data_6G5L
# 
_entry.id   6G5L 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   6G5L         pdb_00006g5l 10.2210/pdb6g5l/pdb 
WWPDB D_1200009427 ?            ?                   
# 
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 2019-03-13 
2 'Structure model' 1 1 2024-01-17 
3 'Structure model' 1 2 2024-11-06 
# 
_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' pdbx_initial_refinement_model 
5 2 'Structure model' struct_conn                   
6 3 'Structure model' pdbx_entry_details            
7 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' '_struct_conn.pdbx_dist_value'         
4  2 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id' 
5  2 'Structure model' '_struct_conn.ptnr1_auth_asym_id'      
6  2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'      
7  2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'       
8  2 'Structure model' '_struct_conn.ptnr1_label_asym_id'     
9  2 'Structure model' '_struct_conn.ptnr1_label_atom_id'     
10 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'     
11 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'      
12 2 'Structure model' '_struct_conn.ptnr2_auth_asym_id'      
13 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'      
14 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'       
15 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'     
16 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'     
17 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                        6G5L 
_pdbx_database_status.recvd_initial_deposition_date   2018-03-29 
_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_
_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                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Eur J Med Chem' 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           1768-3254 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            156 
_citation.language                  ? 
_citation.page_first                61 
_citation.page_last                 78 
_citation.title                     
'Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.' 
_citation.year                      2018 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2018.06.059 
_citation.pdbx_database_id_PubMed   30006175 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zaksauskas, A.'   1 ? 
primary 'Capkauskaite, E.' 2 ? 
primary 'Jezepcikas, L.'   3 ? 
primary 'Linkuviene, V.'   4 ? 
primary 'Kisonaite, M.'    5 ? 
primary 'Smirnov, A.'      6 ? 
primary 'Manakova, E.'     7 ? 
primary 'Grazulis, S.'     8 ? 
primary 'Matulis, D.'      9 ? 
# 
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    ?       ? 
'4-chloro-2-(cyclohexylamino)-N-(2-hydroxyethyl)-5-sulfamoyl-benzamide' ? 
3 non-polymer syn '4-chloranyl-2-(cyclohexylamino)-~{N}-(2-hydroxyethyl)-5-sulfamoyl-benzamide' 375.871   4    ?       ? Zn ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                                62.068    12   ?       ? 
1,2-ETHANEDIOL                                                          ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                       106.120   2    ?       ? ? ? 
6 water       nat water                                                                         18.015    1036 ?       ? ? ? 
# 
_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 '4-chloranyl-2-(cyclohexylamino)-~{N}-(2-hydroxyethyl)-5-sulfamoyl-benzamide' EM5 
4 1,2-ETHANEDIOL                                                                EDO 
5 'DI(HYDROXYETHYL)ETHER'                                                       PEG 
6 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 
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 
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  
EM5 non-polymer         . '4-chloranyl-2-(cyclohexylamino)-~{N}-(2-hydroxyethyl)-5-sulfamoyl-benzamide' ?                 
'C15 H22 Cl N3 O4 S' 375.871 
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   ?   ?   ?   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 EM5 1   302 1    EM5 EA7 A . 
G  4 EDO 1   303 1    EDO EDO A . 
H  5 PEG 1   304 15   PEG PEG A . 
I  4 EDO 1   305 16   EDO EDO A . 
J  2 ZN  1   301 2    ZN  ZN  B . 
K  3 EM5 1   302 2    EM5 EA7 B . 
L  4 EDO 1   303 3    EDO EDO B . 
M  4 EDO 1   304 4    EDO EDO B . 
N  4 EDO 1   305 5    EDO EDO B . 
O  4 EDO 1   306 14   EDO EDO B . 
P  2 ZN  1   301 3    ZN  ZN  C . 
Q  3 EM5 1   302 3    EM5 EA7 C . 
R  4 EDO 1   303 6    EDO EDO C . 
S  2 ZN  1   301 4    ZN  ZN  D . 
T  3 EM5 1   302 4    EM5 EA7 D . 
U  4 EDO 1   303 7    EDO EDO D . 
V  4 EDO 1   304 8    EDO EDO D . 
W  4 EDO 1   305 10   EDO EDO D . 
X  4 EDO 1   306 11   EDO EDO D . 
Y  5 PEG 1   307 12   PEG PEG D . 
Z  4 EDO 1   308 13   EDO EDO D . 
AA 6 HOH 1   401 449  HOH HOH A . 
AA 6 HOH 2   402 693  HOH HOH A . 
AA 6 HOH 3   403 600  HOH HOH A . 
AA 6 HOH 4   404 624  HOH HOH A . 
AA 6 HOH 5   405 492  HOH HOH A . 
AA 6 HOH 6   406 1018 HOH HOH A . 
AA 6 HOH 7   407 656  HOH HOH A . 
AA 6 HOH 8   408 694  HOH HOH A . 
AA 6 HOH 9   409 691  HOH HOH A . 
AA 6 HOH 10  410 601  HOH HOH A . 
AA 6 HOH 11  411 692  HOH HOH A . 
AA 6 HOH 12  412 399  HOH HOH A . 
AA 6 HOH 13  413 218  HOH HOH A . 
AA 6 HOH 14  414 482  HOH HOH A . 
AA 6 HOH 15  415 373  HOH HOH A . 
AA 6 HOH 16  416 13   HOH HOH A . 
AA 6 HOH 17  417 587  HOH HOH A . 
AA 6 HOH 18  418 983  HOH HOH A . 
AA 6 HOH 19  419 545  HOH HOH A . 
AA 6 HOH 20  420 657  HOH HOH A . 
AA 6 HOH 21  421 439  HOH HOH A . 
AA 6 HOH 22  422 226  HOH HOH A . 
AA 6 HOH 23  423 400  HOH HOH A . 
AA 6 HOH 24  424 720  HOH HOH A . 
AA 6 HOH 25  425 979  HOH HOH A . 
AA 6 HOH 26  426 318  HOH HOH A . 
AA 6 HOH 27  427 322  HOH HOH A . 
AA 6 HOH 28  428 715  HOH HOH A . 
AA 6 HOH 29  429 443  HOH HOH A . 
AA 6 HOH 30  430 199  HOH HOH A . 
AA 6 HOH 31  431 336  HOH HOH A . 
AA 6 HOH 32  432 541  HOH HOH A . 
AA 6 HOH 33  433 211  HOH HOH A . 
AA 6 HOH 34  434 716  HOH HOH A . 
AA 6 HOH 35  435 111  HOH HOH A . 
AA 6 HOH 36  436 730  HOH HOH A . 
AA 6 HOH 37  437 293  HOH HOH A . 
AA 6 HOH 38  438 409  HOH HOH A . 
AA 6 HOH 39  439 53   HOH HOH A . 
AA 6 HOH 40  440 8    HOH HOH A . 
AA 6 HOH 41  441 243  HOH HOH A . 
AA 6 HOH 42  442 26   HOH HOH A . 
AA 6 HOH 43  443 729  HOH HOH A . 
AA 6 HOH 44  444 707  HOH HOH A . 
AA 6 HOH 45  445 980  HOH HOH A . 
AA 6 HOH 46  446 500  HOH HOH A . 
AA 6 HOH 47  447 705  HOH HOH A . 
AA 6 HOH 48  448 284  HOH HOH A . 
AA 6 HOH 49  449 102  HOH HOH A . 
AA 6 HOH 50  450 74   HOH HOH A . 
AA 6 HOH 51  451 258  HOH HOH A . 
AA 6 HOH 52  452 4    HOH HOH A . 
AA 6 HOH 53  453 29   HOH HOH A . 
AA 6 HOH 54  454 331  HOH HOH A . 
AA 6 HOH 55  455 718  HOH HOH A . 
AA 6 HOH 56  456 125  HOH HOH A . 
AA 6 HOH 57  457 563  HOH HOH A . 
AA 6 HOH 58  458 613  HOH HOH A . 
AA 6 HOH 59  459 557  HOH HOH A . 
AA 6 HOH 60  460 539  HOH HOH A . 
AA 6 HOH 61  461 676  HOH HOH A . 
AA 6 HOH 62  462 276  HOH HOH A . 
AA 6 HOH 63  463 5    HOH HOH A . 
AA 6 HOH 64  464 825  HOH HOH A . 
AA 6 HOH 65  465 217  HOH HOH A . 
AA 6 HOH 66  466 47   HOH HOH A . 
AA 6 HOH 67  467 183  HOH HOH A . 
AA 6 HOH 68  468 464  HOH HOH A . 
AA 6 HOH 69  469 46   HOH HOH A . 
AA 6 HOH 70  470 480  HOH HOH A . 
AA 6 HOH 71  471 260  HOH HOH A . 
AA 6 HOH 72  472 289  HOH HOH A . 
AA 6 HOH 73  473 229  HOH HOH A . 
AA 6 HOH 74  474 728  HOH HOH A . 
AA 6 HOH 75  475 132  HOH HOH A . 
AA 6 HOH 76  476 130  HOH HOH A . 
AA 6 HOH 77  477 709  HOH HOH A . 
AA 6 HOH 78  478 445  HOH HOH A . 
AA 6 HOH 79  479 245  HOH HOH A . 
AA 6 HOH 80  480 69   HOH HOH A . 
AA 6 HOH 81  481 138  HOH HOH A . 
AA 6 HOH 82  482 249  HOH HOH A . 
AA 6 HOH 83  483 57   HOH HOH A . 
AA 6 HOH 84  484 410  HOH HOH A . 
AA 6 HOH 85  485 168  HOH HOH A . 
AA 6 HOH 86  486 153  HOH HOH A . 
AA 6 HOH 87  487 116  HOH HOH A . 
AA 6 HOH 88  488 420  HOH HOH A . 
AA 6 HOH 89  489 509  HOH HOH A . 
AA 6 HOH 90  490 10   HOH HOH A . 
AA 6 HOH 91  491 833  HOH HOH A . 
AA 6 HOH 92  492 633  HOH HOH A . 
AA 6 HOH 93  493 835  HOH HOH A . 
AA 6 HOH 94  494 14   HOH HOH A . 
AA 6 HOH 95  495 37   HOH HOH A . 
AA 6 HOH 96  496 334  HOH HOH A . 
AA 6 HOH 97  497 122  HOH HOH A . 
AA 6 HOH 98  498 826  HOH HOH A . 
AA 6 HOH 99  499 333  HOH HOH A . 
AA 6 HOH 100 500 394  HOH HOH A . 
AA 6 HOH 101 501 158  HOH HOH A . 
AA 6 HOH 102 502 176  HOH HOH A . 
AA 6 HOH 103 503 679  HOH HOH A . 
AA 6 HOH 104 504 78   HOH HOH A . 
AA 6 HOH 105 505 447  HOH HOH A . 
AA 6 HOH 106 506 114  HOH HOH A . 
AA 6 HOH 107 507 233  HOH HOH A . 
AA 6 HOH 108 508 725  HOH HOH A . 
AA 6 HOH 109 509 43   HOH HOH A . 
AA 6 HOH 110 510 126  HOH HOH A . 
AA 6 HOH 111 511 610  HOH HOH A . 
AA 6 HOH 112 512 227  HOH HOH A . 
AA 6 HOH 113 513 350  HOH HOH A . 
AA 6 HOH 114 514 377  HOH HOH A . 
AA 6 HOH 115 515 440  HOH HOH A . 
AA 6 HOH 116 516 431  HOH HOH A . 
AA 6 HOH 117 517 173  HOH HOH A . 
AA 6 HOH 118 518 673  HOH HOH A . 
AA 6 HOH 119 519 93   HOH HOH A . 
AA 6 HOH 120 520 435  HOH HOH A . 
AA 6 HOH 121 521 485  HOH HOH A . 
AA 6 HOH 122 522 302  HOH HOH A . 
AA 6 HOH 123 523 466  HOH HOH A . 
AA 6 HOH 124 524 361  HOH HOH A . 
AA 6 HOH 125 525 501  HOH HOH A . 
AA 6 HOH 126 526 688  HOH HOH A . 
AA 6 HOH 127 527 27   HOH HOH A . 
AA 6 HOH 128 528 1024 HOH HOH A . 
AA 6 HOH 129 529 255  HOH HOH A . 
AA 6 HOH 130 530 256  HOH HOH A . 
AA 6 HOH 131 531 71   HOH HOH A . 
AA 6 HOH 132 532 824  HOH HOH A . 
AA 6 HOH 133 533 128  HOH HOH A . 
AA 6 HOH 134 534 1021 HOH HOH A . 
AA 6 HOH 135 535 366  HOH HOH A . 
AA 6 HOH 136 536 188  HOH HOH A . 
AA 6 HOH 137 537 831  HOH HOH A . 
AA 6 HOH 138 538 812  HOH HOH A . 
AA 6 HOH 139 539 303  HOH HOH A . 
AA 6 HOH 140 540 162  HOH HOH A . 
AA 6 HOH 141 541 593  HOH HOH A . 
AA 6 HOH 142 542 144  HOH HOH A . 
AA 6 HOH 143 543 191  HOH HOH A . 
AA 6 HOH 144 544 127  HOH HOH A . 
AA 6 HOH 145 545 52   HOH HOH A . 
AA 6 HOH 146 546 568  HOH HOH A . 
AA 6 HOH 147 547 818  HOH HOH A . 
AA 6 HOH 148 548 658  HOH HOH A . 
AA 6 HOH 149 549 567  HOH HOH A . 
AA 6 HOH 150 550 388  HOH HOH A . 
AA 6 HOH 151 551 220  HOH HOH A . 
AA 6 HOH 152 552 829  HOH HOH A . 
AA 6 HOH 153 553 215  HOH HOH A . 
AA 6 HOH 154 554 723  HOH HOH A . 
AA 6 HOH 155 555 660  HOH HOH A . 
AA 6 HOH 156 556 495  HOH HOH A . 
AA 6 HOH 157 557 666  HOH HOH A . 
AA 6 HOH 158 558 263  HOH HOH A . 
AA 6 HOH 159 559 683  HOH HOH A . 
AA 6 HOH 160 560 680  HOH HOH A . 
AA 6 HOH 161 561 295  HOH HOH A . 
AA 6 HOH 162 562 381  HOH HOH A . 
AA 6 HOH 163 563 320  HOH HOH A . 
AA 6 HOH 164 564 990  HOH HOH A . 
AA 6 HOH 165 565 985  HOH HOH A . 
AA 6 HOH 166 566 714  HOH HOH A . 
AA 6 HOH 167 567 296  HOH HOH A . 
AA 6 HOH 168 568 95   HOH HOH A . 
AA 6 HOH 169 569 142  HOH HOH A . 
AA 6 HOH 170 570 9    HOH HOH A . 
AA 6 HOH 171 571 552  HOH HOH A . 
AA 6 HOH 172 572 682  HOH HOH A . 
AA 6 HOH 173 573 209  HOH HOH A . 
AA 6 HOH 174 574 584  HOH HOH A . 
AA 6 HOH 175 575 827  HOH HOH A . 
AA 6 HOH 176 576 690  HOH HOH A . 
AA 6 HOH 177 577 267  HOH HOH A . 
AA 6 HOH 178 578 221  HOH HOH A . 
AA 6 HOH 179 579 702  HOH HOH A . 
AA 6 HOH 180 580 92   HOH HOH A . 
AA 6 HOH 181 581 706  HOH HOH A . 
AA 6 HOH 182 582 291  HOH HOH A . 
AA 6 HOH 183 583 488  HOH HOH A . 
AA 6 HOH 184 584 165  HOH HOH A . 
AA 6 HOH 185 585 340  HOH HOH A . 
AA 6 HOH 186 586 432  HOH HOH A . 
AA 6 HOH 187 587 364  HOH HOH A . 
AA 6 HOH 188 588 975  HOH HOH A . 
AA 6 HOH 189 589 174  HOH HOH A . 
AA 6 HOH 190 590 586  HOH HOH A . 
AA 6 HOH 191 591 1023 HOH HOH A . 
AA 6 HOH 192 592 544  HOH HOH A . 
AA 6 HOH 193 593 727  HOH HOH A . 
AA 6 HOH 194 594 106  HOH HOH A . 
AA 6 HOH 195 595 721  HOH HOH A . 
AA 6 HOH 196 596 602  HOH HOH A . 
AA 6 HOH 197 597 437  HOH HOH A . 
AA 6 HOH 198 598 1025 HOH HOH A . 
AA 6 HOH 199 599 592  HOH HOH A . 
AA 6 HOH 200 600 254  HOH HOH A . 
AA 6 HOH 201 601 686  HOH HOH A . 
AA 6 HOH 202 602 324  HOH HOH A . 
AA 6 HOH 203 603 250  HOH HOH A . 
AA 6 HOH 204 604 184  HOH HOH A . 
AA 6 HOH 205 605 698  HOH HOH A . 
AA 6 HOH 206 606 977  HOH HOH A . 
AA 6 HOH 207 607 434  HOH HOH A . 
AA 6 HOH 208 608 976  HOH HOH A . 
AA 6 HOH 209 609 577  HOH HOH A . 
AA 6 HOH 210 610 413  HOH HOH A . 
AA 6 HOH 211 611 704  HOH HOH A . 
AA 6 HOH 212 612 817  HOH HOH A . 
AA 6 HOH 213 613 689  HOH HOH A . 
AA 6 HOH 214 614 379  HOH HOH A . 
AA 6 HOH 215 615 834  HOH HOH A . 
AA 6 HOH 216 616 988  HOH HOH A . 
AA 6 HOH 217 617 713  HOH HOH A . 
AA 6 HOH 218 618 708  HOH HOH A . 
AA 6 HOH 219 619 819  HOH HOH A . 
AA 6 HOH 220 620 832  HOH HOH A . 
AA 6 HOH 221 621 671  HOH HOH A . 
AA 6 HOH 222 622 687  HOH HOH A . 
AA 6 HOH 223 623 452  HOH HOH A . 
AA 6 HOH 224 624 646  HOH HOH A . 
AA 6 HOH 225 625 987  HOH HOH A . 
AA 6 HOH 226 626 543  HOH HOH A . 
AA 6 HOH 227 627 401  HOH HOH A . 
AA 6 HOH 228 628 189  HOH HOH A . 
AA 6 HOH 229 629 598  HOH HOH A . 
AA 6 HOH 230 630 674  HOH HOH A . 
AA 6 HOH 231 631 661  HOH HOH A . 
AA 6 HOH 232 632 1019 HOH HOH A . 
AA 6 HOH 233 633 697  HOH HOH A . 
AA 6 HOH 234 634 986  HOH HOH A . 
AA 6 HOH 235 635 830  HOH HOH A . 
AA 6 HOH 236 636 665  HOH HOH A . 
AA 6 HOH 237 637 550  HOH HOH A . 
AA 6 HOH 238 638 534  HOH HOH A . 
AA 6 HOH 239 639 695  HOH HOH A . 
AA 6 HOH 240 640 685  HOH HOH A . 
AA 6 HOH 241 641 700  HOH HOH A . 
AA 6 HOH 242 642 386  HOH HOH A . 
AA 6 HOH 243 643 717  HOH HOH A . 
AA 6 HOH 244 644 151  HOH HOH A . 
AA 6 HOH 245 645 974  HOH HOH A . 
AA 6 HOH 246 646 719  HOH HOH A . 
AA 6 HOH 247 647 973  HOH HOH A . 
AA 6 HOH 248 648 726  HOH HOH A . 
AA 6 HOH 249 649 1026 HOH HOH A . 
AA 6 HOH 250 650 681  HOH HOH A . 
AA 6 HOH 251 651 396  HOH HOH A . 
AA 6 HOH 252 652 616  HOH HOH A . 
AA 6 HOH 253 653 981  HOH HOH A . 
AA 6 HOH 254 654 989  HOH HOH A . 
AA 6 HOH 255 655 677  HOH HOH A . 
AA 6 HOH 256 656 724  HOH HOH A . 
AA 6 HOH 257 657 970  HOH HOH A . 
AA 6 HOH 258 658 651  HOH HOH A . 
AA 6 HOH 259 659 722  HOH HOH A . 
AA 6 HOH 260 660 828  HOH HOH A . 
