VAL C  257 ? 0.1793 0.1856 0.1193 0.0494  -0.0003 -0.0041 257 VAL C CG1 
6481  C  CG2 . VAL C  257 ? 0.1933 0.1746 0.1346 0.0595  0.0283  -0.0375 257 VAL C CG2 
6482  N  N   . TYR C  258 ? 0.1333 0.1200 0.1159 0.0108  0.0063  -0.0215 258 TYR C N   
6483  C  CA  . TYR C  258 ? 0.1592 0.1005 0.1243 0.0161  0.0006  -0.0248 258 TYR C CA  
6484  C  C   . TYR C  258 ? 0.1527 0.1224 0.1290 0.0137  0.0035  -0.0166 258 TYR C C   
6485  O  O   . TYR C  258 ? 0.2059 0.1341 0.1445 0.0255  -0.0328 -0.0368 258 TYR C O   
6486  C  CB  . TYR C  258 ? 0.1508 0.1371 0.1435 0.0272  0.0141  -0.0104 258 TYR C CB  
6487  C  CG  . TYR C  258 ? 0.1613 0.1484 0.1184 0.0299  0.0170  -0.0071 258 TYR C CG  
6488  C  CD1 . TYR C  258 ? 0.2212 0.1649 0.1093 0.0196  0.0087  -0.0148 258 TYR C CD1 
6489  C  CD2 . TYR C  258 ? 0.2010 0.1143 0.1599 -0.0031 0.0118  0.0108  258 TYR C CD2 
6490  C  CE1 . TYR C  258 ? 0.3019 0.2077 0.1551 0.0329  0.0097  0.0498  258 TYR C CE1 
6491  C  CE2 . TYR C  258 ? 0.2511 0.1655 0.1398 0.0052  0.0098  0.0351  258 TYR C CE2 
6492  C  CZ  . TYR C  258 ? 0.2608 0.1899 0.1405 0.0450  0.0088  0.0199  258 TYR C CZ  
6493  O  OH  . TYR C  258 ? 0.3440 0.2492 0.1827 0.0650  -0.0230 0.0625  258 TYR C OH  
6494  N  N   . THR C  259 ? 0.1693 0.0991 0.1357 0.0359  0.0028  -0.0111 259 THR C N   
6495  C  CA  . THR C  259 ? 0.1541 0.1265 0.1152 0.0203  0.0254  -0.0240 259 THR C CA  
6496  C  C   . THR C  259 ? 0.1544 0.1522 0.1376 0.0313  0.0233  -0.0026 259 THR C C   
6497  O  O   . THR C  259 ? 0.1933 0.1294 0.1412 0.0355  0.0318  -0.0003 259 THR C O   
6498  C  CB  . THR C  259 ? 0.1574 0.1418 0.1534 0.0161  0.0403  -0.0291 259 THR C CB  
6499  O  OG1 . THR C  259 ? 0.1833 0.1703 0.1657 -0.0261 0.0302  -0.0362 259 THR C OG1 
6500  C  CG2 . THR C  259 ? 0.1595 0.1577 0.1556 0.0200  0.0256  -0.0110 259 THR C CG2 
6501  N  N   . SER C  260 ? 0.1893 0.1337 0.1353 0.0392  0.0286  0.0171  260 SER C N   
6502  C  CA  . SER C  260 ? 0.1877 0.1786 0.1513 0.0562  0.0500  0.0130  260 SER C CA  
6503  C  C   . SER C  260 ? 0.2070 0.1825 0.1759 0.0930  0.0351  0.0006  260 SER C C   
6504  O  O   . SER C  260 ? 0.2357 0.1926 0.2524 0.0957  0.0487  -0.0285 260 SER C O   
6505  C  CB  . SER C  260 ? 0.1635 0.1902 0.1640 0.0520  0.0383  0.0452  260 SER C CB  
6506  O  OG  . SER C  260 ? 0.1795 0.1687 0.1515 0.0419  0.0342  0.0120  260 SER C OG  
6507  N  N   . PHE C  261 ? 0.2193 0.1290 0.2100 0.0447  0.0515  0.0089  261 PHE C N   
6508  C  CA  . PHE C  261 ? 0.2398 0.1283 0.2481 0.0197  0.0379  0.0227  261 PHE C CA  
6509  C  C   . PHE C  261 ? 0.3050 0.1224 0.2892 -0.0104 0.0252  -0.0244 261 PHE C C   
6510  O  O   . PHE C  261 ? 0.2836 0.1942 0.1883 0.0085  0.0375  -0.0339 261 PHE C O   
6511  C  CB  . PHE C  261 ? 0.2802 0.1259 0.2565 0.0441  0.0491  0.0249  261 PHE C CB  
6512  C  CG  . PHE C  261 ? 0.2779 0.1386 0.1502 -0.0055 0.0377  0.0017  261 PHE C CG  
6513  C  CD1 . PHE C  261 ? 0.2948 0.1335 0.1238 0.0175  0.0456  0.0137  261 PHE C CD1 
6514  C  CD2 . PHE C  261 ? 0.2624 0.1382 0.2240 -0.0263 0.0542  -0.0176 261 PHE C CD2 
6515  C  CE1 . PHE C  261 ? 0.2666 0.1479 0.1693 0.0185  0.0368  -0.0098 261 PHE C CE1 
6516  C  CE2 . PHE C  261 ? 0.2576 0.2427 0.2953 -0.0403 0.0808  -0.0662 261 PHE C CE2 
6517  C  CZ  . PHE C  261 ? 0.3019 0.2082 0.1721 -0.0097 0.0610  -0.0275 261 PHE C CZ  
6518  N  N   . SER C  262 ? 0.5684 0.1649 0.1721 -0.0361 -0.0480 -0.0304 262 SER C N   
6519  C  CA  . SER C  262 ? 0.8851 0.1825 0.2488 -0.2391 -0.2408 0.0846  262 SER C CA  
6520  C  C   . SER C  262 ? 1.0836 0.3765 0.6017 -0.1142 -0.1512 0.2612  262 SER C C   
6521  O  O   . SER C  262 ? 1.3566 0.4217 1.8249 0.0364  -0.0368 -0.6076 262 SER C O   
6522  C  CB  . SER C  262 ? 0.7451 0.5489 0.4595 -0.2004 -0.0970 -0.1321 262 SER C CB  
6523  O  OG  . SER C  262 ? 0.4199 0.6406 0.3851 0.0091  0.0171  -0.2477 262 SER C OG  
6524  N  N   . GLN C  263 ? 0.7494 0.1935 0.2854 -0.0820 -0.1045 0.0251  263 GLN C N   
6525  C  CA  . GLN C  263 ? 0.5971 0.1641 0.8120 -0.0847 0.0076  -0.0653 263 GLN C CA  
6526  C  C   . GLN C  263 ? 1.1649 0.6043 0.9512 -0.0895 -0.0936 -0.2222 263 GLN C C   
6527  O  O   . GLN C  263 ? 1.1346 0.4569 0.2782 -0.1106 0.0785  -0.2192 263 GLN C O   
6528  C  CB  . GLN C  263 ? 0.4390 0.1420 0.5884 -0.0675 0.0866  0.0610  263 GLN C CB  
6529  C  CG  . GLN C  263 ? 0.3959 0.3384 0.4467 0.0074  0.0979  -0.0762 263 GLN C CG  
6530  C  CD  . GLN C  263 ? 0.2242 0.3226 0.2570 -0.0926 0.0727  -0.0293 263 GLN C CD  
6531  O  OE1 . GLN C  263 ? 0.3249 0.2563 0.5109 -0.0966 -0.0952 0.0476  263 GLN C OE1 
6532  N  NE2 . GLN C  263 ? 0.3810 0.1515 0.1983 -0.0903 0.0254  -0.0062 263 GLN C NE2 
6533  N  N   . LYS D  3   ? 0.7049 0.3021 0.7131 0.2287  -0.0103 0.0557  3   LYS D N   
6534  C  CA  . LYS D  3   ? 0.7498 0.1838 0.3874 0.0253  0.0317  0.1440  3   LYS D CA  
6535  C  C   . LYS D  3   ? 0.5236 0.1879 0.1799 0.0219  0.0614  0.0164  3   LYS D C   
6536  O  O   . LYS D  3   ? 0.4869 0.1958 0.2066 -0.0355 0.1037  0.0527  3   LYS D O   
6537  C  CB  . LYS D  3   ? 0.8414 0.1775 0.6351 0.0653  0.2149  0.1381  3   LYS D CB  
6538  C  CG  . LYS D  3   ? 0.9737 0.7088 0.6626 -0.2301 0.3580  0.0098  3   LYS D CG  
6539  C  CD  . LYS D  3   ? 1.4201 0.7386 2.3436 0.1928  1.0539  1.0486  3   LYS D CD  
6540  C  CE  . LYS D  3   ? 1.2993 0.4370 4.3169 0.1286  0.4133  0.3851  3   LYS D CE  
6541  N  NZ  . LYS D  3   ? 5.5015 0.5647 4.6090 -1.4220 -0.6768 0.8181  3   LYS D NZ  
6542  N  N   . TRP D  4   ? 0.3129 0.1220 0.1667 -0.0007 0.0320  0.0096  4   TRP D N   
6543  C  CA  . TRP D  4   ? 0.2247 0.1134 0.1340 -0.0121 0.0254  0.0063  4   TRP D CA  
6544  C  C   . TRP D  4   ? 0.2145 0.1109 0.1048 -0.0096 0.0240  0.0074  4   TRP D C   
6545  O  O   . TRP D  4   ? 0.2075 0.1581 0.1237 -0.0010 0.0097  0.0157  4   TRP D O   
6546  C  CB  . TRP D  4   ? 0.2157 0.1353 0.1197 -0.0082 0.0306  -0.0250 4   TRP D CB  
6547  C  CG  . TRP D  4   ? 0.1759 0.0976 0.1158 0.0066  0.0188  -0.0132 4   TRP D CG  
6548  C  CD1 . TRP D  4   ? 0.2238 0.1263 0.1237 0.0331  0.0249  0.0057  4   TRP D CD1 
6549  C  CD2 . TRP D  4   ? 0.1847 0.1028 0.0991 0.0003  0.0057  -0.0093 4   TRP D CD2 
6550  N  NE1 . TRP D  4   ? 0.2064 0.1549 0.1185 0.0516  0.0265  0.0092  4   TRP D NE1 
6551  C  CE2 . TRP D  4   ? 0.1844 0.1362 0.0912 0.0219  0.0035  -0.0034 4   TRP D CE2 
6552  C  CE3 . TRP D  4   ? 0.2010 0.0881 0.1188 -0.0023 0.0035  -0.0318 4   TRP D CE3 
6553  C  CZ2 . TRP D  4   ? 0.2045 0.2025 0.1040 0.0074  -0.0130 -0.0081 4   TRP D CZ2 
6554  C  CZ3 . TRP D  4   ? 0.1981 0.1378 0.1378 -0.0203 -0.0208 -0.0281 4   TRP D CZ3 
6555  C  CH2 . TRP D  4   ? 0.1946 0.1766 0.0958 -0.0132 -0.0125 -0.0017 4   TRP D CH2 
6556  N  N   . THR D  5   ? 0.2052 0.1003 0.1182 -0.0165 0.0304  0.0094  5   THR D N   
6557  C  CA  . THR D  5   ? 0.2029 0.1028 0.1179 -0.0355 0.0186  -0.0120 5   THR D CA  
6558  C  C   . THR D  5   ? 0.1669 0.1382 0.0901 -0.0211 0.0186  -0.0089 5   THR D C   
6559  O  O   . THR D  5   ? 0.1653 0.1076 0.1073 -0.0288 0.0288  -0.0103 5   THR D O   
6560  C  CB  . THR D  5   ? 0.2082 0.1233 0.1256 -0.0353 0.0266  0.0013  5   THR D CB  
6561  O  OG1 . THR D  5   ? 0.2019 0.1522 0.1563 -0.0237 0.0590  0.0212  5   THR D OG1 
6562  C  CG2 . THR D  5   ? 0.3140 0.1044 0.1230 -0.0258 0.0542  0.0130  5   THR D CG2 
6563  N  N   . TYR D  6   ? 0.1842 0.1221 0.1048 -0.0505 0.0211  -0.0028 6   TYR D N   
6564  C  CA  . TYR D  6   ? 0.1574 0.1142 0.1294 -0.0399 0.0465  -0.0003 6   TYR D CA  
6565  C  C   . TYR D  6   ? 0.1728 0.1177 0.1267 -0.0383 0.0397  -0.0027 6   TYR D C   
6566  O  O   . TYR D  6   ? 0.1816 0.1448 0.1260 -0.0342 0.0159  -0.0121 6   TYR D O   
6567  C  CB  . TYR D  6   ? 0.1642 0.1297 0.1204 -0.0456 0.0640  -0.0152 6   TYR D CB  
6568  C  CG  . TYR D  6   ? 0.1553 0.1018 0.0991 -0.0342 0.0388  -0.0059 6   TYR D CG  
6569  C  CD1 . TYR D  6   ? 0.1507 0.0834 0.1120 -0.0287 0.0383  -0.0109 6   TYR D CD1 
6570  C  CD2 . TYR D  6   ? 0.1763 0.0833 0.1042 -0.0308 0.0346  -0.0065 6   TYR D CD2 
6571  C  CE1 . TYR D  6   ? 0.1556 0.0692 0.0935 -0.0113 0.0405  -0.0116 6   TYR D CE1 
6572  C  CE2 . TYR D  6   ? 0.1890 0.0678 0.0989 -0.0043 0.0507  -0.0027 6   TYR D CE2 
6573  C  CZ  . TYR D  6   ? 0.1468 0.0706 0.1037 -0.0041 0.0401  -0.0020 6   TYR D CZ  
6574  O  OH  . TYR D  6   ? 0.1638 0.1279 0.0974 0.0233  0.0515  -0.0041 6   TYR D OH  
6575  N  N   . PHE D  7   ? 0.1739 0.1457 0.1279 -0.0359 0.0544  0.0052  7   PHE D N   
6576  C  CA  . PHE D  7   ? 0.1811 0.1766 0.1836 -0.0465 0.0676  -0.0377 7   PHE D CA  
6577  C  C   . PHE D  7   ? 0.1842 0.2064 0.2161 -0.0171 0.0522  0.0568  7   PHE D C   
6578  O  O   . PHE D  7   ? 0.1811 0.1793 0.2269 -0.0333 0.0441  0.0337  7   PHE D O   
6579  C  CB  . PHE D  7   ? 0.2921 0.2572 0.1585 -0.0544 0.0987  -0.0649 7   PHE D CB  
6580  C  CG  . PHE D  7   ? 0.3438 0.2073 0.2439 -0.0590 0.1500  -0.0645 7   PHE D CG  
6581  C  CD1 . PHE D  7   ? 0.3316 0.3019 0.3152 0.0507  0.1412  -0.0489 7   PHE D CD1 
6582  C  CD2 . PHE D  7   ? 0.4601 0.3368 0.2745 0.0136  0.2558  0.0137  7   PHE D CD2 
6583  C  CE1 . PHE D  7   ? 0.3481 0.3125 0.3723 -0.0108 0.2054  -0.0535 7   PHE D CE1 
6584  C  CE2 . PHE D  7   ? 0.6205 0.3984 0.4645 0.1367  0.4066  0.1084  7   PHE D CE2 
6585  C  CZ  . PHE D  7   ? 0.6489 0.3970 0.4464 0.1199  0.2752  0.0729  7   PHE D CZ  
6586  N  N   . GLY D  8   ? 0.2036 0.1972 0.1854 -0.0353 0.0494  0.0359  8   GLY D N   
6587  C  CA  . GLY D  8   ? 0.2071 0.2030 0.2023 -0.0766 0.0177  0.0346  8   GLY D CA  
6588  C  C   . GLY D  8   ? 0.1660 0.2303 0.1892 -0.0417 0.0231  0.0379  8   GLY D C   
6589  O  O   . GLY D  8   ? 0.1926 0.2057 0.1861 -0.0438 0.0239  0.0368  8   GLY D O   
6590  N  N   . PRO D  9   ? 0.2465 0.2336 0.1781 -0.1039 0.0046  0.0507  9   PRO D N   
6591  C  CA  . PRO D  9   ? 0.2879 0.2226 0.2328 -0.1023 0.0715  0.0281  9   PRO D CA  
6592  C  C   . PRO D  9   ? 0.2285 0.1671 0.1948 -0.1001 0.0038  0.0182  9   PRO D C   
6593  O  O   . PRO D  9   ? 0.2552 0.2420 0.1978 -0.0904 -0.0082 0.0166  9   PRO D O   
6594  C  CB  . PRO D  9   ? 0.3217 0.2416 0.2409 -0.1583 0.0379  0.0562  9   PRO D CB  
6595  C  CG  . PRO D  9   ? 0.5351 0.2430 0.2552 -0.1204 -0.0182 0.0248  9   PRO D CG  
6596  C  CD  . PRO D  9   ? 0.2746 0.2824 0.1793 -0.0674 0.0863  0.0496  9   PRO D CD  
6597  N  N   . ASP D  10  ? 0.2287 0.1515 0.1874 -0.0631 0.0241  0.0264  10  ASP D N   
6598  C  CA  . ASP D  10  ? 0.2440 0.1071 0.1932 -0.0657 0.0030  0.0256  10  ASP D CA  
6599  C  C   . ASP D  10  ? 0.2014 0.1037 0.1396 -0.0450 -0.0017 0.0310  10  ASP D C   
6600  O  O   . ASP D  10  ? 0.1894 0.1145 0.1520 -0.0264 0.0027  0.0087  10  ASP D O   
6601  C  CB  . ASP D  10  ? 0.3014 0.1387 0.1823 -0.0408 -0.0285 0.0496  10  ASP D CB  
6602  C  CG  . ASP D  10  ? 0.5008 0.1562 0.2248 -0.1023 -0.0392 0.0520  10  ASP D CG  
6603  O  OD1 . ASP D  10  ? 0.3950 0.1526 0.3309 -0.0820 -0.0606 0.0483  10  ASP D OD1 
6604  O  OD2 . ASP D  10  ? 0.5939 0.2328 0.2185 -0.1194 -0.0177 0.0802  10  ASP D OD2 
6605  N  N   . GLY D  11  ? 0.2154 0.1028 0.1348 -0.0461 0.0071  0.0328  11  GLY D N   
6606  C  CA  . GLY D  11  ? 0.1665 0.0894 0.1231 -0.0212 0.0114  0.0227  11  GLY D CA  
6607  C  C   . GLY D  11  ? 0.1450 0.0942 0.1136 -0.0241 0.0247  -0.0010 11  GLY D C   
6608  O  O   . GLY D  11  ? 0.1559 0.0739 0.1299 -0.0196 0.0196  0.0027  11  GLY D O   
6609  N  N   . GLU D  12  ? 0.1374 0.0809 0.1127 -0.0141 0.0225  -0.0003 12  GLU D N   
6610  C  CA  . GLU D  12  ? 0.1326 0.0788 0.1055 -0.0184 0.0214  -0.0048 12  GLU D CA  
6611  C  C   . GLU D  12  ? 0.1172 0.0570 0.1206 -0.0063 0.0215  -0.0132 12  GLU D C   
6612  O  O   . GLU D  12  ? 0.1461 0.0815 0.1129 -0.0068 0.0329  -0.0222 12  GLU D O   
6613  C  CB  . GLU D  12  ? 0.1285 0.0685 0.1269 -0.0125 0.0228  -0.0081 12  GLU D CB  
6614  C  CG  . GLU D  12  ? 0.1249 0.0574 0.1299 0.0008  0.0200  -0.0031 12  GLU D CG  
6615  C  CD  . GLU D  12  ? 0.1208 0.0822 0.1048 0.0041  0.0120  -0.0027 12  GLU D CD  
6616  O  OE1 . GLU D  12  ? 0.1322 0.0746 0.1177 -0.0076 0.0250  0.0000  12  GLU D OE1 
6617  O  OE2 . GLU D  12  ? 0.1834 0.0744 0.1077 -0.0181 0.0105  0.0038  12  GLU D OE2 
6618  N  N   . ASN D  13  ? 0.1238 0.0687 0.1321 -0.0121 0.0221  -0.0031 13  ASN D N   
6619  C  CA  . ASN D  13  ? 0.1111 0.0680 0.1375 -0.0092 0.0165  -0.0068 13  ASN D CA  
6620  C  C   . ASN D  13  ? 0.1386 0.0701 0.1356 -0.0181 0.0265  -0.0201 13  ASN D C   
6621  O  O   . ASN D  13  ? 0.1531 0.0827 0.1597 -0.0204 0.0060  -0.0178 13  ASN D O   
6622  C  CB  . ASN D  13  ? 0.1177 0.0716 0.1565 -0.0109 0.0229  -0.0165 13  ASN D CB  
6623  C  CG  . ASN D  13  ? 0.1366 0.0874 0.1209 -0.0324 0.0131  0.0017  13  ASN D CG  
6624  O  OD1 . ASN D  13  ? 0.1312 0.0739 0.1385 -0.0046 0.0320  0.0041  13  ASN D OD1 
6625  N  ND2 . ASN D  13  ? 0.1149 0.1018 0.1190 -0.0035 0.0149  -0.0148 13  ASN D ND2 
6626  N  N   . SER D  14  ? 0.1299 0.0703 0.1448 -0.0010 0.0251  0.0060  14  SER D N   
6627  C  CA  . SER D  14  ? 0.1436 0.0675 0.1486 -0.0096 0.0320  -0.0071 14  SER D CA  
6628  C  C   . SER D  14  ? 0.1410 0.0538 0.1256 -0.0054 0.0200  -0.0066 14  SER D C   
6629  O  O   . SER D  14  ? 0.1538 0.0608 0.1385 -0.0131 0.0359  -0.0142 14  SER D O   
6630  C  CB  . SER D  14  ? 0.1457 0.1021 0.1452 0.0021  0.0789  0.0100  14  SER D CB  
6631  O  OG  . SER D  14  ? 0.1597 0.0978 0.1975 0.0055  0.0680  0.0187  14  SER D OG  
6632  N  N   . TRP D  15  ? 0.1299 0.0757 0.1138 -0.0127 0.0333  -0.0103 15  TRP D N   
6633  C  CA  . TRP D  15  ? 0.1118 0.0728 0.1168 -0.0185 0.0335  -0.0282 15  TRP D CA  
6634  C  C   . TRP D  15  ? 0.1216 0.0782 0.1001 -0.0217 0.0370  -0.0183 15  TRP D C   
6635  O  O   . TRP D  15  ? 0.1502 0.0762 0.1286 0.0060  0.0436  -0.0179 15  TRP D O   
6636  C  CB  . TRP D  15  ? 0.1371 0.0723 0.1229 -0.0329 0.0331  -0.0141 15  TRP D CB  
6637  C  CG  . TRP D  15  ? 0.1218 0.0654 0.1098 -0.0092 0.0311  -0.0114 15  TRP D CG  
6638  C  CD1 . TRP D  15  ? 0.1341 0.0754 0.1118 -0.0054 0.0159  -0.0038 15  TRP D CD1 
6639  C  CD2 . TRP D  15  ? 0.1272 0.0582 0.1107 -0.0060 0.0263  -0.0142 15  TRP D CD2 
6640  N  NE1 . TRP D  15  ? 0.1317 0.0709 0.1039 -0.0071 0.0248  0.0010  15  TRP D NE1 
6641  C  CE2 . TRP D  15  ? 0.1256 0.0719 0.0997 -0.0030 0.0127  -0.0059 15  TRP D CE2 
6642  C  CE3 . TRP D  15  ? 0.1374 0.0610 0.1176 -0.0062 0.0221  -0.0010 15  TRP D CE3 
6643  C  CZ2 . TRP D  15  ? 0.1339 0.0773 0.1106 -0.0030 0.0193  0.0031  15  TRP D CZ2 
6644  C  CZ3 . TRP D  15  ? 0.1377 0.0766 0.1071 -0.0020 0.0252  0.0000  15  TRP D CZ3 
6645  C  CH2 . TRP D  15  ? 0.1362 0.0793 0.0983 0.0166  0.0088  -0.0001 15  TRP D CH2 
6646  N  N   . SER D  16  ? 0.1387 0.0879 0.1023 -0.0259 0.0223  -0.0157 16  SER D N   
6647  C  CA  . SER D  16  ? 0.1721 0.0750 0.1115 -0.0276 0.0196  -0.0322 16  SER D CA  
6648  C  C   . SER D  16  ? 0.1511 0.0841 0.1147 -0.0222 0.0178  -0.0147 16  SER D C   
6649  O  O   . SER D  16  ? 0.2014 0.0802 0.1326 -0.0223 0.0388  -0.0285 16  SER D O   
6650  C  CB  . SER D  16  ? 0.1791 0.1186 0.1163 -0.0232 0.0054  -0.0215 16  SER D CB  
6651  O  OG  . SER D  16  ? 0.2249 0.1475 0.2150 -0.0192 0.0207  -0.0297 16  SER D OG  
6652  N  N   . LYS D  17  ? 0.1649 0.0800 0.1332 -0.0254 0.0372  -0.0038 17  LYS D N   
6653  C  CA  . LYS D  17  ? 0.1563 0.0757 0.1299 -0.0289 0.0436  -0.0234 17  LYS D CA  
6654  C  C   . LYS D  17  ? 0.1477 0.0863 0.1401 -0.0190 0.0527  -0.0322 17  LYS D C   
6655  O  O   . LYS D  17  ? 0.1680 0.0804 0.2098 -0.0300 0.0637  -0.0364 17  LYS D O   
6656  C  CB  . LYS D  17  ? 0.1549 0.0842 0.1642 -0.0131 0.0700  -0.0210 17  LYS D CB  
6657  C  CG  . LYS D  17  ? 0.1301 0.1053 0.1874 -0.0274 0.0608  -0.0093 17  LYS D CG  
6658  C  CD  . LYS D  17  ? 0.1773 0.0866 0.1844 -0.0077 0.0856  -0.0190 17  LYS D CD  
6659  C  CE  . LYS D  17  ? 0.1666 0.0829 0.2069 -0.0212 0.0750  -0.0114 17  LYS D CE  
6660  N  NZ  . LYS D  17  ? 0.1796 0.1222 0.1915 -0.0289 0.0706  -0.0474 17  LYS D NZ  
6661  N  N   . LYS D  18  ? 0.1563 0.0933 0.1369 -0.0157 0.0405  -0.0103 18  LYS D N   
6662  C  CA  . LYS D  18  ? 0.1571 0.0965 0.1592 0.0041  0.0549  0.0073  18  LYS D CA  
6663  C  C   . LYS D  18  ? 0.2007 0.0553 0.1836 -0.0013 0.0693  -0.0174 18  LYS D C   
6664  O  O   . LYS D  18  ? 0.2055 0.0776 0.2317 0.0093  0.0788  0.0031  18  LYS D O   
6665  C  CB  . LYS D  18  ? 0.1791 0.1586 0.1714 -0.0261 0.0291  0.0276  18  LYS D CB  
6666  C  CG  . LYS D  18  ? 0.2601 0.3010 0.1764 -0.1005 0.0335  0.0509  18  LYS D CG  
6667  C  CD  . LYS D  18  ? 0.2786 0.4809 0.1802 -0.1465 0.0297  0.0762  18  LYS D CD  
6668  C  CE  . LYS D  18  ? 0.4788 0.7825 0.5163 -0.2022 0.0152  0.3846  18  LYS D CE  
6669  N  NZ  . LYS D  18  ? 0.7529 4.2699 2.5506 0.0110  -0.8100 -2.5035 18  LYS D NZ  
6670  N  N   . TYR D  19  ? 0.1644 0.0696 0.1103 -0.0133 0.0392  -0.0109 19  TYR D N   
6671  C  CA  . TYR D  19  ? 0.1756 0.0639 0.1137 -0.0147 0.0447  0.0000  19  TYR D CA  
6672  C  C   . TYR D  19  ? 0.1601 0.0836 0.1121 0.0010  0.0472  -0.0178 19  TYR D C   
6673  O  O   . TYR D  19  ? 0.1729 0.0935 0.1179 0.0027  0.0460  -0.0198 19  TYR D O   
6674  C  CB  . TYR D  19  ? 0.2088 0.0834 0.1244 -0.0031 0.0375  -0.0041 19  TYR D CB  
6675  C  CG  . TYR D  19  ? 0.1752 0.0804 0.1378 0.0043  0.0373  -0.0138 19  TYR D CG  
6676  C  CD1 . TYR D  19  ? 0.1694 0.0969 0.1709 -0.0038 0.0130  -0.0008 19  TYR D CD1 
6677  C  CD2 . TYR D  19  ? 0.1737 0.0821 0.1380 -0.0181 0.0308  -0.0238 19  TYR D CD2 
6678  C  CE1 . TYR D  19  ? 0.2084 0.1419 0.1836 0.0230  0.0063  -0.0066 19  TYR D CE1 
6679  C  CE2 . TYR D  19  ? 0.1940 0.1123 0.1518 -0.0310 0.0124  -0.0115 19  TYR D CE2 
6680  C  CZ  . TYR D  19  ? 0.2160 0.1416 0.1659 -0.0087 -0.0013 0.0320  19  TYR D CZ  
6681  O  OH  . TYR D  19  ? 0.3348 0.1664 0.1660 0.0351  -0.0198 0.0228  19  TYR D OH  
6682  N  N   . PRO D  20  ? 0.1897 0.0820 0.1200 -0.0201 0.0463  -0.0186 20  PRO D N   
6683  C  CA  . PRO D  20  ? 0.2148 0.1019 0.1323 -0.0432 0.0251  -0.0230 20  PRO D CA  
6684  C  C   . PRO D  20  ? 0.1908 0.0786 0.1154 -0.0205 0.0147  -0.0401 20  PRO D C   
6685  O  O   . PRO D  20  ? 0.1937 0.1088 0.1290 -0.0076 0.0197  -0.0289 20  PRO D O   
6686  C  CB  . PRO D  20  ? 0.2689 0.1050 0.1676 -0.0516 0.0105  -0.0423 20  PRO D CB  
6687  C  CG  . PRO D  20  ? 0.3296 0.1991 0.1913 0.0742  -0.0322 -0.0859 20  PRO D CG  
6688  C  CD  . PRO D  20  ? 0.2053 0.0904 0.1367 0.0003  0.0467  -0.0370 20  PRO D CD  
6689  N  N   . SER D  21  ? 0.2007 0.0824 0.1066 -0.0178 0.0436  -0.0368 21  SER D N   
6690  C  CA  . SER D  21  ? 0.1720 0.0945 0.1118 -0.0026 0.0491  -0.0208 21  SER D CA  
6691  C  C   . SER D  21  ? 0.1845 0.0942 0.0857 -0.0104 0.0331  -0.0149 21  SER D C   
6692  O  O   . SER D  21  ? 0.2293 0.0933 0.0948 -0.0120 0.0233  0.0000  21  SER D O   
6693  C  CB  . SER D  21  ? 0.1822 0.1111 0.1182 -0.0074 0.0667  -0.0350 21  SER D CB  
6694  O  OG  . SER D  21  ? 0.2398 0.1387 0.1523 0.0024  0.0674  -0.0544 21  SER D OG  
6695  N  N   . CYS D  22  ? 0.1592 0.1001 0.0951 0.0065  0.0386  -0.0298 22  CYS D N   
6696  C  CA  . CYS D  22  ? 0.1595 0.1035 0.1012 0.0192  0.0353  -0.0258 22  CYS D CA  
6697  C  C   . CYS D  22  ? 0.1750 0.1055 0.1049 -0.0137 0.0353  -0.0289 22  CYS D C   
6698  O  O   . CYS D  22  ? 0.1881 0.1066 0.1536 0.0172  0.0010  -0.0315 22  CYS D O   
6699  C  CB  . CYS D  22  ? 0.1689 0.1105 0.1012 -0.0054 0.0535  -0.0226 22  CYS D CB  
6700  S  SG  . CYS D  22  ? 0.1784 0.0827 0.1009 0.0038  0.0340  -0.0143 22  CYS D SG  
6701  N  N   . GLY D  23  ? 0.1844 0.1220 0.1242 -0.0187 0.0093  -0.0320 23  GLY D N   
6702  C  CA  . GLY D  23  ? 0.2026 0.1299 0.1511 -0.0023 -0.0094 -0.0350 23  GLY D CA  
6703  C  C   . GLY D  23  ? 0.2597 0.1319 0.1592 0.0324  -0.0417 -0.0421 23  GLY D C   
6704  O  O   . GLY D  23  ? 0.2301 0.1904 0.1730 0.0241  -0.0337 -0.0335 23  GLY D O   
6705  N  N   . GLY D  24  ? 0.2515 0.1450 0.1283 0.0076  -0.0037 -0.0364 24  GLY D N   
6706  C  CA  . GLY D  24  ? 0.2996 0.1612 0.1216 -0.0425 0.0173  -0.0077 24  GLY D CA  
6707  C  C   . GLY D  24  ? 0.3388 0.1360 0.1215 -0.0489 -0.0263 -0.0294 24  GLY D C   
6708  O  O   . GLY D  24  ? 0.3864 0.1562 0.1766 -0.0205 -0.0456 -0.0192 24  GLY D O   
6709  N  N   . LEU D  25  ? 0.4681 0.1773 0.1202 -0.1054 -0.0229 0.0077  25  LEU D N   
6710  C  CA  . LEU D  25  ? 0.5640 0.1978 0.1234 -0.1733 -0.0684 0.0175  25  LEU D CA  
6711  C  C   . LEU D  25  ? 0.3907 0.1491 0.0910 -0.0654 -0.0026 -0.0073 25  LEU D C   
6712  O  O   . LEU D  25  ? 0.3571 0.1520 0.0876 -0.0297 0.0250  -0.0054 25  LEU D O   
6713  C  CB  . LEU D  25  ? 0.9046 0.3768 0.1158 -0.3257 -0.0498 0.0059  25  LEU D CB  
6714  C  CG  . LEU D  25  ? 1.2798 0.7694 0.3819 -0.1801 -0.4720 -0.2906 25  LEU D CG  
6715  C  CD1 . LEU D  25  ? 1.7948 0.9768 0.3352 -0.5171 -0.4007 0.0485  25  LEU D CD1 
6716  C  CD2 . LEU D  25  ? 1.3730 1.0327 0.0888 -0.2427 -0.1560 -0.1533 25  LEU D CD2 
6717  N  N   . LEU D  26  ? 0.4381 0.1432 0.1168 -0.0771 -0.0114 0.0085  26  LEU D N   
6718  C  CA  . LEU D  26  ? 0.3799 0.1421 0.0915 -0.0320 0.0168  -0.0126 26  LEU D CA  
6719  C  C   . LEU D  26  ? 0.2680 0.1071 0.0843 0.0099  0.0164  0.0184  26  LEU D C   
6720  O  O   . LEU D  26  ? 0.2323 0.1553 0.1089 0.0326  0.0419  0.0065  26  LEU D O   
6721  C  CB  . LEU D  26  ? 0.4989 0.1859 0.0988 -0.0621 0.1001  -0.0073 26  LEU D CB  
6722  C  CG  . LEU D  26  ? 0.8949 0.3583 0.1330 0.1975  0.1001  -0.0078 26  LEU D CG  
6723  C  CD1 . LEU D  26  ? 0.8741 0.3336 0.1468 -0.0293 0.2479  -0.0189 26  LEU D CD1 
6724  C  CD2 . LEU D  26  ? 0.9911 0.2442 0.0996 0.0175  0.0397  -0.0040 26  LEU D CD2 
6725  N  N   . GLN D  27  ? 0.2090 0.1168 0.1014 -0.0186 0.0113  -0.0070 27  GLN D N   
6726  C  CA  . GLN D  27  ? 0.1626 0.0997 0.0795 -0.0020 0.0186  -0.0046 27  GLN D CA  
6727  C  C   . GLN D  27  ? 0.1342 0.0856 0.1129 0.0048  0.0208  -0.0010 27  GLN D C   
6728  O  O   . GLN D  27  ? 0.1827 0.0988 0.1203 0.0142  0.0043  0.0071  27  GLN D O   
6729  C  CB  . GLN D  27  ? 0.1507 0.1005 0.1353 -0.0127 0.0273  0.0003  27  GLN D CB  
6730  C  CG  . GLN D  27  ? 0.1807 0.1146 0.1272 -0.0124 -0.0040 -0.0122 27  GLN D CG  
6731  C  CD  . GLN D  27  ? 0.1896 0.0687 0.0913 -0.0085 0.0205  -0.0126 27  GLN D CD  
6732  O  OE1 . GLN D  27  ? 0.2012 0.0901 0.0863 -0.0109 0.0151  -0.0155 27  GLN D OE1 
6733  N  NE2 . GLN D  27  ? 0.1811 0.0847 0.1033 -0.0176 0.0258  -0.0207 27  GLN D NE2 
6734  N  N   . SER D  28  ? 0.1642 0.0894 0.0890 0.0063  0.0219  0.0023  28  SER D N   
6735  C  CA  . SER D  28  ? 0.1274 0.0917 0.0967 0.0164  0.0288  -0.0080 28  SER D CA  
6736  C  C   . SER D  28  ? 0.1229 0.0741 0.0915 -0.0082 0.0132  0.0043  28  SER D C   
6737  O  O   . SER D  28  ? 0.1420 0.0807 0.1039 -0.0031 0.0379  0.0035  28  SER D O   
6738  C  CB  . SER D  28  ? 0.1438 0.0827 0.0811 0.0109  0.0383  -0.0012 28  SER D CB  
6739  O  OG  . SER D  28  ? 0.1567 0.1030 0.0798 0.0151  0.0412  0.0040  28  SER D OG  
6740  N  N   . PRO D  29  ? 0.1256 0.0685 0.0703 -0.0010 0.0295  0.0057  29  PRO D N   
6741  C  CA  . PRO D  29  ? 0.1331 0.0654 0.0874 0.0078  0.0188  0.0049  29  PRO D CA  
6742  C  C   . PRO D  29  ? 0.1423 0.0834 0.0635 0.0006  0.0322  -0.0046 29  PRO D C   
6743  O  O   . PRO D  29  ? 0.1349 0.0825 0.0876 0.0080  0.0222  0.0052  29  PRO D O   
6744  C  CB  . PRO D  29  ? 0.1585 0.0773 0.0809 -0.0046 0.0348  0.0098  29  PRO D CB  
6745  C  CG  . PRO D  29  ? 0.1342 0.0706 0.1048 -0.0181 0.0294  0.0006  29  PRO D CG  
6746  C  CD  . PRO D  29  ? 0.1211 0.0904 0.0845 0.0000  0.0390  0.0005  29  PRO D CD  
6747  N  N   . ILE D  30  ? 0.1360 0.0730 0.0904 0.0127  0.0275  0.0082  30  ILE D N   
6748  C  CA  . ILE D  30  ? 0.1536 0.0874 0.0759 0.0136  0.0329  0.0044  30  ILE D CA  
6749  C  C   . ILE D  30  ? 0.1402 0.0872 0.0852 0.0219  0.0359  0.0177  30  ILE D C   
6750  O  O   . ILE D  30  ? 0.1351 0.1005 0.0994 0.0242  0.0340  0.0121  30  ILE D O   
6751  C  CB  . ILE D  30  ? 0.1687 0.1199 0.0845 0.0000  0.0399  0.0057  30  ILE D CB  
6752  C  CG1 . ILE D  30  ? 0.1728 0.1580 0.1017 0.0287  0.0419  0.0399  30  ILE D CG1 
6753  C  CG2 . ILE D  30  ? 0.2876 0.1167 0.1036 -0.0070 0.0271  -0.0111 30  ILE D CG2 
6754  C  CD1 . ILE D  30  ? 0.2205 0.1915 0.0909 0.0210  0.0467  0.0278  30  ILE D CD1 
6755  N  N   . ASP D  31  ? 0.1403 0.0872 0.0815 0.0121  0.0390  0.0253  31  ASP D N   
6756  C  CA  . ASP D  31  ? 0.1402 0.0791 0.1062 0.0152  0.0368  0.0222  31  ASP D CA  
6757  C  C   . ASP D  31  ? 0.1353 0.1039 0.0979 0.0120  0.0241  0.0217  31  ASP D C   
6758  O  O   . ASP D  31  ? 0.2001 0.1703 0.1039 -0.0375 0.0078  0.0264  31  ASP D O   
6759  C  CB  . ASP D  31  ? 0.1509 0.1163 0.1263 0.0388  0.0368  0.0190  31  ASP D CB  
6760  C  CG  . ASP D  31  ? 0.1492 0.1466 0.1109 0.0308  0.0320  0.0127  31  ASP D CG  
6761  O  OD1 . ASP D  31  ? 0.1773 0.1168 0.1411 0.0333  0.0142  -0.0007 31  ASP D OD1 
6762  O  OD2 . ASP D  31  ? 0.2694 0.1611 0.1290 0.0734  0.0133  0.0175  31  ASP D OD2 
6763  N  N   . LEU D  32  ? 0.1360 0.1165 0.1006 -0.0077 0.0359  0.0153  32  LEU D N   
6764  C  CA  . LEU D  32  ? 0.1675 0.1195 0.1152 0.0044  0.0584  0.0350  32  LEU D CA  
6765  C  C   . LEU D  32  ? 0.1969 0.1130 0.1124 0.0157  0.0636  0.0220  32  LEU D C   
6766  O  O   . LEU D  32  ? 0.2138 0.1172 0.1489 0.0337  0.0251  0.0137  32  LEU D O   
6767  C  CB  . LEU D  32  ? 0.1799 0.1213 0.1552 0.0003  0.0612  0.0256  32  LEU D CB  
6768  C  CG  . LEU D  32  ? 0.1746 0.1307 0.1172 0.0060  0.0597  0.0156  32  LEU D CG  
6769  C  CD1 . LEU D  32  ? 0.1735 0.1823 0.1495 0.0038  0.0504  0.0082  32  LEU D CD1 
6770  C  CD2 . LEU D  32  ? 0.2253 0.2290 0.1491 0.0317  0.0606  -0.0086 32  LEU D CD2 
6771  N  N   . HIS D  33  ? 0.1926 0.1353 0.1181 0.0066  0.0474  0.0476  33  HIS D N   
6772  C  CA  . HIS D  33  ? 0.1790 0.1432 0.1188 0.0241  0.0430  0.0357  33  HIS D CA  
6773  C  C   . HIS D  33  ? 0.1586 0.1748 0.1215 0.0311  0.0355  0.0483  33  HIS D C   
6774  O  O   . HIS D  33  ? 0.1883 0.1617 0.1328 0.0305  0.0579  0.0571  33  HIS D O   
6775  C  CB  . HIS D  33  ? 0.1859 0.1878 0.1367 -0.0020 0.0520  0.0439  33  HIS D CB  
6776  C  CG  . HIS D  33  ? 0.1958 0.1893 0.1133 -0.0034 0.0489  0.0392  33  HIS D CG  
6777  N  ND1 . HIS D  33  ? 0.3003 0.1923 0.1841 -0.1045 -0.0401 0.0807  33  HIS D ND1 
6778  C  CD2 . HIS D  33  ? 0.2087 0.2757 0.1263 0.0737  0.0337  0.0533  33  HIS D CD2 
6779  C  CE1 . HIS D  33  ? 0.3143 0.2127 0.1698 -0.0696 -0.0254 0.0689  33  HIS D CE1 
6780  N  NE2 . HIS D  33  ? 0.2104 0.3287 0.1328 -0.0012 0.0333  0.0741  33  HIS D NE2 
6781  N  N   . SER D  34  ? 0.1967 0.1597 0.1434 0.0269  0.0417  0.0680  34  SER D N   
6782  C  CA  . SER D  34  ? 0.2488 0.1660 0.1508 0.0171  0.0419  0.0615  34  SER D CA  
6783  C  C   . SER D  34  ? 0.1806 0.2111 0.1346 0.0394  0.0432  0.0771  34  SER D C   
6784  O  O   . SER D  34  ? 0.1942 0.2215 0.1488 0.0463  0.0608  0.0758  34  SER D O   
6785  C  CB  . SER D  34  ? 0.2542 0.1969 0.2466 0.0324  0.0447  0.1495  34  SER D CB  
6786  O  OG  . SER D  34  ? 0.2662 0.2325 0.3260 0.0668  0.0189  0.0681  34  SER D OG  
6787  N  N   . ASP D  35  ? 0.1903 0.1876 0.1362 0.0161  0.0196  0.0320  35  ASP D N   
6788  C  CA  . ASP D  35  ? 0.1721 0.2716 0.1353 0.0353  0.0322  0.0571  35  ASP D CA  
6789  C  C   . ASP D  35  ? 0.1958 0.2439 0.0949 0.0258  0.0445  0.0483  35  ASP D C   
6790  O  O   . ASP D  35  ? 0.2788 0.3046 0.1097 0.0820  0.0315  0.0461  35  ASP D O   
6791  C  CB  . ASP D  35  ? 0.1756 0.2870 0.1917 0.0458  0.0537  0.0264  35  ASP D CB  
6792  C  CG  . ASP D  35  ? 0.2152 0.2639 0.1771 0.0425  0.0283  0.0233  35  ASP D CG  
6793  O  OD1 . ASP D  35  ? 0.2055 0.2982 0.1941 0.0452  0.0294  0.0148  35  ASP D OD1 
6794  O  OD2 . ASP D  35  ? 0.2039 0.3149 0.1802 0.0553  0.0623  0.0368  35  ASP D OD2 
6795  N  N   . ILE D  36  ? 0.1863 0.2196 0.1176 0.0291  0.0559  0.0548  36  ILE D N   
6796  C  CA  . ILE D  36  ? 0.1865 0.2088 0.1741 0.0307  0.0478  0.0513  36  ILE D CA  
6797  C  C   . ILE D  36  ? 0.1879 0.2019 0.1285 0.0288  0.0281  0.0115  36  ILE D C   
6798  O  O   . ILE D  36  ? 0.2070 0.2143 0.1958 0.0700  0.0650  0.0368  36  ILE D O   
6799  C  CB  . ILE D  36  ? 0.2976 0.2081 0.1658 0.0381  0.0366  0.0339  36  ILE D CB  
6800  C  CG1 . ILE D  36  ? 0.3605 0.2075 0.1502 0.0434  0.0542  0.0529  36  ILE D CG1 
6801  C  CG2 . ILE D  36  ? 0.2964 0.2716 0.3089 -0.0243 0.0118  0.0842  36  ILE D CG2 
6802  C  CD1 . ILE D  36  ? 0.3107 0.2244 0.1920 0.0841  0.0445  0.0239  36  ILE D CD1 
6803  N  N   . LEU D  37  ? 0.1807 0.1975 0.1177 0.0159  0.0573  0.0410  37  LEU D N   
6804  C  CA  . LEU D  37  ? 0.1906 0.1820 0.1159 0.0368  0.0456  0.0292  37  LEU D CA  
6805  C  C   . LEU D  37  ? 0.2026 0.2222 0.1387 0.0662  0.0566  0.0746  37  LEU D C   
6806  O  O   . LEU D  37  ? 0.2206 0.2790 0.1772 0.1011  0.0751  0.1053  37  LEU D O   
6807  C  CB  . LEU D  37  ? 0.1692 0.1696 0.1472 0.0230  0.0377  0.0373  37  LEU D CB  
6808  C  CG  . LEU D  37  ? 0.1917 0.2461 0.1339 0.0308  0.0608  0.0215  37  LEU D CG  
6809  C  CD1 . LEU D  37  ? 0.2454 0.2587 0.2062 0.0535  0.0120  -0.0200 37  LEU D CD1 
6810  C  CD2 . LEU D  37  ? 0.2379 0.2300 0.1277 0.0130  0.0709  0.0658  37  LEU D CD2 
6811  N  N   . GLN D  38  ? 0.1919 0.1753 0.1242 0.0507  0.0740  0.0494  38  GLN D N   
6812  C  CA  . GLN D  38  ? 0.2064 0.2068 0.1316 0.0351  0.0802  0.0667  38  GLN D CA  
6813  C  C   . GLN D  38  ? 0.1955 0.1841 0.1188 0.0768  0.0837  0.0579  38  GLN D C   
6814  O  O   . GLN D  38  ? 0.2168 0.1840 0.1252 0.0610  0.0716  0.0646  38  GLN D O   
6815  C  CB  . GLN D  38  ? 0.2233 0.3413 0.1254 0.0195  0.0443  0.0126  38  GLN D CB  
6816  C  CG  . GLN D  38  ? 0.3725 0.3352 0.1444 -0.0031 0.0538  0.0211  38  GLN D CG  
6817  C  CD  . GLN D  38  ? 0.3174 0.6316 0.2206 0.0538  -0.0251 -0.1023 38  GLN D CD  
6818  O  OE1 . GLN D  38  ? 0.3567 0.6434 0.2431 -0.0225 -0.0035 -0.0258 38  GLN D OE1 
6819  N  NE2 . GLN D  38  ? 0.4709 0.4154 0.2156 0.0439  0.0425  0.0790  38  GLN D NE2 
6820  N  N   . TYR D  39  ? 0.2178 0.1994 0.1384 0.0661  0.0948  0.0684  39  TYR D N   
6821  C  CA  . TYR D  39  ? 0.2109 0.1495 0.1098 0.0577  0.0710  0.0430  39  TYR D CA  
6822  C  C   . TYR D  39  ? 0.2039 0.1536 0.1001 0.0403  0.0507  0.0368  39  TYR D C   
6823  O  O   . TYR D  39  ? 0.2230 0.1899 0.1172 0.0657  0.0742  0.0456  39  TYR D O   
6824  C  CB  . TYR D  39  ? 0.2461 0.1283 0.1947 0.0568  0.0988  0.0522  39  TYR D CB  
6825  C  CG  . TYR D  39  ? 0.2242 0.1174 0.1597 0.0324  0.0710  0.0443  39  TYR D CG  
6826  C  CD1 . TYR D  39  ? 0.2370 0.1944 0.1675 0.0542  0.0549  0.0298  39  TYR D CD1 
6827  C  CD2 . TYR D  39  ? 0.2957 0.1554 0.1910 0.0262  0.1168  0.0636  39  TYR D CD2 
6828  C  CE1 . TYR D  39  ? 0.2522 0.1711 0.1852 0.0430  0.0755  0.0522  39  TYR D CE1 
6829  C  CE2 . TYR D  39  ? 0.2678 0.1843 0.1780 0.0296  0.0936  0.0656  39  TYR D CE2 
6830  C  CZ  . TYR D  39  ? 0.2362 0.1615 0.2039 0.0275  0.0741  0.0599  39  TYR D CZ  
6831  O  OH  . TYR D  39  ? 0.2630 0.2233 0.2752 -0.0115 0.1351  0.0048  39  TYR D OH  
6832  N  N   . ASP D  40  ? 0.1818 0.1492 0.1184 0.0478  0.0834  0.0465  40  ASP D N   
6833  C  CA  . ASP D  40  ? 0.1956 0.1382 0.1639 0.0535  0.0890  0.0284  40  ASP D CA  
6834  C  C   . ASP D  40  ? 0.1734 0.1396 0.1226 0.0461  0.0678  0.0172  40  ASP D C   
6835  O  O   . ASP D  40  ? 0.1890 0.2071 0.1234 0.0685  0.0649  0.0286  40  ASP D O   
6836  C  CB  . ASP D  40  ? 0.2220 0.1540 0.1558 0.0465  0.1019  0.0500  40  ASP D CB  
6837  C  CG  . ASP D  40  ? 0.3323 0.1620 0.2449 0.0759  0.1643  0.0641  40  ASP D CG  
6838  O  OD1 . ASP D  40  ? 0.2070 0.1419 0.1892 0.0342  0.0824  0.0247  40  ASP D OD1 
6839  O  OD2 . ASP D  40  ? 0.4559 0.1689 0.3427 0.0860  0.2293  0.0842  40  ASP D OD2 
6840  N  N   . ALA D  41  ? 0.1915 0.1383 0.1112 0.0379  0.0856  0.0040  41  ALA D N   
6841  C  CA  . ALA D  41  ? 0.2143 0.1714 0.1274 0.0379  0.0952  0.0131  41  ALA D CA  
6842  C  C   . ALA D  41  ? 0.2007 0.1637 0.1513 0.0265  0.1040  -0.0010 41  ALA D C   
6843  O  O   . ALA D  41  ? 0.2037 0.1921 0.1915 0.0302  0.0900  0.0137  41  ALA D O   
6844  C  CB  . ALA D  41  ? 0.2721 0.1499 0.1811 0.0272  0.1108  0.0533  41  ALA D CB  
6845  N  N   . SER D  42  ? 0.1944 0.1580 0.1450 0.0476  0.0838  -0.0030 42  SER D N   
6846  C  CA  . SER D  42  ? 0.2235 0.1726 0.2235 0.0548  0.1185  0.0006  42  SER D CA  
6847  C  C   . SER D  42  ? 0.2558 0.2293 0.2237 0.1055  0.1080  0.0802  42  SER D C   
6848  O  O   . SER D  42  ? 0.2746 0.3264 0.3253 0.1551  0.1451  0.1321  42  SER D O   
6849  C  CB  . SER D  42  ? 0.3538 0.1894 0.3307 0.0230  0.2041  0.0020  42  SER D CB  
6850  O  OG  . SER D  42  ? 0.3366 0.1500 0.4655 0.0533  0.2104  0.0658  42  SER D OG  
6851  N  N   . LEU D  43  ? 0.2258 0.2603 0.1827 0.0992  0.1213  0.0768  43  LEU D N   
6852  C  CA  . LEU D  43  ? 0.2052 0.2897 0.2030 0.0658  0.0956  0.0864  43  LEU D CA  
6853  C  C   . LEU D  43  ? 0.1492 0.3127 0.2127 0.0626  0.0927  0.1212  43  LEU D C   
6854  O  O   . LEU D  43  ? 0.2533 0.2874 0.2768 0.0680  0.1203  0.1533  43  LEU D O   
6855  C  CB  . LEU D  43  ? 0.1806 0.2468 0.1784 0.0644  0.1001  0.0665  43  LEU D CB  
6856  C  CG  . LEU D  43  ? 0.2064 0.2529 0.2504 0.0782  0.1005  0.0866  43  LEU D CG  
6857  C  CD1 . LEU D  43  ? 0.2206 0.2930 0.1815 0.0741  0.0702  0.0724  43  LEU D CD1 
6858  C  CD2 . LEU D  43  ? 0.2388 0.2251 0.3400 0.0568  0.0913  0.1234  43  LEU D CD2 
6859  N  N   . THR D  44  ? 0.1886 0.4000 0.1666 0.1067  0.0988  0.0741  44  THR D N   
6860  C  CA  . THR D  44  ? 0.1568 0.4422 0.2178 0.0910  0.1008  0.1634  44  THR D CA  
6861  C  C   . THR D  44  ? 0.2184 0.3553 0.1421 0.0494  0.1036  -0.0005 44  THR D C   
6862  O  O   . THR D  44  ? 0.1926 0.2754 0.1836 0.0825  0.0876  0.0452  44  THR D O   
6863  C  CB  . THR D  44  ? 0.2393 0.4612 0.2116 0.0337  0.1116  0.0410  44  THR D CB  
6864  O  OG1 . THR D  44  ? 0.2538 0.4528 0.3427 0.0847  0.1020  -0.0806 44  THR D OG1 
6865  C  CG2 . THR D  44  ? 0.2008 0.8748 0.1957 0.0908  0.0834  0.0339  44  THR D CG2 
6866  N  N   . PRO D  45  ? 0.2043 0.2472 0.2127 0.0286  0.0630  0.1142  45  PRO D N   
6867  C  CA  . PRO D  45  ? 0.3021 0.2170 0.2050 0.0842  0.0789  0.0511  45  PRO D CA  
6868  C  C   . PRO D  45  ? 0.1703 0.2195 0.2090 0.0551  0.0892  0.0577  45  PRO D C   
6869  O  O   . PRO D  45  ? 0.1969 0.3418 0.2630 0.0935  0.1076  0.0947  45  PRO D O   
6870  C  CB  . PRO D  45  ? 0.3596 0.1385 0.3528 0.0292  0.1517  0.0890  45  PRO D CB  
6871  C  CG  . PRO D  45  ? 0.2082 0.3145 0.2133 0.0322  0.0395  0.0804  45  PRO D CG  
6872  C  CD  . PRO D  45  ? 0.2285 0.3346 0.2027 -0.0219 0.0800  0.0965  45  PRO D CD  
6873  N  N   . LEU D  46  ? 0.2118 0.2407 0.2187 0.0789  0.0922  0.0942  46  LEU D N   
6874  C  CA  . LEU D  46  ? 0.2125 0.1996 0.1951 0.0644  0.0670  0.0480  46  LEU D CA  
6875  C  C   . LEU D  46  ? 0.2377 0.1780 0.2102 0.0315  0.1062  0.0942  46  LEU D C   
6876  O  O   . LEU D  46  ? 0.1799 0.2035 0.2987 0.0156  0.0754  0.0935  46  LEU D O   
6877  C  CB  . LEU D  46  ? 0.2021 0.1737 0.2741 0.0688  0.1081  0.0856  46  LEU D CB  
6878  C  CG  . LEU D  46  ? 0.2149 0.2312 0.3704 0.1096  0.0922  -0.0052 46  LEU D CG  
6879  C  CD1 . LEU D  46  ? 0.2158 0.2935 0.3993 0.0388  0.0856  0.1647  46  LEU D CD1 
6880  C  CD2 . LEU D  46  ? 0.3562 0.3468 0.4903 0.1942  -0.0746 -0.1666 46  LEU D CD2 
6881  N  N   . GLU D  47  ? 0.1892 0.2114 0.2246 0.0648  0.0896  0.0793  47  GLU D N   
6882  C  CA  . GLU D  47  ? 0.2064 0.3111 0.1902 -0.0229 0.0966  0.0951  47  GLU D CA  
6883  C  C   . GLU D  47  ? 0.2136 0.2008 0.2716 0.0063  0.1527  0.0588  47  GLU D C   
6884  O  O   . GLU D  47  ? 0.2813 0.2084 0.2163 0.0153  0.0846  0.0732  47  GLU D O   
6885  C  CB  . GLU D  47  ? 0.2357 0.5508 0.3305 0.1829  0.1739  0.3129  47  GLU D CB  
6886  C  CG  . GLU D  47  ? 0.3021 0.7185 0.4799 0.1353  0.1930  0.4002  47  GLU D CG  
6887  C  CD  . GLU D  47  ? 0.4675 1.0537 0.4512 0.2511  0.2462  0.4555  47  GLU D CD  
6888  O  OE1 . GLU D  47  ? 0.3749 1.3272 0.7123 0.3158  0.2583  0.1559  47  GLU D OE1 
6889  O  OE2 . GLU D  47  ? 0.4196 1.0542 0.6146 0.2211  0.2231  0.4815  47  GLU D OE2 
6890  N  N   . PHE D  48  ? 0.2298 0.1820 0.2685 0.0710  0.1152  0.1089  48  PHE D N   
6891  C  CA  . PHE D  48  ? 0.2363 0.1884 0.2554 0.0412  0.1067  0.0877  48  PHE D CA  
6892  C  C   . PHE D  48  ? 0.2423 0.1942 0.3752 0.0195  0.1800  0.1260  48  PHE D C   
6893  O  O   . PHE D  48  ? 0.2266 0.2457 0.4597 0.0104  0.0351  0.1632  48  PHE D O   
6894  C  CB  . PHE D  48  ? 0.2436 0.1511 0.2727 0.0153  0.0882  0.0366  48  PHE D CB  
6895  C  CG  . PHE D  48  ? 0.2481 0.1489 0.2256 0.0155  0.0877  0.0615  48  PHE D CG  
6896  C  CD1 . PHE D  48  ? 0.2174 0.1610 0.2152 0.0313  0.1336  0.0239  48  PHE D CD1 
6897  C  CD2 . PHE D  48  ? 0.2538 0.1328 0.3160 0.0619  0.0825  0.0731  48  PHE D CD2 
6898  C  CE1 . PHE D  48  ? 0.2129 0.1732 0.2197 0.0317  0.1177  0.0405  48  PHE D CE1 
6899  C  CE2 . PHE D  48  ? 0.2703 0.1520 0.2705 0.0296  0.0430  0.0476  48  PHE D CE2 
6900  C  CZ  . PHE D  48  ? 0.1962 0.1827 0.2486 0.0423  0.1494  0.0553  48  PHE D CZ  
6901  N  N   . GLN D  49  ? 0.2327 0.1817 0.2926 0.0952  0.1479  0.1270  49  GLN D N   
6902  C  CA  . GLN D  49  ? 0.2287 0.2754 0.3844 0.0847  0.1825  0.1497  49  GLN D CA  
6903  C  C   . GLN D  49  ? 0.1272 0.1965 0.3526 0.0614  0.1244  0.0817  49  GLN D C   
6904  O  O   . GLN D  49  ? 0.1777 0.1583 0.2669 0.0449  0.1129  0.0648  49  GLN D O   
6905  C  CB  . GLN D  49  ? 0.2535 0.3465 0.3711 0.1509  0.2343  0.1624  49  GLN D CB  
6906  C  CG  . GLN D  49  ? 0.4348 0.3873 0.3680 0.1513  0.2084  0.1588  49  GLN D CG  
6907  C  CD  . GLN D  49  ? 0.4262 0.5353 0.4216 0.1435  -0.0842 0.1368  49  GLN D CD  
6908  O  OE1 . GLN D  49  ? 0.3856 0.6565 0.7156 0.1548  0.1870  0.3795  49  GLN D OE1 
6909  N  NE2 . GLN D  49  ? 0.3975 0.6585 0.3063 0.1471  0.0995  0.2246  49  GLN D NE2 
6910  N  N   . GLY D  50  ? 0.1425 0.2050 0.2915 0.0388  0.1485  0.0923  50  GLY D N   
6911  C  CA  . GLY D  50  ? 0.1412 0.2330 0.3379 0.0732  0.1229  0.1008  50  GLY D CA  
6912  C  C   . GLY D  50  ? 0.1115 0.1711 0.2504 0.0215  0.0746  0.0637  50  GLY D C   
6913  O  O   . GLY D  50  ? 0.1259 0.1504 0.2825 0.0342  0.0763  0.0527  50  GLY D O   
6914  N  N   . TYR D  51  ? 0.1251 0.1411 0.2978 0.0357  0.1023  0.0518  51  TYR D N   
6915  C  CA  . TYR D  51  ? 0.0940 0.1195 0.3025 0.0159  0.0702  0.0251  51  TYR D CA  
6916  C  C   . TYR D  51  ? 0.1080 0.1041 0.2996 -0.0197 0.0546  0.0520  51  TYR D C   
6917  O  O   . TYR D  51  ? 0.1130 0.1265 0.2694 0.0103  0.0511  0.0416  51  TYR D O   
6918  C  CB  . TYR D  51  ? 0.1138 0.1324 0.2644 0.0099  0.0680  0.0458  51  TYR D CB  
6919  C  CG  . TYR D  51  ? 0.1149 0.1001 0.1949 -0.0003 0.0551  0.0549  51  TYR D CG  
6920  C  CD1 . TYR D  51  ? 0.1721 0.1017 0.2014 0.0262  0.0841  0.0507  51  TYR D CD1 
6921  C  CD2 . TYR D  51  ? 0.1061 0.1298 0.2142 -0.0055 0.0716  0.0417  51  TYR D CD2 
6922  C  CE1 . TYR D  51  ? 0.1493 0.1374 0.1592 0.0414  0.0671  0.0478  51  TYR D CE1 
6923  C  CE2 . TYR D  51  ? 0.1342 0.1042 0.1996 -0.0024 0.0681  0.0115  51  TYR D CE2 
6924  C  CZ  . TYR D  51  ? 0.1414 0.1058 0.1841 0.0309  0.0593  0.0263  51  TYR D CZ  
6925  O  OH  . TYR D  51  ? 0.1738 0.1310 0.1893 0.0359  0.0487  0.0162  51  TYR D OH  
6926  N  N   . ASN D  52  ? 0.1317 0.1448 0.3391 -0.0041 0.0390  0.0608  52  ASN D N   
6927  C  CA  . ASN D  52  ? 0.0954 0.1628 0.3461 -0.0153 0.0480  0.0790  52  ASN D CA  
6928  C  C   . ASN D  52  ? 0.1211 0.1854 0.3433 0.0135  0.0386  0.0693  52  ASN D C   
6929  O  O   . ASN D  52  ? 0.1204 0.2111 0.3808 0.0111  0.0559  0.1055  52  ASN D O   
6930  C  CB  . ASN D  52  ? 0.1400 0.1829 0.3874 -0.0483 0.0131  0.0718  52  ASN D CB  
6931  C  CG  . ASN D  52  ? 0.1304 0.1958 0.4146 -0.0293 0.0333  0.0582  52  ASN D CG  
6932  O  OD1 . ASN D  52  ? 0.2716 0.3657 0.4702 -0.1640 0.0244  0.0450  52  ASN D OD1 
6933  N  ND2 . ASN D  52  ? 0.2614 0.2509 0.6352 -0.1134 0.0284  0.0777  52  ASN D ND2 
6934  N  N   . LEU D  53  ? 0.1359 0.1138 0.3208 -0.0021 0.0357  0.0377  53  LEU D N   
6935  C  CA  . LEU D  53  ? 0.1225 0.1571 0.2763 0.0159  0.0399  0.0264  53  LEU D CA  
6936  C  C   . LEU D  53  ? 0.1312 0.1404 0.2809 -0.0138 0.0522  0.0258  53  LEU D C   
6937  O  O   . LEU D  53  ? 0.1588 0.1811 0.3474 -0.0012 0.0601  -0.0359 53  LEU D O   
6938  C  CB  . LEU D  53  ? 0.1172 0.1594 0.2664 0.0030  0.0474  0.0244  53  LEU D CB  
6939  C  CG  . LEU D  53  ? 0.1116 0.1615 0.3003 -0.0027 0.0179  0.0653  53  LEU D CG  
6940  C  CD1 . LEU D  53  ? 0.1529 0.2129 0.3506 -0.0399 0.0010  0.0917  53  LEU D CD1 
6941  C  CD2 . LEU D  53  ? 0.1913 0.2096 0.2957 0.0255  0.0287  0.0575  53  LEU D CD2 
6942  N  N   . SER D  54  ? 0.1003 0.1823 0.2888 -0.0077 0.0285  0.0281  54  SER D N   
6943  C  CA  . SER D  54  ? 0.1389 0.1829 0.2863 -0.0200 0.0443  -0.0088 54  SER D CA  
6944  C  C   . SER D  54  ? 0.1696 0.1597 0.2955 -0.0155 0.0566  -0.0306 54  SER D C   
6945  O  O   . SER D  54  ? 0.1511 0.1617 0.2935 -0.0093 0.0648  -0.0250 54  SER D O   
6946  C  CB  . SER D  54  ? 0.1061 0.2064 0.2820 0.0010  -0.0137 -0.0410 54  SER D CB  
6947  O  OG  . SER D  54  ? 0.1362 0.2319 0.2865 -0.0127 0.0491  -0.0280 54  SER D OG  
6948  N  N   . ALA D  55  ? 0.2014 0.1727 0.2772 -0.0504 0.0581  -0.0131 55  ALA D N   
6949  C  CA  . ALA D  55  ? 0.2741 0.1561 0.3028 -0.0324 0.1096  -0.0104 55  ALA D CA  
6950  C  C   . ALA D  55  ? 0.1809 0.2495 0.2651 -0.0252 0.0671  -0.0394 55  ALA D C   
6951  O  O   . ALA D  55  ? 0.2362 0.2542 0.2391 -0.0233 0.0803  -0.0762 55  ALA D O   
6952  C  CB  . ALA D  55  ? 0.6802 0.1623 0.3176 -0.0838 0.0452  -0.0255 55  ALA D CB  
6953  N  N   . ASN D  56  ? 0.1856 0.2000 0.3190 -0.0285 0.0631  -0.0736 56  ASN D N   
6954  C  CA  . ASN D  56  ? 0.1896 0.2292 0.2287 -0.0162 0.0766  -0.0373 56  ASN D CA  
6955  C  C   . ASN D  56  ? 0.1194 0.2208 0.3371 0.0088  0.0368  0.0078  56  ASN D C   
6956  O  O   . ASN D  56  ? 0.1721 0.2443 0.5311 0.0172  -0.0350 0.0811  56  ASN D O   
6957  C  CB  . ASN D  56  ? 0.1527 0.2727 0.3788 -0.0608 -0.0035 -0.0706 56  ASN D CB  
6958  C  CG  . ASN D  56  ? 0.6399 0.3106 0.7728 0.0562  -0.2088 -0.3235 56  ASN D CG  
6959  O  OD1 . ASN D  56  ? 0.3522 0.7688 0.6319 -0.0201 -0.0571 -0.4318 56  ASN D OD1 
6960  N  ND2 . ASN D  56  ? 2.1268 0.7943 0.7221 -0.9595 -0.0012 -0.1480 56  ASN D ND2 
6961  N  N   A LYS D  57  ? 0.1021 0.2336 0.3001 0.0218  0.0531  0.0181  57  LYS D N   
6962  N  N   B LYS D  57  ? 0.1529 0.1425 0.2254 -0.0410 0.0625  0.0195  57  LYS D N   
6963  C  CA  A LYS D  57  ? 0.1140 0.2075 0.3251 0.0219  0.0318  0.0419  57  LYS D CA  
6964  C  CA  B LYS D  57  ? 0.1017 0.1574 0.2906 -0.0421 0.0452  0.0263  57  LYS D CA  
6965  C  C   A LYS D  57  ? 0.1394 0.1619 0.2890 0.0066  0.0362  0.0375  57  LYS D C   
6966  C  C   B LYS D  57  ? 0.1213 0.1768 0.2312 -0.0078 0.0264  0.0355  57  LYS D C   
6967  O  O   A LYS D  57  ? 0.1427 0.1730 0.4011 0.0502  0.0507  0.0681  57  LYS D O   
6968  O  O   B LYS D  57  ? 0.1389 0.2003 0.3185 0.0264  0.0728  0.0467  57  LYS D O   
6969  C  CB  A LYS D  57  ? 0.1464 0.3384 0.3221 0.0445  0.0621  0.0137  57  LYS D CB  
6970  C  CB  B LYS D  57  ? 0.2025 0.0809 0.2820 -0.0331 0.0747  0.0324  57  LYS D CB  
6971  C  CG  A LYS D  57  ? 0.2087 0.2402 0.2917 0.0987  0.1008  0.0238  57  LYS D CG  
6972  C  CG  B LYS D  57  ? 0.2154 0.2786 0.2766 -0.1071 0.1412  -0.0511 57  LYS D CG  
6973  C  CD  A LYS D  57  ? 0.3032 0.4774 0.3603 0.0988  0.1184  -0.0913 57  LYS D CD  
6974  C  CD  B LYS D  57  ? 0.3190 0.3689 0.3046 -0.0983 0.1299  -0.0048 57  LYS D CD  
6975  C  CE  A LYS D  57  ? 0.2393 0.5267 0.4730 0.1071  0.0557  -0.0794 57  LYS D CE  
6976  C  CE  B LYS D  57  ? 0.3842 0.4370 0.2872 -0.0188 0.1826  0.0597  57  LYS D CE  