AA 6 HOH 261 661 1027 HOH HOH A . 
AA 6 HOH 262 662 648  HOH HOH A . 
AA 6 HOH 263 663 711  HOH HOH A . 
AA 6 HOH 264 664 672  HOH HOH A . 
AA 6 HOH 265 665 647  HOH HOH A . 
AA 6 HOH 266 666 675  HOH HOH A . 
AA 6 HOH 267 667 72   HOH HOH A . 
AA 6 HOH 268 668 712  HOH HOH A . 
AA 6 HOH 269 669 1029 HOH HOH A . 
AA 6 HOH 270 670 476  HOH HOH A . 
AA 6 HOH 271 671 982  HOH HOH A . 
AA 6 HOH 272 672 382  HOH HOH A . 
AA 6 HOH 273 673 641  HOH HOH A . 
AA 6 HOH 274 674 823  HOH HOH A . 
AA 6 HOH 275 675 984  HOH HOH A . 
AA 6 HOH 276 676 678  HOH HOH A . 
AA 6 HOH 277 677 670  HOH HOH A . 
AA 6 HOH 278 678 360  HOH HOH A . 
AA 6 HOH 279 679 710  HOH HOH A . 
AA 6 HOH 280 680 821  HOH HOH A . 
AA 6 HOH 281 681 971  HOH HOH A . 
AA 6 HOH 282 682 684  HOH HOH A . 
AA 6 HOH 283 683 699  HOH HOH A . 
AA 6 HOH 284 684 418  HOH HOH A . 
BA 6 HOH 1   401 663  HOH HOH B . 
BA 6 HOH 2   402 820  HOH HOH B . 
BA 6 HOH 3   403 880  HOH HOH B . 
BA 6 HOH 4   404 308  HOH HOH B . 
BA 6 HOH 5   405 1003 HOH HOH B . 
BA 6 HOH 6   406 883  HOH HOH B . 
BA 6 HOH 7   407 542  HOH HOH B . 
BA 6 HOH 8   408 422  HOH HOH B . 
BA 6 HOH 9   409 839  HOH HOH B . 
BA 6 HOH 10  410 852  HOH HOH B . 
BA 6 HOH 11  411 618  HOH HOH B . 
BA 6 HOH 12  412 457  HOH HOH B . 
BA 6 HOH 13  413 643  HOH HOH B . 
BA 6 HOH 14  414 244  HOH HOH B . 
BA 6 HOH 15  415 537  HOH HOH B . 
BA 6 HOH 16  416 856  HOH HOH B . 
BA 6 HOH 17  417 23   HOH HOH B . 
BA 6 HOH 18  418 627  HOH HOH B . 
BA 6 HOH 19  419 737  HOH HOH B . 
BA 6 HOH 20  420 579  HOH HOH B . 
BA 6 HOH 21  421 871  HOH HOH B . 
BA 6 HOH 22  422 305  HOH HOH B . 
BA 6 HOH 23  423 369  HOH HOH B . 
BA 6 HOH 24  424 143  HOH HOH B . 
BA 6 HOH 25  425 1030 HOH HOH B . 
BA 6 HOH 26  426 323  HOH HOH B . 
BA 6 HOH 27  427 280  HOH HOH B . 
BA 6 HOH 28  428 731  HOH HOH B . 
BA 6 HOH 29  429 978  HOH HOH B . 
BA 6 HOH 30  430 119  HOH HOH B . 
BA 6 HOH 31  431 113  HOH HOH B . 
BA 6 HOH 32  432 25   HOH HOH B . 
BA 6 HOH 33  433 999  HOH HOH B . 
BA 6 HOH 34  434 608  HOH HOH B . 
BA 6 HOH 35  435 866  HOH HOH B . 
BA 6 HOH 36  436 90   HOH HOH B . 
BA 6 HOH 37  437 572  HOH HOH B . 
BA 6 HOH 38  438 847  HOH HOH B . 
BA 6 HOH 39  439 842  HOH HOH B . 
BA 6 HOH 40  440 319  HOH HOH B . 
BA 6 HOH 41  441 991  HOH HOH B . 
BA 6 HOH 42  442 85   HOH HOH B . 
BA 6 HOH 43  443 515  HOH HOH B . 
BA 6 HOH 44  444 659  HOH HOH B . 
BA 6 HOH 45  445 316  HOH HOH B . 
BA 6 HOH 46  446 390  HOH HOH B . 
BA 6 HOH 47  447 996  HOH HOH B . 
BA 6 HOH 48  448 164  HOH HOH B . 
BA 6 HOH 49  449 19   HOH HOH B . 
BA 6 HOH 50  450 80   HOH HOH B . 
BA 6 HOH 51  451 473  HOH HOH B . 
BA 6 HOH 52  452 391  HOH HOH B . 
BA 6 HOH 53  453 491  HOH HOH B . 
BA 6 HOH 54  454 664  HOH HOH B . 
BA 6 HOH 55  455 612  HOH HOH B . 
BA 6 HOH 56  456 155  HOH HOH B . 
BA 6 HOH 57  457 246  HOH HOH B . 
BA 6 HOH 58  458 380  HOH HOH B . 
BA 6 HOH 59  459 137  HOH HOH B . 
BA 6 HOH 60  460 99   HOH HOH B . 
BA 6 HOH 61  461 419  HOH HOH B . 
BA 6 HOH 62  462 527  HOH HOH B . 
BA 6 HOH 63  463 1020 HOH HOH B . 
BA 6 HOH 64  464 335  HOH HOH B . 
BA 6 HOH 65  465 629  HOH HOH B . 
BA 6 HOH 66  466 248  HOH HOH B . 
BA 6 HOH 67  467 169  HOH HOH B . 
BA 6 HOH 68  468 875  HOH HOH B . 
BA 6 HOH 69  469 112  HOH HOH B . 
BA 6 HOH 70  470 84   HOH HOH B . 
BA 6 HOH 71  471 662  HOH HOH B . 
BA 6 HOH 72  472 61   HOH HOH B . 
BA 6 HOH 73  473 359  HOH HOH B . 
BA 6 HOH 74  474 205  HOH HOH B . 
BA 6 HOH 75  475 311  HOH HOH B . 
BA 6 HOH 76  476 68   HOH HOH B . 
BA 6 HOH 77  477 442  HOH HOH B . 
BA 6 HOH 78  478 203  HOH HOH B . 
BA 6 HOH 79  479 754  HOH HOH B . 
BA 6 HOH 80  480 105  HOH HOH B . 
BA 6 HOH 81  481 148  HOH HOH B . 
BA 6 HOH 82  482 742  HOH HOH B . 
BA 6 HOH 83  483 49   HOH HOH B . 
BA 6 HOH 84  484 855  HOH HOH B . 
BA 6 HOH 85  485 238  HOH HOH B . 
BA 6 HOH 86  486 115  HOH HOH B . 
BA 6 HOH 87  487 581  HOH HOH B . 
BA 6 HOH 88  488 351  HOH HOH B . 
BA 6 HOH 89  489 995  HOH HOH B . 
BA 6 HOH 90  490 357  HOH HOH B . 
BA 6 HOH 91  491 393  HOH HOH B . 
BA 6 HOH 92  492 70   HOH HOH B . 
BA 6 HOH 93  493 287  HOH HOH B . 
BA 6 HOH 94  494 56   HOH HOH B . 
BA 6 HOH 95  495 881  HOH HOH B . 
BA 6 HOH 96  496 161  HOH HOH B . 
BA 6 HOH 97  497 338  HOH HOH B . 
BA 6 HOH 98  498 1001 HOH HOH B . 
BA 6 HOH 99  499 521  HOH HOH B . 
BA 6 HOH 100 500 524  HOH HOH B . 
BA 6 HOH 101 501 149  HOH HOH B . 
BA 6 HOH 102 502 75   HOH HOH B . 
BA 6 HOH 103 503 456  HOH HOH B . 
BA 6 HOH 104 504 858  HOH HOH B . 
BA 6 HOH 105 505 837  HOH HOH B . 
BA 6 HOH 106 506 66   HOH HOH B . 
BA 6 HOH 107 507 36   HOH HOH B . 
BA 6 HOH 108 508 632  HOH HOH B . 
BA 6 HOH 109 509 15   HOH HOH B . 
BA 6 HOH 110 510 301  HOH HOH B . 
BA 6 HOH 111 511 867  HOH HOH B . 
BA 6 HOH 112 512 450  HOH HOH B . 
BA 6 HOH 113 513 185  HOH HOH B . 
BA 6 HOH 114 514 264  HOH HOH B . 
BA 6 HOH 115 515 860  HOH HOH B . 
BA 6 HOH 116 516 76   HOH HOH B . 
BA 6 HOH 117 517 64   HOH HOH B . 
BA 6 HOH 118 518 207  HOH HOH B . 
BA 6 HOH 119 519 800  HOH HOH B . 
BA 6 HOH 120 520 703  HOH HOH B . 
BA 6 HOH 121 521 884  HOH HOH B . 
BA 6 HOH 122 522 749  HOH HOH B . 
BA 6 HOH 123 523 180  HOH HOH B . 
BA 6 HOH 124 524 414  HOH HOH B . 
BA 6 HOH 125 525 585  HOH HOH B . 
BA 6 HOH 126 526 607  HOH HOH B . 
BA 6 HOH 127 527 278  HOH HOH B . 
BA 6 HOH 128 528 167  HOH HOH B . 
BA 6 HOH 129 529 182  HOH HOH B . 
BA 6 HOH 130 530 408  HOH HOH B . 
BA 6 HOH 131 531 514  HOH HOH B . 
BA 6 HOH 132 532 156  HOH HOH B . 
BA 6 HOH 133 533 582  HOH HOH B . 
BA 6 HOH 134 534 110  HOH HOH B . 
BA 6 HOH 135 535 857  HOH HOH B . 
BA 6 HOH 136 536 348  HOH HOH B . 
BA 6 HOH 137 537 96   HOH HOH B . 
BA 6 HOH 138 538 868  HOH HOH B . 
BA 6 HOH 139 539 370  HOH HOH B . 
BA 6 HOH 140 540 196  HOH HOH B . 
BA 6 HOH 141 541 402  HOH HOH B . 
BA 6 HOH 142 542 739  HOH HOH B . 
BA 6 HOH 143 543 347  HOH HOH B . 
BA 6 HOH 144 544 175  HOH HOH B . 
BA 6 HOH 145 545 735  HOH HOH B . 
BA 6 HOH 146 546 32   HOH HOH B . 
BA 6 HOH 147 547 292  HOH HOH B . 
BA 6 HOH 148 548 1000 HOH HOH B . 
BA 6 HOH 149 549 865  HOH HOH B . 
BA 6 HOH 150 550 876  HOH HOH B . 
BA 6 HOH 151 551 626  HOH HOH B . 
BA 6 HOH 152 552 67   HOH HOH B . 
BA 6 HOH 153 553 732  HOH HOH B . 
BA 6 HOH 154 554 55   HOH HOH B . 
BA 6 HOH 155 555 330  HOH HOH B . 
BA 6 HOH 156 556 97   HOH HOH B . 
BA 6 HOH 157 557 2    HOH HOH B . 
BA 6 HOH 158 558 536  HOH HOH B . 
BA 6 HOH 159 559 411  HOH HOH B . 
BA 6 HOH 160 560 363  HOH HOH B . 
BA 6 HOH 161 561 327  HOH HOH B . 
BA 6 HOH 162 562 734  HOH HOH B . 
BA 6 HOH 163 563 755  HOH HOH B . 
BA 6 HOH 164 564 193  HOH HOH B . 
BA 6 HOH 165 565 208  HOH HOH B . 
BA 6 HOH 166 566 740  HOH HOH B . 
BA 6 HOH 167 567 223  HOH HOH B . 
BA 6 HOH 168 568 733  HOH HOH B . 
BA 6 HOH 169 569 969  HOH HOH B . 
BA 6 HOH 170 570 50   HOH HOH B . 
BA 6 HOH 171 571 60   HOH HOH B . 
BA 6 HOH 172 572 1    HOH HOH B . 
BA 6 HOH 173 573 117  HOH HOH B . 
BA 6 HOH 174 574 752  HOH HOH B . 
BA 6 HOH 175 575 154  HOH HOH B . 
BA 6 HOH 176 576 516  HOH HOH B . 
BA 6 HOH 177 577 478  HOH HOH B . 
BA 6 HOH 178 578 748  HOH HOH B . 
BA 6 HOH 179 579 54   HOH HOH B . 
BA 6 HOH 180 580 186  HOH HOH B . 
BA 6 HOH 181 581 163  HOH HOH B . 
BA 6 HOH 182 582 235  HOH HOH B . 
BA 6 HOH 183 583 531  HOH HOH B . 
BA 6 HOH 184 584 870  HOH HOH B . 
BA 6 HOH 185 585 864  HOH HOH B . 
BA 6 HOH 186 586 998  HOH HOH B . 
BA 6 HOH 187 587 667  HOH HOH B . 
BA 6 HOH 188 588 853  HOH HOH B . 
BA 6 HOH 189 589 701  HOH HOH B . 
BA 6 HOH 190 590 475  HOH HOH B . 
BA 6 HOH 191 591 201  HOH HOH B . 
BA 6 HOH 192 592 588  HOH HOH B . 
BA 6 HOH 193 593 738  HOH HOH B . 
BA 6 HOH 194 594 159  HOH HOH B . 
BA 6 HOH 195 595 477  HOH HOH B . 
BA 6 HOH 196 596 617  HOH HOH B . 
BA 6 HOH 197 597 843  HOH HOH B . 
BA 6 HOH 198 598 253  HOH HOH B . 
BA 6 HOH 199 599 874  HOH HOH B . 
BA 6 HOH 200 600 341  HOH HOH B . 
BA 6 HOH 201 601 878  HOH HOH B . 
BA 6 HOH 202 602 838  HOH HOH B . 
BA 6 HOH 203 603 753  HOH HOH B . 
BA 6 HOH 204 604 862  HOH HOH B . 
BA 6 HOH 205 605 836  HOH HOH B . 
BA 6 HOH 206 606 997  HOH HOH B . 
BA 6 HOH 207 607 747  HOH HOH B . 
BA 6 HOH 208 608 636  HOH HOH B . 
BA 6 HOH 209 609 436  HOH HOH B . 
BA 6 HOH 210 610 741  HOH HOH B . 
BA 6 HOH 211 611 746  HOH HOH B . 
BA 6 HOH 212 612 850  HOH HOH B . 
BA 6 HOH 213 613 535  HOH HOH B . 
BA 6 HOH 214 614 549  HOH HOH B . 
BA 6 HOH 215 615 743  HOH HOH B . 
BA 6 HOH 216 616 469  HOH HOH B . 
BA 6 HOH 217 617 993  HOH HOH B . 
BA 6 HOH 218 618 424  HOH HOH B . 
BA 6 HOH 219 619 846  HOH HOH B . 
BA 6 HOH 220 620 849  HOH HOH B . 
BA 6 HOH 221 621 994  HOH HOH B . 
BA 6 HOH 222 622 751  HOH HOH B . 
BA 6 HOH 223 623 512  HOH HOH B . 
BA 6 HOH 224 624 869  HOH HOH B . 
BA 6 HOH 225 625 438  HOH HOH B . 
BA 6 HOH 226 626 872  HOH HOH B . 
BA 6 HOH 227 627 637  HOH HOH B . 
BA 6 HOH 228 628 840  HOH HOH B . 
BA 6 HOH 229 629 532  HOH HOH B . 
BA 6 HOH 230 630 668  HOH HOH B . 
BA 6 HOH 231 631 854  HOH HOH B . 
BA 6 HOH 232 632 479  HOH HOH B . 
BA 6 HOH 233 633 371  HOH HOH B . 
BA 6 HOH 234 634 82   HOH HOH B . 
BA 6 HOH 235 635 744  HOH HOH B . 
BA 6 HOH 236 636 195  HOH HOH B . 
BA 6 HOH 237 637 387  HOH HOH B . 
BA 6 HOH 238 638 506  HOH HOH B . 
BA 6 HOH 239 639 591  HOH HOH B . 
BA 6 HOH 240 640 845  HOH HOH B . 
BA 6 HOH 241 641 873  HOH HOH B . 
BA 6 HOH 242 642 848  HOH HOH B . 
BA 6 HOH 243 643 346  HOH HOH B . 
BA 6 HOH 244 644 306  HOH HOH B . 
BA 6 HOH 245 645 822  HOH HOH B . 
BA 6 HOH 246 646 558  HOH HOH B . 
BA 6 HOH 247 647 395  HOH HOH B . 
BA 6 HOH 248 648 841  HOH HOH B . 
BA 6 HOH 249 649 234  HOH HOH B . 
BA 6 HOH 250 650 1031 HOH HOH B . 
BA 6 HOH 251 651 877  HOH HOH B . 
BA 6 HOH 252 652 571  HOH HOH B . 
BA 6 HOH 253 653 124  HOH HOH B . 
BA 6 HOH 254 654 355  HOH HOH B . 
BA 6 HOH 255 655 745  HOH HOH B . 
BA 6 HOH 256 656 863  HOH HOH B . 
BA 6 HOH 257 657 566  HOH HOH B . 
BA 6 HOH 258 658 546  HOH HOH B . 
BA 6 HOH 259 659 325  HOH HOH B . 
BA 6 HOH 260 660 882  HOH HOH B . 
BA 6 HOH 261 661 655  HOH HOH B . 
BA 6 HOH 262 662 750  HOH HOH B . 
BA 6 HOH 263 663 736  HOH HOH B . 
BA 6 HOH 264 664 528  HOH HOH B . 
BA 6 HOH 265 665 428  HOH HOH B . 
BA 6 HOH 266 666 859  HOH HOH B . 
BA 6 HOH 267 667 861  HOH HOH B . 
BA 6 HOH 268 668 844  HOH HOH B . 
BA 6 HOH 269 669 580  HOH HOH B . 
BA 6 HOH 270 670 669  HOH HOH B . 
BA 6 HOH 271 671 342  HOH HOH B . 
BA 6 HOH 272 672 879  HOH HOH B . 
BA 6 HOH 273 673 367  HOH HOH B . 
BA 6 HOH 274 674 564  HOH HOH B . 
BA 6 HOH 275 675 992  HOH HOH B . 
BA 6 HOH 276 676 525  HOH HOH B . 
BA 6 HOH 277 677 851  HOH HOH B . 
BA 6 HOH 278 678 328  HOH HOH B . 
CA 6 HOH 1   401 530  HOH HOH C . 
CA 6 HOH 2   402 885  HOH HOH C . 
CA 6 HOH 3   403 892  HOH HOH C . 
CA 6 HOH 4   404 157  HOH HOH C . 
CA 6 HOH 5   405 639  HOH HOH C . 
CA 6 HOH 6   406 888  HOH HOH C . 
CA 6 HOH 7   407 384  HOH HOH C . 
CA 6 HOH 8   408 789  HOH HOH C . 
CA 6 HOH 9   409 777  HOH HOH C . 
CA 6 HOH 10  410 540  HOH HOH C . 
CA 6 HOH 11  411 63   HOH HOH C . 
CA 6 HOH 12  412 604  HOH HOH C . 
CA 6 HOH 13  413 309  HOH HOH C . 
CA 6 HOH 14  414 62   HOH HOH C . 
CA 6 HOH 15  415 769  HOH HOH C . 
CA 6 HOH 16  416 561  HOH HOH C . 
CA 6 HOH 17  417 231  HOH HOH C . 
CA 6 HOH 18  418 526  HOH HOH C . 
CA 6 HOH 19  419 470  HOH HOH C . 
CA 6 HOH 20  420 108  HOH HOH C . 
CA 6 HOH 21  421 907  HOH HOH C . 
CA 6 HOH 22  422 788  HOH HOH C . 
CA 6 HOH 23  423 372  HOH HOH C . 
CA 6 HOH 24  424 496  HOH HOH C . 
CA 6 HOH 25  425 179  HOH HOH C . 
CA 6 HOH 26  426 556  HOH HOH C . 
CA 6 HOH 27  427 778  HOH HOH C . 
CA 6 HOH 28  428 283  HOH HOH C . 
CA 6 HOH 29  429 426  HOH HOH C . 
CA 6 HOH 30  430 31   HOH HOH C . 
CA 6 HOH 31  431 696  HOH HOH C . 
CA 6 HOH 32  432 890  HOH HOH C . 
CA 6 HOH 33  433 222  HOH HOH C . 
CA 6 HOH 34  434 638  HOH HOH C . 
CA 6 HOH 35  435 265  HOH HOH C . 
CA 6 HOH 36  436 59   HOH HOH C . 
CA 6 HOH 37  437 266  HOH HOH C . 
CA 6 HOH 38  438 415  HOH HOH C . 
CA 6 HOH 39  439 389  HOH HOH C . 
CA 6 HOH 40  440 89   HOH HOH C . 
CA 6 HOH 41  441 597  HOH HOH C . 
CA 6 HOH 42  442 22   HOH HOH C . 
CA 6 HOH 43  443 772  HOH HOH C . 
CA 6 HOH 44  444 757  HOH HOH C . 
CA 6 HOH 45  445 619  HOH HOH C . 
CA 6 HOH 46  446 1009 HOH HOH C . 
CA 6 HOH 47  447 441  HOH HOH C . 
CA 6 HOH 48  448 197  HOH HOH C . 
CA 6 HOH 49  449 897  HOH HOH C . 
CA 6 HOH 50  450 313  HOH HOH C . 
CA 6 HOH 51  451 133  HOH HOH C . 
CA 6 HOH 52  452 555  HOH HOH C . 
CA 6 HOH 53  453 919  HOH HOH C . 
CA 6 HOH 54  454 326  HOH HOH C . 
CA 6 HOH 55  455 33   HOH HOH C . 
CA 6 HOH 56  456 6    HOH HOH C . 
CA 6 HOH 57  457 194  HOH HOH C . 
CA 6 HOH 58  458 378  HOH HOH C . 
CA 6 HOH 59  459 513  HOH HOH C . 
CA 6 HOH 60  460 455  HOH HOH C . 
CA 6 HOH 61  461 104  HOH HOH C . 
CA 6 HOH 62  462 190  HOH HOH C . 
CA 6 HOH 63  463 623  HOH HOH C . 
CA 6 HOH 64  464 38   HOH HOH C . 
CA 6 HOH 65  465 129  HOH HOH C . 
CA 6 HOH 66  466 83   HOH HOH C . 
CA 6 HOH 67  467 206  HOH HOH C . 
CA 6 HOH 68  468 352  HOH HOH C . 
CA 6 HOH 69  469 213  HOH HOH C . 
CA 6 HOH 70  470 926  HOH HOH C . 
CA 6 HOH 71  471 773  HOH HOH C . 
CA 6 HOH 72  472 631  HOH HOH C . 
CA 6 HOH 73  473 312  HOH HOH C . 
CA 6 HOH 74  474 781  HOH HOH C . 
CA 6 HOH 75  475 620  HOH HOH C . 
CA 6 HOH 76  476 523  HOH HOH C . 
CA 6 HOH 77  477 924  HOH HOH C . 
CA 6 HOH 78  478 285  HOH HOH C . 
CA 6 HOH 79  479 427  HOH HOH C . 
CA 6 HOH 80  480 590  HOH HOH C . 
CA 6 HOH 81  481 304  HOH HOH C . 
CA 6 HOH 82  482 589  HOH HOH C . 
CA 6 HOH 83  483 575  HOH HOH C . 
CA 6 HOH 84  484 172  HOH HOH C . 
CA 6 HOH 85  485 923  HOH HOH C . 
CA 6 HOH 86  486 297  HOH HOH C . 
CA 6 HOH 87  487 886  HOH HOH C . 
CA 6 HOH 88  488 187  HOH HOH C . 
CA 6 HOH 89  489 349  HOH HOH C . 
CA 6 HOH 90  490 783  HOH HOH C . 
CA 6 HOH 91  491 48   HOH HOH C . 
CA 6 HOH 92  492 786  HOH HOH C . 
CA 6 HOH 93  493 471  HOH HOH C . 
CA 6 HOH 94  494 505  HOH HOH C . 
CA 6 HOH 95  495 44   HOH HOH C . 
CA 6 HOH 96  496 547  HOH HOH C . 
CA 6 HOH 97  497 498  HOH HOH C . 
CA 6 HOH 98  498 225  HOH HOH C . 
CA 6 HOH 99  499 630  HOH HOH C . 
CA 6 HOH 100 500 247  HOH HOH C . 
CA 6 HOH 101 501 403  HOH HOH C . 
CA 6 HOH 102 502 339  HOH HOH C . 
CA 6 HOH 103 503 499  HOH HOH C . 
CA 6 HOH 104 504 465  HOH HOH C . 
CA 6 HOH 105 505 7    HOH HOH C . 
CA 6 HOH 106 506 87   HOH HOH C . 
CA 6 HOH 107 507 18   HOH HOH C . 
CA 6 HOH 108 508 421  HOH HOH C . 
CA 6 HOH 109 509 776  HOH HOH C . 
CA 6 HOH 110 510 317  HOH HOH C . 
CA 6 HOH 111 511 770  HOH HOH C . 
CA 6 HOH 112 512 784  HOH HOH C . 
CA 6 HOH 113 513 28   HOH HOH C . 
CA 6 HOH 114 514 928  HOH HOH C . 
CA 6 HOH 115 515 42   HOH HOH C . 
CA 6 HOH 116 516 145  HOH HOH C . 
CA 6 HOH 117 517 609  HOH HOH C . 
CA 6 HOH 118 518 484  HOH HOH C . 
CA 6 HOH 119 519 780  HOH HOH C . 
CA 6 HOH 120 520 123  HOH HOH C . 
CA 6 HOH 121 521 502  HOH HOH C . 
CA 6 HOH 122 522 813  HOH HOH C . 
CA 6 HOH 123 523 497  HOH HOH C . 
CA 6 HOH 124 524 931  HOH HOH C . 
CA 6 HOH 125 525 929  HOH HOH C . 
CA 6 HOH 126 526 98   HOH HOH C . 
CA 6 HOH 127 527 917  HOH HOH C . 
CA 6 HOH 128 528 135  HOH HOH C . 
CA 6 HOH 129 529 397  HOH HOH C . 
CA 6 HOH 130 530 887  HOH HOH C . 
CA 6 HOH 131 531 345  HOH HOH C . 
CA 6 HOH 132 532 1007 HOH HOH C . 
CA 6 HOH 133 533 177  HOH HOH C . 
CA 6 HOH 134 534 121  HOH HOH C . 
CA 6 HOH 135 535 368  HOH HOH C . 
CA 6 HOH 136 536 922  HOH HOH C . 
CA 6 HOH 137 537 277  HOH HOH C . 
CA 6 HOH 138 538 787  HOH HOH C . 
CA 6 HOH 139 539 212  HOH HOH C . 
CA 6 HOH 140 540 79   HOH HOH C . 
CA 6 HOH 141 541 559  HOH HOH C . 
CA 6 HOH 142 542 904  HOH HOH C . 
CA 6 HOH 143 543 899  HOH HOH C . 
CA 6 HOH 144 544 554  HOH HOH C . 
CA 6 HOH 145 545 39   HOH HOH C . 
CA 6 HOH 146 546 423  HOH HOH C . 
CA 6 HOH 147 547 930  HOH HOH C . 
CA 6 HOH 148 548 181  HOH HOH C . 
CA 6 HOH 149 549 489  HOH HOH C . 
CA 6 HOH 150 550 392  HOH HOH C . 
CA 6 HOH 151 551 459  HOH HOH C . 
CA 6 HOH 152 552 81   HOH HOH C . 
CA 6 HOH 153 553 298  HOH HOH C . 
CA 6 HOH 154 554 429  HOH HOH C . 
CA 6 HOH 155 555 1022 HOH HOH C . 
CA 6 HOH 156 556 551  HOH HOH C . 
CA 6 HOH 157 557 486  HOH HOH C . 
CA 6 HOH 158 558 1034 HOH HOH C . 
CA 6 HOH 159 559 310  HOH HOH C . 
CA 6 HOH 160 560 761  HOH HOH C . 
CA 6 HOH 161 561 909  HOH HOH C . 
CA 6 HOH 162 562 578  HOH HOH C . 
CA 6 HOH 163 563 913  HOH HOH C . 
CA 6 HOH 164 564 782  HOH HOH C . 
CA 6 HOH 165 565 271  HOH HOH C . 
CA 6 HOH 166 566 785  HOH HOH C . 
CA 6 HOH 167 567 481  HOH HOH C . 
CA 6 HOH 168 568 362  HOH HOH C . 
CA 6 HOH 169 569 548  HOH HOH C . 
CA 6 HOH 170 570 570  HOH HOH C . 
CA 6 HOH 171 571 756  HOH HOH C . 
CA 6 HOH 172 572 259  HOH HOH C . 
CA 6 HOH 173 573 915  HOH HOH C . 
CA 6 HOH 174 574 921  HOH HOH C . 
CA 6 HOH 175 575 433  HOH HOH C . 
CA 6 HOH 176 576 774  HOH HOH C . 
CA 6 HOH 177 577 906  HOH HOH C . 
CA 6 HOH 178 578 891  HOH HOH C . 
CA 6 HOH 179 579 908  HOH HOH C . 
CA 6 HOH 180 580 925  HOH HOH C . 
CA 6 HOH 181 581 483  HOH HOH C . 
CA 6 HOH 182 582 889  HOH HOH C . 
CA 6 HOH 183 583 1032 HOH HOH C . 
CA 6 HOH 184 584 444  HOH HOH C . 
CA 6 HOH 185 585 1011 HOH HOH C . 
CA 6 HOH 186 586 927  HOH HOH C . 
CA 6 HOH 187 587 775  HOH HOH C . 
CA 6 HOH 188 588 765  HOH HOH C . 
CA 6 HOH 189 589 759  HOH HOH C . 
CA 6 HOH 190 590 903  HOH HOH C . 
CA 6 HOH 191 591 507  HOH HOH C . 
CA 6 HOH 192 592 916  HOH HOH C . 
CA 6 HOH 193 593 918  HOH HOH C . 
CA 6 HOH 194 594 779  HOH HOH C . 
CA 6 HOH 195 595 764  HOH HOH C . 
CA 6 HOH 196 596 214  HOH HOH C . 
CA 6 HOH 197 597 273  HOH HOH C . 
CA 6 HOH 198 598 905  HOH HOH C . 
CA 6 HOH 199 599 622  HOH HOH C . 
CA 6 HOH 200 600 771  HOH HOH C . 
CA 6 HOH 201 601 1036 HOH HOH C . 
CA 6 HOH 202 602 1008 HOH HOH C . 
CA 6 HOH 203 603 1005 HOH HOH C . 
CA 6 HOH 204 604 649  HOH HOH C . 
CA 6 HOH 205 605 1010 HOH HOH C . 
CA 6 HOH 206 606 1006 HOH HOH C . 
CA 6 HOH 207 607 141  HOH HOH C . 
CA 6 HOH 208 608 898  HOH HOH C . 
CA 6 HOH 209 609 1035 HOH HOH C . 
CA 6 HOH 210 610 914  HOH HOH C . 
CA 6 HOH 211 611 650  HOH HOH C . 
CA 6 HOH 212 612 510  HOH HOH C . 
DA 6 HOH 1   401 65   HOH HOH D . 
DA 6 HOH 2   402 300  HOH HOH D . 
DA 6 HOH 3   403 615  HOH HOH D . 
DA 6 HOH 4   404 815  HOH HOH D . 
DA 6 HOH 5   405 791  HOH HOH D . 
DA 6 HOH 6   406 790  HOH HOH D . 
DA 6 HOH 7   407 493  HOH HOH D . 
DA 6 HOH 8   408 241  HOH HOH D . 
DA 6 HOH 9   409 354  HOH HOH D . 
DA 6 HOH 10  410 960  HOH HOH D . 
DA 6 HOH 11  411 237  HOH HOH D . 
DA 6 HOH 12  412 767  HOH HOH D . 
DA 6 HOH 13  413 799  HOH HOH D . 
DA 6 HOH 14  414 518  HOH HOH D . 
DA 6 HOH 15  415 967  HOH HOH D . 
DA 6 HOH 16  416 12   HOH HOH D . 
DA 6 HOH 17  417 625  HOH HOH D . 
DA 6 HOH 18  418 365  HOH HOH D . 
DA 6 HOH 19  419 952  HOH HOH D . 
DA 6 HOH 20  420 957  HOH HOH D . 
DA 6 HOH 21  421 269  HOH HOH D . 
DA 6 HOH 22  422 910  HOH HOH D . 
DA 6 HOH 23  423 462  HOH HOH D . 
DA 6 HOH 24  424 385  HOH HOH D . 
DA 6 HOH 25  425 814  HOH HOH D . 
DA 6 HOH 26  426 949  HOH HOH D . 
DA 6 HOH 27  427 103  HOH HOH D . 
DA 6 HOH 28  428 893  HOH HOH D . 
DA 6 HOH 29  429 257  HOH HOH D . 
DA 6 HOH 30  430 314  HOH HOH D . 
DA 6 HOH 31  431 446  HOH HOH D . 
DA 6 HOH 32  432 1012 HOH HOH D . 
DA 6 HOH 33  433 936  HOH HOH D . 
DA 6 HOH 34  434 337  HOH HOH D . 
DA 6 HOH 35  435 299  HOH HOH D . 
DA 6 HOH 36  436 268  HOH HOH D . 
DA 6 HOH 37  437 86   HOH HOH D . 
DA 6 HOH 38  438 252  HOH HOH D . 
DA 6 HOH 39  439 920  HOH HOH D . 
DA 6 HOH 40  440 34   HOH HOH D . 
DA 6 HOH 41  441 356  HOH HOH D . 
DA 6 HOH 42  442 951  HOH HOH D . 
DA 6 HOH 43  443 895  HOH HOH D . 
DA 6 HOH 44  444 376  HOH HOH D . 
DA 6 HOH 45  445 120  HOH HOH D . 
DA 6 HOH 46  446 210  HOH HOH D . 
DA 6 HOH 47  447 794  HOH HOH D . 
DA 6 HOH 48  448 88   HOH HOH D . 
DA 6 HOH 49  449 950  HOH HOH D . 
DA 6 HOH 50  450 131  HOH HOH D . 
DA 6 HOH 51  451 146  HOH HOH D . 
DA 6 HOH 52  452 606  HOH HOH D . 
DA 6 HOH 53  453 932  HOH HOH D . 
DA 6 HOH 54  454 109  HOH HOH D . 
DA 6 HOH 55  455 171  HOH HOH D . 
DA 6 HOH 56  456 453  HOH HOH D . 
DA 6 HOH 57  457 553  HOH HOH D . 
DA 6 HOH 58  458 358  HOH HOH D . 
DA 6 HOH 59  459 198  HOH HOH D . 
DA 6 HOH 60  460 139  HOH HOH D . 
DA 6 HOH 61  461 768  HOH HOH D . 
DA 6 HOH 62  462 17   HOH HOH D . 
DA 6 HOH 63  463 611  HOH HOH D . 
DA 6 HOH 64  464 937  HOH HOH D . 
DA 6 HOH 65  465 962  HOH HOH D . 
DA 6 HOH 66  466 21   HOH HOH D . 
DA 6 HOH 67  467 160  HOH HOH D . 
DA 6 HOH 68  468 192  HOH HOH D . 
DA 6 HOH 69  469 896  HOH HOH D . 
DA 6 HOH 70  470 938  HOH HOH D . 
DA 6 HOH 71  471 383  HOH HOH D . 
DA 6 HOH 72  472 3    HOH HOH D . 
DA 6 HOH 73  473 228  HOH HOH D . 
DA 6 HOH 74  474 166  HOH HOH D . 
DA 6 HOH 75  475 281  HOH HOH D . 
DA 6 HOH 76  476 41   HOH HOH D . 
DA 6 HOH 77  477 30   HOH HOH D . 
DA 6 HOH 78  478 77   HOH HOH D . 
DA 6 HOH 79  479 224  HOH HOH D . 
DA 6 HOH 80  480 343  HOH HOH D . 
DA 6 HOH 81  481 943  HOH HOH D . 
DA 6 HOH 82  482 425  HOH HOH D . 
DA 6 HOH 83  483 20   HOH HOH D . 
DA 6 HOH 84  484 1017 HOH HOH D . 
DA 6 HOH 85  485 1013 HOH HOH D . 
DA 6 HOH 86  486 152  HOH HOH D . 
DA 6 HOH 87  487 474  HOH HOH D . 
DA 6 HOH 88  488 458  HOH HOH D . 
DA 6 HOH 89  489 240  HOH HOH D . 
DA 6 HOH 90  490 798  HOH HOH D . 
DA 6 HOH 91  491 134  HOH HOH D . 
DA 6 HOH 92  492 374  HOH HOH D . 
DA 6 HOH 93  493 448  HOH HOH D . 
DA 6 HOH 94  494 1016 HOH HOH D . 
DA 6 HOH 95  495 494  HOH HOH D . 
DA 6 HOH 96  496 16   HOH HOH D . 
DA 6 HOH 97  497 894  HOH HOH D . 
DA 6 HOH 98  498 275  HOH HOH D . 
DA 6 HOH 99  499 935  HOH HOH D . 
DA 6 HOH 100 500 94   HOH HOH D . 
DA 6 HOH 101 501 147  HOH HOH D . 
DA 6 HOH 102 502 51   HOH HOH D . 
DA 6 HOH 103 503 24   HOH HOH D . 
DA 6 HOH 104 504 230  HOH HOH D . 
DA 6 HOH 105 505 605  HOH HOH D . 
DA 6 HOH 106 506 468  HOH HOH D . 
DA 6 HOH 107 507 511  HOH HOH D . 
DA 6 HOH 108 508 91   HOH HOH D . 
DA 6 HOH 109 509 508  HOH HOH D . 
DA 6 HOH 110 510 810  HOH HOH D . 
DA 6 HOH 111 511 503  HOH HOH D . 
DA 6 HOH 112 512 35   HOH HOH D . 
DA 6 HOH 113 513 307  HOH HOH D . 
DA 6 HOH 114 514 140  HOH HOH D . 
DA 6 HOH 115 515 806  HOH HOH D . 
DA 6 HOH 116 516 621  HOH HOH D . 
DA 6 HOH 117 517 953  HOH HOH D . 
DA 6 HOH 118 518 40   HOH HOH D . 
DA 6 HOH 119 519 202  HOH HOH D . 
DA 6 HOH 120 520 398  HOH HOH D . 
DA 6 HOH 121 521 614  HOH HOH D . 
DA 6 HOH 122 522 959  HOH HOH D . 
DA 6 HOH 123 523 288  HOH HOH D . 
DA 6 HOH 124 524 603  HOH HOH D . 
DA 6 HOH 125 525 793  HOH HOH D . 
DA 6 HOH 126 526 628  HOH HOH D . 
DA 6 HOH 127 527 118  HOH HOH D . 
DA 6 HOH 128 528 758  HOH HOH D . 
DA 6 HOH 129 529 353  HOH HOH D . 
DA 6 HOH 130 530 460  HOH HOH D . 
DA 6 HOH 131 531 232  HOH HOH D . 
DA 6 HOH 132 532 529  HOH HOH D . 
DA 6 HOH 133 533 200  HOH HOH D . 
DA 6 HOH 134 534 404  HOH HOH D . 
DA 6 HOH 135 535 965  HOH HOH D . 
DA 6 HOH 136 536 634  HOH HOH D . 
DA 6 HOH 137 537 107  HOH HOH D . 
DA 6 HOH 138 538 472  HOH HOH D . 
DA 6 HOH 139 539 595  HOH HOH D . 
DA 6 HOH 140 540 454  HOH HOH D . 
DA 6 HOH 141 541 272  HOH HOH D . 
DA 6 HOH 142 542 375  HOH HOH D . 
DA 6 HOH 143 543 178  HOH HOH D . 
DA 6 HOH 144 544 816  HOH HOH D . 
DA 6 HOH 145 545 270  HOH HOH D . 