6977  N  NZ  A LYS D  57  ? 0.1335 0.3914 0.5931 0.0318  0.0731  -0.1199 57  LYS D NZ  
6978  N  NZ  B LYS D  57  ? 0.4093 0.3844 0.3177 -0.0463 0.1494  0.0555  57  LYS D NZ  
6979  N  N   . GLN D  58  ? 0.1054 0.2005 0.2574 -0.0178 0.0286  0.0046  58  GLN D N   
6980  C  CA  . GLN D  58  ? 0.1066 0.2502 0.2430 -0.0370 0.0152  0.0278  58  GLN D CA  
6981  C  C   . GLN D  58  ? 0.1384 0.1396 0.1838 -0.0041 0.0303  0.0181  58  GLN D C   
6982  O  O   . GLN D  58  ? 0.1466 0.1581 0.2721 0.0131  0.0171  -0.0170 58  GLN D O   
6983  C  CB  . GLN D  58  ? 0.1868 0.5454 0.2393 -0.1076 -0.0247 0.1362  58  GLN D CB  
6984  C  CG  . GLN D  58  ? 0.5274 0.6816 0.2885 -0.1967 -0.0247 0.1495  58  GLN D CG  
6985  C  CD  . GLN D  58  ? 0.3427 1.2969 0.3395 -0.3772 -0.0630 0.2806  58  GLN D CD  
6986  O  OE1 . GLN D  58  ? 0.7861 1.3198 0.6976 -0.3158 -0.3185 0.1351  58  GLN D OE1 
6987  N  NE2 . GLN D  58  ? 0.5613 2.1960 2.0940 -0.1949 -0.4575 1.0891  58  GLN D NE2 
6988  N  N   . PHE D  59  ? 0.1141 0.1707 0.1938 -0.0195 0.0170  0.0364  59  PHE D N   
6989  C  CA  . PHE D  59  ? 0.1154 0.1502 0.1759 -0.0219 0.0082  0.0272  59  PHE D CA  
6990  C  C   . PHE D  59  ? 0.1326 0.1459 0.1659 -0.0124 0.0116  0.0102  59  PHE D C   
6991  O  O   . PHE D  59  ? 0.1396 0.1630 0.1612 -0.0255 0.0197  -0.0103 59  PHE D O   
6992  C  CB  . PHE D  59  ? 0.1389 0.1324 0.1947 0.0094  0.0364  0.0401  59  PHE D CB  
6993  C  CG  . PHE D  59  ? 0.1400 0.1172 0.1755 -0.0037 0.0344  0.0265  59  PHE D CG  
6994  C  CD1 . PHE D  59  ? 0.1301 0.1410 0.1791 -0.0097 0.0237  0.0303  59  PHE D CD1 
6995  C  CD2 . PHE D  59  ? 0.1665 0.1705 0.1623 0.0068  0.0386  0.0194  59  PHE D CD2 
6996  C  CE1 . PHE D  59  ? 0.1421 0.1441 0.2000 0.0131  0.0511  0.0131  59  PHE D CE1 
6997  C  CE2 . PHE D  59  ? 0.1559 0.1504 0.2032 0.0093  0.0283  0.0228  59  PHE D CE2 
6998  C  CZ  . PHE D  59  ? 0.1518 0.1387 0.1932 0.0008  0.0317  0.0261  59  PHE D CZ  
6999  N  N   . LEU D  60  ? 0.1243 0.1590 0.1601 -0.0151 0.0163  0.0166  60  LEU D N   
7000  C  CA  . LEU D  60  ? 0.1407 0.1648 0.1427 -0.0031 0.0217  0.0564  60  LEU D CA  
7001  C  C   . LEU D  60  ? 0.1339 0.1787 0.1350 -0.0201 -0.0044 0.0652  60  LEU D C   
7002  O  O   . LEU D  60  ? 0.1411 0.1730 0.1439 -0.0155 0.0078  0.0322  60  LEU D O   
7003  C  CB  . LEU D  60  ? 0.1673 0.1641 0.2275 -0.0108 0.0324  0.0623  60  LEU D CB  
7004  C  CG  . LEU D  60  ? 0.2594 0.2021 0.3032 -0.0049 0.0121  0.1580  60  LEU D CG  
7005  C  CD1 . LEU D  60  ? 0.3161 0.2014 0.2703 0.0223  0.0829  0.1040  60  LEU D CD1 
7006  C  CD2 . LEU D  60  ? 0.2845 0.1960 0.4187 -0.0394 0.0293  0.1375  60  LEU D CD2 
7007  N  N   . LEU D  61  ? 0.1089 0.2148 0.1283 -0.0357 0.0076  0.0383  61  LEU D N   
7008  C  CA  . LEU D  61  ? 0.1161 0.2037 0.1319 -0.0456 0.0074  0.0410  61  LEU D CA  
7009  C  C   . LEU D  61  ? 0.1484 0.1921 0.1497 -0.0260 -0.0214 0.0636  61  LEU D C   
7010  O  O   . LEU D  61  ? 0.1637 0.2303 0.1497 -0.0379 -0.0226 0.0727  61  LEU D O   
7011  C  CB  . LEU D  61  ? 0.1168 0.2422 0.1412 -0.0377 0.0031  -0.0043 61  LEU D CB  
7012  C  CG  . LEU D  61  ? 0.1592 0.1806 0.1414 -0.0322 0.0173  -0.0092 61  LEU D CG  
7013  C  CD1 . LEU D  61  ? 0.1763 0.1527 0.1486 0.0000  0.0225  0.0085  61  LEU D CD1 
7014  C  CD2 . LEU D  61  ? 0.2187 0.2772 0.1547 -0.0850 0.0204  -0.0333 61  LEU D CD2 
7015  N  N   . THR D  62  ? 0.1271 0.2481 0.1522 -0.0478 -0.0098 0.0817  62  THR D N   
7016  C  CA  . THR D  62  ? 0.1480 0.3203 0.1811 -0.1093 -0.0103 0.0888  62  THR D CA  
7017  C  C   . THR D  62  ? 0.1583 0.3197 0.2111 -0.1172 0.0071  0.1482  62  THR D C   
7018  O  O   . THR D  62  ? 0.1606 0.4293 0.2012 -0.0825 0.0144  0.1641  62  THR D O   
7019  C  CB  . THR D  62  ? 0.2262 0.1915 0.4555 -0.0289 0.0808  0.0935  62  THR D CB  
7020  O  OG1 . THR D  62  ? 0.2888 0.1996 0.3321 0.0439  0.0493  0.0351  62  THR D OG1 
7021  C  CG2 . THR D  62  ? 0.3420 0.2484 0.6212 -0.0795 0.1240  0.1189  62  THR D CG2 
7022  N  N   . ASN D  63  ? 0.1554 0.1847 0.2174 -0.0105 0.0304  0.0263  63  ASN D N   
7023  C  CA  . ASN D  63  ? 0.1876 0.1717 0.2183 -0.0248 0.0592  0.0483  63  ASN D CA  
7024  C  C   . ASN D  63  ? 0.2433 0.1054 0.1495 0.0199  0.0799  0.0205  63  ASN D C   
7025  O  O   . ASN D  63  ? 0.1883 0.1138 0.2529 -0.0138 -0.0087 0.0386  63  ASN D O   
7026  C  CB  . ASN D  63  ? 0.1538 0.2499 0.1425 -0.0496 0.0098  0.0566  63  ASN D CB  
7027  C  CG  . ASN D  63  ? 0.1507 0.1854 0.1671 -0.0592 -0.0126 0.0601  63  ASN D CG  
7028  O  OD1 . ASN D  63  ? 0.1793 0.2206 0.1466 -0.0568 -0.0017 0.0412  63  ASN D OD1 
7029  N  ND2 . ASN D  63  ? 0.2201 0.2036 0.1621 -0.0403 -0.0126 0.0722  63  ASN D ND2 
7030  N  N   . ASN D  64  ? 0.1974 0.1807 0.1534 -0.0003 0.0175  0.0269  64  ASN D N   
7031  C  CA  . ASN D  64  ? 0.2788 0.1526 0.2451 -0.0099 0.1322  -0.0026 64  ASN D CA  
7032  C  C   . ASN D  64  ? 0.2406 0.1680 0.1536 -0.0076 0.0252  0.0086  64  ASN D C   
7033  O  O   . ASN D  64  ? 0.2213 0.1989 0.2081 -0.0019 0.0113  0.0015  64  ASN D O   
7034  C  CB  . ASN D  64  ? 0.2438 0.2161 0.2069 0.0568  0.0551  0.0043  64  ASN D CB  
7035  C  CG  . ASN D  64  ? 0.2221 0.1844 0.1752 -0.0132 0.0342  0.0070  64  ASN D CG  
7036  O  OD1 . ASN D  64  ? 0.2202 0.1375 0.1714 -0.0219 0.0329  0.0048  64  ASN D OD1 
7037  N  ND2 . ASN D  64  ? 0.2820 0.2892 0.1881 0.0281  0.0412  0.0104  64  ASN D ND2 
7038  N  N   . GLY D  65  ? 0.2055 0.3375 0.1211 -0.0549 0.0551  -0.0003 65  GLY D N   
7039  C  CA  . GLY D  65  ? 0.1717 0.3474 0.2018 -0.0425 0.0759  0.0676  65  GLY D CA  
7040  C  C   . GLY D  65  ? 0.2664 0.2662 0.1432 -0.0794 -0.0137 0.0584  65  GLY D C   
7041  O  O   . GLY D  65  ? 0.1998 0.3786 0.2168 -0.0878 0.0394  0.0324  65  GLY D O   
7042  N  N   . HIS D  66  ? 0.2021 0.1773 0.1480 -0.0388 0.0054  0.0031  66  HIS D N   
7043  C  CA  . HIS D  66  ? 0.2172 0.1407 0.1471 -0.0177 -0.0199 -0.0089 66  HIS D CA  
7044  C  C   . HIS D  66  ? 0.1535 0.1693 0.1412 -0.0304 0.0447  -0.0172 66  HIS D C   
7045  O  O   . HIS D  66  ? 0.1854 0.1086 0.1844 0.0175  0.0289  0.0013  66  HIS D O   
7046  C  CB  . HIS D  66  ? 0.2664 0.1441 0.1344 0.0292  -0.0026 0.0087  66  HIS D CB  
7047  C  CG  . HIS D  66  ? 0.2278 0.1795 0.1642 -0.0179 -0.0178 -0.0073 66  HIS D CG  
7048  N  ND1 . HIS D  66  ? 0.2386 0.1694 0.1502 -0.0243 -0.0073 -0.0135 66  HIS D ND1 
7049  C  CD2 . HIS D  66  ? 0.2714 0.2048 0.1179 0.0165  -0.0007 0.0031  66  HIS D CD2 
7050  C  CE1 . HIS D  66  ? 0.2036 0.1405 0.1242 -0.0645 0.0081  0.0131  66  HIS D CE1 
7051  N  NE2 . HIS D  66  ? 0.2053 0.2685 0.1777 -0.0500 0.0159  0.0335  66  HIS D NE2 
7052  N  N   A SER D  67  ? 0.1689 0.1306 0.1687 -0.0135 0.0342  0.0107  67  SER D N   
7053  N  N   B SER D  67  ? 0.1699 0.1328 0.1671 -0.0120 0.0355  0.0103  67  SER D N   
7054  C  CA  A SER D  67  ? 0.1509 0.1660 0.1376 -0.0156 0.0187  0.0000  67  SER D CA  
7055  C  CA  B SER D  67  ? 0.1504 0.1752 0.1475 -0.0093 0.0173  -0.0003 67  SER D CA  
7056  C  C   A SER D  67  ? 0.1858 0.1389 0.1401 -0.0256 0.0151  0.0373  67  SER D C   
7057  C  C   B SER D  67  ? 0.1842 0.1398 0.1401 -0.0232 0.0168  0.0353  67  SER D C   
7058  O  O   A SER D  67  ? 0.1804 0.1597 0.1807 -0.0020 -0.0008 0.0181  67  SER D O   
7059  O  O   B SER D  67  ? 0.1809 0.1603 0.1800 -0.0013 -0.0017 0.0188  67  SER D O   
7060  C  CB  A SER D  67  ? 0.2114 0.1278 0.1392 -0.0322 0.0289  0.0388  67  SER D CB  
7061  C  CB  B SER D  67  ? 0.2350 0.1797 0.1491 -0.0041 0.0124  0.0208  67  SER D CB  
7062  O  OG  A SER D  67  ? 0.0987 0.1030 0.0782 -0.0104 0.0357  0.0337  67  SER D OG  
7063  O  OG  B SER D  67  ? 0.1666 0.1493 0.1606 -0.0046 0.0340  -0.0046 67  SER D OG  
7064  N  N   A VAL D  68  ? 0.1782 0.1288 0.1748 -0.0113 0.0276  0.0218  68  VAL D N   
7065  N  N   B VAL D  68  ? 0.1779 0.1283 0.1757 -0.0104 0.0269  0.0216  68  VAL D N   
7066  C  CA  A VAL D  68  ? 0.1577 0.1355 0.2303 0.0132  0.0304  -0.0284 68  VAL D CA  
7067  C  CA  B VAL D  68  ? 0.1453 0.1730 0.2416 0.0040  0.0381  -0.0298 68  VAL D CA  
7068  C  C   A VAL D  68  ? 0.1571 0.2084 0.2029 -0.0518 0.0570  0.0516  68  VAL D C   
7069  C  C   B VAL D  68  ? 0.1459 0.2452 0.1962 -0.0384 0.0604  0.0285  68  VAL D C   
7070  O  O   A VAL D  68  ? 0.1563 0.2445 0.1237 -0.0220 0.0432  -0.0299 68  VAL D O   
7071  O  O   B VAL D  68  ? 0.1536 0.2601 0.1292 -0.0177 0.0520  -0.0337 68  VAL D O   
7072  C  CB  A VAL D  68  ? 0.1962 0.1332 0.1773 -0.0027 0.0292  0.0154  68  VAL D CB  
7073  C  CB  B VAL D  68  ? 0.1976 0.1738 0.1865 -0.0026 0.0333  0.0017  68  VAL D CB  
7074  C  CG1 A VAL D  68  ? 0.1711 0.1247 0.1152 -0.0037 0.0531  -0.0320 68  VAL D CG1 
7075  C  CG1 B VAL D  68  ? 0.2504 0.2211 0.2364 0.0001  0.0353  0.0359  68  VAL D CG1 
7076  C  CG2 A VAL D  68  ? 0.2170 0.3314 0.2373 0.0193  -0.0135 0.0635  68  VAL D CG2 
7077  C  CG2 B VAL D  68  ? 0.1881 0.2012 0.1610 0.0054  0.0091  0.0229  68  VAL D CG2 
7078  N  N   . LYS D  69  ? 0.1581 0.3023 0.0957 -0.0351 0.0063  0.0544  69  LYS D N   
7079  C  CA  . LYS D  69  ? 0.1303 0.1723 0.1172 -0.0401 0.0182  0.0322  69  LYS D CA  
7080  C  C   . LYS D  69  ? 0.1249 0.1290 0.1173 -0.0184 0.0098  0.0326  69  LYS D C   
7081  O  O   . LYS D  69  ? 0.1455 0.2492 0.1269 -0.0522 -0.0120 0.0829  69  LYS D O   
7082  C  CB  . LYS D  69  ? 0.2057 0.1551 0.2118 -0.0373 -0.0283 0.0401  69  LYS D CB  
7083  C  CG  . LYS D  69  ? 0.2129 0.1790 0.2739 -0.0186 -0.0573 0.0093  69  LYS D CG  
7084  C  CD  . LYS D  69  ? 0.2996 0.1114 0.4072 0.0175  -0.0131 -0.0441 69  LYS D CD  
7085  C  CE  . LYS D  69  ? 0.2499 0.1852 0.4038 -0.0200 -0.0214 0.0226  69  LYS D CE  
7086  N  NZ  . LYS D  69  ? 0.4706 0.1994 0.3030 -0.0176 -0.0458 0.0237  69  LYS D NZ  
7087  N  N   . LEU D  70  ? 0.1172 0.1071 0.1036 0.0000  0.0292  -0.0041 70  LEU D N   
7088  C  CA  . LEU D  70  ? 0.0998 0.1109 0.1328 -0.0006 0.0263  -0.0062 70  LEU D CA  
7089  C  C   . LEU D  70  ? 0.1513 0.0861 0.1136 0.0000  0.0225  0.0147  70  LEU D C   
7090  O  O   . LEU D  70  ? 0.1224 0.1039 0.1208 0.0044  0.0247  0.0076  70  LEU D O   
7091  C  CB  . LEU D  70  ? 0.1310 0.0965 0.1391 0.0000  0.0285  -0.0201 70  LEU D CB  
7092  C  CG  . LEU D  70  ? 0.1271 0.1100 0.1486 -0.0138 0.0375  -0.0068 70  LEU D CG  
7093  C  CD1 . LEU D  70  ? 0.1304 0.1775 0.1509 0.0017  0.0038  -0.0085 70  LEU D CD1 
7094  C  CD2 . LEU D  70  ? 0.1687 0.1289 0.1932 -0.0252 0.0326  -0.0092 70  LEU D CD2 
7095  N  N   . ASN D  71  ? 0.1389 0.0834 0.1182 0.0103  0.0278  0.0070  71  ASN D N   
7096  C  CA  . ASN D  71  ? 0.1439 0.0915 0.1483 0.0108  0.0522  0.0109  71  ASN D CA  
7097  C  C   . ASN D  71  ? 0.1326 0.1274 0.1360 0.0241  0.0412  0.0093  71  ASN D C   
7098  O  O   . ASN D  71  ? 0.1610 0.1744 0.1571 -0.0179 0.0416  -0.0063 71  ASN D O   
7099  C  CB  . ASN D  71  ? 0.2465 0.1360 0.1578 0.0635  0.0529  0.0373  71  ASN D CB  
7100  C  CG  . ASN D  71  ? 0.3111 0.1495 0.1911 0.0452  0.1145  0.0640  71  ASN D CG  
7101  O  OD1 . ASN D  71  ? 0.3370 0.1664 0.2761 -0.0476 0.1088  0.0028  71  ASN D OD1 
7102  N  ND2 . ASN D  71  ? 0.4435 0.1574 0.3097 0.0137  0.0430  0.1084  71  ASN D ND2 
7103  N  N   . LEU D  72  ? 0.1596 0.1012 0.1414 0.0217  0.0412  0.0105  72  LEU D N   
7104  C  CA  . LEU D  72  ? 0.1554 0.1053 0.1545 0.0348  0.0668  0.0370  72  LEU D CA  
7105  C  C   . LEU D  72  ? 0.1630 0.1049 0.1447 0.0364  0.0483  0.0142  72  LEU D C   
7106  O  O   . LEU D  72  ? 0.2093 0.1134 0.1840 0.0199  0.0949  0.0098  72  LEU D O   
7107  C  CB  . LEU D  72  ? 0.1167 0.1102 0.1574 0.0170  0.0493  0.0218  72  LEU D CB  
7108  C  CG  . LEU D  72  ? 0.1617 0.0936 0.1648 0.0175  0.0394  0.0132  72  LEU D CG  
7109  C  CD1 . LEU D  72  ? 0.1164 0.1356 0.1543 0.0052  0.0474  0.0384  72  LEU D CD1 
7110  C  CD2 . LEU D  72  ? 0.1500 0.1243 0.2000 0.0144  0.0498  -0.0087 72  LEU D CD2 
7111  N  N   . PRO D  73  ? 0.1547 0.1173 0.1756 0.0271  0.0637  0.0131  73  PRO D N   
7112  C  CA  . PRO D  73  ? 0.1775 0.1317 0.2020 0.0384  0.0855  -0.0051 73  PRO D CA  
7113  C  C   . PRO D  73  ? 0.2233 0.1262 0.1741 0.0285  0.0878  0.0259  73  PRO D C   
7114  O  O   . PRO D  73  ? 0.2147 0.1842 0.2095 0.0436  0.0938  0.0593  73  PRO D O   
7115  C  CB  . PRO D  73  ? 0.1574 0.1662 0.2685 0.0375  0.0742  0.0599  73  PRO D CB  
7116  C  CG  . PRO D  73  ? 0.1516 0.1653 0.2469 0.0320  0.0775  0.0326  73  PRO D CG  
7117  C  CD  . PRO D  73  ? 0.1518 0.1368 0.2099 0.0220  0.0568  0.0438  73  PRO D CD  
7118  N  N   . SER D  74  ? 0.2890 0.1775 0.1990 0.0666  0.1052  0.0074  74  SER D N   
7119  C  CA  . SER D  74  ? 0.2567 0.2096 0.1929 0.0395  0.0837  0.0342  74  SER D CA  
7120  C  C   . SER D  74  ? 0.2833 0.2089 0.2718 0.1067  0.1410  0.0639  74  SER D C   
7121  O  O   . SER D  74  ? 0.3165 0.3393 0.2201 0.0910  0.1476  0.0745  74  SER D O   
7122  C  CB  . SER D  74  ? 0.4226 0.2196 0.2325 0.1318  0.0939  0.0120  74  SER D CB  
7123  O  OG  . SER D  74  ? 0.4293 0.2222 0.3283 0.1301  0.1269  -0.0175 74  SER D OG  
7124  N  N   A ASP D  75  ? 0.2280 0.2325 0.2592 0.0930  0.1290  0.1080  75  ASP D N   
7125  N  N   B ASP D  75  ? 0.2285 0.2364 0.2605 0.0926  0.1288  0.1057  75  ASP D N   
7126  C  CA  A ASP D  75  ? 0.2184 0.2457 0.3648 0.1163  0.1648  0.1632  75  ASP D CA  
7127  C  CA  B ASP D  75  ? 0.2246 0.2515 0.3752 0.1133  0.1710  0.1553  75  ASP D CA  
7128  C  C   A ASP D  75  ? 0.2255 0.2001 0.2777 0.0890  0.1341  0.1169  75  ASP D C   
7129  C  C   B ASP D  75  ? 0.2269 0.2057 0.2777 0.0847  0.1368  0.1146  75  ASP D C   
7130  O  O   A ASP D  75  ? 0.2118 0.3043 0.3314 0.0781  0.1387  0.1722  75  ASP D O   
7131  O  O   B ASP D  75  ? 0.2116 0.2987 0.3323 0.0851  0.1300  0.1750  75  ASP D O   
7132  C  CB  A ASP D  75  ? 0.1835 0.2863 0.5066 0.1110  0.1827  0.2222  75  ASP D CB  
7133  C  CB  B ASP D  75  ? 0.2608 0.3671 0.5450 0.0560  0.1280  0.1745  75  ASP D CB  
7134  C  CG  A ASP D  75  ? 0.1899 0.5501 0.4780 0.1358  0.1621  0.2374  75  ASP D CG  
7135  C  CG  B ASP D  75  ? 0.2813 0.4766 0.5629 0.1164  0.1991  0.2436  75  ASP D CG  
7136  O  OD1 A ASP D  75  ? 0.3041 0.3682 0.6491 0.0694  0.2937  0.2171  75  ASP D OD1 
7137  O  OD1 B ASP D  75  ? 0.3655 0.4144 0.6529 0.1748  0.2576  0.1240  75  ASP D OD1 
7138  O  OD2 A ASP D  75  ? 0.2770 0.9334 0.8460 -0.0082 0.1914  -0.2194 75  ASP D OD2 
7139  O  OD2 B ASP D  75  ? 0.4081 0.9243 0.8044 -0.1841 0.0676  0.1708  75  ASP D OD2 
7140  N  N   . MET D  76  ? 0.1924 0.1788 0.2606 0.0662  0.1022  0.0857  76  MET D N   
7141  C  CA  . MET D  76  ? 0.1577 0.1870 0.2307 0.0355  0.0932  0.0749  76  MET D CA  
7142  C  C   . MET D  76  ? 0.1351 0.1699 0.2351 0.0555  0.0973  0.0952  76  MET D C   
7143  O  O   . MET D  76  ? 0.1620 0.1617 0.2190 0.0410  0.1097  0.0456  76  MET D O   
7144  C  CB  . MET D  76  ? 0.1702 0.1897 0.2673 0.0518  0.1275  0.0623  76  MET D CB  
7145  C  CG  . MET D  76  ? 0.1689 0.1351 0.2247 0.0346  0.0910  0.0315  76  MET D CG  
7146  S  SD  . MET D  76  ? 0.1592 0.1592 0.2211 0.0105  0.0771  0.0297  76  MET D SD  
7147  C  CE  . MET D  76  ? 0.1592 0.1389 0.2093 0.0017  0.0747  0.0232  76  MET D CE  
7148  N  N   . HIS D  77  ? 0.1779 0.2312 0.2113 0.1093  0.1182  0.0998  77  HIS D N   
7149  C  CA  . HIS D  77  ? 0.1960 0.1676 0.2091 0.0763  0.1106  0.0965  77  HIS D CA  
7150  C  C   . HIS D  77  ? 0.1879 0.2016 0.1944 0.0861  0.1238  0.1050  77  HIS D C   
7151  O  O   . HIS D  77  ? 0.2466 0.1809 0.2087 0.0799  0.1115  0.0727  77  HIS D O   
7152  C  CB  . HIS D  77  ? 0.2030 0.2544 0.2434 0.1259  0.1238  0.0588  77  HIS D CB  
7153  C  CG  . HIS D  77  ? 0.3070 0.2032 0.2587 0.1309  0.1687  0.0741  77  HIS D CG  
7154  N  ND1 . HIS D  77  ? 0.2680 0.2569 0.4077 0.1089  0.2020  0.1190  77  HIS D ND1 
7155  C  CD2 . HIS D  77  ? 0.3465 0.3242 0.3316 0.1141  0.2422  0.1604  77  HIS D CD2 
7156  C  CE1 . HIS D  77  ? 0.2833 0.3102 0.3312 0.0302  0.2052  0.0265  77  HIS D CE1 
7157  N  NE2 . HIS D  77  ? 0.2962 0.3537 0.4494 0.0970  0.2414  0.1062  77  HIS D NE2 
7158  N  N   A ILE D  78  ? 0.1976 0.1498 0.1904 0.1162  0.1057  0.0582  78  ILE D N   
7159  N  N   B ILE D  78  ? 0.2488 0.1897 0.1735 0.0507  0.0803  0.0753  78  ILE D N   
7160  C  CA  A ILE D  78  ? 0.2199 0.1892 0.1658 0.1261  0.1103  0.0834  78  ILE D CA  
7161  C  CA  B ILE D  78  ? 0.2023 0.1430 0.1421 0.0154  0.0697  0.0469  78  ILE D CA  
7162  C  C   A ILE D  78  ? 0.2170 0.2233 0.1766 0.1720  0.1186  0.1037  78  ILE D C   
7163  C  C   B ILE D  78  ? 0.1826 0.1962 0.1213 -0.0322 -0.0116 0.0060  78  ILE D C   
7164  O  O   A ILE D  78  ? 0.3271 0.2878 0.0733 0.2492  -0.0082 0.0423  78  ILE D O   
7165  O  O   B ILE D  78  ? 0.1401 0.1524 0.0635 0.0434  -0.0259 0.0405  78  ILE D O   
7166  C  CB  A ILE D  78  ? 0.2364 0.1125 0.1005 0.0690  0.0746  0.0359  78  ILE D CB  
7167  C  CB  B ILE D  78  ? 0.1745 0.1836 0.1644 -0.0219 0.0190  -0.0243 78  ILE D CB  
7168  C  CG1 A ILE D  78  ? 0.2199 0.1870 0.1346 0.0615  0.1052  0.0270  78  ILE D CG1 
7169  C  CG1 B ILE D  78  ? 0.1756 0.1199 0.1796 0.0099  0.0461  -0.0151 78  ILE D CG1 
7170  C  CG2 A ILE D  78  ? 0.2499 0.1814 0.1858 0.1102  0.1216  0.1221  78  ILE D CG2 
7171  C  CG2 B ILE D  78  ? 0.1845 0.1506 0.1447 -0.0132 0.0269  0.0073  78  ILE D CG2 
7172  C  CD1 A ILE D  78  ? 0.2102 0.1642 0.1314 0.0727  0.0333  0.0328  78  ILE D CD1 
7173  C  CD1 B ILE D  78  ? 0.1662 0.1240 0.2055 0.0291  -0.0052 -0.0194 78  ILE D CD1 
7174  N  N   . GLN D  79  ? 0.2585 0.1962 0.2161 0.0654  0.1456  0.0753  79  GLN D N   
7175  C  CA  . GLN D  79  ? 0.3626 0.2621 0.2352 0.1097  0.2032  0.0678  79  GLN D CA  
7176  C  C   . GLN D  79  ? 0.4375 0.1633 0.2030 0.0855  0.0807  0.0684  79  GLN D C   
7177  O  O   . GLN D  79  ? 0.5676 0.2517 0.2215 0.1752  0.1513  0.0758  79  GLN D O   
7178  C  CB  . GLN D  79  ? 0.3407 0.4183 0.5220 0.1876  0.2644  0.2513  79  GLN D CB  
7179  C  CG  . GLN D  79  ? 0.3952 0.6779 0.5145 0.2454  0.2212  0.3355  79  GLN D CG  
7180  N  N   . GLY D  80  ? 0.6036 0.1712 0.1831 0.0570  0.1247  0.0013  80  GLY D N   
7181  C  CA  . GLY D  80  ? 0.3116 0.1544 0.2896 -0.0548 0.1709  -0.0375 80  GLY D CA  
7182  C  C   . GLY D  80  ? 0.7587 0.4253 0.5803 -0.1580 0.1439  -0.0957 80  GLY D C   
7183  O  O   . GLY D  80  ? 2.0137 0.8755 5.2481 -0.2206 -1.1233 2.0192  80  GLY D O   
7184  N  N   . LEU D  81  ? 0.2782 0.1432 0.1418 -0.0111 0.0487  -0.0244 81  LEU D N   
7185  C  CA  . LEU D  81  ? 0.2623 0.1543 0.1554 -0.0091 0.0346  -0.0283 81  LEU D CA  
7186  C  C   . LEU D  81  ? 0.3061 0.1520 0.1216 -0.0293 0.0652  -0.0263 81  LEU D C   
7187  O  O   . LEU D  81  ? 0.3409 0.2025 0.2669 -0.0294 0.0746  -0.0612 81  LEU D O   
7188  C  CB  . LEU D  81  ? 0.4111 0.1721 0.1549 0.0768  0.1438  0.0217  81  LEU D CB  
7189  C  CG  . LEU D  81  ? 0.3402 0.1667 0.1756 0.1108  0.1023  0.0157  81  LEU D CG  
7190  C  CD1 . LEU D  81  ? 0.4277 0.2222 0.1540 0.1221  0.1200  0.0511  81  LEU D CD1 
7191  C  CD2 . LEU D  81  ? 0.3481 0.1928 0.1868 0.0947  0.0971  0.0551  81  LEU D CD2 
7192  N  N   . GLN D  82  ? 0.2563 0.1462 0.1374 0.0148  0.0463  -0.0104 82  GLN D N   
7193  C  CA  . GLN D  82  ? 0.2260 0.1834 0.1538 0.0351  -0.0040 -0.0634 82  GLN D CA  
7194  C  C   . GLN D  82  ? 0.2317 0.1748 0.1240 -0.0076 0.0710  -0.0229 82  GLN D C   
7195  O  O   . GLN D  82  ? 0.2472 0.1759 0.1359 -0.0034 0.0636  -0.0289 82  GLN D O   
7196  C  CB  . GLN D  82  ? 0.2545 0.1858 0.1662 -0.0208 0.0141  -0.0229 82  GLN D CB  
7197  C  CG  . GLN D  82  ? 0.2278 0.2143 0.2414 -0.0175 0.0797  -0.0175 82  GLN D CG  
7198  C  CD  . GLN D  82  ? 0.3014 0.1378 0.2337 0.0020  0.0498  -0.0304 82  GLN D CD  
7199  O  OE1 . GLN D  82  ? 0.3296 0.1770 0.2567 -0.0131 0.0526  -0.0474 82  GLN D OE1 
7200  N  NE2 . GLN D  82  ? 0.3212 0.1612 0.2050 0.0093  0.0610  0.0086  82  GLN D NE2 
7201  N  N   . SER D  83  ? 0.2635 0.1646 0.1387 0.0172  0.0683  0.0044  83  SER D N   
7202  C  CA  . SER D  83  ? 0.2720 0.1243 0.1626 0.0260  0.0794  -0.0286 83  SER D CA  
7203  C  C   . SER D  83  ? 0.2958 0.0931 0.1247 0.0375  0.0644  0.0232  83  SER D C   
7204  O  O   . SER D  83  ? 0.3756 0.1075 0.1541 0.0542  0.1360  0.0306  83  SER D O   
7205  C  CB  . SER D  83  ? 0.2579 0.1396 0.1700 0.0103  0.0373  -0.0077 83  SER D CB  
7206  O  OG  . SER D  83  ? 0.3420 0.1799 0.1639 0.0644  0.0175  -0.0104 83  SER D OG  
7207  N  N   . ARG D  84  ? 0.2552 0.2309 0.1019 0.0154  0.1020  0.0351  84  ARG D N   
7208  C  CA  . ARG D  84  ? 0.2310 0.1569 0.1784 0.0306  0.0874  0.0645  84  ARG D CA  
7209  C  C   . ARG D  84  ? 0.2443 0.1168 0.1804 0.0425  0.1360  0.0328  84  ARG D C   
7210  O  O   . ARG D  84  ? 0.2878 0.1280 0.1984 0.0571  0.1679  0.0373  84  ARG D O   
7211  C  CB  . ARG D  84  ? 0.2307 0.2529 0.1691 0.0167  0.0737  0.0285  84  ARG D CB  
7212  C  CG  . ARG D  84  ? 0.2743 0.2185 0.2289 0.0747  -0.0130 -0.0171 84  ARG D CG  
7213  C  CD  . ARG D  84  ? 0.3452 0.3677 0.2445 -0.0874 -0.0680 0.1379  84  ARG D CD  
7214  N  NE  . ARG D  84  ? 0.3248 0.2391 0.2743 0.0808  0.0447  0.0335  84  ARG D NE  
7215  C  CZ  . ARG D  84  ? 0.2456 0.3073 0.2649 0.0710  0.0494  0.1102  84  ARG D CZ  
7216  N  NH1 . ARG D  84  ? 0.3257 0.4587 0.5289 0.1544  0.2128  0.1160  84  ARG D NH1 
7217  N  NH2 . ARG D  84  ? 0.4651 0.3763 0.2734 0.1964  0.0930  0.1682  84  ARG D NH2 
7218  N  N   . TYR D  85  ? 0.2353 0.1228 0.1375 0.0518  0.1103  0.0432  85  TYR D N   
7219  C  CA  . TYR D  85  ? 0.2118 0.1152 0.1278 0.0531  0.1000  0.0408  85  TYR D CA  
7220  C  C   . TYR D  85  ? 0.1960 0.1382 0.1671 0.0465  0.1147  0.0469  85  TYR D C   
7221  O  O   . TYR D  85  ? 0.1694 0.1590 0.1912 0.0230  0.0617  0.0540  85  TYR D O   
7222  C  CB  . TYR D  85  ? 0.1827 0.1398 0.1392 0.0436  0.0927  0.0062  85  TYR D CB  
7223  C  CG  . TYR D  85  ? 0.1965 0.0851 0.1254 0.0373  0.0487  -0.0035 85  TYR D CG  
7224  C  CD1 . TYR D  85  ? 0.2188 0.1267 0.1213 0.0593  0.0742  0.0171  85  TYR D CD1 
7225  C  CD2 . TYR D  85  ? 0.2028 0.0842 0.1430 0.0511  0.0653  -0.0038 85  TYR D CD2 
7226  C  CE1 . TYR D  85  ? 0.2502 0.1331 0.1204 0.0331  0.0615  0.0361  85  TYR D CE1 
7227  C  CE2 . TYR D  85  ? 0.2246 0.1085 0.1137 0.0487  0.0719  0.0024  85  TYR D CE2 
7228  C  CZ  . TYR D  85  ? 0.2307 0.0945 0.1287 0.0496  0.0710  0.0023  85  TYR D CZ  
7229  O  OH  . TYR D  85  ? 0.2669 0.1455 0.1279 0.0318  0.0271  -0.0037 85  TYR D OH  
7230  N  N   . SER D  86  ? 0.1735 0.1454 0.1249 0.0471  0.0838  0.0421  86  SER D N   
7231  C  CA  . SER D  86  ? 0.1647 0.1362 0.1412 0.0533  0.0819  0.0034  86  SER D CA  
7232  C  C   . SER D  86  ? 0.1754 0.0856 0.1441 0.0388  0.0824  0.0046  86  SER D C   
7233  O  O   . SER D  86  ? 0.1905 0.1143 0.1308 0.0329  0.0878  0.0024  86  SER D O   
7234  C  CB  . SER D  86  ? 0.2017 0.1626 0.1757 0.0841  0.1261  0.0313  86  SER D CB  
7235  O  OG  . SER D  86  ? 0.2086 0.1930 0.1622 0.0834  0.1146  0.0031  86  SER D OG  
7236  N  N   . ALA D  87  ? 0.1772 0.1036 0.1493 0.0491  0.1019  0.0384  87  ALA D N   
7237  C  CA  . ALA D  87  ? 0.1764 0.1107 0.1425 0.0236  0.0978  0.0118  87  ALA D CA  
7238  C  C   . ALA D  87  ? 0.1940 0.1186 0.1321 0.0658  0.0903  0.0241  87  ALA D C   
7239  O  O   . ALA D  87  ? 0.1642 0.1439 0.1563 0.0571  0.0891  0.0326  87  ALA D O   
7240  C  CB  . ALA D  87  ? 0.1726 0.1432 0.1554 0.0122  0.0870  0.0120  87  ALA D CB  
7241  N  N   . THR D  88  ? 0.1687 0.1107 0.1091 0.0375  0.0892  0.0093  88  THR D N   
7242  C  CA  . THR D  88  ? 0.1908 0.1028 0.1052 0.0286  0.0662  0.0170  88  THR D CA  
7243  C  C   . THR D  88  ? 0.1355 0.0646 0.1097 0.0157  0.0384  0.0038  88  THR D C   
7244  O  O   . THR D  88  ? 0.1590 0.0888 0.1125 0.0297  0.0443  0.0088  88  THR D O   
7245  C  CB  . THR D  88  ? 0.2346 0.1028 0.1163 0.0203  0.0586  0.0076  88  THR D CB  
7246  O  OG1 . THR D  88  ? 0.3010 0.1179 0.1411 -0.0153 0.0494  0.0046  88  THR D OG1 
7247  C  CG2 . THR D  88  ? 0.1928 0.1344 0.1815 0.0031  0.0575  -0.0542 88  THR D CG2 
7248  N  N   . GLN D  89  ? 0.1380 0.0865 0.1003 0.0223  0.0540  0.0087  89  GLN D N   
7249  C  CA  . GLN D  89  ? 0.1369 0.0755 0.0965 0.0159  0.0623  0.0113  89  GLN D CA  
7250  C  C   . GLN D  89  ? 0.1118 0.0820 0.0983 0.0115  0.0428  0.0027  89  GLN D C   
7251  O  O   . GLN D  89  ? 0.1335 0.0935 0.0899 0.0287  0.0377  0.0076  89  GLN D O   
7252  C  CB  . GLN D  89  ? 0.1533 0.0825 0.1114 0.0051  0.0540  -0.0006 89  GLN D CB  
7253  C  CG  . GLN D  89  ? 0.1452 0.1146 0.1304 -0.0071 0.0544  -0.0190 89  GLN D CG  
7254  C  CD  . GLN D  89  ? 0.1310 0.1228 0.1216 0.0088  0.0258  0.0032  89  GLN D CD  
7255  O  OE1 . GLN D  89  ? 0.1344 0.1088 0.1448 0.0104  0.0467  0.0000  89  GLN D OE1 
7256  N  NE2 . GLN D  89  ? 0.1940 0.1155 0.2409 -0.0131 0.0296  0.0083  89  GLN D NE2 
7257  N  N   . LEU D  90  ? 0.1096 0.0651 0.1098 0.0041  0.0507  0.0041  90  LEU D N   
7258  C  CA  . LEU D  90  ? 0.1125 0.0583 0.0987 0.0057  0.0535  0.0035  90  LEU D CA  
7259  C  C   . LEU D  90  ? 0.0952 0.0675 0.0966 -0.0005 0.0351  0.0144  90  LEU D C   
7260  O  O   . LEU D  90  ? 0.1143 0.0820 0.0957 0.0049  0.0445  0.0120  90  LEU D O   
7261  C  CB  . LEU D  90  ? 0.1115 0.0876 0.1247 -0.0005 0.0489  0.0154  90  LEU D CB  
7262  C  CG  . LEU D  90  ? 0.0978 0.0773 0.1558 -0.0034 0.0264  0.0083  90  LEU D CG  
7263  C  CD1 . LEU D  90  ? 0.1425 0.0829 0.1419 -0.0135 0.0430  -0.0233 90  LEU D CD1 
7264  C  CD2 . LEU D  90  ? 0.1337 0.0825 0.1761 -0.0173 0.0113  0.0109  90  LEU D CD2 
7265  N  N   . HIS D  91  ? 0.0980 0.0618 0.1032 0.0006  0.0502  -0.0040 91  HIS D N   
7266  C  CA  . HIS D  91  ? 0.1012 0.0671 0.0926 0.0023  0.0507  -0.0007 91  HIS D CA  
7267  C  C   . HIS D  91  ? 0.0870 0.0798 0.1048 0.0086  0.0381  -0.0031 91  HIS D C   
7268  O  O   . HIS D  91  ? 0.1121 0.0744 0.0954 0.0102  0.0427  0.0118  91  HIS D O   
7269  C  CB  . HIS D  91  ? 0.1116 0.0832 0.0798 -0.0092 0.0348  0.0216  91  HIS D CB  
7270  C  CG  . HIS D  91  ? 0.1115 0.0741 0.0797 -0.0043 0.0408  0.0077  91  HIS D CG  
7271  N  ND1 . HIS D  91  ? 0.1142 0.0730 0.1028 -0.0030 0.0460  -0.0008 91  HIS D ND1 
7272  C  CD2 . HIS D  91  ? 0.1230 0.0746 0.0772 -0.0046 0.0350  0.0043  91  HIS D CD2 
7273  C  CE1 . HIS D  91  ? 0.1008 0.0962 0.0948 0.0024  0.0397  -0.0041 91  HIS D CE1 
7274  N  NE2 . HIS D  91  ? 0.1057 0.0759 0.0768 -0.0017 0.0406  -0.0035 91  HIS D NE2 
7275  N  N   . LEU D  92  ? 0.0935 0.0824 0.1027 0.0099  0.0362  -0.0006 92  LEU D N   
7276  C  CA  . LEU D  92  ? 0.0994 0.0680 0.1010 0.0076  0.0337  -0.0097 92  LEU D CA  
7277  C  C   . LEU D  92  ? 0.1046 0.0719 0.0727 0.0046  0.0322  -0.0043 92  LEU D C   
7278  O  O   . LEU D  92  ? 0.1129 0.0732 0.1062 0.0027  0.0318  0.0034  92  LEU D O   
7279  C  CB  . LEU D  92  ? 0.1106 0.1102 0.1378 -0.0086 0.0322  -0.0333 92  LEU D CB  
7280  C  CG  . LEU D  92  ? 0.1057 0.1441 0.1281 -0.0168 0.0342  -0.0317 92  LEU D CG  
7281  C  CD1 . LEU D  92  ? 0.1448 0.1691 0.2127 0.0126  -0.0027 -0.0093 92  LEU D CD1 
7282  C  CD2 . LEU D  92  ? 0.1405 0.1048 0.2574 -0.0205 0.0240  0.0306  92  LEU D CD2 
7283  N  N   . HIS D  93  ? 0.0973 0.0757 0.0900 0.0062  0.0460  -0.0108 93  HIS D N   
7284  C  CA  . HIS D  93  ? 0.0985 0.0781 0.0861 -0.0071 0.0395  -0.0159 93  HIS D CA  
7285  C  C   . HIS D  93  ? 0.0940 0.0662 0.0690 -0.0015 0.0357  -0.0019 93  HIS D C   
7286  O  O   . HIS D  93  ? 0.1125 0.0702 0.0890 -0.0076 0.0423  -0.0031 93  HIS D O   
7287  C  CB  . HIS D  93  ? 0.1125 0.0769 0.0870 0.0096  0.0282  -0.0203 93  HIS D CB  
7288  C  CG  . HIS D  93  ? 0.1164 0.0675 0.0724 0.0000  0.0368  -0.0001 93  HIS D CG  
7289  N  ND1 . HIS D  93  ? 0.1134 0.0687 0.0850 -0.0054 0.0326  -0.0046 93  HIS D ND1 
7290  C  CD2 . HIS D  93  ? 0.1052 0.0851 0.0644 0.0043  0.0351  -0.0052 93  HIS D CD2 
7291  C  CE1 . HIS D  93  ? 0.1225 0.0769 0.0791 0.0063  0.0498  -0.0010 93  HIS D CE1 
7292  N  NE2 . HIS D  93  ? 0.1134 0.0651 0.0684 0.0028  0.0373  0.0020  93  HIS D NE2 
7293  N  N   . TRP D  94  ? 0.0976 0.0646 0.0895 0.0031  0.0456  -0.0122 94  TRP D N   
7294  C  CA  . TRP D  94  ? 0.1012 0.0776 0.0926 0.0076  0.0394  -0.0110 94  TRP D CA  
7295  C  C   . TRP D  94  ? 0.1177 0.0773 0.0730 -0.0021 0.0416  -0.0020 94  TRP D C   
7296  O  O   . TRP D  94  ? 0.1055 0.0854 0.0886 0.0000  0.0375  -0.0096 94  TRP D O   
7297  C  CB  . TRP D  94  ? 0.1247 0.0622 0.1021 -0.0137 0.0408  -0.0051 94  TRP D CB  
7298  C  CG  . TRP D  94  ? 0.1186 0.0590 0.0960 -0.0098 0.0306  -0.0070 94  TRP D CG  
7299  C  CD1 . TRP D  94  ? 0.1138 0.0625 0.1102 -0.0041 0.0373  -0.0031 94  TRP D CD1 
7300  C  CD2 . TRP D  94  ? 0.1331 0.0653 0.0872 -0.0087 0.0241  -0.0142 94  TRP D CD2 
7301  N  NE1 . TRP D  94  ? 0.1310 0.0723 0.1130 0.0007  0.0450  -0.0003 94  TRP D NE1 
7302  C  CE2 . TRP D  94  ? 0.1163 0.0712 0.1026 0.0006  0.0299  -0.0065 94  TRP D CE2 
7303  C  CE3 . TRP D  94  ? 0.1326 0.0878 0.0913 -0.0012 0.0333  -0.0195 94  TRP D CE3 
7304  C  CZ2 . TRP D  94  ? 0.1292 0.0775 0.1262 -0.0020 0.0428  -0.0071 94  TRP D CZ2 
7305  C  CZ3 . TRP D  94  ? 0.1206 0.1165 0.0942 0.0028  0.0307  -0.0152 94  TRP D CZ3 
7306  C  CH2 . TRP D  94  ? 0.1136 0.1082 0.1123 0.0082  0.0331  -0.0077 94  TRP D CH2 
7307  N  N   . GLY D  95  ? 0.1111 0.0939 0.0912 0.0065  0.0571  -0.0099 95  GLY D N   
7308  C  CA  . GLY D  95  ? 0.1098 0.0983 0.0985 0.0076  0.0529  -0.0093 95  GLY D CA  
7309  C  C   . GLY D  95  ? 0.1127 0.1057 0.1071 -0.0098 0.0603  -0.0217 95  GLY D C   
7310  O  O   . GLY D  95  ? 0.1367 0.1073 0.0834 -0.0012 0.0529  -0.0087 95  GLY D O   
7311  N  N   . ASN D  96  ? 0.1290 0.1313 0.1008 -0.0109 0.0592  -0.0410 96  ASN D N   
7312  C  CA  . ASN D  96  ? 0.1685 0.1267 0.0982 -0.0010 0.0658  -0.0200 96  ASN D CA  
7313  C  C   . ASN D  96  ? 0.1152 0.1685 0.1247 0.0001  0.0507  -0.0483 96  ASN D C   
7314  O  O   . ASN D  96  ? 0.1685 0.1371 0.1439 0.0044  0.0777  -0.0533 96  ASN D O   
7315  C  CB  . ASN D  96  ? 0.1971 0.1391 0.1446 -0.0071 0.0904  -0.0087 96  ASN D CB  
7316  C  CG  . ASN D  96  ? 0.2003 0.1694 0.2483 -0.0060 0.1441  -0.0487 96  ASN D CG  
7317  O  OD1 . ASN D  96  ? 0.2109 0.2745 0.3707 -0.0535 0.1738  -0.1880 96  ASN D OD1 
7318  N  ND2 . ASN D  96  ? 0.1497 0.1784 0.2637 0.0096  0.1066  -0.0088 96  ASN D ND2 
7319  N  N   . PRO D  97  ? 0.1606 0.2294 0.1292 -0.0024 0.0643  -0.0657 97  PRO D N   
7320  C  CA  . PRO D  97  ? 0.2021 0.2791 0.1744 -0.0097 0.0803  -0.1386 97  PRO D CA  
7321  C  C   . PRO D  97  ? 0.2226 0.2072 0.1536 -0.0120 0.0769  -0.1027 97  PRO D C   
7322  O  O   . PRO D  97  ? 0.4122 0.2278 0.2779 -0.0200 0.1009  -0.1583 97  PRO D O   
7323  C  CB  . PRO D  97  ? 0.2337 0.4004 0.1703 0.0450  0.0568  -0.1423 97  PRO D CB  
7324  C  CG  . PRO D  97  ? 0.2500 0.4122 0.1599 0.0467  0.0163  -0.1059 97  PRO D CG  
7325  C  CD  . PRO D  97  ? 0.1854 0.3170 0.1233 0.0586  0.0244  -0.0215 97  PRO D CD  
7326  N  N   . ASN D  98  ? 0.1705 0.2436 0.1389 0.0265  0.0608  -0.0553 98  ASN D N   
7327  C  CA  . ASN D  98  ? 0.2213 0.2806 0.1736 0.0331  0.0384  -0.0452 98  ASN D CA  
7328  C  C   . ASN D  98  ? 0.2994 0.2197 0.1687 0.0750  0.0903  -0.0236 98  ASN D C   
7329  O  O   . ASN D  98  ? 0.3167 0.4237 0.2190 0.1733  0.0982  -0.0109 98  ASN D O   
7330  C  CB  . ASN D  98  ? 0.2105 0.4580 0.2443 0.0573  0.1623  0.0122  98  ASN D CB  
7331  C  CG  . ASN D  98  ? 0.4595 0.7375 0.4311 0.0157  -0.0086 0.0320  98  ASN D CG  
7332  O  OD1 . ASN D  98  ? 4.3533 2.3110 0.9747 -2.3059 1.3550  -0.8528 98  ASN D OD1 
7333  N  ND2 . ASN D  98  ? 0.5145 0.8784 0.1527 -0.2454 0.0173  0.0447  98  ASN D ND2 
7334  N  N   . ASP D  99  ? 0.1756 0.1942 0.1351 0.0049  0.0790  -0.0155 99  ASP D N   
7335  C  CA  . ASP D  99  ? 0.1818 0.2167 0.1437 -0.0178 0.0813  -0.0300 99  ASP D CA  
7336  C  C   . ASP D  99  ? 0.1655 0.1125 0.1326 0.0041  0.0399  -0.0211 99  ASP D C   
7337  O  O   . ASP D  99  ? 0.1617 0.1142 0.1482 -0.0006 0.0549  -0.0183 99  ASP D O   
7338  C  CB  . ASP D  99  ? 0.1669 0.2276 0.1714 -0.0233 0.0608  -0.0085 99  ASP D CB  
7339  C  CG  . ASP D  99  ? 0.2691 0.1924 0.1651 -0.0474 0.0747  -0.0065 99  ASP D CG  
7340  O  OD1 . ASP D  99  ? 0.2766 0.2113 0.1874 -0.0218 0.0329  -0.0071 99  ASP D OD1 
7341  O  OD2 . ASP D  99  ? 0.2357 0.2698 0.2100 -0.0280 0.0164  -0.0337 99  ASP D OD2 
7342  N  N   . PRO D  100 ? 0.1852 0.0987 0.1247 0.0003  0.0653  -0.0362 100 PRO D N   
7343  C  CA  . PRO D  100 ? 0.1838 0.1138 0.1324 -0.0173 0.0684  -0.0362 100 PRO D CA  
7344  C  C   . PRO D  100 ? 0.1513 0.0901 0.1369 -0.0046 0.0621  -0.0342 100 PRO D C   
7345  O  O   . PRO D  100 ? 0.1809 0.1154 0.1638 -0.0181 0.0732  -0.0425 100 PRO D O   
7346  C  CB  . PRO D  100 ? 0.2334 0.1576 0.1535 -0.0126 0.0136  -0.0480 100 PRO D CB  
7347  C  CG  . PRO D  100 ? 0.2752 0.1254 0.1614 -0.0148 0.0439  -0.0292 100 PRO D CG  
7348  C  CD  . PRO D  100 ? 0.2655 0.1093 0.1416 -0.0081 0.0736  -0.0489 100 PRO D CD  
7349  N  N   . HIS D  101 ? 0.1289 0.0982 0.1400 0.0013  0.0449  -0.0228 101 HIS D N   
7350  C  CA  . HIS D  101 ? 0.1471 0.1307 0.1159 0.0165  0.0544  -0.0166 101 HIS D CA  
7351  C  C   . HIS D  101 ? 0.1055 0.1256 0.1259 -0.0157 0.0403  -0.0188 101 HIS D C   
7352  O  O   . HIS D  101 ? 0.1355 0.1481 0.1709 0.0043  0.0397  -0.0335 101 HIS D O   
7353  C  CB  . HIS D  101 ? 0.1723 0.1860 0.1364 0.0463  0.0599  0.0126  101 HIS D CB  
7354  C  CG  . HIS D  101 ? 0.1818 0.1888 0.2059 0.0318  0.0329  0.0089  101 HIS D CG  
7355  N  ND1 . HIS D  101 ? 0.2540 0.1826 0.3014 0.0190  0.0430  0.0181  101 HIS D ND1 
7356  C  CD2 . HIS D  101 ? 0.2283 0.1423 0.1989 0.0185  0.0670  -0.0035 101 HIS D CD2 
7357  C  CE1 . HIS D  101 ? 0.2940 0.1689 0.2867 0.0781  0.0362  0.0478  101 HIS D CE1 
7358  N  NE2 . HIS D  101 ? 0.2881 0.1448 0.2657 0.0511  0.0274  0.0098  101 HIS D NE2 
7359  N  N   . GLY D  102 ? 0.1215 0.1014 0.0987 -0.0020 0.0465  -0.0017 102 GLY D N   
7360  C  CA  . GLY D  102 ? 0.1335 0.0936 0.1093 -0.0074 0.0471  -0.0074 102 GLY D CA  
7361  C  C   . GLY D  102 ? 0.1155 0.0793 0.0915 0.0031  0.0288  -0.0104 102 GLY D C   
7362  O  O   . GLY D  102 ? 0.1380 0.0843 0.1070 -0.0028 0.0397  0.0028  102 GLY D O   
7363  N  N   . SER D  103 ? 0.1145 0.0879 0.0897 0.0068  0.0368  -0.0054 103 SER D N   
7364  C  CA  . SER D  103 ? 0.1149 0.0782 0.0874 -0.0038 0.0353  -0.0035 103 SER D CA  
7365  C  C   . SER D  103 ? 0.1098 0.0824 0.0882 0.0032  0.0318  -0.0073 103 SER D C   
7366  O  O   . SER D  103 ? 0.1111 0.1036 0.1165 0.0034  0.0344  -0.0271 103 SER D O   
7367  C  CB  . SER D  103 ? 0.1132 0.0737 0.1120 0.0097  0.0384  0.0177  103 SER D CB  
7368  O  OG  . SER D  103 ? 0.1188 0.0737 0.1115 0.0089  0.0295  0.0100  103 SER D OG  
7369  N  N   . GLU D  104 ? 0.1221 0.0681 0.0748 0.0017  0.0364  0.0046  104 GLU D N   
7370  C  CA  . GLU D  104 ? 0.1251 0.0662 0.0903 0.0070  0.0201  0.0017  104 GLU D CA  
7371  C  C   . GLU D  104 ? 0.1048 0.0725 0.0757 0.0046  0.0269  -0.0115 104 GLU D C   
7372  O  O   . GLU D  104 ? 0.1224 0.0768 0.0890 -0.0015 0.0264  0.0024  104 GLU D O   
7373  C  CB  . GLU D  104 ? 0.1398 0.0964 0.0806 0.0233  0.0261  0.0040  104 GLU D CB  
7374  C  CG  . GLU D  104 ? 0.1523 0.0771 0.0766 0.0230  0.0243  -0.0037 104 GLU D CG  
7375  C  CD  . GLU D  104 ? 0.1308 0.0838 0.0724 0.0027  0.0421  -0.0006 104 GLU D CD  
7376  O  OE1 . GLU D  104 ? 0.1254 0.0755 0.1006 -0.0068 0.0414  -0.0153 104 GLU D OE1 
7377  O  OE2 . GLU D  104 ? 0.1218 0.0890 0.1116 0.0038  0.0432  0.0057  104 GLU D OE2 
7378  N  N   . HIS D  105 ? 0.1114 0.0816 0.0836 0.0065  0.0359  0.0135  105 HIS D N   
7379  C  CA  . HIS D  105 ? 0.1211 0.0757 0.0857 0.0205  0.0406  0.0149  105 HIS D CA  
7380  C  C   . HIS D  105 ? 0.1418 0.0660 0.0895 0.0015  0.0262  0.0028  105 HIS D C   
7381  O  O   . HIS D  105 ? 0.1362 0.0757 0.1015 0.0147  0.0264  -0.0010 105 HIS D O   
7382  C  CB  . HIS D  105 ? 0.1365 0.0798 0.0970 0.0003  0.0425  0.0076  105 HIS D CB  
7383  C  CG  . HIS D  105 ? 0.1308 0.0854 0.0966 0.0164  0.0489  0.0132  105 HIS D CG  
7384  N  ND1 . HIS D  105 ? 0.1350 0.0894 0.0838 0.0062  0.0384  0.0034  105 HIS D ND1 
7385  C  CD2 . HIS D  105 ? 0.1543 0.0773 0.0892 0.0019  0.0533  -0.0071 105 HIS D CD2 
7386  C  CE1 . HIS D  105 ? 0.1495 0.1163 0.0818 -0.0015 0.0337  -0.0068 105 HIS D CE1 
7387  N  NE2 . HIS D  105 ? 0.1307 0.1096 0.1028 0.0066  0.0529  -0.0130 105 HIS D NE2 
7388  N  N   . THR D  106 ? 0.1319 0.0954 0.0958 0.0252  0.0276  0.0031  106 THR D N   
7389  C  CA  . THR D  106 ? 0.1392 0.0781 0.1247 0.0195  0.0445  0.0195  106 THR D CA  
7390  C  C   . THR D  106 ? 0.1373 0.0971 0.1176 0.0281  0.0104  0.0076  106 THR D C   
7391  O  O   . THR D  106 ? 0.1513 0.0945 0.1076 0.0105  0.0204  0.0019  106 THR D O   
7392  C  CB  . THR D  106 ? 0.1525 0.0940 0.1091 0.0275  0.0197  0.0024  106 THR D CB  
7393  O  OG1 . THR D  106 ? 0.1429 0.1107 0.1253 0.0120  0.0205  -0.0063 106 THR D OG1 
7394  C  CG2 . THR D  106 ? 0.1595 0.0827 0.1339 -0.0032 0.0635  0.0080  106 THR D CG2 
7395  N  N   . VAL D  107 ? 0.1453 0.0824 0.1177 0.0154  0.0265  0.0143  107 VAL D N   
7396  C  CA  . VAL D  107 ? 0.1581 0.0843 0.1407 0.0189  0.0113  0.0263  107 VAL D CA  
7397  C  C   . VAL D  107 ? 0.1759 0.0718 0.1475 0.0207  0.0098  0.0251  107 VAL D C   
7398  O  O   . VAL D  107 ? 0.1716 0.0876 0.1820 0.0405  0.0054  0.0000  107 VAL D O   
7399  C  CB  . VAL D  107 ? 0.1533 0.1032 0.1985 -0.0037 0.0227  0.0322  107 VAL D CB  
7400  C  CG1 . VAL D  107 ? 0.1887 0.1296 0.2301 0.0049  0.0535  0.0612  107 VAL D CG1 
7401  C  CG2 . VAL D  107 ? 0.1802 0.1377 0.1813 0.0294  0.0225  0.0428  107 VAL D CG2 
7402  N  N   . SER D  108 ? 0.1585 0.1066 0.1560 0.0300  0.0308  0.0384  108 SER D N   
7403  C  CA  . SER D  108 ? 0.1791 0.1206 0.1773 0.0305  0.0184  0.0362  108 SER D CA  
7404  C  C   . SER D  108 ? 0.1500 0.1091 0.1412 0.0342  0.0070  0.0052  108 SER D C   
7405  O  O   . SER D  108 ? 0.1808 0.1127 0.1809 0.0416  0.0119  -0.0102 108 SER D O   
7406  C  CB  . SER D  108 ? 0.1994 0.1216 0.2775 0.0570  0.0590  0.0617  108 SER D CB  
7407  O  OG  . SER D  108 ? 0.2238 0.1787 0.2504 0.0366  0.0390  0.0891  108 SER D OG  
7408  N  N   . GLY D  109 ? 0.1572 0.1136 0.1332 0.0166  0.0175  0.0229  109 GLY D N   
7409  C  CA  . GLY D  109 ? 0.1280 0.1579 0.1529 0.0178  0.0214  0.0154  109 GLY D CA  
7410  C  C   . GLY D  109 ? 0.1562 0.1879 0.1402 0.0335  0.0397  -0.0110 109 GLY D C   
7411  O  O   . GLY D  109 ? 0.1924 0.3517 0.1543 0.0099  0.0403  0.0171  109 GLY D O   
7412  N  N   A GLN D  110 ? 0.1556 0.1447 0.1506 0.0414  0.0104  -0.0119 110 GLN D N   
7413  N  N   B GLN D  110 ? 0.1554 0.1448 0.1529 0.0417  0.0115  -0.0110 110 GLN D N   
7414  C  CA  A GLN D  110 ? 0.1775 0.1328 0.1700 0.0441  -0.0132 -0.0153 110 GLN D CA  
7415  C  CA  B GLN D  110 ? 0.1807 0.1445 0.1687 0.0549  -0.0086 -0.0120 110 GLN D CA  
7416  C  C   A GLN D  110 ? 0.1356 0.1263 0.1463 0.0274  0.0212  0.0000  110 GLN D C   
7417  C  C   B GLN D  110 ? 0.1353 0.1263 0.1479 0.0271  0.0212  0.0024  110 GLN D C   
7418  O  O   A GLN D  110 ? 0.1492 0.0881 0.1374 0.0233  0.0357  -0.0049 110 GLN D O   
7419  O  O   B GLN D  110 ? 0.1492 0.0906 0.1339 0.0207  0.0342  -0.0010 110 GLN D O   
7420  C  CB  A GLN D  110 ? 0.2152 0.1111 0.2470 0.0406  -0.0254 -0.0230 110 GLN D CB  
7421  C  CB  B GLN D  110 ? 0.1353 0.1637 0.2441 0.0063  0.0273  0.0483  110 GLN D CB  
7422  C  CG  A GLN D  110 ? 0.2145 0.1215 0.3032 0.0658  0.0658  -0.0055 110 GLN D CG  
7423  C  CG  B GLN D  110 ? 0.2716 0.2592 0.3248 0.1255  -0.0177 -0.0412 110 GLN D CG  
7424  C  CD  A GLN D  110 ? 0.2228 0.1597 0.1786 0.0749  0.0498  0.0152  110 GLN D CD  
7425  C  CD  B GLN D  110 ? 0.2773 0.2488 0.3610 0.0615  0.0238  0.0969  110 GLN D CD  
7426  O  OE1 A GLN D  110 ? 0.2858 0.1956 0.1933 0.0577  0.0680  -0.0577 110 GLN D OE1 
7427  O  OE1 B GLN D  110 ? 0.4573 0.4702 0.4612 -0.0688 0.1062  0.1070  110 GLN D OE1 
7428  N  NE2 A GLN D  110 ? 0.2105 0.2096 0.2610 0.0118  0.0513  0.0978  110 GLN D NE2 
7429  N  NE2 B GLN D  110 ? 0.2755 0.5138 0.5304 0.0905  0.1387  -0.0210 110 GLN D NE2 
7430  N  N   . HIS D  111 ? 0.1455 0.1387 0.1298 0.0227  0.0289  -0.0088 111 HIS D N   
7431  C  CA  . HIS D  111 ? 0.1384 0.1080 0.1294 0.0062  0.0271  0.0119  111 HIS D CA  
7432  C  C   . HIS D  111 ? 0.1240 0.0926 0.1759 0.0263  0.0265  -0.0120 111 HIS D C   
7433  O  O   . HIS D  111 ? 0.1509 0.1145 0.2865 0.0476  0.0171  -0.0463 111 HIS D O   
7434  C  CB  . HIS D  111 ? 0.1518 0.1036 0.1482 -0.0109 0.0410  0.0038  111 HIS D CB  
7435  C  CG  . HIS D  111 ? 0.1365 0.1134 0.1203 0.0142  0.0384  -0.0035 111 HIS D CG  
7436  N  ND1 . HIS D  111 ? 0.1605 0.1222 0.1237 0.0299  0.0324  -0.0060 111 HIS D ND1 
7437  C  CD2 . HIS D  111 ? 0.1443 0.1107 0.1741 -0.0186 0.0381  -0.0259 111 HIS D CD2 
7438  C  CE1 . HIS D  111 ? 0.1452 0.1559 0.1414 0.0088  0.0390  -0.0131 111 HIS D CE1 
7439  N  NE2 . HIS D  111 ? 0.1683 0.1344 0.2114 -0.0127 0.0590  -0.0254 111 HIS D NE2 
7440  N  N   . PHE D  112 ? 0.1156 0.0802 0.1391 0.0156  0.0299  0.0071  112 PHE D N   
7441  C  CA  . PHE D  112 ? 0.1279 0.0811 0.1218 0.0071  0.0434  0.0133  112 PHE D CA  
7442  C  C   . PHE D  112 ? 0.1064 0.0608 0.1233 0.0111  0.0368  0.0048  112 PHE D C   
7443  O  O   . PHE D  112 ? 0.1233 0.0811 0.1238 0.0012  0.0432  0.0010  112 PHE D O   
7444  C  CB  . PHE D  112 ? 0.1531 0.0969 0.1434 0.0184  0.0454  0.0210  112 PHE D CB  
7445  C  CG  . PHE D  112 ? 0.1551 0.1377 0.1523 0.0566  0.0621  0.0478  112 PHE D CG  
7446  C  CD1 . PHE D  112 ? 0.2197 0.2594 0.1414 0.1099  0.0724  0.0566  112 PHE D CD1 
7447  C  CD2 . PHE D  112 ? 0.2197 0.1588 0.2574 -0.0167 0.0659  0.0828  112 PHE D CD2 
7448  C  CE1 . PHE D  112 ? 0.2594 0.2664 0.1763 0.1129  0.0745  0.0860  112 PHE D CE1 
7449  C  CE2 . PHE D  112 ? 0.2619 0.1917 0.3420 0.0144  0.1142  0.1372  112 PHE D CE2 
7450  C  CZ  . PHE D  112 ? 0.3077 0.2632 0.2463 0.0711  0.1146  0.1381  112 PHE D CZ  
7451  N  N   . ALA D  113 ? 0.1150 0.0674 0.1179 0.0114  0.0331  -0.0109 113 ALA D N   
7452  C  CA  . ALA D  113 ? 0.1141 0.0804 0.1249 0.0043  0.0337  -0.0093 113 ALA D CA  
7453  C  C   . ALA D  113 ? 0.1070 0.0730 0.0962 -0.0037 0.0406  -0.0104 113 ALA D C   
7454  O  O   . ALA D  113 ? 0.1254 0.0847 0.1010 -0.0048 0.0445  -0.0104 113 ALA D O   
7455  C  CB  . ALA D  113 ? 0.1611 0.1059 0.1337 -0.0054 0.0359  -0.0472 113 ALA D CB  
7456  N  N   . ALA D  114 ? 0.1146 0.0601 0.0915 0.0041  0.0476  -0.0115 114 ALA D N   
7457  C  CA  . ALA D  114 ? 0.1054 0.0671 0.0994 0.0161  0.0450  -0.0208 114 ALA D CA  
7458  C  C   . ALA D  114 ? 0.0971 0.0674 0.0908 0.0020  0.0394  -0.0068 114 ALA D C   
7459  O  O   . ALA D  114 ? 0.1035 0.0662 0.1001 0.0035  0.0386  -0.0070 114 ALA D O   
7460  C  CB  . ALA D  114 ? 0.1071 0.0845 0.1125 0.0076  0.0230  0.0097  114 ALA D CB  
7461  N  N   . GLU D  115 ? 0.0878 0.0672 0.0949 0.0076  0.0362  -0.0125 115 GLU D N   
7462  C  CA  . GLU D  115 ? 0.1001 0.0710 0.0967 0.0074  0.0505  -0.0073 115 GLU D CA  
7463  C  C   . GLU D  115 ? 0.1024 0.0451 0.0913 0.0019  0.0412  -0.0071 115 GLU D C   
7464  O  O   . GLU D  115 ? 0.1037 0.0745 0.1116 0.0003  0.0450  0.0136  115 GLU D O   
7465  C  CB  . GLU D  115 ? 0.1125 0.0834 0.0904 -0.0015 0.0472  -0.0115 115 GLU D CB  
7466  C  CG  . GLU D  115 ? 0.1089 0.0935 0.0859 0.0065  0.0428  -0.0023 115 GLU D CG  
7467  C  CD  . GLU D  115 ? 0.1094 0.0681 0.0917 -0.0013 0.0267  0.0077  115 GLU D CD  
7468  O  OE1 . GLU D  115 ? 0.1240 0.0998 0.0901 0.0068  0.0344  0.0087  115 GLU D OE1 
7469  O  OE2 . GLU D  115 ? 0.1278 0.1023 0.0936 0.0098  0.0368  0.0026  115 GLU D OE2 
7470  N  N   . LEU D  116 ? 0.0917 0.0658 0.0967 0.0131  0.0507  -0.0026 116 LEU D N   
7471  C  CA  . LEU D  116 ? 0.0885 0.0802 0.0942 0.0140  0.0438  0.0000  116 LEU D CA  
7472  C  C   . LEU D  116 ? 0.1045 0.0732 0.0870 0.0120  0.0553  0.0154  116 LEU D C   
7473  O  O   . LEU D  116 ? 0.1195 0.0693 0.1021 0.0093  0.0610  0.0137  116 LEU D O   