DA 6 HOH 146 546 406  HOH HOH D . 
DA 6 HOH 147 547 329  HOH HOH D . 
DA 6 HOH 148 548 344  HOH HOH D . 
DA 6 HOH 149 549 964  HOH HOH D . 
DA 6 HOH 150 550 150  HOH HOH D . 
DA 6 HOH 151 551 796  HOH HOH D . 
DA 6 HOH 152 552 792  HOH HOH D . 
DA 6 HOH 153 553 562  HOH HOH D . 
DA 6 HOH 154 554 332  HOH HOH D . 
DA 6 HOH 155 555 902  HOH HOH D . 
DA 6 HOH 156 556 294  HOH HOH D . 
DA 6 HOH 157 557 100  HOH HOH D . 
DA 6 HOH 158 558 239  HOH HOH D . 
DA 6 HOH 159 559 948  HOH HOH D . 
DA 6 HOH 160 560 538  HOH HOH D . 
DA 6 HOH 161 561 430  HOH HOH D . 
DA 6 HOH 162 562 45   HOH HOH D . 
DA 6 HOH 163 563 762  HOH HOH D . 
DA 6 HOH 164 564 11   HOH HOH D . 
DA 6 HOH 165 565 942  HOH HOH D . 
DA 6 HOH 166 566 944  HOH HOH D . 
DA 6 HOH 167 567 1004 HOH HOH D . 
DA 6 HOH 168 568 956  HOH HOH D . 
DA 6 HOH 169 569 58   HOH HOH D . 
DA 6 HOH 170 570 73   HOH HOH D . 
DA 6 HOH 171 571 216  HOH HOH D . 
DA 6 HOH 172 572 101  HOH HOH D . 
DA 6 HOH 173 573 463  HOH HOH D . 
DA 6 HOH 174 574 412  HOH HOH D . 
DA 6 HOH 175 575 405  HOH HOH D . 
DA 6 HOH 176 576 955  HOH HOH D . 
DA 6 HOH 177 577 807  HOH HOH D . 
DA 6 HOH 178 578 219  HOH HOH D . 
DA 6 HOH 179 579 261  HOH HOH D . 
DA 6 HOH 180 580 274  HOH HOH D . 
DA 6 HOH 181 581 760  HOH HOH D . 
DA 6 HOH 182 582 946  HOH HOH D . 
DA 6 HOH 183 583 461  HOH HOH D . 
DA 6 HOH 184 584 321  HOH HOH D . 
DA 6 HOH 185 585 262  HOH HOH D . 
DA 6 HOH 186 586 933  HOH HOH D . 
DA 6 HOH 187 587 136  HOH HOH D . 
DA 6 HOH 188 588 251  HOH HOH D . 
DA 6 HOH 189 589 242  HOH HOH D . 
DA 6 HOH 190 590 416  HOH HOH D . 
DA 6 HOH 191 591 1033 HOH HOH D . 
DA 6 HOH 192 592 522  HOH HOH D . 
DA 6 HOH 193 593 945  HOH HOH D . 
DA 6 HOH 194 594 451  HOH HOH D . 
DA 6 HOH 195 595 286  HOH HOH D . 
DA 6 HOH 196 596 569  HOH HOH D . 
DA 6 HOH 197 597 635  HOH HOH D . 
DA 6 HOH 198 598 573  HOH HOH D . 
DA 6 HOH 199 599 504  HOH HOH D . 
DA 6 HOH 200 600 519  HOH HOH D . 
DA 6 HOH 201 601 940  HOH HOH D . 
DA 6 HOH 202 602 490  HOH HOH D . 
DA 6 HOH 203 603 947  HOH HOH D . 
DA 6 HOH 204 604 911  HOH HOH D . 
DA 6 HOH 205 605 801  HOH HOH D . 
DA 6 HOH 206 606 640  HOH HOH D . 
DA 6 HOH 207 607 1015 HOH HOH D . 
DA 6 HOH 208 608 934  HOH HOH D . 
DA 6 HOH 209 609 803  HOH HOH D . 
DA 6 HOH 210 610 1028 HOH HOH D . 
DA 6 HOH 211 611 912  HOH HOH D . 
DA 6 HOH 212 612 583  HOH HOH D . 
DA 6 HOH 213 613 417  HOH HOH D . 
DA 6 HOH 214 614 972  HOH HOH D . 
DA 6 HOH 215 615 645  HOH HOH D . 
DA 6 HOH 216 616 596  HOH HOH D . 
DA 6 HOH 217 617 797  HOH HOH D . 
DA 6 HOH 218 618 961  HOH HOH D . 
DA 6 HOH 219 619 170  HOH HOH D . 
DA 6 HOH 220 620 900  HOH HOH D . 
DA 6 HOH 221 621 939  HOH HOH D . 
DA 6 HOH 222 622 766  HOH HOH D . 
DA 6 HOH 223 623 642  HOH HOH D . 
DA 6 HOH 224 624 520  HOH HOH D . 
DA 6 HOH 225 625 594  HOH HOH D . 
DA 6 HOH 226 626 407  HOH HOH D . 
DA 6 HOH 227 627 941  HOH HOH D . 
DA 6 HOH 228 628 290  HOH HOH D . 
DA 6 HOH 229 629 560  HOH HOH D . 
DA 6 HOH 230 630 315  HOH HOH D . 
DA 6 HOH 231 631 809  HOH HOH D . 
DA 6 HOH 232 632 599  HOH HOH D . 
DA 6 HOH 233 633 653  HOH HOH D . 
DA 6 HOH 234 634 279  HOH HOH D . 
DA 6 HOH 235 635 966  HOH HOH D . 
DA 6 HOH 236 636 795  HOH HOH D . 
DA 6 HOH 237 637 574  HOH HOH D . 
DA 6 HOH 238 638 487  HOH HOH D . 
DA 6 HOH 239 639 811  HOH HOH D . 
DA 6 HOH 240 640 517  HOH HOH D . 
DA 6 HOH 241 641 467  HOH HOH D . 
DA 6 HOH 242 642 236  HOH HOH D . 
DA 6 HOH 243 643 763  HOH HOH D . 
DA 6 HOH 244 644 808  HOH HOH D . 
DA 6 HOH 245 645 282  HOH HOH D . 
DA 6 HOH 246 646 1002 HOH HOH D . 
DA 6 HOH 247 647 652  HOH HOH D . 
DA 6 HOH 248 648 576  HOH HOH D . 
DA 6 HOH 249 649 901  HOH HOH D . 
DA 6 HOH 250 650 968  HOH HOH D . 
DA 6 HOH 251 651 802  HOH HOH D . 
DA 6 HOH 252 652 958  HOH HOH D . 
DA 6 HOH 253 653 804  HOH HOH D . 
DA 6 HOH 254 654 204  HOH HOH D . 
DA 6 HOH 255 655 1014 HOH HOH D . 
DA 6 HOH 256 656 644  HOH HOH D . 
DA 6 HOH 257 657 805  HOH HOH D . 
DA 6 HOH 258 658 654  HOH HOH D . 
DA 6 HOH 259 659 565  HOH HOH D . 
DA 6 HOH 260 660 963  HOH HOH D . 
DA 6 HOH 261 661 954  HOH HOH D . 
DA 6 HOH 262 662 533  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 LYS 3   ? CD  ? A LYS 3   CD  
2  1 Y 1 A LYS 3   ? CE  ? A LYS 3   CE  
3  1 Y 1 A LYS 3   ? NZ  ? A LYS 3   NZ  
4  1 Y 1 A LYS 57  ? NZ  ? A LYS 57  NZ  
5  1 Y 1 B SER 136 ? OG  ? B SER 136 OG  
6  1 Y 1 B GLU 137 ? CG  ? B GLU 137 CG  
7  1 Y 1 B GLU 137 ? CD  ? B GLU 137 CD  
8  1 Y 1 B GLU 137 ? OE1 ? B GLU 137 OE1 
9  1 Y 1 B GLU 137 ? OE2 ? B GLU 137 OE2 
10 1 Y 1 B ARG 194 ? NE  ? B ARG 194 NE  
11 1 Y 1 B ARG 194 ? CZ  ? B ARG 194 CZ  
12 1 Y 1 B ARG 194 ? NH1 ? B ARG 194 NH1 
13 1 Y 1 B ARG 194 ? NH2 ? B ARG 194 NH2 
14 1 Y 1 B GLU 254 ? CB  ? B GLU 254 CB  
15 1 Y 1 B GLU 254 ? CG  ? B GLU 254 CG  
16 1 Y 1 B GLU 254 ? CD  ? B GLU 254 CD  
17 1 Y 1 B GLU 254 ? OE1 ? B GLU 254 OE1 
18 1 Y 1 B GLU 254 ? OE2 ? B GLU 254 OE2 
19 1 Y 1 C LYS 3   ? CG  ? C LYS 3   CG  
20 1 Y 1 C LYS 3   ? CD  ? C LYS 3   CD  
21 1 Y 1 C LYS 3   ? CE  ? C LYS 3   CE  
22 1 Y 1 C LYS 3   ? NZ  ? C LYS 3   NZ  
23 1 Y 1 C GLU 47  ? CD  ? C GLU 47  CD  
24 1 Y 1 C GLU 47  ? OE1 ? C GLU 47  OE1 
25 1 Y 1 C GLU 47  ? OE2 ? C GLU 47  OE2 
26 1 Y 1 C LYS 57  ? CD  ? C LYS 57  CD  
27 1 Y 1 C LYS 57  ? CE  ? C LYS 57  CE  
28 1 Y 1 C LYS 57  ? NZ  ? C LYS 57  NZ  
29 1 Y 1 C GLN 82  ? CG  ? C GLN 82  CG  
30 1 Y 1 C GLN 82  ? CD  ? C GLN 82  CD  
31 1 Y 1 C GLN 82  ? OE1 ? C GLN 82  OE1 
32 1 Y 1 C GLN 82  ? NE2 ? C GLN 82  NE2 
33 1 Y 1 C GLN 219 ? CG  ? C GLN 219 CG  
34 1 Y 1 C GLN 219 ? CD  ? C GLN 219 CD  
35 1 Y 1 C GLN 219 ? OE1 ? C GLN 219 OE1 
36 1 Y 1 C GLN 219 ? NE2 ? C GLN 219 NE2 
37 1 Y 1 C ASP 235 ? CB  ? C ASP 235 CB  
38 1 Y 1 C ASP 235 ? CG  ? C ASP 235 CG  
39 1 Y 1 C ASP 235 ? OD1 ? C ASP 235 OD1 
40 1 Y 1 C ASP 235 ? OD2 ? C ASP 235 OD2 
41 1 Y 1 C ARG 240 ? NE  ? C ARG 240 NE  
42 1 Y 1 C ARG 240 ? CZ  ? C ARG 240 CZ  
43 1 Y 1 C ARG 240 ? NH1 ? C ARG 240 NH1 
44 1 Y 1 C ARG 240 ? NH2 ? C ARG 240 NH2 
45 1 Y 1 D LYS 3   ? CD  ? D LYS 3   CD  
46 1 Y 1 D LYS 3   ? CE  ? D LYS 3   CE  
47 1 Y 1 D LYS 3   ? NZ  ? D LYS 3   NZ  
48 1 Y 1 D LYS 166 ? CE  ? D LYS 166 CE  
49 1 Y 1 D LYS 166 ? NZ  ? D LYS 166 NZ  
50 1 Y 1 D GLU 185 ? CD  ? D GLU 185 CD  
51 1 Y 1 D GLU 185 ? OE1 ? D GLU 185 OE1 
52 1 Y 1 D GLU 185 ? OE2 ? D GLU 185 OE2 
53 1 Y 1 D ARG 240 ? CG  ? D ARG 240 CG  
54 1 Y 1 D ARG 240 ? CD  ? D ARG 240 CD  
55 1 Y 1 D ARG 240 ? NE  ? D ARG 240 NE  
56 1 Y 1 D ARG 240 ? CZ  ? D ARG 240 CZ  
57 1 Y 1 D ARG 240 ? NH1 ? D ARG 240 NH1 
58 1 Y 1 D ARG 240 ? NH2 ? D ARG 240 NH2 
59 1 Y 1 D GLN 263 ? CB  ? D GLN 263 CB  
60 1 Y 1 D GLN 263 ? CG  ? D GLN 263 CG  
61 1 Y 1 D GLN 263 ? CD  ? D GLN 263 CD  
62 1 Y 1 D GLN 263 ? OE1 ? D GLN 263 OE1 
63 1 Y 1 D GLN 263 ? NE2 ? D GLN 263 NE2 
# 
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      ? ? ? . 1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? . 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? . 3 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? . 4 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? . 5 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? . 6 
# 
_cell.entry_id           6G5L 
_cell.length_a           77.127 
_cell.length_b           74.235 
_cell.length_c           91.527 
_cell.angle_alpha        90.000 
_cell.angle_beta         108.640 
_cell.angle_gamma        90.000 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         6G5L 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.Int_Tables_number                4 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_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                   6G5L 
_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            2.08 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.78 
_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 30% 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 PILATUS3 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         2014-01-08 
# 
_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   0.975522 
_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        0.975522 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.entry_id                     6G5L 
_reflns.d_resolution_high            1.210 
_reflns.d_resolution_low             73.083 
_reflns.pdbx_number_measured_all     1978101 
_reflns.number_all                   284311 
_reflns.number_obs                   284311 
_reflns.pdbx_netI_over_av_sigmaI     4.278 
_reflns.pdbx_netI_over_sigmaI        20.200 
_reflns.pdbx_Rsym_value              0.043 
_reflns.pdbx_redundancy              7.000 
_reflns.percent_possible_obs         95.900 
_reflns.pdbx_Rrim_I_all              0.053 
_reflns.pdbx_Rpim_I_all              0.020 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_CC_half                 ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_CC_half 
1.210 1.280  ? 266665 ? ? 0.421 1.7  0.421 ? 6.600 ? 4.600  ? 40120 ? ? 0.500 ? 92.900 0.500 0.191 ? 1  ? 
1.280 1.350  ? 271141 ? ? 0.292 2.5  0.292 ? 7.000 ? 6.400  ? 38567 ? ? 0.346 ? 94.400 0.346 0.128 ? 2  ? 
1.350 1.450  ? 255480 ? ? 0.190 3.9  0.190 ? 7.000 ? 8.800  ? 36472 ? ? 0.227 ? 95.100 0.227 0.085 ? 3  ? 
1.450 1.560  ? 238944 ? ? 0.113 6.5  0.113 ? 7.000 ? 12.800 ? 34235 ? ? 0.139 ? 95.700 0.139 0.052 ? 4  ? 
1.560 1.710  ? 217854 ? ? 0.070 10.4 0.070 ? 6.900 ? 18.100 ? 31674 ? ? 0.089 ? 96.100 0.089 0.034 ? 5  ? 
1.710 1.910  ? 204649 ? ? 0.046 14.9 0.046 ? 7.100 ? 25.800 ? 28883 ? ? 0.060 ? 97.000 0.060 0.022 ? 6  ? 
1.910 2.210  ? 184462 ? ? 0.034 18.4 0.034 ? 7.100 ? 36.200 ? 25894 ? ? 0.044 ? 98.300 0.044 0.016 ? 7  ? 
2.210 2.710  ? 153845 ? ? 0.030 19.7 0.030 ? 7.000 ? 42.400 ? 21898 ? ? 0.039 ? 98.400 0.039 0.015 ? 8  ? 
2.710 3.830  ? 120726 ? ? 0.031 11.5 0.031 ? 7.000 ? 49.900 ? 17136 ? ? 0.038 ? 99.000 0.038 0.014 ? 9  ? 
3.830 73.083 ? 64335  ? ? 0.040 8.6  0.040 ? 6.800 ? 52.600 ? 9432  ? ? 0.049 ? 98.000 0.049 0.019 ? 10 ? 
# 
_refine.entry_id                                 6G5L 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.2100 
_refine.ls_d_res_low                             73.0800 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    95.6700 
_refine.ls_number_reflns_obs                     284275 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1396 
_refine.ls_R_factor_R_work                       0.1359 
_refine.ls_wR_factor_R_work                      0.1395 
_refine.ls_R_factor_R_free                       0.1734 
_refine.ls_wR_factor_R_free                      0.1804 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_number_reflns_R_free                  28370 
_refine.ls_number_reflns_R_work                  255905 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.0494 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.2900 
_refine.aniso_B[2][2]                            0.3600 
_refine.aniso_B[3][3]                            -0.1000 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            0.0800 
_refine.aniso_B[2][3]                            -0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9780 
_refine.correlation_coeff_Fo_to_Fc_free          0.9710 
_refine.overall_SU_R_Cruickshank_DPI             0.0416 
_refine.overall_SU_R_free                        0.0430 
_refine.pdbx_overall_ESU_R                       0.0420 
_refine.pdbx_overall_ESU_R_Free                  0.0430 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      1JD0 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.8973 
_refine.B_iso_max                                149.770 
_refine.B_iso_min                                7.090 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.000 
_refine.occupancy_min                            0.500 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8327 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         162 
_refine_hist.number_atoms_solvent             1036 
_refine_hist.number_atoms_total               9525 
_refine_hist.d_res_high                       1.2100 
_refine_hist.d_res_low                        73.0800 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' r_bond_refined_d       8973  0.029  0.019  ? ? 
'X-RAY DIFFRACTION' r_angle_refined_deg    12232 2.514  1.963  ? ? 
'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 1082  6.961  5.000  ? ? 
'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 435   37.228 24.690 ? ? 
'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 1366  12.059 15.000 ? ? 
'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 29    17.376 15.000 ? ? 
'X-RAY DIFFRACTION' r_chiral_restr         1273  0.185  0.200  ? ? 
'X-RAY DIFFRACTION' r_gen_planes_refined   7050  0.018  0.021  ? ? 
'X-RAY DIFFRACTION' r_mcbond_it            4280  3.123  1.621  ? ? 
'X-RAY DIFFRACTION' r_mcangle_it           5378  3.699  2.440  ? ? 
'X-RAY DIFFRACTION' r_scbond_it            4693  5.123  1.972  ? ? 
'X-RAY DIFFRACTION' r_rigid_bond_restr     8973  8.235  3.000  ? ? 
'X-RAY DIFFRACTION' r_sphericity_free      660   22.794 5.000  ? ? 
'X-RAY DIFFRACTION' r_sphericity_bonded    9087  15.163 5.000  ? ? 
# 
_refine_ls_shell.d_res_high                       1.2100 
_refine_ls_shell.d_res_low                        1.2410 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               91.7900 
_refine_ls_shell.number_reflns_R_work             18045 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.1760 
_refine_ls_shell.R_factor_R_free                  0.2060 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             2093 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                20138 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                     6G5L 
_struct.title                        
;Crystal structure of human carbonic anhydrase isozyme XII with 4-chloro-2-(cyclohexylamino)-N-(2-hydroxyethyl)-5-sulfamoyl-benzamide
;
_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        6G5L 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor comple, 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 5 ? 
I  N N 4 ? 
J  N N 2 ? 
K  N N 3 ? 
L  N N 4 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 4 ? 
P  N N 2 ? 
Q  N N 3 ? 
R  N N 4 ? 
S  N N 2 ? 
T  N N 3 ? 
U  N N 4 ? 
V  N N 4 ? 
W  N N 4 ? 
X  N N 4 ? 
Y  N N 5 ? 
Z  N N 4 ? 
AA N N 6 ? 
BA N N 6 ? 
CA N N 6 ? 
DA N N 6 ? 
# 
_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 6G5L A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 6G5L B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 6G5L C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 6G5L 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 6G5L MET A 1 ? UNP O43570 ? ? 'initiating methionine' 1 1 
2 6G5L MET B 1 ? UNP O43570 ? ? 'initiating methionine' 1 2 
3 6G5L MET C 1 ? UNP O43570 ? ? 'initiating methionine' 1 3 
4 6G5L 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_defined_assembly ? dimeric 2 
2 author_defined_assembly ? 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,AA,BA 
2 1 C,D,P,Q,R,S,T,U,V,W,X,Y,Z,CA,DA 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 none ? 
2 2 none ? 
# 
_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 
# 
_struct_biol.id        1 
_struct_biol.details   'The asymmetric unit contains two dimers:' 
# 
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   ? ASN A 13  ? PHE A 7   ASN A 13  5 ? 7  
HELX_P HELX_P2  AA2 SER A 14  ? TYR A 19  ? SER A 14  TYR A 19  1 ? 6  
HELX_P HELX_P3  AA3 PRO A 20  ? GLY A 24  ? PRO A 20  GLY A 24  5 ? 5  
HELX_P HELX_P4  AA4 HIS A 33  ? ASP A 35  ? HIS A 33  ASP A 35  5 ? 3  
HELX_P HELX_P5  AA5 ASP A 128 ? SER A 133 ? ASP A 128 SER A 133 1 ? 6  
HELX_P HELX_P6  AA6 ASN A 152 ? SER A 160 ? ASN A 152 SER A 160 1 ? 9  
HELX_P HELX_P7  AA7 HIS A 161 ? LYS A 166 ? HIS A 161 LYS A 166 5 ? 6  
HELX_P HELX_P8  AA8 ASN A 178 ? LEU A 183 ? ASN A 178 LEU A 183 5 ? 6  
HELX_P HELX_P9  AA9 SER A 218 ? ALA A 228 ? SER A 218 ALA A 228 1 ? 11 
HELX_P HELX_P10 AB1 GLY B 11  ? LYS B 18  ? GLY B 11  LYS B 18  5 ? 8  
HELX_P HELX_P11 AB2 TYR B 19  ? GLY B 24  ? TYR B 19  GLY B 24  5 ? 6  
HELX_P HELX_P12 AB3 HIS B 33  ? ASP B 35  ? HIS B 33  ASP B 35  5 ? 3  
HELX_P HELX_P13 AB4 ASP B 128 ? SER B 133 ? ASP B 128 SER B 133 1 ? 6  
HELX_P HELX_P14 AB5 ASN B 152 ? SER B 160 ? ASN B 152 SER B 160 1 ? 9  
HELX_P HELX_P15 AB6 HIS B 161 ? VAL B 165 ? HIS B 161 VAL B 165 5 ? 5  
HELX_P HELX_P16 AB7 ASN B 178 ? LEU B 183 ? ASN B 178 LEU B 183 5 ? 6  
HELX_P HELX_P17 AB8 SER B 218 ? LEU B 229 ? SER B 218 LEU B 229 1 ? 12 
HELX_P HELX_P18 AB9 GLY C 11  ? TRP C 15  ? GLY C 11  TRP C 15  5 ? 5  
HELX_P HELX_P19 AC1 TYR C 19  ? GLY C 24  ? TYR C 19  GLY C 24  5 ? 6  
HELX_P HELX_P20 AC2 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P21 AC3 ASP C 128 ? SER C 133 ? ASP C 128 SER C 133 1 ? 6  
HELX_P HELX_P22 AC4 ASN C 152 ? SER C 160 ? ASN C 152 SER C 160 1 ? 9  
HELX_P HELX_P23 AC5 HIS C 161 ? VAL C 165 ? HIS C 161 VAL C 165 5 ? 5  
HELX_P HELX_P24 AC6 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P25 AC7 SER C 218 ? ALA C 228 ? SER C 218 ALA C 228 1 ? 11 
HELX_P HELX_P26 AC8 GLY D 11  ? LYS D 18  ? GLY D 11  LYS D 18  5 ? 8  
HELX_P HELX_P27 AC9 TYR D 19  ? GLY D 24  ? TYR D 19  GLY D 24  5 ? 6  
HELX_P HELX_P28 AD1 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P29 AD2 ASP D 128 ? SER D 133 ? ASP D 128 SER D 133 1 ? 6  
HELX_P HELX_P30 AD3 ASN D 152 ? SER D 160 ? ASN D 152 SER D 160 1 ? 9  
HELX_P HELX_P31 AD4 HIS D 161 ? LYS D 166 ? HIS D 161 LYS D 166 5 ? 6  
HELX_P HELX_P32 AD5 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P33 AD6 GLN D 219 ? LEU D 229 ? GLN D 219 LEU D 229 1 ? 11 
# 
_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 ? ? ? ? ? ? ? 2.028 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf4  disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 202 SG ? ? D CYS 22  D CYS 202 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc1  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F EM5 .   N5 A ? A ZN  301 A EM5 302 1_555 ? ? ? ? ? ? ? 1.958 ? ? 
metalc5  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F EM5 .   N5 B ? A ZN  301 A EM5 302 1_555 ? ? ? ? ? ? ? 1.958 ? ? 
metalc6  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc7  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc8  metalc ? ? B HIS 117 ND1 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 1.999 ? ? 
metalc9  metalc ? ? J ZN  .   ZN  ? ? ? 1_555 K EM5 .   N5 A ? B ZN  301 B EM5 302 1_555 ? ? ? ? ? ? ? 1.955 ? ? 
metalc10 metalc ? ? J ZN  .   ZN  ? ? ? 1_555 K EM5 .   N5 B ? B ZN  301 B EM5 302 1_555 ? ? ? ? ? ? ? 1.940 ? ? 
metalc11 metalc ? ? J ZN  .   ZN  ? ? ? 1_555 K EM5 .   S1 A ? B ZN  301 B EM5 302 1_555 ? ? ? ? ? ? ? 2.991 ? ? 
metalc12 metalc ? ? J ZN  .   ZN  ? ? ? 1_555 K EM5 .   S1 B ? B ZN  301 B EM5 302 1_555 ? ? ? ? ? ? ? 2.992 ? ? 
metalc13 metalc ? ? C HIS 91  NE2 ? ? ? 1_555 P ZN  .   ZN ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc14 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 P ZN  .   ZN ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc15 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 P ZN  .   ZN ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 1.994 ? ? 
metalc16 metalc ? ? P ZN  .   ZN  ? ? ? 1_555 Q EM5 .   N5 ? ? C ZN  301 C EM5 302 1_555 ? ? ? ? ? ? ? 1.966 ? ? 
metalc17 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 S ZN  .   ZN ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 2.008 ? ? 
metalc18 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 S ZN  .   ZN ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc19 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 S ZN  .   ZN ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc20 metalc ? ? S ZN  .   ZN  ? ? ? 1_555 T EM5 .   N5 ? ? D ZN  301 D EM5 302 1_555 ? ? ? ? ? ? ? 1.959 ? ? 
# 
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_555 101.4 ? 
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_555 113.1 ? 
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 N5  A F EM5 .   ? A EM5 302 ? 1_555 108.8 ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  A F EM5 .   ? A EM5 302 ? 1_555 115.8 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  A F EM5 .   ? A EM5 302 ? 1_555 116.5 ? 
7  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  B F EM5 .   ? A EM5 302 ? 1_555 108.0 ? 
8  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  B F EM5 .   ? A EM5 302 ? 1_555 115.6 ? 
9  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  B F EM5 .   ? A EM5 302 ? 1_555 117.4 ? 
10 N5  A F EM5 .   ? A EM5 302 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N5  B F EM5 .   ? A EM5 302 ? 1_555 0.9   ? 
11 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 103.0 ? 
12 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 112.9 ? 
13 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 98.7  ? 
14 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N5  A K EM5 .   ? B EM5 302 ? 1_555 108.4 ? 
15 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N5  A K EM5 .   ? B EM5 302 ? 1_555 116.2 ? 
16 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N5  A K EM5 .   ? B EM5 302 ? 1_555 116.8 ? 
17 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N5  B K EM5 .   ? B EM5 302 ? 1_555 109.2 ? 
18 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N5  B K EM5 .   ? B EM5 302 ? 1_555 114.9 ? 
19 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N5  B K EM5 .   ? B EM5 302 ? 1_555 117.1 ? 
20 N5  A K EM5 .   ? B EM5 302 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N5  B K EM5 .   ? B EM5 302 ? 1_555 1.3   ? 
21 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 S1  A K EM5 .   ? B EM5 302 ? 1_555 98.9  ? 
22 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 S1  A K EM5 .   ? B EM5 302 ? 1_555 143.7 ? 
23 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 S1  A K EM5 .   ? B EM5 302 ? 1_555 99.0  ? 
24 N5  A K EM5 .   ? B EM5 302 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 S1  A K EM5 .   ? B EM5 302 ? 1_555 28.0  ? 
25 N5  B K EM5 .   ? B EM5 302 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 S1  A K EM5 .   ? B EM5 302 ? 1_555 29.3  ? 
26 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 S1  B K EM5 .   ? B EM5 302 ? 1_555 98.9  ? 
27 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 S1  B K EM5 .   ? B EM5 302 ? 1_555 143.6 ? 
28 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 S1  B K EM5 .   ? B EM5 302 ? 1_555 99.1  ? 
29 N5  A K EM5 .   ? B EM5 302 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 S1  B K EM5 .   ? B EM5 302 ? 1_555 28.0  ? 
30 N5  B K EM5 .   ? B EM5 302 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 S1  B K EM5 .   ? B EM5 302 ? 1_555 29.2  ? 
31 S1  A K EM5 .   ? B EM5 302 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 S1  B K EM5 .   ? B EM5 302 ? 1_555 0.1   ? 
32 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? P ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 101.3 ? 
33 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? P ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 114.9 ? 
34 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? P ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 99.1  ? 
35 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? P ZN . ? C ZN 301 ? 1_555 N5  ? Q EM5 .   ? C EM5 302 ? 1_555 108.9 ? 
36 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? P ZN . ? C ZN 301 ? 1_555 N5  ? Q EM5 .   ? C EM5 302 ? 1_555 115.8 ? 
37 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? P ZN . ? C ZN 301 ? 1_555 N5  ? Q EM5 .   ? C EM5 302 ? 1_555 115.7 ? 
38 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 102.7 ? 
39 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 112.7 ? 
40 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 99.5  ? 
41 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 N5  ? T EM5 .   ? D EM5 302 ? 1_555 110.0 ? 
42 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 N5  ? T EM5 .   ? D EM5 302 ? 1_555 114.6 ? 
43 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 N5  ? T EM5 .   ? D EM5 302 ? 1_555 116.3 ? 
# 
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 -0.16 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 3.47  
3 SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 -3.48 
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 -0.72 
5 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 9.90  
6 SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 2.03  
7 PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 2.04  
8 SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 1.38  
9 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 5.05  
# 
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 ? MET C 148 ? LEU C 139 MET C 148 
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 ? MET C 148 ? LEU C 139 MET C 148 
AA9 6  VAL C 215 ? ILE C 217 ? VAL C 215 ILE C 217 
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 ? GLY D 149 ? LEU D 139 GLY D 149 
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 ? GLY D 149 ? LEU D 139 GLY D 149 
AB3 6  VAL D 215 ? SER D 218 ? VAL D 215 SER D 218 
# 
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 LEU A 142 ? O LEU A 142 N ILE A 118 ? N ILE A 118 
AA2 6 7  O VAL A 119 ? O VAL A 119 N GLN A 89  ? N GLN A 89  
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 GLU A 47  ? N GLU A 47  O GLN A 79  ? O GLN A 79  
AA3 2 3  N ILE A 78  ? N ILE A 78  O TYR A 85  ? O TYR A 85  
AA3 3 4  N GLN A 89  ? N GLN A 89  O VAL A 119 ? O VAL A 119 
AA3 4 5  N ILE A 118 ? N ILE A 118 O LEU A 142 ? O LEU A 142 
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 VAL B 257 ? O VAL B 257 
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 GLU B 47  ? N GLU B 47  O GLN B 79  ? O GLN B 79  
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 ASN C 71  ? O ASN C 71  N LEU C 60  ? N LEU C 60  
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 GLU C 147 ? N GLU C 147 O VAL C 215 ? O VAL C 215 
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 VAL D 119 ? O VAL D 119 N GLN D 89  ? N GLN D 89  
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 GLU D 47  ? N GLU D 47  O GLN D 79  ? O GLN D 79  
AB3 2 3  N ILE D 78  ? N ILE D 78  O TYR D 85  ? O TYR D 85  
AB3 3 4  N GLN D 89  ? N GLN D 89  O VAL D 119 ? O VAL D 119 
AB3 4 5  N ILE D 118 ? N ILE D 118 O LEU D 142 ? O LEU D 142 
AB3 5 6  N GLY D 149 ? N GLY D 149 O ILE D 217 ? O ILE D 217 
# 
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 EM5 302 ? 19 'binding site for residue EM5 A 302' 
AC3 Software A EDO 303 ? 4  'binding site for residue EDO A 303' 
AC4 Software A PEG 304 ? 6  'binding site for residue PEG A 304' 
AC5 Software A EDO 305 ? 5  'binding site for residue EDO A 305' 
AC6 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC7 Software B EM5 302 ? 18 'binding site for residue EM5 B 302' 
AC8 Software B EDO 303 ? 7  'binding site for residue EDO B 303' 
AC9 Software B EDO 304 ? 9  'binding site for residue EDO B 304' 
AD1 Software B EDO 305 ? 5  'binding site for residue EDO B 305' 
AD2 Software B EDO 306 ? 5  'binding site for residue EDO B 306' 
AD3 Software C ZN  301 ? 4  'binding site for residue ZN C 301'  
AD4 Software C EM5 302 ? 15 'binding site for residue EM5 C 302' 
AD5 Software C EDO 303 ? 5  'binding site for residue EDO C 303' 
AD6 Software D ZN  301 ? 4  'binding site for residue ZN D 301'  
AD7 Software D EM5 302 ? 13 'binding site for residue EM5 D 302' 
AD8 Software D EDO 303 ? 5  'binding site for residue EDO D 303' 
AD9 Software D EDO 304 ? 7  'binding site for residue EDO D 304' 
AE1 Software D EDO 305 ? 4  'binding site for residue EDO D 305' 
AE2 Software D EDO 306 ? 6  'binding site for residue EDO D 306' 
AE3 Software D PEG 307 ? 7  'binding site for residue PEG D 307' 
AE4 Software D EDO 308 ? 5  'binding site for residue EDO D 308' 
# 
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  EM5 F  .   ? EM5 A 302 . ? 1_555 ? 