7474  C  CB  . LEU D  116 ? 0.1030 0.0755 0.1371 0.0043  0.0230  -0.0054 116 LEU D CB  
7475  C  CG  . LEU D  116 ? 0.0958 0.0780 0.1508 -0.0008 0.0294  -0.0065 116 LEU D CG  
7476  C  CD1 . LEU D  116 ? 0.1295 0.1036 0.1468 -0.0034 0.0344  0.0092  116 LEU D CD1 
7477  C  CD2 . LEU D  116 ? 0.1252 0.0944 0.2029 -0.0028 0.0417  0.0137  116 LEU D CD2 
7478  N  N   . HIS D  117 ? 0.0997 0.0520 0.0877 0.0096  0.0379  0.0049  117 HIS D N   
7479  C  CA  . HIS D  117 ? 0.1019 0.0776 0.0903 0.0034  0.0441  -0.0035 117 HIS D CA  
7480  C  C   . HIS D  117 ? 0.1049 0.0627 0.0705 0.0037  0.0450  0.0031  117 HIS D C   
7481  O  O   . HIS D  117 ? 0.1181 0.0899 0.0908 0.0136  0.0533  0.0078  117 HIS D O   
7482  C  CB  . HIS D  117 ? 0.1015 0.0671 0.1050 -0.0055 0.0401  -0.0024 117 HIS D CB  
7483  C  CG  . HIS D  117 ? 0.0935 0.0730 0.0888 0.0087  0.0463  -0.0027 117 HIS D CG  
7484  N  ND1 . HIS D  117 ? 0.1010 0.0956 0.0623 0.0040  0.0309  -0.0089 117 HIS D ND1 
7485  C  CD2 . HIS D  117 ? 0.1240 0.0811 0.0821 0.0082  0.0285  -0.0132 117 HIS D CD2 
7486  C  CE1 . HIS D  117 ? 0.1001 0.0915 0.0725 0.0015  0.0428  -0.0030 117 HIS D CE1 
7487  N  NE2 . HIS D  117 ? 0.1116 0.0918 0.0827 -0.0017 0.0285  0.0057  117 HIS D NE2 
7488  N  N   . ILE D  118 ? 0.1100 0.0807 0.0994 0.0140  0.0670  0.0118  118 ILE D N   
7489  C  CA  . ILE D  118 ? 0.1100 0.0851 0.1202 0.0248  0.0601  0.0204  118 ILE D CA  
7490  C  C   . ILE D  118 ? 0.1044 0.0834 0.0978 0.0239  0.0507  0.0245  118 ILE D C   
7491  O  O   . ILE D  118 ? 0.1437 0.0789 0.0974 0.0318  0.0597  0.0174  118 ILE D O   
7492  C  CB  . ILE D  118 ? 0.1206 0.0885 0.1263 0.0059  0.0656  0.0038  118 ILE D CB  
7493  C  CG1 . ILE D  118 ? 0.1301 0.0793 0.1626 -0.0068 0.0687  -0.0099 118 ILE D CG1 
7494  C  CG2 . ILE D  118 ? 0.1141 0.1274 0.1394 0.0127  0.0559  0.0028  118 ILE D CG2 
7495  C  CD1 . ILE D  118 ? 0.1477 0.1218 0.1942 -0.0310 0.0768  -0.0074 118 ILE D CD1 
7496  N  N   . VAL D  119 ? 0.1483 0.0739 0.0983 0.0297  0.0584  0.0114  119 VAL D N   
7497  C  CA  . VAL D  119 ? 0.1581 0.0705 0.0961 0.0204  0.0753  -0.0027 119 VAL D CA  
7498  C  C   . VAL D  119 ? 0.1540 0.0800 0.1030 0.0322  0.0702  0.0074  119 VAL D C   
7499  O  O   . VAL D  119 ? 0.1495 0.1071 0.1057 0.0428  0.0608  0.0108  119 VAL D O   
7500  C  CB  . VAL D  119 ? 0.1405 0.0886 0.1102 0.0208  0.0681  0.0171  119 VAL D CB  
7501  C  CG1 . VAL D  119 ? 0.1978 0.0721 0.1317 0.0048  0.0571  -0.0001 119 VAL D CG1 
7502  C  CG2 . VAL D  119 ? 0.1344 0.1091 0.1130 0.0027  0.0724  -0.0063 119 VAL D CG2 
7503  N  N   . HIS D  120 ? 0.1624 0.0797 0.0970 0.0262  0.0776  0.0098  120 HIS D N   
7504  C  CA  . HIS D  120 ? 0.1619 0.0938 0.1071 0.0293  0.0833  -0.0017 120 HIS D CA  
7505  C  C   . HIS D  120 ? 0.1568 0.1212 0.0961 0.0414  0.0794  0.0071  120 HIS D C   
7506  O  O   . HIS D  120 ? 0.1904 0.1086 0.1100 0.0513  0.0742  0.0065  120 HIS D O   
7507  C  CB  . HIS D  120 ? 0.1763 0.1106 0.1086 0.0390  0.0768  0.0151  120 HIS D CB  
7508  C  CG  . HIS D  120 ? 0.1698 0.0938 0.0947 0.0348  0.0732  0.0204  120 HIS D CG  
7509  N  ND1 . HIS D  120 ? 0.1946 0.0757 0.1412 0.0267  0.1026  0.0142  120 HIS D ND1 
7510  C  CD2 . HIS D  120 ? 0.1897 0.0782 0.1412 0.0173  0.0706  0.0163  120 HIS D CD2 
7511  C  CE1 . HIS D  120 ? 0.1344 0.1261 0.1269 0.0068  0.0738  0.0223  120 HIS D CE1 
7512  N  NE2 . HIS D  120 ? 0.1559 0.0989 0.1576 -0.0015 0.0711  0.0243  120 HIS D NE2 
7513  N  N   . TYR D  121 ? 0.1901 0.0953 0.1129 0.0463  0.0932  0.0137  121 TYR D N   
7514  C  CA  . TYR D  121 ? 0.2353 0.0737 0.1138 0.0439  0.1005  -0.0098 121 TYR D CA  
7515  C  C   . TYR D  121 ? 0.2059 0.0917 0.1028 0.0675  0.0794  0.0074  121 TYR D C   
7516  O  O   . TYR D  121 ? 0.1917 0.1149 0.1307 0.0610  0.0830  0.0291  121 TYR D O   
7517  C  CB  . TYR D  121 ? 0.1935 0.0834 0.1240 0.0276  0.0768  0.0132  121 TYR D CB  
7518  C  CG  . TYR D  121 ? 0.2106 0.1150 0.1012 0.0241  0.0866  0.0161  121 TYR D CG  
7519  C  CD1 . TYR D  121 ? 0.2522 0.0920 0.1208 0.0399  0.0529  0.0190  121 TYR D CD1 
7520  C  CD2 . TYR D  121 ? 0.2021 0.0965 0.1173 0.0395  0.0621  0.0203  121 TYR D CD2 
7521  C  CE1 . TYR D  121 ? 0.2090 0.1960 0.1784 -0.0028 0.0493  0.0771  121 TYR D CE1 
7522  C  CE2 . TYR D  121 ? 0.2093 0.1626 0.1834 0.0491  0.0841  0.0729  121 TYR D CE2 
7523  C  CZ  . TYR D  121 ? 0.2175 0.2205 0.1917 0.0269  0.0628  0.0833  121 TYR D CZ  
7524  O  OH  . TYR D  121 ? 0.2069 0.2863 0.3267 0.0522  0.0234  0.1488  121 TYR D OH  
7525  N  N   . ASN D  122 ? 0.2061 0.0909 0.1053 0.0529  0.0886  0.0094  122 ASN D N   
7526  C  CA  . ASN D  122 ? 0.2016 0.1127 0.1294 0.0617  0.1055  0.0030  122 ASN D CA  
7527  C  C   . ASN D  122 ? 0.1874 0.1158 0.1382 0.0511  0.1178  0.0240  122 ASN D C   
7528  O  O   . ASN D  122 ? 0.2624 0.0960 0.1423 0.0759  0.1027  0.0164  122 ASN D O   
7529  C  CB  . ASN D  122 ? 0.2132 0.1378 0.1115 0.0577  0.0621  0.0020  122 ASN D CB  
7530  C  CG  . ASN D  122 ? 0.2520 0.1435 0.1106 0.0688  0.0662  -0.0165 122 ASN D CG  
7531  O  OD1 . ASN D  122 ? 0.2800 0.1421 0.1242 0.0683  0.0993  0.0205  122 ASN D OD1 
7532  N  ND2 . ASN D  122 ? 0.2836 0.1703 0.1243 0.0895  0.0687  0.0097  122 ASN D ND2 
7533  N  N   . SER D  123 ? 0.1877 0.1373 0.1344 0.0649  0.1190  0.0205  123 SER D N   
7534  C  CA  . SER D  123 ? 0.1741 0.1562 0.2021 0.0489  0.0996  -0.0068 123 SER D CA  
7535  C  C   . SER D  123 ? 0.2208 0.1369 0.2037 0.0627  0.1254  0.0197  123 SER D C   
7536  O  O   . SER D  123 ? 0.2933 0.1468 0.2567 0.0892  0.1828  0.0392  123 SER D O   
7537  C  CB  . SER D  123 ? 0.2075 0.1392 0.2132 0.0483  0.1171  0.0340  123 SER D CB  
7538  O  OG  . SER D  123 ? 0.2770 0.1324 0.2109 0.0324  0.1289  0.0186  123 SER D OG  
7539  N  N   . ASP D  124 ? 0.2644 0.1721 0.1579 0.0760  0.1492  0.0198  124 ASP D N   
7540  C  CA  . ASP D  124 ? 0.2689 0.1578 0.1507 0.0198  0.1318  0.0041  124 ASP D CA  
7541  C  C   . ASP D  124 ? 0.2578 0.1328 0.1980 0.0681  0.1077  0.0236  124 ASP D C   
7542  O  O   . ASP D  124 ? 0.3127 0.1367 0.2998 0.0364  0.1773  -0.0266 124 ASP D O   
7543  C  CB  . ASP D  124 ? 0.2818 0.1473 0.1513 0.0040  0.1018  0.0000  124 ASP D CB  
7544  C  CG  . ASP D  124 ? 0.1748 0.2287 0.1802 -0.0173 0.0553  -0.0949 124 ASP D CG  
7545  O  OD1 . ASP D  124 ? 0.2062 0.2057 0.1365 0.0098  0.0856  -0.0214 124 ASP D OD1 
7546  O  OD2 . ASP D  124 ? 0.2504 0.1899 0.1991 0.0340  0.0807  -0.0080 124 ASP D OD2 
7547  N  N   . LEU D  125 ? 0.2522 0.1439 0.1220 0.0619  0.0926  0.0154  125 LEU D N   
7548  C  CA  . LEU D  125 ? 0.2908 0.1218 0.1263 0.0590  0.0504  0.0091  125 LEU D CA  
7549  C  C   . LEU D  125 ? 0.2678 0.1138 0.1272 0.0597  0.0441  -0.0089 125 LEU D C   
7550  O  O   . LEU D  125 ? 0.3133 0.1265 0.1538 0.0773  0.0524  -0.0174 125 LEU D O   
7551  C  CB  . LEU D  125 ? 0.2860 0.1597 0.1057 0.0811  0.0425  0.0171  125 LEU D CB  
7552  C  CG  . LEU D  125 ? 0.2930 0.1904 0.1437 -0.0048 0.0223  0.0114  125 LEU D CG  
7553  C  CD1 . LEU D  125 ? 0.3274 0.2003 0.2073 -0.0142 0.0140  0.0081  125 LEU D CD1 
7554  C  CD2 . LEU D  125 ? 0.3470 0.2822 0.1489 0.0173  0.0104  0.0630  125 LEU D CD2 
7555  N  N   . TYR D  126 ? 0.2235 0.1357 0.1163 0.0630  0.0507  0.0024  126 TYR D N   
7556  C  CA  . TYR D  126 ? 0.2370 0.1432 0.1111 0.0538  0.0485  0.0153  126 TYR D CA  
7557  C  C   . TYR D  126 ? 0.2572 0.1317 0.1405 0.0496  0.0520  -0.0044 126 TYR D C   
7558  O  O   . TYR D  126 ? 0.2346 0.1696 0.1272 0.0443  0.0414  0.0205  126 TYR D O   
7559  C  CB  . TYR D  126 ? 0.2321 0.1303 0.1259 0.0428  0.0480  0.0052  126 TYR D CB  
7560  C  CG  . TYR D  126 ? 0.2289 0.1411 0.0985 0.0546  0.0542  0.0003  126 TYR D CG  
7561  C  CD1 . TYR D  126 ? 0.2818 0.1468 0.1298 0.0573  0.0553  0.0024  126 TYR D CD1 
7562  C  CD2 . TYR D  126 ? 0.2287 0.1136 0.1053 0.0436  0.0204  0.0092  126 TYR D CD2 
7563  C  CE1 . TYR D  126 ? 0.2885 0.1062 0.1474 0.0403  0.0392  -0.0038 126 TYR D CE1 
7564  C  CE2 . TYR D  126 ? 0.2294 0.1303 0.0935 0.0176  0.0439  0.0000  126 TYR D CE2 
7565  C  CZ  . TYR D  126 ? 0.2759 0.1070 0.1190 0.0318  0.0189  -0.0037 126 TYR D CZ  
7566  O  OH  . TYR D  126 ? 0.2405 0.1339 0.1290 0.0337  0.0419  -0.0148 126 TYR D OH  
7567  N  N   . PRO D  127 ? 0.2318 0.1536 0.1633 0.0573  0.0048  0.0204  127 PRO D N   
7568  C  CA  . PRO D  127 ? 0.2222 0.2226 0.2108 0.0860  0.0267  0.0737  127 PRO D CA  
7569  C  C   . PRO D  127 ? 0.2581 0.2213 0.1793 -0.0060 0.0107  0.0913  127 PRO D C   
7570  O  O   . PRO D  127 ? 0.2982 0.3630 0.1633 -0.0308 0.0024  0.0688  127 PRO D O   
7571  C  CB  . PRO D  127 ? 0.2646 0.2490 0.2930 0.0663  0.0274  0.1437  127 PRO D CB  
7572  C  CG  . PRO D  127 ? 0.3373 0.1847 0.2547 0.0509  -0.0083 0.0869  127 PRO D CG  
7573  C  CD  . PRO D  127 ? 0.2870 0.1353 0.1912 0.0476  0.0478  0.0313  127 PRO D CD  
7574  N  N   . ASP D  128 ? 0.2689 0.1796 0.1263 -0.0017 0.0357  0.0480  128 ASP D N   
7575  C  CA  . ASP D  128 ? 0.2587 0.1738 0.1272 -0.0476 0.0162  0.0182  128 ASP D CA  
7576  C  C   . ASP D  128 ? 0.2761 0.1425 0.1045 -0.0340 0.0241  0.0199  128 ASP D C   
7577  O  O   . ASP D  128 ? 0.2565 0.1590 0.1100 -0.0206 0.0447  0.0065  128 ASP D O   
7578  C  CB  . ASP D  128 ? 0.2610 0.2662 0.1926 -0.0318 0.0060  0.1149  128 ASP D CB  
7579  C  CG  . ASP D  128 ? 0.2818 0.2078 0.1550 0.0174  -0.0006 0.0584  128 ASP D CG  
7580  O  OD1 . ASP D  128 ? 0.3257 0.2336 0.2245 0.0390  0.0178  -0.0252 128 ASP D OD1 
7581  O  OD2 . ASP D  128 ? 0.3077 0.1662 0.3962 0.0146  0.0612  -0.0612 128 ASP D OD2 
7582  N  N   . ALA D  129 ? 0.2721 0.1637 0.1156 -0.0419 0.0529  0.0103  129 ALA D N   
7583  C  CA  . ALA D  129 ? 0.2784 0.1199 0.1071 -0.0183 0.0590  -0.0225 129 ALA D CA  
7584  C  C   . ALA D  129 ? 0.2578 0.1360 0.0851 -0.0308 0.0540  -0.0003 129 ALA D C   
7585  O  O   . ALA D  129 ? 0.2946 0.1067 0.1322 -0.0006 0.0507  -0.0110 129 ALA D O   
7586  C  CB  . ALA D  129 ? 0.3959 0.1797 0.1141 -0.0815 0.0766  -0.0604 129 ALA D CB  
7587  N  N   A SER D  130 ? 0.2793 0.0983 0.1398 0.0094  0.0390  -0.0063 130 SER D N   
7588  N  N   B SER D  130 ? 0.2806 0.1595 0.0733 -0.0593 0.0597  0.0140  130 SER D N   
7589  C  CA  A SER D  130 ? 0.2856 0.1680 0.1286 -0.0255 0.0467  0.0214  130 SER D CA  
7590  C  CA  B SER D  130 ? 0.2741 0.1283 0.0789 -0.0559 0.0198  0.0071  130 SER D CA  
7591  C  C   A SER D  130 ? 0.2240 0.0965 0.1412 -0.0223 0.0406  0.0322  130 SER D C   
7592  C  C   B SER D  130 ? 0.2492 0.1030 0.1195 0.0076  0.0115  -0.0238 130 SER D C   
7593  O  O   A SER D  130 ? 0.2651 0.2276 0.1301 0.0208  0.0177  -0.0015 130 SER D O   
7594  O  O   B SER D  130 ? 0.2791 0.1032 0.1429 -0.0384 0.0161  -0.0005 130 SER D O   
7595  C  CB  A SER D  130 ? 0.3433 0.1098 0.1674 -0.0767 0.0863  0.0344  130 SER D CB  
7596  C  CB  B SER D  130 ? 0.2549 0.1800 0.0706 -0.0412 0.0046  0.0133  130 SER D CB  
7597  O  OG  A SER D  130 ? 0.5523 0.2154 0.1850 -0.0930 -0.0130 0.0210  130 SER D OG  
7598  O  OG  B SER D  130 ? 0.2626 0.1588 0.1730 -0.0452 0.0138  0.0746  130 SER D OG  
7599  N  N   . THR D  131 ? 0.2642 0.1039 0.1106 0.0001  0.0331  -0.0063 131 THR D N   
7600  C  CA  . THR D  131 ? 0.2933 0.1041 0.1161 0.0088  0.0197  -0.0007 131 THR D CA  
7601  C  C   . THR D  131 ? 0.2477 0.0922 0.1314 0.0153  0.0289  -0.0049 131 THR D C   
7602  O  O   . THR D  131 ? 0.2694 0.0976 0.1522 0.0284  0.0178  -0.0142 131 THR D O   
7603  C  CB  . THR D  131 ? 0.2759 0.1305 0.1322 0.0328  0.0026  -0.0153 131 THR D CB  
7604  O  OG1 . THR D  131 ? 0.3007 0.1226 0.1667 0.0242  0.0059  -0.0003 131 THR D OG1 
7605  C  CG2 . THR D  131 ? 0.3244 0.1450 0.1405 0.0504  0.0287  -0.0277 131 THR D CG2 
7606  N  N   . ALA D  132 ? 0.2398 0.1024 0.0910 0.0263  0.0355  0.0065  132 ALA D N   
7607  C  CA  . ALA D  132 ? 0.2608 0.0744 0.1140 0.0122  0.0307  0.0119  132 ALA D CA  
7608  C  C   . ALA D  132 ? 0.2648 0.1200 0.0917 0.0148  0.0417  -0.0121 132 ALA D C   
7609  O  O   . ALA D  132 ? 0.2628 0.1221 0.0906 0.0390  0.0516  -0.0076 132 ALA D O   
7610  C  CB  . ALA D  132 ? 0.2642 0.0926 0.0961 0.0233  0.0754  -0.0080 132 ALA D CB  
7611  N  N   . SER D  133 ? 0.2646 0.1234 0.0931 0.0346  0.0582  -0.0076 133 SER D N   
7612  C  CA  . SER D  133 ? 0.2439 0.1441 0.1039 0.0326  0.0537  0.0052  133 SER D CA  
7613  C  C   . SER D  133 ? 0.2325 0.1170 0.1010 0.0241  0.0687  0.0221  133 SER D C   
7614  O  O   . SER D  133 ? 0.2524 0.1268 0.1253 0.0344  0.0524  0.0188  133 SER D O   
7615  C  CB  . SER D  133 ? 0.3300 0.1651 0.1121 0.0172  0.0659  0.0399  133 SER D CB  
7616  O  OG  . SER D  133 ? 0.3686 0.2256 0.1186 0.0546  0.0666  0.0472  133 SER D OG  
7617  N  N   . ASN D  134 ? 0.2748 0.1185 0.1102 0.0175  0.0637  0.0131  134 ASN D N   
7618  C  CA  . ASN D  134 ? 0.2451 0.1253 0.1247 0.0218  0.0355  0.0423  134 ASN D CA  
7619  C  C   . ASN D  134 ? 0.2239 0.1186 0.1439 0.0225  0.0579  0.0342  134 ASN D C   
7620  O  O   . ASN D  134 ? 0.2809 0.1847 0.1633 -0.0557 0.0575  0.0007  134 ASN D O   
7621  C  CB  . ASN D  134 ? 0.3075 0.1167 0.1806 0.0003  0.0803  0.0322  134 ASN D CB  
7622  C  CG  . ASN D  134 ? 0.3188 0.1384 0.2154 0.0026  0.0833  0.0789  134 ASN D CG  
7623  O  OD1 . ASN D  134 ? 0.2804 0.1306 0.2073 0.0040  0.0542  0.0010  134 ASN D OD1 
7624  N  ND2 . ASN D  134 ? 0.2973 0.1305 0.2391 -0.0017 0.0467  0.0197  134 ASN D ND2 
7625  N  N   . LYS D  135 ? 0.2434 0.1021 0.1218 0.0313  0.0593  0.0160  135 LYS D N   
7626  C  CA  . LYS D  135 ? 0.2377 0.1552 0.0913 0.0269  0.0463  0.0195  135 LYS D CA  
7627  C  C   . LYS D  135 ? 0.2425 0.1371 0.0886 0.0259  0.0745  -0.0107 135 LYS D C   
7628  O  O   . LYS D  135 ? 0.2382 0.1304 0.1037 0.0366  0.0513  0.0027  135 LYS D O   
7629  C  CB  . LYS D  135 ? 0.2436 0.1538 0.1023 0.0324  0.0702  0.0031  135 LYS D CB  
7630  C  CG  . LYS D  135 ? 0.2655 0.1161 0.1576 0.0348  0.0421  -0.0052 135 LYS D CG  
7631  C  CD  . LYS D  135 ? 0.2660 0.1394 0.1809 0.0175  0.0024  -0.0185 135 LYS D CD  
7632  C  CE  . LYS D  135 ? 0.2973 0.1174 0.2018 0.0114  0.0055  0.0010  135 LYS D CE  
7633  N  NZ  . LYS D  135 ? 0.3156 0.1299 0.2053 0.0005  0.0175  -0.0066 135 LYS D NZ  
7634  N  N   A SER D  136 ? 0.1960 0.2427 0.0771 0.0313  0.0582  0.0071  136 SER D N   
7635  N  N   B SER D  136 ? 0.2721 0.0886 0.1006 0.0381  0.0388  0.0164  136 SER D N   
7636  C  CA  A SER D  136 ? 0.3109 0.1929 0.1734 -0.0109 0.0482  0.0252  136 SER D CA  
7637  C  CA  B SER D  136 ? 0.2777 0.1168 0.0892 0.0142  0.0450  0.0244  136 SER D CA  
7638  C  C   A SER D  136 ? 0.2639 0.1405 0.1263 0.0560  0.0282  0.0020  136 SER D C   
7639  C  C   B SER D  136 ? 0.2633 0.1249 0.0327 0.0397  0.0414  0.0032  136 SER D C   
7640  O  O   A SER D  136 ? 0.2134 0.1134 0.0658 0.0068  0.0350  -0.0179 136 SER D O   
7641  O  O   B SER D  136 ? 0.2449 0.1172 0.1240 0.0309  0.0438  0.0104  136 SER D O   
7642  C  CB  A SER D  136 ? 0.3594 0.2178 0.1393 -0.0126 0.0493  0.0452  136 SER D CB  
7643  C  CB  B SER D  136 ? 0.2088 0.1577 0.1003 -0.0198 0.0463  -0.0074 136 SER D CB  
7644  O  OG  A SER D  136 ? 0.2921 0.1994 0.1917 0.0109  0.0553  0.0513  136 SER D OG  
7645  O  OG  B SER D  136 ? 0.1712 0.2427 0.1745 -0.0368 0.0412  -0.0210 136 SER D OG  
7646  N  N   . GLU D  137 ? 0.3066 0.1145 0.0967 0.0362  0.0685  -0.0060 137 GLU D N   
7647  C  CA  . GLU D  137 ? 0.2847 0.1161 0.0899 0.0406  0.0595  0.0027  137 GLU D CA  
7648  C  C   . GLU D  137 ? 0.2499 0.0926 0.1213 0.0310  0.0579  -0.0155 137 GLU D C   
7649  O  O   . GLU D  137 ? 0.2490 0.1055 0.0864 0.0276  0.0537  0.0028  137 GLU D O   
7650  C  CB  . GLU D  137 ? 0.3395 0.0891 0.0872 0.0200  0.0560  0.0062  137 GLU D CB  
7651  C  CG  . GLU D  137 ? 0.4153 0.1923 0.0700 0.0687  0.0696  0.0026  137 GLU D CG  
7652  C  CD  . GLU D  137 ? 0.7427 0.2300 0.0962 0.2278  0.1190  0.0311  137 GLU D CD  
7653  O  OE1 . GLU D  137 ? 0.6200 0.2145 0.2985 0.1259  -0.0186 0.0277  137 GLU D OE1 
7654  O  OE2 . GLU D  137 ? 0.7707 0.5497 0.3447 0.4541  -0.0802 -0.0846 137 GLU D OE2 
7655  N  N   . GLY D  138 ? 0.2378 0.1105 0.0930 0.0458  0.0560  0.0027  138 GLY D N   
7656  C  CA  . GLY D  138 ? 0.2840 0.0961 0.0791 0.0364  0.0377  -0.0051 138 GLY D CA  
7657  C  C   . GLY D  138 ? 0.2041 0.0847 0.0901 0.0277  0.0392  0.0131  138 GLY D C   
7658  O  O   . GLY D  138 ? 0.1962 0.0949 0.0922 0.0357  0.0511  -0.0027 138 GLY D O   
7659  N  N   . LEU D  139 ? 0.2296 0.0886 0.0825 0.0430  0.0706  0.0078  139 LEU D N   
7660  C  CA  . LEU D  139 ? 0.2260 0.0895 0.0732 0.0207  0.0738  0.0120  139 LEU D CA  
7661  C  C   . LEU D  139 ? 0.1838 0.1001 0.0841 0.0230  0.0573  0.0034  139 LEU D C   
7662  O  O   . LEU D  139 ? 0.2070 0.1024 0.0881 0.0456  0.0637  0.0015  139 LEU D O   
7663  C  CB  . LEU D  139 ? 0.1966 0.0920 0.0992 0.0076  0.0864  -0.0065 139 LEU D CB  
7664  C  CG  . LEU D  139 ? 0.1933 0.1109 0.0870 0.0113  0.0538  0.0031  139 LEU D CG  
7665  C  CD1 . LEU D  139 ? 0.2187 0.1202 0.1082 0.0144  0.0685  -0.0010 139 LEU D CD1 
7666  C  CD2 . LEU D  139 ? 0.1914 0.1434 0.1249 0.0170  0.0280  0.0104  139 LEU D CD2 
7667  N  N   . ALA D  140 ? 0.1790 0.0909 0.1042 0.0357  0.0595  0.0063  140 ALA D N   
7668  C  CA  . ALA D  140 ? 0.2073 0.0825 0.0997 0.0399  0.0948  0.0080  140 ALA D CA  
7669  C  C   . ALA D  140 ? 0.1699 0.0667 0.1003 0.0329  0.0688  0.0165  140 ALA D C   
7670  O  O   . ALA D  140 ? 0.1680 0.1067 0.1199 0.0460  0.0662  0.0109  140 ALA D O   
7671  C  CB  . ALA D  140 ? 0.2511 0.1055 0.1335 0.0507  0.1212  0.0326  140 ALA D CB  
7672  N  N   . VAL D  141 ? 0.1606 0.0764 0.0883 0.0292  0.0667  0.0104  141 VAL D N   
7673  C  CA  . VAL D  141 ? 0.1520 0.0776 0.0760 0.0163  0.0656  0.0159  141 VAL D CA  
7674  C  C   . VAL D  141 ? 0.1552 0.0857 0.0918 0.0238  0.0705  0.0176  141 VAL D C   
7675  O  O   . VAL D  141 ? 0.1741 0.0922 0.0881 0.0278  0.0551  0.0163  141 VAL D O   
7676  C  CB  . VAL D  141 ? 0.1351 0.0873 0.1075 0.0055  0.0592  -0.0030 141 VAL D CB  
7677  C  CG1 . VAL D  141 ? 0.1475 0.1231 0.0969 -0.0003 0.0579  -0.0126 141 VAL D CG1 
7678  C  CG2 . VAL D  141 ? 0.1614 0.0948 0.1015 0.0017  0.0379  0.0038  141 VAL D CG2 
7679  N  N   . LEU D  142 ? 0.1436 0.0829 0.0958 0.0192  0.0679  0.0138  142 LEU D N   
7680  C  CA  . LEU D  142 ? 0.1247 0.0714 0.1071 0.0265  0.0621  0.0076  142 LEU D CA  
7681  C  C   . LEU D  142 ? 0.1351 0.0676 0.0952 0.0126  0.0593  0.0188  142 LEU D C   
7682  O  O   . LEU D  142 ? 0.1780 0.0921 0.0926 0.0368  0.0544  0.0089  142 LEU D O   
7683  C  CB  . LEU D  142 ? 0.1428 0.0922 0.1226 0.0155  0.0672  0.0236  142 LEU D CB  
7684  C  CG  . LEU D  142 ? 0.1572 0.0976 0.1477 0.0288  0.0732  0.0118  142 LEU D CG  
7685  C  CD1 . LEU D  142 ? 0.1669 0.1222 0.1759 0.0284  0.0562  0.0373  142 LEU D CD1 
7686  C  CD2 . LEU D  142 ? 0.2102 0.1739 0.1213 0.0799  0.1097  0.0662  142 LEU D CD2 
7687  N  N   . ALA D  143 ? 0.1285 0.0678 0.1123 0.0131  0.0617  0.0099  143 ALA D N   
7688  C  CA  . ALA D  143 ? 0.1213 0.0800 0.1028 0.0099  0.0627  0.0000  143 ALA D CA  
7689  C  C   . ALA D  143 ? 0.1217 0.0730 0.0922 0.0063  0.0661  0.0130  143 ALA D C   
7690  O  O   . ALA D  143 ? 0.1518 0.0694 0.1093 0.0144  0.0617  0.0203  143 ALA D O   
7691  C  CB  . ALA D  143 ? 0.1369 0.0964 0.1073 0.0096  0.0577  0.0211  143 ALA D CB  
7692  N  N   . VAL D  144 ? 0.1233 0.0660 0.1084 0.0151  0.0631  0.0008  144 VAL D N   
7693  C  CA  . VAL D  144 ? 0.1163 0.0739 0.1046 0.0010  0.0502  -0.0155 144 VAL D CA  
7694  C  C   . VAL D  144 ? 0.1303 0.0625 0.0900 0.0055  0.0498  0.0008  144 VAL D C   
7695  O  O   . VAL D  144 ? 0.1360 0.0615 0.1149 0.0100  0.0595  0.0107  144 VAL D O   
7696  C  CB  . VAL D  144 ? 0.1294 0.0807 0.1262 -0.0017 0.0577  0.0031  144 VAL D CB  
7697  C  CG1 . VAL D  144 ? 0.1420 0.0851 0.1581 -0.0092 0.0419  -0.0149 144 VAL D CG1 
7698  C  CG2 . VAL D  144 ? 0.1238 0.0825 0.1601 0.0171  0.0615  0.0006  144 VAL D CG2 
7699  N  N   . LEU D  145 ? 0.1168 0.0733 0.1050 0.0166  0.0483  0.0013  145 LEU D N   
7700  C  CA  . LEU D  145 ? 0.1091 0.0879 0.1202 0.0093  0.0505  -0.0204 145 LEU D CA  
7701  C  C   . LEU D  145 ? 0.1298 0.0631 0.1127 0.0076  0.0476  0.0031  145 LEU D C   
7702  O  O   . LEU D  145 ? 0.1357 0.0848 0.1349 -0.0266 0.0568  -0.0049 145 LEU D O   
7703  C  CB  . LEU D  145 ? 0.1355 0.0897 0.1407 0.0196  0.0255  -0.0080 145 LEU D CB  
7704  C  CG  . LEU D  145 ? 0.1773 0.1014 0.1423 0.0115  0.0175  -0.0034 145 LEU D CG  
7705  C  CD1 . LEU D  145 ? 0.1822 0.1683 0.1297 0.0441  0.0205  0.0065  145 LEU D CD1 
7706  C  CD2 . LEU D  145 ? 0.2027 0.1384 0.1703 0.0110  0.0043  0.0003  145 LEU D CD2 
7707  N  N   . ILE D  146 ? 0.1377 0.0762 0.0983 0.0048  0.0460  -0.0203 146 ILE D N   
7708  C  CA  . ILE D  146 ? 0.1046 0.0718 0.1215 -0.0035 0.0469  -0.0136 146 ILE D CA  
7709  C  C   . ILE D  146 ? 0.1161 0.0744 0.1064 -0.0066 0.0505  -0.0166 146 ILE D C   
7710  O  O   . ILE D  146 ? 0.1141 0.0845 0.1421 -0.0034 0.0537  -0.0173 146 ILE D O   
7711  C  CB  . ILE D  146 ? 0.1159 0.0851 0.1121 0.0023  0.0281  -0.0171 146 ILE D CB  
7712  C  CG1 . ILE D  146 ? 0.1199 0.0922 0.1468 0.0066  0.0410  0.0049  146 ILE D CG1 
7713  C  CG2 . ILE D  146 ? 0.1484 0.1040 0.1358 0.0034  0.0275  -0.0241 146 ILE D CG2 
7714  C  CD1 . ILE D  146 ? 0.1398 0.0920 0.1675 0.0130  0.0434  0.0078  146 ILE D CD1 
7715  N  N   A GLU D  147 ? 0.0917 0.0556 0.1177 0.0189  0.0251  -0.0086 147 GLU D N   
7716  N  N   B GLU D  147 ? 0.1190 0.0745 0.1046 -0.0097 0.0231  -0.0221 147 GLU D N   
7717  C  CA  A GLU D  147 ? 0.1403 0.0856 0.1409 0.0368  0.0155  -0.0403 147 GLU D CA  
7718  C  CA  B GLU D  147 ? 0.1340 0.0739 0.1190 -0.0175 0.0403  -0.0052 147 GLU D CA  
7719  C  C   A GLU D  147 ? 0.1220 0.0706 0.1251 0.0160  0.0405  -0.0155 147 GLU D C   
7720  C  C   B GLU D  147 ? 0.1234 0.0836 0.1240 0.0020  0.0417  -0.0115 147 GLU D C   
7721  O  O   A GLU D  147 ? 0.1118 0.0994 0.0908 0.0217  0.0370  -0.0087 147 GLU D O   
7722  O  O   B GLU D  147 ? 0.1322 0.1125 0.1316 -0.0071 0.0293  0.0115  147 GLU D O   
7723  C  CB  A GLU D  147 ? 0.1944 0.0915 0.2470 0.1052  -0.0364 -0.0355 147 GLU D CB  
7724  C  CB  B GLU D  147 ? 0.1571 0.1132 0.0904 0.0307  -0.0003 0.0135  147 GLU D CB  
7725  C  CG  A GLU D  147 ? 0.2802 0.1937 0.2400 0.0443  0.0309  0.0153  147 GLU D CG  
7726  C  CG  B GLU D  147 ? 0.1824 0.1186 0.1580 0.0377  0.0557  0.0186  147 GLU D CG  
7727  C  CD  A GLU D  147 ? 0.3183 0.3580 0.2407 0.1186  0.1685  0.1307  147 GLU D CD  
7728  C  CD  B GLU D  147 ? 0.2879 0.1111 0.2233 0.0331  0.0798  0.0548  147 GLU D CD  
7729  O  OE1 A GLU D  147 ? 0.4126 0.1477 0.2806 0.1404  0.1067  0.0992  147 GLU D OE1 
7730  O  OE1 B GLU D  147 ? 0.3328 0.1911 0.2612 0.0991  0.1207  0.0168  147 GLU D OE1 
7731  O  OE2 A GLU D  147 ? 0.4453 0.2502 0.2415 0.0980  -0.1279 -0.0480 147 GLU D OE2 
7732  O  OE2 B GLU D  147 ? 0.4190 0.1908 0.3294 0.1289  0.1683  0.0549  147 GLU D OE2 
7733  N  N   . MET D  148 ? 0.1308 0.0785 0.1225 0.0088  0.0430  -0.0024 148 MET D N   
7734  C  CA  . MET D  148 ? 0.1324 0.0847 0.1224 0.0137  0.0507  0.0034  148 MET D CA  
7735  C  C   . MET D  148 ? 0.1213 0.0791 0.1270 0.0337  0.0417  -0.0060 148 MET D C   
7736  O  O   . MET D  148 ? 0.1725 0.0753 0.1784 0.0256  0.0063  -0.0068 148 MET D O   
7737  C  CB  . MET D  148 ? 0.1471 0.1344 0.1299 0.0234  0.0579  -0.0126 148 MET D CB  
7738  C  CG  . MET D  148 ? 0.1942 0.1475 0.1283 0.0116  0.0776  0.0019  148 MET D CG  
7739  S  SD  . MET D  148 ? 0.2152 0.1401 0.1664 0.0073  0.0918  -0.0065 148 MET D SD  
7740  C  CE  . MET D  148 ? 0.2048 0.1544 0.2116 -0.0157 0.1035  -0.0281 148 MET D CE  
7741  N  N   . GLY D  149 ? 0.1231 0.0845 0.1322 0.0120  0.0379  0.0015  149 GLY D N   
7742  C  CA  . GLY D  149 ? 0.1289 0.0915 0.1323 -0.0116 0.0417  0.0046  149 GLY D CA  
7743  C  C   . GLY D  149 ? 0.1314 0.0597 0.1377 0.0192  0.0339  -0.0157 149 GLY D C   
7744  O  O   . GLY D  149 ? 0.1526 0.0838 0.1310 0.0121  0.0322  -0.0006 149 GLY D O   
7745  N  N   . SER D  150 ? 0.1143 0.0845 0.1657 0.0137  0.0243  -0.0019 150 SER D N   
7746  C  CA  . SER D  150 ? 0.1286 0.0723 0.1495 0.0071  0.0252  0.0054  150 SER D CA  
7747  C  C   . SER D  150 ? 0.1448 0.0737 0.1590 0.0108  0.0283  0.0059  150 SER D C   
7748  O  O   . SER D  150 ? 0.1685 0.0791 0.1814 0.0147  0.0185  0.0035  150 SER D O   
7749  C  CB  . SER D  150 ? 0.1326 0.0750 0.1924 -0.0051 0.0308  0.0163  150 SER D CB  
7750  O  OG  . SER D  150 ? 0.1554 0.0815 0.1836 0.0162  0.0351  0.0233  150 SER D OG  
7751  N  N   . PHE D  151 ? 0.1425 0.0751 0.1741 0.0103  0.0190  0.0098  151 PHE D N   
7752  C  CA  . PHE D  151 ? 0.1386 0.0744 0.1649 0.0168  0.0083  0.0046  151 PHE D CA  
7753  C  C   . PHE D  151 ? 0.1280 0.0662 0.1926 -0.0044 0.0160  0.0054  151 PHE D C   
7754  O  O   . PHE D  151 ? 0.1658 0.0723 0.2075 -0.0111 0.0294  0.0093  151 PHE D O   
7755  C  CB  . PHE D  151 ? 0.1580 0.0813 0.1881 0.0149  0.0060  -0.0008 151 PHE D CB  
7756  C  CG  . PHE D  151 ? 0.1562 0.1070 0.1841 0.0175  -0.0140 0.0062  151 PHE D CG  
7757  C  CD1 . PHE D  151 ? 0.1999 0.1062 0.1826 -0.0032 -0.0252 -0.0125 151 PHE D CD1 
7758  C  CD2 . PHE D  151 ? 0.1817 0.1218 0.2493 0.0333  -0.0388 0.0060  151 PHE D CD2 
7759  C  CE1 . PHE D  151 ? 0.2170 0.1360 0.1931 0.0063  -0.0504 -0.0019 151 PHE D CE1 
7760  C  CE2 . PHE D  151 ? 0.1809 0.1375 0.2266 0.0412  -0.0136 0.0046  151 PHE D CE2 
7761  C  CZ  . PHE D  151 ? 0.2434 0.1042 0.2138 0.0335  -0.0581 -0.0171 151 PHE D CZ  
7762  N  N   . ASN D  152 ? 0.1439 0.0621 0.1637 -0.0041 0.0197  0.0071  152 ASN D N   
7763  C  CA  . ASN D  152 ? 0.1197 0.1001 0.1973 0.0108  0.0384  -0.0261 152 ASN D CA  
7764  C  C   . ASN D  152 ? 0.1204 0.0962 0.1818 -0.0046 0.0357  -0.0066 152 ASN D C   
7765  O  O   . ASN D  152 ? 0.1283 0.0874 0.1994 -0.0035 0.0335  0.0127  152 ASN D O   
7766  C  CB  . ASN D  152 ? 0.1301 0.0957 0.1723 0.0049  0.0189  -0.0168 152 ASN D CB  
7767  C  CG  . ASN D  152 ? 0.1143 0.0960 0.1987 0.0010  0.0272  0.0054  152 ASN D CG  
7768  O  OD1 . ASN D  152 ? 0.1204 0.1094 0.2037 0.0163  0.0324  0.0126  152 ASN D OD1 
7769  N  ND2 . ASN D  152 ? 0.1367 0.0759 0.1930 -0.0078 0.0326  0.0041  152 ASN D ND2 
7770  N  N   A PRO D  153 ? 0.1028 0.0876 0.2382 -0.0040 0.0164  0.0430  153 PRO D N   
7771  N  N   B PRO D  153 ? 0.1150 0.0994 0.2422 -0.0135 0.0303  -0.0333 153 PRO D N   
7772  C  CA  A PRO D  153 ? 0.1137 0.1305 0.2346 0.0006  -0.0353 -0.0096 153 PRO D CA  
7773  C  CA  B PRO D  153 ? 0.1719 0.1268 0.2170 -0.0034 -0.0071 -0.0621 153 PRO D CA  
7774  C  C   A PRO D  153 ? 0.1028 0.0771 0.2684 -0.0427 0.0425  0.0252  153 PRO D C   
7775  C  C   B PRO D  153 ? 0.1459 0.1170 0.2552 0.0377  0.0038  -0.0331 153 PRO D C   
7776  O  O   A PRO D  153 ? 0.1331 0.1502 0.2538 0.0401  0.0000  0.0068  153 PRO D O   
7777  O  O   B PRO D  153 ? 0.2285 0.1080 0.2529 0.0010  0.0390  -0.0035 153 PRO D O   
7778  C  CB  A PRO D  153 ? 0.1330 0.0949 0.3641 -0.0020 -0.0729 0.0091  153 PRO D CB  
7779  C  CB  B PRO D  153 ? 0.2061 0.1676 0.3246 -0.0549 -0.0126 0.0087  153 PRO D CB  
7780  C  CG  A PRO D  153 ? 0.1184 0.0929 0.2770 -0.0113 0.0230  0.0186  153 PRO D CG  
7781  C  CG  B PRO D  153 ? 0.1599 0.2003 0.3953 -0.0253 -0.0041 0.0551  153 PRO D CG  
7782  C  CD  A PRO D  153 ? 0.1567 0.0921 0.3258 -0.0242 -0.0120 0.0109  153 PRO D CD  
7783  C  CD  B PRO D  153 ? 0.1374 0.1076 0.3041 -0.0237 0.0423  -0.0307 153 PRO D CD  
7784  N  N   . SER D  154 ? 0.1182 0.1324 0.2436 0.0052  0.0410  -0.0083 154 SER D N   
7785  C  CA  . SER D  154 ? 0.1480 0.1133 0.2565 0.0124  0.0575  0.0125  154 SER D CA  
7786  C  C   . SER D  154 ? 0.1312 0.0970 0.2436 0.0157  0.0114  -0.0010 154 SER D C   
7787  O  O   . SER D  154 ? 0.1420 0.1046 0.2590 0.0277  0.0305  -0.0168 154 SER D O   
7788  C  CB  . SER D  154 ? 0.1626 0.1576 0.2554 -0.0288 0.0626  0.0074  154 SER D CB  
7789  O  OG  . SER D  154 ? 0.1987 0.1933 0.3131 -0.0612 0.0750  0.0081  154 SER D OG  
7790  N  N   . TYR D  155 ? 0.1220 0.1114 0.2093 -0.0052 0.0230  -0.0068 155 TYR D N   
7791  C  CA  . TYR D  155 ? 0.1195 0.0908 0.1960 0.0046  0.0252  -0.0038 155 TYR D CA  
7792  C  C   . TYR D  155 ? 0.1156 0.0913 0.2188 0.0088  -0.0034 0.0115  155 TYR D C   
7793  O  O   . TYR D  155 ? 0.1538 0.0812 0.2296 -0.0027 0.0222  -0.0077 155 TYR D O   
7794  C  CB  . TYR D  155 ? 0.1050 0.0996 0.2113 0.0059  0.0272  -0.0250 155 TYR D CB  
7795  C  CG  . TYR D  155 ? 0.1290 0.0730 0.2050 0.0074  0.0318  -0.0167 155 TYR D CG  
7796  C  CD1 . TYR D  155 ? 0.1389 0.0662 0.2215 -0.0021 0.0348  -0.0054 155 TYR D CD1 
7797  C  CD2 . TYR D  155 ? 0.1188 0.0966 0.1985 -0.0030 0.0315  -0.0136 155 TYR D CD2 
7798  C  CE1 . TYR D  155 ? 0.1209 0.0918 0.2116 0.0104  0.0215  -0.0082 155 TYR D CE1 
7799  C  CE2 . TYR D  155 ? 0.1405 0.1032 0.1928 0.0060  0.0201  -0.0081 155 TYR D CE2 
7800  C  CZ  . TYR D  155 ? 0.1261 0.0843 0.1833 0.0077  0.0480  0.0006  155 TYR D CZ  
7801  O  OH  . TYR D  155 ? 0.1351 0.0940 0.1863 0.0185  0.0399  -0.0076 155 TYR D OH  
7802  N  N   . ASP D  156 ? 0.1233 0.1089 0.1980 0.0102  0.0170  -0.0162 156 ASP D N   
7803  C  CA  . ASP D  156 ? 0.1587 0.0897 0.2305 0.0122  0.0052  -0.0228 156 ASP D CA  
7804  C  C   . ASP D  156 ? 0.1495 0.0676 0.2363 0.0070  0.0311  -0.0087 156 ASP D C   
7805  O  O   . ASP D  156 ? 0.2009 0.0903 0.2229 0.0015  0.0074  0.0147  156 ASP D O   
7806  C  CB  . ASP D  156 ? 0.2373 0.1277 0.1926 0.0252  0.0229  -0.0148 156 ASP D CB  
7807  C  CG  . ASP D  156 ? 0.2623 0.1350 0.2034 0.0195  -0.0258 0.0074  156 ASP D CG  
7808  O  OD1 . ASP D  156 ? 0.2657 0.1168 0.1822 0.0584  -0.0258 0.0046  156 ASP D OD1 
7809  O  OD2 . ASP D  156 ? 0.2561 0.1965 0.2012 -0.0125 -0.0445 0.0132  156 ASP D OD2 
7810  N  N   . LYS D  157 ? 0.1353 0.1085 0.2292 0.0137  0.0122  0.0048  157 LYS D N   
7811  C  CA  . LYS D  157 ? 0.1711 0.0935 0.2608 0.0294  0.0310  -0.0021 157 LYS D CA  
7812  C  C   . LYS D  157 ? 0.1626 0.0994 0.3352 0.0179  0.0310  0.0322  157 LYS D C   
7813  O  O   . LYS D  157 ? 0.2599 0.1066 0.3646 0.0410  -0.0225 0.0303  157 LYS D O   
7814  C  CB  . LYS D  157 ? 0.1454 0.1307 0.3312 0.0239  0.0533  -0.0188 157 LYS D CB  
7815  C  CG  . LYS D  157 ? 0.1319 0.1526 0.3271 0.0208  0.0511  -0.0049 157 LYS D CG  
7816  C  CD  . LYS D  157 ? 0.1914 0.1629 0.3646 0.0237  0.0650  -0.0154 157 LYS D CD  
7817  C  CE  . LYS D  157 ? 0.1741 0.2021 0.3899 -0.0297 0.0454  0.0124  157 LYS D CE  
7818  N  NZ  . LYS D  157 ? 0.2581 0.2226 0.4113 -0.0211 0.0807  0.0315  157 LYS D NZ  
7819  N  N   . ILE D  158 ? 0.1913 0.0891 0.2199 0.0115  0.0185  -0.0136 158 ILE D N   
7820  C  CA  . ILE D  158 ? 0.2375 0.0869 0.1967 0.0046  0.0452  -0.0209 158 ILE D CA  
7821  C  C   . ILE D  158 ? 0.1572 0.0879 0.2039 0.0131  0.0162  -0.0104 158 ILE D C   
7822  O  O   . ILE D  158 ? 0.2127 0.0969 0.1890 0.0054  -0.0043 0.0044  158 ILE D O   
7823  C  CB  . ILE D  158 ? 0.3027 0.0895 0.1860 -0.0281 0.0538  -0.0256 158 ILE D CB  
7824  C  CG1 . ILE D  158 ? 0.3907 0.1457 0.2176 -0.0540 0.1114  -0.0680 158 ILE D CG1 
7825  C  CG2 . ILE D  158 ? 0.2935 0.1181 0.1671 -0.0516 0.0189  -0.0115 158 ILE D CG2 
7826  C  CD1 . ILE D  158 ? 0.4377 0.2088 0.1831 -0.1252 0.0885  -0.0776 158 ILE D CD1 
7827  N  N   . PHE D  159 ? 0.1692 0.0901 0.2111 0.0076  0.0259  -0.0161 159 PHE D N   
7828  C  CA  . PHE D  159 ? 0.1531 0.1055 0.2289 0.0153  0.0060  -0.0182 159 PHE D CA  
7829  C  C   . PHE D  159 ? 0.1642 0.1046 0.2181 -0.0182 0.0046  -0.0144 159 PHE D C   
7830  O  O   . PHE D  159 ? 0.1738 0.1504 0.2309 -0.0099 0.0178  -0.0163 159 PHE D O   
7831  C  CB  . PHE D  159 ? 0.1425 0.1036 0.2337 -0.0170 -0.0190 -0.0239 159 PHE D CB  
7832  C  CG  . PHE D  159 ? 0.1297 0.1156 0.1962 0.0059  0.0048  -0.0087 159 PHE D CG  
7833  C  CD1 . PHE D  159 ? 0.2030 0.1278 0.2255 -0.0260 -0.0443 -0.0200 159 PHE D CD1 
7834  C  CD2 . PHE D  159 ? 0.1378 0.1246 0.2287 0.0114  0.0362  -0.0013 159 PHE D CD2 
7835  C  CE1 . PHE D  159 ? 0.1709 0.1552 0.2082 -0.0394 -0.0259 0.0000  159 PHE D CE1 
7836  C  CE2 . PHE D  159 ? 0.1565 0.1443 0.2300 0.0010  0.0154  0.0119  159 PHE D CE2 
7837  C  CZ  . PHE D  159 ? 0.1421 0.1482 0.2542 -0.0008 0.0184  -0.0171 159 PHE D CZ  
7838  N  N   . SER D  160 ? 0.1659 0.1277 0.1897 -0.0026 -0.0030 -0.0337 160 SER D N   
7839  C  CA  . SER D  160 ? 0.1869 0.1351 0.1883 -0.0277 -0.0159 -0.0275 160 SER D CA  
7840  C  C   . SER D  160 ? 0.1720 0.1764 0.1868 -0.0099 -0.0063 -0.0098 160 SER D C   
7841  O  O   . SER D  160 ? 0.2285 0.1791 0.1850 -0.0173 -0.0243 0.0001  160 SER D O   
7842  C  CB  . SER D  160 ? 0.2046 0.1829 0.2640 -0.0419 -0.0103 -0.0469 160 SER D CB  
7843  O  OG  . SER D  160 ? 0.1974 0.1971 0.2339 -0.0195 -0.0060 -0.0527 160 SER D OG  
7844  N  N   . HIS D  161 ? 0.1416 0.1430 0.2005 -0.0219 -0.0113 -0.0085 161 HIS D N   
7845  C  CA  . HIS D  161 ? 0.2028 0.1159 0.2114 -0.0331 -0.0015 -0.0028 161 HIS D CA  
7846  C  C   . HIS D  161 ? 0.1622 0.1795 0.2028 -0.0351 -0.0452 0.0551  161 HIS D C   
7847  O  O   . HIS D  161 ? 0.1984 0.1673 0.2296 -0.0362 -0.0287 0.0331  161 HIS D O   
7848  C  CB  . HIS D  161 ? 0.1802 0.1410 0.1933 -0.0103 -0.0148 -0.0096 161 HIS D CB  
7849  C  CG  . HIS D  161 ? 0.1770 0.1570 0.1728 0.0155  0.0005  -0.0351 161 HIS D CG  
7850  N  ND1 . HIS D  161 ? 0.2143 0.1723 0.2011 0.0215  -0.0155 -0.0120 161 HIS D ND1 
7851  C  CD2 . HIS D  161 ? 0.1660 0.1335 0.2585 0.0035  0.0261  -0.0491 161 HIS D CD2 
7852  C  CE1 . HIS D  161 ? 0.2150 0.1624 0.2675 0.0092  0.0032  -0.0370 161 HIS D CE1 
7853  N  NE2 . HIS D  161 ? 0.1656 0.1541 0.2617 0.0073  0.0129  -0.0399 161 HIS D NE2 
7854  N  N   . LEU D  162 ? 0.1762 0.1719 0.2678 -0.0410 -0.0469 0.0362  162 LEU D N   
7855  C  CA  . LEU D  162 ? 0.1775 0.2822 0.2712 -0.0758 -0.0571 0.1207  162 LEU D CA  
7856  C  C   . LEU D  162 ? 0.1795 0.2030 0.2246 0.0000  -0.0060 0.0432  162 LEU D C   
7857  O  O   . LEU D  162 ? 0.1958 0.2554 0.3206 -0.0678 -0.0320 0.1194  162 LEU D O   
7858  C  CB  . LEU D  162 ? 0.1888 0.3407 0.3014 -0.0710 -0.0531 0.1343  162 LEU D CB  
7859  C  CG  . LEU D  162 ? 0.2156 0.3844 0.2913 -0.1370 -0.0877 0.1454  162 LEU D CG  
7860  C  CD1 . LEU D  162 ? 0.1525 0.7753 0.5952 -0.0236 -0.0815 0.3704  162 LEU D CD1 
7861  C  CD2 . LEU D  162 ? 0.3779 0.4559 0.3310 -0.1686 -0.1964 0.0983  162 LEU D CD2 
7862  N  N   . GLN D  163 ? 0.1744 0.2766 0.3003 0.0126  0.0135  -0.0263 163 GLN D N   
7863  C  CA  . GLN D  163 ? 0.1926 0.2926 0.3253 0.0097  0.0603  0.0253  163 GLN D CA  
7864  C  C   . GLN D  163 ? 0.2272 0.2933 0.2667 0.0194  -0.0115 0.0750  163 GLN D C   
7865  O  O   . GLN D  163 ? 0.3490 0.2727 0.3472 0.0469  0.1093  0.0907  163 GLN D O   
7866  C  CB  . GLN D  163 ? 0.3102 0.5293 0.4850 -0.1495 -0.1193 -0.0905 163 GLN D CB  
7867  C  CG  . GLN D  163 ? 0.5827 0.9490 0.7562 0.2223  -0.0617 -0.1495 163 GLN D CG  
7868  C  CD  . GLN D  163 ? 0.4005 0.2043 0.8219 0.0238  -0.0645 -0.1471 163 GLN D CD  
7869  O  OE1 . GLN D  163 ? 0.4133 0.3167 0.4529 0.0518  -0.1307 -0.1150 163 GLN D OE1 
7870  N  NE2 . GLN D  163 ? 0.3587 0.2233 0.4842 0.0287  -0.1513 0.0166  163 GLN D NE2 
7871  N  N   . HIS D  164 ? 0.1885 0.1917 0.2499 -0.0186 -0.0478 -0.0104 164 HIS D N   
7872  C  CA  . HIS D  164 ? 0.2249 0.2029 0.1797 -0.0238 -0.0262 0.0520  164 HIS D CA  
7873  C  C   . HIS D  164 ? 0.2141 0.1516 0.2073 -0.0118 -0.0157 0.0405  164 HIS D C   
7874  O  O   . HIS D  164 ? 0.2276 0.2075 0.2017 -0.0035 -0.0346 0.0412  164 HIS D O   
7875  C  CB  . HIS D  164 ? 0.1824 0.2587 0.2451 -0.0086 -0.0305 0.0133  164 HIS D CB  
7876  C  CG  . HIS D  164 ? 0.1723 0.3621 0.3036 -0.0342 -0.0480 -0.0204 164 HIS D CG  
7877  N  ND1 . HIS D  164 ? 0.2547 0.6049 0.3488 -0.0419 -0.0860 -0.0812 164 HIS D ND1 
7878  C  CD2 . HIS D  164 ? 0.3535 0.4972 0.5134 -0.1538 -0.2348 0.0568  164 HIS D CD2 
7879  C  CE1 . HIS D  164 ? 0.3296 0.7164 0.3181 -0.1360 -0.0978 -0.0936 164 HIS D CE1 
7880  N  NE2 . HIS D  164 ? 0.3244 0.7846 0.5699 -0.1905 -0.1896 -0.0313 164 HIS D NE2 
7881  N  N   . VAL D  165 ? 0.1745 0.1974 0.1571 -0.0364 -0.0188 0.0452  165 VAL D N   
7882  C  CA  . VAL D  165 ? 0.1755 0.2057 0.1703 -0.0562 -0.0119 0.0252  165 VAL D CA  
7883  C  C   . VAL D  165 ? 0.2169 0.1967 0.1590 -0.0763 -0.0408 0.0852  165 VAL D C   
7884  O  O   . VAL D  165 ? 0.1479 0.1978 0.1642 -0.0471 -0.0010 0.0599  165 VAL D O   
7885  C  CB  . VAL D  165 ? 0.2045 0.2398 0.1930 -0.0843 -0.0307 0.0348  165 VAL D CB  
7886  C  CG1 . VAL D  165 ? 0.1754 0.2545 0.2265 -0.0542 -0.0035 0.0076  165 VAL D CG1 
7887  C  CG2 . VAL D  165 ? 0.2201 0.2567 0.1879 -0.0681 -0.0266 0.1055  165 VAL D CG2 
7888  N  N   . LYS D  166 ? 0.1847 0.1597 0.1743 -0.0394 -0.0296 0.0234  166 LYS D N   
7889  C  CA  . LYS D  166 ? 0.2109 0.1576 0.1644 -0.0460 -0.0249 0.0285  166 LYS D CA  
7890  C  C   . LYS D  166 ? 0.1693 0.1411 0.1457 -0.0065 -0.0076 0.0292  166 LYS D C   
7891  O  O   . LYS D  166 ? 0.1601 0.1414 0.1624 -0.0197 0.0046  0.0366  166 LYS D O   
7892  C  CB  . LYS D  166 ? 0.2554 0.1630 0.1944 -0.0463 -0.0034 -0.0098 166 LYS D CB  
7893  C  CG  . LYS D  166 ? 0.3115 0.2118 0.1978 0.0037  -0.0074 0.0614  166 LYS D CG  
7894  C  CD  . LYS D  166 ? 0.5921 0.1847 0.1897 -0.0680 -0.0822 0.0116  166 LYS D CD  
7895  C  CE  . LYS D  166 ? 0.7498 0.3115 0.7457 -0.1712 -0.2732 0.0649  166 LYS D CE  
7896  N  NZ  . LYS D  166 ? 0.9032 0.6134 0.4185 0.1370  0.1609  0.1821  166 LYS D NZ  
7897  N  N   . TYR D  167 ? 0.1703 0.1270 0.1344 -0.0318 0.0104  0.0234  167 TYR D N   
7898  C  CA  . TYR D  167 ? 0.1723 0.1195 0.1071 -0.0262 0.0370  0.0076  167 TYR D CA  
7899  C  C   . TYR D  167 ? 0.1895 0.1292 0.1058 -0.0331 0.0283  0.0130  167 TYR D C   
7900  O  O   . TYR D  167 ? 0.1737 0.1430 0.1249 -0.0313 0.0370  0.0089  167 TYR D O   
7901  C  CB  . TYR D  167 ? 0.1989 0.1253 0.1115 -0.0141 0.0474  0.0087  167 TYR D CB  
7902  C  CG  . TYR D  167 ? 0.2321 0.1030 0.1313 -0.0249 0.0344  0.0186  167 TYR D CG  
7903  C  CD1 . TYR D  167 ? 0.2328 0.1249 0.1738 0.0093  0.0604  0.0291  167 TYR D CD1 
7904  C  CD2 . TYR D  167 ? 0.2980 0.1348 0.1116 -0.0013 0.0355  0.0186  167 TYR D CD2 
7905  C  CE1 . TYR D  167 ? 0.2741 0.1150 0.1852 0.0287  0.0564  0.0313  167 TYR D CE1 
7906  C  CE2 . TYR D  167 ? 0.2958 0.1659 0.1714 -0.0046 0.0230  -0.0098 167 TYR D CE2 
7907  C  CZ  . TYR D  167 ? 0.3113 0.2016 0.1438 0.0223  0.1005  -0.0074 167 TYR D CZ  
7908  O  OH  . TYR D  167 ? 0.4989 0.2694 0.1847 0.0969  0.1409  0.0082  167 TYR D OH  
7909  N  N   . LYS D  168 ? 0.1782 0.1808 0.1091 -0.0520 0.0231  -0.0019 168 LYS D N   
7910  C  CA  . LYS D  168 ? 0.2544 0.2445 0.1168 -0.0982 0.0368  -0.0175 168 LYS D CA  
7911  C  C   . LYS D  168 ? 0.2461 0.2278 0.1524 -0.1026 0.0641  -0.0588 168 LYS D C   
7912  O  O   . LYS D  168 ? 0.2178 0.1666 0.2048 -0.0149 0.0621  -0.0370 168 LYS D O   
7913  C  CB  . LYS D  168 ? 0.2114 0.2908 0.1365 -0.0720 0.0362  -0.0627 168 LYS D CB  
7914  C  CG  . LYS D  168 ? 0.2847 0.3400 0.1683 -0.1317 0.0746  -0.1259 168 LYS D CG  
7915  C  CD  . LYS D  168 ? 0.2587 0.3292 0.1702 -0.0535 -0.0107 -0.0712 168 LYS D CD  
7916  C  CE  . LYS D  168 ? 0.4289 0.6948 0.5207 -0.1515 0.0773  -0.4009 168 LYS D CE  
7917  N  NZ  . LYS D  168 ? 0.3546 0.6503 0.7236 -0.0894 -0.0043 -0.4853 168 LYS D NZ  
7918  N  N   . GLY D  169 ? 0.1975 0.3118 0.2057 -0.1092 0.0799  -0.0957 169 GLY D N   
7919  C  CA  . GLY D  169 ? 0.2287 0.3242 0.2973 -0.0826 0.1023  -0.1627 169 GLY D CA  
7920  C  C   . GLY D  169 ? 0.1875 0.2847 0.3612 -0.1036 0.0895  -0.1026 169 GLY D C   
7921  O  O   . GLY D  169 ? 0.2048 0.3208 0.3910 -0.0522 0.1089  -0.1066 169 GLY D O   
7922  N  N   . GLN D  170 ? 0.1854 0.2073 0.1639 -0.0498 0.0303  -0.0027 170 GLN D N   
7923  C  CA  . GLN D  170 ? 0.1942 0.1790 0.1457 -0.0283 0.0242  0.0283  170 GLN D CA  
7924  C  C   . GLN D  170 ? 0.1648 0.2337 0.1684 -0.0487 0.0082  0.0671  170 GLN D C   
7925  O  O   . GLN D  170 ? 0.1844 0.2804 0.1378 -0.0588 0.0081  0.0370  170 GLN D O   
7926  C  CB  . GLN D  170 ? 0.1905 0.1738 0.1708 -0.0182 0.0263  0.0644  170 GLN D CB  
7927  C  CG  . GLN D  170 ? 0.2157 0.1852 0.1799 0.0083  0.0593  0.0645  170 GLN D CG  
7928  C  CD  . GLN D  170 ? 0.2148 0.2188 0.1509 0.0315  0.0035  0.0582  170 GLN D CD  
7929  O  OE1 . GLN D  170 ? 0.2433 0.1841 0.1330 0.0074  -0.0170 0.0220  170 GLN D OE1 
7930  N  NE2 . GLN D  170 ? 0.3648 0.2285 0.1660 0.1220  0.0491  0.0737  170 GLN D NE2 
7931  N  N   . GLU D  171 ? 0.1344 0.2922 0.1930 -0.0107 0.0168  0.0813  171 GLU D N   
7932  C  CA  . GLU D  171 ? 0.1617 0.2330 0.2145 -0.0595 0.0057  0.0973  171 GLU D CA  
7933  C  C   . GLU D  171 ? 0.1480 0.3659 0.2109 -0.0722 -0.0225 0.0942  171 GLU D C   
7934  O  O   . GLU D  171 ? 0.2129 0.4551 0.1926 -0.0603 -0.0326 0.1533  171 GLU D O   
7935  C  CB  . GLU D  171 ? 0.1901 0.3377 0.3208 0.0006  0.1036  0.0675  171 GLU D CB  
7936  C  CG  . GLU D  171 ? 0.3007 0.2718 0.3914 -0.0215 0.1272  0.0089  171 GLU D CG  
7937  C  CD  . GLU D  171 ? 0.4451 0.3537 0.8032 -0.0370 0.2942  -0.0041 171 GLU D CD  
7938  O  OE1 . GLU D  171 ? 0.5332 0.3944 0.7401 0.0741  0.2392  0.3154  171 GLU D OE1 
7939  O  OE2 . GLU D  171 ? 0.7799 0.4356 0.7842 -0.0052 0.4404  -0.1387 171 GLU D OE2 
7940  N  N   . ALA D  172 ? 0.1608 0.3583 0.1606 -0.0595 -0.0048 0.0891  172 ALA D N   
7941  C  CA  . ALA D  172 ? 0.1558 0.3941 0.1517 -0.0750 -0.0081 0.0878  172 ALA D CA  
7942  C  C   . ALA D  172 ? 0.1540 0.2910 0.1263 -0.0496 -0.0038 0.0406  172 ALA D C   
7943  O  O   . ALA D  172 ? 0.1423 0.3946 0.1357 -0.0577 -0.0103 0.0635  172 ALA D O   
7944  C  CB  . ALA D  172 ? 0.1860 0.4397 0.1728 -0.1115 0.0220  0.0003  172 ALA D CB  
7945  N  N   . PHE D  173 ? 0.1844 0.3043 0.1480 -0.0975 -0.0094 0.0346  173 PHE D N   
7946  C  CA  . PHE D  173 ? 0.1401 0.2488 0.1764 -0.0623 -0.0068 0.0546  173 PHE D CA  
7947  C  C   . PHE D  173 ? 0.1599 0.2235 0.1872 -0.0610 0.0026  0.0126  173 PHE D C   
7948  O  O   . PHE D  173 ? 0.2813 0.3122 0.2057 -0.0720 -0.0005 -0.0487 173 PHE D O   
7949  C  CB  . PHE D  173 ? 0.1544 0.2896 0.2606 -0.0513 -0.0186 0.0568  173 PHE D CB  
7950  C  CG  . PHE D  173 ? 0.1694 0.2416 0.3878 -0.0302 -0.0307 0.0693  173 PHE D CG  
7951  C  CD1 . PHE D  173 ? 0.1843 0.2685 0.3594 0.0178  0.0269  0.0344  173 PHE D CD1 
7952  C  CD2 . PHE D  173 ? 0.3605 0.2969 0.5622 0.0916  0.0170  0.1342  173 PHE D CD2 
7953  C  CE1 . PHE D  173 ? 0.2483 0.3353 0.5419 0.0944  -0.0559 0.0087  173 PHE D CE1 
7954  C  CE2 . PHE D  173 ? 0.5350 0.3413 0.5225 0.1576  0.0656  0.1317  173 PHE D CE2 
7955  C  CZ  . PHE D  173 ? 0.3697 0.2890 0.5468 0.1272  0.0452  0.0113  173 PHE D CZ  
7956  N  N   . VAL D  174 ? 0.1592 0.1798 0.1863 -0.0397 0.0335  0.0154  174 VAL D N   
7957  C  CA  . VAL D  174 ? 0.1453 0.1721 0.2265 -0.0509 0.0120  -0.0226 174 VAL D CA  
7958  C  C   . VAL D  174 ? 0.1308 0.1700 0.2048 -0.0218 0.0232  -0.0239 174 VAL D C   
7959  O  O   . VAL D  174 ? 0.1500 0.1728 0.2161 -0.0292 0.0392  -0.0212 174 VAL D O   
7960  C  CB  . VAL D  174 ? 0.1050 0.1775 0.2658 -0.0026 0.0296  -0.0355 174 VAL D CB  
7961  C  CG1 . VAL D  174 ? 0.1768 0.1554 0.3379 -0.0206 0.0507  -0.0439 174 VAL D CG1 
7962  C  CG2 . VAL D  174 ? 0.1470 0.1967 0.2811 -0.0333 0.0469  -0.0265 174 VAL D CG2 
7963  N  N   . PRO D  175 ? 0.1324 0.1773 0.2089 -0.0153 0.0098  -0.0263 175 PRO D N   
7964  C  CA  . PRO D  175 ? 0.1335 0.1827 0.2023 -0.0329 0.0215  -0.0062 175 PRO D CA  
7965  C  C   . PRO D  175 ? 0.1404 0.1286 0.2186 -0.0043 0.0428  0.0085  175 PRO D C   
7966  O  O   . PRO D  175 ? 0.1574 0.1444 0.2249 0.0136  0.0456  0.0008  175 PRO D O   
7967  C  CB  . PRO D  175 ? 0.2061 0.1949 0.2316 -0.0436 0.0171  -0.0136 175 PRO D CB  
7968  C  CG  . PRO D  175 ? 0.1673 0.2996 0.2685 -0.0788 0.0421  -0.0220 175 PRO D CG  
7969  C  CD  . PRO D  175 ? 0.1640 0.2190 0.1973 -0.0344 0.0297  -0.0392 175 PRO D CD  
7970  N  N   . GLY D  176 ? 0.1493 0.1601 0.2021 -0.0059 0.0454  0.0166  176 GLY D N   