5   AC2 19 TRP A  4   ? TRP A 4   . ? 1_555 ? 
6   AC2 19 ASN A  64  ? ASN A 64  . ? 1_555 ? 
7   AC2 19 HIS A  66  ? HIS A 66  . ? 1_555 ? 
8   AC2 19 GLN A  89  ? GLN A 89  . ? 1_555 ? 
9   AC2 19 HIS A  91  ? HIS A 91  . ? 1_555 ? 
10  AC2 19 HIS A  93  ? HIS A 93  . ? 1_555 ? 
11  AC2 19 HIS A  117 ? HIS A 117 . ? 1_555 ? 
12  AC2 19 ALA A  129 ? ALA A 129 . ? 1_555 ? 
13  AC2 19 VAL A  141 ? VAL A 141 . ? 1_555 ? 
14  AC2 19 LEU A  197 ? LEU A 197 . ? 1_555 ? 
15  AC2 19 THR A  198 ? THR A 198 . ? 1_555 ? 
16  AC2 19 THR A  199 ? THR A 199 . ? 1_555 ? 
17  AC2 19 TRP A  208 ? TRP A 208 . ? 1_555 ? 
18  AC2 19 ZN  E  .   ? ZN  A 301 . ? 1_555 ? 
19  AC2 19 PEG H  .   ? PEG A 304 . ? 1_555 ? 
20  AC2 19 HOH AA .   ? HOH A 401 . ? 1_555 ? 
21  AC2 19 HOH AA .   ? HOH A 405 . ? 1_555 ? 
22  AC2 19 HOH AA .   ? HOH A 414 . ? 1_555 ? 
23  AC2 19 HOH AA .   ? HOH A 538 . ? 1_555 ? 
24  AC3 4  ASN A  134 ? ASN A 134 . ? 1_555 ? 
25  AC3 4  SER A  136 ? SER A 136 . ? 1_555 ? 
26  AC3 4  PRO A  204 ? PRO A 204 . ? 1_555 ? 
27  AC3 4  HOH AA .   ? HOH A 404 . ? 1_555 ? 
28  AC4 6  SER A  133 ? SER A 133 . ? 1_555 ? 
29  AC4 6  PRO A  201 ? PRO A 201 . ? 1_555 ? 
30  AC4 6  ASN A  203 ? ASN A 203 . ? 1_555 ? 
31  AC4 6  EM5 F  .   ? EM5 A 302 . ? 1_555 ? 
32  AC4 6  HOH AA .   ? HOH A 414 . ? 1_555 ? 
33  AC4 6  HOH AA .   ? HOH A 552 . ? 1_555 ? 
34  AC5 5  GLY A  50  ? GLY A 50  . ? 1_555 ? 
35  AC5 5  ASN A  52  ? ASN A 52  . ? 1_555 ? 
36  AC5 5  LEU A  53  ? LEU A 53  . ? 1_555 ? 
37  AC5 5  ASP A  75  ? ASP A 75  . ? 1_555 ? 
38  AC5 5  GLN B  49  ? GLN B 49  . ? 1_655 ? 
39  AC6 4  HIS B  91  ? HIS B 91  . ? 1_555 ? 
40  AC6 4  HIS B  93  ? HIS B 93  . ? 1_555 ? 
41  AC6 4  HIS B  117 ? HIS B 117 . ? 1_555 ? 
42  AC6 4  EM5 K  .   ? EM5 B 302 . ? 1_555 ? 
43  AC7 18 ASN B  64  ? ASN B 64  . ? 1_555 ? 
44  AC7 18 HIS B  66  ? HIS B 66  . ? 1_555 ? 
45  AC7 18 GLN B  89  ? GLN B 89  . ? 1_555 ? 
46  AC7 18 HIS B  91  ? HIS B 91  . ? 1_555 ? 
47  AC7 18 HIS B  93  ? HIS B 93  . ? 1_555 ? 
48  AC7 18 HIS B  117 ? HIS B 117 . ? 1_555 ? 
49  AC7 18 ALA B  129 ? ALA B 129 . ? 1_555 ? 
50  AC7 18 SER B  130 ? SER B 130 . ? 1_555 ? 
51  AC7 18 VAL B  141 ? VAL B 141 . ? 1_555 ? 
52  AC7 18 LEU B  197 ? LEU B 197 . ? 1_555 ? 
53  AC7 18 THR B  198 ? THR B 198 . ? 1_555 ? 
54  AC7 18 THR B  199 ? THR B 199 . ? 1_555 ? 
55  AC7 18 TRP B  208 ? TRP B 208 . ? 1_555 ? 
56  AC7 18 ZN  J  .   ? ZN  B 301 . ? 1_555 ? 
57  AC7 18 EDO O  .   ? EDO B 306 . ? 1_555 ? 
58  AC7 18 HOH BA .   ? HOH B 404 . ? 1_555 ? 
59  AC7 18 HOH BA .   ? HOH B 408 . ? 1_555 ? 
60  AC7 18 HOH BA .   ? HOH B 569 . ? 1_555 ? 
61  AC8 7  LEU B  183 ? LEU B 183 . ? 1_555 ? 
62  AC8 7  PRO B  184 ? PRO B 184 . ? 1_555 ? 
63  AC8 7  GLU B  185 ? GLU B 185 . ? 1_555 ? 
64  AC8 7  VAL B  215 ? VAL B 215 . ? 1_555 ? 
65  AC8 7  HOH BA .   ? HOH B 414 . ? 1_555 ? 
66  AC8 7  HOH BA .   ? HOH B 502 . ? 1_555 ? 
67  AC8 7  HOH BA .   ? HOH B 544 . ? 1_555 ? 
68  AC9 9  SER B  42  ? SER B 42  . ? 1_555 ? 
69  AC9 9  THR B  44  ? THR B 44  . ? 1_555 ? 
70  AC9 9  LEU B  46  ? LEU B 46  . ? 1_555 ? 
71  AC9 9  GLY B  80  ? GLY B 80  . ? 1_555 ? 
72  AC9 9  LEU B  81  ? LEU B 81  . ? 1_555 ? 
73  AC9 9  TYR B  190 ? TYR B 190 . ? 1_555 ? 
74  AC9 9  ARG B  192 ? ARG B 192 . ? 1_555 ? 
75  AC9 9  HOH BA .   ? HOH B 409 . ? 1_555 ? 
76  AC9 9  HOH BA .   ? HOH B 578 . ? 1_555 ? 
77  AD1 5  ARG B  255 ? ARG B 255 . ? 1_555 ? 
78  AD1 5  LEU B  256 ? LEU B 256 . ? 1_555 ? 
79  AD1 5  TYR B  258 ? TYR B 258 . ? 1_555 ? 
80  AD1 5  HOH BA .   ? HOH B 510 . ? 1_555 ? 
81  AD1 5  HOH BA .   ? HOH B 564 . ? 1_555 ? 
82  AD2 5  ASN B  64  ? ASN B 64  . ? 1_555 ? 
83  AD2 5  LYS B  69  ? LYS B 69  . ? 1_555 ? 
84  AD2 5  GLN B  89  ? GLN B 89  . ? 1_555 ? 
85  AD2 5  EM5 K  .   ? EM5 B 302 . ? 1_555 ? 
86  AD2 5  HOH BA .   ? HOH B 453 . ? 1_555 ? 
87  AD3 4  HIS C  91  ? HIS C 91  . ? 1_555 ? 
88  AD3 4  HIS C  93  ? HIS C 93  . ? 1_555 ? 
89  AD3 4  HIS C  117 ? HIS C 117 . ? 1_555 ? 
90  AD3 4  EM5 Q  .   ? EM5 C 302 . ? 1_555 ? 
91  AD4 15 GLN C  89  ? GLN C 89  . ? 1_555 ? 
92  AD4 15 HIS C  91  ? HIS C 91  . ? 1_555 ? 
93  AD4 15 HIS C  93  ? HIS C 93  . ? 1_555 ? 
94  AD4 15 HIS C  117 ? HIS C 117 . ? 1_555 ? 
95  AD4 15 ALA C  129 ? ALA C 129 . ? 1_555 ? 
96  AD4 15 VAL C  141 ? VAL C 141 . ? 1_555 ? 
97  AD4 15 LEU C  197 ? LEU C 197 . ? 1_555 ? 
98  AD4 15 THR C  198 ? THR C 198 . ? 1_555 ? 
99  AD4 15 THR C  199 ? THR C 199 . ? 1_555 ? 
100 AD4 15 TRP C  208 ? TRP C 208 . ? 1_555 ? 
101 AD4 15 ZN  P  .   ? ZN  C 301 . ? 1_555 ? 
102 AD4 15 HOH CA .   ? HOH C 441 . ? 1_555 ? 
103 AD4 15 HOH CA .   ? HOH C 478 . ? 1_555 ? 
104 AD4 15 HOH CA .   ? HOH C 522 . ? 1_555 ? 
105 AD4 15 HOH CA .   ? HOH C 562 . ? 1_555 ? 
106 AD5 5  PRO C  201 ? PRO C 201 . ? 1_555 ? 
107 AD5 5  ASN C  203 ? ASN C 203 . ? 1_555 ? 
108 AD5 5  HOH CA .   ? HOH C 406 . ? 1_555 ? 
109 AD5 5  HOH CA .   ? HOH C 510 . ? 1_555 ? 
110 AD5 5  HOH CA .   ? HOH C 546 . ? 1_555 ? 
111 AD6 4  HIS D  91  ? HIS D 91  . ? 1_555 ? 
112 AD6 4  HIS D  93  ? HIS D 93  . ? 1_555 ? 
113 AD6 4  HIS D  117 ? HIS D 117 . ? 1_555 ? 
114 AD6 4  EM5 T  .   ? EM5 D 302 . ? 1_555 ? 
115 AD7 13 TRP D  4   ? TRP D 4   . ? 1_555 ? 
116 AD7 13 GLN D  89  ? GLN D 89  . ? 1_555 ? 
117 AD7 13 HIS D  91  ? HIS D 91  . ? 1_555 ? 
118 AD7 13 HIS D  93  ? HIS D 93  . ? 1_555 ? 
119 AD7 13 HIS D  117 ? HIS D 117 . ? 1_555 ? 
120 AD7 13 VAL D  141 ? VAL D 141 . ? 1_555 ? 
121 AD7 13 LEU D  197 ? LEU D 197 . ? 1_555 ? 
122 AD7 13 THR D  198 ? THR D 198 . ? 1_555 ? 
123 AD7 13 THR D  199 ? THR D 199 . ? 1_555 ? 
124 AD7 13 TRP D  208 ? TRP D 208 . ? 1_555 ? 
125 AD7 13 ZN  S  .   ? ZN  D 301 . ? 1_555 ? 
126 AD7 13 HOH DA .   ? HOH D 425 . ? 1_555 ? 
127 AD7 13 HOH DA .   ? HOH D 539 . ? 1_555 ? 
128 AD8 5  HIS D  33  ? HIS D 33  . ? 1_555 ? 
129 AD8 5  SER D  34  ? SER D 34  . ? 1_555 ? 
130 AD8 5  SER D  108 ? SER D 108 . ? 1_555 ? 
131 AD8 5  HOH DA .   ? HOH D 427 . ? 1_555 ? 
132 AD8 5  HOH DA .   ? HOH D 586 . ? 1_555 ? 
133 AD9 7  SER D  42  ? SER D 42  . ? 1_555 ? 
134 AD9 7  THR D  44  ? THR D 44  . ? 1_555 ? 
135 AD9 7  LEU D  46  ? LEU D 46  . ? 1_555 ? 
136 AD9 7  GLY D  80  ? GLY D 80  . ? 1_555 ? 
137 AD9 7  TYR D  190 ? TYR D 190 . ? 1_555 ? 
138 AD9 7  ARG D  192 ? ARG D 192 . ? 1_555 ? 
139 AD9 7  HOH DA .   ? HOH D 499 . ? 1_555 ? 
140 AE1 4  ASN D  134 ? ASN D 134 . ? 1_555 ? 
141 AE1 4  ASN D  203 ? ASN D 203 . ? 1_555 ? 
142 AE1 4  HOH DA .   ? HOH D 403 . ? 1_555 ? 
143 AE1 4  HOH DA .   ? HOH D 505 . ? 1_555 ? 
144 AE2 6  GLU A  171 ? GLU A 171 . ? 1_454 ? 
145 AE2 6  PHE A  173 ? PHE A 173 . ? 1_454 ? 
146 AE2 6  HIS D  164 ? HIS D 164 . ? 1_555 ? 
147 AE2 6  ALA D  172 ? ALA D 172 . ? 1_555 ? 
148 AE2 6  PHE D  173 ? PHE D 173 . ? 1_555 ? 
149 AE2 6  HOH DA .   ? HOH D 424 . ? 1_555 ? 
150 AE3 7  LEU D  26  ? LEU D 26  . ? 1_555 ? 
151 AE3 7  ARG D  194 ? ARG D 194 . ? 1_555 ? 
152 AE3 7  ARG D  255 ? ARG D 255 . ? 1_555 ? 
153 AE3 7  LEU D  256 ? LEU D 256 . ? 1_555 ? 
154 AE3 7  TYR D  258 ? TYR D 258 . ? 1_555 ? 
155 AE3 7  HOH DA .   ? HOH D 480 . ? 1_555 ? 
156 AE3 7  HOH DA .   ? HOH D 532 . ? 1_555 ? 
157 AE4 5  LYS D  251 ? LYS D 251 . ? 1_555 ? 
158 AE4 5  PHE D  252 ? PHE D 252 . ? 1_555 ? 
159 AE4 5  ASP D  253 ? ASP D 253 . ? 1_555 ? 
160 AE4 5  HOH DA .   ? HOH D 402 . ? 1_555 ? 
161 AE4 5  HOH DA .   ? HOH D 461 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   6G5L 
_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 OD2 C ASP 253 ? A O C HOH 401 ? ? 1.93 
2 1 O   A HOH 631 ? ? O B HOH 608 ? ? 2.11 
3 1 OG  B SER 16  ? ? O B HOH 401 ? ? 2.11 
4 1 OD2 B ASP 253 ? ? O B HOH 402 ? ? 2.14 
5 1 O   D HOH 601 ? ? O D HOH 627 ? ? 2.17 
6 1 O17 A EM5 302 ? A O A HOH 401 ? ? 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_1            C 
_pdbx_validate_rmsd_bond.auth_comp_id_1            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             93 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CD2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            C 
_pdbx_validate_rmsd_bond.auth_comp_id_2            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             93 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.434 
_pdbx_validate_rmsd_bond.bond_target_value         1.354 
_pdbx_validate_rmsd_bond.bond_deviation            0.080 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.009 
_pdbx_validate_rmsd_bond.linker_flag               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 CB B LEU 256 ? ? CG B LEU 256 ? ? CD1 B LEU 256 ? ? 99.39  111.00 -11.61 1.70 N 
2 1 CB C ASP 253 ? B CG C ASP 253 ? B OD1 C ASP 253 ? B 125.56 118.30 7.26   0.90 N 
# 
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  ? ? -153.41 78.84   
2  1 ASN A 245 ? ? -94.91  53.73   
3  1 ASN B 245 ? ? -94.41  53.93   
4  1 PHE C 7   ? ? -152.02 -157.15 
5  1 ASP C 99  ? ? -151.61 77.41   
6  1 ASN C 245 ? ? -94.91  51.44   
7  1 PHE C 252 ? B -152.83 89.47   
8  1 LEU D 26  ? ? 73.21   39.47   
9  1 ASN D 245 ? ? -94.42  55.59   
10 1 GLU D 254 ? ? 76.33   -0.02   
# 
_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            -142.06 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ILE 
_pdbx_validate_main_chain_plane.auth_asym_id             C 
_pdbx_validate_main_chain_plane.auth_seq_id              158 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   11.49 
# 
_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 ? A HOH 684 ? 6.21 . 
2 1 O ? D HOH 662 ? 5.94 . 
# 
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 C SER 2 ? C SER 2 
7 1 Y 1 D MET 1 ? D MET 1 
8 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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
EM5 C6   C  Y N 98  
EM5 C7   C  Y N 99  
EM5 C8   C  Y N 100 
EM5 C9   C  Y N 101 
EM5 C10  C  Y N 102 
EM5 C12  C  N N 103 
EM5 C2   C  Y N 104 
EM5 N5   N  N N 105 
EM5 C15  C  N N 106 
EM5 C16  C  N N 107 
EM5 O13  O  N N 108 
EM5 N14  N  N N 109 
EM5 O17  O  N N 110 
EM5 S1   S  N N 111 
EM5 O4   O  N N 112 
EM5 O3   O  N N 113 
EM5 CL1  CL N N 114 
EM5 N18  N  N N 115 
EM5 C19  C  N N 116 
EM5 C23  C  N N 117 
EM5 C24  C  N N 118 
EM5 C22  C  N N 119 
EM5 C21  C  N N 120 
EM5 C20  C  N N 121 
EM5 H1   H  N N 122 
EM5 H2   H  N N 123 
EM5 H3   H  N N 124 
EM5 H4   H  N N 125 
EM5 H5   H  N N 126 
EM5 H6   H  N N 127 
EM5 H7   H  N N 128 
EM5 H8   H  N N 129 
EM5 H9   H  N N 130 
EM5 H10  H  N N 131 
EM5 H11  H  N N 132 
EM5 H12  H  N N 133 
EM5 H13  H  N N 134 
EM5 H14  H  N N 135 
EM5 H15  H  N N 136 
EM5 H16  H  N N 137 
EM5 H17  H  N N 138 
EM5 H18  H  N N 139 
EM5 H19  H  N N 140 
EM5 H20  H  N N 141 
EM5 H21  H  N N 142 
EM5 H22  H  N N 143 
GLN N    N  N N 144 
GLN CA   C  N S 145 
GLN C    C  N N 146 
GLN O    O  N N 147 
GLN CB   C  N N 148 
GLN CG   C  N N 149 
GLN CD   C  N N 150 
GLN OE1  O  N N 151 
GLN NE2  N  N N 152 
GLN OXT  O  N N 153 
GLN H    H  N N 154 
GLN H2   H  N N 155 
GLN HA   H  N N 156 
GLN HB2  H  N N 157 
GLN HB3  H  N N 158 
GLN HG2  H  N N 159 
GLN HG3  H  N N 160 
GLN HE21 H  N N 161 
GLN HE22 H  N N 162 
GLN HXT  H  N N 163 
GLU N    N  N N 164 
GLU CA   C  N S 165 
GLU C    C  N N 166 
GLU O    O  N N 167 
GLU CB   C  N N 168 
GLU CG   C  N N 169 
GLU CD   C  N N 170 
GLU OE1  O  N N 171 
GLU OE2  O  N N 172 
GLU OXT  O  N N 173 
GLU H    H  N N 174 
GLU H2   H  N N 175 
GLU HA   H  N N 176 
GLU HB2  H  N N 177 
GLU HB3  H  N N 178 
GLU HG2  H  N N 179 
GLU HG3  H  N N 180 
GLU HE2  H  N N 181 
GLU HXT  H  N N 182 
GLY N    N  N N 183 
GLY CA   C  N N 184 
GLY C    C  N N 185 
GLY O    O  N N 186 
GLY OXT  O  N N 187 
GLY H    H  N N 188 
GLY H2   H  N N 189 
GLY HA2  H  N N 190 
GLY HA3  H  N N 191 
GLY HXT  H  N N 192 
HIS N    N  N N 193 
HIS CA   C  N S 194 
HIS C    C  N N 195 
HIS O    O  N N 196 
HIS CB   C  N N 197 
HIS CG   C  Y N 198 
HIS ND1  N  Y N 199 
HIS CD2  C  Y N 200 
HIS CE1  C  Y N 201 
HIS NE2  N  Y N 202 
HIS OXT  O  N N 203 
HIS H    H  N N 204 
HIS H2   H  N N 205 
HIS HA   H  N N 206 
HIS HB2  H  N N 207 
HIS HB3  H  N N 208 
HIS HD1  H  N N 209 
HIS HD2  H  N N 210 
HIS HE1  H  N N 211 
HIS HE2  H  N N 212 
HIS HXT  H  N N 213 
HOH O    O  N N 214 
HOH H1   H  N N 215 
HOH H2   H  N N 216 
ILE N    N  N N 217 
ILE CA   C  N S 218 
ILE C    C  N N 219 
ILE O    O  N N 220 
ILE CB   C  N S 221 
ILE CG1  C  N N 222 
ILE CG2  C  N N 223 
ILE CD1  C  N N 224 
ILE OXT  O  N N 225 
ILE H    H  N N 226 
ILE H2   H  N N 227 
ILE HA   H  N N 228 
ILE HB   H  N N 229 
ILE HG12 H  N N 230 
ILE HG13 H  N N 231 
ILE HG21 H  N N 232 
ILE HG22 H  N N 233 
ILE HG23 H  N N 234 
ILE HD11 H  N N 235 
ILE HD12 H  N N 236 
ILE HD13 H  N N 237 
ILE HXT  H  N N 238 
LEU N    N  N N 239 
LEU CA   C  N S 240 
LEU C    C  N N 241 
LEU O    O  N N 242 
LEU CB   C  N N 243 
LEU CG   C  N N 244 
LEU CD1  C  N N 245 
LEU CD2  C  N N 246 
LEU OXT  O  N N 247 
LEU H    H  N N 248 
LEU H2   H  N N 249 
LEU HA   H  N N 250 
LEU HB2  H  N N 251 
LEU HB3  H  N N 252 
LEU HG   H  N N 253 
LEU HD11 H  N N 254 
LEU HD12 H  N N 255 
LEU HD13 H  N N 256 
LEU HD21 H  N N 257 
LEU HD22 H  N N 258 
LEU HD23 H  N N 259 
LEU HXT  H  N N 260 
LYS N    N  N N 261 
LYS CA   C  N S 262 
LYS C    C  N N 263 
LYS O    O  N N 264 
LYS CB   C  N N 265 
LYS CG   C  N N 266 
LYS CD   C  N N 267 
LYS CE   C  N N 268 
LYS NZ   N  N N 269 
LYS OXT  O  N N 270 
LYS H    H  N N 271 
LYS H2   H  N N 272 
LYS HA   H  N N 273 
LYS HB2  H  N N 274 
LYS HB3  H  N N 275 
LYS HG2  H  N N 276 
LYS HG3  H  N N 277 
LYS HD2  H  N N 278 
LYS HD3  H  N N 279 
LYS HE2  H  N N 280 
LYS HE3  H  N N 281 
LYS HZ1  H  N N 282 
LYS HZ2  H  N N 283 
LYS HZ3  H  N N 284 
LYS HXT  H  N N 285 
MET N    N  N N 286 
MET CA   C  N S 287 
MET C    C  N N 288 
MET O    O  N N 289 
MET CB   C  N N 290 
MET CG   C  N N 291 
MET SD   S  N N 292 