7971  C  CA  . GLY D  176 ? 0.1569 0.1179 0.2463 -0.0034 0.0553  0.0054  176 GLY D CA  
7972  C  C   . GLY D  176 ? 0.1186 0.1369 0.2439 -0.0027 0.0531  -0.0060 176 GLY D C   
7973  O  O   . GLY D  176 ? 0.1561 0.1702 0.2718 -0.0116 0.0386  -0.0125 176 GLY D O   
7974  N  N   . PHE D  177 ? 0.1405 0.1230 0.3134 0.0245  0.0307  0.0052  177 PHE D N   
7975  C  CA  . PHE D  177 ? 0.1364 0.1106 0.3458 0.0113  0.0195  -0.0108 177 PHE D CA  
7976  C  C   . PHE D  177 ? 0.1235 0.0938 0.3134 -0.0126 0.0395  0.0131  177 PHE D C   
7977  O  O   . PHE D  177 ? 0.1723 0.0996 0.2754 0.0000  0.0355  0.0164  177 PHE D O   
7978  C  CB  . PHE D  177 ? 0.1588 0.1333 0.3115 0.0105  0.0194  -0.0249 177 PHE D CB  
7979  C  CG  . PHE D  177 ? 0.1653 0.1457 0.2626 0.0377  0.0241  -0.0163 177 PHE D CG  
7980  C  CD1 . PHE D  177 ? 0.1495 0.1789 0.2387 0.0397  0.0579  -0.0359 177 PHE D CD1 
7981  C  CD2 . PHE D  177 ? 0.1784 0.1535 0.3598 0.0333  0.0322  -0.0003 177 PHE D CD2 
7982  C  CE1 . PHE D  177 ? 0.1341 0.1874 0.2662 0.0469  0.0573  -0.0231 177 PHE D CE1 
7983  C  CE2 . PHE D  177 ? 0.1599 0.1844 0.3018 0.0504  0.0617  -0.0103 177 PHE D CE2 
7984  C  CZ  . PHE D  177 ? 0.1452 0.1886 0.3578 0.0364  0.0597  0.0147  177 PHE D CZ  
7985  N  N   . ASN D  178 ? 0.1671 0.1277 0.4133 -0.0230 0.0198  0.0476  178 ASN D N   
7986  C  CA  . ASN D  178 ? 0.1221 0.1120 0.4293 -0.0076 0.0538  0.0456  178 ASN D CA  
7987  C  C   . ASN D  178 ? 0.1362 0.0976 0.3134 0.0085  0.0401  0.0540  178 ASN D C   
7988  O  O   . ASN D  178 ? 0.1457 0.1052 0.3142 0.0110  0.0428  0.0303  178 ASN D O   
7989  C  CB  . ASN D  178 ? 0.1647 0.1396 0.4590 -0.0175 0.0200  0.1159  178 ASN D CB  
7990  C  CG  . ASN D  178 ? 0.1457 0.1461 0.4676 -0.0270 0.0339  0.1093  178 ASN D CG  
7991  O  OD1 . ASN D  178 ? 0.1553 0.1544 0.4050 0.0049  0.0857  0.0863  178 ASN D OD1 
7992  N  ND2 . ASN D  178 ? 0.2899 0.1590 0.5016 -0.0483 0.0784  0.0864  178 ASN D ND2 
7993  N  N   . ILE D  179 ? 0.1292 0.1030 0.3066 -0.0068 0.0662  0.0322  179 ILE D N   
7994  C  CA  . ILE D  179 ? 0.1292 0.1177 0.2251 0.0024  0.0524  0.0284  179 ILE D CA  
7995  C  C   . ILE D  179 ? 0.1185 0.1382 0.2752 0.0153  0.0808  0.0454  179 ILE D C   
7996  O  O   . ILE D  179 ? 0.1310 0.1075 0.2531 0.0186  0.0509  0.0060  179 ILE D O   
7997  C  CB  . ILE D  179 ? 0.1457 0.0926 0.2355 -0.0082 0.0606  0.0248  179 ILE D CB  
7998  C  CG1 . ILE D  179 ? 0.1610 0.1195 0.2547 0.0006  0.0847  0.0368  179 ILE D CG1 
7999  C  CG2 . ILE D  179 ? 0.1142 0.1362 0.2856 -0.0130 0.0812  -0.0190 179 ILE D CG2 
8000  C  CD1 . ILE D  179 ? 0.1878 0.1062 0.2782 0.0205  0.0718  0.0261  179 ILE D CD1 
8001  N  N   A GLU D  180 ? 0.1308 0.1265 0.1901 0.0258  0.0705  -0.0193 180 GLU D N   
8002  N  N   B GLU D  180 ? 0.1734 0.0746 0.2883 -0.0040 0.0958  0.0392  180 GLU D N   
8003  C  CA  A GLU D  180 ? 0.1111 0.1430 0.2477 0.0353  0.0852  0.0116  180 GLU D CA  
8004  C  CA  B GLU D  180 ? 0.1304 0.1497 0.2685 0.0403  0.1081  0.0447  180 GLU D CA  
8005  C  C   A GLU D  180 ? 0.1586 0.0944 0.2463 0.0306  0.0852  0.0372  180 GLU D C   
8006  C  C   B GLU D  180 ? 0.1147 0.1152 0.2479 0.0000  0.1058  0.0366  180 GLU D C   
8007  O  O   A GLU D  180 ? 0.1416 0.0926 0.2341 0.0052  0.0947  0.0657  180 GLU D O   
8008  O  O   B GLU D  180 ? 0.1735 0.0909 0.2520 0.0193  0.0870  -0.0043 180 GLU D O   
8009  C  CB  A GLU D  180 ? 0.1308 0.1684 0.2736 0.0120  0.0901  0.0098  180 GLU D CB  
8010  C  CB  B GLU D  180 ? 0.1154 0.2075 0.2928 0.0417  0.0987  0.0776  180 GLU D CB  
8011  C  CG  A GLU D  180 ? 0.2136 0.2348 0.3267 0.1017  0.1398  0.0724  180 GLU D CG  
8012  C  CG  B GLU D  180 ? 0.1416 0.2057 0.2951 -0.0020 0.1102  0.0405  180 GLU D CG  
8013  C  CD  A GLU D  180 ? 0.2254 0.1391 0.3355 0.0675  0.1335  0.0083  180 GLU D CD  
8014  C  CD  B GLU D  180 ? 0.2450 0.1639 0.2985 -0.0974 0.1228  -0.0093 180 GLU D CD  
8015  O  OE1 A GLU D  180 ? 0.2073 0.1865 0.3249 0.0038  0.1208  0.0909  180 GLU D OE1 
8016  O  OE1 B GLU D  180 ? 0.3120 0.2263 0.2384 -0.0926 0.1371  -0.0668 180 GLU D OE1 
8017  O  OE2 A GLU D  180 ? 0.3100 0.3179 0.4781 0.0357  0.1068  0.1714  180 GLU D OE2 
8018  O  OE2 B GLU D  180 ? 0.2657 0.4676 0.5020 -0.0386 0.2542  0.0680  180 GLU D OE2 
8019  N  N   . GLU D  181 ? 0.1269 0.1000 0.2748 0.0060  0.0806  0.0333  181 GLU D N   
8020  C  CA  . GLU D  181 ? 0.1322 0.0863 0.2897 -0.0065 0.0723  0.0152  181 GLU D CA  
8021  C  C   . GLU D  181 ? 0.1238 0.0872 0.2468 0.0171  0.0504  0.0057  181 GLU D C   
8022  O  O   . GLU D  181 ? 0.1527 0.0961 0.2561 -0.0026 0.0666  -0.0107 181 GLU D O   
8023  C  CB  . GLU D  181 ? 0.1167 0.1732 0.3088 -0.0094 0.0593  -0.0152 181 GLU D CB  
8024  C  CG  . GLU D  181 ? 0.1226 0.1705 0.3562 -0.0192 0.0542  -0.0104 181 GLU D CG  
8025  C  CD  . GLU D  181 ? 0.1755 0.2324 0.4129 -0.0754 0.0350  -0.0313 181 GLU D CD  
8026  O  OE1 . GLU D  181 ? 0.1836 0.2734 0.4390 -0.0313 0.0538  -0.0189 181 GLU D OE1 
8027  O  OE2 . GLU D  181 ? 0.1865 0.1981 0.4557 -0.0500 0.0171  -0.0178 181 GLU D OE2 
8028  N  N   . LEU D  182 ? 0.1213 0.0854 0.2292 -0.0059 0.0668  0.0099  182 LEU D N   
8029  C  CA  . LEU D  182 ? 0.1138 0.0983 0.2348 -0.0148 0.0428  0.0210  182 LEU D CA  
8030  C  C   . LEU D  182 ? 0.1215 0.0824 0.1992 0.0153  0.0524  0.0000  182 LEU D C   
8031  O  O   . LEU D  182 ? 0.1168 0.1115 0.2030 0.0119  0.0496  -0.0052 182 LEU D O   
8032  C  CB  . LEU D  182 ? 0.1340 0.0894 0.2081 0.0083  0.0450  0.0203  182 LEU D CB  
8033  C  CG  . LEU D  182 ? 0.1102 0.0909 0.1948 -0.0006 0.0478  -0.0038 182 LEU D CG  
8034  C  CD1 . LEU D  182 ? 0.1405 0.0978 0.2522 -0.0038 0.0582  0.0328  182 LEU D CD1 
8035  C  CD2 . LEU D  182 ? 0.1384 0.1046 0.2096 0.0040  0.0280  0.0081  182 LEU D CD2 
8036  N  N   . LEU D  183 ? 0.1604 0.0861 0.2011 -0.0054 0.0637  0.0315  183 LEU D N   
8037  C  CA  . LEU D  183 ? 0.1641 0.0940 0.1921 0.0221  0.0644  0.0320  183 LEU D CA  
8038  C  C   . LEU D  183 ? 0.1317 0.1037 0.1832 -0.0209 0.0538  0.0122  183 LEU D C   
8039  O  O   . LEU D  183 ? 0.1443 0.1204 0.2244 -0.0108 0.0425  0.0017  183 LEU D O   
8040  C  CB  . LEU D  183 ? 0.1707 0.1277 0.2299 0.0210  0.0843  0.0251  183 LEU D CB  
8041  C  CG  . LEU D  183 ? 0.2081 0.1147 0.2000 0.0154  0.0662  0.0310  183 LEU D CG  
8042  C  CD1 . LEU D  183 ? 0.3140 0.1757 0.2224 0.0674  0.1513  0.0183  183 LEU D CD1 
8043  C  CD2 . LEU D  183 ? 0.2193 0.1305 0.2741 0.0127  0.0742  -0.0373 183 LEU D CD2 
8044  N  N   . PRO D  184 ? 0.1511 0.0886 0.1730 0.0096  0.0577  0.0236  184 PRO D N   
8045  C  CA  . PRO D  184 ? 0.1577 0.0895 0.2348 0.0037  0.0538  0.0048  184 PRO D CA  
8046  C  C   . PRO D  184 ? 0.2619 0.1000 0.2149 -0.0121 0.0943  -0.0098 184 PRO D C   
8047  O  O   . PRO D  184 ? 0.2152 0.1256 0.2560 -0.0220 0.0944  0.0252  184 PRO D O   
8048  C  CB  . PRO D  184 ? 0.1689 0.1398 0.1784 0.0161  0.0326  0.0060  184 PRO D CB  
8049  C  CG  . PRO D  184 ? 0.1824 0.1217 0.1728 0.0200  0.0293  0.0149  184 PRO D CG  
8050  C  CD  . PRO D  184 ? 0.1502 0.1107 0.1787 -0.0239 0.0590  0.0126  184 PRO D CD  
8051  N  N   . GLU D  185 ? 0.2030 0.1071 0.2291 0.0020  0.0531  0.0491  185 GLU D N   
8052  C  CA  . GLU D  185 ? 0.2321 0.1163 0.2518 0.0108  0.0515  0.0733  185 GLU D CA  
8053  C  C   . GLU D  185 ? 0.1887 0.1702 0.2163 -0.0186 0.0408  0.0480  185 GLU D C   
8054  O  O   . GLU D  185 ? 0.2172 0.1660 0.2526 -0.0381 0.0725  0.0456  185 GLU D O   
8055  C  CB  . GLU D  185 ? 0.3219 0.1269 0.2479 0.0165  0.0333  0.0060  185 GLU D CB  
8056  C  CG  . GLU D  185 ? 0.5257 0.1349 0.2196 -0.0216 0.0270  0.0326  185 GLU D CG  
8057  C  CD  . GLU D  185 ? 0.7605 0.3655 0.6220 0.1934  -0.0706 -0.2495 185 GLU D CD  
8058  O  OE1 . GLU D  185 ? 0.5480 0.3244 0.7760 0.1616  0.2198  0.1011  185 GLU D OE1 
8059  O  OE2 . GLU D  185 ? 1.0369 0.9111 0.5464 -0.1067 -0.1064 -0.2312 185 GLU D OE2 
8060  N  N   . ARG D  186 ? 0.2172 0.1075 0.2703 -0.0052 0.1063  0.0194  186 ARG D N   
8061  C  CA  . ARG D  186 ? 0.2041 0.1421 0.2485 -0.0020 0.0723  0.0668  186 ARG D CA  
8062  C  C   . ARG D  186 ? 0.2026 0.1155 0.2721 -0.0044 0.1032  0.0697  186 ARG D C   
8063  O  O   . ARG D  186 ? 0.1938 0.1419 0.2485 0.0135  0.0868  0.0190  186 ARG D O   
8064  C  CB  . ARG D  186 ? 0.2797 0.1263 0.3323 0.0175  0.0566  0.0646  186 ARG D CB  
8065  C  CG  . ARG D  186 ? 0.4207 0.1100 0.4296 0.0032  0.1048  0.0970  186 ARG D CG  
8066  C  CD  . ARG D  186 ? 0.4670 0.1924 0.3961 0.0653  0.0822  0.1328  186 ARG D CD  
8067  N  NE  . ARG D  186 ? 0.5985 0.1791 0.2800 -0.0222 0.0847  0.0612  186 ARG D NE  
8068  C  CZ  . ARG D  186 ? 0.7120 0.2136 0.3677 0.0684  0.1624  -0.0351 186 ARG D CZ  
8069  N  NH1 . ARG D  186 ? 0.9093 0.2655 0.4022 0.0074  -0.0612 0.0961  186 ARG D NH1 
8070  N  NH2 . ARG D  186 ? 0.6250 0.3700 0.6396 0.1465  0.1765  -0.0838 186 ARG D NH2 
8071  N  N   . THR D  187 ? 0.2037 0.1130 0.2404 0.0159  0.0947  0.0683  187 THR D N   
8072  C  CA  . THR D  187 ? 0.1671 0.1286 0.2312 0.0175  0.0944  0.0692  187 THR D CA  
8073  C  C   . THR D  187 ? 0.1714 0.1455 0.2181 0.0271  0.0684  0.0863  187 THR D C   
8074  O  O   . THR D  187 ? 0.1741 0.1719 0.1802 0.0126  0.0927  0.0489  187 THR D O   
8075  C  CB  . THR D  187 ? 0.1571 0.1444 0.2107 0.0102  0.0799  0.0628  187 THR D CB  
8076  O  OG1 . THR D  187 ? 0.1657 0.1750 0.2790 0.0311  0.0697  0.0795  187 THR D OG1 
8077  C  CG2 . THR D  187 ? 0.2048 0.1624 0.2345 0.0373  0.0617  0.0247  187 THR D CG2 
8078  N  N   . ALA D  188 ? 0.1621 0.1814 0.2169 0.0057  0.0983  0.0843  188 ALA D N   
8079  C  CA  . ALA D  188 ? 0.1815 0.2236 0.2109 0.0204  0.1058  0.1256  188 ALA D CA  
8080  C  C   . ALA D  188 ? 0.1572 0.1473 0.2026 0.0177  0.0987  0.0921  188 ALA D C   
8081  O  O   . ALA D  188 ? 0.1662 0.1709 0.2301 0.0245  0.0920  0.0680  188 ALA D O   
8082  C  CB  . ALA D  188 ? 0.2084 0.2730 0.2418 -0.0178 0.0960  0.1282  188 ALA D CB  
8083  N  N   A GLU D  189 ? 0.2087 0.1314 0.2061 0.0751  0.0767  0.0542  189 GLU D N   
8084  N  N   B GLU D  189 ? 0.1377 0.1260 0.2673 -0.0219 0.1251  0.0750  189 GLU D N   
8085  C  CA  A GLU D  189 ? 0.1809 0.1173 0.2170 0.0034  0.0750  0.0869  189 GLU D CA  
8086  C  CA  B GLU D  189 ? 0.1587 0.0800 0.1786 -0.0027 0.0828  0.0304  189 GLU D CA  
8087  C  C   A GLU D  189 ? 0.1317 0.0964 0.1635 0.0242  0.0746  0.0644  189 GLU D C   
8088  C  C   B GLU D  189 ? 0.1656 0.0579 0.1491 0.0114  0.0623  0.0329  189 GLU D C   
8089  O  O   A GLU D  189 ? 0.1714 0.0961 0.1935 0.0152  0.1199  0.0820  189 GLU D O   
8090  O  O   B GLU D  189 ? 0.1493 0.1407 0.1480 0.0060  0.0381  -0.0328 189 GLU D O   
8091  C  CB  A GLU D  189 ? 0.1863 0.0750 0.2077 -0.0291 -0.0027 0.0826  189 GLU D CB  
8092  C  CB  B GLU D  189 ? 0.2078 0.1001 0.1468 0.0573  0.0456  0.0458  189 GLU D CB  
8093  C  CG  A GLU D  189 ? 0.2174 0.1037 0.2910 -0.0507 0.0035  0.1009  189 GLU D CG  
8094  C  CG  B GLU D  189 ? 0.1888 0.1511 0.1999 0.0107  0.0445  0.0507  189 GLU D CG  
8095  C  CD  A GLU D  189 ? 0.2427 0.1443 0.3499 -0.0313 0.0887  0.1198  189 GLU D CD  
8096  C  CD  B GLU D  189 ? 0.2545 0.1646 0.3587 -0.0546 0.0795  -0.0031 189 GLU D CD  
8097  O  OE1 A GLU D  189 ? 0.2536 0.1814 0.2494 -0.0573 0.0586  0.0269  189 GLU D OE1 
8098  O  OE1 B GLU D  189 ? 0.2540 0.1486 0.5482 0.0293  0.1704  -0.0816 189 GLU D OE1 
8099  O  OE2 A GLU D  189 ? 0.2763 0.1475 0.4106 -0.0252 0.0357  0.0942  189 GLU D OE2 
8100  O  OE2 B GLU D  189 ? 0.3873 0.1678 0.2655 -0.0250 0.0697  0.0331  189 GLU D OE2 
8101  N  N   . TYR D  190 ? 0.1696 0.0978 0.1597 0.0076  0.0900  0.0280  190 TYR D N   
8102  C  CA  . TYR D  190 ? 0.1638 0.0856 0.1251 0.0178  0.0668  0.0384  190 TYR D CA  
8103  C  C   . TYR D  190 ? 0.1843 0.0782 0.1317 0.0366  0.0631  0.0344  190 TYR D C   
8104  O  O   . TYR D  190 ? 0.1915 0.1080 0.1351 0.0326  0.0812  0.0498  190 TYR D O   
8105  C  CB  . TYR D  190 ? 0.1799 0.1137 0.1335 0.0414  0.0878  0.0445  190 TYR D CB  
8106  C  CG  . TYR D  190 ? 0.1693 0.1062 0.1217 0.0344  0.0860  0.0476  190 TYR D CG  
8107  C  CD1 . TYR D  190 ? 0.1872 0.0904 0.1249 0.0229  0.0731  0.0156  190 TYR D CD1 
8108  C  CD2 . TYR D  190 ? 0.1822 0.1486 0.1346 0.0392  0.0850  0.0505  190 TYR D CD2 
8109  C  CE1 . TYR D  190 ? 0.2069 0.1152 0.1445 0.0359  0.1098  0.0480  190 TYR D CE1 
8110  C  CE2 . TYR D  190 ? 0.1836 0.1401 0.1317 0.0390  0.0917  0.0524  190 TYR D CE2 
8111  C  CZ  . TYR D  190 ? 0.2064 0.1301 0.1263 0.0529  0.0767  0.0419  190 TYR D CZ  
8112  O  OH  . TYR D  190 ? 0.2460 0.1604 0.1316 0.0769  0.1106  0.0516  190 TYR D OH  
8113  N  N   . TYR D  191 ? 0.1710 0.0854 0.1174 0.0233  0.0745  0.0333  191 TYR D N   
8114  C  CA  . TYR D  191 ? 0.1903 0.1018 0.1107 0.0274  0.0807  0.0195  191 TYR D CA  
8115  C  C   . TYR D  191 ? 0.1481 0.1071 0.0987 0.0320  0.0557  0.0324  191 TYR D C   
8116  O  O   . TYR D  191 ? 0.2023 0.1071 0.0895 0.0256  0.0496  0.0276  191 TYR D O   
8117  C  CB  . TYR D  191 ? 0.1709 0.1076 0.1112 0.0355  0.0665  0.0386  191 TYR D CB  
8118  C  CG  . TYR D  191 ? 0.1527 0.0945 0.1039 0.0038  0.0617  0.0318  191 TYR D CG  
8119  C  CD1 . TYR D  191 ? 0.1504 0.1001 0.1477 0.0199  0.0705  0.0463  191 TYR D CD1 
8120  C  CD2 . TYR D  191 ? 0.1601 0.0863 0.1156 0.0093  0.0617  0.0219  191 TYR D CD2 
8121  C  CE1 . TYR D  191 ? 0.1689 0.1109 0.1666 0.0247  0.0628  0.0299  191 TYR D CE1 
8122  C  CE2 . TYR D  191 ? 0.1535 0.0992 0.1574 0.0013  0.0750  0.0100  191 TYR D CE2 
8123  C  CZ  . TYR D  191 ? 0.1375 0.1132 0.1746 0.0238  0.0762  0.0234  191 TYR D CZ  
8124  O  OH  . TYR D  191 ? 0.1951 0.1513 0.2100 0.0482  0.0923  -0.0049 191 TYR D OH  
8125  N  N   . ARG D  192 ? 0.1981 0.0996 0.1030 0.0119  0.0623  0.0218  192 ARG D N   
8126  C  CA  . ARG D  192 ? 0.1987 0.1071 0.1008 0.0295  0.0505  0.0283  192 ARG D CA  
8127  C  C   . ARG D  192 ? 0.1942 0.1079 0.0917 0.0226  0.0439  0.0285  192 ARG D C   
8128  O  O   . ARG D  192 ? 0.1966 0.1154 0.1021 0.0218  0.0344  0.0167  192 ARG D O   
8129  C  CB  . ARG D  192 ? 0.1718 0.1551 0.1719 0.0562  0.0666  -0.0092 192 ARG D CB  
8130  C  CG  . ARG D  192 ? 0.2743 0.2387 0.2319 0.1171  0.0883  -0.0116 192 ARG D CG  
8131  C  CD  . ARG D  192 ? 0.3883 0.1692 0.1410 0.0160  0.0788  0.0635  192 ARG D CD  
8132  N  NE  . ARG D  192 ? 0.2940 0.1730 0.2361 0.1262  0.0236  -0.0035 192 ARG D NE  
8133  C  CZ  . ARG D  192 ? 0.3100 0.1741 0.1319 0.1502  0.0403  0.0003  192 ARG D CZ  
8134  N  NH1 . ARG D  192 ? 0.4115 0.2808 0.1438 0.2046  0.0935  0.0573  192 ARG D NH1 
8135  N  NH2 . ARG D  192 ? 0.2685 0.1782 0.1613 0.0802  0.0612  0.0397  192 ARG D NH2 
8136  N  N   . TYR D  193 ? 0.1981 0.1093 0.0915 0.0372  0.0741  0.0272  193 TYR D N   
8137  C  CA  . TYR D  193 ? 0.2081 0.1044 0.0958 0.0230  0.0297  0.0259  193 TYR D CA  
8138  C  C   . TYR D  193 ? 0.2021 0.1030 0.0895 0.0160  0.0346  0.0074  193 TYR D C   
8139  O  O   . TYR D  193 ? 0.2280 0.1106 0.0947 0.0513  0.0416  0.0132  193 TYR D O   
8140  C  CB  . TYR D  193 ? 0.1944 0.1252 0.0961 0.0154  0.0417  0.0335  193 TYR D CB  
8141  C  CG  . TYR D  193 ? 0.1612 0.0956 0.1125 0.0258  0.0331  0.0160  193 TYR D CG  
8142  C  CD1 . TYR D  193 ? 0.1741 0.0904 0.1161 0.0249  0.0452  0.0083  193 TYR D CD1 
8143  C  CD2 . TYR D  193 ? 0.1953 0.0974 0.1041 0.0129  0.0474  0.0197  193 TYR D CD2 
8144  C  CE1 . TYR D  193 ? 0.1571 0.0987 0.1089 0.0111  0.0509  0.0182  193 TYR D CE1 
8145  C  CE2 . TYR D  193 ? 0.1755 0.0915 0.0958 0.0331  0.0384  0.0071  193 TYR D CE2 
8146  C  CZ  . TYR D  193 ? 0.1583 0.0922 0.1094 0.0304  0.0582  0.0120  193 TYR D CZ  
8147  O  OH  . TYR D  193 ? 0.1513 0.1021 0.0940 0.0102  0.0465  0.0046  193 TYR D OH  
8148  N  N   A ARG D  194 ? 0.2676 0.1012 0.0992 0.0027  0.0353  0.0110  194 ARG D N   
8149  N  N   B ARG D  194 ? 0.2678 0.1012 0.0992 0.0027  0.0353  0.0110  194 ARG D N   
8150  C  CA  A ARG D  194 ? 0.3325 0.1009 0.1032 0.0026  0.0608  0.0127  194 ARG D CA  
8151  C  CA  B ARG D  194 ? 0.3328 0.1012 0.1021 0.0032  0.0623  0.0129  194 ARG D CA  
8152  C  C   A ARG D  194 ? 0.2235 0.1059 0.1010 0.0085  0.0161  0.0000  194 ARG D C   
8153  C  C   B ARG D  194 ? 0.2233 0.1061 0.1003 0.0087  0.0165  0.0000  194 ARG D C   
8154  O  O   A ARG D  194 ? 0.2728 0.1305 0.1296 0.0065  -0.0091 0.0337  194 ARG D O   
8155  O  O   B ARG D  194 ? 0.2730 0.1305 0.1295 0.0065  -0.0092 0.0339  194 ARG D O   
8156  C  CB  A ARG D  194 ? 0.4460 0.1777 0.0807 0.0020  0.0674  0.0007  194 ARG D CB  
8157  C  CB  B ARG D  194 ? 0.4492 0.1759 0.0843 0.0032  0.0641  0.0000  194 ARG D CB  
8158  C  CG  A ARG D  194 ? 0.7177 0.2242 0.1572 -0.1022 0.1688  -0.0485 194 ARG D CG  
8159  C  CG  B ARG D  194 ? 0.7056 0.2671 0.1741 -0.0438 0.2065  -0.0065 194 ARG D CG  
8160  C  CD  A ARG D  194 ? 0.6316 0.2949 0.3745 -0.0020 0.2193  -0.1351 194 ARG D CD  
8161  C  CD  B ARG D  194 ? 0.6700 0.4756 0.2640 -0.0773 0.1130  -0.0970 194 ARG D CD  
8162  N  NE  A ARG D  194 ? 0.7269 0.7175 0.4780 -0.1676 0.0590  -0.1561 194 ARG D NE  
8163  N  NE  B ARG D  194 ? 0.9272 0.5613 0.3161 -0.0864 -0.0803 0.0129  194 ARG D NE  
8164  C  CZ  A ARG D  194 ? 1.3394 1.2345 0.5169 0.3497  0.1173  -0.0834 194 ARG D CZ  
8165  C  CZ  B ARG D  194 ? 1.1898 1.4488 0.5324 0.4472  0.0676  0.0772  194 ARG D CZ  
8166  N  NH1 A ARG D  194 ? 1.0149 1.5003 0.5054 0.5619  0.2032  0.2039  194 ARG D NH1 
8167  N  NH1 B ARG D  194 ? 1.3860 1.4141 0.5548 0.4119  -0.0055 0.1737  194 ARG D NH1 
8168  N  NH2 A ARG D  194 ? 2.0641 1.8033 0.4781 0.2910  0.2861  0.5903  194 ARG D NH2 
8169  N  NH2 B ARG D  194 ? 1.2430 1.8607 0.7322 0.6807  0.2486  0.1015  194 ARG D NH2 
8170  N  N   . GLY D  195 ? 0.2239 0.1050 0.0764 0.0167  0.0339  0.0015  195 GLY D N   
8171  C  CA  . GLY D  195 ? 0.2183 0.0957 0.0901 0.0109  0.0498  0.0245  195 GLY D CA  
8172  C  C   . GLY D  195 ? 0.2190 0.0926 0.0786 0.0137  0.0331  -0.0194 195 GLY D C   
8173  O  O   . GLY D  195 ? 0.2116 0.1071 0.0797 0.0153  0.0538  0.0000  195 GLY D O   
8174  N  N   . SER D  196 ? 0.1669 0.0843 0.0913 0.0137  0.0408  -0.0076 196 SER D N   
8175  C  CA  . SER D  196 ? 0.1844 0.0772 0.0807 0.0088  0.0263  0.0031  196 SER D CA  
8176  C  C   . SER D  196 ? 0.1653 0.0782 0.0864 0.0230  0.0456  -0.0057 196 SER D C   
8177  O  O   . SER D  196 ? 0.1588 0.0860 0.0868 0.0140  0.0366  -0.0062 196 SER D O   
8178  C  CB  . SER D  196 ? 0.1694 0.1003 0.1001 0.0175  0.0395  -0.0200 196 SER D CB  
8179  O  OG  . SER D  196 ? 0.1829 0.0739 0.0970 0.0132  0.0390  -0.0108 196 SER D OG  
8180  N  N   A LEU D  197 ? 0.1650 0.0921 0.0807 0.0247  0.0292  0.0000  197 LEU D N   
8181  N  N   B LEU D  197 ? 0.1630 0.0908 0.0820 0.0229  0.0294  0.0000  197 LEU D N   
8182  C  CA  A LEU D  197 ? 0.1748 0.0854 0.0698 0.0237  0.0447  0.0015  197 LEU D CA  
8183  C  CA  B LEU D  197 ? 0.1739 0.0809 0.0710 0.0198  0.0439  0.0038  197 LEU D CA  
8184  C  C   A LEU D  197 ? 0.1400 0.0798 0.0790 0.0041  0.0215  -0.0104 197 LEU D C   
8185  C  C   B LEU D  197 ? 0.1407 0.0793 0.0791 0.0034  0.0203  -0.0099 197 LEU D C   
8186  O  O   A LEU D  197 ? 0.1631 0.0795 0.0785 0.0135  0.0329  -0.0043 197 LEU D O   
8187  O  O   B LEU D  197 ? 0.1628 0.0795 0.0782 0.0132  0.0326  -0.0043 197 LEU D O   
8188  C  CB  A LEU D  197 ? 0.1723 0.0872 0.0696 0.0416  0.0474  -0.0041 197 LEU D CB  
8189  C  CB  B LEU D  197 ? 0.1766 0.0818 0.1082 0.0194  0.0300  0.0098  197 LEU D CB  
8190  C  CG  A LEU D  197 ? 0.1843 0.1254 0.1312 0.0619  -0.0007 -0.0104 197 LEU D CG  
8191  C  CG  B LEU D  197 ? 0.2127 0.0657 0.1039 0.0317  0.0243  0.0131  197 LEU D CG  
8192  C  CD1 A LEU D  197 ? 0.1699 0.1032 0.1026 0.0507  0.0593  0.0271  197 LEU D CD1 
8193  C  CD1 B LEU D  197 ? 0.2111 0.0511 0.2412 0.0324  -0.0190 0.0252  197 LEU D CD1 
8194  C  CD2 A LEU D  197 ? 0.2439 0.2034 0.0807 0.0821  0.0308  -0.0172 197 LEU D CD2 
8195  C  CD2 B LEU D  197 ? 0.1978 0.0802 0.1922 0.0331  0.0511  0.0313  197 LEU D CD2 
8196  N  N   . THR D  198 ? 0.1374 0.0833 0.0834 0.0113  0.0313  -0.0153 198 THR D N   
8197  C  CA  . THR D  198 ? 0.1268 0.0687 0.0877 0.0015  0.0452  -0.0021 198 THR D CA  
8198  C  C   . THR D  198 ? 0.1360 0.0678 0.0866 -0.0049 0.0318  -0.0148 198 THR D C   
8199  O  O   . THR D  198 ? 0.1423 0.0730 0.0958 -0.0030 0.0377  0.0010  198 THR D O   
8200  C  CB  . THR D  198 ? 0.1365 0.0562 0.0890 0.0038  0.0285  -0.0015 198 THR D CB  
8201  O  OG1 . THR D  198 ? 0.1240 0.0725 0.0904 0.0035  0.0271  -0.0068 198 THR D OG1 
8202  C  CG2 . THR D  198 ? 0.1506 0.0800 0.0974 0.0137  0.0461  0.0166  198 THR D CG2 
8203  N  N   . THR D  199 ? 0.1693 0.0645 0.0865 0.0104  0.0125  -0.0163 199 THR D N   
8204  C  CA  . THR D  199 ? 0.2470 0.0623 0.0804 0.0198  0.0121  0.0043  199 THR D CA  
8205  C  C   . THR D  199 ? 0.1782 0.0728 0.0852 0.0013  0.0136  -0.0035 199 THR D C   
8206  O  O   . THR D  199 ? 0.1983 0.0881 0.0807 -0.0118 0.0322  -0.0182 199 THR D O   
8207  C  CB  . THR D  199 ? 0.2759 0.1666 0.0908 -0.0460 -0.0104 -0.0379 199 THR D CB  
8208  O  OG1 . THR D  199 ? 0.2675 0.2535 0.2289 0.0675  -0.0461 -0.0872 199 THR D OG1 
8209  C  CG2 . THR D  199 ? 0.3194 0.1028 0.1396 0.0077  -0.0395 -0.0253 199 THR D CG2 
8210  N  N   . PRO D  200 ? 0.1534 0.0719 0.0922 0.0059  0.0215  -0.0082 200 PRO D N   
8211  C  CA  . PRO D  200 ? 0.1529 0.0723 0.1068 0.0008  0.0287  -0.0131 200 PRO D CA  
8212  C  C   . PRO D  200 ? 0.1471 0.0755 0.1084 0.0013  0.0337  0.0021  200 PRO D C   
8213  O  O   . PRO D  200 ? 0.1680 0.1143 0.1260 0.0066  0.0060  0.0001  200 PRO D O   
8214  C  CB  . PRO D  200 ? 0.1599 0.0906 0.1080 -0.0038 0.0526  -0.0111 200 PRO D CB  
8215  C  CG  . PRO D  200 ? 0.1628 0.1156 0.1066 0.0062  0.0390  -0.0200 200 PRO D CG  
8216  C  CD  . PRO D  200 ? 0.1567 0.1014 0.0879 0.0130  0.0302  -0.0044 200 PRO D CD  
8217  N  N   A PRO D  201 ? 0.1671 0.0660 0.1133 0.0024  0.0454  0.0021  201 PRO D N   
8218  N  N   B PRO D  201 ? 0.1683 0.0764 0.1177 0.0110  0.0421  -0.0006 201 PRO D N   
8219  C  CA  A PRO D  201 ? 0.1752 0.0754 0.0885 0.0103  0.0566  -0.0165 201 PRO D CA  
8220  C  CA  B PRO D  201 ? 0.1741 0.0872 0.1024 0.0021  0.0527  -0.0093 201 PRO D CA  
8221  C  C   A PRO D  201 ? 0.1854 0.0850 0.0766 -0.0115 0.0520  -0.0204 201 PRO D C   
8222  C  C   B PRO D  201 ? 0.1868 0.0854 0.0897 -0.0097 0.0538  -0.0221 201 PRO D C   
8223  O  O   A PRO D  201 ? 0.1978 0.0904 0.1075 -0.0182 0.0395  -0.0339 201 PRO D O   
8224  O  O   B PRO D  201 ? 0.2017 0.0839 0.1089 -0.0179 0.0491  -0.0274 201 PRO D O   
8225  C  CB  A PRO D  201 ? 0.1976 0.0721 0.1590 0.0163  0.0496  -0.0432 201 PRO D CB  
8226  C  CB  B PRO D  201 ? 0.2202 0.0834 0.1383 0.0193  0.0627  -0.0107 201 PRO D CB  
8227  C  CG  A PRO D  201 ? 0.2585 0.1233 0.1161 0.0910  0.0392  -0.0559 201 PRO D CG  
8228  C  CG  B PRO D  201 ? 0.2027 0.2077 0.1717 0.0671  0.0220  -0.0531 201 PRO D CG  
8229  C  CD  A PRO D  201 ? 0.1657 0.1082 0.1717 0.0157  0.0627  -0.0013 201 PRO D CD  
8230  C  CD  B PRO D  201 ? 0.1651 0.0960 0.1861 0.0220  0.0258  -0.0055 201 PRO D CD  
8231  N  N   . CYS D  202 ? 0.1523 0.0755 0.0929 -0.0012 0.0388  -0.0082 202 CYS D N   
8232  C  CA  . CYS D  202 ? 0.1631 0.0966 0.0734 0.0093  0.0337  -0.0065 202 CYS D CA  
8233  C  C   . CYS D  202 ? 0.1854 0.0719 0.0776 0.0043  0.0254  -0.0137 202 CYS D C   
8234  O  O   . CYS D  202 ? 0.1969 0.0996 0.0838 0.0013  0.0285  -0.0200 202 CYS D O   
8235  C  CB  . CYS D  202 ? 0.1678 0.1012 0.0957 0.0035  0.0348  -0.0078 202 CYS D CB  
8236  S  SG  . CYS D  202 ? 0.1714 0.0958 0.0897 0.0015  0.0370  -0.0161 202 CYS D SG  
8237  N  N   A ASN D  203 ? 0.1844 0.0845 0.0818 -0.0052 0.0540  -0.0196 203 ASN D N   
8238  N  N   B ASN D  203 ? 0.2018 0.0938 0.1066 0.0098  0.0518  -0.0410 203 ASN D N   
8239  C  CA  A ASN D  203 ? 0.1786 0.0614 0.0732 0.0182  0.0416  -0.0078 203 ASN D CA  
8240  C  CA  B ASN D  203 ? 0.2748 0.1213 0.1019 0.0315  0.0697  -0.0239 203 ASN D CA  
8241  C  C   A ASN D  203 ? 0.1859 0.0768 0.0864 0.0000  0.0582  -0.0136 203 ASN D C   
8242  C  C   B ASN D  203 ? 0.1938 0.1030 0.0802 0.0017  0.0627  -0.0456 203 ASN D C   
8243  O  O   A ASN D  203 ? 0.1459 0.0759 0.0797 0.0361  0.0584  -0.0146 203 ASN D O   
8244  O  O   B ASN D  203 ? 0.1274 0.0763 0.0843 0.0197  0.0348  -0.0109 203 ASN D O   
8245  C  CB  A ASN D  203 ? 0.1659 0.0328 0.1044 -0.0012 0.0445  0.0051  203 ASN D CB  
8246  C  CB  B ASN D  203 ? 0.2359 0.1547 0.1082 0.0063  0.1011  -0.0450 203 ASN D CB  
8247  C  CG  A ASN D  203 ? 0.1456 0.0596 0.0825 -0.0006 0.0555  0.0081  203 ASN D CG  
8248  C  CG  B ASN D  203 ? 0.2640 0.1883 0.1923 -0.0020 0.0593  -0.0219 203 ASN D CG  
8249  O  OD1 A ASN D  203 ? 0.2114 0.0676 0.0818 0.0179  0.0392  0.0030  203 ASN D OD1 
8250  O  OD1 B ASN D  203 ? 0.2343 0.1260 0.2833 0.0299  0.0608  0.0546  203 ASN D OD1 
8251  N  ND2 A ASN D  203 ? 0.2809 0.0493 0.1141 0.0100  0.1080  -0.0190 203 ASN D ND2 
8252  N  ND2 B ASN D  203 ? 0.2928 0.2583 0.1844 0.0436  0.0816  -0.0270 203 ASN D ND2 
8253  N  N   . PRO D  204 ? 0.2129 0.0974 0.0903 0.0046  0.0377  -0.0140 204 PRO D N   
8254  C  CA  . PRO D  204 ? 0.1926 0.0997 0.1067 0.0102  0.0361  0.0015  204 PRO D CA  
8255  C  C   . PRO D  204 ? 0.2012 0.1009 0.0888 0.0153  0.0653  0.0027  204 PRO D C   
8256  O  O   . PRO D  204 ? 0.2361 0.1886 0.0901 0.0361  0.0588  0.0068  204 PRO D O   
8257  C  CB  . PRO D  204 ? 0.2485 0.1360 0.0987 -0.0362 0.0086  -0.0149 204 PRO D CB  
8258  C  CG  . PRO D  204 ? 0.2702 0.1423 0.1159 -0.0306 0.0288  -0.0085 204 PRO D CG  
8259  C  CD  . PRO D  204 ? 0.2500 0.1136 0.1075 -0.0181 0.0296  -0.0386 204 PRO D CD  
8260  N  N   . THR D  205 ? 0.1777 0.1066 0.0949 0.0390  0.0452  -0.0065 205 THR D N   
8261  C  CA  . THR D  205 ? 0.1881 0.0848 0.1221 0.0256  0.0351  -0.0074 205 THR D CA  
8262  C  C   . THR D  205 ? 0.2063 0.0908 0.0728 0.0280  0.0621  0.0054  205 THR D C   
8263  O  O   . THR D  205 ? 0.2003 0.1061 0.1027 0.0267  0.0615  -0.0060 205 THR D O   
8264  C  CB  . THR D  205 ? 0.2045 0.1109 0.0882 0.0261  0.0489  0.0096  205 THR D CB  
8265  O  OG1 . THR D  205 ? 0.2336 0.1042 0.0965 0.0259  0.0529  -0.0013 205 THR D OG1 
8266  C  CG2 . THR D  205 ? 0.2592 0.0843 0.1125 0.0284  0.0276  -0.0242 205 THR D CG2 
8267  N  N   . VAL D  206 ? 0.2104 0.0745 0.0973 0.0144  0.0454  -0.0086 206 VAL D N   
8268  C  CA  . VAL D  206 ? 0.1883 0.0935 0.0771 0.0241  0.0516  0.0143  206 VAL D CA  
8269  C  C   . VAL D  206 ? 0.2168 0.1009 0.0895 0.0419  0.0472  -0.0007 206 VAL D C   
8270  O  O   . VAL D  206 ? 0.2208 0.1001 0.1115 0.0195  0.0211  0.0156  206 VAL D O   
8271  C  CB  . VAL D  206 ? 0.1967 0.1046 0.0764 0.0073  0.0439  -0.0013 206 VAL D CB  
8272  C  CG1 . VAL D  206 ? 0.1712 0.1217 0.0798 0.0152  0.0443  -0.0066 206 VAL D CG1 
8273  C  CG2 . VAL D  206 ? 0.1887 0.1328 0.0760 0.0403  0.0562  0.0250  206 VAL D CG2 
8274  N  N   . LEU D  207 ? 0.2063 0.0863 0.0775 0.0098  0.0631  0.0086  207 LEU D N   
8275  C  CA  . LEU D  207 ? 0.2458 0.0782 0.0854 0.0251  0.0873  0.0073  207 LEU D CA  
8276  C  C   . LEU D  207 ? 0.2292 0.0997 0.0626 0.0306  0.0494  0.0174  207 LEU D C   
8277  O  O   . LEU D  207 ? 0.1969 0.0900 0.1041 0.0287  0.0582  0.0173  207 LEU D O   
8278  C  CB  . LEU D  207 ? 0.2874 0.1251 0.1230 -0.0024 0.1242  0.0231  207 LEU D CB  
8279  C  CG  . LEU D  207 ? 0.3526 0.1409 0.1420 -0.0392 0.0952  0.0241  207 LEU D CG  
8280  C  CD1 . LEU D  207 ? 0.3350 0.2014 0.1554 0.0024  0.0921  0.0355  207 LEU D CD1 
8281  C  CD2 . LEU D  207 ? 0.4242 0.3000 0.2944 -0.0381 0.1353  0.1444  207 LEU D CD2 
8282  N  N   . TRP D  208 ? 0.1957 0.0852 0.0917 0.0252  0.0531  0.0124  208 TRP D N   
8283  C  CA  . TRP D  208 ? 0.1933 0.0899 0.0873 0.0182  0.0496  0.0060  208 TRP D CA  
8284  C  C   . TRP D  208 ? 0.1676 0.1014 0.0838 0.0239  0.0509  0.0249  208 TRP D C   
8285  O  O   . TRP D  208 ? 0.2524 0.0929 0.0913 0.0362  0.0494  0.0245  208 TRP D O   
8286  C  CB  . TRP D  208 ? 0.1717 0.0933 0.1172 0.0194  0.0461  0.0171  208 TRP D CB  
8287  C  CG  . TRP D  208 ? 0.1969 0.0755 0.0809 0.0287  0.0416  -0.0001 208 TRP D CG  
8288  C  CD1 . TRP D  208 ? 0.1671 0.0949 0.1009 0.0286  0.0472  0.0054  208 TRP D CD1 
8289  C  CD2 . TRP D  208 ? 0.1771 0.0834 0.0870 0.0340  0.0463  -0.0010 208 TRP D CD2 
8290  N  NE1 . TRP D  208 ? 0.1504 0.1018 0.0843 0.0197  0.0403  -0.0120 208 TRP D NE1 
8291  C  CE2 . TRP D  208 ? 0.1538 0.0806 0.0861 0.0225  0.0403  -0.0041 208 TRP D CE2 
8292  C  CE3 . TRP D  208 ? 0.1662 0.0938 0.0885 0.0206  0.0493  -0.0091 208 TRP D CE3 
8293  C  CZ2 . TRP D  208 ? 0.1356 0.1073 0.0794 0.0335  0.0560  0.0020  208 TRP D CZ2 
8294  C  CZ3 . TRP D  208 ? 0.1527 0.0940 0.0948 0.0168  0.0520  -0.0083 208 TRP D CZ3 
8295  C  CH2 . TRP D  208 ? 0.1612 0.0861 0.0994 0.0197  0.0441  -0.0105 208 TRP D CH2 
8296  N  N   . THR D  209 ? 0.1445 0.0913 0.1000 0.0201  0.0571  0.0275  209 THR D N   
8297  C  CA  . THR D  209 ? 0.1620 0.0818 0.1208 0.0276  0.0793  0.0052  209 THR D CA  
8298  C  C   . THR D  209 ? 0.1499 0.0753 0.0890 0.0227  0.0570  0.0458  209 THR D C   
8299  O  O   . THR D  209 ? 0.1840 0.0895 0.0922 0.0392  0.0498  0.0274  209 THR D O   
8300  C  CB  . THR D  209 ? 0.1739 0.0874 0.1299 0.0232  0.0672  0.0197  209 THR D CB  
8301  O  OG1 . THR D  209 ? 0.2057 0.0966 0.1299 0.0361  0.1086  0.0342  209 THR D OG1 
8302  C  CG2 . THR D  209 ? 0.1852 0.0944 0.2077 0.0331  0.1014  0.0200  209 THR D CG2 
8303  N  N   . VAL D  210 ? 0.1526 0.0744 0.1042 0.0272  0.0680  0.0233  210 VAL D N   
8304  C  CA  . VAL D  210 ? 0.1423 0.0719 0.1054 0.0073  0.0644  0.0160  210 VAL D CA  
8305  C  C   . VAL D  210 ? 0.1403 0.0775 0.1224 0.0255  0.0603  0.0303  210 VAL D C   
8306  O  O   . VAL D  210 ? 0.1561 0.0870 0.1143 0.0274  0.0685  0.0267  210 VAL D O   
8307  C  CB  . VAL D  210 ? 0.1389 0.0970 0.1012 0.0092  0.0476  0.0098  210 VAL D CB  
8308  C  CG1 . VAL D  210 ? 0.1639 0.1163 0.1125 0.0195  0.0689  0.0136  210 VAL D CG1 
8309  C  CG2 . VAL D  210 ? 0.1585 0.1115 0.1055 0.0032  0.0522  0.0165  210 VAL D CG2 
8310  N  N   . PHE D  211 ? 0.1193 0.0723 0.1163 0.0071  0.0632  0.0196  211 PHE D N   
8311  C  CA  . PHE D  211 ? 0.1218 0.0793 0.1420 0.0065  0.0505  0.0242  211 PHE D CA  
8312  C  C   . PHE D  211 ? 0.1500 0.0723 0.1436 -0.0030 0.0806  0.0196  211 PHE D C   
8313  O  O   . PHE D  211 ? 0.1518 0.0879 0.1384 0.0032  0.0763  0.0152  211 PHE D O   
8314  C  CB  . PHE D  211 ? 0.1402 0.1075 0.1365 0.0035  0.0701  0.0021  211 PHE D CB  
8315  C  CG  . PHE D  211 ? 0.1393 0.0909 0.1543 -0.0054 0.0621  0.0414  211 PHE D CG  
8316  C  CD1 . PHE D  211 ? 0.1534 0.0818 0.1586 -0.0107 0.0758  0.0116  211 PHE D CD1 
8317  C  CD2 . PHE D  211 ? 0.1669 0.0685 0.1720 0.0017  0.0610  0.0282  211 PHE D CD2 
8318  C  CE1 . PHE D  211 ? 0.1489 0.1212 0.1953 0.0121  0.0913  0.0164  211 PHE D CE1 
8319  C  CE2 . PHE D  211 ? 0.1595 0.0759 0.2443 -0.0027 0.0834  0.0439  211 PHE D CE2 
8320  C  CZ  . PHE D  211 ? 0.1896 0.0811 0.2238 0.0109  0.0768  0.0339  211 PHE D CZ  
8321  N  N   . ARG D  212 ? 0.1438 0.0845 0.1604 0.0115  0.0837  0.0340  212 ARG D N   
8322  C  CA  . ARG D  212 ? 0.1761 0.0710 0.1443 0.0237  0.0698  0.0183  212 ARG D CA  
8323  C  C   . ARG D  212 ? 0.1407 0.0709 0.1538 0.0194  0.0529  0.0162  212 ARG D C   
8324  O  O   . ARG D  212 ? 0.1899 0.1089 0.1705 0.0315  0.0910  0.0277  212 ARG D O   
8325  C  CB  . ARG D  212 ? 0.1992 0.0927 0.1619 0.0284  0.0693  0.0410  212 ARG D CB  
8326  C  CG  . ARG D  212 ? 0.1766 0.1208 0.1984 0.0504  0.0509  0.0621  212 ARG D CG  
8327  C  CD  . ARG D  212 ? 0.2545 0.1103 0.1739 0.0759  0.0716  0.0630  212 ARG D CD  
8328  N  NE  . ARG D  212 ? 0.2874 0.1353 0.2090 0.0768  0.0487  0.0597  212 ARG D NE  
8329  C  CZ  . ARG D  212 ? 0.3206 0.1520 0.2630 0.1203  0.1054  0.0786  212 ARG D CZ  
8330  N  NH1 . ARG D  212 ? 0.3792 0.1612 0.3039 0.0658  0.1298  0.1068  212 ARG D NH1 
8331  N  NH2 . ARG D  212 ? 0.3785 0.2238 0.2763 0.1633  0.0443  0.0619  212 ARG D NH2 
8332  N  N   . ASN D  213 ? 0.1703 0.0795 0.1362 0.0065  0.0441  0.0194  213 ASN D N   
8333  C  CA  . ASN D  213 ? 0.1707 0.0861 0.1441 0.0052  0.0295  0.0172  213 ASN D CA  
8334  C  C   . ASN D  213 ? 0.1659 0.0716 0.1675 0.0000  0.0436  0.0126  213 ASN D C   
8335  O  O   . ASN D  213 ? 0.1852 0.0733 0.1626 0.0226  0.0758  0.0280  213 ASN D O   
8336  C  CB  . ASN D  213 ? 0.2150 0.0886 0.2001 -0.0337 0.0447  0.0383  213 ASN D CB  
8337  C  CG  . ASN D  213 ? 0.2734 0.0957 0.2193 0.0219  0.0775  0.0333  213 ASN D CG  
8338  O  OD1 . ASN D  213 ? 0.3149 0.1875 0.4562 0.0461  0.1278  0.1964  213 ASN D OD1 
8339  N  ND2 . ASN D  213 ? 0.3829 0.1594 0.3048 0.0217  0.1708  0.1048  213 ASN D ND2 
8340  N  N   . PRO D  214 ? 0.1565 0.0830 0.1538 0.0212  0.0509  0.0173  214 PRO D N   
8341  C  CA  . PRO D  214 ? 0.1305 0.0888 0.1515 0.0041  0.0511  0.0231  214 PRO D CA  
8342  C  C   . PRO D  214 ? 0.1332 0.0723 0.1488 0.0034  0.0423  -0.0035 214 PRO D C   
8343  O  O   . PRO D  214 ? 0.1818 0.0815 0.1917 -0.0124 0.0515  0.0291  214 PRO D O   
8344  C  CB  . PRO D  214 ? 0.1444 0.1107 0.1967 0.0201  0.0529  -0.0043 214 PRO D CB  
8345  C  CG  . PRO D  214 ? 0.2017 0.1581 0.1919 0.0709  0.0604  0.0247  214 PRO D CG  
8346  C  CD  . PRO D  214 ? 0.2097 0.1066 0.1676 0.0564  0.0619  -0.0006 214 PRO D CD  
8347  N  N   . VAL D  215 ? 0.1331 0.0885 0.1506 0.0000  0.0465  0.0122  215 VAL D N   
8348  C  CA  . VAL D  215 ? 0.1170 0.0854 0.1441 -0.0089 0.0557  0.0092  215 VAL D CA  
8349  C  C   . VAL D  215 ? 0.1145 0.0791 0.1570 -0.0108 0.0472  0.0093  215 VAL D C   
8350  O  O   . VAL D  215 ? 0.1224 0.1023 0.1511 -0.0140 0.0571  -0.0088 215 VAL D O   
8351  C  CB  . VAL D  215 ? 0.1141 0.0736 0.1720 0.0092  0.0623  -0.0015 215 VAL D CB  
8352  C  CG1 . VAL D  215 ? 0.1441 0.1215 0.1856 0.0048  0.0793  -0.0142 215 VAL D CG1 
8353  C  CG2 . VAL D  215 ? 0.1222 0.0890 0.1779 0.0083  0.0375  0.0118  215 VAL D CG2 
8354  N  N   . GLN D  216 ? 0.1396 0.0732 0.1317 -0.0008 0.0449  0.0055  216 GLN D N   
8355  C  CA  . GLN D  216 ? 0.1710 0.0760 0.1222 0.0179  0.0516  0.0068  216 GLN D CA  
8356  C  C   . GLN D  216 ? 0.1132 0.0851 0.1463 0.0074  0.0313  -0.0082 216 GLN D C   
8357  O  O   . GLN D  216 ? 0.1154 0.1181 0.1644 0.0060  0.0381  0.0017  216 GLN D O   
8358  C  CB  . GLN D  216 ? 0.1711 0.0854 0.1434 0.0166  0.0245  0.0037  216 GLN D CB  
8359  C  CG  . GLN D  216 ? 0.1847 0.0878 0.1811 0.0174  0.0185  0.0080  216 GLN D CG  
8360  C  CD  . GLN D  216 ? 0.2154 0.1035 0.1796 0.0060  0.0133  0.0219  216 GLN D CD  
8361  O  OE1 . GLN D  216 ? 0.1915 0.1147 0.1572 -0.0007 0.0333  0.0082  216 GLN D OE1 
8362  N  NE2 . GLN D  216 ? 0.4905 0.1254 0.2443 0.0253  -0.0769 0.0212  216 GLN D NE2 
8363  N  N   . ILE D  217 ? 0.1308 0.0739 0.1340 0.0020  0.0311  0.0000  217 ILE D N   
8364  C  CA  . ILE D  217 ? 0.1374 0.0676 0.1331 0.0164  0.0299  -0.0020 217 ILE D CA  
8365  C  C   . ILE D  217 ? 0.1231 0.0614 0.1333 0.0088  0.0285  0.0104  217 ILE D C   
8366  O  O   . ILE D  217 ? 0.1170 0.0741 0.1464 0.0236  0.0335  0.0065  217 ILE D O   
8367  C  CB  . ILE D  217 ? 0.1398 0.0642 0.1507 -0.0104 0.0270  -0.0116 217 ILE D CB  
8368  C  CG1 . ILE D  217 ? 0.1410 0.0725 0.1639 -0.0176 0.0478  0.0097  217 ILE D CG1 
8369  C  CG2 . ILE D  217 ? 0.1420 0.0667 0.1788 0.0076  0.0487  -0.0115 217 ILE D CG2 
8370  C  CD1 . ILE D  217 ? 0.1845 0.0782 0.1941 -0.0160 0.0504  -0.0096 217 ILE D CD1 
8371  N  N   . SER D  218 ? 0.1337 0.0718 0.1355 0.0020  0.0346  -0.0008 218 SER D N   
8372  C  CA  . SER D  218 ? 0.1430 0.0645 0.1374 0.0156  0.0241  -0.0003 218 SER D CA  
8373  C  C   . SER D  218 ? 0.1377 0.0900 0.1147 0.0020  0.0266  0.0109  218 SER D C   
8374  O  O   . SER D  218 ? 0.1667 0.0789 0.1368 -0.0121 0.0328  0.0081  218 SER D O   
8375  C  CB  . SER D  218 ? 0.1768 0.0737 0.1290 0.0071  -0.0015 -0.0111 218 SER D CB  
8376  O  OG  . SER D  218 ? 0.1500 0.0900 0.1483 0.0068  0.0126  0.0054  218 SER D OG  
8377  N  N   . GLN D  219 ? 0.1353 0.1001 0.1274 0.0114  0.0355  0.0006  219 GLN D N   
8378  C  CA  . GLN D  219 ? 0.1324 0.1495 0.1457 0.0142  0.0472  0.0461  219 GLN D CA  
8379  C  C   . GLN D  219 ? 0.1592 0.1120 0.1064 0.0048  0.0293  -0.0038 219 GLN D C   
8380  O  O   . GLN D  219 ? 0.1723 0.1014 0.1430 -0.0124 0.0392  0.0049  219 GLN D O   
8381  C  CB  . GLN D  219 ? 0.2086 0.2248 0.1922 0.0707  0.1234  0.0540  219 GLN D CB  
8382  C  CG  . GLN D  219 ? 0.2196 0.3269 0.2624 0.0922  0.1228  0.1168  219 GLN D CG  
8383  C  CD  . GLN D  219 ? 0.2152 0.3362 0.2653 0.0294  0.0259  0.0844  219 GLN D CD  
8384  O  OE1 . GLN D  219 ? 0.3111 0.4286 0.2339 0.1204  0.0373  -0.0778 219 GLN D OE1 
8385  N  NE2 . GLN D  219 ? 0.2556 0.3767 0.4889 -0.0394 0.0206  0.2142  219 GLN D NE2 
8386  N  N   . GLU D  220 ? 0.1838 0.1045 0.1127 0.0051  0.0259  -0.0028 220 GLU D N   
8387  C  CA  . GLU D  220 ? 0.2134 0.0888 0.1280 0.0013  0.0077  -0.0044 220 GLU D CA  
8388  C  C   . GLU D  220 ? 0.1586 0.0888 0.1324 -0.0008 0.0188  0.0007  220 GLU D C   
8389  O  O   . GLU D  220 ? 0.1838 0.0935 0.1165 -0.0070 0.0173  -0.0007 220 GLU D O   
8390  C  CB  . GLU D  220 ? 0.2511 0.1473 0.1242 0.0017  0.0062  -0.0384 220 GLU D CB  
8391  C  CG  . GLU D  220 ? 0.2592 0.1272 0.1640 0.0109  0.0060  -0.0195 220 GLU D CG  
8392  C  CD  . GLU D  220 ? 0.3662 0.1714 0.1453 0.0119  0.0368  -0.0071 220 GLU D CD  
8393  O  OE1 . GLU D  220 ? 0.3366 0.1256 0.1811 -0.0195 0.0513  -0.0027 220 GLU D OE1 
8394  O  OE2 . GLU D  220 ? 0.7502 0.1915 0.2860 0.0772  0.1853  -0.0171 220 GLU D OE2 
8395  N  N   . GLN D  221 ? 0.1551 0.0863 0.1315 -0.0038 0.0221  0.0027  221 GLN D N   
8396  C  CA  . GLN D  221 ? 0.1576 0.0769 0.1437 -0.0086 0.0262  -0.0082 221 GLN D CA  
8397  C  C   . GLN D  221 ? 0.1491 0.0776 0.1416 -0.0012 0.0274  -0.0013 221 GLN D C   
8398  O  O   . GLN D  221 ? 0.1560 0.0680 0.1583 0.0063  0.0318  0.0027  221 GLN D O   
8399  C  CB  . GLN D  221 ? 0.1457 0.0964 0.1396 -0.0168 0.0259  -0.0026 221 GLN D CB  
8400  C  CG  . GLN D  221 ? 0.1246 0.0965 0.1809 -0.0059 0.0130  0.0038  221 GLN D CG  
8401  C  CD  . GLN D  221 ? 0.1296 0.0800 0.1524 -0.0068 0.0015  -0.0020 221 GLN D CD  
8402  O  OE1 . GLN D  221 ? 0.1360 0.0836 0.1583 0.0066  0.0120  0.0060  221 GLN D OE1 
8403  N  NE2 . GLN D  221 ? 0.1423 0.0908 0.1817 0.0088  0.0049  -0.0087 221 GLN D NE2 
8404  N  N   . LEU D  222 ? 0.1409 0.0953 0.1120 -0.0001 0.0225  -0.0088 222 LEU D N   
8405  C  CA  . LEU D  222 ? 0.1483 0.0903 0.1154 -0.0017 0.0188  0.0038  222 LEU D CA  
8406  C  C   . LEU D  222 ? 0.1513 0.0571 0.1262 0.0136  0.0114  -0.0007 222 LEU D C   
8407  O  O   . LEU D  222 ? 0.1554 0.0701 0.1340 -0.0060 0.0250  -0.0040 222 LEU D O   
8408  C  CB  . LEU D  222 ? 0.1574 0.1106 0.1289 0.0093  0.0340  -0.0087 222 LEU D CB  
8409  C  CG  . LEU D  222 ? 0.1824 0.1028 0.1605 -0.0094 0.0568  -0.0070 222 LEU D CG  
8410  C  CD1 . LEU D  222 ? 0.2425 0.1194 0.1393 0.0082  0.0326  -0.0010 222 LEU D CD1 
8411  C  CD2 . LEU D  222 ? 0.2242 0.1359 0.1362 0.0237  -0.0006 -0.0403 222 LEU D CD2 
8412  N  N   . LEU D  223 ? 0.1541 0.0838 0.1225 -0.0121 0.0206  -0.0107 223 LEU D N   
8413  C  CA  . LEU D  223 ? 0.1872 0.0832 0.1213 0.0060  0.0335  0.0013  223 LEU D CA  
8414  C  C   . LEU D  223 ? 0.1795 0.0742 0.1174 0.0038  0.0217  -0.0028 223 LEU D C   
8415  O  O   . LEU D  223 ? 0.1937 0.0811 0.1463 -0.0096 0.0253  0.0093  223 LEU D O   
8416  C  CB  . LEU D  223 ? 0.1969 0.1155 0.1111 -0.0153 0.0296  -0.0085 223 LEU D CB  
8417  C  CG  . LEU D  223 ? 0.1924 0.1102 0.1545 0.0107  0.0425  0.0115  223 LEU D CG  
8418  C  CD1 . LEU D  223 ? 0.1985 0.1684 0.1915 -0.0065 0.0546  -0.0218 223 LEU D CD1 
8419  C  CD2 . LEU D  223 ? 0.2201 0.1543 0.1195 -0.0035 0.0401  -0.0096 223 LEU D CD2 
8420  N  N   . ALA D  224 ? 0.1599 0.1147 0.1398 0.0024  0.0046  -0.0013 224 ALA D N   
8421  C  CA  . ALA D  224 ? 0.1671 0.1102 0.1750 0.0063  -0.0035 0.0126  224 ALA D CA  
8422  C  C   . ALA D  224 ? 0.1513 0.0969 0.1635 0.0063  0.0254  0.0179  224 ALA D C   
8423  O  O   . ALA D  224 ? 0.1948 0.0864 0.2120 -0.0020 0.0317  0.0283  224 ALA D O   
8424  C  CB  . ALA D  224 ? 0.1789 0.1374 0.2384 -0.0179 -0.0295 0.0148  224 ALA D CB  
8425  N  N   . LEU D  225 ? 0.1488 0.0924 0.1791 -0.0043 0.0253  -0.0049 225 LEU D N   
8426  C  CA  . LEU D  225 ? 0.1249 0.1093 0.1578 -0.0130 0.0340  0.0060  225 LEU D CA  
8427  C  C   . LEU D  225 ? 0.1444 0.0745 0.1668 0.0070  0.0243  -0.0059 225 LEU D C   
8428  O  O   . LEU D  225 ? 0.1579 0.0719 0.2213 0.0049  0.0533  -0.0020 225 LEU D O   
8429  C  CB  . LEU D  225 ? 0.1414 0.0910 0.1755 -0.0012 0.0500  -0.0171 225 LEU D CB  
8430  C  CG  . LEU D  225 ? 0.1689 0.1138 0.1669 0.0161  0.0028  -0.0010 225 LEU D CG  
8431  C  CD1 . LEU D  225 ? 0.1642 0.1152 0.1851 0.0196  0.0165  -0.0265 225 LEU D CD1 
8432  C  CD2 . LEU D  225 ? 0.1588 0.1389 0.1628 0.0127  0.0234  -0.0065 225 LEU D CD2 
8433  N  N   . GLU D  226 ? 0.1265 0.0967 0.1540 0.0015  0.0252  -0.0066 226 GLU D N   
8434  C  CA  . GLU D  226 ? 0.1444 0.1111 0.1398 0.0000  0.0111  0.0035  226 GLU D CA  
8435  C  C   . GLU D  226 ? 0.1594 0.0900 0.1532 -0.0170 0.0196  0.0219  226 GLU D C   
8436  O  O   . GLU D  226 ? 0.2002 0.1766 0.2096 -0.0851 -0.0153 0.0299  226 GLU D O   
8437  C  CB  . GLU D  226 ? 0.1470 0.0996 0.1335 0.0017  0.0340  0.0244  226 GLU D CB  
8438  C  CG  . GLU D  226 ? 0.1606 0.1058 0.1172 -0.0063 0.0342  0.0040  226 GLU D CG  
8439  C  CD  . GLU D  226 ? 0.1702 0.1394 0.0961 -0.0046 0.0476  0.0089  226 GLU D CD  
8440  O  OE1 . GLU D  226 ? 0.1800 0.1558 0.1256 0.0234  0.0524  -0.0003 226 GLU D OE1 
8441  O  OE2 . GLU D  226 ? 0.2849 0.1023 0.1218 0.0081  0.0302  0.0041  226 GLU D OE2 
8442  N  N   . THR D  227 ? 0.1558 0.0979 0.1172 0.0007  0.0284  0.0017  227 THR D N   
8443  C  CA  . THR D  227 ? 0.1899 0.1154 0.1173 0.0060  0.0346  0.0068  227 THR D CA  
8444  C  C   . THR D  227 ? 0.2061 0.1057 0.1252 -0.0006 0.0060  0.0160  227 THR D C   
8445  O  O   . THR D  227 ? 0.2676 0.1405 0.1545 0.0212  0.0392  0.0313  227 THR D O   
8446  C  CB  . THR D  227 ? 0.1833 0.1421 0.1398 0.0041  0.0474  -0.0068 227 THR D CB  
8447  O  OG1 . THR D  227 ? 0.2224 0.1235 0.1549 -0.0165 0.0206  0.0037  227 THR D OG1 
8448  C  CG2 . THR D  227 ? 0.2000 0.1632 0.1657 0.0340  0.0370  -0.0062 227 THR D CG2 
8449  N  N   . ALA D  228 ? 0.1717 0.1100 0.1529 0.0035  0.0184  0.0126  228 ALA D N   
8450  C  CA  . ALA D  228 ? 0.2027 0.0933 0.1885 0.0043  -0.0080 0.0115  228 ALA D CA  
8451  C  C   . ALA D  228 ? 0.2380 0.1037 0.1692 -0.0099 -0.0377 0.0197  228 ALA D C   
8452  O  O   . ALA D  228 ? 0.3273 0.1075 0.2265 -0.0254 -0.0953 0.0355  228 ALA D O   
8453  C  CB  . ALA D  228 ? 0.1457 0.1233 0.3016 0.0003  0.0204  0.0166  228 ALA D CB  
8454  N  N   . LEU D  229 ? 0.1692 0.0978 0.1596 -0.0240 0.0231  0.0188  229 LEU D N   
8455  C  CA  . LEU D  229 ? 0.1689 0.0951 0.1983 -0.0121 -0.0282 0.0080  229 LEU D CA  
8456  C  C   . LEU D  229 ? 0.1556 0.1123 0.1905 -0.0048 -0.0295 0.0206  229 LEU D C   
8457  O  O   . LEU D  229 ? 0.1583 0.0969 0.2034 -0.0160 -0.0023 0.0463  229 LEU D O   
8458  C  CB  . LEU D  229 ? 0.1870 0.1152 0.1856 -0.0074 -0.0111 -0.0006 229 LEU D CB  
8459  C  CG  . LEU D  229 ? 0.1703 0.1102 0.1726 -0.0142 0.0048  0.0183  229 LEU D CG  
8460  C  CD1 . LEU D  229 ? 0.2009 0.2436 0.1628 -0.0001 0.0275  -0.0244 229 LEU D CD1 
8461  C  CD2 . LEU D  229 ? 0.1838 0.1711 0.3194 -0.0410 -0.0294 0.0997  229 LEU D CD2 
8462  N  N   . TYR D  230 ? 0.1730 0.0988 0.2258 -0.0171 -0.0245 0.0351  230 TYR D N   
8463  C  CA  . TYR D  230 ? 0.1840 0.1044 0.2029 -0.0344 0.0015  0.0522  230 TYR D CA  
8464  C  C   . TYR D  230 ? 0.2007 0.1235 0.1692 -0.0357 -0.0277 0.0671  230 TYR D C   
8465  O  O   . TYR D  230 ? 0.1789 0.1186 0.2291 -0.0276 -0.0024 0.0298  230 TYR D O   
8466  C  CB  . TYR D  230 ? 0.2089 0.1380 0.1847 -0.0253 -0.0102 0.0318  230 TYR D CB  
8467  C  CG  . TYR D  230 ? 0.2248 0.1389 0.1856 -0.0172 -0.0159 0.0203  230 TYR D CG  
8468  C  CD1 . TYR D  230 ? 0.2459 0.2010 0.3562 0.0198  -0.0156 -0.0734 230 TYR D CD1 
8469  C  CD2 . TYR D  230 ? 0.2404 0.1852 0.1965 0.0217  -0.0273 -0.0068 230 TYR D CD2 
8470  C  CE1 . TYR D  230 ? 0.3425 0.2467 0.4262 0.0267  -0.0406 -0.1349 230 TYR D CE1 
8471  C  CE2 . TYR D  230 ? 0.2680 0.2179 0.2325 0.0240  -0.0068 -0.0081 230 TYR D CE2 
8472  C  CZ  . TYR D  230 ? 0.3068 0.3260 0.4180 0.0878  -0.0368 -0.2136 230 TYR D CZ  
8473  O  OH  . TYR D  230 ? 0.3021 0.4512 0.6122 0.0219  0.1041  -0.3224 230 TYR D OH  
8474  N  N   . CYS D  231 ? 0.1861 0.1624 0.1545 -0.0557 0.0141  0.0627  231 CYS D N   
8475  C  CA  . CYS D  231 ? 0.1956 0.1856 0.1556 -0.0784 -0.0210 0.0729  231 CYS D CA  
8476  C  C   . CYS D  231 ? 0.1829 0.1752 0.1517 -0.0549 0.0443  0.0207  231 CYS D C   
8477  O  O   . CYS D  231 ? 0.2341 0.2012 0.1549 -0.0535 0.0443  0.0302  231 CYS D O   
8478  C  CB  . CYS D  231 ? 0.2391 0.2037 0.1919 -0.0719 -0.0203 0.0856  231 CYS D CB  
8479  S  SG  . CYS D  231 ? 0.2506 0.1908 0.1890 -0.0544 -0.0046 0.0482  231 CYS D SG  
8480  N  N   . THR D  232 ? 0.1976 0.1595 0.1396 -0.0557 0.0122  0.0500  232 THR D N   
8481  C  CA  . THR D  232 ? 0.1923 0.1499 0.1199 -0.0590 0.0275  0.0303  232 THR D CA  
8482  C  C   . THR D  232 ? 0.1890 0.1341 0.1082 -0.0390 0.0544  0.0155  232 THR D C   
8483  O  O   . THR D  232 ? 0.1851 0.1220 0.1356 -0.0425 0.0425  0.0206  232 THR D O   
8484  C  CB  . THR D  232 ? 0.2168 0.1089 0.1585 -0.0388 0.0242  0.0275  232 THR D CB  
8485  O  OG1 . THR D  232 ? 0.2014 0.1174 0.1571 -0.0167 0.0553  0.0263  232 THR D OG1 
8486  C  CG2 . THR D  232 ? 0.1998 0.1835 0.2206 -0.0557 0.0231  0.0126  232 THR D CG2 
8487  N  N   A HIS D  233 ? 0.2027 0.1244 0.1483 -0.0313 0.0394  0.0255  233 HIS D N   
8488  N  N   B HIS D  233 ? 0.2029 0.1246 0.1483 -0.0315 0.0392  0.0254  233 HIS D N   
8489  C  CA  A HIS D  233 ? 0.2008 0.1297 0.1579 -0.0099 0.0342  0.0071  233 HIS D CA  
8490  C  CA  B HIS D  233 ? 0.2021 0.1360 0.1577 -0.0115 0.0344  0.0073  233 HIS D CA  
8491  C  C   A HIS D  233 ? 0.2282 0.1253 0.1342 -0.0359 0.0299  0.0364  233 HIS D C   
8492  C  C   B HIS D  233 ? 0.2287 0.1254 0.1344 -0.0346 0.0294  0.0353  233 HIS D C   
8493  O  O   A HIS D  233 ? 0.2238 0.1225 0.1499 -0.0214 0.0430  0.0434  233 HIS D O   
8494  O  O   B HIS D  233 ? 0.2249 0.1254 0.1527 -0.0230 0.0410  0.0449  233 HIS D O   
8495  C  CB  A HIS D  233 ? 0.2804 0.1323 0.1856 0.0361  0.0156  -0.0137 233 HIS D CB  
8496  C  CB  B HIS D  233 ? 0.3072 0.1430 0.2194 0.0105  0.0333  -0.0133 233 HIS D CB  
8497  C  CG  A HIS D  233 ? 0.2700 0.1100 0.2881 -0.0408 0.1283  -0.0798 233 HIS D CG  
8498  C  CG  B HIS D  233 ? 0.3490 0.2088 0.3307 0.0450  0.0308  -0.0399 233 HIS D CG  
8499  N  ND1 A HIS D  233 ? 0.3486 0.2867 0.3952 0.0091  0.0082  -0.2062 233 HIS D ND1 
8500  N  ND1 B HIS D  233 ? 0.5080 0.3075 0.3919 0.0555  0.2569  -0.0652 233 HIS D ND1 
8501  C  CD2 A HIS D  233 ? 0.2921 0.2138 0.2619 -0.0375 0.1594  -0.0824 233 HIS D CD2 
8502  C  CD2 B HIS D  233 ? 0.4120 0.2860 0.4330 -0.0126 0.1315  -0.1064 233 HIS D CD2 
8503  C  CE1 A HIS D  233 ? 0.4558 0.3253 0.5643 0.0299  0.1595  -0.2793 233 HIS D CE1 
8504  C  CE1 B HIS D  233 ? 0.4268 0.2342 0.5453 -0.0043 0.2867  0.0674  233 HIS D CE1 
8505  N  NE2 A HIS D  233 ? 0.6672 0.1811 0.2669 -0.0529 0.2964  -0.0756 233 HIS D NE2 
8506  N  NE2 B HIS D  233 ? 0.6581 0.5297 0.3948 0.1538  0.2320  0.0298  233 HIS D NE2 
8507  N  N   . MET D  234 ? 0.2576 0.1138 0.1155 -0.0048 0.0199  0.0282  234 MET D N   
8508  C  CA  . MET D  234 ? 0.2592 0.1723 0.0996 -0.0287 0.0109  0.0342  234 MET D CA  
8509  C  C   . MET D  234 ? 0.3037 0.1723 0.1048 0.0026  0.0410  0.0368  234 MET D C   
8510  O  O   . MET D  234 ? 0.3091 0.2443 0.1253 -0.0427 0.0671  0.0044  234 MET D O   
8511  C  CB  . MET D  234 ? 0.2648 0.1967 0.1380 0.0168  -0.0077 0.0137  234 MET D CB  
8512  C  CG  . MET D  234 ? 0.2287 0.2913 0.1662 -0.0274 0.0094  -0.0253 234 MET D CG  
8513  S  SD  . MET D  234 ? 0.2904 0.5360 0.2231 -0.0168 -0.0003 -0.0590 234 MET D SD  
8514  C  CE  . MET D  234 ? 0.3034 0.4708 0.2700 -0.0201 0.0397  -0.0678 234 MET D CE  
8515  N  N   A ASP D  235 ? 0.3763 0.1385 0.2274 -0.0221 -0.0185 0.1010  235 ASP D N   
8516  N  N   B ASP D  235 ? 0.2476 0.1863 0.1452 -0.0599 0.0406  0.0483  235 ASP D N   
8517  C  CA  A ASP D  235 ? 0.3170 0.2425 0.1766 0.0006  0.0520  0.0778  235 ASP D CA  
8518  C  CA  B ASP D  235 ? 0.2136 0.2125 0.2032 -0.0206 0.1023  0.0373  235 ASP D CA  
8519  C  C   A ASP D  235 ? 0.2673 0.2206 0.2784 0.0132  0.0322  0.1299  235 ASP D C   
8520  C  C   B ASP D  235 ? 0.2680 0.1516 0.1912 -0.0538 0.0353  0.0983  235 ASP D C   
8521  O  O   A ASP D  235 ? 0.4059 0.1560 0.3009 -0.0384 0.0612  0.0275  235 ASP D O   
8522  O  O   B ASP D  235 ? 0.2711 0.1191 0.1615 -0.0395 0.0667  0.0612  235 ASP D O   
8523  C  CB  A ASP D  235 ? 0.2921 0.1933 0.1448 -0.0526 0.0137  0.1282  235 ASP D CB  
8524  C  CB  B ASP D  235 ? 0.3240 0.3479 0.0985 -0.0071 0.0315  0.0786  235 ASP D CB  
8525  C  CG  A ASP D  235 ? 0.3741 0.1901 0.2344 -0.0166 0.0732  0.1022  235 ASP D CG  
8526  C  CG  B ASP D  235 ? 0.3249 0.5863 0.1818 0.0467  -0.0153 0.1649  235 ASP D CG  
8527  O  OD1 A ASP D  235 ? 0.4444 0.1687 0.2678 -0.0303 -0.0057 0.0485  235 ASP D OD1 
8528  O  OD1 B ASP D  235 ? 0.5511 0.6226 0.2111 0.1462  0.0099  0.1080  235 ASP D OD1 
8529  O  OD2 A ASP D  235 ? 0.4309 0.2578 0.3684 0.0891  -0.0364 0.0912  235 ASP D OD2 
8530  O  OD2 B ASP D  235 ? 0.4598 0.7006 0.2718 0.1914  0.0896  0.1957  235 ASP D OD2 
8531  N  N   . ASP D  236 ? 0.2476 0.1605 0.2048 -0.0322 0.0230  0.0724  236 ASP D N   
8532  C  CA  . ASP D  236 ? 0.2415 0.1991 0.2368 -0.0658 0.0187  0.0799  236 ASP D CA  
8533  C  C   . ASP D  236 ? 0.2303 0.2213 0.3070 -0.0741 0.0599  0.0408  236 ASP D C   
8534  O  O   . ASP D  236 ? 0.2908 0.2330 0.2337 -0.0723 0.0954  0.0452  236 ASP D O   
8535  C  CB  . ASP D  236 ? 0.2989 0.1809 0.2425 -0.0976 0.0032  0.0864  236 ASP D CB  
8536  C  CG  . ASP D  236 ? 0.2606 0.1826 0.2414 -0.0693 0.0458  0.0038  236 ASP D CG  
8537  O  OD1 . ASP D  236 ? 0.2470 0.2091 0.2958 -0.0615 0.0340  -0.0143 236 ASP D OD1 
8538  O  OD2 . ASP D  236 ? 0.2896 0.2827 0.2558 -0.0953 0.0698  0.0288  236 ASP D OD2 
8539  N  N   . PRO D  237 ? 0.2712 0.1981 0.3339 -0.0571 0.0964  0.0681  237 PRO D N   
8540  C  CA  . PRO D  237 ? 0.3476 0.2249 0.3625 -0.0551 0.1477  0.0986  237 PRO D CA  
8541  C  C   . PRO D  237 ? 0.3222 0.2099 0.3772 -0.0439 0.1580  0.0983  237 PRO D C   
8542  O  O   . PRO D  237 ? 0.3397 0.3237 0.3407 -0.0078 0.1776  0.1517  237 PRO D O   
8543  C  CB  . PRO D  237 ? 0.3470 0.2129 0.3434 -0.0820 0.0870  0.0769  237 PRO D CB  
8544  C  CG  . PRO D  237 ? 0.4043 0.1481 0.5759 -0.0538 0.2282  0.0824  237 PRO D CG  
8545  C  CD  . PRO D  237 ? 0.3269 0.2183 0.2967 -0.1221 0.0650  0.0759  237 PRO D CD  
8546  N  N   . SER D  238 ? 0.2745 0.1962 0.3298 -0.0678 0.0998  0.0908  238 SER D N   
8547  C  CA  . SER D  238 ? 0.2962 0.1717 0.3282 -0.0648 0.0690  0.0679  238 SER D CA  
8548  C  C   . SER D  238 ? 0.2030 0.2305 0.2170 -0.0230 0.0544  0.0672  238 SER D C   
8549  O  O   . SER D  238 ? 0.2132 0.2066 0.2700 -0.0535 0.0469  0.0812  238 SER D O   
8550  C  CB  . SER D  238 ? 0.3483 0.2662 0.4115 -0.2001 0.0256  0.0905  238 SER D CB  
8551  O  OG  . SER D  238 ? 0.4325 0.4031 0.4681 -0.1518 0.1492  0.0538  238 SER D OG  
8552  N  N   . PRO D  239 ? 0.2260 0.1897 0.2300 -0.0228 0.0640  0.0878  239 PRO D N   
8553  C  CA  . PRO D  239 ? 0.2319 0.1799 0.1933 -0.0531 0.0368  0.0706  239 PRO D CA  
8554  C  C   . PRO D  239 ? 0.1696 0.1687 0.2176 -0.0197 0.0582  0.0785  239 PRO D C   
8555  O  O   . PRO D  239 ? 0.2129 0.2100 0.2023 -0.0375 0.0403  0.0680  239 PRO D O   
8556  C  CB  . PRO D  239 ? 0.2213 0.2039 0.2190 -0.0662 0.0458  0.0480  239 PRO D CB  
8557  C  CG  . PRO D  239 ? 0.4875 0.3129 0.2465 -0.1805 0.1325  0.0255  239 PRO D CG  
8558  C  CD  . PRO D  239 ? 0.3019 0.2274 0.2089 -0.0439 0.0817  0.0513  239 PRO D CD  
8559  N  N   . ARG D  240 ? 0.1782 0.1490 0.1732 -0.0232 0.0322  0.0362  240 ARG D N   
8560  C  CA  . ARG D  240 ? 0.1897 0.1822 0.1550 -0.0428 0.0178  0.0707  240 ARG D CA  
8561  C  C   . ARG D  240 ? 0.2000 0.1971 0.1904 -0.0465 0.0362  0.0767  240 ARG D C   
8562  O  O   . ARG D  240 ? 0.1763 0.1694 0.2048 -0.0370 0.0208  0.0719  240 ARG D O   
8563  C  CB  . ARG D  240 ? 0.2012 0.2161 0.1904 -0.0665 0.0081  0.0522  240 ARG D CB  
8564  C  CG  . ARG D  240 ? 0.2014 0.2515 0.2266 -0.0857 0.0207  -0.0010 240 ARG D CG  
8565  C  CD  . ARG D  240 ? 0.2773 0.3508 0.2026 -0.0891 0.0232  -0.0220 240 ARG D CD  
8566  N  NE  . ARG D  240 ? 0.2612 0.3283 0.2303 -0.0733 0.0425  -0.0394 240 ARG D NE  
8567  C  CZ  . ARG D  240 ? 0.2763 0.2623 0.2418 -0.0252 0.0308  0.0386  240 ARG D CZ  
8568  N  NH1 . ARG D  240 ? 0.3264 0.2039 0.2266 -0.0781 0.0190  0.0041  240 ARG D NH1 
8569  N  NH2 . ARG D  240 ? 0.3134 0.2078 0.5461 0.0262  -0.1108 -0.0908 240 ARG D NH2 
8570  N  N   . GLU D  241 ? 0.1762 0.1549 0.2080 -0.0239 0.0223  0.0684  241 GLU D N   
8571  C  CA  . GLU D  241 ? 0.2002 0.1624 0.1764 -0.0412 0.0377  0.0736  241 GLU D CA  
8572  C  C   . GLU D  241 ? 0.1881 0.1267 0.1708 -0.0388 0.0005  0.0549  241 GLU D C   
8573  O  O   . GLU D  241 ? 0.1904 0.1520 0.1993 -0.0606 0.0109  0.0697  241 GLU D O   
8574  C  CB  . GLU D  241 ? 0.2495 0.1759 0.2513 -0.0098 0.0678  0.1084  241 GLU D CB  
8575  C  CG  . GLU D  241 ? 0.3386 0.1931 0.2312 -0.0041 0.0913  0.0491  241 GLU D CG  
8576  C  CD  . GLU D  241 ? 0.4095 0.2576 0.4780 0.0701  0.1525  0.0505  241 GLU D CD  
8577  O  OE1 . GLU D  241 ? 0.4753 0.4820 0.5758 0.0701  0.1875  -0.0802 241 GLU D OE1 
8578  O  OE2 . GLU D  241 ? 0.6277 0.5016 0.6212 0.1608  -0.0617 -0.2085 241 GLU D OE2 
8579  N  N   . MET D  242 ? 0.1755 0.1321 0.1592 -0.0229 0.0299  0.0681  242 MET D N   
8580  C  CA  . MET D  242 ? 0.1825 0.1130 0.1409 -0.0172 -0.0215 0.0438  242 MET D CA  
8581  C  C   . MET D  242 ? 0.1492 0.1231 0.1186 -0.0071 0.0003  0.0159  242 MET D C   
8582  O  O   . MET D  242 ? 0.1667 0.1220 0.1432 -0.0408 0.0109  0.0362  242 MET D O   
8583  C  CB  . MET D  242 ? 0.1689 0.1303 0.1684 -0.0195 -0.0241 0.0653  242 MET D CB  
8584  C  CG  . MET D  242 ? 0.1972 0.1280 0.1660 -0.0441 -0.0361 0.0496  242 MET D CG  
8585  S  SD  . MET D  242 ? 0.1768 0.1249 0.1656 -0.0326 0.0013  0.0357  242 MET D SD  
8586  C  CE  . MET D  242 ? 0.2211 0.1308 0.2197 -0.0351 -0.0294 0.0564  242 MET D CE  
8587  N  N   . ILE D  243 ? 0.1561 0.1115 0.1121 -0.0305 0.0032  0.0307  243 ILE D N   
8588  C  CA  . ILE D  243 ? 0.1527 0.1130 0.1009 -0.0176 0.0115  0.0140  243 ILE D CA  
8589  C  C   . ILE D  243 ? 0.1213 0.0915 0.0989 -0.0118 0.0419  0.0122  243 ILE D C   
8590  O  O   . ILE D  243 ? 0.1351 0.0989 0.1001 -0.0170 0.0379  0.0013  243 ILE D O   
8591  C  CB  . ILE D  243 ? 0.1787 0.1409 0.1046 -0.0303 0.0368  -0.0082 243 ILE D CB  
8592  C  CG1 . ILE D  243 ? 0.1766 0.1984 0.1194 -0.0456 0.0746  -0.0115 243 ILE D CG1 
8593  C  CG2 . ILE D  243 ? 0.2513 0.1822 0.0890 -0.0187 0.0182  -0.0103 243 ILE D CG2 
8594  C  CD1 . ILE D  243 ? 0.2161 0.2653 0.1488 -0.0384 0.0957  -0.0430 243 ILE D CD1 
8595  N  N   . ASN D  244 ? 0.0948 0.0965 0.0899 -0.0051 0.0350  0.0109  244 ASN D N   
8596  C  CA  . ASN D  244 ? 0.1036 0.0970 0.0994 -0.0054 0.0397  -0.0078 244 ASN D CA  
8597  C  C   . ASN D  244 ? 0.1134 0.0872 0.0890 -0.0204 0.0348  0.0115  244 ASN D C   
8598  O  O   . ASN D  244 ? 0.1075 0.0921 0.1114 -0.0107 0.0315  -0.0071 244 ASN D O   
8599  C  CB  . ASN D  244 ? 0.1001 0.1146 0.1217 0.0019  0.0403  -0.0088 244 ASN D CB  
8600  C  CG  . ASN D  244 ? 0.1048 0.1387 0.1297 -0.0046 0.0465  -0.0265 244 ASN D CG  
8601  O  OD1 . ASN D  244 ? 0.1191 0.1301 0.1692 0.0120  0.0531  -0.0215 244 ASN D OD1 
8602  N  ND2 . ASN D  244 ? 0.1671 0.1829 0.1748 -0.0373 0.1052  -0.0458 244 ASN D ND2 
8603  N  N   . ASN D  245 ? 0.0992 0.0793 0.0868 -0.0149 0.0399  -0.0006 245 ASN D N   
8604  C  CA  . ASN D  245 ? 0.1017 0.0694 0.0895 -0.0013 0.0445  -0.0017 245 ASN D CA  
8605  C  C   . ASN D  245 ? 0.0882 0.0681 0.0868 -0.0204 0.0335  -0.0174 245 ASN D C   
8606  O  O   . ASN D  245 ? 0.1030 0.1184 0.0967 -0.0006 0.0518  0.0119  245 ASN D O   
8607  C  CB  . ASN D  245 ? 0.1185 0.0794 0.0954 -0.0120 0.0381  0.0099  245 ASN D CB  
8608  C  CG  . ASN D  245 ? 0.1114 0.0698 0.0885 -0.0115 0.0425  0.0116  245 ASN D CG  
8609  O  OD1 . ASN D  245 ? 0.1080 0.0696 0.1410 -0.0116 0.0282  0.0149  245 ASN D OD1 
8610  N  ND2 . ASN D  245 ? 0.1186 0.1044 0.1428 0.0130  0.0172  -0.0065 245 ASN D ND2 
8611  N  N   . PHE D  246 ? 0.1012 0.0809 0.0836 -0.0063 0.0267  -0.0099 246 PHE D N   
8612  C  CA  . PHE D  246 ? 0.1091 0.0750 0.0750 -0.0209 0.0259  -0.0129 246 PHE D CA  
8613  C  C   . PHE D  246 ? 0.0915 0.0784 0.0815 0.0013  0.0331  -0.0071 246 PHE D C   
8614  O  O   . PHE D  246 ? 0.0960 0.0793 0.0890 -0.0049 0.0286  -0.0104 246 PHE D O   
8615  C  CB  . PHE D  246 ? 0.1093 0.0737 0.1033 -0.0066 0.0480  -0.0059 246 PHE D CB  
8616  C  CG  . PHE D  246 ? 0.1286 0.0707 0.1030 -0.0110 0.0377  0.0010  246 PHE D CG  
8617  C  CD1 . PHE D  246 ? 0.1195 0.0723 0.1111 -0.0252 0.0399  -0.0184 246 PHE D CD1 
8618  C  CD2 . PHE D  246 ? 0.1434 0.0894 0.1188 0.0010  0.0215  -0.0023 246 PHE D CD2 
8619  C  CE1 . PHE D  246 ? 0.1033 0.0985 0.1184 -0.0013 0.0251  -0.0100 246 PHE D CE1 
8620  C  CE2 . PHE D  246 ? 0.1436 0.1066 0.1270 0.0313  0.0089  -0.0013 246 PHE D CE2 
8621  C  CZ  . PHE D  246 ? 0.1374 0.1005 0.1168 -0.0131 0.0199  0.0027  246 PHE D CZ  
8622  N  N   . ARG D  247 ? 0.1050 0.0689 0.0748 -0.0031 0.0196  -0.0049 247 ARG D N   
8623  C  CA  . ARG D  247 ? 0.1058 0.0830 0.0778 -0.0015 0.0205  -0.0060 247 ARG D CA  
8624  C  C   . ARG D  247 ? 0.1102 0.0676 0.0897 -0.0040 0.0296  0.0010  247 ARG D C   
8625  O  O   . ARG D  247 ? 0.1195 0.0710 0.0910 -0.0006 0.0285  0.0048  247 ARG D O   
8626  C  CB  . ARG D  247 ? 0.1270 0.0879 0.0751 -0.0052 0.0239  -0.0120 247 ARG D CB  
8627  C  CG  . ARG D  247 ? 0.1218 0.0800 0.0856 0.0099  0.0188  -0.0182 247 ARG D CG  
8628  C  CD  . ARG D  247 ? 0.1453 0.0649 0.0821 -0.0052 0.0351  -0.0167 247 ARG D CD  
8629  N  NE  . ARG D  247 ? 0.1438 0.0734 0.0912 -0.0060 0.0243  -0.0099 247 ARG D NE  
8630  C  CZ  . ARG D  247 ? 0.1613 0.0649 0.0847 -0.0012 0.0388  -0.0083 247 ARG D CZ  
8631  N  NH1 . ARG D  247 ? 0.1599 0.0864 0.0983 0.0055  0.0403  -0.0001 247 ARG D NH1 
8632  N  NH2 . ARG D  247 ? 0.1526 0.0778 0.0971 0.0038  0.0225  -0.0105 247 ARG D NH2 
8633  N  N   . GLN D  248 ? 0.1102 0.0725 0.0737 -0.0007 0.0226  -0.0057 248 GLN D N   
8634  C  CA  . GLN D  248 ? 0.1066 0.0931 0.0730 -0.0027 0.0201  0.0136  248 GLN D CA  
8635  C  C   . GLN D  248 ? 0.1086 0.0897 0.0764 0.0035  0.0168  0.0063  248 GLN D C   
8636  O  O   . GLN D  248 ? 0.1256 0.0957 0.0851 0.0010  0.0307  -0.0041 248 GLN D O   
8637  C  CB  . GLN D  248 ? 0.1206 0.0922 0.0890 -0.0030 0.0375  -0.0006 248 GLN D CB  
8638  C  CG  . GLN D  248 ? 0.1256 0.0904 0.0829 -0.0076 0.0296  -0.0132 248 GLN D CG  
8639  C  CD  . GLN D  248 ? 0.1019 0.0897 0.0888 -0.0052 0.0193  0.0030  248 GLN D CD  
8640  O  OE1 . GLN D  248 ? 0.1120 0.0876 0.1077 -0.0032 0.0035  -0.0107 248 GLN D OE1 
8641  N  NE2 . GLN D  248 ? 0.1482 0.1040 0.1064 0.0377  -0.0083 -0.0170 248 GLN D NE2 
8642  N  N   . VAL D  249 ? 0.1258 0.0924 0.0719 0.0063  0.0201  0.0129  249 VAL D N   
8643  C  CA  . VAL D  249 ? 0.1420 0.0802 0.0705 -0.0024 0.0170  0.0142  249 VAL D CA  
8644  C  C   . VAL D  249 ? 0.1290 0.0908 0.0827 -0.0017 0.0201  0.0038  249 VAL D C   
8645  O  O   . VAL D  249 ? 0.1403 0.1008 0.0944 0.0008  0.0148  -0.0010 249 VAL D O   
8646  C  CB  . VAL D  249 ? 0.1523 0.0838 0.1054 0.0000  0.0390  0.0148  249 VAL D CB  
8647  C  CG1 . VAL D  249 ? 0.1834 0.1208 0.0882 -0.0223 0.0262  0.0000  249 VAL D CG1 
8648  C  CG2 . VAL D  249 ? 0.1680 0.1233 0.1265 0.0149  0.0225  0.0285  249 VAL D CG2 
8649  N  N   . GLN D  250 ? 0.1597 0.0866 0.0830 -0.0015 0.0185  -0.0027 250 GLN D N   
8650  C  CA  . GLN D  250 ? 0.1376 0.1033 0.0895 -0.0015 0.0024  -0.0034 250 GLN D CA  
8651  C  C   . GLN D  250 ? 0.1628 0.1145 0.0775 -0.0149 0.0281  0.0000  250 GLN D C   
8652  O  O   . GLN D  250 ? 0.1940 0.1215 0.1039 -0.0175 0.0241  0.0183  250 GLN D O   
8653  C  CB  . GLN D  250 ? 0.1450 0.1159 0.0952 0.0030  0.0233  -0.0063 250 GLN D CB  
8654  C  CG  . GLN D  250 ? 0.1547 0.0878 0.1261 -0.0207 0.0062  -0.0003 250 GLN D CG  
8655  C  CD  . GLN D  250 ? 0.1301 0.0685 0.1238 0.0003  0.0208  -0.0024 250 GLN D CD  
8656  O  OE1 . GLN D  250 ? 0.1703 0.0960 0.1046 -0.0233 0.0297  -0.0035 250 GLN D OE1 
8657  N  NE2 . GLN D  250 ? 0.1489 0.0964 0.1003 0.0052  0.0206  -0.0057 250 GLN D NE2 
8658  N  N   . LYS D  251 ? 0.1613 0.1685 0.0723 0.0122  0.0167  -0.0076 251 LYS D N   
8659  C  CA  . LYS D  251 ? 0.1648 0.2330 0.0811 -0.0131 0.0214  0.0159  251 LYS D CA  
8660  C  C   . LYS D  251 ? 0.1881 0.2054 0.0705 0.0192  0.0294  0.0000  251 LYS D C   
8661  O  O   . LYS D  251 ? 0.1957 0.1495 0.0933 -0.0038 0.0297  0.0091  251 LYS D O   
8662  C  CB  . LYS D  251 ? 0.1906 0.2985 0.0636 -0.0516 0.0226  -0.0166 251 LYS D CB  
8663  C  CG  . LYS D  251 ? 0.2043 0.2445 0.0958 -0.0179 0.0463  0.0175  251 LYS D CG  
8664  C  CD  . LYS D  251 ? 0.2294 0.3172 0.1161 0.0219  0.0601  0.0516  251 LYS D CD  
8665  C  CE  . LYS D  251 ? 0.1683 0.3215 0.0685 -0.0148 0.0222  0.0186  251 LYS D CE  
8666  N  NZ  . LYS D  251 ? 0.2084 0.2125 0.0623 -0.0340 0.0244  0.0065  251 LYS D NZ  
8667  N  N   . PHE D  252 ? 0.2071 0.2301 0.0420 -0.0124 0.0175  0.0043  252 PHE D N   
8668  C  CA  . PHE D  252 ? 0.1937 0.2048 0.0517 0.0297  0.0165  0.0083  252 PHE D CA  
8669  C  C   . PHE D  252 ? 0.2113 0.1404 0.1203 -0.0143 0.0841  0.0408  252 PHE D C   
8670  O  O   . PHE D  252 ? 0.2109 0.1626 0.1141 0.0144  0.0650  0.0485  252 PHE D O   
8671  C  CB  . PHE D  252 ? 0.2064 0.1610 0.1308 -0.0241 0.0329  0.0000  252 PHE D CB  
8672  C  CG  . PHE D  252 ? 0.1972 0.1213 0.1944 -0.0555 0.0130  0.0751  252 PHE D CG  
8673  C  CD1 . PHE D  252 ? 0.1919 0.1337 0.2795 -0.0606 -0.0057 0.0458  252 PHE D CD1 
8674  C  CD2 . PHE D  252 ? 0.2800 0.2578 0.2363 -0.0957 0.1055  0.1036  252 PHE D CD2 
8675  C  CE1 . PHE D  252 ? 0.2143 0.1606 0.3009 -0.0306 0.0031  -0.0204 252 PHE D CE1 
8676  C  CE2 . PHE D  252 ? 0.2612 0.2397 0.3047 -0.1048 -0.0452 0.2331  252 PHE D CE2 
8677  C  CZ  . PHE D  252 ? 0.2354 0.1097 0.2046 -0.0030 -0.0252 0.0153  252 PHE D CZ  
8678  N  N   . ASP D  253 ? 0.2381 0.2222 0.0833 -0.0579 0.0297  -0.0104 253 ASP D N   
8679  C  CA  . ASP D  253 ? 0.2413 0.2020 0.2467 -0.0747 0.1098  -0.0555 253 ASP D CA  
8680  C  C   . ASP D  253 ? 0.2027 0.3461 0.2106 -0.0653 0.0291  -0.0052 253 ASP D C   
8681  O  O   . ASP D  253 ? 0.3476 0.4873 0.1682 -0.0759 0.1121  -0.0326 253 ASP D O   
8682  C  CB  . ASP D  253 ? 0.2481 0.3501 0.2666 -0.0142 0.0943  0.0151  253 ASP D CB  
8683  C  CG  . ASP D  253 ? 0.3028 0.2170 0.1165 0.0961  0.0489  -0.0286 253 ASP D CG  
8684  O  OD1 . ASP D  253 ? 0.2851 0.3068 0.2468 0.0926  0.0529  0.0736  253 ASP D OD1 
8685  O  OD2 . ASP D  253 ? 0.2549 0.1951 0.1526 0.0441  -0.0066 -0.0406 253 ASP D OD2 
8686  N  N   . GLU D  254 ? 0.3912 0.3847 0.1427 -0.0732 -0.0256 0.0386  254 GLU D N   
8687  C  CA  . GLU D  254 ? 0.5266 0.2847 0.1969 -0.1607 -0.0868 0.0784  254 GLU D CA  
8688  C  C   . GLU D  254 ? 0.4093 0.4468 0.2132 -0.0872 -0.0230 0.0769  254 GLU D C   
8689  O  O   . GLU D  254 ? 0.5106 0.4063 0.2424 -0.1773 -0.0627 0.1077  254 GLU D O   
8690  C  CB  . GLU D  254 ? 0.7134 0.4131 0.1513 -0.0612 -0.0302 0.0071  254 GLU D CB  
8691  C  CG  . GLU D  254 ? 0.8137 0.8855 0.4158 0.1251  -0.1929 -0.2651 254 GLU D CG  
8692  C  CD  . GLU D  254 ? 0.6441 0.8348 1.1081 0.0478  -0.5139 -0.4438 254 GLU D CD  
8693  O  OE1 . GLU D  254 ? 1.9096 0.8810 2.0761 0.1301  0.0217  -0.6369 254 GLU D OE1 
8694  O  OE2 . GLU D  254 ? 1.0374 0.3111 1.4693 0.2804  -0.5275 -0.1958 254 GLU D OE2 
8695  N  N   . ARG D  255 ? 0.2764 0.3258 0.2483 -0.0038 0.0540  0.0153  255 ARG D N   
8696  C  CA  . ARG D  255 ? 0.2707 0.2221 0.1484 0.0120  0.0463  0.0073  255 ARG D CA  
8697  C  C   . ARG D  255 ? 0.2951 0.2592 0.2020 -0.0252 0.0606  -0.0540 255 ARG D C   
8698  O  O   . ARG D  255 ? 0.2759 0.4160 0.3052 0.0115  0.0706  -0.1257 255 ARG D O   
8699  C  CB  . ARG D  255 ? 0.3057 0.2443 0.1730 0.0681  0.0828  0.0408  255 ARG D CB  
8700  C  CG  . ARG D  255 ? 0.3603 0.2585 0.1842 0.0741  0.0702  0.0582  255 ARG D CG  
8701  C  CD  . ARG D  255 ? 0.4580 0.3364 0.0628 0.1359  0.0680  -0.0146 255 ARG D CD  
8702  N  NE  . ARG D  255 ? 0.2702 0.2648 0.1815 -0.0804 0.0091  0.0423  255 ARG D NE  
8703  C  CZ  . ARG D  255 ? 0.3420 0.2402 0.1698 0.0654  0.0225  0.0603  255 ARG D CZ  
8704  N  NH1 . ARG D  255 ? 0.2323 0.1181 0.1942 0.0052  -0.0043 0.0390  255 ARG D NH1 
8705  N  NH2 . ARG D  255 ? 0.2761 0.2396 0.1322 0.0820  0.0219  -0.0217 255 ARG D NH2 
8706  N  N   . LEU D  256 ? 0.3152 0.2599 0.1705 -0.0414 0.0553  -0.0103 256 LEU D N   
8707  C  CA  . LEU D  256 ? 0.2982 0.2054 0.1727 -0.0098 0.0149  0.0331  256 LEU D CA  
8708  C  C   . LEU D  256 ? 0.3395 0.1820 0.1161 0.0438  0.0265  0.0152  256 LEU D C   
8709  O  O   . LEU D  256 ? 0.3445 0.1615 0.2378 0.0097  -0.0131 -0.0217 256 LEU D O   
8710  C  CB  . LEU D  256 ? 0.4120 0.2632 0.1308 -0.0211 -0.0206 0.0121  256 LEU D CB  
8711  C  CG  . LEU D  256 ? 0.3964 0.3098 0.1480 0.0220  -0.0335 -0.0313 256 LEU D CG  
8712  C  CD1 . LEU D  256 ? 0.7473 0.3569 0.1646 0.0428  -0.0434 0.0597  256 LEU D CD1 
8713  C  CD2 . LEU D  256 ? 0.4004 0.4979 0.1748 0.1140  -0.0507 -0.0104 256 LEU D CD2 
8714  N  N   . VAL D  257 ? 0.2694 0.1860 0.1137 -0.0164 0.0339  0.0141  257 VAL D N   
8715  C  CA  . VAL D  257 ? 0.2165 0.1559 0.1177 0.0126  0.0331  0.0308  257 VAL D CA  
8716  C  C   . VAL D  257 ? 0.2023 0.1568 0.1331 0.0263  0.0333  0.0328  257 VAL D C   
8717  O  O   . VAL D  257 ? 0.2205 0.1766 0.1814 0.0659  0.0687  0.0764  257 VAL D O   
8718  C  CB  . VAL D  257 ? 0.2179 0.1675 0.1307 0.0091  0.0678  0.0259  257 VAL D CB  
8719  C  CG1 . VAL D  257 ? 0.2099 0.1685 0.1489 0.0040  0.0502  0.0126  257 VAL D CG1 
8720  C  CG2 . VAL D  257 ? 0.2371 0.1457 0.1550 -0.0186 0.0588  0.0143  257 VAL D CG2 
8721  N  N   . TYR D  258 ? 0.1895 0.1515 0.1185 0.0439  0.0568  0.0467  258 TYR D N   
8722  C  CA  . TYR D  258 ? 0.1944 0.1502 0.1306 0.0274  0.0601  0.0344  258 TYR D CA  
8723  C  C   . TYR D  258 ? 0.1728 0.1402 0.1365 0.0164  0.0467  0.0645  258 TYR D C   
8724  O  O   . TYR D  258 ? 0.2542 0.1504 0.1240 0.0255  0.0234  0.0675  258 TYR D O   
8725  C  CB  . TYR D  258 ? 0.2459 0.1660 0.1367 0.0381  0.0724  0.0209  258 TYR D CB  
8726  C  CG  . TYR D  258 ? 0.2843 0.1635 0.1457 0.0379  0.0921  0.0091  258 TYR D CG  
8727  C  CD1 . TYR D  258 ? 0.3472 0.2285 0.1263 0.0309  0.0496  0.0300  258 TYR D CD1 
8728  C  CD2 . TYR D  258 ? 0.3271 0.1642 0.1551 0.0430  0.0357  0.0015  258 TYR D CD2 
8729  C  CE1 . TYR D  258 ? 0.3472 0.2486 0.1671 0.0156  0.0652  -0.0024 258 TYR D CE1 
8730  C  CE2 . TYR D  258 ? 0.3704 0.2312 0.1930 0.0193  -0.0308 -0.0052 258 TYR D CE2 
8731  C  CZ  . TYR D  258 ? 0.3280 0.2253 0.1702 0.0066  0.0306  -0.0031 258 TYR D CZ  
8732  O  OH  . TYR D  258 ? 0.4652 0.2777 0.2167 -0.0445 0.0238  -0.0199 258 TYR D OH  
8733  N  N   . THR D  259 ? 0.1624 0.1405 0.1414 0.0305  0.0804  0.0472  259 THR D N   
8734  C  CA  . THR D  259 ? 0.1705 0.1240 0.1301 0.0326  0.0762  0.0659  259 THR D CA  
8735  C  C   . THR D  259 ? 0.1578 0.1446 0.1459 0.0505  0.0822  0.0619  259 THR D C   
8736  O  O   . THR D  259 ? 0.2134 0.1544 0.1278 0.0559  0.0821  0.0568  259 THR D O   
8737  C  CB  . THR D  259 ? 0.1671 0.1466 0.1306 0.0414  0.0689  0.0621  259 THR D CB  
8738  O  OG1 . THR D  259 ? 0.2145 0.1777 0.1468 0.0861  0.0851  0.0570  259 THR D OG1 
8739  C  CG2 . THR D  259 ? 0.1799 0.1791 0.1540 0.0317  0.0888  0.0560  259 THR D CG2 
8740  N  N   . SER D  260 ? 0.1756 0.1556 0.1292 0.0361  0.0966  0.0667  260 SER D N   
8741  C  CA  . SER D  260 ? 0.1865 0.2026 0.1570 0.0229  0.1152  0.0777  260 SER D CA  
8742  C  C   . SER D  260 ? 0.2441 0.1894 0.2181 0.0230  0.1519  0.1022  260 SER D C   
8743  O  O   . SER D  260 ? 0.2574 0.2212 0.3336 0.0166  0.1413  0.1493  260 SER D O   
8744  C  CB  . SER D  260 ? 0.2158 0.2254 0.1617 0.0653  0.1098  0.0813  260 SER D CB  
8745  O  OG  . SER D  260 ? 0.1897 0.1987 0.1662 0.0311  0.1107  0.0715  260 SER D OG  
8746  N  N   . PHE D  261 ? 0.2606 0.1294 0.2138 0.0310  0.1174  0.0603  261 PHE D N   
8747  C  CA  . PHE D  261 ? 0.2626 0.1466 0.2244 0.0280  0.0822  0.0811  261 PHE D CA  
8748  C  C   . PHE D  261 ? 0.3061 0.1515 0.2477 0.0080  0.0693  0.0892  261 PHE D C   
8749  O  O   . PHE D  261 ? 0.2849 0.1902 0.2314 0.0346  0.0674  0.1191  261 PHE D O   
8750  C  CB  . PHE D  261 ? 0.2448 0.1215 0.2265 0.0264  0.0807  0.0392  261 PHE D CB  
8751  C  CG  . PHE D  261 ? 0.2490 0.1206 0.1949 0.0465  0.0850  0.0270  261 PHE D CG  
8752  C  CD1 . PHE D  261 ? 0.2860 0.1642 0.2263 0.0703  0.1407  0.0861  261 PHE D CD1 
8753  C  CD2 . PHE D  261 ? 0.2824 0.1526 0.1292 0.0727  0.0888  0.0377  261 PHE D CD2 
8754  C  CE1 . PHE D  261 ? 0.2402 0.1861 0.2395 0.0364  0.0829  0.0879  261 PHE D CE1 
8755  C  CE2 . PHE D  261 ? 0.2485 0.1367 0.1675 0.0108  0.0727  -0.0231 261 PHE D CE2 
8756  C  CZ  . PHE D  261 ? 0.2362 0.1535 0.2111 -0.0035 0.0661  0.0370  261 PHE D CZ  
8757  N  N   . SER D  262 ? 0.5296 0.2070 0.6233 -0.0366 -0.0995 0.2307  262 SER D N   
8758  C  CA  . SER D  262 ? 0.6033 0.2158 0.6229 -0.0114 -0.1994 0.1406  262 SER D CA  
8759  C  C   . SER D  262 ? 0.8946 0.3785 1.0206 0.0366  -0.0331 0.0623  262 SER D C   
8760  O  O   . SER D  262 ? 1.1126 0.5120 0.8342 0.1464  0.2299  0.0417  262 SER D O   
8761  C  CB  . SER D  262 ? 0.9233 0.4947 0.5839 0.2847  -0.0399 0.1513  262 SER D CB  
8762  O  OG  . SER D  262 ? 1.3363 0.4234 0.4146 0.3621  -0.3030 -0.0643 262 SER D OG  
8763  N  N   . GLN D  263 ? 0.7167 0.2212 1.3944 -0.0441 0.0223  0.2734  263 GLN D N   
8764  C  CA  . GLN D  263 ? 0.7962 0.5842 1.3811 0.3003  -0.1211 0.0675  263 GLN D CA  
8765  C  CB  . GLN D  263 ? 1.3411 0.2509 1.5411 -0.1744 -0.4259 0.5838  263 GLN D CB  
8766  C  CG  . GLN D  263 ? 1.2115 0.4767 1.4378 0.3490  -0.1808 -0.0833 263 GLN D CG  
8767  C  CD  . GLN D  263 ? 0.9610 0.5238 0.8970 0.1878  -0.0675 0.2237  263 GLN D CD  
8768  O  OE1 . GLN D  263 ? 0.5986 0.5788 0.8364 -0.1352 0.0463  0.3217  263 GLN D OE1 
8769  N  NE2 . GLN D  263 ? 0.5426 0.6869 1.0336 -0.3172 -0.1509 0.4826  263 GLN D NE2 
8770  ZN ZN  . ZN  E  .   ? 0.0883 0.1055 0.1057 0.0035  0.0100  0.0252  301 ZN  A ZN  
8771  F  F18 A 3TV F  .   ? 0.1294 0.1834 0.2754 -0.0612 0.0353  0.0697  302 3TV A F18 
8772  F  F18 B 3TV F  .   ? 0.2899 0.4180 0.2978 0.0063  0.0121  0.0737  302 3TV A F18 
8773  C  C7  A 3TV F  .   ? 0.1256 0.1321 0.1791 -0.0292 -0.0152 0.0940  302 3TV A C7  
8774  C  C7  B 3TV F  .   ? 0.2578 0.1470 0.2919 -0.0303 0.0320  -0.0200 302 3TV A C7  
8775  C  C6  A 3TV F  .   ? 0.1382 0.1423 0.1795 -0.0222 0.0008  0.0366  302 3TV A C6  
8776  C  C6  B 3TV F  .   ? 0.1633 0.1994 0.2143 -0.0247 0.0308  0.0212  302 3TV A C6  
8777  F  F17 A 3TV F  .   ? 0.1464 0.1425 0.1903 -0.0193 0.0443  0.0305  302 3TV A F17 
8778  F  F17 B 3TV F  .   ? 0.1635 0.2486 0.1956 -0.0125 0.0529  0.0295  302 3TV A F17 
8779  C  C8  A 3TV F  .   ? 0.1750 0.1975 0.1773 -0.1110 -0.0640 0.0615  302 3TV A C8  
8780  C  C8  B 3TV F  .   ? 0.4259 0.3978 0.1689 -0.0318 0.0544  -0.0027 302 3TV A C8  
8781  S  S11 A 3TV F  .   ? 0.3835 0.2436 0.3143 -0.2136 -0.0734 0.0570  302 3TV A S11 
8782  S  S11 B 3TV F  .   ? 0.4882 0.6564 0.7727 -0.0259 -0.0496 -0.2515 302 3TV A S11 
8783  C  C12 A 3TV F  .   ? 0.2565 0.3833 0.4241 -0.2182 -0.0505 0.0632  302 3TV A C12 
8784  C  C12 B 3TV F  .   ? 0.2526 0.3637 0.2161 -0.2702 -0.0577 0.1238  302 3TV A C12 
8785  C  C13 A 3TV F  .   ? 0.1376 0.4730 0.5842 -0.1186 0.0882  0.0133  302 3TV A C13 
8786  C  C13 B 3TV F  .   ? 0.2944 0.4126 0.3452 -0.3027 -0.0408 0.0675  302 3TV A C13 
8787  C  C14 A 3TV F  .   ? 0.4223 0.3939 0.3562 -0.3201 -0.0690 0.0474  302 3TV A C14 
8788  C  C14 B 3TV F  .   ? 0.5322 0.3133 0.2578 -0.0092 -0.2149 0.0962  302 3TV A C14 
8789  C  C9  A 3TV F  .   ? 0.1967 0.1870 0.1933 -0.0675 -0.0439 0.0597  302 3TV A C9  
8790  C  C9  B 3TV F  .   ? 0.2899 0.2398 0.1658 -0.0579 -0.0522 0.0251  302 3TV A C9  
8791  F  F15 A 3TV F  .   ? 0.4361 0.3472 0.2002 0.0288  -0.0675 0.0417  302 3TV A F15 
8792  F  F15 B 3TV F  .   ? 0.3463 0.1969 0.2300 -0.1456 -0.0355 -0.0307 302 3TV A F15 
8793  C  C10 A 3TV F  .   ? 0.1456 0.1673 0.2055 -0.0305 -0.0230 -0.0034 302 3TV A C10 
8794  C  C10 B 3TV F  .   ? 0.2089 0.1622 0.2235 -0.0194 0.0315  0.0628  302 3TV A C10 
8795  F  F16 A 3TV F  .   ? 0.2728 0.1738 0.1802 0.0671  -0.0227 0.0062  302 3TV A F16 
8796  F  F16 B 3TV F  .   ? 0.3483 0.4023 0.2976 -0.2161 0.0866  -0.0472 302 3TV A F16 
8797  C  C5  A 3TV F  .   ? 0.1001 0.1297 0.1656 -0.0250 -0.0127 0.0306  302 3TV A C5  
8798  C  C5  B 3TV F  .   ? 0.1477 0.1204 0.1773 -0.0154 0.0005  0.0843  302 3TV A C5  
8799  S  S1  A 3TV F  .   ? 0.1000 0.1154 0.1231 -0.0019 -0.0040 0.0390  302 3TV A S1  
8800  S  S1  B 3TV F  .   ? 0.1003 0.1730 0.1294 0.0031  0.0104  0.0619  302 3TV A S1  
8801  O  O3  A 3TV F  .   ? 0.0800 0.1614 0.1342 -0.0027 -0.0153 0.0408  302 3TV A O3  
8802  O  O3  B 3TV F  .   ? 0.0980 0.1917 0.1215 0.0153  0.0357  0.0736  302 3TV A O3  
8803  O  O4  A 3TV F  .   ? 0.1237 0.1012 0.1256 -0.0023 0.0077  0.0344  302 3TV A O4  
8804  O  O4  B 3TV F  .   ? 0.0626 0.1648 0.1461 -0.0200 0.0041  0.0617  302 3TV A O4  
8805  N  N2  A 3TV F  .   ? 0.0728 0.1213 0.1644 0.0096  -0.0082 0.0412  302 3TV A N2  
8806  N  N2  B 3TV F  .   ? 0.1395 0.1545 0.0818 -0.0115 0.0137  0.0824  302 3TV A N2  
8807  C  C1  . EDO G  .   ? 0.3267 0.3014 0.2802 -0.0744 0.0199  -0.0226 303 EDO A C1  
8808  O  O1  . EDO G  .   ? 0.2887 0.3066 0.4654 -0.1089 -0.0551 0.0187  303 EDO A O1  
8809  C  C2  . EDO G  .   ? 0.4343 0.4995 0.3129 -0.0148 0.1358  -0.0746 303 EDO A C2  
8810  O  O2  . EDO G  .   ? 0.2046 0.2815 0.3510 -0.0626 -0.0078 -0.0201 303 EDO A O2  
8811  C  C1  . EDO H  .   ? 0.8859 0.8884 0.4986 0.0130  -0.3070 0.0772  304 EDO A C1  
8812  O  O1  . EDO H  .   ? 0.9318 0.4457 0.4363 -0.3582 -0.1882 0.1626  304 EDO A O1  
8813  C  C2  . EDO H  .   ? 0.5325 0.3729 0.8659 0.2157  0.0252  -0.0560 304 EDO A C2  
8814  O  O2  . EDO H  .   ? 0.4104 0.5141 0.6337 0.1288  0.2069  0.1862  304 EDO A O2  
8815  C  C1  . EDO I  .   ? 0.2583 0.5979 0.3481 -0.0348 -0.0504 0.0710  305 EDO A C1  
8816  O  O1  . EDO I  .   ? 0.2684 0.5827 0.2768 -0.0203 -0.0242 0.0038  305 EDO A O1  
8817  C  C2  . EDO I  .   ? 0.3364 0.4766 0.2127 0.0310  -0.0293 0.0296  305 EDO A C2  
8818  O  O2  . EDO I  .   ? 0.3585 0.5268 0.1693 0.0846  0.0295  -0.0020 305 EDO A O2  
8819  C  C1  . PEG J  .   ? 0.5200 0.3262 0.5182 0.0795  0.0414  0.0891  306 PEG A C1  
8820  O  O1  . PEG J  .   ? 0.3898 0.2737 0.3781 -0.0108 0.0017  0.1494  306 PEG A O1  
8821  C  C2  . PEG J  .   ? 1.0484 0.3368 0.3849 -0.2207 0.0562  0.1607  306 PEG A C2  
8822  O  O2  . PEG J  .   ? 0.5975 0.4620 0.6305 -0.0288 0.1120  0.0043  306 PEG A O2  
8823  C  C3  . PEG J  .   ? 0.4977 0.2554 0.2601 0.0913  -0.0028 0.0825  306 PEG A C3  
8824  C  C4  . PEG J  .   ? 0.4813 0.6177 0.8335 0.1142  0.0133  0.4377  306 PEG A C4  
8825  O  O4  . PEG J  .   ? 0.3334 1.0650 0.6704 0.0296  -0.0076 0.5770  306 PEG A O4  
8826  C  C1  . EDO K  .   ? 0.2818 0.2971 0.2712 -0.0105 -0.0087 0.0221  307 EDO A C1  
8827  O  O1  . EDO K  .   ? 0.4115 0.3648 0.3914 -0.0027 -0.0031 0.0205  307 EDO A O1  
8828  C  C2  . EDO K  .   ? 0.3201 0.3226 0.3677 -0.0126 0.0129  -0.0206 307 EDO A C2  
8829  O  O2  . EDO K  .   ? 0.3034 0.2894 0.3068 -0.0208 -0.0127 0.0185  307 EDO A O2  
8830  C  C1  . EDO L  .   ? 0.3815 0.3713 0.3549 -0.0142 0.0405  -0.0115 308 EDO A C1  
8831  O  O1  . EDO L  .   ? 0.4004 0.4124 0.4464 0.0142  0.0227  0.0024  308 EDO A O1  
8832  C  C2  . EDO L  .   ? 0.3429 0.3616 0.3341 -0.0068 -0.0054 0.0141  308 EDO A C2  
8833  O  O2  . EDO L  .   ? 0.3659 0.3835 0.3941 0.0017  -0.0060 0.0078  308 EDO A O2  
8834  C  C1  . EDO M  .   ? 0.2522 0.2874 0.2540 -0.0137 0.0375  0.0274  309 EDO A C1  
8835  O  O1  . EDO M  .   ? 0.3046 0.3075 0.3134 -0.0217 0.0205  0.0118  309 EDO A O1  
8836  C  C2  . EDO M  .   ? 0.2806 0.3364 0.3125 0.0186  -0.0030 0.0198  309 EDO A C2  
8837  O  O2  . EDO M  .   ? 0.3262 0.3598 0.3486 0.0164  -0.0283 -0.0035 309 EDO A O2  
8838  C  C1  . EDO N  .   ? 0.3355 0.3283 0.3226 -0.0425 0.0162  -0.0051 310 EDO A C1  
8839  O  O1  . EDO N  .   ? 0.2842 0.3217 0.2551 0.0005  0.0152  -0.0041 310 EDO A O1  
8840  C  C2  . EDO N  .   ? 0.3156 0.3152 0.3395 -0.0353 -0.0052 -0.0259 310 EDO A C2  
8841  O  O2  . EDO N  .   ? 0.3346 0.3407 0.3603 0.0027  -0.0082 0.0062  310 EDO A O2  
8842  ZN ZN  . ZN  O  .   ? 0.0788 0.0683 0.0841 0.0024  0.0293  0.0030  301 ZN  B ZN  
8843  F  F18 A 3TV P  .   ? 0.1565 0.0878 0.1942 0.0236  0.0272  0.0214  302 3TV B F18 
8844  F  F18 B 3TV P  .   ? 0.4201 0.2714 0.2148 0.1850  0.0931  0.1058  302 3TV B F18 
8845  C  C7  A 3TV P  .   ? 0.1226 0.0822 0.1814 0.0441  -0.0003 -0.0295 302 3TV B C7  
8846  C  C7  B 3TV P  .   ? 0.2599 0.1911 0.1962 0.0838  0.0364  0.0623  302 3TV B C7  
8847  C  C6  A 3TV P  .   ? 0.0962 0.0791 0.1509 0.0386  0.0126  -0.0232 302 3TV B C6  
8848  C  C6  B 3TV P  .   ? 0.2475 0.1213 0.1796 0.0080  -0.0247 0.0496  302 3TV B C6  
8849  F  F17 A 3TV P  .   ? 0.0832 0.0669 0.1712 0.0099  0.0304  0.0188  302 3TV B F17 
8850  F  F17 B 3TV P  .   ? 0.4442 0.4005 0.1552 0.0307  -0.0007 0.0120  302 3TV B F17 
8851  C  C8  A 3TV P  .   ? 0.1341 0.0795 0.2190 0.0482  -0.0524 -0.0483 302 3TV B C8  
8852  C  C8  B 3TV P  .   ? 0.2165 0.1456 0.2849 0.0601  0.0511  0.0340  302 3TV B C8  
8853  S  S11 A 3TV P  .   ? 0.2017 0.1023 0.2919 0.0445  0.0071  0.0131  302 3TV B S11 
8854  S  S11 B 3TV P  .   ? 0.4255 0.2389 0.3738 0.1750  0.0480  0.0780  302 3TV B S11 
8855  C  C12 A 3TV P  .   ? 0.2247 0.1387 0.2239 0.0834  0.0140  -0.0502 302 3TV B C12 
8856  C  C12 B 3TV P  .   ? 0.3046 0.5249 0.5927 0.0615  -0.0648 -0.0513 302 3TV B C12 
8857  C  C13 A 3TV P  .   ? 0.2267 0.1137 0.2371 0.0659  0.0430  -0.0302 302 3TV B C13 
8858  C  C13 B 3TV P  .   ? 0.5141 0.3867 0.4812 0.1022  -0.1066 0.1181  302 3TV B C13 
8859  C  C14 A 3TV P  .   ? 0.2449 0.2236 0.2992 0.0357  0.0392  -0.1239 302 3TV B C14 
8860  C  C14 B 3TV P  .   ? 0.4988 0.5394 0.6159 0.1730  -0.0085 -0.0542 302 3TV B C14 
8861  C  C9  A 3TV P  .   ? 0.1059 0.1332 0.1671 0.0401  -0.0304 -0.0318 302 3TV B C9  
8862  C  C9  B 3TV P  .   ? 0.1203 0.1430 0.2477 0.0238  0.0342  -0.0051 302 3TV B C9  
8863  F  F15 A 3TV P  .   ? 0.1068 0.1405 0.4038 0.0438  -0.0155 -0.0662 302 3TV B F15 
8864  F  F15 B 3TV P  .   ? 0.2150 0.1763 0.4694 0.0640  0.1573  -0.0136 302 3TV B F15 
8865  C  C10 A 3TV P  .   ? 0.0617 0.1059 0.2407 0.0188  -0.0397 -0.0649 302 3TV B C10 
8866  C  C10 B 3TV P  .   ? 0.1799 0.1448 0.1353 0.0179  -0.0136 0.0148  302 3TV B C10 
8867  F  F16 A 3TV P  .   ? 0.0868 0.1288 0.3303 0.0196  0.0092  -0.0564 302 3TV B F16 
8868  F  F16 B 3TV P  .   ? 0.2324 0.1457 0.2021 0.0559  0.0930  0.0031  302 3TV B F16 
8869  C  C5  A 3TV P  .   ? 0.0562 0.1064 0.1680 0.0326  0.0278  -0.0447 302 3TV B C5  
8870  C  C5  B 3TV P  .   ? 0.1615 0.1436 0.1371 0.0082  -0.0241 0.0041  302 3TV B C5  
8871  S  S1  A 3TV P  .   ? 0.0931 0.1054 0.1177 0.0200  0.0199  -0.0331 302 3TV B S1  
8872  S  S1  B 3TV P  .   ? 0.0960 0.1251 0.1437 -0.0049 0.0163  -0.0344 302 3TV B S1  
8873  O  O3  A 3TV P  .   ? 0.0908 0.1896 0.2055 -0.0269 0.0222  -0.0516 302 3TV B O3  
8874  O  O3  B 3TV P  .   ? 0.0924 0.1324 0.1014 -0.0116 0.0518  -0.0535 302 3TV B O3  
8875  O  O4  A 3TV P  .   ? 0.0868 0.1098 0.1383 0.0181  0.0148  -0.0370 302 3TV B O4  
8876  O  O4  B 3TV P  .   ? 0.0983 0.0949 0.1308 0.0000  0.0201  -0.0192 302 3TV B O4  
8877  N  N2  A 3TV P  .   ? 0.0988 0.0782 0.1265 0.0010  0.0174  -0.0714 302 3TV B N2  
8878  N  N2  B 3TV P  .   ? 0.0854 0.1762 0.1133 0.0118  0.0265  0.0203  302 3TV B N2  
8879  C  C1  . EDO Q  .   ? 0.3810 0.3824 0.3731 -0.1218 0.1356  0.0146  303 EDO B C1  
8880  O  O1  . EDO Q  .   ? 0.2922 0.4138 0.2872 -0.0044 0.0663  -0.0027 303 EDO B O1  
8881  C  C2  . EDO Q  .   ? 0.2032 0.4422 0.4126 0.0209  0.1675  0.0463  303 EDO B C2  
8882  O  O2  . EDO Q  .   ? 0.1998 0.2202 0.1624 0.0253  0.0724  0.0318  303 EDO B O2  
8883  C  C1  . PEG R  .   ? 0.8004 0.7574 0.7807 0.0729  -0.0568 -0.1387 304 PEG B C1  
8884  O  O1  . PEG R  .   ? 0.3370 0.7253 0.7432 0.0800  -0.1182 -0.4406 304 PEG B O1  
8885  C  C2  . PEG R  .   ? 0.3625 0.3492 0.6413 -0.0403 -0.1339 -0.0209 304 PEG B C2  
8886  O  O2  . PEG R  .   ? 0.4106 0.6908 0.6661 0.1316  -0.2064 0.0288  304 PEG B O2  
8887  C  C3  . PEG R  .   ? 0.3860 0.1316 0.4133 0.0573  -0.1242 0.0237  304 PEG B C3  
8888  C  C4  . PEG R  .   ? 0.2737 0.2635 0.4025 0.1044  -0.0208 -0.0980 304 PEG B C4  
8889  O  O4  . PEG R  .   ? 0.5910 0.1847 0.5910 -0.1207 -0.1168 0.0148  304 PEG B O4  
8890  C  C1  . CIT S  .   ? 0.3007 0.2964 0.1351 0.0399  0.0636  -0.0533 305 CIT B C1  
8891  O  O1  . CIT S  .   ? 0.5479 0.3540 0.3111 0.0516  -0.0204 0.0436  305 CIT B O1  
8892  O  O2  . CIT S  .   ? 0.3653 0.4837 0.4582 -0.0206 -0.0335 0.0161  305 CIT B O2  
8893  C  C2  . CIT S  .   ? 0.1560 0.2183 0.1809 0.0546  0.0089  -0.0419 305 CIT B C2  
8894  C  C3  . CIT S  .   ? 0.2684 0.3625 0.2264 0.0263  -0.0392 0.0335  305 CIT B C3  
8895  O  O7  . CIT S  .   ? 0.3964 0.4842 0.4734 0.0639  -0.0028 0.0104  305 CIT B O7  
8896  C  C4  . CIT S  .   ? 0.2976 0.3348 0.2479 0.0406  -0.0439 0.0249  305 CIT B C4  
8897  C  C5  . CIT S  .   ? 0.2732 0.0918 0.2937 0.0060  -0.0174 -0.0606 305 CIT B C5  
8898  O  O3  . CIT S  .   ? 0.3754 0.4183 0.5598 0.1080  -0.0294 -0.0542 305 CIT B O3  
8899  O  O4  . CIT S  .   ? 0.2815 0.1055 0.3828 0.0024  -0.0416 -0.0386 305 CIT B O4  
8900  C  C6  . CIT S  .   ? 0.3003 0.3587 0.2912 0.0900  -0.0120 0.0838  305 CIT B C6  
8901  O  O5  . CIT S  .   ? 0.3100 0.1931 0.3483 0.0020  -0.0740 0.1074  305 CIT B O5  
8902  O  O6  . CIT S  .   ? 0.5066 0.5737 0.3037 -0.0507 -0.0368 0.0997  305 CIT B O6  
8903  ZN ZN  . ZN  T  .   ? 0.1574 0.2113 0.0712 -0.0432 0.0017  -0.0093 301 ZN  C ZN  
8904  F  F18 . 3TV U  .   ? 0.4052 0.3206 0.1583 -0.1418 0.0105  -0.0516 302 3TV C F18 
8905  C  C7  . 3TV U  .   ? 0.3289 0.2869 0.1129 -0.1312 -0.0049 -0.0458 302 3TV C C7  
8906  C  C6  . 3TV U  .   ? 0.1946 0.2046 0.1317 -0.0405 0.0083  -0.0108 302 3TV C C6  
8907  F  F17 . 3TV U  .   ? 0.2630 0.2779 0.1278 -0.0287 -0.0092 -0.0284 302 3TV C F17 
8908  C  C8  . 3TV U  .   ? 0.2599 0.3095 0.1770 -0.1472 -0.0395 -0.0439 302 3TV C C8  
8909  S  S11 . 3TV U  .   ? 0.4934 0.4555 0.3382 -0.3005 0.1018  -0.1781 302 3TV C S11 
8910  C  C12 . 3TV U  .   ? 0.5936 0.4627 0.2305 -0.0736 0.0467  -0.1499 302 3TV C C12 
8911  C  C13 . 3TV U  .   ? 0.6308 0.4823 0.4343 0.0467  0.1588  0.0370  302 3TV C C13 
8912  C  C14 . 3TV U  .   ? 0.4000 0.5708 0.3208 -0.1351 0.0152  0.0549  302 3TV C C14 
8913  C  C9  . 3TV U  .   ? 0.2080 0.2154 0.1687 -0.0825 0.0200  -0.0377 302 3TV C C9  
8914  F  F15 . 3TV U  .   ? 0.2177 0.2319 0.2177 -0.0798 0.0109  0.0135  302 3TV C F15 
8915  C  C10 . 3TV U  .   ? 0.1840 0.2213 0.1335 -0.0584 0.0226  -0.0256 302 3TV C C10 
8916  F  F16 . 3TV U  .   ? 0.1836 0.2145 0.1457 -0.0480 0.0342  -0.0308 302 3TV C F16 
8917  C  C5  . 3TV U  .   ? 0.1565 0.2348 0.0885 -0.0329 -0.0055 -0.0094 302 3TV C C5  
8918  S  S1  . 3TV U  .   ? 0.1518 0.1750 0.0913 -0.0152 -0.0006 -0.0027 302 3TV C S1  
8919  O  O3  . 3TV U  .   ? 0.1924 0.1939 0.0777 -0.0421 -0.0171 0.0133  302 3TV C O3  
8920  O  O4  . 3TV U  .   ? 0.1340 0.1676 0.1080 -0.0178 0.0023  -0.0164 302 3TV C O4  
8921  N  N2  . 3TV U  .   ? 0.1556 0.1612 0.0886 -0.0209 0.0082  0.0065  302 3TV C N2  
8922  C  C1  . EDO V  .   ? 0.3118 0.1511 0.2538 0.0199  -0.0135 -0.0408 303 EDO C C1  
8923  O  O1  . EDO V  .   ? 0.3025 0.2208 0.2630 0.0052  -0.0557 -0.0148 303 EDO C O1  
8924  C  C2  . EDO V  .   ? 0.3591 0.2721 0.2294 -0.0825 -0.0201 0.0116  303 EDO C C2  
8925  O  O2  . EDO V  .   ? 0.2605 0.3034 0.2389 -0.0666 -0.0696 0.0020  303 EDO C O2  
8926  C  C1  . PEG W  .   ? 0.4705 0.2163 0.4569 0.0925  -0.0005 -0.0304 304 PEG C C1  
8927  O  O1  . PEG W  .   ? 0.3425 0.3382 1.3004 -0.0636 0.1380  -0.2978 304 PEG C O1  
8928  C  C2  . PEG W  .   ? 0.4979 0.1461 0.4034 0.1835  0.0059  0.0185  304 PEG C C2  
8929  O  O2  . PEG W  .   ? 0.4806 0.7168 0.6934 -0.0595 -0.0483 -0.0728 304 PEG C O2  
8930  C  C3  . PEG W  .   ? 0.3547 0.1560 0.5767 -0.0505 0.0130  -0.0898 304 PEG C C3  
8931  C  C4  . PEG W  .   ? 0.3447 0.4040 0.9979 0.0190  -0.2154 -0.1365 304 PEG C C4  
8932  O  O4  . PEG W  .   ? 0.8465 0.2944 0.8887 0.0560  -0.5002 -0.0712 304 PEG C O4  
8933  C  C1  . EDO X  .   ? 0.3479 0.3465 0.3765 0.0231  0.0146  0.0176  305 EDO C C1  
8934  O  O1  . EDO X  .   ? 0.3449 0.3564 0.3352 0.0181  -0.0041 0.0040  305 EDO C O1  
8935  C  C2  . EDO X  .   ? 0.3323 0.3255 0.2732 -0.0006 -0.0031 0.0152  305 EDO C C2  
8936  O  O2  . EDO X  .   ? 0.3524 0.3533 0.2922 -0.0115 0.0046  0.0108  305 EDO C O2  
8937  ZN ZN  . ZN  Y  .   ? 0.1133 0.0719 0.0784 -0.0020 0.0421  -0.0043 301 ZN  D ZN  
8938  F  F18 A 3TV Z  .   ? 0.1730 0.1027 0.1601 0.0675  0.0553  0.0030  302 3TV D F18 
8939  F  F18 B 3TV Z  .   ? 0.3183 0.4120 0.1940 -0.0910 -0.0773 0.0993  302 3TV D F18 
8940  C  C7  A 3TV Z  .   ? 0.1190 0.0797 0.1401 0.0412  0.0337  0.0017  302 3TV D C7  
8941  C  C7  B 3TV Z  .   ? 0.3813 0.2964 0.2463 0.0183  -0.2466 0.0153  302 3TV D C7  
8942  C  C6  A 3TV Z  .   ? 0.1045 0.0728 0.1042 0.0283  0.0296  0.0082  302 3TV D C6  
8943  C  C6  B 3TV Z  .   ? 0.1773 0.2784 0.4047 0.0450  -0.0852 -0.0579 302 3TV D C6  
8944  F  F17 A 3TV Z  .   ? 0.1708 0.0628 0.1305 0.0357  0.0829  -0.0013 302 3TV D F17 
8945  F  F17 B 3TV Z  .   ? 0.2858 0.2066 0.3145 0.0535  0.0173  -0.0368 302 3TV D F17 
8946  C  C8  A 3TV Z  .   ? 0.1553 0.0754 0.1872 0.0263  0.0458  0.0242  302 3TV D C8  
8947  C  C8  B 3TV Z  .   ? 0.2472 0.2741 0.2711 0.0980  -0.0756 -0.0781 302 3TV D C8  
8948  S  S11 A 3TV Z  .   ? 0.3030 0.1195 0.3422 0.0749  0.0171  0.0637  302 3TV D S11 
8949  S  S11 B 3TV Z  .   ? 0.4079 0.2908 0.8611 0.0989  -0.2476 -0.1066 302 3TV D S11 
8950  C  C12 A 3TV Z  .   ? 0.3612 0.0879 0.1635 0.0154  0.1831  -0.0282 302 3TV D C12 
8951  C  C12 B 3TV Z  .   ? 0.3912 0.4041 0.3427 -0.2345 0.0728  -0.0161 302 3TV D C12 
8952  C  C13 A 3TV Z  .   ? 0.4742 0.2078 0.4548 0.0546  0.1176  0.1876  302 3TV D C13 
8953  C  C13 B 3TV Z  .   ? 0.2400 0.1350 0.3341 0.0185  0.0096  0.0081  302 3TV D C13 
8954  C  C14 A 3TV Z  .   ? 0.6869 0.4316 0.2185 0.0333  0.1471  0.0373  302 3TV D C14 
8955  C  C14 B 3TV Z  .   ? 0.2917 0.2989 0.2305 0.0031  0.1412  -0.0825 302 3TV D C14 
8956  C  C9  A 3TV Z  .   ? 0.1852 0.0583 0.1335 -0.0083 0.0331  0.0331  302 3TV D C9  
8957  C  C9  B 3TV Z  .   ? 0.2276 0.2177 0.1475 0.0531  -0.0048 -0.0520 302 3TV D C9  
8958  F  F15 A 3TV Z  .   ? 0.3185 0.1272 0.1123 0.0296  0.0000  0.0502  302 3TV D F15 
8959  F  F15 B 3TV Z  .   ? 0.2851 0.2583 0.2019 0.0278  0.0463  0.0201  302 3TV D F15 
8960  C  C10 A 3TV Z  .   ? 0.1391 0.0548 0.0966 -0.0187 0.0113  0.0206  302 3TV D C10 
8961  C  C10 B 3TV Z  .   ? 0.2208 0.2177 0.2326 0.0663  0.0024  -0.0249 302 3TV D C10 
8962  F  F16 A 3TV Z  .   ? 0.2806 0.1921 0.0953 0.0122  0.0423  0.0250  302 3TV D F16 
8963  F  F16 B 3TV Z  .   ? 0.2084 0.1781 0.1833 0.0175  0.0423  0.0241  302 3TV D F16 
8964  C  C5  A 3TV Z  .   ? 0.1263 0.0944 0.0685 -0.0085 0.0366  0.0026  302 3TV D C5  
8965  C  C5  B 3TV Z  .   ? 0.1772 0.1520 0.2242 0.0732  0.0291  -0.0789 302 3TV D C5  