MET CE   C  N N 293 
MET OXT  O  N N 294 
MET H    H  N N 295 
MET H2   H  N N 296 
MET HA   H  N N 297 
MET HB2  H  N N 298 
MET HB3  H  N N 299 
MET HG2  H  N N 300 
MET HG3  H  N N 301 
MET HE1  H  N N 302 
MET HE2  H  N N 303 
MET HE3  H  N N 304 
MET HXT  H  N N 305 
PEG C1   C  N N 306 
PEG O1   O  N N 307 
PEG C2   C  N N 308 
PEG O2   O  N N 309 
PEG C3   C  N N 310 
PEG C4   C  N N 311 
PEG O4   O  N N 312 
PEG H11  H  N N 313 
PEG H12  H  N N 314 
PEG HO1  H  N N 315 
PEG H21  H  N N 316 
PEG H22  H  N N 317 
PEG H31  H  N N 318 
PEG H32  H  N N 319 
PEG H41  H  N N 320 
PEG H42  H  N N 321 
PEG HO4  H  N N 322 
PHE N    N  N N 323 
PHE CA   C  N S 324 
PHE C    C  N N 325 
PHE O    O  N N 326 
PHE CB   C  N N 327 
PHE CG   C  Y N 328 
PHE CD1  C  Y N 329 
PHE CD2  C  Y N 330 
PHE CE1  C  Y N 331 
PHE CE2  C  Y N 332 
PHE CZ   C  Y N 333 
PHE OXT  O  N N 334 
PHE H    H  N N 335 
PHE H2   H  N N 336 
PHE HA   H  N N 337 
PHE HB2  H  N N 338 
PHE HB3  H  N N 339 
PHE HD1  H  N N 340 
PHE HD2  H  N N 341 
PHE HE1  H  N N 342 
PHE HE2  H  N N 343 
PHE HZ   H  N N 344 
PHE HXT  H  N N 345 
PRO N    N  N N 346 
PRO CA   C  N S 347 
PRO C    C  N N 348 
PRO O    O  N N 349 
PRO CB   C  N N 350 
PRO CG   C  N N 351 
PRO CD   C  N N 352 
PRO OXT  O  N N 353 
PRO H    H  N N 354 
PRO HA   H  N N 355 
PRO HB2  H  N N 356 
PRO HB3  H  N N 357 
PRO HG2  H  N N 358 
PRO HG3  H  N N 359 
PRO HD2  H  N N 360 
PRO HD3  H  N N 361 
PRO HXT  H  N N 362 
SER N    N  N N 363 
SER CA   C  N S 364 
SER C    C  N N 365 
SER O    O  N N 366 
SER CB   C  N N 367 
SER OG   O  N N 368 
SER OXT  O  N N 369 
SER H    H  N N 370 
SER H2   H  N N 371 
SER HA   H  N N 372 
SER HB2  H  N N 373 
SER HB3  H  N N 374 
SER HG   H  N N 375 
SER HXT  H  N N 376 
THR N    N  N N 377 
THR CA   C  N S 378 
THR C    C  N N 379 
THR O    O  N N 380 
THR CB   C  N R 381 
THR OG1  O  N N 382 
THR CG2  C  N N 383 
THR OXT  O  N N 384 
THR H    H  N N 385 
THR H2   H  N N 386 
THR HA   H  N N 387 
THR HB   H  N N 388 
THR HG1  H  N N 389 
THR HG21 H  N N 390 
THR HG22 H  N N 391 
THR HG23 H  N N 392 
THR HXT  H  N N 393 
TRP N    N  N N 394 
TRP CA   C  N S 395 
TRP C    C  N N 396 
TRP O    O  N N 397 
TRP CB   C  N N 398 
TRP CG   C  Y N 399 
TRP CD1  C  Y N 400 
TRP CD2  C  Y N 401 
TRP NE1  N  Y N 402 
TRP CE2  C  Y N 403 
TRP CE3  C  Y N 404 
TRP CZ2  C  Y N 405 
TRP CZ3  C  Y N 406 
TRP CH2  C  Y N 407 
TRP OXT  O  N N 408 
TRP H    H  N N 409 
TRP H2   H  N N 410 
TRP HA   H  N N 411 
TRP HB2  H  N N 412 
TRP HB3  H  N N 413 
TRP HD1  H  N N 414 
TRP HE1  H  N N 415 
TRP HE3  H  N N 416 
TRP HZ2  H  N N 417 
TRP HZ3  H  N N 418 
TRP HH2  H  N N 419 
TRP HXT  H  N N 420 
TYR N    N  N N 421 
TYR CA   C  N S 422 
TYR C    C  N N 423 
TYR O    O  N N 424 
TYR CB   C  N N 425 
TYR CG   C  Y N 426 
TYR CD1  C  Y N 427 
TYR CD2  C  Y N 428 
TYR CE1  C  Y N 429 
TYR CE2  C  Y N 430 
TYR CZ   C  Y N 431 
TYR OH   O  N N 432 
TYR OXT  O  N N 433 
TYR H    H  N N 434 
TYR H2   H  N N 435 
TYR HA   H  N N 436 
TYR HB2  H  N N 437 
TYR HB3  H  N N 438 
TYR HD1  H  N N 439 
TYR HD2  H  N N 440 
TYR HE1  H  N N 441 
TYR HE2  H  N N 442 
TYR HH   H  N N 443 
TYR HXT  H  N N 444 
VAL N    N  N N 445 
VAL CA   C  N S 446 
VAL C    C  N N 447 
VAL O    O  N N 448 
VAL CB   C  N N 449 
VAL CG1  C  N N 450 
VAL CG2  C  N N 451 
VAL OXT  O  N N 452 
VAL H    H  N N 453 
VAL H2   H  N N 454 
VAL HA   H  N N 455 
VAL HB   H  N N 456 
VAL HG11 H  N N 457 
VAL HG12 H  N N 458 
VAL HG13 H  N N 459 
VAL HG21 H  N N 460 
VAL HG22 H  N N 461 
VAL HG23 H  N N 462 
VAL HXT  H  N N 463 
ZN  ZN   ZN N N 464 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
EM5 CL1 C6   sing N N 92  
EM5 O4  S1   doub N N 93  
EM5 C21 C22  sing N N 94  
EM5 C21 C20  sing N N 95  
EM5 C6  C7   doub Y N 96  
EM5 C6  C2   sing Y N 97  
EM5 C7  C8   sing Y N 98  
EM5 C22 C24  sing N N 99  
EM5 C24 C23  sing N N 100 
EM5 S1  O3   doub N N 101 
EM5 S1  C2   sing N N 102 
EM5 S1  N5   sing N N 103 
EM5 C19 C20  sing N N 104 
EM5 C19 C23  sing N N 105 
EM5 C19 N18  sing N N 106 
EM5 C2  C10  doub Y N 107 
EM5 C8  N18  sing N N 108 
EM5 C8  C9   doub Y N 109 
EM5 C10 C9   sing Y N 110 
EM5 C9  C12  sing N N 111 
EM5 C12 N14  sing N N 112 
EM5 C12 O13  doub N N 113 
EM5 N14 C15  sing N N 114 
EM5 C15 C16  sing N N 115 
EM5 C16 O17  sing N N 116 
EM5 C7  H1   sing N N 117 
EM5 C10 H2   sing N N 118 
EM5 N5  H3   sing N N 119 
EM5 N5  H4   sing N N 120 
EM5 C15 H5   sing N N 121 
EM5 C15 H6   sing N N 122 
EM5 C16 H7   sing N N 123 
EM5 C16 H8   sing N N 124 
EM5 N14 H9   sing N N 125 
EM5 O17 H10  sing N N 126 
EM5 N18 H11  sing N N 127 
EM5 C19 H12  sing N N 128 
EM5 C23 H13  sing N N 129 
EM5 C23 H14  sing N N 130 
EM5 C24 H15  sing N N 131 
EM5 C24 H16  sing N N 132 
EM5 C22 H17  sing N N 133 
EM5 C22 H18  sing N N 134 
EM5 C21 H19  sing N N 135 
EM5 C21 H20  sing N N 136 
EM5 C20 H21  sing N N 137 
EM5 C20 H22  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   1JD0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6G5L 
_atom_sites.fract_transf_matrix[1][1]   0.012966 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004373 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013471 
_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]   0.011530 
_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  
CL 
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   ? 17.096  16.543  19.349  1.00 45.93  ? 3   LYS A N   1 
ATOM   2    C  CA  . LYS A  1 3   ? 17.290  16.321  17.913  1.00 40.68  ? 3   LYS A CA  1 
ATOM   3    C  C   . LYS A  1 3   ? 16.481  15.046  17.753  1.00 40.17  ? 3   LYS A C   1 
ATOM   4    O  O   . LYS A  1 3   ? 15.351  14.935  18.346  1.00 47.76  ? 3   LYS A O   1 
ATOM   5    C  CB  . LYS A  1 3   ? 18.795  16.189  17.577  1.00 53.44  ? 3   LYS A CB  1 
ATOM   6    C  CG  . LYS A  1 3   ? 19.213  16.569  16.127  1.00 47.51  ? 3   LYS A CG  1 
ATOM   7    N  N   . TRP A  1 4   ? 17.070  14.036  17.200  1.00 18.92  ? 4   TRP A N   1 
ATOM   8    C  CA  . TRP A  1 4   ? 16.260  12.986  16.622  1.00 15.89  ? 4   TRP A CA  1 
ATOM   9    C  C   . TRP A  1 4   ? 16.218  11.882  17.611  1.00 16.11  ? 4   TRP A C   1 
ATOM   10   O  O   . TRP A  1 4   ? 17.163  11.644  18.405  1.00 17.60  ? 4   TRP A O   1 
ATOM   11   C  CB  . TRP A  1 4   ? 16.791  12.614  15.261  1.00 14.98  ? 4   TRP A CB  1 
ATOM   12   C  CG  . TRP A  1 4   ? 18.141  11.965  15.235  1.00 13.49  ? 4   TRP A CG  1 
ATOM   13   C  CD1 . TRP A  1 4   ? 19.346  12.586  15.100  1.00 15.71  ? 4   TRP A CD1 1 
ATOM   14   C  CD2 . TRP A  1 4   ? 18.408  10.553  15.336  1.00 12.68  ? 4   TRP A CD2 1 
ATOM   15   N  NE1 . TRP A  1 4   ? 20.342  11.645  15.026  1.00 15.73  ? 4   TRP A NE1 1 
ATOM   16   C  CE2 . TRP A  1 4   ? 19.801  10.397  15.230  1.00 13.23  ? 4   TRP A CE2 1 
ATOM   17   C  CE3 . TRP A  1 4   ? 17.605  9.416   15.505  1.00 12.63  ? 4   TRP A CE3 1 
ATOM   18   C  CZ2 . TRP A  1 4   ? 20.412  9.136   15.269  1.00 14.74  ? 4   TRP A CZ2 1 
ATOM   19   C  CZ3 . TRP A  1 4   ? 18.185  8.137   15.504  1.00 13.75  ? 4   TRP A CZ3 1 
ATOM   20   C  CH2 . TRP A  1 4   ? 19.587  8.025   15.396  1.00 13.55  ? 4   TRP A CH2 1 
ATOM   21   N  N   . THR A  1 5   ? 15.100  11.120  17.551  1.00 15.51  ? 5   THR A N   1 
ATOM   22   C  CA  . THR A  1 5   ? 14.868  10.027  18.456  1.00 15.89  ? 5   THR A CA  1 
ATOM   23   C  C   . THR A  1 5   ? 14.188  8.939   17.659  1.00 12.99  ? 5   THR A C   1 
ATOM   24   O  O   . THR A  1 5   ? 13.911  9.007   16.477  1.00 13.41  ? 5   THR A O   1 
ATOM   25   C  CB  . THR A  1 5   ? 13.925  10.396  19.646  1.00 17.44  ? 5   THR A CB  1 
ATOM   26   O  OG1 . THR A  1 5   ? 12.616  10.570  19.037  1.00 19.65  ? 5   THR A OG1 1 
ATOM   27   C  CG2 . THR A  1 5   ? 14.436  11.611  20.456  1.00 21.40  ? 5   THR A CG2 1 
ATOM   28   N  N   . TYR A  1 6   ? 13.860  7.807   18.381  1.00 15.22  ? 6   TYR A N   1 
ATOM   29   C  CA  . TYR A  1 6   ? 13.066  6.739   17.802  1.00 14.84  ? 6   TYR A CA  1 
ATOM   30   C  C   . TYR A  1 6   ? 11.635  6.756   18.361  1.00 15.05  ? 6   TYR A C   1 
ATOM   31   O  O   . TYR A  1 6   ? 10.916  5.785   18.208  1.00 16.59  ? 6   TYR A O   1 
ATOM   32   C  CB  . TYR A  1 6   ? 13.690  5.370   18.084  1.00 17.53  ? 6   TYR A CB  1 
ATOM   33   C  CG  . TYR A  1 6   ? 14.946  5.112   17.283  1.00 13.57  ? 6   TYR A CG  1 
ATOM   34   C  CD1 . TYR A  1 6   ? 14.873  4.574   15.997  1.00 13.01  ? 6   TYR A CD1 1 
ATOM   35   C  CD2 . TYR A  1 6   ? 16.184  5.404   17.833  1.00 15.61  ? 6   TYR A CD2 1 
ATOM   36   C  CE1 . TYR A  1 6   ? 16.029  4.308   15.281  1.00 11.90  ? 6   TYR A CE1 1 
ATOM   37   C  CE2 . TYR A  1 6   ? 17.333  5.118   17.149  1.00 15.29  ? 6   TYR A CE2 1 
ATOM   38   C  CZ  . TYR A  1 6   ? 17.264  4.564   15.856  1.00 12.90  ? 6   TYR A CZ  1 
ATOM   39   O  OH  . TYR A  1 6   ? 18.421  4.247   15.174  1.00 12.63  ? 6   TYR A OH  1 
ATOM   40   N  N   . PHE A  1 7   ? 11.135  7.807   18.929  1.00 24.54  ? 7   PHE A N   1 
ATOM   41   C  CA  . PHE A  1 7   ? 9.804   7.833   19.422  1.00 27.84  ? 7   PHE A CA  1 
ATOM   42   C  C   . PHE A  1 7   ? 9.351   9.240   19.613  1.00 32.81  ? 7   PHE A C   1 
ATOM   43   O  O   . PHE A  1 7   ? 10.056  10.166  19.478  1.00 36.26  ? 7   PHE A O   1 
ATOM   44   C  CB  . PHE A  1 7   ? 9.710   7.194   20.785  1.00 49.62  ? 7   PHE A CB  1 
ATOM   45   C  CG  . PHE A  1 7   ? 10.259  8.159   21.856  1.00 44.46  ? 7   PHE A CG  1 
ATOM   46   C  CD1 . PHE A  1 7   ? 11.654  8.429   21.894  1.00 42.51  ? 7   PHE A CD1 1 
ATOM   47   C  CD2 . PHE A  1 7   ? 9.416   8.826   22.800  1.00 62.05  ? 7   PHE A CD2 1 
ATOM   48   C  CE1 . PHE A  1 7   ? 12.211  9.350   22.786  1.00 42.28  ? 7   PHE A CE1 1 
ATOM   49   C  CE2 . PHE A  1 7   ? 9.973   9.743   23.694  1.00 80.20  ? 7   PHE A CE2 1 
ATOM   50   C  CZ  . PHE A  1 7   ? 11.367  9.997   23.693  1.00 69.87  ? 7   PHE A CZ  1 
ATOM   51   N  N   . GLY A  1 8   ? 8.112   9.433   20.108  1.00 29.18  ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A  1 8   ? 7.565   10.769  20.412  1.00 27.14  ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A  1 8   ? 7.507   11.693  19.197  1.00 30.65  ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A  1 8   ? 7.588   11.148  18.060  1.00 33.33  ? 8   GLY A O   1 
ATOM   55   N  N   . PRO A  1 9   ? 7.704   12.967  19.339  1.00 25.26  ? 9   PRO A N   1 
ATOM   56   C  CA  . PRO A  1 9   ? 7.420   13.752  18.138  1.00 28.48  ? 9   PRO A CA  1 
ATOM   57   C  C   . PRO A  1 9   ? 8.720   13.982  17.382  1.00 25.03  ? 9   PRO A C   1 
ATOM   58   O  O   . PRO A  1 9   ? 8.664   14.531  16.310  1.00 22.83  ? 9   PRO A O   1 
ATOM   59   C  CB  . PRO A  1 9   ? 6.705   15.061  18.611  1.00 32.66  ? 9   PRO A CB  1 
ATOM   60   C  CG  . PRO A  1 9   ? 7.454   15.196  19.795  1.00 28.57  ? 9   PRO A CG  1 
ATOM   61   C  CD  . PRO A  1 9   ? 7.515   13.801  20.533  1.00 33.06  ? 9   PRO A CD  1 
ATOM   62   N  N   . ASP A  1 10  ? 9.883   13.523  17.895  1.00 23.38  ? 10  ASP A N   1 
ATOM   63   C  CA  . ASP A  1 10  ? 11.115  13.632  17.138  1.00 19.81  ? 10  ASP A CA  1 
ATOM   64   C  C   . ASP A  1 10  ? 11.594  12.293  16.535  1.00 16.13  ? 10  ASP A C   1 
ATOM   65   O  O   . ASP A  1 10  ? 12.793  12.151  16.064  1.00 16.90  ? 10  ASP A O   1 
ATOM   66   C  CB  . ASP A  1 10  ? 12.254  14.207  18.072  1.00 23.27  ? 10  ASP A CB  1 
ATOM   67   C  CG  . ASP A  1 10  ? 11.955  15.614  18.521  1.00 36.85  ? 10  ASP A CG  1 
ATOM   68   O  OD1 . ASP A  1 10  ? 11.490  16.392  17.670  1.00 38.58  ? 10  ASP A OD1 1 
ATOM   69   O  OD2 . ASP A  1 10  ? 12.186  15.889  19.730  1.00 44.53  ? 10  ASP A OD2 1 
ATOM   70   N  N   . GLY A  1 11  ? 10.686  11.346  16.438  1.00 16.92  ? 11  GLY A N   1 
ATOM   71   C  CA  . GLY A  1 11  ? 10.828  10.019  15.930  1.00 14.31  ? 11  GLY A CA  1 
ATOM   72   C  C   . GLY A  1 11  ? 10.916  9.994   14.435  1.00 12.30  ? 11  GLY A C   1 
ATOM   73   O  O   . GLY A  1 11  ? 10.911  11.025  13.711  1.00 13.11  ? 11  GLY A O   1 
ATOM   74   N  N   . GLU A  1 12  ? 10.946  8.752   13.883  1.00 12.15  ? 12  GLU A N   1 
ATOM   75   C  CA  . GLU A  1 12  ? 11.405  8.559   12.507  1.00 11.00  ? 12  GLU A CA  1 
ATOM   76   C  C   . GLU A  1 12  ? 10.516  9.210   11.471  1.00 10.57  ? 12  GLU A C   1 
ATOM   77   O  O   . GLU A  1 12  ? 11.010  9.539   10.389  1.00 11.06  ? 12  GLU A O   1 
ATOM   78   C  CB  . GLU A  1 12  ? 11.610  7.059   12.221  1.00 11.14  ? 12  GLU A CB  1 
ATOM   79   C  CG  . GLU A  1 12  ? 10.274  6.272   12.171  1.00 11.17  ? 12  GLU A CG  1 
ATOM   80   C  CD  . GLU A  1 12  ? 10.566  4.784   12.307  1.00 10.59  ? 12  GLU A CD  1 
ATOM   81   O  OE1 . GLU A  1 12  ? 10.816  4.128   11.323  1.00 10.46  ? 12  GLU A OE1 1 
ATOM   82   O  OE2 . GLU A  1 12  ? 10.562  4.344   13.501  1.00 12.76  ? 12  GLU A OE2 1 
ATOM   83   N  N   . ASN A  1 13  ? 9.179   9.382   11.719  1.00 10.97  ? 13  ASN A N   1 
ATOM   84   C  CA  . ASN A  1 13  ? 8.384   10.032  10.698  1.00 10.77  ? 13  ASN A CA  1 
ATOM   85   C  C   . ASN A  1 13  ? 8.699   11.520  10.528  1.00 10.63  ? 13  ASN A C   1 
ATOM   86   O  O   . ASN A  1 13  ? 8.281   12.107  9.574   1.00 11.97  ? 13  ASN A O   1 
ATOM   87   C  CB  . ASN A  1 13  ? 6.883   9.904   11.024  1.00 11.32  ? 13  ASN A CB  1 
ATOM   88   C  CG  . ASN A  1 13  ? 6.378   8.482   10.889  1.00 10.55  ? 13  ASN A CG  1 
ATOM   89   O  OD1 . ASN A  1 13  ? 7.097   7.591   10.392  1.00 11.70  ? 13  ASN A OD1 1 
ATOM   90   N  ND2 . ASN A  1 13  ? 5.159   8.239   11.334  1.00 11.11  ? 13  ASN A ND2 1 
ATOM   91   N  N   . SER A  1 14  ? 9.419   12.072  11.543  1.00 11.30  ? 14  SER A N   1 
ATOM   92   C  CA  . SER A  1 14  ? 9.812   13.495  11.489  1.00 11.50  ? 14  SER A CA  1 
ATOM   93   C  C   . SER A  1 14  ? 11.252  13.711  11.098  1.00 11.34  ? 14  SER A C   1 