8966  S  S1  A 3TV Z  .   ? 0.1254 0.0944 0.0926 0.0071  0.0370  -0.0186 302 3TV D S1  
8967  S  S1  B 3TV Z  .   ? 0.1527 0.1238 0.1225 -0.0065 0.0375  -0.0414 302 3TV D S1  
8968  O  O3  A 3TV Z  .   ? 0.1644 0.0854 0.0979 -0.0021 0.0416  -0.0430 302 3TV D O3  
8969  O  O3  B 3TV Z  .   ? 0.1337 0.1585 0.1574 0.0052  0.0697  -0.0388 302 3TV D O3  
8970  O  O4  A 3TV Z  .   ? 0.1328 0.0940 0.1052 0.0135  0.0286  -0.0263 302 3TV D O4  
8971  O  O4  B 3TV Z  .   ? 0.1685 0.1310 0.1147 0.0054  0.0485  -0.0487 302 3TV D O4  
8972  N  N2  A 3TV Z  .   ? 0.1622 0.1337 0.0755 -0.0060 0.0456  -0.0384 302 3TV D N2  
8973  N  N2  B 3TV Z  .   ? 0.1268 0.0431 0.1360 0.0078  0.0190  -0.0413 302 3TV D N2  
8974  C  C1  . PEG AA .   ? 0.7566 0.8815 0.6557 -0.1331 0.0750  -0.1859 303 PEG D C1  
8975  O  O1  . PEG AA .   ? 0.5871 1.0865 0.9861 -0.0944 0.2878  0.2937  303 PEG D O1  
8976  C  C2  . PEG AA .   ? 0.8183 0.9593 0.4977 -0.0225 0.1792  0.0753  303 PEG D C2  
8977  O  O2  . PEG AA .   ? 0.5988 1.2093 0.5224 -0.1820 0.1834  -0.3185 303 PEG D O2  
8978  C  C3  . PEG AA .   ? 0.3138 0.3734 0.6248 0.0785  -0.0627 -0.3777 303 PEG D C3  
8979  C  C4  . PEG AA .   ? 0.6665 0.6406 0.5620 -0.0401 0.1217  0.1111  303 PEG D C4  
8980  O  O4  . PEG AA .   ? 1.1979 0.3871 0.5778 0.1844  -0.0366 -0.0417 303 PEG D O4  
8981  C  C1  . CIT BA .   ? 1.2653 0.5449 0.1951 0.1527  -0.0373 0.1036  304 CIT D C1  
8982  O  O1  . CIT BA .   ? 1.1660 1.3404 0.5131 0.2515  -0.2419 0.0623  304 CIT D O1  
8983  O  O2  . CIT BA .   ? 1.8747 0.5016 1.8415 -0.2874 -0.5076 0.0817  304 CIT D O2  
8984  C  C2  . CIT BA .   ? 0.6158 0.6615 0.3370 0.0881  0.0403  -0.1280 304 CIT D C2  
8985  C  C3  . CIT BA .   ? 0.4192 0.2876 0.2361 0.1534  0.0170  -0.0081 304 CIT D C3  
8986  O  O7  . CIT BA .   ? 1.1591 0.3673 0.9636 0.2944  -0.0599 -0.0362 304 CIT D O7  
8987  C  C4  . CIT BA .   ? 0.5859 0.3903 0.4695 0.0105  0.0772  -0.0621 304 CIT D C4  
8988  C  C5  . CIT BA .   ? 0.2852 0.2793 0.5731 0.0441  0.0197  0.0320  304 CIT D C5  
8989  O  O3  . CIT BA .   ? 0.7846 0.7955 0.9218 0.1096  -0.3499 0.1571  304 CIT D O3  
8990  O  O4  . CIT BA .   ? 0.3158 0.3790 0.2743 0.0885  0.1096  0.1077  304 CIT D O4  
8991  C  C6  . CIT BA .   ? 0.5738 0.4444 0.3880 0.0852  -0.1600 0.0621  304 CIT D C6  
8992  O  O5  . CIT BA .   ? 1.0647 0.5116 0.7307 -0.2296 0.0649  -0.0449 304 CIT D O5  
8993  O  O6  . CIT BA .   ? 0.3264 0.1204 0.1716 0.0239  0.0538  -0.0133 304 CIT D O6  
8994  C  C1  . EDO CA .   ? 1.0509 0.6826 0.4273 0.0060  -0.1079 -0.1684 305 EDO D C1  
8995  O  O1  . EDO CA .   ? 1.1506 0.3734 0.2727 0.2211  -0.0196 -0.0966 305 EDO D O1  
8996  C  C2  . EDO CA .   ? 0.7764 0.4377 0.3328 -0.2340 0.0698  -0.0851 305 EDO D C2  
8997  O  O2  . EDO CA .   ? 0.5710 0.3224 0.3761 -0.1521 -0.0005 0.0394  305 EDO D O2  
8998  C  C1  . CIT DA .   ? 0.3346 0.2712 0.3253 0.0527  0.1545  -0.0416 306 CIT D C1  
8999  O  O1  . CIT DA .   ? 0.3213 0.3194 0.5292 -0.0619 0.0961  -0.0912 306 CIT D O1  
9000  O  O2  . CIT DA .   ? 0.4047 0.2655 0.3332 0.0958  0.0441  0.0364  306 CIT D O2  
9001  C  C2  . CIT DA .   ? 0.1365 0.2167 0.1953 0.0606  0.0551  -0.0370 306 CIT D C2  
9002  C  C3  . CIT DA .   ? 0.3637 0.3528 0.2351 -0.0032 -0.0082 0.0057  306 CIT D C3  
9003  O  O7  . CIT DA .   ? 0.4645 0.4458 0.4989 0.1120  0.0891  0.0410  306 CIT D O7  
9004  C  C4  . CIT DA .   ? 0.2910 0.3930 0.3802 -0.0093 0.0753  -0.0182 306 CIT D C4  
9005  C  C5  . CIT DA .   ? 0.2637 0.0757 0.2353 -0.0102 0.0181  -0.0471 306 CIT D C5  
9006  O  O3  . CIT DA .   ? 0.3885 0.4461 0.4655 0.0640  -0.0331 -0.0093 306 CIT D O3  
9007  O  O4  . CIT DA .   ? 0.3086 0.1287 0.4280 0.0156  -0.0606 -0.0667 306 CIT D O4  
9008  C  C6  . CIT DA .   ? 0.2757 0.4325 0.2827 0.0324  0.1312  0.0754  306 CIT D C6  
9009  O  O5  . CIT DA .   ? 0.4517 0.1495 0.2646 0.0208  -0.0705 0.0463  306 CIT D O5  
9010  O  O6  . CIT DA .   ? 0.6841 0.6166 0.5002 0.0093  -0.0494 -0.0807 306 CIT D O6  
9011  C  C1  . EDO EA .   ? 0.3285 0.3580 0.2680 -0.0248 -0.0080 -0.0098 307 EDO D C1  
9012  O  O1  . EDO EA .   ? 0.2754 0.3246 0.2442 -0.0173 -0.0282 0.0175  307 EDO D O1  
9013  C  C2  . EDO EA .   ? 0.3136 0.3585 0.3072 -0.0320 0.0098  -0.0322 307 EDO D C2  
9014  O  O2  . EDO EA .   ? 0.3156 0.3271 0.2890 -0.0131 -0.0130 -0.0094 307 EDO D O2  
9015  O  O   . HOH FA .   ? 0.3495 0.4560 0.5059 -0.0531 0.1345  -0.1738 401 HOH A O   
9016  O  O   . HOH FA .   ? 0.4036 0.4106 0.3461 0.1498  0.2177  0.1260  402 HOH A O   
9017  O  O   . HOH FA .   ? 0.2156 0.4461 0.4341 0.0240  0.0954  0.0903  403 HOH A O   
9018  O  O   . HOH FA .   ? 0.4336 0.4996 0.4808 0.0250  -0.0401 -0.0197 404 HOH A O   
9019  O  O   . HOH FA .   ? 0.4869 0.4799 0.4289 -0.0144 0.1988  -0.1375 405 HOH A O   
9020  O  O   . HOH FA .   ? 0.5472 0.5450 0.3420 -0.0251 0.0023  -0.0956 406 HOH A O   
9021  O  O   . HOH FA .   ? 0.2784 0.5806 0.3734 -0.0129 0.0293  0.1444  407 HOH A O   
9022  O  O   . HOH FA .   ? 0.2919 0.7570 0.3174 0.0136  -0.0592 -0.1475 408 HOH A O   
9023  O  O   . HOH FA .   ? 0.4464 0.2527 0.4679 0.1220  -0.1058 -0.0888 409 HOH A O   
9024  O  O   . HOH FA .   ? 0.3707 0.4505 0.3391 -0.0463 0.1228  0.0240  410 HOH A O   
9025  O  O   . HOH FA .   ? 0.2405 0.4475 0.2203 -0.0646 -0.0080 0.1229  411 HOH A O   
9026  O  O   . HOH FA .   ? 0.6567 0.4705 0.5023 -0.0071 0.2040  -0.1812 412 HOH A O   
9027  O  O   . HOH FA .   ? 0.2499 0.2206 0.3749 0.0096  0.0297  0.0109  413 HOH A O   
9028  O  O   . HOH FA .   ? 0.5813 0.1960 0.4817 0.0129  0.0474  0.0137  414 HOH A O   
9029  O  O   . HOH FA .   ? 0.6632 0.4444 0.2570 -0.0832 -0.0553 0.0370  415 HOH A O   
9030  O  O   . HOH FA .   ? 0.2078 0.4683 0.3580 -0.0700 0.0364  -0.0027 416 HOH A O   
9031  O  O   . HOH FA .   ? 0.4140 0.5175 0.6715 0.0800  0.2469  -0.0546 417 HOH A O   
9032  O  O   . HOH FA .   ? 0.3964 0.2520 0.2657 0.0038  0.0684  0.0643  418 HOH A O   
9033  O  O   . HOH FA .   ? 0.3267 0.3691 0.3583 -0.0384 0.0083  -0.0313 419 HOH A O   
9034  O  O   . HOH FA .   ? 0.3273 0.4794 0.2705 0.0144  -0.1018 0.0234  420 HOH A O   
9035  O  O   . HOH FA .   ? 0.5178 0.3984 0.5611 0.0337  0.0207  0.0725  421 HOH A O   
9036  O  O   . HOH FA .   ? 0.1635 0.1734 0.1755 0.0019  0.0210  0.0645  422 HOH A O   
9037  O  O   . HOH FA .   ? 0.2567 0.5386 0.1869 0.0264  0.0187  0.0129  423 HOH A O   
9038  O  O   . HOH FA .   ? 0.4805 0.6445 0.6281 0.2412  -0.3018 -0.2937 424 HOH A O   
9039  O  O   . HOH FA .   ? 0.1843 0.4194 0.2210 -0.1216 0.0362  0.0234  425 HOH A O   
9040  O  O   . HOH FA .   ? 0.3007 0.5843 0.1924 0.0384  0.0384  0.0560  426 HOH A O   
9041  O  O   . HOH FA .   ? 0.2075 0.2073 0.3440 0.0474  0.0960  0.0207  427 HOH A O   
9042  O  O   . HOH FA .   ? 0.2779 0.2578 0.4408 -0.0088 -0.0758 0.0619  428 HOH A O   
9043  O  O   . HOH FA .   ? 0.3413 0.2563 0.2991 0.0513  0.0648  0.0683  429 HOH A O   
9044  O  O   . HOH FA .   ? 0.4410 0.5103 0.4375 -0.0610 -0.0672 0.0696  430 HOH A O   
9045  O  O   . HOH FA .   ? 0.1527 0.1213 0.1452 -0.0131 0.0200  0.0137  431 HOH A O   
9046  O  O   . HOH FA .   ? 0.4771 0.5375 0.2759 -0.0135 -0.0844 0.0256  432 HOH A O   
9047  O  O   . HOH FA .   ? 0.2797 0.3883 0.2960 -0.0241 -0.0151 0.0478  433 HOH A O   
9048  O  O   . HOH FA .   ? 0.3052 0.4453 0.2518 0.0854  0.0394  0.0176  434 HOH A O   
9049  O  O   . HOH FA .   ? 0.2700 0.2642 0.2644 -0.0998 0.1014  -0.0540 435 HOH A O   
9050  O  O   . HOH FA .   ? 0.5762 0.3731 0.4320 0.1673  0.2169  0.0917  436 HOH A O   
9051  O  O   . HOH FA .   ? 0.2935 0.4192 0.7809 -0.1036 -0.0170 0.2621  437 HOH A O   
9052  O  O   . HOH FA .   ? 0.1948 0.3718 0.2120 -0.0003 0.0241  0.0000  438 HOH A O   
9053  O  O   . HOH FA .   ? 0.5174 0.5038 0.2800 -0.0357 0.0041  0.0872  439 HOH A O   
9054  O  O   . HOH FA .   ? 0.6437 0.6812 0.2467 -0.1875 0.0644  0.0516  440 HOH A O   
9055  O  O   . HOH FA .   ? 0.1680 0.1200 0.1805 -0.0138 -0.0193 0.0087  441 HOH A O   
9056  O  O   . HOH FA .   ? 0.8809 0.4508 0.5697 0.2836  -0.0900 0.0776  442 HOH A O   
9057  O  O   . HOH FA .   ? 0.2712 0.2475 0.2166 0.0113  0.0364  -0.0308 443 HOH A O   
9058  O  O   . HOH FA .   ? 0.4528 0.4092 0.2651 -0.0797 -0.0346 0.0020  444 HOH A O   
9059  O  O   . HOH FA .   ? 0.3106 0.2806 0.2310 0.0399  -0.0285 0.0663  445 HOH A O   
9060  O  O   . HOH FA .   ? 0.3635 0.6729 0.2888 0.0353  0.0092  -0.0489 446 HOH A O   
9061  O  O   . HOH FA .   ? 0.2529 0.3097 0.2840 0.0533  0.0886  0.0593  447 HOH A O   
9062  O  O   . HOH FA .   ? 0.3138 0.2723 0.3260 -0.0269 -0.0200 -0.0043 448 HOH A O   
9063  O  O   . HOH FA .   ? 0.1515 0.3303 0.2976 0.0017  0.0326  0.1177  449 HOH A O   
9064  O  O   . HOH FA .   ? 0.4776 0.4194 0.4223 -0.2134 -0.1259 0.0949  450 HOH A O   
9065  O  O   . HOH FA .   ? 0.4544 0.4210 0.1527 0.1694  0.0322  0.0930  451 HOH A O   
9066  O  O   . HOH FA .   ? 0.1389 0.1517 0.2066 0.0051  -0.0232 0.0551  452 HOH A O   
9067  O  O   . HOH FA .   ? 0.3447 0.8004 0.3546 0.0922  0.1431  -0.1495 453 HOH A O   
9068  O  O   . HOH FA .   ? 0.2219 0.3941 0.3648 -0.0511 0.1501  -0.0261 454 HOH A O   
9069  O  O   . HOH FA .   ? 0.4651 0.3003 0.2793 0.0763  0.1146  0.0370  455 HOH A O   
9070  O  O   . HOH FA .   ? 0.1532 0.3560 0.1761 0.0167  0.0186  0.1045  456 HOH A O   
9071  O  O   . HOH FA .   ? 0.3025 0.2626 0.3765 0.0577  -0.0535 -0.0253 457 HOH A O   
9072  O  O   . HOH FA .   ? 0.3722 0.6966 0.3163 -0.2378 0.0555  0.0057  458 HOH A O   
9073  O  O   . HOH FA .   ? 0.2423 0.3569 0.7168 -0.0093 0.0013  0.2628  459 HOH A O   
9074  O  O   . HOH FA .   ? 0.1393 0.1333 0.2287 0.0060  0.0003  0.0017  460 HOH A O   
9075  O  O   . HOH FA .   ? 0.2960 0.3213 0.1944 -0.0458 -0.0908 0.0526  461 HOH A O   
9076  O  O   . HOH FA .   ? 0.5756 0.4921 0.2838 -0.3176 -0.0337 0.0154  462 HOH A O   
9077  O  O   . HOH FA .   ? 0.5925 0.4910 0.3919 -0.0789 -0.1929 0.0714  463 HOH A O   
9078  O  O   . HOH FA .   ? 0.1321 0.2111 0.2147 0.0031  -0.0006 0.0171  464 HOH A O   
9079  O  O   . HOH FA .   ? 0.1565 0.2387 0.2111 0.0119  0.0351  0.0903  465 HOH A O   
9080  O  O   . HOH FA .   ? 0.4022 0.5189 0.7247 0.0203  -0.1485 -0.2711 466 HOH A O   
9081  O  O   . HOH FA .   ? 0.6284 0.4995 0.2264 -0.2904 -0.0637 0.0597  467 HOH A O   
9082  O  O   . HOH FA .   ? 0.2447 0.2030 0.2642 -0.0350 0.0051  0.1066  468 HOH A O   
9083  O  O   . HOH FA .   ? 0.1172 0.1429 0.1542 -0.0148 0.0315  0.0236  469 HOH A O   
9084  O  O   . HOH FA .   ? 0.5601 0.4025 0.3253 0.2267  0.1287  0.0307  470 HOH A O   
9085  O  O   . HOH FA .   ? 0.3935 0.2851 0.4809 0.1339  0.0419  0.1381  471 HOH A O   
9086  O  O   . HOH FA .   ? 0.1646 0.2768 0.4476 -0.0265 -0.0198 0.0046  472 HOH A O   
9087  O  O   . HOH FA .   ? 0.4729 0.4154 0.5898 -0.0233 -0.2552 -0.0373 473 HOH A O   
9088  O  O   . HOH FA .   ? 0.1437 0.2434 0.2343 0.0322  0.0483  0.0234  474 HOH A O   
9089  O  O   . HOH FA .   ? 0.1197 0.1543 0.1453 0.0038  0.0115  0.0302  475 HOH A O   
9090  O  O   . HOH FA .   ? 0.2199 0.2816 0.2777 0.0003  0.0295  0.0228  476 HOH A O   
9091  O  O   . HOH FA .   ? 0.2561 0.2060 0.4065 0.0844  0.1613  0.1001  477 HOH A O   
9092  O  O   . HOH FA .   ? 0.3889 0.3443 0.2702 -0.0401 0.0478  -0.0227 478 HOH A O   
9093  O  O   . HOH FA .   ? 0.4180 0.5720 0.4363 -0.1885 0.0388  0.0405  479 HOH A O   
9094  O  O   . HOH FA .   ? 0.1387 0.2881 0.6776 0.0179  -0.0043 0.0031  480 HOH A O   
9095  O  O   . HOH FA .   ? 0.1872 0.3684 0.2048 0.0074  0.0631  0.0549  481 HOH A O   
9096  O  O   . HOH FA .   ? 0.1787 0.3129 0.1446 -0.0654 -0.0102 0.0763  482 HOH A O   
9097  O  O   . HOH FA .   ? 0.1560 0.1278 0.1349 0.0000  0.0405  0.0310  483 HOH A O   
9098  O  O   . HOH FA .   ? 0.2913 0.3068 0.1951 0.0549  -0.0217 -0.0307 484 HOH A O   
9099  O  O   . HOH FA .   ? 0.3075 0.3504 0.3289 -0.0953 -0.0419 0.0024  485 HOH A O   
9100  O  O   . HOH FA .   ? 0.3592 0.4264 0.2152 0.0537  -0.0666 0.0791  486 HOH A O   
9101  O  O   . HOH FA .   ? 0.3497 0.5774 0.6642 -0.1597 0.2222  -0.3416 487 HOH A O   
9102  O  O   . HOH FA .   ? 0.1502 0.2479 0.3005 -0.0241 0.0104  0.0342  488 HOH A O   
9103  O  O   . HOH FA .   ? 0.1190 0.1197 0.1502 0.0006  0.0035  0.0414  489 HOH A O   
9104  O  O   . HOH FA .   ? 0.1518 0.1962 0.2271 -0.0073 -0.0244 0.0326  490 HOH A O   
9105  O  O   . HOH FA .   ? 0.3576 0.6417 0.2237 0.0971  0.0366  0.1614  491 HOH A O   
9106  O  O   . HOH FA .   ? 0.2346 0.3240 0.1380 0.0239  0.0344  0.0370  492 HOH A O   
9107  O  O   . HOH FA .   ? 0.0954 0.0994 0.1324 0.0057  0.0215  0.0226  493 HOH A O   
9108  O  O   . HOH FA .   ? 0.4370 0.3662 0.3364 0.2282  0.1409  0.1713  494 HOH A O   
9109  O  O   . HOH FA .   ? 0.3574 0.4018 0.3957 -0.0786 0.1247  0.0251  495 HOH A O   
9110  O  O   . HOH FA .   ? 0.2391 0.5052 0.3822 0.1386  0.0381  0.1577  496 HOH A O   
9111  O  O   . HOH FA .   ? 0.4912 0.4798 0.4609 0.0430  -0.0038 0.0381  497 HOH A O   
9112  O  O   . HOH FA .   ? 0.4913 0.4735 0.4449 -0.0008 -0.0230 0.0141  498 HOH A O   
9113  O  O   . HOH FA .   ? 0.3249 0.3106 0.4043 0.0520  0.0511  0.0487  499 HOH A O   
9114  O  O   . HOH FA .   ? 0.3709 0.3391 0.2646 -0.0353 0.0172  -0.0351 500 HOH A O   
9115  O  O   . HOH FA .   ? 0.1850 0.3093 0.2053 0.0679  0.0350  0.0120  501 HOH A O   
9116  O  O   . HOH FA .   ? 0.3124 0.2644 0.1913 -0.0571 0.0250  0.0599  502 HOH A O   
9117  O  O   . HOH FA .   ? 0.2712 0.3486 0.1953 0.0144  0.0094  0.0176  503 HOH A O   
9118  O  O   . HOH FA .   ? 0.3459 0.3118 0.2381 0.0666  0.0048  0.0659  504 HOH A O   
9119  O  O   . HOH FA .   ? 0.2660 0.4975 0.5018 -0.0621 -0.1440 0.1237  505 HOH A O   
9120  O  O   . HOH FA .   ? 0.5490 0.2608 0.3819 -0.1749 0.0272  0.0549  506 HOH A O   
9121  O  O   . HOH FA .   ? 0.2276 0.1172 0.2239 -0.0441 -0.0266 0.0044  507 HOH A O   
9122  O  O   . HOH FA .   ? 0.2554 0.2373 0.4097 -0.0197 -0.0914 0.0734  508 HOH A O   
9123  O  O   . HOH FA .   ? 0.3240 0.2032 0.3215 0.0263  0.0013  0.0395  509 HOH A O   
9124  O  O   . HOH FA .   ? 0.2741 0.2267 0.2364 0.0445  -0.0285 0.0305  510 HOH A O   
9125  O  O   . HOH FA .   ? 0.7425 0.6355 0.3716 -0.0548 0.0000  0.1081  511 HOH A O   
9126  O  O   . HOH FA .   ? 0.1705 0.2151 0.2053 0.0135  0.0460  0.0615  512 HOH A O   
9127  O  O   . HOH FA .   ? 0.1965 0.1673 0.1398 0.0137  0.0160  -0.0102 513 HOH A O   
9128  O  O   . HOH FA .   ? 0.3804 0.4518 0.3319 0.1001  0.1055  0.1112  514 HOH A O   
9129  O  O   . HOH FA .   ? 0.3515 0.2763 0.3370 0.0294  0.0000  0.0395  515 HOH A O   
9130  O  O   . HOH FA .   ? 0.3880 0.5906 0.7415 0.0830  -0.0348 0.2357  516 HOH A O   
9131  O  O   . HOH FA .   ? 0.2599 0.7591 0.5580 0.1444  0.0734  0.2159  517 HOH A O   
9132  O  O   . HOH FA .   ? 0.2084 0.2231 0.2208 -0.0163 0.0887  -0.0187 518 HOH A O   
9133  O  O   . HOH FA .   ? 0.5454 0.3416 0.4930 0.0163  -0.2583 -0.1252 519 HOH A O   
9134  O  O   . HOH FA .   ? 0.4598 0.6833 0.3499 0.0210  0.1537  0.0830  520 HOH A O   
9135  O  O   . HOH FA .   ? 0.3384 0.8737 0.4968 -0.2238 -0.2149 0.3400  521 HOH A O   
9136  O  O   . HOH FA .   ? 0.4196 0.3907 0.2217 -0.0998 0.0921  -0.0197 522 HOH A O   
9137  O  O   . HOH FA .   ? 0.2055 0.3398 0.2813 -0.0110 0.0859  -0.0544 523 HOH A O   
9138  O  O   . HOH FA .   ? 0.2346 0.2314 0.2310 0.0866  0.0500  0.0582  524 HOH A O   
9139  O  O   . HOH FA .   ? 0.2206 0.5903 0.2536 0.0331  0.0750  -0.1702 525 HOH A O   
9140  O  O   . HOH FA .   ? 0.8327 0.3497 0.6014 -0.0132 0.2185  -0.0873 526 HOH A O   
9141  O  O   . HOH FA .   ? 0.0983 0.0964 0.1278 -0.0012 0.0234  0.0322  527 HOH A O   
9142  O  O   . HOH FA .   ? 0.3097 0.2870 0.2481 -0.0432 0.0348  -0.0592 528 HOH A O   
9143  O  O   . HOH FA .   ? 0.1290 0.1172 0.1164 0.0087  0.0373  -0.0071 529 HOH A O   
9144  O  O   . HOH FA .   ? 0.3643 0.4334 0.2976 -0.1509 -0.0588 0.0386  530 HOH A O   
9145  O  O   . HOH FA .   ? 0.1353 0.1310 0.2202 -0.0313 -0.0190 0.0546  531 HOH A O   
9146  O  O   . HOH FA .   ? 0.3177 0.2044 0.6036 -0.0122 -0.0855 0.0606  532 HOH A O   
9147  O  O   . HOH FA .   ? 0.2658 0.2321 0.3224 -0.0487 -0.0412 0.0513  533 HOH A O   
9148  O  O   . HOH FA .   ? 0.2718 0.1434 0.2967 0.0296  0.0467  0.0888  534 HOH A O   
9149  O  O   . HOH FA .   ? 0.4323 0.4770 0.4171 0.0094  0.0652  0.0706  535 HOH A O   
9150  O  O   . HOH FA .   ? 0.3935 0.3296 0.2285 -0.0785 0.0299  0.1518  536 HOH A O   
9151  O  O   . HOH FA .   ? 0.2188 0.4526 0.3874 -0.0384 -0.0207 0.1054  537 HOH A O   
9152  O  O   . HOH FA .   ? 0.3077 0.3907 0.2096 -0.1216 0.1225  -0.0456 538 HOH A O   
9153  O  O   . HOH FA .   ? 0.2027 0.2226 0.2838 -0.0237 0.0480  0.0513  539 HOH A O   
9154  O  O   . HOH FA .   ? 0.4875 0.9579 0.3100 0.0294  0.1178  -0.0560 540 HOH A O   
9155  O  O   . HOH FA .   ? 0.1940 0.2231 0.2172 0.0357  0.0249  0.0159  541 HOH A O   
9156  O  O   . HOH FA .   ? 0.4670 0.4569 0.3521 0.0242  -0.0405 -0.0285 542 HOH A O   
9157  O  O   . HOH FA .   ? 0.1314 0.0724 0.1914 -0.0081 -0.0015 0.0276  543 HOH A O   
9158  O  O   . HOH FA .   ? 0.5051 0.5422 0.4931 -0.0628 0.0428  0.0625  544 HOH A O   
9159  O  O   . HOH FA .   ? 0.2314 0.3474 0.3657 0.0549  -0.0326 -0.0062 545 HOH A O   
9160  O  O   . HOH FA .   ? 0.1286 0.0967 0.1553 -0.0028 -0.0030 0.0194  546 HOH A O   
9161  O  O   . HOH FA .   ? 0.2476 0.4715 0.2418 -0.0709 -0.0054 0.1403  547 HOH A O   
9162  O  O   . HOH FA .   ? 0.2870 0.1847 0.4399 0.0030  0.1450  0.0263  548 HOH A O   
9163  O  O   . HOH FA .   ? 0.4426 0.5022 0.1835 0.0046  0.0285  0.0754  549 HOH A O   
9164  O  O   . HOH FA .   ? 0.1669 0.1508 0.2470 0.0174  0.0720  0.0355  550 HOH A O   
9165  O  O   . HOH FA .   ? 0.3650 0.4180 0.3161 -0.0015 0.0866  0.0635  551 HOH A O   
9166  O  O   . HOH FA .   ? 0.1304 0.0891 0.1947 -0.0288 -0.0165 0.0379  552 HOH A O   
9167  O  O   . HOH FA .   ? 0.2800 0.4020 0.1949 0.0060  0.0198  0.0709  553 HOH A O   
9168  O  O   . HOH FA .   ? 0.7573 0.9965 0.4083 0.0584  0.1749  -0.0646 554 HOH A O   
9169  O  O   . HOH FA .   ? 0.1966 0.2127 0.2357 -0.0174 0.0480  -0.0542 555 HOH A O   
9170  O  O   . HOH FA .   ? 0.2815 0.4769 0.7091 -0.0472 0.2176  -0.2687 556 HOH A O   
9171  O  O   . HOH FA .   ? 0.1439 0.1481 0.3138 0.0065  0.0203  0.0160  557 HOH A O   
9172  O  O   . HOH FA .   ? 0.4433 0.2711 0.5698 -0.0381 -0.1962 0.1120  558 HOH A O   
9173  O  O   . HOH FA .   ? 0.3068 0.2381 0.1709 -0.0518 -0.0557 0.0778  559 HOH A O   
9174  O  O   . HOH FA .   ? 0.1832 0.2669 0.1771 0.0028  0.0432  0.0348  560 HOH A O   
9175  O  O   . HOH FA .   ? 0.3310 0.4090 0.2908 -0.1324 -0.0219 0.1022  561 HOH A O   
9176  O  O   . HOH FA .   ? 0.4663 0.5098 1.2979 -0.0527 -0.2653 0.4316  562 HOH A O   
9177  O  O   . HOH FA .   ? 0.2373 0.2321 0.2163 0.0015  0.0278  0.0803  563 HOH A O   
9178  O  O   . HOH FA .   ? 0.3592 0.5820 0.3420 0.0412  -0.1208 -0.0252 564 HOH A O   
9179  O  O   . HOH FA .   ? 0.4077 0.2373 0.5504 -0.0151 0.0127  0.0397  565 HOH A O   
9180  O  O   . HOH FA .   ? 0.3811 0.1990 0.3747 0.0168  0.2111  0.0737  566 HOH A O   
9181  O  O   . HOH FA .   ? 0.1971 0.2720 0.2023 0.0423  0.0608  0.0627  567 HOH A O   
9182  O  O   . HOH FA .   ? 0.4934 0.3826 0.1481 -0.1576 -0.0966 0.0712  568 HOH A O   
9183  O  O   . HOH FA .   ? 0.2921 0.5347 0.8679 -0.0842 -0.0864 -0.0922 569 HOH A O   
9184  O  O   . HOH FA .   ? 0.1389 0.1423 0.1775 -0.0263 0.0068  0.0582  570 HOH A O   
9185  O  O   . HOH FA .   ? 0.2727 0.4560 0.3005 0.0094  0.0399  0.1502  571 HOH A O   
9186  O  O   . HOH FA .   ? 0.6353 0.2500 0.6345 0.0292  -0.3917 -0.0725 572 HOH A O   
9187  O  O   . HOH FA .   ? 0.3885 0.3124 0.4140 0.1389  0.0582  0.0102  573 HOH A O   
9188  O  O   . HOH FA .   ? 0.2869 0.6862 0.3718 -0.0993 0.1014  -0.2014 574 HOH A O   
9189  O  O   . HOH FA .   ? 0.3623 0.2957 0.5856 0.0759  0.0454  0.1741  575 HOH A O   
9190  O  O   . HOH FA .   ? 0.3003 0.4117 0.3470 0.0662  -0.0131 0.0480  576 HOH A O   
9191  O  O   . HOH FA .   ? 0.7522 0.4964 0.5537 -0.3361 -0.0265 0.1045  577 HOH A O   
9192  O  O   . HOH FA .   ? 0.2660 0.4217 0.2958 0.0526  0.1776  0.0527  578 HOH A O   
9193  O  O   . HOH FA .   ? 0.1693 0.2509 0.2075 -0.0258 -0.0086 0.0637  579 HOH A O   
9194  O  O   . HOH FA .   ? 0.1209 0.1213 0.1657 0.0063  0.0181  0.0414  580 HOH A O   
9195  O  O   . HOH FA .   ? 0.5041 0.4773 0.3443 0.0250  -0.0088 0.0263  581 HOH A O   
9196  O  O   . HOH FA .   ? 0.2483 0.3898 0.3353 0.1430  -0.0151 -0.0436 582 HOH A O   
9197  O  O   . HOH FA .   ? 0.3190 0.3677 0.7059 0.0789  0.0395  -0.0003 583 HOH A O   
9198  O  O   . HOH FA .   ? 0.7552 0.3966 0.2644 0.0570  -0.0324 -0.0199 584 HOH A O   
9199  O  O   . HOH FA .   ? 0.2777 0.4068 0.1578 -0.0745 0.0524  0.0854  585 HOH A O   
9200  O  O   . HOH FA .   ? 0.3264 0.2468 0.3366 0.0895  0.0020  0.0121  586 HOH A O   
9201  O  O   . HOH FA .   ? 0.2563 0.2766 0.2606 0.1492  0.0318  0.0229  587 HOH A O   
9202  O  O   . HOH FA .   ? 0.3966 0.2590 0.3312 -0.0417 -0.0700 0.0266  588 HOH A O   
9203  O  O   . HOH FA .   ? 0.2456 0.2506 0.1483 -0.0127 0.0610  0.0562  589 HOH A O   
9204  O  O   . HOH FA .   ? 0.3416 0.4068 0.4289 -0.0205 0.0031  -0.0208 590 HOH A O   
9205  O  O   . HOH FA .   ? 0.3698 0.2799 0.2851 -0.0096 0.0952  0.0421  591 HOH A O   
9206  O  O   . HOH FA .   ? 0.4092 0.4329 0.3217 0.1391  0.0467  0.0463  592 HOH A O   
9207  O  O   . HOH FA .   ? 0.2538 0.1577 0.2082 -0.0300 0.0711  0.0520  593 HOH A O   
9208  O  O   . HOH FA .   ? 0.6269 0.7242 0.3625 0.3921  0.0706  -0.0315 594 HOH A O   
9209  O  O   . HOH FA .   ? 0.2282 0.4266 0.9200 -0.0288 0.0772  -0.1235 595 HOH A O   
9210  O  O   . HOH FA .   ? 0.2682 0.5066 0.4856 -0.1274 -0.0280 0.0684  596 HOH A O   
9211  O  O   . HOH FA .   ? 0.3991 0.2861 0.2421 0.0091  0.0148  0.0566  597 HOH A O   
9212  O  O   . HOH FA .   ? 0.1867 0.2782 0.2269 -0.0125 0.0183  -0.0068 598 HOH A O   
9213  O  O   . HOH FA .   ? 0.1569 0.1956 0.2082 0.0113  0.0384  0.0820  599 HOH A O   
9214  O  O   . HOH FA .   ? 0.4655 0.3210 0.5354 -0.0476 0.0216  0.0557  600 HOH A O   
9215  O  O   . HOH FA .   ? 0.2944 0.6581 0.6068 0.1877  0.1341  0.3560  601 HOH A O   
9216  O  O   . HOH FA .   ? 0.6855 0.2949 0.3084 -0.1162 0.1381  -0.0243 602 HOH A O   
9217  O  O   . HOH FA .   ? 0.2412 0.2389 0.2397 -0.0259 0.0366  -0.0059 603 HOH A O   
9218  O  O   . HOH FA .   ? 0.2675 0.5961 0.5382 0.0617  -0.0662 0.2766  604 HOH A O   
9219  O  O   . HOH FA .   ? 0.4246 0.4535 0.4007 0.0406  0.0685  -0.0054 605 HOH A O   
9220  O  O   . HOH FA .   ? 0.1745 0.3666 0.2590 0.1116  0.0586  0.0732  606 HOH A O   
9221  O  O   . HOH FA .   ? 0.5115 0.4169 0.5475 -0.0502 -0.0427 0.3395  607 HOH A O   
9222  O  O   . HOH FA .   ? 0.4554 0.3747 0.4900 -0.1369 0.0608  -0.1292 608 HOH A O   
9223  O  O   . HOH FA .   ? 0.3562 0.2533 0.5957 -0.0820 0.0908  -0.0857 609 HOH A O   
9224  O  O   . HOH FA .   ? 0.1418 0.1365 0.1811 0.0221  0.0351  0.0147  610 HOH A O   
9225  O  O   . HOH FA .   ? 0.6305 0.4557 0.1793 -0.0905 -0.0839 0.0254  611 HOH A O   
9226  O  O   . HOH FA .   ? 0.1084 0.1931 0.1953 0.0153  0.0000  -0.0194 612 HOH A O   
9227  O  O   . HOH FA .   ? 0.2657 0.3409 0.5744 0.0108  0.0668  0.1780  613 HOH A O   
9228  O  O   . HOH FA .   ? 0.4720 0.5633 0.8051 -0.2070 -0.2818 0.0894  614 HOH A O   
9229  O  O   . HOH FA .   ? 0.4566 0.5762 0.1887 -0.2996 0.0564  -0.0207 615 HOH A O   
9230  O  O   . HOH FA .   ? 0.5501 0.2615 0.1901 0.1081  0.0357  0.0333  616 HOH A O   
9231  O  O   . HOH FA .   ? 0.3427 0.2375 0.2233 -0.0720 0.0362  0.0538  617 HOH A O   
9232  O  O   . HOH FA .   ? 0.2321 0.2436 0.2919 0.0125  -0.0092 -0.0088 618 HOH A O   
9233  O  O   . HOH FA .   ? 0.3037 0.4480 0.2680 0.0221  0.1145  0.0471  619 HOH A O   
9234  O  O   . HOH FA .   ? 0.3470 0.1834 0.3987 0.0322  -0.2261 0.0208  620 HOH A O   
9235  O  O   . HOH FA .   ? 0.2524 0.2644 0.2949 -0.0749 -0.0199 -0.0093 621 HOH A O   
9236  O  O   . HOH FA .   ? 0.1588 0.1272 0.2585 -0.0297 -0.0419 0.0980  622 HOH A O   
9237  O  O   . HOH FA .   ? 0.1911 0.5982 0.2278 -0.0432 0.0320  0.0780  623 HOH A O   
9238  O  O   . HOH FA .   ? 0.2985 0.2558 0.3404 -0.0285 0.0546  0.0762  624 HOH A O   
9239  O  O   . HOH FA .   ? 0.5893 0.5917 0.4999 0.3404  -0.0741 -0.1347 625 HOH A O   
9240  O  O   . HOH FA .   ? 0.3639 0.4842 0.5059 -0.1783 -0.1824 0.2168  626 HOH A O   
9241  O  O   . HOH FA .   ? 0.2628 0.7289 0.5356 -0.0888 -0.0421 0.2854  627 HOH A O   
9242  O  O   . HOH FA .   ? 0.6370 0.2858 0.2461 -0.1106 -0.0249 -0.0719 628 HOH A O   
9243  O  O   . HOH FA .   ? 0.6294 0.3756 0.4967 0.1826  -0.1090 -0.0926 629 HOH A O   
9244  O  O   . HOH FA .   ? 0.3057 0.8583 0.4005 -0.2202 0.0847  -0.0732 630 HOH A O   
9245  O  O   . HOH FA .   ? 0.6085 0.4884 0.4271 -0.1565 0.1853  -0.0706 631 HOH A O   
9246  O  O   . HOH FA .   ? 0.2985 0.4449 0.3819 0.0659  -0.1074 0.0142  632 HOH A O   
9247  O  O   . HOH FA .   ? 0.2592 0.2946 0.2425 0.0049  0.0987  0.0133  633 HOH A O   
9248  O  O   . HOH FA .   ? 0.2515 0.1743 0.4785 -0.0351 -0.0109 0.0674  634 HOH A O   
9249  O  O   . HOH FA .   ? 0.6790 0.6838 0.5554 0.3422  -0.2073 0.0183  635 HOH A O   
9250  O  O   . HOH FA .   ? 0.4386 0.3106 0.2926 0.0216  0.0093  0.0467  636 HOH A O   
9251  O  O   . HOH FA .   ? 0.5497 0.4755 0.4461 0.0996  -0.0511 -0.1318 637 HOH A O   
9252  O  O   . HOH FA .   ? 0.2840 0.4469 0.2386 -0.0219 -0.0118 -0.1058 638 HOH A O   
9253  O  O   . HOH FA .   ? 0.3777 0.2772 0.4041 0.1265  -0.0078 0.0065  639 HOH A O   
9254  O  O   . HOH FA .   ? 0.6105 0.2802 0.4767 0.0109  -0.0619 -0.1164 640 HOH A O   
9255  O  O   . HOH FA .   ? 0.6919 0.3634 0.4043 -0.1809 -0.0815 0.0379  641 HOH A O   
9256  O  O   . HOH FA .   ? 0.4077 0.2637 0.8291 -0.0628 0.1687  -0.0930 642 HOH A O   
9257  O  O   . HOH FA .   ? 0.1560 0.1586 0.1984 0.0024  0.0241  0.0636  643 HOH A O   
9258  O  O   . HOH FA .   ? 0.2800 0.3873 0.3849 0.1489  0.0641  -0.0939 644 HOH A O   
9259  O  O   . HOH FA .   ? 0.6150 0.5447 0.3977 0.0756  0.2524  0.1967  645 HOH A O   
9260  O  O   . HOH FA .   ? 0.3494 0.3257 0.2612 -0.0288 0.0043  -0.0174 646 HOH A O   
9261  O  O   . HOH FA .   ? 0.2834 0.3192 0.2251 0.0340  0.0938  0.0535  647 HOH A O   
9262  O  O   . HOH FA .   ? 0.1454 0.3050 0.3016 -0.0143 0.0283  0.1132  648 HOH A O   
9263  O  O   . HOH FA .   ? 0.3975 0.3413 0.5946 0.0043  0.0608  -0.0998 649 HOH A O   
9264  O  O   . HOH FA .   ? 0.2768 0.1816 0.6201 0.0110  0.0469  0.0054  650 HOH A O   
9265  O  O   . HOH FA .   ? 0.4300 0.1998 0.7372 -0.1256 -0.0998 0.0337  651 HOH A O   
9266  O  O   . HOH FA .   ? 0.5235 0.4625 0.5336 -0.0381 -0.0820 -0.0483 652 HOH A O   
9267  O  O   . HOH FA .   ? 0.2370 0.4059 0.2524 -0.0024 0.0240  0.0712  653 HOH A O   
9268  O  O   . HOH FA .   ? 0.1741 0.3045 0.4174 0.0248  0.0167  -0.0333 654 HOH A O   
9269  O  O   . HOH FA .   ? 0.4729 0.3986 0.5006 -0.0417 0.1870  -0.1275 655 HOH A O   
9270  O  O   . HOH FA .   ? 0.2488 0.2834 0.3704 -0.0027 0.0555  0.0190  656 HOH A O   
9271  O  O   . HOH FA .   ? 0.5224 0.5458 0.4517 0.1717  -0.1216 -0.0790 657 HOH A O   
9272  O  O   . HOH FA .   ? 0.5049 0.4120 0.4172 -0.0905 0.0621  -0.0601 658 HOH A O   
9273  O  O   . HOH FA .   ? 0.3066 0.3427 0.3741 -0.0925 0.1591  -0.0988 659 HOH A O   
9274  O  O   . HOH FA .   ? 0.6018 0.4640 0.5476 0.0093  0.0505  -0.1889 660 HOH A O   
9275  O  O   . HOH FA .   ? 0.4397 0.2768 0.3926 -0.0395 -0.0427 0.0264  661 HOH A O   
9276  O  O   . HOH FA .   ? 0.7799 0.4440 0.5103 -0.2106 -0.1037 0.1970  662 HOH A O   
9277  O  O   . HOH FA .   ? 0.3310 0.2939 0.4760 -0.0421 -0.0148 0.0788  663 HOH A O   
9278  O  O   . HOH FA .   ? 0.3989 0.5695 0.7842 -0.0953 -0.0355 0.0681  664 HOH A O   
9279  O  O   . HOH FA .   ? 0.4174 0.8299 0.6524 0.1519  0.1975  0.3122  665 HOH A O   
9280  O  O   . HOH FA .   ? 0.2633 0.4352 0.6868 -0.0227 0.1288  0.1395  666 HOH A O   
9281  O  O   . HOH FA .   ? 0.6158 0.6524 0.4903 -0.1960 0.1511  -0.0772 667 HOH A O   
9282  O  O   . HOH FA .   ? 0.4189 0.3158 0.5353 0.0216  -0.0315 0.0456  668 HOH A O   
9283  O  O   . HOH FA .   ? 0.3750 1.1742 0.6338 0.1138  0.1040  0.4474  669 HOH A O   
9284  O  O   . HOH FA .   ? 0.5103 0.3095 0.2964 -0.0658 -0.1011 -0.0195 670 HOH A O   
9285  O  O   . HOH FA .   ? 0.8780 1.3476 0.4485 -0.0461 0.0383  0.0983  671 HOH A O   
9286  O  O   . HOH FA .   ? 0.4372 0.3801 0.3177 0.1228  0.0631  0.1275  672 HOH A O   
9287  O  O   . HOH FA .   ? 0.4490 0.5106 0.2865 0.2176  -0.1207 -0.1770 673 HOH A O   
9288  O  O   . HOH FA .   ? 0.2520 0.8783 0.9307 -0.1022 0.0399  -0.4945 674 HOH A O   
9289  O  O   . HOH FA .   ? 0.5850 0.3375 0.3260 0.0390  0.1246  -0.0124 675 HOH A O   
9290  O  O   . HOH FA .   ? 0.4248 0.3889 0.3783 -0.2152 -0.0833 0.1327  676 HOH A O   
9291  O  O   . HOH FA .   ? 0.4706 0.5677 0.4771 -0.0568 -0.0888 -0.0485 677 HOH A O   
9292  O  O   . HOH FA .   ? 0.4253 0.4893 0.4316 -0.0017 0.0551  0.0381  678 HOH A O   
9293  O  O   . HOH FA .   ? 0.4912 0.5085 0.4803 0.0153  -0.0091 0.0621  679 HOH A O   
9294  O  O   . HOH FA .   ? 0.5214 0.5052 0.4997 -0.0220 0.0322  -0.0566 680 HOH A O   
9295  O  O   . HOH FA .   ? 0.3309 0.3201 0.3158 -0.0803 0.0078  -0.0187 681 HOH A O   
9296  O  O   . HOH FA .   ? 0.1920 0.5740 0.7583 -0.0566 -0.0129 0.0625  682 HOH A O   
9297  O  O   . HOH FA .   ? 0.3761 0.2599 0.1884 0.0412  -0.0100 0.0003  683 HOH A O   
9298  O  O   . HOH FA .   ? 0.2671 0.2894 0.2791 0.1106  -0.0031 0.0230  684 HOH A O   
9299  O  O   . HOH FA .   ? 0.5723 0.3337 0.4762 0.1933  0.2270  0.1067  685 HOH A O   
9300  O  O   . HOH FA .   ? 0.4857 0.4449 0.4420 0.0328  -0.0024 0.0026  686 HOH A O   
9301  O  O   . HOH FA .   ? 0.4122 0.3953 0.5974 0.1310  0.0797  0.1495  687 HOH A O   
9302  O  O   . HOH FA .   ? 0.8299 1.2954 1.4198 -0.2980 0.3009  -0.4801 688 HOH A O   
9303  O  O   . HOH FA .   ? 0.5149 0.5066 0.2921 -0.2187 -0.0386 0.0087  689 HOH A O   
9304  O  O   . HOH FA .   ? 0.2712 0.4216 0.6923 0.1432  0.1739  0.3106  690 HOH A O   
9305  O  O   . HOH FA .   ? 0.6384 0.4108 0.2703 0.1801  0.0174  0.0670  691 HOH A O   
9306  O  O   . HOH FA .   ? 0.3865 0.4835 0.5042 0.0807  -0.0265 0.0005  692 HOH A O   
9307  O  O   . HOH FA .   ? 0.3167 1.1403 0.3373 0.2504  0.0057  0.1958  693 HOH A O   
9308  O  O   . HOH FA .   ? 0.4914 0.3239 0.2953 0.0922  0.0348  -0.0930 694 HOH A O   
9309  O  O   . HOH FA .   ? 0.4022 0.3901 0.4706 -0.0584 0.0976  0.1080  695 HOH A O   
9310  O  O   . HOH FA .   ? 0.5306 0.3953 0.4656 -0.0035 -0.0038 -0.0082 696 HOH A O   
9311  O  O   . HOH FA .   ? 0.5723 0.4248 0.7050 0.1352  0.0925  0.3152  697 HOH A O   
9312  O  O   . HOH FA .   ? 0.6687 0.4047 0.4081 0.0074  -0.1365 0.0828  698 HOH A O   
9313  O  O   . HOH FA .   ? 0.5471 0.5705 0.5515 -0.0062 0.0076  0.0414  699 HOH A O   
9314  O  O   . HOH FA .   ? 0.6445 0.3935 0.3438 0.0303  0.1395  0.0615  700 HOH A O   
9315  O  O   . HOH FA .   ? 0.2865 0.3260 0.3776 -0.0068 -0.0368 0.1557  701 HOH A O   
9316  O  O   . HOH FA .   ? 0.2247 0.5916 0.4945 -0.0111 -0.0949 -0.0696 702 HOH A O   
9317  O  O   . HOH FA .   ? 0.3749 0.3580 0.3657 0.0641  0.0219  0.0386  703 HOH A O   
9318  O  O   . HOH FA .   ? 0.5080 0.3447 0.8234 -0.0632 0.1401  0.1711  704 HOH A O   
9319  O  O   . HOH FA .   ? 0.4147 0.6786 0.3763 -0.1645 0.1140  0.0746  705 HOH A O   
9320  O  O   . HOH FA .   ? 0.3747 0.4454 0.3731 0.0274  0.0487  0.0286  706 HOH A O   
9321  O  O   . HOH FA .   ? 1.5013 0.3449 2.5183 0.0684  -0.0103 0.1039  707 HOH A O   
9322  O  O   . HOH FA .   ? 0.2824 0.3628 0.3143 -0.0093 0.0166  0.0083  708 HOH A O   
9323  O  O   . HOH FA .   ? 0.2213 0.3161 0.2644 0.0210  -0.0043 0.0573  709 HOH A O   
9324  O  O   . HOH FA .   ? 2.9474 0.7052 0.3914 0.5392  0.7566  0.3273  710 HOH A O   
9325  O  O   . HOH FA .   ? 0.2797 0.4334 0.4314 0.0813  0.0434  -0.0513 711 HOH A O   
9326  O  O   . HOH FA .   ? 0.4009 0.4763 0.4895 0.0035  0.1147  0.1164  712 HOH A O   
9327  O  O   . HOH FA .   ? 0.6189 0.4806 0.9212 -0.0606 0.1316  -0.1492 713 HOH A O   
9328  O  O   . HOH FA .   ? 0.3073 0.2251 0.2382 -0.0392 0.0208  -0.0013 714 HOH A O   
9329  O  O   . HOH FA .   ? 0.3704 0.6298 0.4975 0.2630  -0.0071 -0.0041 715 HOH A O   
9330  O  O   . HOH FA .   ? 0.3953 0.5295 0.2705 0.0333  0.1310  0.0562  716 HOH A O   
9331  O  O   . HOH FA .   ? 0.8729 0.3091 1.0678 -0.1284 -0.4593 0.0930  717 HOH A O   
9332  O  O   . HOH FA .   ? 0.2096 0.1648 0.2242 -0.0211 -0.0210 0.0105  718 HOH A O   
9333  O  O   . HOH FA .   ? 0.5486 0.4558 0.3549 0.1674  -0.0276 0.0599  719 HOH A O   
9334  O  O   . HOH FA .   ? 0.4501 0.4368 0.3316 0.1477  0.1766  0.1158  720 HOH A O   
9335  O  O   . HOH FA .   ? 0.4422 0.4359 0.3122 0.0044  0.0696  0.0540  721 HOH A O   
9336  O  O   . HOH FA .   ? 0.4097 0.4518 0.4745 0.0222  0.1159  0.0098  722 HOH A O   
9337  O  O   . HOH FA .   ? 0.3729 0.6243 0.2396 0.1064  0.0261  0.1719  723 HOH A O   
9338  O  O   . HOH FA .   ? 0.6528 1.0631 0.4972 -0.4199 -0.1569 -0.0041 724 HOH A O   
9339  O  O   . HOH FA .   ? 0.4844 0.4357 0.4359 0.0221  0.0806  -0.0040 725 HOH A O   
9340  O  O   . HOH FA .   ? 0.5383 0.6130 0.2308 -0.1450 0.0052  0.0671  726 HOH A O   
9341  O  O   . HOH FA .   ? 0.3070 0.8338 0.1673 0.1456  0.0304  0.0283  727 HOH A O   
9342  O  O   . HOH FA .   ? 0.4309 0.2847 0.6058 0.1173  -0.0377 0.0661  728 HOH A O   
9343  O  O   . HOH FA .   ? 0.4494 0.3899 0.4284 0.0964  -0.0041 0.0364  729 HOH A O   
9344  O  O   . HOH FA .   ? 0.4503 0.4165 0.4223 -0.1105 -0.0015 0.1138  730 HOH A O   
9345  O  O   . HOH FA .   ? 0.3411 0.4332 0.3163 0.1587  -0.0254 0.0790  731 HOH A O   
9346  O  O   . HOH FA .   ? 0.5271 0.4932 0.4608 0.0331  -0.0210 -0.0239 732 HOH A O   
9347  O  O   . HOH FA .   ? 0.6130 0.5357 0.4187 -0.2104 -0.0842 0.0869  733 HOH A O   
9348  O  O   . HOH FA .   ? 0.3944 0.4717 0.4338 0.0800  -0.0670 0.0987  734 HOH A O   
9349  O  O   . HOH FA .   ? 0.2405 0.3815 0.5095 -0.0241 0.0813  0.1213  735 HOH A O   
9350  O  O   . HOH FA .   ? 0.3212 0.7128 0.2739 -0.0052 0.0377  0.0736  736 HOH A O   
9351  O  O   . HOH FA .   ? 0.4777 0.4652 0.4677 0.0362  0.0742  0.0206  737 HOH A O   
9352  O  O   . HOH FA .   ? 0.4598 0.4817 0.4083 -0.0285 0.0057  0.0628  738 HOH A O   
9353  O  O   . HOH FA .   ? 0.3643 0.3404 0.3553 0.0778  0.1465  0.0926  739 HOH A O   
9354  O  O   . HOH FA .   ? 0.5587 0.2854 0.4853 -0.1063 0.2158  -0.0524 740 HOH A O   
9355  O  O   . HOH FA .   ? 0.4896 0.4523 0.4988 -0.0472 0.0533  0.0361  741 HOH A O   
9356  O  O   . HOH FA .   ? 0.3016 0.4099 0.3064 -0.0281 0.0258  -0.0604 742 HOH A O   
9357  O  O   . HOH FA .   ? 0.3314 0.4117 0.6148 -0.1168 0.0273  0.1221  743 HOH A O   
9358  O  O   . HOH FA .   ? 0.4803 0.3447 0.5956 0.0604  0.1349  0.0086  744 HOH A O   
9359  O  O   . HOH FA .   ? 0.5845 0.3043 0.4562 0.1473  -0.1612 -0.0776 745 HOH A O   
9360  O  O   . HOH FA .   ? 0.5020 0.4871 0.3826 -0.0066 -0.0441 0.0368  746 HOH A O   
9361  O  O   . HOH FA .   ? 0.4586 0.4264 0.4036 -0.0603 0.0474  -0.1486 747 HOH A O   
9362  O  O   . HOH FA .   ? 0.2745 0.5130 0.6079 -0.2509 0.0568  0.0812  748 HOH A O   
9363  O  O   . HOH FA .   ? 0.3795 0.2606 0.9168 -0.0164 -0.1315 0.1341  749 HOH A O   
9364  O  O   . HOH FA .   ? 0.6331 0.3860 0.4323 0.1597  -0.1712 0.1177  750 HOH A O   
9365  O  O   . HOH FA .   ? 0.5015 0.5532 0.3249 0.1710  -0.0693 -0.0725 751 HOH A O   
9366  O  O   . HOH FA .   ? 0.6316 0.4619 0.7153 -0.2973 0.2660  -0.0614 752 HOH A O   
9367  O  O   . HOH FA .   ? 0.3120 0.3585 0.5011 -0.0071 0.0917  0.1924  753 HOH A O   
9368  O  O   . HOH FA .   ? 0.2924 0.2181 0.5336 0.0129  -0.0551 0.0894  754 HOH A O   
9369  O  O   . HOH FA .   ? 0.2800 0.2946 0.4579 -0.0644 0.1325  -0.0546 755 HOH A O   
9370  O  O   . HOH FA .   ? 0.1437 0.1662 0.6636 -0.0515 0.0108  0.1116  756 HOH A O   
9371  O  O   . HOH FA .   ? 0.3282 0.6599 0.4630 -0.1215 0.0277  0.2197  757 HOH A O   
9372  O  O   . HOH FA .   ? 0.3632 0.4993 0.3869 -0.0255 -0.0671 0.1764  758 HOH A O   
9373  O  O   . HOH FA .   ? 0.5638 0.7181 0.3677 -0.3603 0.1955  -0.1946 759 HOH A O   
9374  O  O   . HOH FA .   ? 0.7203 0.4781 0.1815 0.1694  0.0294  0.0949  760 HOH A O   
9375  O  O   . HOH FA .   ? 0.4187 0.4449 0.4352 -0.0450 0.0031  -0.0436 761 HOH A O   
9376  O  O   . HOH FA .   ? 0.4860 0.3675 0.5821 0.1110  0.0703  -0.0913 762 HOH A O   
9377  O  O   . HOH FA .   ? 0.2465 0.4711 0.3061 0.0238  0.0511  0.1361  763 HOH A O   
9378  O  O   . HOH FA .   ? 0.3998 0.5529 0.6671 -0.0825 0.0856  0.2195  764 HOH A O   
9379  O  O   . HOH FA .   ? 0.4007 0.3607 0.2937 0.0168  0.0342  0.1165  765 HOH A O   
9380  O  O   . HOH FA .   ? 0.2962 0.1962 0.4741 0.0251  0.0754  0.0632  766 HOH A O   
9381  O  O   . HOH FA .   ? 0.5590 0.2075 0.3600 0.0232  -0.0661 0.0355  767 HOH A O   
9382  O  O   . HOH FA .   ? 0.4481 0.4336 0.4522 0.0351  0.0196  0.0225  768 HOH A O   
9383  O  O   . HOH FA .   ? 0.2939 0.5274 0.3267 0.0948  0.0900  0.2468  769 HOH A O   
9384  O  O   . HOH FA .   ? 0.4665 0.3411 0.8877 -0.0795 0.1879  0.0425  770 HOH A O   
9385  O  O   . HOH FA .   ? 0.8507 0.5508 0.4568 0.0760  0.1764  0.2630  771 HOH A O   
9386  O  O   . HOH FA .   ? 0.7127 0.3343 0.5715 0.1473  0.1011  0.1186  772 HOH A O   
9387  O  O   . HOH FA .   ? 0.5383 0.2874 0.2111 -0.0952 0.0013  -0.0020 773 HOH A O   
9388  O  O   . HOH FA .   ? 1.2287 0.6703 0.5831 0.1493  -0.1207 -0.0193 774 HOH A O   
9389  O  O   . HOH FA .   ? 0.4734 0.5119 0.4740 -0.0266 0.0293  0.0320  775 HOH A O   
9390  O  O   . HOH FA .   ? 0.5838 0.5738 0.2678 0.0619  0.1671  0.0571  776 HOH A O   
9391  O  O   . HOH FA .   ? 0.3977 0.5823 0.7463 0.0886  0.1812  0.3571  777 HOH A O   
9392  O  O   . HOH FA .   ? 0.7091 0.4435 0.5365 0.2869  -0.2190 -0.1616 778 HOH A O   
9393  O  O   . HOH FA .   ? 0.7171 0.5932 0.6351 0.2087  -0.2426 -0.3668 779 HOH A O   
9394  O  O   . HOH FA .   ? 0.5766 0.5734 0.3251 0.0472  -0.1133 0.1579  780 HOH A O   
9395  O  O   . HOH GA .   ? 0.3822 0.1932 0.4014 -0.0678 -0.0063 0.0579  401 HOH B O   
9396  O  O   . HOH GA .   ? 0.5073 0.5978 0.6800 -0.2198 0.1710  0.0679  402 HOH B O   
9397  O  O   . HOH GA .   ? 0.9493 0.2079 0.2946 -0.0649 -0.1168 0.0952  403 HOH B O   
9398  O  O   . HOH GA .   ? 0.2861 0.2046 0.1748 0.0826  0.0606  0.0705  404 HOH B O   
9399  O  O   . HOH GA .   ? 0.8877 0.2244 0.6481 -0.1124 -0.3445 0.1274  405 HOH B O   
9400  O  O   . HOH GA .   ? 0.3346 0.2885 0.4796 -0.0436 -0.1002 0.1136  406 HOH B O   
9401  O  O   . HOH GA .   ? 0.6162 0.2716 0.3343 0.1527  -0.1863 -0.1011 407 HOH B O   
9402  O  O   . HOH GA .   ? 0.3601 0.3122 0.3224 0.0118  0.0149  -0.0212 408 HOH B O   
9403  O  O   . HOH GA .   ? 0.3140 0.2682 0.3889 0.1033  -0.0472 -0.1054 409 HOH B O   
9404  O  O   . HOH GA .   ? 0.2050 0.5296 0.4598 0.0333  0.0430  -0.0687 410 HOH B O   
9405  O  O   . HOH GA .   ? 0.3508 0.2802 0.3289 0.0922  0.1366  0.0619  411 HOH B O   
9406  O  O   . HOH GA .   ? 0.6212 0.7982 0.3847 0.2782  0.2599  0.3138  412 HOH B O   
9407  O  O   . HOH GA .   ? 0.3488 0.2495 0.4153 0.1031  -0.0046 0.0472  413 HOH B O   
9408  O  O   . HOH GA .   ? 0.4257 1.4756 0.5015 -0.2333 0.0703  -0.3379 414 HOH B O   
9409  O  O   . HOH GA .   ? 0.3118 0.3233 0.3452 0.0244  0.0089  0.0562  415 HOH B O   
9410  O  O   . HOH GA .   ? 0.5148 0.2118 0.2851 -0.0087 0.0939  -0.0274 416 HOH B O   
9411  O  O   . HOH GA .   ? 0.3213 0.4979 0.3528 0.0754  0.0974  -0.0449 417 HOH B O   
9412  O  O   . HOH GA .   ? 0.3923 0.5917 0.2082 0.0917  0.0250  0.0693  418 HOH B O   
9413  O  O   . HOH GA .   ? 0.3278 0.3637 0.3754 0.0412  0.0126  -0.0452 419 HOH B O   
9414  O  O   . HOH GA .   ? 0.3756 0.5625 0.5702 -0.0087 -0.0263 0.0782  420 HOH B O   
9415  O  O   . HOH GA .   ? 0.4490 0.4809 0.2878 0.0627  0.0261  -0.0297 421 HOH B O   
9416  O  O   . HOH GA .   ? 0.1604 0.1811 0.5853 -0.0105 0.0478  0.1114  422 HOH B O   
9417  O  O   . HOH GA .   ? 0.3510 0.9125 0.3829 0.1367  -0.1158 -0.0781 423 HOH B O   
9418  O  O   . HOH GA .   ? 0.5059 0.4569 0.4341 -0.0295 0.0052  0.0737  424 HOH B O   
9419  O  O   . HOH GA .   ? 0.2296 0.3185 0.2574 -0.0546 -0.0275 -0.0328 425 HOH B O   
9420  O  O   . HOH GA .   ? 0.3874 0.2854 0.6092 -0.0511 0.1466  -0.0065 426 HOH B O   
9421  O  O   . HOH GA .   ? 0.3661 0.5127 0.5661 0.1636  -0.0324 -0.0913 427 HOH B O   
9422  O  O   . HOH GA .   ? 0.4162 0.6858 0.5483 0.0439  0.2099  -0.1464 428 HOH B O   
9423  O  O   . HOH GA .   ? 0.5157 0.4722 0.3768 0.2509  0.1207  0.1545  429 HOH B O   
9424  O  O   . HOH GA .   ? 0.1468 0.1138 0.1222 0.0170  0.0392  0.0250  430 HOH B O   
9425  O  O   . HOH GA .   ? 1.0894 0.1057 0.1931 0.1438  0.0097  0.0518  431 HOH B O   
9426  O  O   . HOH GA .   ? 0.6563 0.2472 0.2175 -0.2214 -0.0104 0.0502  432 HOH B O   
9427  O  O   . HOH GA .   ? 0.7580 0.1581 0.6664 0.0041  0.4774  -0.0232 433 HOH B O   
9428  O  O   . HOH GA .   ? 0.1951 0.4676 0.2089 0.0812  0.0337  -0.0295 434 HOH B O   
9429  O  O   . HOH GA .   ? 0.3364 0.4079 0.3583 0.0401  -0.0835 -0.0687 435 HOH B O   
9430  O  O   . HOH GA .   ? 0.2599 0.1568 0.2086 -0.0024 0.0606  -0.0494 436 HOH B O   
9431  O  O   . HOH GA .   ? 0.3808 0.4029 0.5498 0.0621  -0.0498 -0.0948 437 HOH B O   
9432  O  O   . HOH GA .   ? 0.2328 0.1502 0.2062 0.0000  0.0386  -0.0185 438 HOH B O   
9433  O  O   . HOH GA .   ? 0.7818 0.3729 0.6491 -0.0375 -0.1747 0.0641  439 HOH B O   
9434  O  O   . HOH GA .   ? 0.2071 0.4181 0.3450 -0.0443 -0.0137 0.0425  440 HOH B O   
9435  O  O   . HOH GA .   ? 0.3711 0.6607 0.4293 0.2278  0.0458  0.0531  441 HOH B O   
9436  O  O   . HOH GA .   ? 0.3930 0.4493 0.2632 -0.0452 -0.0120 0.0171  442 HOH B O   
9437  O  O   . HOH GA .   ? 0.4070 0.3395 0.4174 0.1695  -0.1554 -0.0496 443 HOH B O   
9438  O  O   . HOH GA .   ? 0.2872 0.5533 0.7170 -0.0196 0.1032  -0.3398 444 HOH B O   
9439  O  O   . HOH GA .   ? 0.3176 0.3729 0.3224 0.1099  0.1288  0.1621  445 HOH B O   
9440  O  O   . HOH GA .   ? 0.2527 0.2707 0.2023 -0.0766 0.0303  0.0421  446 HOH B O   
9441  O  O   . HOH GA .   ? 0.4176 0.2549 0.5812 0.0912  0.0494  -0.0531 447 HOH B O   
9442  O  O   . HOH GA .   ? 0.7182 0.4253 0.5367 0.1555  -0.1447 0.0895  448 HOH B O   
9443  O  O   . HOH GA .   ? 0.1543 0.2163 0.2174 0.0174  0.0271  -0.0121 449 HOH B O   
9444  O  O   . HOH GA .   ? 0.3212 0.3246 0.9974 0.1221  -0.0535 -0.1879 450 HOH B O   
9445  O  O   . HOH GA .   ? 0.3982 0.5072 0.4375 -0.0087 -0.0219 0.0516  451 HOH B O   
9446  O  O   . HOH GA .   ? 0.2025 0.2211 0.1996 -0.0491 -0.0197 0.0590  452 HOH B O   
9447  O  O   . HOH GA .   ? 0.2544 0.2174 0.2897 -0.0219 0.0173  0.0313  453 HOH B O   
9448  O  O   . HOH GA .   ? 0.5896 0.6304 0.7321 -0.0425 -0.3265 0.1381  454 HOH B O   
9449  O  O   . HOH GA .   ? 0.4684 0.3806 0.1912 -0.0353 -0.0654 0.1000  455 HOH B O   
9450  O  O   . HOH GA .   ? 0.1527 0.1893 0.2003 0.0318  0.0140  0.0166  456 HOH B O   
9451  O  O   . HOH GA .   ? 0.3305 0.2476 0.3285 0.0287  0.0533  0.0759  457 HOH B O   
9452  O  O   . HOH GA .   ? 0.3623 0.2563 0.1948 0.0505  -0.0926 0.0141  458 HOH B O   
9453  O  O   . HOH GA .   ? 0.3107 0.2592 0.2481 0.0320  0.0166  0.0263  459 HOH B O   
9454  O  O   . HOH GA .   ? 0.1520 0.1939 0.2475 0.0052  0.0500  0.0493  460 HOH B O   
9455  O  O   . HOH GA .   ? 0.4111 0.3722 0.9688 0.0898  0.2518  0.2242  461 HOH B O   
9456  O  O   . HOH GA .   ? 0.1779 0.1640 0.2156 0.0017  0.0100  0.0370  462 HOH B O   
9457  O  O   . HOH GA .   ? 0.3842 0.1820 0.2723 -0.0657 -0.0612 -0.0066 463 HOH B O   
9458  O  O   . HOH GA .   ? 0.3239 0.5066 0.3862 0.1486  0.1714  0.1563  464 HOH B O   
9459  O  O   . HOH GA .   ? 0.2346 0.2479 0.2246 -0.0768 -0.0274 0.0776  465 HOH B O   
9460  O  O   . HOH GA .   ? 0.4618 0.2351 0.6520 -0.0702 -0.1747 0.1879  466 HOH B O   
9461  O  O   . HOH GA .   ? 0.4413 0.6875 0.3059 -0.0141 -0.1190 0.0878  467 HOH B O   
9462  O  O   . HOH GA .   ? 0.3921 0.7285 0.3544 0.1454  0.1982  0.1279  468 HOH B O   