ATOM   94   O  O   . SER A  1 14  ? 11.625  14.895  10.922  1.00 12.35  ? 14  SER A O   1 
ATOM   95   C  CB  . SER A  1 14  ? 9.591   14.100  12.916  1.00 15.14  ? 14  SER A CB  1 
ATOM   96   O  OG  . SER A  1 14  ? 8.157   14.184  13.116  1.00 21.65  ? 14  SER A OG  1 
ATOM   97   N  N   . TRP A  1 15  ? 12.045  12.667  10.932  1.00 10.47  ? 15  TRP A N   1 
ATOM   98   C  CA  . TRP A  1 15  ? 13.483  12.877  10.594  1.00 10.32  ? 15  TRP A CA  1 
ATOM   99   C  C   . TRP A  1 15  ? 13.607  13.731  9.327   1.00 11.01  ? 15  TRP A C   1 
ATOM   100  O  O   . TRP A  1 15  ? 14.582  14.492  9.248   1.00 10.98  ? 15  TRP A O   1 
ATOM   101  C  CB  . TRP A  1 15  ? 14.164  11.534  10.376  1.00 10.64  ? 15  TRP A CB  1 
ATOM   102  C  CG  . TRP A  1 15  ? 14.311  10.706  11.614  1.00 10.16  ? 15  TRP A CG  1 
ATOM   103  C  CD1 . TRP A  1 15  ? 14.072  11.028  12.915  1.00 11.12  ? 15  TRP A CD1 1 
ATOM   104  C  CD2 . TRP A  1 15  ? 14.757  9.353   11.618  1.00 9.92   ? 15  TRP A CD2 1 
ATOM   105  N  NE1 . TRP A  1 15  ? 14.335  9.963   13.758  1.00 11.51  ? 15  TRP A NE1 1 
ATOM   106  C  CE2 . TRP A  1 15  ? 14.795  8.917   12.948  1.00 10.50  ? 15  TRP A CE2 1 
ATOM   107  C  CE3 . TRP A  1 15  ? 15.192  8.495   10.595  1.00 10.31  ? 15  TRP A CE3 1 
ATOM   108  C  CZ2 . TRP A  1 15  ? 15.217  7.591   13.324  1.00 10.57  ? 15  TRP A CZ2 1 
ATOM   109  C  CZ3 . TRP A  1 15  ? 15.619  7.178   10.945  1.00 10.71  ? 15  TRP A CZ3 1 
ATOM   110  C  CH2 . TRP A  1 15  ? 15.607  6.785   12.269  1.00 10.68  ? 15  TRP A CH2 1 
ATOM   111  N  N   . SER A  1 16  ? 12.744  13.546  8.346   1.00 10.51  ? 16  SER A N   1 
ATOM   112  C  CA  . SER A  1 16  ? 12.920  14.198  7.079   1.00 11.33  ? 16  SER A CA  1 
ATOM   113  C  C   . SER A  1 16  ? 12.811  15.717  7.143   1.00 11.74  ? 16  SER A C   1 
ATOM   114  O  O   . SER A  1 16  ? 13.242  16.392  6.191   1.00 12.06  ? 16  SER A O   1 
ATOM   115  C  CB  . SER A  1 16  ? 11.929  13.672  6.025   1.00 11.95  ? 16  SER A CB  1 
ATOM   116  O  OG  . SER A  1 16  ? 10.608  14.093  6.502   1.00 14.11  ? 16  SER A OG  1 
ATOM   117  N  N   A LYS A  1 17  ? 12.340  16.244  8.321   0.50 11.72  ? 17  LYS A N   1 
ATOM   118  N  N   B LYS A  1 17  ? 12.246  16.287  8.145   0.50 10.71  ? 17  LYS A N   1 
ATOM   119  C  CA  A LYS A  1 17  ? 12.187  17.749  8.587   0.50 10.60  ? 17  LYS A CA  1 
ATOM   120  C  CA  B LYS A  1 17  ? 12.273  17.744  8.135   0.50 9.64   ? 17  LYS A CA  1 
ATOM   121  C  C   A LYS A  1 17  ? 13.559  18.394  8.619   0.50 11.56  ? 17  LYS A C   1 
ATOM   122  C  C   B LYS A  1 17  ? 13.733  18.262  8.239   0.50 9.46   ? 17  LYS A C   1 
ATOM   123  O  O   A LYS A  1 17  ? 13.804  19.372  8.001   0.50 11.71  ? 17  LYS A O   1 
ATOM   124  O  O   B LYS A  1 17  ? 14.106  19.135  7.424   0.50 9.47   ? 17  LYS A O   1 
ATOM   125  C  CB  A LYS A  1 17  ? 11.455  18.046  9.901   0.50 11.62  ? 17  LYS A CB  1 
ATOM   126  C  CB  B LYS A  1 17  ? 11.461  18.240  9.327   0.50 9.90   ? 17  LYS A CB  1 
ATOM   127  C  CG  A LYS A  1 17  ? 10.028  17.671  9.709   0.50 16.68  ? 17  LYS A CG  1 
ATOM   128  C  CG  B LYS A  1 17  ? 11.401  19.723  9.516   0.50 13.32  ? 17  LYS A CG  1 
ATOM   129  C  CD  A LYS A  1 17  ? 9.452   17.874  11.043  0.50 19.47  ? 17  LYS A CD  1 
ATOM   130  C  CD  B LYS A  1 17  ? 10.540  20.152  10.668  0.50 14.72  ? 17  LYS A CD  1 
ATOM   131  C  CE  A LYS A  1 17  ? 8.131   17.135  11.154  0.50 22.36  ? 17  LYS A CE  1 
ATOM   132  C  CE  B LYS A  1 17  ? 9.051   19.947  10.514  0.50 16.42  ? 17  LYS A CE  1 
ATOM   133  N  NZ  A LYS A  1 17  ? 7.508   17.425  12.543  0.50 23.65  ? 17  LYS A NZ  1 
ATOM   134  N  NZ  B LYS A  1 17  ? 8.276   20.250  11.715  0.50 17.74  ? 17  LYS A NZ  1 
ATOM   135  N  N   . LYS A  1 18  ? 14.514  17.806  9.291   1.00 11.40  ? 18  LYS A N   1 
ATOM   136  C  CA  . LYS A  1 18  ? 15.854  18.300  9.404   1.00 12.83  ? 18  LYS A CA  1 
ATOM   137  C  C   . LYS A  1 18  ? 16.803  17.557  8.492   1.00 13.21  ? 18  LYS A C   1 
ATOM   138  O  O   . LYS A  1 18  ? 17.915  18.082  8.211   1.00 16.68  ? 18  LYS A O   1 
ATOM   139  C  CB  . LYS A  1 18  ? 16.344  18.212  10.868  1.00 14.72  ? 18  LYS A CB  1 
ATOM   140  C  CG  . LYS A  1 18  ? 17.768  18.602  11.148  1.00 23.04  ? 18  LYS A CG  1 
ATOM   141  C  CD  . LYS A  1 18  ? 17.958  18.595  12.682  1.00 29.80  ? 18  LYS A CD  1 
ATOM   142  C  CE  . LYS A  1 18  ? 19.233  19.324  13.057  1.00 39.57  ? 18  LYS A CE  1 
ATOM   143  N  NZ  . LYS A  1 18  ? 20.423  18.970  12.243  1.00 53.67  ? 18  LYS A NZ  1 
ATOM   144  N  N   . TYR A  1 19  ? 16.508  16.327  8.107   1.00 11.71  ? 19  TYR A N   1 
ATOM   145  C  CA  . TYR A  1 19  ? 17.389  15.438  7.389   1.00 12.40  ? 19  TYR A CA  1 
ATOM   146  C  C   . TYR A  1 19  ? 16.698  15.019  6.104   1.00 12.11  ? 19  TYR A C   1 
ATOM   147  O  O   . TYR A  1 19  ? 16.053  13.961  6.042   1.00 11.69  ? 19  TYR A O   1 
ATOM   148  C  CB  . TYR A  1 19  ? 17.792  14.227  8.286   1.00 12.03  ? 19  TYR A CB  1 
ATOM   149  C  CG  . TYR A  1 19  ? 18.444  14.625  9.519   1.00 12.69  ? 19  TYR A CG  1 
ATOM   150  C  CD1 . TYR A  1 19  ? 19.844  14.968  9.512   1.00 13.49  ? 19  TYR A CD1 1 
ATOM   151  C  CD2 . TYR A  1 19  ? 17.740  14.611  10.721  1.00 13.47  ? 19  TYR A CD2 1 
ATOM   152  C  CE1 . TYR A  1 19  ? 20.471  15.254  10.763  1.00 15.86  ? 19  TYR A CE1 1 
ATOM   153  C  CE2 . TYR A  1 19  ? 18.330  14.955  11.938  1.00 13.84  ? 19  TYR A CE2 1 
ATOM   154  C  CZ  . TYR A  1 19  ? 19.721  15.271  11.945  1.00 15.43  ? 19  TYR A CZ  1 
ATOM   155  O  OH  . TYR A  1 19  ? 20.383  15.569  13.122  1.00 19.72  ? 19  TYR A OH  1 
ATOM   156  N  N   . PRO A  1 20  ? 16.735  15.846  5.038   1.00 12.28  ? 20  PRO A N   1 
ATOM   157  C  CA  . PRO A  1 20  ? 15.870  15.628  3.879   1.00 11.92  ? 20  PRO A CA  1 
ATOM   158  C  C   . PRO A  1 20  ? 16.083  14.274  3.235   1.00 11.69  ? 20  PRO A C   1 
ATOM   159  O  O   . PRO A  1 20  ? 15.172  13.717  2.615   1.00 11.90  ? 20  PRO A O   1 
ATOM   160  C  CB  . PRO A  1 20  ? 16.149  16.756  2.939   1.00 15.03  ? 20  PRO A CB  1 
ATOM   161  C  CG  . PRO A  1 20  ? 16.743  17.812  3.847   1.00 17.13  ? 20  PRO A CG  1 
ATOM   162  C  CD  . PRO A  1 20  ? 17.527  17.140  4.965   1.00 13.47  ? 20  PRO A CD  1 
ATOM   163  N  N   . SER A  1 21  ? 17.305  13.679  3.324   1.00 11.63  ? 21  SER A N   1 
ATOM   164  C  CA  . SER A  1 21  ? 17.487  12.390  2.630   1.00 11.04  ? 21  SER A CA  1 
ATOM   165  C  C   . SER A  1 21  ? 16.642  11.266  3.281   1.00 10.30  ? 21  SER A C   1 
ATOM   166  O  O   . SER A  1 21  ? 16.415  10.253  2.629   1.00 10.98  ? 21  SER A O   1 
ATOM   167  C  CB  . SER A  1 21  ? 18.989  11.934  2.696   1.00 12.01  ? 21  SER A CB  1 
ATOM   168  O  OG  . SER A  1 21  ? 19.744  12.830  1.851   1.00 14.94  ? 21  SER A OG  1 
ATOM   169  N  N   . CYS A  1 22  ? 16.182  11.475  4.521   1.00 10.47  ? 22  CYS A N   1 
ATOM   170  C  CA  . CYS A  1 22  ? 15.338  10.467  5.161   1.00 10.87  ? 22  CYS A CA  1 
ATOM   171  C  C   . CYS A  1 22  ? 14.004  10.309  4.456   1.00 10.61  ? 22  CYS A C   1 
ATOM   172  O  O   . CYS A  1 22  ? 13.345  9.307   4.707   1.00 11.70  ? 22  CYS A O   1 
ATOM   173  C  CB  . CYS A  1 22  ? 15.148  10.764  6.647   1.00 11.03  ? 22  CYS A CB  1 
ATOM   174  S  SG  . CYS A  1 22  ? 16.688  10.841  7.618   1.00 11.71  ? 22  CYS A SG  1 
ATOM   175  N  N   . GLY A  1 23  ? 13.607  11.258  3.618   1.00 11.84  ? 23  GLY A N   1 
ATOM   176  C  CA  . GLY A  1 23  ? 12.422  11.151  2.753   1.00 11.92  ? 23  GLY A CA  1 
ATOM   177  C  C   . GLY A  1 23  ? 12.744  10.938  1.333   1.00 11.75  ? 23  GLY A C   1 
ATOM   178  O  O   . GLY A  1 23  ? 11.853  11.042  0.459   1.00 13.13  ? 23  GLY A O   1 
ATOM   179  N  N   . GLY A  1 24  ? 14.002  10.634  0.986   1.00 12.37  ? 24  GLY A N   1 
ATOM   180  C  CA  . GLY A  1 24  ? 14.419  10.433  -0.380  1.00 13.62  ? 24  GLY A CA  1 
ATOM   181  C  C   . GLY A  1 24  ? 14.543  9.023   -0.842  1.00 13.04  ? 24  GLY A C   1 
ATOM   182  O  O   . GLY A  1 24  ? 13.848  8.126   -0.316  1.00 15.75  ? 24  GLY A O   1 
ATOM   183  N  N   . LEU A  1 25  ? 15.337  8.795   -1.884  1.00 14.11  ? 25  LEU A N   1 
ATOM   184  C  CA  . LEU A  1 25  ? 15.436  7.493   -2.472  1.00 15.48  ? 25  LEU A CA  1 
ATOM   185  C  C   . LEU A  1 25  ? 16.405  6.587   -1.671  1.00 14.16  ? 25  LEU A C   1 
ATOM   186  O  O   . LEU A  1 25  ? 17.177  7.031   -0.810  1.00 14.20  ? 25  LEU A O   1 
ATOM   187  C  CB  . LEU A  1 25  ? 16.129  7.690   -3.893  1.00 19.23  ? 25  LEU A CB  1 
ATOM   188  C  CG  . LEU A  1 25  ? 15.355  8.606   -4.836  1.00 25.44  ? 25  LEU A CG  1 
ATOM   189  C  CD1 . LEU A  1 25  ? 16.102  8.888   -6.130  1.00 30.29  ? 25  LEU A CD1 1 
ATOM   190  C  CD2 . LEU A  1 25  ? 13.982  8.046   -5.034  1.00 29.91  ? 25  LEU A CD2 1 
ATOM   191  N  N   . LEU A  1 26  ? 16.318  5.297   -2.021  1.00 14.44  ? 26  LEU A N   1 
ATOM   192  C  CA  . LEU A  1 26  ? 17.212  4.217   -1.609  1.00 14.30  ? 26  LEU A CA  1 
ATOM   193  C  C   . LEU A  1 26  ? 17.218  4.025   -0.102  1.00 12.67  ? 26  LEU A C   1 
ATOM   194  O  O   . LEU A  1 26  ? 18.258  3.694   0.465   1.00 14.24  ? 26  LEU A O   1 
ATOM   195  C  CB  . LEU A  1 26  ? 18.694  4.473   -2.141  1.00 16.51  ? 26  LEU A CB  1 
ATOM   196  C  CG  . LEU A  1 26  ? 18.864  4.497   -3.693  1.00 20.29  ? 26  LEU A CG  1 
ATOM   197  C  CD1 . LEU A  1 26  ? 20.368  4.675   -4.041  1.00 27.07  ? 26  LEU A CD1 1 
ATOM   198  C  CD2 . LEU A  1 26  ? 18.231  3.335   -4.368  1.00 22.65  ? 26  LEU A CD2 1 
ATOM   199  N  N   . GLN A  1 27  ? 16.082  4.250   0.571   1.00 11.31  ? 27  GLN A N   1 
ATOM   200  C  CA  . GLN A  1 27  ? 16.121  4.148   2.047   1.00 10.24  ? 27  GLN A CA  1 
ATOM   201  C  C   . GLN A  1 27  ? 16.159  2.719   2.562   1.00 9.80   ? 27  GLN A C   1 
ATOM   202  O  O   . GLN A  1 27  ? 15.545  1.793   2.025   1.00 12.72  ? 27  GLN A O   1 
ATOM   203  C  CB  . GLN A  1 27  ? 14.927  4.853   2.645   1.00 10.50  ? 27  GLN A CB  1 
ATOM   204  C  CG  . GLN A  1 27  ? 14.984  6.378   2.362   1.00 11.06  ? 27  GLN A CG  1 
ATOM   205  C  CD  . GLN A  1 27  ? 16.163  7.027   3.071   1.00 10.55  ? 27  GLN A CD  1 
ATOM   206  O  OE1 . GLN A  1 27  ? 16.135  7.207   4.290   1.00 9.93   ? 27  GLN A OE1 1 
ATOM   207  N  NE2 . GLN A  1 27  ? 17.232  7.278   2.316   1.00 10.69  ? 27  GLN A NE2 1 
ATOM   208  N  N   . SER A  1 28  ? 16.846  2.523   3.666   1.00 9.55   ? 28  SER A N   1 
ATOM   209  C  CA  . SER A  1 28  ? 16.987  1.283   4.419   1.00 9.30   ? 28  SER A CA  1 
ATOM   210  C  C   . SER A  1 28  ? 16.402  1.490   5.801   1.00 9.16   ? 28  SER A C   1 
ATOM   211  O  O   . SER A  1 28  ? 16.307  2.629   6.318   1.00 9.54   ? 28  SER A O   1 
ATOM   212  C  CB  . SER A  1 28  ? 18.469  0.973   4.540   1.00 10.06  ? 28  SER A CB  1 
ATOM   213  O  OG  . SER A  1 28  ? 19.047  0.691   3.280   1.00 9.80   ? 28  SER A OG  1 
ATOM   214  N  N   . PRO A  1 29  ? 16.039  0.396   6.535   1.00 9.10   ? 29  PRO A N   1 
ATOM   215  C  CA  . PRO A  1 29  ? 16.142  -1.009  6.145   1.00 8.99   ? 29  PRO A CA  1 
ATOM   216  C  C   . PRO A  1 29  ? 14.919  -1.431  5.317   1.00 8.63   ? 29  PRO A C   1 
ATOM   217  O  O   . PRO A  1 29  ? 14.000  -0.617  5.094   1.00 9.98   ? 29  PRO A O   1 
ATOM   218  C  CB  . PRO A  1 29  ? 16.165  -1.695  7.523   1.00 9.46   ? 29  PRO A CB  1 
ATOM   219  C  CG  . PRO A  1 29  ? 15.172  -0.859  8.322   1.00 9.88   ? 29  PRO A CG  1 
ATOM   220  C  CD  . PRO A  1 29  ? 15.485  0.571   7.894   1.00 8.88   ? 29  PRO A CD  1 
ATOM   221  N  N   . ILE A  1 30  ? 14.928  -2.666  4.878   1.00 9.69   ? 30  ILE A N   1 
ATOM   222  C  CA  . ILE A  1 30  ? 13.882  -3.246  4.038   1.00 10.14  ? 30  ILE A CA  1 
ATOM   223  C  C   . ILE A  1 30  ? 13.578  -4.642  4.523   1.00 9.84   ? 30  ILE A C   1 
ATOM   224  O  O   . ILE A  1 30  ? 14.371  -5.291  5.265   1.00 11.03  ? 30  ILE A O   1 
ATOM   225  C  CB  . ILE A  1 30  ? 14.327  -3.266  2.558   1.00 10.90  ? 30  ILE A CB  1 
ATOM   226  C  CG1 . ILE A  1 30  ? 15.569  -4.141  2.318   1.00 11.80  ? 30  ILE A CG1 1 
ATOM   227  C  CG2 . ILE A  1 30  ? 14.499  -1.842  2.072   1.00 13.35  ? 30  ILE A CG2 1 
ATOM   228  C  CD1 . ILE A  1 30  ? 15.875  -4.389  0.844   1.00 13.44  ? 30  ILE A CD1 1 
ATOM   229  N  N   . ASP A  1 31  ? 12.414  -5.145  4.086   1.00 10.94  ? 31  ASP A N   1 
ATOM   230  C  CA  . ASP A  1 31  ? 12.060  -6.566  4.282   1.00 10.90  ? 31  ASP A CA  1 
ATOM   231  C  C   . ASP A  1 31  ? 12.670  -7.363  3.165   1.00 10.59  ? 31  ASP A C   1 
ATOM   232  O  O   . ASP A  1 31  ? 12.494  -7.136  1.959   1.00 13.87  ? 31  ASP A O   1 
ATOM   233  C  CB  . ASP A  1 31  ? 10.591  -6.665  4.230   1.00 12.33  ? 31  ASP A CB  1 
ATOM   234  C  CG  . ASP A  1 31  ? 10.116  -8.150  4.455   1.00 13.31  ? 31  ASP A CG  1 
ATOM   235  O  OD1 . ASP A  1 31  ? 10.677  -8.828  5.330   1.00 13.49  ? 31  ASP A OD1 1 
ATOM   236  O  OD2 . ASP A  1 31  ? 9.084   -8.487  3.829   1.00 17.70  ? 31  ASP A OD2 1 
ATOM   237  N  N   . LEU A  1 32  ? 13.427  -8.363  3.539   1.00 12.23  ? 32  LEU A N   1 
ATOM   238  C  CA  . LEU A  1 32  ? 14.117  -9.297  2.600   1.00 12.55  ? 32  LEU A CA  1 
ATOM   239  C  C   . LEU A  1 32  ? 13.166  -10.477 2.359   1.00 13.99  ? 32  LEU A C   1 
ATOM   240  O  O   . LEU A  1 32  ? 13.031  -11.364 3.181   1.00 15.18  ? 32  LEU A O   1 
ATOM   241  C  CB  . LEU A  1 32  ? 15.437  -9.794  3.202   1.00 13.76  ? 32  LEU A CB  1 
ATOM   242  C  CG  . LEU A  1 32  ? 16.354  -8.578  3.632   1.00 11.86  ? 32  LEU A CG  1 
ATOM   243  C  CD1 . LEU A  1 32  ? 17.512  -9.115  4.441   1.00 14.58  ? 32  LEU A CD1 1 
ATOM   244  C  CD2 . LEU A  1 32  ? 16.904  -7.859  2.422   1.00 17.10  ? 32  LEU A CD2 1 
ATOM   245  N  N   . HIS A  1 33  