9463  O  O   . HOH GA .   ? 0.5910 0.4688 0.4622 0.1086  -0.0635 -0.0163 469 HOH B O   
9464  O  O   . HOH GA .   ? 0.3797 0.5133 0.3240 0.0776  -0.0476 -0.0535 470 HOH B O   
9465  O  O   . HOH GA .   ? 0.2463 0.2151 0.1536 0.0447  0.0184  0.0204  471 HOH B O   
9466  O  O   . HOH GA .   ? 0.3770 0.5978 0.2734 0.0851  0.0885  -0.1977 472 HOH B O   
9467  O  O   . HOH GA .   ? 0.1468 0.1058 0.1509 -0.0087 0.0074  0.0333  473 HOH B O   
9468  O  O   . HOH GA .   ? 0.6593 0.4323 0.8632 0.0131  0.0953  0.2576  474 HOH B O   
9469  O  O   . HOH GA .   ? 0.1247 0.1197 0.1062 0.0298  0.0273  0.0221  475 HOH B O   
9470  O  O   . HOH GA .   ? 0.2578 0.2048 0.1633 0.0807  -0.0091 -0.0066 476 HOH B O   
9471  O  O   . HOH GA .   ? 0.5188 0.4658 0.3946 0.1190  0.0080  0.0368  477 HOH B O   
9472  O  O   . HOH GA .   ? 0.2014 0.1190 0.1482 -0.0024 0.0277  0.0537  478 HOH B O   
9473  O  O   . HOH GA .   ? 0.2576 0.2206 0.2249 -0.0120 0.0262  0.0175  479 HOH B O   
9474  O  O   . HOH GA .   ? 0.2319 0.3089 0.9746 -0.0043 0.2585  0.1837  480 HOH B O   
9475  O  O   . HOH GA .   ? 0.3486 0.2145 0.1547 -0.0485 0.0228  -0.0098 481 HOH B O   
9476  O  O   . HOH GA .   ? 0.1296 0.0985 0.1847 -0.0049 -0.0019 0.0097  482 HOH B O   
9477  O  O   . HOH GA .   ? 0.2811 0.2673 0.3657 -0.1094 0.0333  0.0395  483 HOH B O   
9478  O  O   . HOH GA .   ? 0.3339 0.3255 0.2811 0.0494  0.0098  -0.0186 484 HOH B O   
9479  O  O   . HOH GA .   ? 0.2994 0.2239 0.2230 0.0676  -0.0964 -0.0439 485 HOH B O   
9480  O  O   . HOH GA .   ? 0.2280 0.2398 0.2138 0.0082  0.0344  0.0626  486 HOH B O   
9481  O  O   . HOH GA .   ? 0.1667 0.3759 0.2269 0.0362  0.0441  0.0582  487 HOH B O   
9482  O  O   . HOH GA .   ? 0.2657 0.3695 0.2755 0.0401  0.0689  -0.0038 488 HOH B O   
9483  O  O   . HOH GA .   ? 0.1775 0.1001 0.1337 -0.0098 0.0575  0.0105  489 HOH B O   
9484  O  O   . HOH GA .   ? 0.4573 0.2263 0.2293 -0.0140 -0.0276 -0.0087 490 HOH B O   
9485  O  O   . HOH GA .   ? 0.4219 0.1849 0.3896 -0.0820 -0.0555 -0.0573 491 HOH B O   
9486  O  O   . HOH GA .   ? 0.3643 0.1881 0.7526 -0.0068 -0.1497 -0.1256 492 HOH B O   
9487  O  O   . HOH GA .   ? 0.1116 0.1172 0.3930 -0.0100 -0.0251 -0.0060 493 HOH B O   
9488  O  O   . HOH GA .   ? 0.5659 0.4232 0.3711 -0.3070 0.1404  -0.0526 494 HOH B O   
9489  O  O   . HOH GA .   ? 0.4972 0.3323 0.2720 0.1723  0.0817  0.0419  495 HOH B O   
9490  O  O   . HOH GA .   ? 0.2612 0.2247 0.1696 0.0110  -0.0417 -0.0516 496 HOH B O   
9491  O  O   . HOH GA .   ? 0.2100 0.1637 0.2088 0.0251  -0.0230 0.0103  497 HOH B O   
9492  O  O   . HOH GA .   ? 0.1071 0.0935 0.1353 0.0051  0.0324  0.0237  498 HOH B O   
9493  O  O   . HOH GA .   ? 0.2815 0.1493 0.4569 -0.0313 -0.1216 0.0935  499 HOH B O   
9494  O  O   . HOH GA .   ? 0.1233 0.1301 0.1391 0.0000  0.0181  0.0244  500 HOH B O   
9495  O  O   . HOH GA .   ? 0.3797 0.2104 0.2333 -0.0132 -0.0568 0.0252  501 HOH B O   
9496  O  O   . HOH GA .   ? 0.2068 0.2213 0.2416 0.0854  0.0185  0.0359  502 HOH B O   
9497  O  O   . HOH GA .   ? 0.3050 0.2020 0.3328 0.0161  -0.0979 0.0147  503 HOH B O   
9498  O  O   . HOH GA .   ? 0.3276 0.2888 0.3057 0.0251  -0.0170 -0.0098 504 HOH B O   
9499  O  O   . HOH GA .   ? 0.4169 0.4907 0.2903 0.1269  0.0368  0.0417  505 HOH B O   
9500  O  O   . HOH GA .   ? 0.4918 0.2529 0.2707 0.1541  -0.0329 -0.0254 506 HOH B O   
9501  O  O   . HOH GA .   ? 0.1504 0.2378 0.3702 0.0143  0.0505  0.0471  507 HOH B O   
9502  O  O   . HOH GA .   ? 0.1832 0.1935 0.2461 -0.0254 0.0535  0.0557  508 HOH B O   
9503  O  O   . HOH GA .   ? 0.2982 0.4436 0.6125 -0.1389 0.0243  0.0601  509 HOH B O   
9504  O  O   . HOH GA .   ? 0.1951 0.1676 0.2759 -0.0285 0.0723  -0.0138 510 HOH B O   
9505  O  O   . HOH GA .   ? 0.2887 0.2736 0.3084 -0.0068 -0.0086 -0.0065 511 HOH B O   
9506  O  O   . HOH GA .   ? 0.1656 0.0998 0.2166 0.0043  -0.0094 -0.0093 512 HOH B O   
9507  O  O   . HOH GA .   ? 0.2642 0.4068 0.3966 0.0329  -0.0675 0.0313  513 HOH B O   
9508  O  O   . HOH GA .   ? 0.2606 0.1556 0.2406 -0.0348 -0.0362 0.0524  514 HOH B O   
9509  O  O   . HOH GA .   ? 0.3100 0.5839 0.3280 0.0375  0.0520  -0.0643 515 HOH B O   
9510  O  O   . HOH GA .   ? 0.3070 0.5343 0.4846 0.0445  0.0927  -0.1907 516 HOH B O   
9511  O  O   . HOH GA .   ? 0.1942 0.1407 0.2992 0.0051  0.0373  -0.0230 517 HOH B O   
9512  O  O   . HOH GA .   ? 0.2052 0.3768 0.6003 0.1288  0.1509  0.2727  518 HOH B O   
9513  O  O   . HOH GA .   ? 0.2255 0.2714 0.1768 -0.0342 0.0315  0.0447  519 HOH B O   
9514  O  O   . HOH GA .   ? 0.2152 0.2840 0.1942 0.0758  0.0406  0.0412  520 HOH B O   
9515  O  O   . HOH GA .   ? 0.2836 0.3086 0.2199 0.0555  0.0815  0.0055  521 HOH B O   
9516  O  O   . HOH GA .   ? 0.2579 0.4305 0.7379 0.0154  0.0861  -0.2987 522 HOH B O   
9517  O  O   . HOH GA .   ? 0.3763 0.4507 0.2314 0.0006  -0.0718 0.1570  523 HOH B O   
9518  O  O   . HOH GA .   ? 0.2892 0.1653 0.2615 -0.0222 0.0231  -0.0527 524 HOH B O   
9519  O  O   . HOH GA .   ? 0.2676 0.2014 0.2578 -0.0388 -0.0046 0.0702  525 HOH B O   
9520  O  O   . HOH GA .   ? 0.5357 0.4390 0.3093 -0.2240 -0.0750 0.0939  526 HOH B O   
9521  O  O   . HOH GA .   ? 0.1414 0.2118 0.2387 -0.0425 0.0500  0.0507  527 HOH B O   
9522  O  O   . HOH GA .   ? 0.1152 0.0933 0.1659 -0.0083 0.0070  0.0276  528 HOH B O   
9523  O  O   . HOH GA .   ? 0.1603 0.1633 0.2549 0.0142  -0.0043 0.0278  529 HOH B O   
9524  O  O   . HOH GA .   ? 0.2782 0.1829 0.6265 -0.0052 -0.0304 -0.1010 530 HOH B O   
9525  O  O   . HOH GA .   ? 0.5709 0.5981 0.5874 0.1920  -0.0362 -0.2272 531 HOH B O   
9526  O  O   . HOH GA .   ? 0.2725 0.2890 0.3009 -0.0401 0.0027  -0.0164 532 HOH B O   
9527  O  O   . HOH GA .   ? 0.4785 0.5676 0.1827 -0.2184 0.0192  0.0615  533 HOH B O   
9528  O  O   . HOH GA .   ? 0.4117 0.3747 0.2655 0.1375  0.1368  0.0118  534 HOH B O   
9529  O  O   . HOH GA .   ? 0.2763 0.6495 0.2709 -0.0540 -0.0458 -0.0001 535 HOH B O   
9530  O  O   . HOH GA .   ? 0.1835 0.0985 0.2057 0.0436  0.0280  -0.0037 536 HOH B O   
9531  O  O   . HOH GA .   ? 0.1005 0.0802 0.1419 0.0031  0.0116  0.0227  537 HOH B O   
9532  O  O   . HOH GA .   ? 0.3282 0.2301 0.1130 0.0665  0.0588  0.0186  538 HOH B O   
9533  O  O   . HOH GA .   ? 0.2878 0.2236 0.2244 -0.0271 -0.0584 0.0344  539 HOH B O   
9534  O  O   . HOH GA .   ? 0.5322 0.4598 0.3079 0.0509  0.0599  -0.0551 540 HOH B O   
9535  O  O   . HOH GA .   ? 0.1307 0.0965 0.1082 0.0077  0.0445  0.0324  541 HOH B O   
9536  O  O   . HOH GA .   ? 0.1829 0.1684 0.1450 0.0236  0.0226  0.0142  542 HOH B O   
9537  O  O   . HOH GA .   ? 0.4712 0.4609 0.2115 -0.1325 0.0288  -0.0839 543 HOH B O   
9538  O  O   . HOH GA .   ? 0.3973 0.2078 0.2538 -0.1081 0.0588  -0.0027 544 HOH B O   
9539  O  O   . HOH GA .   ? 0.1536 0.2497 0.1802 -0.0027 0.0502  0.0716  545 HOH B O   
9540  O  O   . HOH GA .   ? 0.2592 0.2960 0.3467 0.0449  0.0944  0.0546  546 HOH B O   
9541  O  O   . HOH GA .   ? 0.2425 0.2048 0.3781 -0.0461 -0.0614 0.0654  547 HOH B O   
9542  O  O   . HOH GA .   ? 0.2384 0.9072 0.3528 -0.0248 -0.0044 0.2547  548 HOH B O   
9543  O  O   . HOH GA .   ? 0.1984 0.1917 0.2030 -0.0156 0.0337  0.0623  549 HOH B O   
9544  O  O   . HOH GA .   ? 0.2834 0.1604 0.1689 0.0146  0.1008  0.0310  550 HOH B O   
9545  O  O   . HOH GA .   ? 0.3878 0.2211 0.7351 0.0010  0.0768  -0.0366 551 HOH B O   
9546  O  O   . HOH GA .   ? 2.0487 0.1114 0.4864 0.2052  0.3928  0.1143  552 HOH B O   
9547  O  O   . HOH GA .   ? 0.3914 0.4041 0.2745 0.0214  -0.0640 0.1028  553 HOH B O   
9548  O  O   . HOH GA .   ? 0.4433 0.1570 0.4257 0.0631  -0.1143 0.0153  554 HOH B O   
9549  O  O   . HOH GA .   ? 0.5983 0.4566 0.4079 0.0562  0.1243  -0.0969 555 HOH B O   
9550  O  O   . HOH GA .   ? 0.2215 0.1865 0.2359 -0.0074 0.1191  -0.0231 556 HOH B O   
9551  O  O   . HOH GA .   ? 0.3267 0.3010 0.3366 -0.0037 0.1539  0.0864  557 HOH B O   
9552  O  O   . HOH GA .   ? 0.4803 0.3957 0.3817 -0.2010 0.1968  -0.0719 558 HOH B O   
9553  O  O   . HOH GA .   ? 0.8248 1.9332 0.6211 1.0214  -0.6579 -0.8140 559 HOH B O   
9554  O  O   . HOH GA .   ? 0.2843 0.2603 0.2127 0.0081  0.0040  0.0544  560 HOH B O   
9555  O  O   . HOH GA .   ? 0.3635 0.3504 0.5691 -0.0916 0.0837  0.0000  561 HOH B O   
9556  O  O   . HOH GA .   ? 0.3573 0.3226 0.3693 -0.1233 -0.0640 0.0644  562 HOH B O   
9557  O  O   . HOH GA .   ? 0.3370 0.2982 0.5914 -0.0445 -0.0135 0.1767  563 HOH B O   
9558  O  O   . HOH GA .   ? 0.3251 0.2361 0.3012 -0.0148 0.0658  -0.0678 564 HOH B O   
9559  O  O   . HOH GA .   ? 0.4099 0.6097 0.3722 0.0205  -0.1120 -0.0778 565 HOH B O   
9560  O  O   . HOH GA .   ? 0.4493 0.3088 0.3016 -0.1500 -0.0582 0.1178  566 HOH B O   
9561  O  O   . HOH GA .   ? 0.2904 0.2406 0.1893 0.0043  0.0799  0.0124  567 HOH B O   
9562  O  O   . HOH GA .   ? 0.2064 0.3336 0.3666 0.0888  0.0966  0.1200  568 HOH B O   
9563  O  O   . HOH GA .   ? 0.3255 0.3461 0.1080 -0.0507 0.0103  0.0768  569 HOH B O   
9564  O  O   . HOH GA .   ? 0.3772 0.4907 0.2344 -0.0192 0.0491  0.1595  570 HOH B O   
9565  O  O   . HOH GA .   ? 0.2230 0.4286 0.3434 -0.1206 0.1278  -0.0326 571 HOH B O   
9566  O  O   . HOH GA .   ? 0.5149 0.3964 0.2651 0.0333  0.1133  0.0408  572 HOH B O   
9567  O  O   . HOH GA .   ? 0.8744 0.1669 0.3883 -0.0206 -0.3930 0.0593  573 HOH B O   
9568  O  O   . HOH GA .   ? 0.1278 0.2415 0.2829 -0.0392 -0.0226 0.0632  574 HOH B O   
9569  O  O   . HOH GA .   ? 0.2597 0.2901 0.2689 -0.0751 -0.0381 0.0277  575 HOH B O   
9570  O  O   . HOH GA .   ? 0.2770 0.2567 0.4429 0.0740  0.0773  0.0610  576 HOH B O   
9571  O  O   . HOH GA .   ? 0.2906 0.2680 0.4264 -0.0254 -0.1233 0.0116  577 HOH B O   
9572  O  O   . HOH GA .   ? 0.2178 0.1263 0.1457 0.0038  -0.0137 -0.0065 578 HOH B O   
9573  O  O   . HOH GA .   ? 0.2100 0.1456 0.2041 -0.0031 0.0507  0.0000  579 HOH B O   
9574  O  O   . HOH GA .   ? 0.2574 0.2366 0.1843 -0.0236 0.0049  0.0579  580 HOH B O   
9575  O  O   . HOH GA .   ? 0.1994 0.2285 0.2563 -0.0471 0.0741  0.0147  581 HOH B O   
9576  O  O   . HOH GA .   ? 0.6636 0.2989 0.2316 -0.1121 0.0756  -0.0763 582 HOH B O   
9577  O  O   . HOH GA .   ? 0.3303 0.5939 0.1520 -0.0617 -0.0015 0.0127  583 HOH B O   
9578  O  O   . HOH GA .   ? 0.5511 0.5435 0.2856 0.2412  -0.0294 -0.0375 584 HOH B O   
9579  O  O   . HOH GA .   ? 0.4778 0.3591 0.3111 -0.0610 0.0337  0.0015  585 HOH B O   
9580  O  O   . HOH GA .   ? 0.4480 0.3321 0.3639 0.1203  -0.0037 -0.0414 586 HOH B O   
9581  O  O   . HOH GA .   ? 0.3327 0.6213 0.4189 -0.1474 -0.0262 0.1660  587 HOH B O   
9582  O  O   . HOH GA .   ? 0.3264 0.5094 0.3411 0.1471  0.0529  -0.0337 588 HOH B O   
9583  O  O   . HOH GA .   ? 0.2657 0.5311 0.4533 -0.0006 0.1404  0.2284  589 HOH B O   
9584  O  O   . HOH GA .   ? 0.4408 0.3468 0.6464 0.0993  -0.0637 -0.2084 590 HOH B O   
9585  O  O   . HOH GA .   ? 0.2596 0.2563 0.3377 0.0935  -0.0551 -0.0824 591 HOH B O   
9586  O  O   . HOH GA .   ? 0.4352 0.4602 0.4501 0.1638  -0.0834 -0.0860 592 HOH B O   
9587  O  O   . HOH GA .   ? 0.1500 0.2007 0.2994 -0.0568 0.0082  0.0010  593 HOH B O   
9588  O  O   . HOH GA .   ? 0.1326 0.1274 0.1912 -0.0097 0.0007  0.0454  594 HOH B O   
9589  O  O   . HOH GA .   ? 0.1195 0.1147 0.1429 -0.0102 0.0218  0.0179  595 HOH B O   
9590  O  O   . HOH GA .   ? 0.2134 0.0903 0.3052 -0.0126 -0.0944 0.0043  596 HOH B O   
9591  O  O   . HOH GA .   ? 0.2258 0.2267 0.5307 -0.0377 0.1590  0.0983  597 HOH B O   
9592  O  O   . HOH GA .   ? 0.1498 0.2504 0.2023 0.0245  0.0249  0.0000  598 HOH B O   
9593  O  O   . HOH GA .   ? 0.6434 0.3659 0.2619 -0.2151 0.0154  -0.0509 599 HOH B O   
9594  O  O   . HOH GA .   ? 0.2820 0.1450 0.2080 0.0395  0.0991  -0.0060 600 HOH B O   
9595  O  O   . HOH GA .   ? 0.4505 0.2433 0.1561 0.0130  0.0740  -0.0120 601 HOH B O   
9596  O  O   . HOH GA .   ? 0.2569 0.3097 0.1542 0.0746  0.0264  -0.0083 602 HOH B O   
9597  O  O   . HOH GA .   ? 0.5724 0.3871 0.3465 -0.2883 0.0043  0.0696  603 HOH B O   
9598  O  O   . HOH GA .   ? 0.2946 0.3768 0.6510 -0.0401 -0.0200 0.2960  604 HOH B O   
9599  O  O   . HOH GA .   ? 0.5723 0.2540 0.4857 0.0401  0.0068  -0.0614 605 HOH B O   
9600  O  O   . HOH GA .   ? 0.3533 0.3393 0.3018 0.0434  -0.0456 -0.0164 606 HOH B O   
9601  O  O   . HOH GA .   ? 0.1975 0.2565 0.2547 0.0107  0.0038  0.0681  607 HOH B O   
9602  O  O   . HOH GA .   ? 0.3235 0.6704 0.2014 0.1492  0.0306  0.0297  608 HOH B O   
9603  O  O   . HOH GA .   ? 0.2493 0.3319 0.1648 0.0516  0.0684  0.0700  609 HOH B O   
9604  O  O   . HOH GA .   ? 0.3197 0.2287 0.1680 -0.1208 -0.0296 0.0504  610 HOH B O   
9605  O  O   . HOH GA .   ? 0.2066 0.2906 0.2901 -0.0989 0.0542  0.0650  611 HOH B O   
9606  O  O   . HOH GA .   ? 0.3325 0.2423 0.4923 0.0403  0.0390  0.0062  612 HOH B O   
9607  O  O   . HOH GA .   ? 0.1200 0.1524 0.1375 -0.0164 0.0287  0.0234  613 HOH B O   
9608  O  O   . HOH GA .   ? 0.5049 0.4377 0.7750 0.1840  -0.1272 -0.1263 614 HOH B O   
9609  O  O   . HOH GA .   ? 0.4756 0.4526 0.5371 -0.0170 0.0373  -0.0138 615 HOH B O   
9610  O  O   . HOH GA .   ? 0.3770 0.3014 0.7134 -0.0149 0.2443  0.1177  616 HOH B O   
9611  O  O   . HOH GA .   ? 0.3382 0.2245 0.3513 -0.0680 -0.0740 0.0976  617 HOH B O   
9612  O  O   . HOH GA .   ? 1.1310 0.3601 0.5496 -0.3242 -0.2177 0.0065  618 HOH B O   
9613  O  O   . HOH GA .   ? 0.3319 0.4133 0.3014 -0.0579 0.0010  0.2389  619 HOH B O   
9614  O  O   . HOH GA .   ? 0.4522 0.4860 0.7505 0.0055  0.0810  -0.3057 620 HOH B O   
9615  O  O   . HOH GA .   ? 0.2752 0.8647 0.1253 -0.1035 0.0043  0.0020  621 HOH B O   
9616  O  O   . HOH GA .   ? 0.1705 0.2813 0.2967 0.0434  0.0412  0.1476  622 HOH B O   
9617  O  O   . HOH GA .   ? 0.3916 0.2847 0.3048 -0.0918 -0.0048 0.1081  623 HOH B O   
9618  O  O   . HOH GA .   ? 0.3361 0.5080 0.2529 0.1125  -0.0115 0.0149  624 HOH B O   
9619  O  O   . HOH GA .   ? 0.4435 0.2479 0.5152 -0.0230 -0.0992 0.1127  625 HOH B O   
9620  O  O   . HOH GA .   ? 0.6417 0.2284 0.4654 0.1506  0.2847  0.1044  626 HOH B O   
9621  O  O   . HOH GA .   ? 0.6269 0.2842 0.2775 0.0445  -0.0324 -0.0540 627 HOH B O   
9622  O  O   . HOH GA .   ? 0.6704 0.3492 0.4142 0.2445  0.2128  0.1391  628 HOH B O   
9623  O  O   . HOH GA .   ? 0.2163 0.2230 0.2314 0.0315  0.0304  -0.0348 629 HOH B O   
9624  O  O   . HOH GA .   ? 0.4151 0.4054 0.6438 -0.1567 -0.0869 0.2378  630 HOH B O   
9625  O  O   . HOH GA .   ? 0.7850 0.3763 0.7378 0.2615  0.4352  0.2827  631 HOH B O   
9626  O  O   . HOH GA .   ? 0.2689 0.2892 0.4440 -0.0997 0.1133  -0.0406 632 HOH B O   
9627  O  O   . HOH GA .   ? 0.7935 0.3424 0.2669 0.2049  0.1031  0.0944  633 HOH B O   
9628  O  O   . HOH GA .   ? 0.1806 0.2630 0.2413 0.0003  0.0228  -0.0395 634 HOH B O   
9629  O  O   . HOH GA .   ? 0.1905 0.3411 0.4255 0.0049  0.0874  0.0353  635 HOH B O   
9630  O  O   . HOH GA .   ? 0.2657 0.4097 0.3097 0.0974  0.0573  0.0416  636 HOH B O   
9631  O  O   . HOH GA .   ? 0.2885 0.3041 0.4232 -0.0259 0.0038  0.0421  637 HOH B O   
9632  O  O   . HOH GA .   ? 0.3562 0.2730 0.1728 -0.0544 -0.0964 0.0410  638 HOH B O   
9633  O  O   . HOH GA .   ? 0.4043 0.2254 0.3010 0.0421  0.1715  0.0581  639 HOH B O   
9634  O  O   . HOH GA .   ? 0.4347 0.3330 0.3601 -0.0353 0.0381  -0.1121 640 HOH B O   
9635  O  O   . HOH GA .   ? 0.4943 0.3167 0.3874 0.0359  0.0241  0.0944  641 HOH B O   
9636  O  O   . HOH GA .   ? 0.8483 0.3612 0.4408 0.0172  -0.2840 -0.0153 642 HOH B O   
9637  O  O   . HOH GA .   ? 0.2463 0.3154 0.4018 0.0807  0.1228  0.0366  643 HOH B O   
9638  O  O   . HOH GA .   ? 0.2138 0.2847 0.2775 0.0054  -0.0579 0.0086  644 HOH B O   
9639  O  O   . HOH GA .   ? 0.3700 0.2664 0.6772 0.0271  -0.0505 0.0846  645 HOH B O   
9640  O  O   . HOH GA .   ? 0.1811 0.1296 0.2330 -0.0120 -0.0057 -0.0054 646 HOH B O   
9641  O  O   . HOH GA .   ? 0.2400 0.2903 0.3488 0.0082  0.0020  0.0172  647 HOH B O   
9642  O  O   . HOH GA .   ? 0.3833 0.4377 0.2766 0.1810  0.0337  -0.0092 648 HOH B O   
9643  O  O   . HOH GA .   ? 0.3508 0.2587 0.3449 0.0688  0.0590  -0.0049 649 HOH B O   
9644  O  O   . HOH GA .   ? 0.4228 0.3610 0.3885 0.0592  0.0092  0.0366  650 HOH B O   
9645  O  O   . HOH GA .   ? 0.8230 0.2781 0.3779 -0.0899 0.0608  0.0434  651 HOH B O   
9646  O  O   . HOH GA .   ? 0.3273 0.4426 0.3727 -0.0379 0.0163  -0.1085 652 HOH B O   
9647  O  O   . HOH GA .   ? 0.4632 0.7515 0.2581 -0.1005 0.1632  -0.0916 653 HOH B O   
9648  O  O   . HOH GA .   ? 0.4099 0.4268 0.3073 0.1343  0.0035  -0.0087 654 HOH B O   
9649  O  O   . HOH GA .   ? 0.3750 0.4855 0.3885 -0.0513 -0.0324 0.0549  655 HOH B O   
9650  O  O   . HOH GA .   ? 0.4508 0.3255 0.6464 0.2197  0.3138  0.2881  656 HOH B O   
9651  O  O   . HOH GA .   ? 0.2883 0.2021 0.3046 -0.0130 -0.0357 0.0386  657 HOH B O   
9652  O  O   . HOH GA .   ? 0.4074 0.5350 0.7713 -0.1116 0.2552  -0.0976 658 HOH B O   
9653  O  O   . HOH GA .   ? 0.3639 0.6265 0.3838 0.1465  0.0826  -0.0197 659 HOH B O   
9654  O  O   . HOH GA .   ? 0.4305 0.3623 0.3149 -0.0355 -0.1571 0.0322  660 HOH B O   
9655  O  O   . HOH GA .   ? 0.3400 0.4681 1.3865 -0.0211 -0.1184 -0.3720 661 HOH B O   
9656  O  O   . HOH GA .   ? 0.5425 0.5127 0.4716 -0.1111 -0.0379 -0.0467 662 HOH B O   
9657  O  O   . HOH GA .   ? 0.4874 0.5509 0.6251 0.1536  -0.2256 -0.2396 663 HOH B O   
9658  O  O   . HOH GA .   ? 0.7134 0.2795 0.6108 0.1281  -0.2413 -0.0222 664 HOH B O   
9659  O  O   . HOH GA .   ? 0.5821 0.5960 0.5310 0.2296  0.2421  -0.0731 665 HOH B O   
9660  O  O   . HOH GA .   ? 0.7343 0.2926 0.6420 0.0133  0.1518  0.1722  666 HOH B O   
9661  O  O   . HOH GA .   ? 0.6589 0.5590 0.2737 -0.0104 -0.0107 -0.1010 667 HOH B O   
9662  O  O   . HOH GA .   ? 0.4778 0.4241 0.4684 -0.1321 -0.0390 0.1194  668 HOH B O   
9663  O  O   . HOH GA .   ? 0.1863 0.1926 0.7333 -0.0001 0.0041  0.0705  669 HOH B O   
9664  O  O   . HOH GA .   ? 0.7080 0.2951 0.4623 -0.1585 -0.0755 0.0597  670 HOH B O   
9665  O  O   . HOH GA .   ? 0.4269 0.5701 0.5095 0.0362  0.0157  0.1784  671 HOH B O   
9666  O  O   . HOH GA .   ? 0.4801 1.0650 0.3846 0.0252  -0.0384 0.1656  672 HOH B O   
9667  O  O   . HOH GA .   ? 0.3093 0.3190 0.1982 0.0882  0.0494  0.0553  673 HOH B O   
9668  O  O   . HOH GA .   ? 0.7311 0.3679 0.4034 0.0916  0.0372  -0.0148 674 HOH B O   
9669  O  O   . HOH GA .   ? 0.3255 0.1996 0.2739 -0.0679 -0.0498 0.0626  675 HOH B O   
9670  O  O   . HOH GA .   ? 0.4806 0.3691 0.2811 0.1528  0.0754  0.0230  676 HOH B O   
9671  O  O   . HOH GA .   ? 0.7203 0.3014 0.8468 -0.0384 0.4641  -0.0883 677 HOH B O   
9672  O  O   . HOH GA .   ? 0.6455 0.3142 1.0300 0.0929  0.2085  0.1114  678 HOH B O   
9673  O  O   . HOH GA .   ? 0.4203 0.4207 0.3634 -0.2230 0.1243  -0.0289 679 HOH B O   
9674  O  O   . HOH GA .   ? 0.2193 0.4801 0.5885 0.0038  -0.0397 -0.0886 680 HOH B O   
9675  O  O   . HOH GA .   ? 0.4816 0.3447 0.2998 0.0599  -0.0634 0.0359  681 HOH B O   
9676  O  O   . HOH GA .   ? 0.5365 0.3292 0.4205 0.0406  -0.0652 0.1251  682 HOH B O   
9677  O  O   . HOH GA .   ? 0.2554 0.3343 0.5264 0.0008  -0.0504 0.1799  683 HOH B O   
9678  O  O   . HOH GA .   ? 0.6578 0.5551 0.2612 -0.3357 0.0754  0.0487  684 HOH B O   
9679  O  O   . HOH GA .   ? 0.6757 0.6161 0.2633 -0.3440 0.0110  0.0364  685 HOH B O   
9680  O  O   . HOH GA .   ? 0.5904 0.3571 0.4697 -0.0166 -0.0828 0.0370  686 HOH B O   
9681  O  O   . HOH GA .   ? 0.4099 0.3244 0.3036 0.0926  -0.0052 0.1094  687 HOH B O   
9682  O  O   . HOH GA .   ? 0.3932 0.7069 0.3253 0.0436  -0.0557 0.1086  688 HOH B O   
9683  O  O   . HOH GA .   ? 0.5593 0.2142 0.3346 0.0714  -0.1439 -0.0491 689 HOH B O   
9684  O  O   . HOH GA .   ? 0.1500 1.0040 0.2386 -0.0595 0.0328  -0.1340 690 HOH B O   
9685  O  O   . HOH GA .   ? 0.4365 0.6086 0.6008 -0.1430 -0.0185 -0.0302 691 HOH B O   
9686  O  O   . HOH GA .   ? 0.2572 1.1725 0.2858 -0.0373 -0.0068 0.0408  692 HOH B O   
9687  O  O   . HOH GA .   ? 0.3503 0.3535 0.5271 0.0918  -0.1155 -0.0551 693 HOH B O   
9688  O  O   . HOH GA .   ? 0.2759 0.2858 0.4939 -0.0680 0.0741  0.1058  694 HOH B O   
9689  O  O   . HOH GA .   ? 0.6474 0.9240 0.4160 0.0645  -0.0126 -0.1049 695 HOH B O   
9690  O  O   . HOH GA .   ? 0.2476 0.4232 0.3289 -0.0463 -0.0244 0.0233  696 HOH B O   
9691  O  O   . HOH GA .   ? 0.3984 0.3899 0.3639 -0.0219 -0.0238 -0.0821 697 HOH B O   
9692  O  O   . HOH GA .   ? 0.2861 0.3916 0.2267 -0.0489 0.0443  0.0982  698 HOH B O   
9693  O  O   . HOH GA .   ? 0.3702 0.2506 0.5861 -0.0601 0.1014  -0.1894 699 HOH B O   
9694  O  O   . HOH GA .   ? 0.4178 0.2240 0.5795 0.0181  -0.1835 -0.0261 700 HOH B O   
9695  O  O   . HOH GA .   ? 0.4343 0.2694 0.3573 -0.0065 -0.0288 -0.0240 701 HOH B O   
9696  O  O   . HOH GA .   ? 0.1797 0.1921 0.2301 0.0107  0.0120  0.0582  702 HOH B O   
9697  O  O   . HOH GA .   ? 0.3380 0.2527 0.3431 0.0027  0.0597  0.0729  703 HOH B O   
9698  O  O   . HOH GA .   ? 0.3661 0.3479 0.1932 0.0635  0.0480  -0.0063 704 HOH B O   
9699  O  O   . HOH GA .   ? 0.8338 0.3316 0.4027 0.2078  -0.0608 0.0414  705 HOH B O   
9700  O  O   . HOH GA .   ? 0.6615 0.5206 0.3463 0.1689  0.1397  0.1272  706 HOH B O   
9701  O  O   . HOH GA .   ? 0.4133 0.4421 0.2293 -0.0619 0.0520  0.0427  707 HOH B O   
9702  O  O   . HOH GA .   ? 0.4426 0.2231 0.2935 0.0060  0.1143  -0.0430 708 HOH B O   
9703  O  O   . HOH GA .   ? 0.1689 0.2718 0.6101 -0.0372 0.0551  0.0910  709 HOH B O   
9704  O  O   . HOH GA .   ? 0.3016 0.2693 0.5321 -0.0118 0.1655  0.0259  710 HOH B O   
9705  O  O   . HOH GA .   ? 0.4244 0.3772 0.3064 0.1879  0.0803  0.0063  711 HOH B O   
9706  O  O   . HOH GA .   ? 0.7366 0.2210 0.2933 -0.1599 0.0306  0.0443  712 HOH B O   
9707  O  O   . HOH GA .   ? 0.2055 0.3151 0.6966 -0.0518 -0.0531 0.0252  713 HOH B O   
9708  O  O   . HOH GA .   ? 0.4921 0.3725 0.5723 0.2416  -0.0196 -0.0146 714 HOH B O   
9709  O  O   . HOH GA .   ? 0.3833 0.7475 0.2231 -0.0031 -0.0816 0.0239  715 HOH B O   
9710  O  O   . HOH GA .   ? 0.3659 0.2703 0.4773 0.0855  0.2161  0.1468  716 HOH B O   
9711  O  O   . HOH GA .   ? 0.5343 0.2080 0.5726 -0.0471 0.2169  -0.0469 717 HOH B O   
9712  O  O   . HOH GA .   ? 0.5467 0.3167 0.5680 -0.1917 0.3407  -0.2001 718 HOH B O   
9713  O  O   . HOH GA .   ? 0.7630 0.3278 0.3388 -0.0164 -0.0931 -0.0233 719 HOH B O   
9714  O  O   . HOH GA .   ? 0.4241 0.3995 0.3253 -0.0100 0.1368  0.0212  720 HOH B O   
9715  O  O   . HOH GA .   ? 0.3912 0.5224 0.4482 -0.1172 -0.0342 0.2549  721 HOH B O   
9716  O  O   . HOH GA .   ? 0.3765 0.6514 0.4411 0.1551  -0.0498 -0.0489 722 HOH B O   
9717  O  O   . HOH GA .   ? 0.7275 0.3555 0.2748 0.1621  -0.0720 0.0636  723 HOH B O   
9718  O  O   . HOH GA .   ? 0.2957 0.3158 1.1051 0.0496  -0.0631 0.1720  724 HOH B O   
9719  O  O   . HOH GA .   ? 0.9851 0.7077 0.4316 0.0531  0.1032  0.0487  725 HOH B O   
9720  O  O   . HOH GA .   ? 0.3470 0.3125 0.3289 -0.0068 0.0296  0.1592  726 HOH B O   
9721  O  O   . HOH GA .   ? 0.3319 0.4447 0.2867 0.0313  0.0219  0.1107  727 HOH B O   
9722  O  O   . HOH GA .   ? 0.1651 0.2588 0.1756 0.0046  0.0560  0.0209  728 HOH B O   
9723  O  O   . HOH GA .   ? 0.2642 0.2773 0.2470 -0.0432 -0.0215 0.0364  729 HOH B O   
9724  O  O   . HOH GA .   ? 0.6643 0.6258 0.2662 0.0157  0.0038  -0.1494 730 HOH B O   
9725  O  O   . HOH GA .   ? 0.3526 0.3079 0.3490 0.0386  -0.0164 0.0812  731 HOH B O   
9726  O  O   . HOH GA .   ? 0.7350 0.2565 0.3197 0.0625  0.2358  0.0797  732 HOH B O   
9727  O  O   . HOH GA .   ? 0.2730 0.4302 0.3465 0.0074  0.1053  0.0193  733 HOH B O   
9728  O  O   . HOH GA .   ? 1.0260 0.1972 0.2197 0.0399  0.1212  0.0649  734 HOH B O   
9729  O  O   . HOH GA .   ? 0.7673 0.6470 0.5286 0.3348  -0.1899 -0.1474 735 HOH B O   
9730  O  O   . HOH GA .   ? 0.3438 0.3429 0.3158 0.1372  -0.0513 -0.0507 736 HOH B O   
9731  O  O   . HOH GA .   ? 0.4755 0.4758 0.4666 0.0020  -0.0421 -0.0628 737 HOH B O   
9732  O  O   . HOH GA .   ? 0.3668 0.2405 0.9404 -0.0062 0.0228  -0.2578 738 HOH B O   
9733  O  O   . HOH GA .   ? 0.5249 0.2264 0.5816 0.0142  -0.1209 -0.0185 739 HOH B O   
9734  O  O   . HOH GA .   ? 0.4269 0.8558 0.5343 0.0936  -0.0822 -0.3307 740 HOH B O   
9735  O  O   . HOH GA .   ? 0.6917 0.4970 0.8511 0.2299  -0.1353 -0.3461 741 HOH B O   
9736  O  O   . HOH GA .   ? 0.4320 0.4142 0.4557 -0.0368 -0.1042 -0.0612 742 HOH B O   
9737  O  O   . HOH GA .   ? 0.3215 0.4041 0.5443 0.0992  0.1216  0.2316  743 HOH B O   
9738  O  O   . HOH GA .   ? 0.3713 0.3267 0.2332 0.0214  -0.0559 0.0443  744 HOH B O   
9739  O  O   . HOH GA .   ? 0.5507 0.2379 0.2718 0.0031  0.0436  -0.0008 745 HOH B O   
9740  O  O   . HOH GA .   ? 0.5702 0.3547 0.9304 -0.1218 -0.0317 0.0065  746 HOH B O   
9741  O  O   . HOH GA .   ? 0.4142 0.1748 0.5401 0.1137  -0.0020 0.0529  747 HOH B O   
9742  O  O   . HOH GA .   ? 0.5133 0.4591 0.3314 -0.0242 -0.0331 0.0414  748 HOH B O   
9743  O  O   . HOH GA .   ? 0.5177 0.4235 0.4248 -0.0694 -0.0037 0.0335  749 HOH B O   
9744  O  O   . HOH GA .   ? 0.5281 0.4246 0.4787 -0.0498 0.0105  0.0041  750 HOH B O   
9745  O  O   . HOH GA .   ? 0.3032 0.3975 0.5518 0.0628  0.0509  0.2449  751 HOH B O   
9746  O  O   . HOH GA .   ? 0.5243 0.5315 0.6930 0.1898  -0.1622 -0.0952 752 HOH B O   
9747  O  O   . HOH GA .   ? 0.3578 0.2300 0.1784 0.0355  0.0856  -0.0096 753 HOH B O   
9748  O  O   . HOH GA .   ? 0.4756 0.5480 0.5034 0.0417  -0.0706 0.2477  754 HOH B O   
9749  O  O   . HOH GA .   ? 0.4154 0.3222 0.4368 -0.1155 0.0454  0.1036  755 HOH B O   
9750  O  O   . HOH GA .   ? 0.4203 0.4670 0.6844 0.1215  -0.0015 -0.2087 756 HOH B O   
9751  O  O   . HOH GA .   ? 0.9430 0.2845 0.2167 0.0540  -0.0568 0.0017  757 HOH B O   
9752  O  O   . HOH GA .   ? 0.3569 0.4169 0.2913 -0.1606 -0.0974 0.2185  758 HOH B O   
9753  O  O   . HOH GA .   ? 0.5029 0.1980 0.6877 -0.0465 0.0921  -0.0799 759 HOH B O   
9754  O  O   . HOH GA .   ? 0.3675 0.2018 0.5052 0.0057  -0.0423 -0.0386 760 HOH B O   
9755  O  O   . HOH GA .   ? 0.4110 0.4523 0.4997 0.1226  0.0458  0.2451  761 HOH B O   
9756  O  O   . HOH GA .   ? 0.4846 0.4745 0.4433 0.0601  0.0096  -0.0165 762 HOH B O   
9757  O  O   . HOH GA .   ? 0.4196 1.0334 0.5430 -0.2775 -0.1870 0.3136  763 HOH B O   
9758  O  O   . HOH GA .   ? 0.6089 0.9144 0.3305 0.2224  0.0907  -0.0631 764 HOH B O   
9759  O  O   . HOH GA .   ? 0.4852 0.4419 0.3855 -0.0487 -0.0068 0.0256  765 HOH B O   
9760  O  O   . HOH GA .   ? 0.6523 0.4469 0.4248 -0.1949 0.0088  -0.1572 766 HOH B O   
9761  O  O   . HOH GA .   ? 0.2685 0.2971 0.4151 0.0627  0.0895  -0.0190 767 HOH B O   
9762  O  O   . HOH GA .   ? 0.5886 0.5527 0.7721 0.3296  -0.1048 -0.1560 768 HOH B O   
9763  O  O   . HOH GA .   ? 0.4483 0.4694 0.4773 -0.0588 0.0750  0.0259  769 HOH B O   
9764  O  O   . HOH GA .   ? 0.4040 0.5651 0.5911 -0.0474 -0.1097 -0.1238 770 HOH B O   
9765  O  O   . HOH GA .   ? 0.5285 0.4941 0.5364 -0.0118 0.0362  -0.0712 771 HOH B O   
9766  O  O   . HOH GA .   ? 0.4207 0.3106 0.4712 -0.1562 -0.0401 0.1177  772 HOH B O   
9767  O  O   . HOH GA .   ? 0.7134 0.3898 0.3959 -0.1650 0.1743  -0.0403 773 HOH B O   
9768  O  O   . HOH GA .   ? 0.4352 0.6373 0.2820 0.2387  0.0746  0.1315  774 HOH B O   
9769  O  O   . HOH GA .   ? 1.0098 0.9977 0.4826 -0.1946 0.0223  -0.0877 775 HOH B O   
9770  O  O   . HOH GA .   ? 0.4695 0.3375 0.4808 -0.0615 0.1137  0.1979  776 HOH B O   
9771  O  O   . HOH GA .   ? 0.4242 0.4059 0.4849 -0.0291 0.0641  0.2069  777 HOH B O   
9772  O  O   . HOH GA .   ? 0.6773 0.5498 0.5390 -0.3016 0.1150  0.1826  778 HOH B O   
9773  O  O   . HOH GA .   ? 0.4559 0.4932 0.4225 -0.0533 0.1124  0.0310  779 HOH B O   
9774  O  O   . HOH GA .   ? 0.2761 0.1825 0.1904 0.0012  0.0211  0.0522  780 HOH B O   
9775  O  O   . HOH GA .   ? 1.0364 0.4415 0.5787 -0.0461 0.0427  -0.1981 781 HOH B O   
9776  O  O   . HOH HA .   ? 0.2420 0.4059 0.4120 -0.0098 0.0843  0.0648  401 HOH C O   
9777  O  O   . HOH HA .   ? 0.3815 0.4695 0.3556 0.0966  -0.0031 -0.0364 402 HOH C O   
9778  O  O   . HOH HA .   ? 0.2795 0.3781 0.2183 -0.0065 0.0810  -0.0017 403 HOH C O   
9779  O  O   . HOH HA .   ? 0.5437 0.3416 0.4359 -0.0335 0.0000  -0.0505 404 HOH C O   
9780  O  O   . HOH HA .   ? 0.3919 0.3824 0.3610 0.0125  -0.0636 -0.0803 405 HOH C O   
9781  O  O   . HOH HA .   ? 0.6597 0.2411 0.2395 0.0904  0.0137  -0.0328 406 HOH C O   
9782  O  O   . HOH HA .   ? 0.2202 0.6317 0.4228 -0.1351 -0.0074 -0.0676 407 HOH C O   
9783  O  O   . HOH HA .   ? 0.3370 0.6205 0.1671 0.1009  0.0120  0.0104  408 HOH C O   
9784  O  O   . HOH HA .   ? 0.3470 0.4742 0.6258 -0.0192 0.1049  0.3282  409 HOH C O   
9785  O  O   . HOH HA .   ? 0.4903 0.4838 0.4885 -0.0447 -0.0066 0.0359  410 HOH C O   
9786  O  O   . HOH HA .   ? 0.2712 0.2984 0.3086 -0.0178 -0.0280 -0.0480 411 HOH C O   
9787  O  O   . HOH HA .   ? 0.4077 0.5756 0.4332 0.2231  0.0333  0.1774  412 HOH C O   
9788  O  O   . HOH HA .   ? 0.2757 0.1333 0.1994 -0.0551 0.0183  -0.0498 413 HOH C O   
9789  O  O   . HOH HA .   ? 0.5504 0.4600 0.2027 0.0133  -0.0694 -0.0500 414 HOH C O   
9790  O  O   . HOH HA .   ? 0.4620 0.6730 0.2955 -0.2339 0.0812  -0.1184 415 HOH C O   
9791  O  O   . HOH HA .   ? 0.5224 0.2748 0.5497 -0.0593 -0.3179 0.0032  416 HOH C O   
9792  O  O   . HOH HA .   ? 0.4029 0.8450 0.5376 0.0284  -0.1328 -0.0887 417 HOH C O   
9793  O  O   . HOH HA .   ? 0.3495 0.5594 0.5098 0.1900  -0.0658 -0.2739 418 HOH C O   
9794  O  O   . HOH HA .   ? 0.8820 0.5058 0.3668 -0.2054 0.0026  0.1462  419 HOH C O   
9795  O  O   . HOH HA .   ? 0.4138 0.3935 0.3819 -0.0599 -0.0140 -0.0303 420 HOH C O   
9796  O  O   . HOH HA .   ? 0.5769 0.7821 0.1221 0.0122  0.0315  0.0159  421 HOH C O   
9797  O  O   . HOH HA .   ? 0.4591 0.3233 0.4402 0.0798  -0.0309 0.0386  422 HOH C O   
9798  O  O   . HOH HA .   ? 0.5052 0.4253 0.3400 -0.0812 0.1251  0.0038  423 HOH C O   
9799  O  O   . HOH HA .   ? 0.2228 0.2612 0.0879 -0.0538 0.0226  -0.0304 424 HOH C O   
9800  O  O   . HOH HA .   ? 0.4461 0.2838 0.4480 0.0463  0.2377  0.0828  425 HOH C O   
9801  O  O   . HOH HA .   ? 0.4769 0.6140 0.2430 0.1045  0.0115  0.0634  426 HOH C O   
9802  O  O   . HOH HA .   ? 0.5135 0.3449 0.2451 -0.1341 -0.0109 0.0260  427 HOH C O   
9803  O  O   . HOH HA .   ? 0.5543 0.4796 0.4219 0.0206  0.1220  0.0231  428 HOH C O   
9804  O  O   . HOH HA .   ? 0.2766 0.3061 0.2745 -0.1463 -0.0144 0.0344  429 HOH C O   
9805  O  O   . HOH HA .   ? 0.4450 0.6254 0.5666 -0.1536 0.0441  -0.1972 430 HOH C O   
9806  O  O   . HOH HA .   ? 0.3348 0.3213 0.2418 0.0017  -0.0753 -0.0340 431 HOH C O   
9807  O  O   . HOH HA .   ? 0.4117 0.4401 0.1729 -0.1033 -0.0114 0.1199  432 HOH C O   
9808  O  O   . HOH HA .   ? 0.7415 0.5214 0.4291 -0.2578 -0.1918 -0.0256 433 HOH C O   
9809  O  O   . HOH HA .   ? 0.4557 0.7896 0.4694 0.1984  -0.2072 -0.1703 434 HOH C O   
9810  O  O   . HOH HA .   ? 0.2718 0.2980 0.2111 -0.0854 0.1134  -0.0816 435 HOH C O   
9811  O  O   . HOH HA .   ? 0.6905 0.5924 0.2662 -0.0860 0.0260  0.1086  436 HOH C O   
9812  O  O   . HOH HA .   ? 0.2594 0.2910 0.1106 -0.0388 0.0269  0.0392  437 HOH C O   
9813  O  O   . HOH HA .   ? 0.3269 0.3740 0.1985 -0.0138 0.0815  0.0527  438 HOH C O   
9814  O  O   . HOH HA .   ? 0.2800 0.8090 0.2443 0.1553  0.0256  0.0723  439 HOH C O   
9815  O  O   . HOH HA .   ? 0.5051 0.4205 0.4763 -0.0636 -0.1235 0.0143  440 HOH C O   
9816  O  O   . HOH HA .   ? 0.1631 0.3018 0.3722 -0.0258 -0.0020 -0.1464 441 HOH C O   
9817  O  O   . HOH HA .   ? 0.3145 0.4226 0.2267 -0.0381 0.0187  0.0967  442 HOH C O   
9818  O  O   . HOH HA .   ? 0.3635 0.5081 0.2994 0.0083  0.0174  0.1988  443 HOH C O   
9819  O  O   . HOH HA .   ? 0.2339 0.2890 0.2375 -0.0432 -0.0544 -0.0211 444 HOH C O   
9820  O  O   . HOH HA .   ? 0.7329 0.3174 0.3862 0.1085  0.2240  0.0285  445 HOH C O   
9821  O  O   . HOH HA .   ? 0.3068 0.3817 0.3276 0.0041  0.1022  0.0430  446 HOH C O   
9822  O  O   . HOH HA .   ? 0.1649 0.2224 0.2221 0.0153  0.0335  -0.0803 447 HOH C O   
9823  O  O   . HOH HA .   ? 0.3680 0.2117 0.2585 -0.0331 -0.0681 0.0126  448 HOH C O   
9824  O  O   . HOH HA .   ? 0.1683 0.1427 0.2204 0.0074  0.0450  -0.0406 449 HOH C O   
9825  O  O   . HOH HA .   ? 0.2301 0.3203 0.2411 0.0203  0.0340  0.1090  450 HOH C O   
9826  O  O   . HOH HA .   ? 0.2109 0.1858 0.2120 -0.0313 0.0350  -0.0337 451 HOH C O   
9827  O  O   . HOH HA .   ? 0.2768 0.2072 0.1005 -0.0553 0.0172  -0.0335 452 HOH C O   
9828  O  O   . HOH HA .   ? 0.1533 0.3549 0.2354 0.0034  0.0076  -0.0216 453 HOH C O   
9829  O  O   . HOH HA .   ? 0.3670 0.6039 0.2984 0.0013  0.0489  -0.1557 454 HOH C O   
9830  O  O   . HOH HA .   ? 0.4947 0.4719 0.1800 -0.0245 -0.0731 -0.0513 455 HOH C O   
9831  O  O   . HOH HA .   ? 0.2035 0.1425 0.1777 -0.0142 0.0392  0.0057  456 HOH C O   
9832  O  O   . HOH HA .   ? 0.3824 0.8090 0.2545 0.0961  0.1040  0.1152  457 HOH C O   
9833  O  O   . HOH HA .   ? 0.2966 0.3118 0.4510 -0.0292 0.0207  -0.0395 458 HOH C O   
9834  O  O   . HOH HA .   ? 0.4864 0.7434 0.2962 0.0232  -0.0062 0.2189  459 HOH C O   
9835  O  O   . HOH HA .   ? 0.5795 0.4056 0.3549 0.1114  0.2570  0.1081  460 HOH C O   
9836  O  O   . HOH HA .   ? 0.3486 0.2454 0.3362 -0.0342 -0.0715 0.0340  461 HOH C O   
9837  O  O   . HOH HA .   ? 0.6122 0.3680 0.2378 0.1948  0.0049  -0.0900 462 HOH C O   
9838  O  O   . HOH HA .   ? 0.3986 0.1906 0.1457 -0.0322 -0.0063 -0.0493 463 HOH C O   
9839  O  O   . HOH HA .   ? 0.1385 0.0936 0.1337 0.0024  0.0137  -0.0131 464 HOH C O   
9840  O  O   . HOH HA .   ? 0.3477 0.2940 0.3115 -0.0049 -0.0833 -0.0174 465 HOH C O   
9841  O  O   . HOH HA .   ? 0.3425 0.4411 0.1894 0.0237  0.0344  0.0868  466 HOH C O   
9842  O  O   . HOH HA .   ? 0.1518 0.1466 0.1181 0.0012  0.0252  0.0027  467 HOH C O   
9843  O  O   . HOH HA .   ? 0.5235 0.4630 0.2043 0.0162  0.0262  -0.0049 468 HOH C O   
9844  O  O   . HOH HA .   ? 0.2059 0.5891 0.3005 -0.0901 0.0372  0.0505  469 HOH C O   
9845  O  O   . HOH HA .   ? 0.3434 0.3280 0.1914 -0.0120 -0.0262 -0.0258 470 HOH C O   
9846  O  O   . HOH HA .   ? 0.7764 0.2786 0.4396 -0.1766 -0.0111 -0.0049 471 HOH C O   
9847  O  O   . HOH HA .   ? 0.1590 0.2576 0.0987 -0.0538 -0.0076 0.0248  472 HOH C O   
9848  O  O   . HOH HA .   ? 0.1560 0.1086 0.1676 0.0060  -0.0147 0.0070  473 HOH C O   
9849  O  O   . HOH HA .   ? 0.4287 0.1877 0.3682 -0.0838 0.1067  -0.0297 474 HOH C O   
9850  O  O   . HOH HA .   ? 0.3054 0.3170 0.2445 -0.0628 0.0504  -0.0863 475 HOH C O   
9851  O  O   . HOH HA .   ? 0.1571 0.1230 0.1875 -0.0394 0.0205  -0.0250 476 HOH C O   
9852  O  O   . HOH HA .   ? 0.4365 0.3519 0.3370 0.0619  0.1532  0.0038  477 HOH C O   
9853  O  O   . HOH HA .   ? 0.3885 0.5270 0.4063 -0.0035 0.0820  0.2178  478 HOH C O   
9854  O  O   . HOH HA .   ? 0.1782 0.2325 0.2461 -0.0006 0.0841  -0.0249 479 HOH C O   
9855  O  O   . HOH HA .   ? 0.3274 0.2750 0.6775 -0.0652 0.0199  -0.0546 480 HOH C O   
9856  O  O   . HOH HA .   ? 0.4347 0.5606 0.4457 -0.1094 0.1035  0.1722  481 HOH C O   
9857  O  O   . HOH HA .   ? 0.3314 0.4029 0.5465 -0.1063 0.0296  0.0952  482 HOH C O   
9858  O  O   . HOH HA .   ? 0.1274 0.1726 0.1400 -0.0015 0.0201  0.0098  483 HOH C O   
9859  O  O   . HOH HA .   ? 0.3003 0.3634 0.2073 0.0295  0.0842  0.0878  484 HOH C O   
9860  O  O   . HOH HA .   ? 0.2574 0.1911 0.1696 0.0055  -0.0237 0.0443  485 HOH C O   
9861  O  O   . HOH HA .   ? 0.2820 0.2251 0.1865 -0.0147 0.0399  0.0478  486 HOH C O   
9862  O  O   . HOH HA .   ? 0.4386 0.2319 0.8871 0.0127  -0.0807 -0.0303 487 HOH C O   
9863  O  O   . HOH HA .   ? 0.2646 0.4632 0.2290 0.0121  0.0266  0.0379  488 HOH C O   
9864  O  O   . HOH HA .   ? 0.3890 0.3393 0.3846 0.1463  0.1204  0.1993  489 HOH C O   
9865  O  O   . HOH HA .   ? 0.2382 0.3431 0.8507 -0.0001 0.0939  -0.1022 490 HOH C O   
9866  O  O   . HOH HA .   ? 0.4027 0.4300 0.2693 -0.1430 -0.0154 -0.0340 491 HOH C O   
9867  O  O   . HOH HA .   ? 0.4187 0.3574 0.4345 0.0597  0.0702  0.0654  492 HOH C O   
9868  O  O   . HOH HA .   ? 0.2448 0.2048 0.2148 0.0197  0.0370  0.0005  493 HOH C O   
9869  O  O   . HOH HA .   ? 0.2978 0.2549 0.2623 -0.0485 -0.0104 0.0176  494 HOH C O   
9870  O  O   . HOH HA .   ? 0.5800 0.3292 0.9658 0.1046  -0.1631 0.0760  495 HOH C O   
9871  O  O   . HOH HA .   ? 0.2549 0.1642 0.1745 -0.0120 0.0489  0.0142  496 HOH C O   
9872  O  O   . HOH HA .   ? 0.3118 0.2220 0.1466 -0.0772 0.0116  0.0092  497 HOH C O   
9873  O  O   . HOH HA .   ? 0.1551 0.1297 0.0857 -0.0098 0.0250  -0.0024 498 HOH C O   
9874  O  O   . HOH HA .   ? 0.2248 0.4816 0.4268 0.0318  -0.0896 0.0794  499 HOH C O   
9875  O  O   . HOH HA .   ? 0.2242 0.2117 0.1736 0.0088  0.0231  -0.0348 500 HOH C O   
9876  O  O   . HOH HA .   ? 0.1904 0.2285 0.1357 0.0229  0.0373  0.0531  501 HOH C O   
9877  O  O   . HOH HA .   ? 0.5273 0.6270 0.4471 -0.0630 -0.0760 0.3000  502 HOH C O   
9878  O  O   . HOH HA .   ? 0.2452 0.2224 0.3853 -0.0215 -0.0881 0.0465  503 HOH C O   
9879  O  O   . HOH HA .   ? 0.2274 0.5295 0.4562 -0.0296 0.0126  0.0992  504 HOH C O   
9880  O  O   . HOH HA .   ? 0.4334 0.3258 0.2572 -0.0878 0.0621  -0.0243 505 HOH C O   
9881  O  O   . HOH HA .   ? 0.1685 0.1732 0.2732 0.0227  -0.0078 -0.0355 506 HOH C O   
9882  O  O   . HOH HA .   ? 0.2996 0.5119 0.2757 0.0666  0.0324  0.1225  507 HOH C O   
9883  O  O   . HOH HA .   ? 0.4370 0.2741 0.2434 0.0478  0.0670  0.0406  508 HOH C O   
9884  O  O   . HOH HA .   ? 0.6094 0.4961 0.3404 -0.1274 -0.1297 -0.0082 509 HOH C O   
9885  O  O   . HOH HA .   ? 0.7864 0.3702 0.3876 0.1263  -0.0785 0.1220  510 HOH C O   
9886  O  O   . HOH HA .   ? 0.3149 0.4250 0.3756 -0.0129 0.0219  -0.1092 511 HOH C O   
9887  O  O   . HOH HA .   ? 0.2048 0.3926 0.3513 -0.0771 0.0059  0.0388  512 HOH C O   
9888  O  O   . HOH HA .   ? 0.1709 0.0878 0.1457 -0.0003 0.0207  -0.0066 513 HOH C O   
9889  O  O   . HOH HA .   ? 0.5109 0.3222 0.3206 -0.0518 0.0962  -0.0907 514 HOH C O   
9890  O  O   . HOH HA .   ? 0.4420 0.2436 0.5924 -0.1358 0.1789  -0.0661 515 HOH C O   
9891  O  O   . HOH HA .   ? 0.5659 0.7154 0.5529 -0.1497 0.1036  -0.2836 516 HOH C O   
9892  O  O   . HOH HA .   ? 0.3564 0.2788 0.3016 -0.0592 -0.0680 -0.0277 517 HOH C O   
9893  O  O   . HOH HA .   ? 0.3248 0.1617 0.2910 0.0729  0.1037  0.1121  518 HOH C O   
9894  O  O   . HOH HA .   ? 0.1678 0.1271 0.1770 -0.0008 -0.0287 -0.0024 519 HOH C O   
9895  O  O   . HOH HA .   ? 0.2081 0.2332 0.2291 0.0781  0.0667  0.0353  520 HOH C O   
9896  O  O   . HOH HA .   ? 0.1262 0.0852 0.1098 -0.0054 0.0240  -0.0035 521 HOH C O   
9897  O  O   . HOH HA .   ? 0.3312 0.5351 0.1045 -0.0917 -0.0439 -0.0044 522 HOH C O   
9898  O  O   . HOH HA .   ? 0.3526 2.3190 0.4691 -0.3073 -0.1865 0.6391  523 HOH C O   
9899  O  O   . HOH HA .   ? 0.6322 0.5042 0.4580 0.0027  -0.0183 -0.0120 524 HOH C O   
9900  O  O   . HOH HA .   ? 0.3416 0.4081 0.2269 -0.1121 0.0306  0.0068  525 HOH C O   
9901  O  O   . HOH HA .   ? 0.1592 0.1091 0.1197 -0.0066 0.0166  -0.0024 526 HOH C O   
9902  O  O   . HOH HA .   ? 0.2208 0.2860 0.1746 0.0768  0.0582  0.0564  527 HOH C O   
9903  O  O   . HOH HA .   ? 0.3131 0.3810 0.3853 -0.0887 -0.0192 -0.0522 528 HOH C O   
9904  O  O   . HOH HA .   ? 0.1590 0.0897 0.1741 -0.0111 0.0119  -0.0267 529 HOH C O   
9905  O  O   . HOH HA .   ? 0.3077 0.3916 0.3973 -0.0055 0.0344  0.0958  530 HOH C O   
9906  O  O   . HOH HA .   ? 0.7300 0.4776 0.3837 0.0606  -0.1076 -0.2226 531 HOH C O   
9907  O  O   . HOH HA .   ? 0.2529 0.3707 0.3240 -0.0942 0.0601  -0.0844 532 HOH C O   
9908  O  O   . HOH HA .   ? 0.3402 0.6276 0.5643 0.2453  -0.0615 0.0104  533 HOH C O   
9909  O  O   . HOH HA .   ? 0.6161 0.3916 0.5199 -0.1351 0.3025  -0.0329 534 HOH C O   
9910  O  O   . HOH HA .   ? 0.2694 0.5932 0.3996 -0.0471 0.0838  0.1333  535 HOH C O   
9911  O  O   . HOH HA .   ? 0.2691 0.4853 0.2457 -0.0463 -0.0017 0.1067  536 HOH C O   
9912  O  O   . HOH HA .   ? 0.2845 0.3380 0.2714 0.0186  0.0337  0.1261  537 HOH C O   
9913  O  O   . HOH HA .   ? 0.3136 0.5038 0.2017 -0.0917 -0.0189 0.1298  538 HOH C O   
9914  O  O   . HOH HA .   ? 0.7243 0.3957 0.1958 0.0780  0.0675  -0.0192 539 HOH C O   
9915  O  O   . HOH HA .   ? 0.3325 0.3790 0.3461 0.0601  -0.0430 -0.1435 540 HOH C O   
9916  O  O   . HOH HA .   ? 0.3014 0.5562 0.2971 0.0225  0.0674  0.1581  541 HOH C O   
9917  O  O   . HOH HA .   ? 0.1642 0.1281 0.1261 0.0097  0.0300  -0.0013 542 HOH C O   
9918  O  O   . HOH HA .   ? 0.2231 0.1700 0.1312 -0.0256 -0.0304 -0.0010 543 HOH C O   
9919  O  O   . HOH HA .   ? 0.2569 0.3986 0.1710 0.0041  0.0702  0.0644  544 HOH C O   
9920  O  O   . HOH HA .   ? 0.3061 0.2486 0.0881 -0.0715 -0.0249 -0.0103 545 HOH C O   
9921  O  O   . HOH HA .   ? 0.6643 0.3201 0.2529 0.0571  0.1369  0.0073  546 HOH C O   
9922  O  O   . HOH HA .   ? 0.4221 0.3786 0.4616 0.1859  -0.0454 0.0877  547 HOH C O   
9923  O  O   . HOH HA .   ? 0.3158 0.2475 0.2190 -0.0728 -0.0293 0.0406  548 HOH C O   
9924  O  O   . HOH HA .   ? 0.1831 0.5264 0.1462 -0.0377 0.0262  0.0203  549 HOH C O   
9925  O  O   . HOH HA .   ? 0.3824 0.1887 0.1405 -0.0461 0.0854  0.0167  550 HOH C O   
9926  O  O   . HOH HA .   ? 0.1694 0.0942 0.1299 -0.0166 0.0230  0.0023  551 HOH C O   
9927  O  O   . HOH HA .   ? 0.3366 1.0214 0.3303 -0.2728 0.0615  -0.0819 552 HOH C O   
9928  O  O   . HOH HA .   ? 0.3012 0.4458 0.2569 0.0035  0.1386  0.0024  553 HOH C O   
9929  O  O   . HOH HA .   ? 0.2499 0.1942 0.1163 -0.0089 0.0419  -0.0035 554 HOH C O   
9930  O  O   . HOH HA .   ? 0.5494 0.3547 0.3944 0.0107  0.1128  -0.1360 555 HOH C O   
9931  O  O   . HOH HA .   ? 0.5576 0.2658 0.5619 0.0996  0.0154  -0.0930 556 HOH C O   
9932  O  O   . HOH HA .   ? 0.3824 0.3416 0.4282 -0.0148 0.0226  0.2132  557 HOH C O   
9933  O  O   . HOH HA .   ? 0.2134 0.2852 0.1865 -0.0445 0.0102  0.0502  558 HOH C O   
9934  O  O   . HOH HA .   ? 0.4374 0.4435 0.4551 -0.0480 0.0381  -0.0667 559 HOH C O   
9935  O  O   . HOH HA .   ? 0.3147 0.4140 0.4108 -0.1228 0.0652  -0.0666 560 HOH C O   
9936  O  O   . HOH HA .   ? 0.7153 0.5371 0.6191 0.4447  0.0160  -0.0461 561 HOH C O   
9937  O  O   . HOH HA .   ? 0.2678 0.1513 0.3332 0.0181  -0.0253 -0.0863 562 HOH C O   
9938  O  O   . HOH HA .   ? 0.4047 0.6340 0.3499 -0.0311 0.0164  0.2402  563 HOH C O   
9939  O  O   . HOH HA .   ? 0.2380 0.1452 0.2220 0.0003  -0.0645 0.0006  564 HOH C O   
9940  O  O   . HOH HA .   ? 0.3485 0.5550 0.6805 -0.1900 -0.0057 0.0195  565 HOH C O   
9941  O  O   . HOH HA .   ? 0.3077 0.4004 0.1931 -0.0256 0.0148  0.0538  566 HOH C O   
9942  O  O   . HOH HA .   ? 0.2148 0.1475 0.3300 -0.0313 0.0142  -0.0595 567 HOH C O   
9943  O  O   . HOH HA .   ? 0.2759 0.2470 0.4647 0.0242  0.0992  0.0346  568 HOH C O   
9944  O  O   . HOH HA .   ? 0.2951 0.2242 0.2601 -0.0793 0.0697  0.0120  569 HOH C O   
9945  O  O   . HOH HA .   ? 0.2718 0.3641 0.2143 -0.0054 0.0406  0.1248  570 HOH C O   
9946  O  O   . HOH HA .   ? 0.2515 0.3300 0.2793 -0.0082 -0.0375 -0.0085 571 HOH C O   
9947  O  O   . HOH HA .   ? 0.3461 0.5540 0.3237 0.1318  0.0164  0.2606  572 HOH C O   
9948  O  O   . HOH HA .   ? 0.4541 0.8891 0.1971 0.0593  0.0631  0.0432  573 HOH C O   
9949  O  O   . HOH HA .   ? 0.3591 0.6067 0.2316 -0.1456 -0.0668 -0.0275 574 HOH C O   
9950  O  O   . HOH HA .   ? 0.6924 0.3355 0.6080 -0.0230 -0.3630 0.0803  575 HOH C O   
9951  O  O   . HOH HA .   ? 0.3828 0.3048 0.2718 0.0274  0.0494  0.0742  576 HOH C O   
9952  O  O   . HOH HA .   ? 0.1543 0.1468 0.1527 0.0086  0.0137  -0.0494 577 HOH C O   
9953  O  O   . HOH HA .   ? 0.2867 0.8503 0.4327 -0.1631 -0.0384 0.0687  578 HOH C O   
9954  O  O   . HOH HA .   ? 0.2461 0.1809 0.1341 -0.0405 0.0269  -0.0115 579 HOH C O   
9955  O  O   . HOH HA .   ? 0.2111 0.2237 0.2829 0.0759  0.0562  0.1136  580 HOH C O   
9956  O  O   . HOH HA .   ? 0.3100 0.4156 0.4020 0.1832  0.1111  0.1093  581 HOH C O   
9957  O  O   . HOH HA .   ? 0.1847 0.1944 0.2163 -0.0392 0.0035  -0.0329 582 HOH C O   
9958  O  O   . HOH HA .   ? 0.5260 0.2937 0.2885 0.0375  0.0165  -0.0560 583 HOH C O   
9959  O  O   . HOH HA .   ? 0.2583 0.4429 0.3012 -0.0425 0.0653  -0.0896 584 HOH C O   
9960  O  O   . HOH HA .   ? 0.3398 0.4449 0.1929 0.0048  0.0489  0.0020  585 HOH C O   
9961  O  O   . HOH HA .   ? 0.5623 0.4075 0.8759 -0.2334 -0.0795 -0.0916 586 HOH C O   
9962  O  O   . HOH HA .   ? 0.6521 0.2985 0.4476 0.1226  -0.1562 0.0813  587 HOH C O   
9963  O  O   . HOH HA .   ? 0.4068 0.3707 0.2163 0.0010  0.0785  -0.0269 588 HOH C O   
9964  O  O   . HOH HA .   ? 0.5018 0.3892 0.3555 0.0965  -0.1274 -0.0098 589 HOH C O   
9965  O  O   . HOH HA .   ? 0.3265 0.6338 0.5820 0.1689  -0.0272 0.2109  590 HOH C O   
9966  O  O   . HOH HA .   ? 0.5504 0.2998 0.2892 -0.0652 -0.0873 0.0544  591 HOH C O   
9967  O  O   . HOH HA .   ? 0.1892 0.1165 0.1710 -0.0259 -0.0271 0.0317  592 HOH C O   
9968  O  O   . HOH HA .   ? 0.5831 0.4277 0.5141 -0.1430 0.1351  -0.1397 593 HOH C O   
9969  O  O   . HOH HA .   ? 0.3418 0.5788 0.3962 0.1632  -0.0082 0.1392  594 HOH C O   
9970  O  O   . HOH HA .   ? 0.5798 0.3519 0.2578 -0.0688 -0.0688 -0.0763 595 HOH C O   
9971  O  O   . HOH HA .   ? 0.3131 0.2336 0.2301 -0.0353 0.0187  0.0306  596 HOH C O   
9972  O  O   . HOH HA .   ? 0.3490 0.6197 0.3718 -0.0518 -0.1176 0.0688  597 HOH C O   
9973  O  O   . HOH HA .   ? 0.4320 0.4662 0.4790 -0.0681 -0.0551 -0.2327 598 HOH C O   
9974  O  O   . HOH HA .   ? 0.2691 0.2285 0.1940 -0.0083 0.0293  0.1061  599 HOH C O   
9975  O  O   . HOH HA .   ? 0.2644 0.5468 0.5751 0.0917  -0.0494 0.1500  600 HOH C O   
9976  O  O   . HOH HA .   ? 0.3003 0.4255 0.1953 -0.0447 0.0463  -0.0489 601 HOH C O   
9977  O  O   . HOH HA .   ? 0.4508 0.4668 0.4762 0.0489  -0.0688 -0.0546 602 HOH C O   
9978  O  O   . HOH HA .   ? 0.3547 0.2676 0.4627 -0.0063 -0.1035 0.0604  603 HOH C O   
9979  O  O   . HOH HA .   ? 0.7845 0.8411 0.4431 0.1403  -0.0230 -0.1404 604 HOH C O   
9980  O  O   . HOH HA .   ? 0.6100 0.5760 0.7293 -0.1701 -0.1703 -0.1387 605 HOH C O   
9981  O  O   . HOH HA .   ? 0.6959 0.7402 0.4543 0.4007  0.2412  0.2410  606 HOH C O   
9982  O  O   . HOH HA .   ? 0.3930 0.7458 0.4372 0.2869  0.0800  0.3458  607 HOH C O   
9983  O  O   . HOH HA .   ? 0.4433 0.4612 0.4483 0.0097  0.1208  -0.1838 608 HOH C O   
9984  O  O   . HOH HA .   ? 0.6018 0.2976 0.3693 -0.0966 -0.1492 0.0648  609 HOH C O   
9985  O  O   . HOH HA .   ? 0.3415 0.2169 0.4496 -0.0239 -0.0899 -0.0504 610 HOH C O   
9986  O  O   . HOH HA .   ? 0.2777 0.2463 0.2454 -0.0063 -0.0118 0.0649  611 HOH C O   
9987  O  O   . HOH HA .   ? 0.2354 0.3118 0.2467 0.0182  0.0163  0.0114  612 HOH C O   
9988  O  O   . HOH HA .   ? 0.7225 0.6549 0.2878 0.2511  0.1253  0.0935  613 HOH C O   
9989  O  O   . HOH HA .   ? 0.5705 0.5199 0.2673 -0.2476 0.0204  -0.0125 614 HOH C O   
9990  O  O   . HOH HA .   ? 0.4383 0.4501 0.4269 -0.0542 -0.1379 0.0241  615 HOH C O   
9991  O  O   . HOH HA .   ? 0.3829 0.3436 0.4056 -0.0579 0.0038  0.0201  616 HOH C O   
9992  O  O   . HOH HA .   ? 0.3944 0.4461 0.3030 -0.0663 0.0108  -0.1597 617 HOH C O   
9993  O  O   . HOH HA .   ? 0.4153 0.3567 0.4778 -0.0137 0.0471  0.0405  618 HOH C O   
9994  O  O   . HOH HA .   ? 0.7768 0.6455 0.5479 0.0170  -0.1788 0.2535  619 HOH C O   
9995  O  O   . HOH HA .   ? 0.5440 0.4375 0.3695 -0.0003 -0.1808 0.0636  620 HOH C O   
9996  O  O   . HOH HA .   ? 0.6395 0.8058 0.3339 0.0683  0.0582  -0.2157 621 HOH C O   
9997  O  O   . HOH HA .   ? 0.3713 0.5231 0.3488 -0.0241 0.0310  -0.1010 622 HOH C O   
9998  O  O   . HOH HA .   ? 0.4885 0.4805 0.3781 0.0308  0.0148  0.0133  623 HOH C O   
9999  O  O   . HOH HA .   ? 0.8931 0.2878 0.9226 -0.1272 -0.1378 -0.0535 624 HOH C O   
10000 O  O   . HOH HA .   ? 0.3648 0.3971 0.6664 -0.0601 0.2381  0.0096  625 HOH C O   
10001 O  O   . HOH HA .   ? 0.4011 0.5137 0.4972 0.1448  -0.0527 -0.1585 626 HOH C O   
10002 O  O   . HOH HA .   ? 0.5123 0.4810 0.5512 -0.0746 0.0416  0.1017  627 HOH C O   
10003 O  O   . HOH HA .   ? 0.9628 0.4397 0.4352 0.0632  -0.2230 -0.0307 628 HOH C O   
10004 O  O   . HOH HA .   ? 0.2269 0.3962 0.5982 0.1105  -0.1413 -0.2240 629 HOH C O   
10005 O  O   . HOH HA .   ? 0.4582 0.4521 0.4225 -0.0062 0.0035  -0.0153 630 HOH C O   
10006 O  O   . HOH HA .   ? 0.4135 0.8012 0.8276 0.1694  0.0315  0.0173  631 HOH C O   
10007 O  O   . HOH HA .   ? 0.6116 0.3009 0.2364 -0.1257 0.0230  -0.0261 632 HOH C O   
10008 O  O   . HOH HA .   ? 0.4196 0.4239 0.4298 0.0357  -0.0236 -0.0344 633 HOH C O   
10009 O  O   . HOH HA .   ? 0.3143 1.2218 0.6169 -0.1878 -0.1093 0.2316  634 HOH C O   
10010 O  O   . HOH HA .   ? 0.4529 0.3716 0.5663 -0.0697 0.0504  0.0236  635 HOH C O   
10011 O  O   . HOH HA .   ? 0.2526 0.3359 0.4645 0.0860  0.0813  0.0232  636 HOH C O   
10012 O  O   . HOH HA .   ? 0.3181 0.3910 0.7160 -0.0513 -0.1044 0.0359  637 HOH C O   
10013 O  O   . HOH HA .   ? 0.8934 0.3357 0.2639 -0.0694 -0.0326 -0.0776 638 HOH C O   
10014 O  O   . HOH HA .   ? 0.3450 0.2549 0.2170 0.0207  0.0957  0.0386  639 HOH C O   
10015 O  O   . HOH HA .   ? 0.4262 0.3048 0.5389 -0.0185 0.0811  0.1335  640 HOH C O   
10016 O  O   . HOH HA .   ? 0.3050 0.5191 0.5942 0.0259  0.0760  0.0631  641 HOH C O   
10017 O  O   . HOH HA .   ? 0.4573 0.2861 0.3186 0.0654  -0.1027 0.0078  642 HOH C O   
10018 O  O   . HOH HA .   ? 0.3650 0.3727 0.2542 -0.0357 0.0780  -0.0303 643 HOH C O   
10019 O  O   . HOH HA .   ? 0.4970 3.2193 0.4454 -0.0027 -0.1150 0.0425  644 HOH C O   
10020 O  O   . HOH HA .   ? 0.3697 0.7044 0.2838 -0.1124 -0.0944 -0.0097 645 HOH C O   
10021 O  O   . HOH HA .   ? 0.3416 0.2957 0.2666 0.0074  0.0395  0.0496  646 HOH C O   
10022 O  O   . HOH HA .   ? 0.4686 0.9194 0.3400 0.2081  0.0421  0.3143  647 HOH C O   
10023 O  O   . HOH HA .   ? 0.3944 0.7749 0.8981 -0.1687 -0.3041 0.2500  648 HOH C O   
10024 O  O   . HOH HA .   ? 0.3447 0.3436 0.4268 -0.1010 0.0746  0.1297  649 HOH C O   
10025 O  O   . HOH HA .   ? 0.2526 0.5843 0.2509 -0.0368 0.0266  0.0105  650 HOH C O   
10026 O  O   . HOH HA .   ? 0.3192 0.4970 0.4257 0.1708  0.0690  0.0665  651 HOH C O   
10027 O  O   . HOH HA .   ? 0.4785 0.6880 0.4863 0.0500  -0.0763 -0.2058 652 HOH C O   
10028 O  O   . HOH HA .   ? 0.6270 0.4490 0.4735 0.0176  -0.0719 -0.3111 653 HOH C O   
10029 O  O   . HOH HA .   ? 0.3727 0.5417 0.4550 0.0527  -0.0359 0.0619  654 HOH C O   
10030 O  O   . HOH HA .   ? 0.7674 0.6837 0.2440 -0.4239 -0.0971 0.2246  655 HOH C O   
10031 O  O   . HOH HA .   ? 0.4278 0.4939 0.3359 0.0026  0.0264  0.0828  656 HOH C O   
10032 O  O   . HOH HA .   ? 0.2967 0.2082 0.3600 0.0353  -0.0540 -0.0308 657 HOH C O   
10033 O  O   . HOH HA .   ? 0.5680 0.5629 0.4918 -0.0144 0.2673  -0.0671 658 HOH C O   
10034 O  O   . HOH HA .   ? 0.3734 0.2755 0.3864 -0.1155 0.1986  -0.0992 659 HOH C O   
10035 O  O   . HOH HA .   ? 0.3544 0.3278 0.5759 -0.0535 0.1460  0.0577  660 HOH C O   
10036 O  O   . HOH HA .   ? 0.2141 0.3115 0.2813 0.0571  0.0346  -0.0231 661 HOH C O   
10037 O  O   . HOH HA .   ? 0.2734 0.2170 0.1832 -0.0344 0.0037  -0.0200 662 HOH C O   
10038 O  O   . HOH HA .   ? 0.6963 0.8982 0.2536 0.5074  -0.0856 -0.1080 663 HOH C O   
10039 O  O   . HOH HA .   ? 0.5202 0.4034 0.2739 0.1142  0.1008  0.0372  664 HOH C O   
10040 O  O   . HOH HA .   ? 0.2937 0.2488 0.5285 -0.0074 0.0588  0.0230  665 HOH C O   
10041 O  O   . HOH HA .   ? 0.6527 0.5877 0.2269 -0.4853 0.0593  -0.0267 666 HOH C O   
10042 O  O   . HOH HA .   ? 0.3797 0.3454 0.6154 0.0868  0.0450  -0.0071 667 HOH C O   
10043 O  O   . HOH HA .   ? 0.4309 0.4047 0.4582 0.0606  0.0485  0.0939  668 HOH C O   
10044 O  O   . HOH HA .   ? 0.5745 0.6725 0.4370 -0.0722 0.1703  -0.1908 669 HOH C O   
10045 O  O   . HOH HA .   ? 0.4084 0.4853 0.4007 0.0118  0.0270  -0.0119 670 HOH C O   
10046 O  O   . HOH HA .   ? 0.5120 0.4798 0.2551 0.1580  -0.0116 -0.0566 671 HOH C O   
10047 O  O   . HOH HA .   ? 0.3242 0.3253 0.6001 -0.0326 0.0482  -0.0535 672 HOH C O   
10048 O  O   . HOH HA .   ? 0.4813 0.3971 0.3892 -0.0164 -0.0256 -0.0595 673 HOH C O   
10049 O  O   . HOH HA .   ? 0.3264 0.6378 0.2944 0.1229  0.0744  0.0705  674 HOH C O   
10050 O  O   . HOH HA .   ? 0.3943 0.3549 0.2949 0.1763  0.0329  0.0023  675 HOH C O   
10051 O  O   . HOH HA .   ? 0.5634 0.7572 0.4129 0.0024  -0.0507 0.1200  676 HOH C O   
10052 O  O   . HOH HA .   ? 0.2434 0.4438 0.5835 -0.0392 0.0093  0.2377  677 HOH C O   
10053 O  O   . HOH HA .   ? 0.4924 0.7574 0.6991 0.0253  -0.0283 -0.2017 678 HOH C O   
10054 O  O   . HOH HA .   ? 0.5202 0.2892 0.5005 0.0666  -0.1625 0.0465  679 HOH C O   
10055 O  O   . HOH HA .   ? 0.6013 0.2239 0.5277 0.0610  0.3034  0.0781  680 HOH C O   
10056 O  O   . HOH HA .   ? 0.5891 0.4680 0.3037 0.1098  -0.1595 -0.0386 681 HOH C O   
10057 O  O   . HOH HA .   ? 0.1962 0.2441 0.1725 0.0454  0.0397  0.0300  682 HOH C O   
10058 O  O   . HOH HA .   ? 0.5389 1.3585 0.4839 0.2363  0.1010  0.2093  683 HOH C O   
10059 O  O   . HOH HA .   ? 0.4307 0.7631 0.6111 0.0948  -0.0636 0.3206  684 HOH C O   
10060 O  O   . HOH HA .   ? 0.8098 0.2960 0.2156 0.0763  0.0763  -0.0040 685 HOH C O   
10061 O  O   . HOH HA .   ? 0.3030 0.4025 0.4311 -0.1352 0.1209  -0.1413 686 HOH C O   
10062 O  O   . HOH HA .   ? 0.4375 0.4156 0.5625 -0.0024 -0.0745 0.0006  687 HOH C O   
10063 O  O   . HOH HA .   ? 0.1984 0.1754 0.5126 -0.0526 0.0359  0.0241  688 HOH C O   
10064 O  O   . HOH HA .   ? 0.4595 0.3639 0.2689 -0.0023 -0.0460 0.0631  689 HOH C O   
10065 O  O   . HOH HA .   ? 0.6215 0.3537 0.5978 0.1825  0.1678  0.1852  690 HOH C O   
10066 O  O   . HOH HA .   ? 0.4253 0.4106 0.4579 -0.0366 0.0778  0.0068  691 HOH C O   
10067 O  O   . HOH HA .   ? 0.4235 0.3300 0.7350 0.0028  -0.0604 0.1650  692 HOH C O   
10068 O  O   . HOH HA .   ? 0.7203 0.4679 0.6258 -0.2545 -0.1914 -0.0421 693 HOH C O   
10069 O  O   . HOH HA .   ? 0.5943 0.4465 0.7161 0.0041  0.0392  0.1587  694 HOH C O   
10070 O  O   . HOH HA .   ? 0.3601 0.3161 0.3411 -0.0750 0.1221  0.0529  695 HOH C O   
10071 O  O   . HOH HA .   ? 0.4104 0.3806 0.3215 0.1512  0.2143  0.1563  696 HOH C O   
10072 O  O   . HOH HA .   ? 0.3989 0.1890 0.4733 0.0253  0.1040  0.0621  697 HOH C O   
10073 O  O   . HOH HA .   ? 0.2994 0.4731 0.2005 0.0667  0.1196  0.1124  698 HOH C O   
10074 O  O   . HOH HA .   ? 0.2222 0.4032 0.2531 0.0608  0.0412  0.0568  699 HOH C O   
10075 O  O   . HOH HA .   ? 0.3862 0.4605 0.3592 0.0225  -0.0005 -0.1277 700 HOH C O   
10076 O  O   . HOH HA .   ? 0.4210 0.5479 0.6281 -0.0856 -0.0141 0.2678  701 HOH C O   
10077 O  O   . HOH HA .   ? 0.3316 0.3725 0.2635 -0.1102 0.1277  -0.1140 702 HOH C O   
10078 O  O   . HOH HA .   ? 0.4486 0.2870 0.4000 0.0377  -0.0489 0.0847  703 HOH C O   
10079 O  O   . HOH HA .   ? 0.7602 0.2933 0.5188 0.0800  -0.1225 0.0617  704 HOH C O   
10080 O  O   . HOH HA .   ? 0.5353 0.3819 0.1671 0.1685  0.0483  0.0172  705 HOH C O   
10081 O  O   . HOH HA .   ? 0.3650 0.3181 0.2678 0.0292  0.0496  0.0670  706 HOH C O   
10082 O  O   . HOH HA .   ? 0.5217 0.6873 0.5429 0.0324  -0.1136 -0.2626 707 HOH C O   
10083 O  O   . HOH HA .   ? 0.5895 0.5354 0.4594 0.3169  0.0685  -0.0351 708 HOH C O   
10084 O  O   . HOH HA .   ? 0.4460 0.5507 0.5552 -0.1504 0.0922  0.1162  709 HOH C O   
10085 O  O   . HOH HA .   ? 0.3323 0.8399 0.3571 0.0958  0.0114  0.1639  710 HOH C O   
10086 O  O   . HOH HA .   ? 0.6165 0.3370 0.6506 0.2626  -0.0759 -0.0948 711 HOH C O   
10087 O  O   . HOH HA .   ? 0.3673 0.4952 0.5038 0.0606  0.0197  0.1679  712 HOH C O   
10088 O  O   . HOH HA .   ? 0.8371 0.4086 0.2454 0.2825  -0.0344 0.0119  713 HOH C O   
10089 O  O   . HOH HA .   ? 0.9900 0.5450 0.4174 0.0498  0.1304  0.0859  714 HOH C O   
10090 O  O   . HOH IA .   ? 0.5587 0.3533 0.3702 0.0432  -0.0329 -0.0485 401 HOH D O   
10091 O  O   . HOH IA .   ? 1.1111 2.0418 1.0305 0.6000  0.4950  0.7458  402 HOH D O   
10092 O  O   . HOH IA .   ? 0.3176 0.2381 0.1820 0.0436  0.0634  0.0219  403 HOH D O   
10093 O  O   . HOH IA .   ? 0.3711 0.4708 0.4038 0.0725  0.0820  0.1887  404 HOH D O   
10094 O  O   . HOH IA .   ? 0.3619 0.3788 0.2897 -0.0555 0.1111  -0.0229 405 HOH D O   
10095 O  O   . HOH IA .   ? 0.4192 0.4018 0.5857 0.1325  -0.0653 -0.0819 406 HOH D O   
10096 O  O   . HOH IA .   ? 0.5339 0.2775 0.3186 0.0427  0.0949  0.1384  407 HOH D O   
10097 O  O   . HOH IA .   ? 0.5648 0.2808 0.3468 0.0969  0.1826  0.0487  408 HOH D O   
10098 O  O   . HOH IA .   ? 0.7200 0.2194 0.2606 0.0513  0.2094  0.0120  409 HOH D O   
10099 O  O   . HOH IA .   ? 0.5113 0.5745 0.5139 -0.0320 -0.0749 -0.0692 410 HOH D O   
10100 O  O   . HOH IA .   ? 0.2411 0.2303 0.5103 0.0010  0.1580  0.1105  411 HOH D O   
10101 O  O   . HOH IA .   ? 0.6715 0.5206 0.3754 0.1527  -0.1142 -0.1324 412 HOH D O   
10102 O  O   . HOH IA .   ? 0.4562 0.2619 0.4354 -0.0026 0.0644  -0.0076 413 HOH D O   
10103 O  O   . HOH IA .   ? 0.3246 0.1401 0.2617 0.0513  0.0232  -0.0344 414 HOH D O   
10104 O  O   . HOH IA .   ? 1.4953 0.3217 1.2788 -0.0701 0.3357  -0.0469 415 HOH D O   
10105 O  O   . HOH IA .   ? 0.4354 0.1707 0.7524 0.0292  0.1631  0.0615  416 HOH D O   
10106 O  O   . HOH IA .   ? 0.6151 0.5109 0.5396 0.3063  0.1969  0.1326  417 HOH D O   
10107 O  O   . HOH IA .   ? 0.4748 0.5839 0.1865 0.1290  0.0399  0.0318  418 HOH D O   
10108 O  O   . HOH IA .   ? 0.2788 0.3544 0.3016 -0.0013 0.1098  0.0494  419 HOH D O   
10109 O  O   . HOH IA .   ? 0.3364 0.4688 0.3147 0.1054  0.0829  -0.0729 420 HOH D O   
10110 O  O   . HOH IA .   ? 0.3077 0.2504 0.3425 0.0306  0.0315  0.0186  421 HOH D O   
10111 O  O   . HOH IA .   ? 0.4476 0.4803 0.4967 -0.0245 0.1001  0.0094  422 HOH D O   
10112 O  O   . HOH IA .   ? 0.3084 0.3808 0.3037 0.0238  0.1106  -0.0237 423 HOH D O   
10113 O  O   . HOH IA .   ? 0.3316 0.2184 0.3634 0.0727  -0.0769 -0.0159 424 HOH D O   
10114 O  O   . HOH IA .   ? 0.5008 0.3738 0.2971 -0.1738 0.0303  -0.0441 425 HOH D O   
10115 O  O   . HOH IA .   ? 0.3456 0.2897 0.2552 -0.0035 0.0441  -0.0170 426 HOH D O   
10116 O  O   . HOH IA .   ? 0.4591 0.1845 0.1931 0.0118  0.0729  0.0208  427 HOH D O   
10117 O  O   . HOH IA .   ? 0.3133 0.3709 0.2204 -0.0917 0.0049  -0.0263 428 HOH D O   
10118 O  O   . HOH IA .   ? 0.7233 0.3634 0.4754 0.1413  -0.3452 0.0675  429 HOH D O   
10119 O  O   . HOH IA .   ? 0.2867 0.4453 0.3215 0.0948  0.0197  -0.0019 430 HOH D O   
10120 O  O   . HOH IA .   ? 0.1703 0.1093 0.0891 0.0102  0.0474  0.0078  431 HOH D O   
10121 O  O   . HOH IA .   ? 0.2483 0.2267 1.2249 0.1221  -0.0966 -0.1986 432 HOH D O   
10122 O  O   . HOH IA .   ? 0.4131 0.5683 0.2131 -0.1753 0.1330  -0.0712 433 HOH D O   
10123 O  O   . HOH IA .   ? 0.2953 0.2461 0.5403 -0.0252 0.0375  -0.1879 434 HOH D O   
10124 O  O   . HOH IA .   ? 0.2861 0.1701 0.5605 -0.0555 0.0846  -0.0737 435 HOH D O   
10125 O  O   . HOH IA .   ? 0.5796 0.2283 0.5214 -0.0073 0.0248  0.1324  436 HOH D O   
10126 O  O   . HOH IA .   ? 0.7013 0.2874 0.1872 0.1298  -0.0428 -0.0421 437 HOH D O   
10127 O  O   . HOH IA .   ? 0.3515 0.3941 0.2955 -0.0348 -0.0250 0.0979  438 HOH D O   
10128 O  O   . HOH IA .   ? 0.5612 0.4745 0.3066 -0.0745 0.1567  -0.0838 439 HOH D O   
10129 O  O   . HOH IA .   ? 0.3027 0.1991 0.1535 0.0509  -0.0124 -0.0055 440 HOH D O   
10130 O  O   . HOH IA .   ? 0.6468 0.8421 0.2445 -0.1042 0.2349  -0.0458 441 HOH D O   
10131 O  O   . HOH IA .   ? 0.3032 0.3118 0.3406 0.0173  -0.0397 -0.0285 442 HOH D O   
10132 O  O   . HOH IA .   ? 0.2037 0.1940 0.1536 0.0153  0.0416  0.0093  443 HOH D O   
10133 O  O   . HOH IA .   ? 0.3436 0.2190 0.4022 -0.0091 0.1077  -0.0687 444 HOH D O   
10134 O  O   . HOH IA .   ? 0.2029 0.2084 0.2486 0.0331  0.0825  -0.0236 445 HOH D O   
10135 O  O   . HOH IA .   ? 0.3695 0.8280 0.2520 -0.2282 0.0724  -0.0960 446 HOH D O   
10136 O  O   . HOH IA .   ? 0.7135 0.3968 0.8158 0.0579  -0.0399 0.2761  447 HOH D O   
10137 O  O   . HOH IA .   ? 0.3068 0.1604 0.3935 -0.0833 0.0041  -0.0315 448 HOH D O   
10138 O  O   . HOH IA .   ? 0.3289 0.1777 0.4597 -0.0489 -0.0083 -0.0261 449 HOH D O   
10139 O  O   . HOH IA .   ? 0.2865 0.3790 0.2842 0.0740  0.0702  0.0260  450 HOH D O   
10140 O  O   . HOH IA .   ? 0.3558 0.2321 0.7286 -0.0887 0.0423  -0.0700 451 HOH D O   
10141 O  O   . HOH IA .   ? 0.8174 0.3734 0.2908 0.2310  -0.0723 -0.1132 452 HOH D O   
10142 O  O   . HOH IA .   ? 0.3770 0.2318 0.2840 0.0164  0.1935  -0.0024 453 HOH D O   
10143 O  O   . HOH IA .   ? 0.4415 0.2301 0.1629 0.0918  0.1287  0.0196  454 HOH D O   
10144 O  O   . HOH IA .   ? 0.2373 0.2818 0.2502 -0.0767 0.0107  0.0302  455 HOH D O   
10145 O  O   . HOH IA .   ? 0.3907 0.7075 0.2928 0.1481  0.1664  0.0252  456 HOH D O   
10146 O  O   . HOH IA .   ? 0.4889 0.4043 0.2748 -0.2311 0.2002  -0.1680 457 HOH D O   
10147 O  O   . HOH IA .   ? 0.5274 0.1879 0.1782 0.1377  0.0637  -0.0086 458 HOH D O   
10148 O  O   . HOH IA .   ? 0.1592 0.7746 0.4476 0.0216  -0.0219 -0.2240 459 HOH D O   
10149 O  O   . HOH IA .   ? 0.7411 0.4767 0.4410 -0.1360 -0.0219 0.1829  460 HOH D O   
10150 O  O   . HOH IA .   ? 0.3169 0.2352 0.3574 0.0722  -0.0878 -0.0755 461 HOH D O   
10151 O  O   . HOH IA .   ? 0.2574 0.1878 0.2382 -0.0355 -0.0309 -0.0439 462 HOH D O   
10152 O  O   . HOH IA .   ? 0.6003 0.3600 0.8999 0.1664  -0.0129 -0.0364 463 HOH D O   
10153 O  O   . HOH IA .   ? 0.3143 0.1793 0.6743 -0.0104 0.0798  -0.0866 464 HOH D O   
10154 O  O   . HOH IA .   ? 0.4180 0.2008 0.4278 0.0080  0.0262  0.0109  465 HOH D O   
10155 O  O   . HOH IA .   ? 0.2337 0.1863 0.1326 -0.0186 0.0318  -0.0046 466 HOH D O   
10156 O  O   . HOH IA .   ? 0.1775 0.0897 0.1317 -0.0115 0.0167  0.0013  467 HOH D O   
10157 O  O   . HOH IA .   ? 0.2160 0.4896 0.4485 -0.0712 0.0881  0.0813  468 HOH D O   
10158 O  O   . HOH IA .   ? 0.1946 0.1430 0.1768 -0.0083 0.0177  -0.0194 469 HOH D O   
10159 O  O   . HOH IA .   ? 0.2883 0.4363 0.7041 -0.0021 -0.0943 -0.2795 470 HOH D O   
10160 O  O   . HOH IA .   ? 0.2565 0.2384 0.5307 -0.0816 0.1062  -0.0001 471 HOH D O   
10161 O  O   . HOH IA .   ? 0.5673 0.3179 0.3075 0.0672  -0.0370 -0.0807 472 HOH D O   
10162 O  O   . HOH IA .   ? 0.3522 0.3635 0.3398 0.0527  -0.0693 0.0388  473 HOH D O   
10163 O  O   . HOH IA .   ? 0.4874 0.4717 0.3176 -0.0215 0.0259  0.0777  474 HOH D O   
10164 O  O   . HOH IA .   ? 0.2445 0.2208 0.1577 -0.0478 0.0003  0.0342  475 HOH D O   
10165 O  O   . HOH IA .   ? 0.4738 0.1879 0.2953 0.0487  0.2093  0.0685  476 HOH D O   
10166 O  O   . HOH IA .   ? 0.7182 0.3436 0.3292 -0.1618 0.2569  -0.0144 477 HOH D O   
10167 O  O   . HOH IA .   ? 0.4084 0.1807 0.5784 -0.1186 -0.1908 0.1194  478 HOH D O   
10168 O  O   . HOH IA .   ? 0.2257 0.2341 0.4111 0.1052  0.0652  0.0590  479 HOH D O   
10169 O  O   . HOH IA .   ? 0.1588 0.1554 0.1915 -0.0038 0.0441  -0.0144 480 HOH D O   
10170 O  O   . HOH IA .   ? 0.2264 0.2014 0.3813 -0.0096 0.1105  0.0230  481 HOH D O   
10171 O  O   . HOH IA .   ? 0.2069 0.3714 0.2982 0.1032  0.1055  0.1080  482 HOH D O   
10172 O  O   . HOH IA .   ? 0.5090 0.3865 0.3867 0.0394  -0.0037 0.0020  483 HOH D O   
10173 O  O   . HOH IA .   ? 0.1894 0.1199 0.1545 -0.0124 0.0098  -0.0027 484 HOH D O   
10174 O  O   . HOH IA .   ? 0.1574 0.1527 0.1208 -0.0059 0.0293  -0.0166 485 HOH D O   
10175 O  O   . HOH IA .   ? 0.3955 0.8446 0.2624 -0.1970 -0.0243 0.1605  486 HOH D O   
10176 O  O   . HOH IA .   ? 0.2111 0.2044 0.1844 -0.0544 0.0062  0.0157  487 HOH D O   
10177 O  O   . HOH IA .   ? 0.5142 0.4907 0.4756 0.0463  -0.0272 -0.0996 488 HOH D O   
10178 O  O   . HOH IA .   ? 0.2125 0.0998 0.1332 0.0397  0.0868  0.0276  489 HOH D O   
10179 O  O   . HOH IA .   ? 0.6877 0.5008 0.2921 -0.0826 0.0793  0.0390  490 HOH D O   
10180 O  O   . HOH IA .   ? 0.4266 0.4756 0.4591 0.1868  0.2380  0.1339  491 HOH D O   
10181 O  O   . HOH IA .   ? 0.2637 0.3194 0.2623 0.0381  0.0753  -0.0120 492 HOH D O   
10182 O  O   . HOH IA .   ? 0.7296 0.3190 0.6223 0.0799  -0.2178 -0.0575 493 HOH D O   
10183 O  O   . HOH IA .   ? 0.2088 0.2294 0.2809 -0.0143 0.0373  -0.0032 494 HOH D O   
10184 O  O   . HOH IA .   ? 0.3003 0.2761 0.4573 0.0179  0.1261  0.0197  495 HOH D O   
10185 O  O   . HOH IA .   ? 0.2059 0.1132 0.3036 -0.0149 0.0842  -0.0074 496 HOH D O   
10186 O  O   . HOH IA .   ? 0.3515 0.2953 0.2275 0.0649  0.0364  -0.0188 497 HOH D O   
10187 O  O   . HOH IA .   ? 0.6470 0.3278 0.2750 0.1888  0.0803  0.0606  498 HOH D O   
10188 O  O   . HOH IA .   ? 0.2583 0.1808 0.4183 -0.0274 0.0711  -0.0078 499 HOH D O   
10189 O  O   . HOH IA .   ? 0.9401 0.2352 0.2644 0.1432  -0.1756 -0.0529 500 HOH D O   
10190 O  O   . HOH IA .   ? 0.5942 0.3531 0.2951 0.1403  -0.0775 0.1272  501 HOH D O   
10191 O  O   . HOH IA .   ? 0.4906 0.2493 0.3718 0.0436  0.0832  -0.0156 502 HOH D O   
10192 O  O   . HOH IA .   ? 0.2939 0.3407 0.7304 0.0138  -0.0806 -0.1334 503 HOH D O   
10193 O  O   . HOH IA .   ? 0.4162 0.4891 0.1669 -0.0917 0.0414  -0.0665 504 HOH D O   
10194 O  O   . HOH IA .   ? 0.3996 0.2260 0.1809 -0.0285 0.0555  0.0219  505 HOH D O   
10195 O  O   . HOH IA .   ? 0.2811 0.1676 0.7724 -0.0182 0.0794  -0.1008 506 HOH D O   
10196 O  O   . HOH IA .   ? 0.1283 0.0909 0.1073 0.0041  0.0423  0.0041  507 HOH D O   
10197 O  O   . HOH IA .   ? 0.1937 0.1109 0.1565 -0.0302 -0.0116 0.0377  508 HOH D O   
10198 O  O   . HOH IA .   ? 0.2185 0.2127 0.4259 0.0114  0.1635  0.1159  509 HOH D O   
10199 O  O   . HOH IA .   ? 0.2032 0.0894 0.1335 -0.0308 0.0643  -0.0182 510 HOH D O   
10200 O  O   . HOH IA .   ? 0.4902 0.2364 0.3023 -0.0798 0.0980  -0.1360 511 HOH D O   
10201 O  O   . HOH IA .   ? 0.2939 0.3282 0.1834 0.1319  0.1136  0.0555  512 HOH D O   
10202 O  O   . HOH IA .   ? 0.2386 0.2052 0.4036 -0.0390 -0.0816 0.0000  513 HOH D O   
10203 O  O   . HOH IA .   ? 0.3260 0.5497 0.1506 0.0351  0.0265  -0.0421 514 HOH D O   
10204 O  O   . HOH IA .   ? 0.4269 0.3529 0.5835 -0.0502 0.0038  0.1870  515 HOH D O   
10205 O  O   . HOH IA .   ? 0.2540 0.1669 0.2603 0.0027  0.0414  -0.0114 516 HOH D O   
10206 O  O   . HOH IA .   ? 0.4189 0.5217 0.7682 -0.0261 0.2283  -0.2569 517 HOH D O   
10207 O  O   . HOH IA .   ? 0.4959 0.1835 0.8578 -0.0243 0.2212  -0.1300 518 HOH D O   
10208 O  O   . HOH IA .   ? 0.4742 0.4979 0.5239 -0.1092 0.0654  -0.1174 519 HOH D O   
10209 O  O   . HOH IA .   ? 0.1756 0.0839 0.1500 0.0138  0.0865  0.0329  520 HOH D O   
10210 O  O   . HOH IA .   ? 0.7312 0.6207 0.3885 0.2802  -0.0856 0.0439  521 HOH D O   
10211 O  O   . HOH IA .   ? 0.3034 0.2148 0.2240 0.1141  0.0641  0.0189  522 HOH D O   
10212 O  O   . HOH IA .   ? 0.1924 0.0983 0.1748 0.0430  0.0588  0.0157  523 HOH D O   
10213 O  O   . HOH IA .   ? 0.1687 0.1048 0.1283 -0.0026 0.0489  -0.0080 524 HOH D O   
10214 O  O   . HOH IA .   ? 0.5060 0.5443 0.3912 -0.3088 -0.0720 0.1090  525 HOH D O   
10215 O  O   . HOH IA .   ? 0.3767 0.4950 0.4788 0.0055  0.0791  0.0568  526 HOH D O   
10216 O  O   . HOH IA .   ? 0.1386 0.1057 0.1094 0.0031  0.0194  -0.0184 527 HOH D O   
10217 O  O   . HOH IA .   ? 0.9169 0.3325 0.2348 0.1625  0.1105  -0.0188 528 HOH D O   
10218 O  O   . HOH IA .   ? 0.5309 0.2258 0.3718 0.1028  -0.0003 0.0601  529 HOH D O   
10219 O  O   . HOH IA .   ? 0.2723 0.2820 0.2314 -0.0724 0.0266  0.0200  530 HOH D O   
10220 O  O   . HOH IA .   ? 0.4237 0.3840 0.3583 0.1336  0.0141  -0.0759 531 HOH D O   
10221 O  O   . HOH IA .   ? 0.3050 0.2215 0.2145 0.0515  0.0091  -0.0635 532 HOH D O   
10222 O  O   . HOH IA .   ? 0.2955 0.4444 0.6071 -0.1352 0.0768  -0.0065 533 HOH D O   
10223 O  O   . HOH IA .   ? 0.2463 0.1845 0.1387 0.0066  0.0179  0.0087  534 HOH D O   
10224 O  O   . HOH IA .   ? 0.2734 0.2168 0.2063 0.0372  0.0688  0.0206  535 HOH D O   
10225 O  O   . HOH IA .   ? 0.2727 0.5018 0.3892 -0.0474 0.1371  -0.1808 536 HOH D O   
10226 O  O   . HOH IA .   ? 0.2714 0.1736 0.2560 0.0812  0.0766  0.0186  537 HOH D O   
10227 O  O   . HOH IA .   ? 0.2305 0.1773 0.3104 -0.0065 0.0529  0.0074  538 HOH D O   
10228 O  O   . HOH IA .   ? 0.4162 0.1723 0.6338 0.0416  0.1416  -0.0549 539 HOH D O   
10229 O  O   . HOH IA .   ? 0.6818 0.3555 0.2188 -0.0242 0.0100  -0.0648 540 HOH D O   
10230 O  O   . HOH IA .   ? 0.6129 0.5627 0.2915 -0.3104 -0.0135 0.0344  541 HOH D O   
10231 O  O   . HOH IA .   ? 0.1613 0.0800 0.1100 -0.0046 0.0183  -0.0080 542 HOH D O   
10232 O  O   . HOH IA .   ? 0.1772 0.2441 0.2624 0.0052  0.0251  0.0131  543 HOH D O   
10233 O  O   . HOH IA .   ? 0.2865 0.3057 0.2680 -0.0621 -0.0288 0.0186  544 HOH D O   
10234 O  O   . HOH IA .   ? 0.3847 0.2721 0.1946 -0.0500 0.0595  0.0273  545 HOH D O   
10235 O  O   . HOH IA .   ? 0.4888 0.3413 0.8783 0.0140  0.2371  0.0251  546 HOH D O   
10236 O  O   . HOH IA .   ? 0.2305 0.3337 0.2536 0.1231  0.1668  0.1555  547 HOH D O   
10237 O  O   . HOH IA .   ? 0.3055 0.2293 0.3962 -0.0954 0.1128  -0.0759 548 HOH D O   
10238 O  O   . HOH IA .   ? 0.5802 0.2318 0.2039 0.0612  -0.0778 0.0031  549 HOH D O   
10239 O  O   . HOH IA .   ? 0.4072 0.2705 0.4397 -0.1279 0.0182  0.1164  550 HOH D O   
10240 O  O   . HOH IA .   ? 0.9466 0.2698 0.9588 -0.0273 -0.3273 0.0452  551 HOH D O   
10241 O  O   . HOH IA .   ? 0.2975 0.6032 0.4171 -0.1439 0.0164  -0.0021 552 HOH D O   
10242 O  O   . HOH IA .   ? 0.3675 0.2912 0.2682 -0.1280 -0.0049 0.0625  553 HOH D O   
10243 O  O   . HOH IA .   ? 0.5241 0.4275 0.3521 -0.2337 0.1808  -0.0549 554 HOH D O   
10244 O  O   . HOH IA .   ? 0.3614 0.3120 0.3684 0.0219  0.0392  -0.0163 555 HOH D O   
10245 O  O   . HOH IA .   ? 0.6194 0.4246 0.4828 0.0957  0.1922  0.1199  556 HOH D O   
10246 O  O   . HOH IA .   ? 0.4716 0.1744 0.7181 -0.1287 0.1062  -0.0582 557 HOH D O   
10247 O  O   . HOH IA .   ? 0.1684 0.1447 0.1984 0.0054  0.0010  -0.0015 558 HOH D O   
10248 O  O   . HOH IA .   ? 0.3251 0.1965 0.1958 -0.0414 0.0092  0.0280  559 HOH D O   
10249 O  O   . HOH IA .   ? 0.5655 0.2204 0.1967 -0.1872 0.1114  -0.0454 560 HOH D O   
10250 O  O   . HOH IA .   ? 0.2299 0.4695 0.4181 0.0522  0.1298  0.1378  561 HOH D O   
10251 O  O   . HOH IA .   ? 0.3438 0.3948 0.3070 0.2064  0.0071  -0.0879 562 HOH D O   
10252 O  O   . HOH IA .   ? 0.2578 0.2657 0.1648 -0.0463 0.0230  0.0200  563 HOH D O   
10253 O  O   . HOH IA .   ? 0.7429 0.5867 0.5135 -0.4257 -0.3077 0.3210  564 HOH D O   
10254 O  O   . HOH IA .   ? 0.1897 0.1314 0.2676 -0.0256 0.0364  -0.0176 565 HOH D O   
10255 O  O   . HOH IA .   ? 0.2113 0.1490 0.2314 -0.0271 0.0706  0.0340  566 HOH D O   
10256 O  O   . HOH IA .   ? 0.3143 0.2384 0.5515 0.0518  0.1508  -0.0119 567 HOH D O   
10257 O  O   . HOH IA .   ? 0.5386 0.5487 0.4723 0.2766  0.1721  0.1357  568 HOH D O   
10258 O  O   . HOH IA .   ? 0.4056 0.3384 0.4956 -0.0463 0.1272  0.0070  569 HOH D O   
10259 O  O   . HOH IA .   ? 0.2779 0.2581 0.6430 -0.0553 -0.0746 -0.0108 570 HOH D O   
10260 O  O   . HOH IA .   ? 0.4070 0.1296 0.8741 0.0125  -0.0935 0.0082  571 HOH D O   
10261 O  O   . HOH IA .   ? 0.4300 0.1680 0.1658 -0.0214 0.0716  -0.0577 572 HOH D O   
10262 O  O   . HOH IA .   ? 0.2786 0.2382 0.2748 -0.0731 0.0337  0.0148  573 HOH D O   
10263 O  O   . HOH IA .   ? 0.2263 0.1378 0.2971 0.0031  -0.0516 -0.0421 574 HOH D O   
10264 O  O   . HOH IA .   ? 0.3962 0.1434 0.1206 0.0557  0.0771  -0.0209 575 HOH D O   
10265 O  O   . HOH IA .   ? 0.4795 0.1800 0.7215 0.1129  -0.1255 0.0526  576 HOH D O   
10266 O  O   . HOH IA .   ? 0.8054 0.4305 0.2766 -0.1489 -0.0826 -0.0368 577 HOH D O   
10267 O  O   . HOH IA .   ? 0.5685 0.2185 0.6394 -0.0208 0.2576  -0.0130 578 HOH D O   
10268 O  O   . HOH IA .   ? 0.5065 0.3242 0.5867 -0.0436 0.1419  -0.2478 579 HOH D O   
10269 O  O   . HOH IA .   ? 0.2991 0.1903 0.2285 -0.0333 -0.0286 -0.0298 580 HOH D O   
10270 O  O   . HOH IA .   ? 0.1930 0.1671 0.2036 0.0465  0.0790  0.0008  581 HOH D O   
10271 O  O   . HOH IA .   ? 0.1583 0.1770 0.3339 -0.0478 0.0483  -0.0449 582 HOH D O   
10272 O  O   . HOH IA .   ? 0.2258 0.1477 0.1644 -0.0271 0.0428  -0.0062 583 HOH D O   
10273 O  O   . HOH IA .   ? 0.3495 0.2433 0.1411 -0.1582 -0.0147 0.0204  584 HOH D O   
10274 O  O   . HOH IA .   ? 0.4519 0.4396 0.4652 -0.0560 0.0000  0.0441  585 HOH D O   
10275 O  O   . HOH IA .   ? 0.3282 0.2490 0.4165 0.0295  0.0826  -0.0147 586 HOH D O   
10276 O  O   . HOH IA .   ? 0.3666 0.1606 0.2973 0.0109  -0.0684 -0.0163 587 HOH D O   
10277 O  O   . HOH IA .   ? 0.4891 0.2955 0.2720 0.0917  -0.0136 -0.0527 588 HOH D O   
10278 O  O   . HOH IA .   ? 0.5501 0.4596 0.3133 -0.3052 0.0166  0.0603  589 HOH D O   
10279 O  O   . HOH IA .   ? 0.3217 0.1884 0.1225 -0.0068 0.0643  -0.0214 590 HOH D O   
10280 O  O   . HOH IA .   ? 0.2960 0.5554 0.6255 0.0012  -0.0065 -0.3655 591 HOH D O   
10281 O  O   . HOH IA .   ? 0.2381 0.1974 0.3407 0.0267  0.0247  -0.0364 592 HOH D O   
10282 O  O   . HOH IA .   ? 0.2060 0.2632 0.2734 -0.0776 0.0421  0.0296  593 HOH D O   
10283 O  O   . HOH IA .   ? 0.3003 0.1319 0.0982 -0.0166 0.0390  -0.0143 594 HOH D O   
10284 O  O   . HOH IA .   ? 1.1770 0.7161 0.2467 0.1554  0.0901  -0.1181 595 HOH D O   
10285 O  O   . HOH IA .   ? 0.2007 0.2691 0.1771 0.0108  0.0241  -0.0856 596 HOH D O   
10286 O  O   . HOH IA .   ? 0.7210 0.2278 0.2585 -0.2372 -0.1682 0.0776  597 HOH D O   
10287 O  O   . HOH IA .   ? 0.2131 0.1942 0.1768 -0.0416 0.0127  0.0377  598 HOH D O   
10288 O  O   . HOH IA .   ? 0.2341 0.2678 0.2879 -0.0065 0.0756  0.0241  599 HOH D O   
10289 O  O   . HOH IA .   ? 0.2791 0.2820 0.2382 0.0184  0.0727  -0.0076 600 HOH D O   
10290 O  O   . HOH IA .   ? 1.3129 0.6323 1.4113 -0.1018 -0.1032 0.0610  601 HOH D O   
10291 O  O   . HOH IA .   ? 0.2903 0.2858 0.4730 0.0445  0.1483  0.0601  602 HOH D O   
10292 O  O   . HOH IA .   ? 0.2222 0.1829 0.2867 -0.0671 0.0566  -0.0076 603 HOH D O   
10293 O  O   . HOH IA .   ? 0.1964 0.1511 0.1437 -0.0264 0.0308  -0.0021 604 HOH D O   
10294 O  O   . HOH IA .   ? 0.1434 0.1121 0.1147 -0.0142 0.0366  -0.0060 605 HOH D O   
10295 O  O   . HOH IA .   ? 0.4066 0.4891 0.4002 -0.0171 0.1151  0.1259  606 HOH D O   
10296 O  O   . HOH IA .   ? 0.1757 0.3998 0.4389 -0.0944 -0.0421 0.2354  607 HOH D O   
10297 O  O   . HOH IA .   ? 0.4165 1.0819 0.4077 -0.0546 -0.0373 0.2851  608 HOH D O   
10298 O  O   . HOH IA .   ? 0.2691 0.3591 0.5827 -0.0939 0.1951  0.0355  609 HOH D O   
10299 O  O   . HOH IA .   ? 1.0348 0.7605 0.7533 -0.2066 0.2275  -0.1511 610 HOH D O   
10300 O  O   . HOH IA .   ? 0.4483 0.1545 0.2418 0.0276  0.0463  -0.0041 611 HOH D O   
10301 O  O   . HOH IA .   ? 0.1450 0.1254 0.2095 -0.0024 0.0719  0.0331  612 HOH D O   
10302 O  O   . HOH IA .   ? 0.5145 0.4517 0.4135 0.0447  0.0048  -0.0308 613 HOH D O   
10303 O  O   . HOH IA .   ? 0.5443 0.3542 0.3267 0.2370  0.1800  0.0640  614 HOH D O   
10304 O  O   . HOH IA .   ? 0.7542 0.2185 0.2255 -0.0649 0.0676  -0.0384 615 HOH D O   
10305 O  O   . HOH IA .   ? 0.2518 0.3037 0.1886 0.0844  0.0940  0.0155  616 HOH D O   
10306 O  O   . HOH IA .   ? 0.3093 0.3750 0.6301 0.0927  0.0030  0.2311  617 HOH D O   
10307 O  O   . HOH IA .   ? 0.6833 0.5544 0.3177 -0.4654 0.0568  -0.0296 618 HOH D O   
10308 O  O   . HOH IA .   ? 0.3416 0.2973 0.4036 0.1226  0.1212  0.0346  619 HOH D O   
10309 O  O   . HOH IA .   ? 0.2412 0.1416 0.1730 0.0377  0.0505  -0.0271 620 HOH D O   
10310 O  O   . HOH IA .   ? 0.3614 0.4354 0.2651 0.1036  0.1191  0.1895  621 HOH D O   
10311 O  O   . HOH IA .   ? 0.3725 0.4637 0.4727 0.1356  0.1978  0.1096  622 HOH D O   
10312 O  O   . HOH IA .   ? 0.8962 0.3400 0.7397 0.2427  0.4713  0.2003  623 HOH D O   
10313 O  O   . HOH IA .   ? 0.3693 0.1960 0.2382 0.0104  0.0414  0.0267  624 HOH D O   
10314 O  O   . HOH IA .   ? 0.7637 0.4988 0.2599 0.0228  -0.0566 -0.0636 625 HOH D O   
10315 O  O   . HOH IA .   ? 0.3961 0.3075 0.2585 0.0342  0.1500  0.0568  626 HOH D O   
10316 O  O   . HOH IA .   ? 0.2412 0.4648 0.2581 -0.1019 0.0886  -0.1138 627 HOH D O   
10317 O  O   . HOH IA .   ? 0.4379 0.4889 0.6230 0.1441  -0.0288 -0.2484 628 HOH D O   
10318 O  O   . HOH IA .   ? 0.3046 0.5110 0.5135 -0.0305 0.1368  0.0905  629 HOH D O   
10319 O  O   . HOH IA .   ? 0.2799 0.3842 0.2750 0.0233  0.0502  -0.0048 630 HOH D O   
10320 O  O   . HOH IA .   ? 0.2664 0.5200 0.3278 -0.0684 -0.0434 0.2408  631 HOH D O   
10321 O  O   . HOH IA .   ? 0.6488 0.2357 0.4104 0.1891  0.0737  0.0951  632 HOH D O   
10322 O  O   . HOH IA .   ? 0.3057 0.3005 0.2328 -0.0175 0.0277  0.0239  633 HOH D O   
10323 O  O   . HOH IA .   ? 0.3210 0.2502 0.3131 -0.0921 0.1330  -0.0366 634 HOH D O   
10324 O  O   . HOH IA .   ? 0.1845 0.2161 0.3125 -0.0060 0.0460  -0.0654 635 HOH D O   
10325 O  O   . HOH IA .   ? 0.3650 0.3641 0.9606 -0.1547 0.1138  -0.0496 636 HOH D O   
10326 O  O   . HOH IA .   ? 0.4839 0.3849 0.3003 0.0023  0.1159  -0.0460 637 HOH D O   
10327 O  O   . HOH IA .   ? 0.3291 0.2581 0.3558 0.0487  -0.0348 -0.0245 638 HOH D O   
10328 O  O   . HOH IA .   ? 0.2476 0.2741 0.4523 -0.0635 0.1447  0.0777  639 HOH D O   
10329 O  O   . HOH IA .   ? 0.2576 0.2696 0.2962 0.0324  0.0244  -0.0992 640 HOH D O   
10330 O  O   . HOH IA .   ? 0.1743 0.1310 0.2642 -0.0017 0.0348  0.0021  641 HOH D O   
10331 O  O   . HOH IA .   ? 0.2732 0.1463 0.1642 -0.0044 0.0000  0.0054  642 HOH D O   
10332 O  O   . HOH IA .   ? 0.4359 0.4587 0.1547 0.1503  0.0658  -0.0432 643 HOH D O   
10333 O  O   . HOH IA .   ? 0.4126 0.1935 0.2377 -0.0720 -0.0671 0.0276  644 HOH D O   
10334 O  O   . HOH IA .   ? 0.4896 0.4431 0.4541 -0.0447 -0.0432 0.0177  645 HOH D O   
10335 O  O   . HOH IA .   ? 0.2628 0.2494 0.3503 -0.0031 -0.0129 -0.0694 646 HOH D O   
10336 O  O   . HOH IA .   ? 0.3652 0.1964 0.2637 -0.0251 0.0772  -0.0524 647 HOH D O   
10337 O  O   . HOH IA .   ? 0.3118 0.2852 0.2185 0.0542  0.0366  -0.0040 648 HOH D O   
10338 O  O   . HOH IA .   ? 0.6399 0.2693 0.4404 0.0917  0.0688  0.0238  649 HOH D O   
10339 O  O   . HOH IA .   ? 0.4255 0.7082 0.2800 -0.3174 0.0687  -0.0948 650 HOH D O   
10340 O  O   . HOH IA .   ? 0.4176 0.6516 0.4648 0.0059  0.0768  0.0017  651 HOH D O   
10341 O  O   . HOH IA .   ? 0.3535 0.4731 0.3424 -0.0304 0.1574  -0.0621 652 HOH D O   
10342 O  O   . HOH IA .   ? 0.4180 0.3291 0.5338 0.0390  -0.2070 -0.1226 653 HOH D O   
10343 O  O   . HOH IA .   ? 0.5156 0.4751 0.3612 -0.0804 -0.0701 -0.1449 654 HOH D O   
10344 O  O   . HOH IA .   ? 1.2668 0.4740 0.3883 -0.1847 0.2044  -0.1348 655 HOH D O   
10345 O  O   . HOH IA .   ? 0.9760 0.2168 0.5144 -0.0392 0.2777  0.0693  656 HOH D O   
10346 O  O   . HOH IA .   ? 0.4338 0.3962 0.3319 0.0681  0.1155  0.1168  657 HOH D O   
10347 O  O   . HOH IA .   ? 0.3930 0.5947 0.7675 0.1178  0.1081  0.1030  658 HOH D O   
10348 O  O   . HOH IA .   ? 0.4167 0.3998 0.4593 0.1001  0.0276  -0.0784 659 HOH D O   
10349 O  O   . HOH IA .   ? 0.6065 0.5256 0.6510 0.3127  -0.1789 -0.2143 660 HOH D O   
10350 O  O   . HOH IA .   ? 0.2861 0.1903 0.3027 0.0076  0.0062  -0.0006 661 HOH D O   
10351 O  O   . HOH IA .   ? 0.5116 0.5479 0.5149 -0.0027 0.0555  0.0483  662 HOH D O   
10352 O  O   . HOH IA .   ? 1.0040 0.2328 0.5145 0.0507  -0.1515 -0.0313 663 HOH D O   
10353 O  O   . HOH IA .   ? 0.4295 0.3996 0.4052 0.0724  0.1396  -0.0133 664 HOH D O   
10354 O  O   . HOH IA .   ? 0.3885 0.2806 0.4472 -0.0465 0.1352  -0.0599 665 HOH D O   
10355 O  O   . HOH IA .   ? 0.6793 0.3838 0.6653 0.0086  0.3718  0.1098  666 HOH D O   
10356 O  O   . HOH IA .   ? 0.4826 0.3285 0.4244 0.0588  0.1645  -0.0460 667 HOH D O   
10357 O  O   . HOH IA .   ? 0.4668 0.7924 0.3483 -0.3298 -0.0599 0.1292  668 HOH D O   
10358 O  O   . HOH IA .   ? 0.4887 0.4849 0.5329 0.0017  -0.0146 -0.0026 669 HOH D O   
10359 O  O   . HOH IA .   ? 0.4887 1.3402 1.0585 0.0961  0.0904  -0.0570 670 HOH D O   
10360 O  O   . HOH IA .   ? 0.4767 0.5041 0.2904 0.2556  0.0926  -0.0410 671 HOH D O   
10361 O  O   . HOH IA .   ? 0.3795 0.6991 0.6881 0.0267  -0.1147 0.0310  672 HOH D O   
10362 O  O   . HOH IA .   ? 0.4257 0.3474 0.5321 0.1217  0.0384  0.0900  673 HOH D O   
10363 O  O   . HOH IA .   ? 0.4532 0.2481 0.5205 -0.1155 -0.0288 0.0366  674 HOH D O   
10364 O  O   . HOH IA .   ? 0.3923 0.4268 1.5102 -0.1094 -0.1861 0.2813  675 HOH D O   
10365 O  O   . HOH IA .   ? 0.2336 0.2035 0.3810 -0.0233 0.0428  0.0476  676 HOH D O   
10366 O  O   . HOH IA .   ? 0.2953 0.2285 0.2526 -0.0260 0.0102  0.0030  677 HOH D O   
10367 O  O   . HOH IA .   ? 0.5723 0.6017 0.4314 0.0807  -0.0970 -0.1613 678 HOH D O   
10368 O  O   . HOH IA .   ? 0.4476 0.6378 0.4180 -0.1365 -0.0178 -0.1037 679 HOH D O   
10369 O  O   . HOH IA .   ? 0.4147 0.3239 0.2298 -0.0901 0.0212  -0.0232 680 HOH D O   
10370 O  O   . HOH IA .   ? 0.2305 0.2125 0.2360 0.0292  0.0970  0.0284  681 HOH D O   
10371 O  O   . HOH IA .   ? 0.3208 0.2504 0.2628 -0.0357 0.0562  0.0890  682 HOH D O   
10372 O  O   . HOH IA .   ? 0.8410 0.5041 0.5756 0.2599  0.3666  0.0917  683 HOH D O   
10373 O  O   . HOH IA .   ? 1.0579 0.4652 0.3531 -0.2155 0.1159  -0.0679 684 HOH D O   
10374 O  O   . HOH IA .   ? 0.3330 0.1870 0.2603 0.0586  0.1150  0.0693  685 HOH D O   
10375 O  O   . HOH IA .   ? 0.2930 0.3203 0.3294 0.0564  0.1146  -0.0132 686 HOH D O   
10376 O  O   . HOH IA .   ? 0.2145 0.9258 0.8752 -0.0364 0.0581  0.0318  687 HOH D O   
10377 O  O   . HOH IA .   ? 0.8622 0.3441 5.7465 0.3377  1.2620  0.7882  688 HOH D O   
10378 O  O   . HOH IA .   ? 0.5411 0.3817 0.3826 0.1445  0.0653  0.0788  689 HOH D O   
10379 O  O   . HOH IA .   ? 0.4957 0.3194 0.3409 0.0285  0.0557  0.0021  690 HOH D O   
10380 O  O   . HOH IA .   ? 0.2118 0.2626 0.1942 -0.0308 0.0601  -0.0026 691 HOH D O   
10381 O  O   . HOH IA .   ? 0.3334 0.2646 0.4354 0.0815  0.2552  0.1237  692 HOH D O   
10382 O  O   . HOH IA .   ? 0.4230 0.4106 0.8173 -0.1111 0.1067  0.1226  693 HOH D O   
10383 O  O   . HOH IA .   ? 0.2804 0.3170 0.6147 -0.0060 0.0715  0.1008  694 HOH D O   
10384 O  O   . HOH IA .   ? 0.2170 0.2077 0.1883 0.0186  0.0116  0.0307  695 HOH D O   
10385 O  O   . HOH IA .   ? 0.2646 0.3095 0.2493 0.0030  0.0218  -0.0017 696 HOH D O   
10386 O  O   . HOH IA .   ? 0.4720 0.4332 0.3935 -0.0253 -0.0771 0.0873  697 HOH D O   
10387 O  O   . HOH IA .   ? 0.5001 0.2689 0.5659 0.1948  0.0471  -0.1609 698 HOH D O   
10388 O  O   . HOH IA .   ? 0.3855 0.3824 0.7387 -0.1010 0.1648  -0.3129 699 HOH D O   
10389 O  O   . HOH IA .   ? 0.6238 0.9440 0.4203 -0.3912 0.1336  -0.1843 700 HOH D O   
10390 O  O   . HOH IA .   ? 0.4088 0.1799 0.5099 0.0447  -0.0921 -0.0428 701 HOH D O   
10391 O  O   . HOH IA .   ? 0.2827 0.2617 0.4553 0.0417  0.1405  0.0623  702 HOH D O   
10392 O  O   . HOH IA .   ? 0.2447 0.3849 0.1484 0.0229  0.0590  0.0034  703 HOH D O   
10393 O  O   . HOH IA .   ? 0.4400 0.4648 0.7226 -0.0063 0.1889  -0.0916 704 HOH D O   
10394 O  O   . HOH IA .   ? 0.6098 0.7021 0.3201 -0.1093 0.0670  -0.0296 705 HOH D O   
10395 O  O   . HOH IA .   ? 0.5943 0.4848 0.4314 -0.0071 0.0097  -0.0031 706 HOH D O   
10396 O  O   . HOH IA .   ? 0.3937 0.3549 0.5436 0.1221  0.0515  0.0131  707 HOH D O   
10397 O  O   . HOH IA .   ? 0.9175 0.3246 0.2800 -0.0838 0.1379  -0.0529 708 HOH D O   
10398 O  O   . HOH IA .   ? 0.3411 0.3901 0.4115 -0.0041 0.1880  -0.0137 709 HOH D O   
10399 O  O   . HOH IA .   ? 0.7505 0.3111 0.3240 0.2234  0.1097  0.0989  710 HOH D O   
10400 O  O   . HOH IA .   ? 0.4225 0.2321 0.4680 -0.0498 0.2066  -0.0057 711 HOH D O   
10401 O  O   . HOH IA .   ? 0.4043 0.2592 0.5266 -0.0100 0.1064  -0.0214 712 HOH D O   
10402 O  O   . HOH IA .   ? 0.3840 0.3231 0.3582 0.0000  0.1254  0.1262  713 HOH D O   
10403 O  O   . HOH IA .   ? 0.5203 0.2569 0.2481 -0.0452 0.1045  0.0390  714 HOH D O   
10404 O  O   . HOH IA .   ? 0.3682 0.2269 0.2653 0.0212  -0.0181 0.0375  715 HOH D O   
10405 O  O   . HOH IA .   ? 0.2310 0.5927 0.2463 -0.0324 0.0715  0.1348  716 HOH D O   
10406 O  O   . HOH IA .   ? 0.6816 0.2728 0.4519 0.1206  0.0289  0.0601  717 HOH D O   
10407 O  O   . HOH IA .   ? 0.3048 0.3170 0.2157 -0.1217 0.0410  0.0186  718 HOH D O   
10408 O  O   . HOH IA .   ? 0.4705 0.9323 0.5871 0.1247  -0.0544 0.2338  719 HOH D O   
10409 O  O   . HOH IA .   ? 0.2583 0.3224 0.3273 0.0507  0.0487  0.0093  720 HOH D O   
10410 O  O   . HOH IA .   ? 0.3695 0.3894 0.3799 -0.2070 -0.0808 -0.0421 721 HOH D O   
10411 O  O   . HOH IA .   ? 0.3314 0.6122 0.5837 -0.1316 0.2099  -0.0092 722 HOH D O   
10412 O  O   . HOH IA .   ? 0.2357 0.2409 0.2522 -0.0241 0.0013  0.0313  723 HOH D O   
10413 O  O   . HOH IA .   ? 0.6930 0.2021 0.3632 0.0634  -0.0131 0.0266  724 HOH D O   
10414 O  O   . HOH IA .   ? 0.4997 0.4375 0.5078 0.0021  0.0342  0.0203  725 HOH D O   
10415 O  O   . HOH IA .   ? 1.6440 0.2301 0.7947 -0.0362 0.7649  -0.2383 726 HOH D O   
10416 O  O   . HOH IA .   ? 0.6158 0.4302 0.4199 0.2748  0.2276  0.2178  727 HOH D O   
10417 O  O   . HOH IA .   ? 0.3260 0.2208 0.2143 0.0746  0.0326  -0.0940 728 HOH D O   
10418 O  O   . HOH IA .   ? 0.5401 0.5410 0.3163 0.2017  -0.1275 -0.1218 729 HOH D O   
10419 O  O   . HOH IA .   ? 0.3786 0.3515 0.3195 0.1264  -0.0251 -0.0309 730 HOH D O   
10420 O  O   . HOH IA .   ? 0.5485 0.5371 0.5644 0.1066  -0.0425 0.0291  731 HOH D O   
10421 O  O   . HOH IA .   ? 0.3404 0.3174 0.3124 -0.0172 -0.0722 0.0601  732 HOH D O   
10422 O  O   . HOH IA .   ? 0.2913 0.4013 0.4133 -0.0065 0.0568  0.1978  733 HOH D O   
10423 O  O   . HOH IA .   ? 0.3010 0.2725 0.5432 -0.0021 0.0560  0.1106  734 HOH D O   
10424 O  O   . HOH IA .   ? 0.8120 0.2100 0.2748 0.0397  0.1630  -0.0281 735 HOH D O   
10425 O  O   . HOH IA .   ? 0.4643 0.7867 0.3950 0.1307  0.1199  0.3140  736 HOH D O   
10426 O  O   . HOH IA .   ? 0.7037 0.4910 0.5487 0.1459  0.2404  -0.0725 737 HOH D O   
10427 O  O   . HOH IA .   ? 0.5429 0.3194 0.2263 0.0606  0.0161  -0.0302 738 HOH D O   
10428 O  O   . HOH IA .   ? 0.4576 0.5906 0.3799 0.0615  0.1280  0.1796  739 HOH D O   
10429 O  O   . HOH IA .   ? 0.3582 0.6100 0.4207 0.1155  0.0974  -0.0971 740 HOH D O   
10430 O  O   . HOH IA .   ? 0.5019 0.4190 0.2649 -0.0104 -0.0294 0.0087  741 HOH D O   
10431 O  O   . HOH IA .   ? 0.4799 0.4616 0.4548 0.1964  -0.1014 -0.0619 742 HOH D O   
10432 O  O   . HOH IA .   ? 0.4490 0.5473 0.9250 0.1554  -0.1674 -0.1049 743 HOH D O   
10433 O  O   . HOH IA .   ? 0.4110 0.3386 0.3046 0.0948  0.0428  0.0395  744 HOH D O   
10434 O  O   . HOH IA .   ? 0.5411 0.3262 0.7329 0.0140  0.1926  0.1421  745 HOH D O   
10435 O  O   . HOH IA .   ? 0.6585 0.3847 0.2610 0.1398  0.0649  0.0544  746 HOH D O   
10436 O  O   . HOH IA .   ? 0.5606 0.1946 0.3792 0.0238  0.2340  0.0571  747 HOH D O   
10437 O  O   . HOH IA .   ? 0.4708 0.5005 0.4641 -0.0080 -0.0027 -0.0071 748 HOH D O   
10438 O  O   . HOH IA .   ? 0.5228 0.3280 0.6625 -0.1124 0.1898  -0.0350 749 HOH D O   
10439 O  O   . HOH IA .   ? 0.2840 0.2560 0.2100 0.0080  0.0516  -0.0251 750 HOH D O   
10440 O  O   . HOH IA .   ? 0.4449 0.4670 0.5167 0.0324  0.0719  -0.1562 751 HOH D O   
10441 O  O   . HOH IA .   ? 0.6722 0.2542 0.2939 0.2046  0.2646  0.1174  752 HOH D O   
10442 O  O   . HOH IA .   ? 0.4857 0.4823 0.4968 -0.0679 0.0136  0.0082  753 HOH D O   
10443 O  O   . HOH IA .   ? 0.2601 0.2208 0.2339 0.0280  0.1074  -0.0729 754 HOH D O   
10444 O  O   . HOH IA .   ? 0.6057 0.4018 0.3589 0.1761  0.1071  0.1256  755 HOH D O   
10445 O  O   . HOH IA .   ? 0.3553 0.3583 0.2475 -0.0198 0.1178  0.0747  756 HOH D O   
10446 O  O   . HOH IA .   ? 0.5756 0.4000 0.3055 -0.0703 0.0208  -0.0626 757 HOH D O   
10447 O  O   . HOH IA .   ? 0.5669 0.5383 0.3680 -0.0284 -0.0197 0.0297  758 HOH D O   
10448 O  O   . HOH IA .   ? 0.4812 0.4547 0.4072 -0.0559 0.0685  0.0487  759 HOH D O   
10449 O  O   . HOH IA .   ? 0.3603 0.7088 0.3573 0.0120  -0.0373 0.0295  760 HOH D O   
10450 O  O   . HOH IA .   ? 0.4701 0.5536 0.4801 -0.3204 -0.0883 0.2471  761 HOH D O   
10451 O  O   . HOH IA .   ? 0.4126 0.3591 0.5329 -0.0277 0.1107  -0.1255 762 HOH D O   
10452 O  O   . HOH IA .   ? 0.3115 0.4554 0.7129 0.0608  -0.0133 -0.2370 763 HOH D O   
10453 O  O   . HOH IA .   ? 0.6481 0.3928 0.4410 -0.0041 -0.2070 0.0304  764 HOH D O   
10454 O  O   . HOH IA .   ? 0.2935 0.2545 0.1807 0.0304  0.0255  -0.0331 765 HOH D O   
10455 O  O   . HOH IA .   ? 0.6927 0.4108 0.5512 -0.2272 -0.0505 0.1867  766 HOH D O   
10456 O  O   . HOH IA .   ? 0.7142 0.3844 0.3217 0.0807  0.0489  -0.0904 767 HOH D O   
# 
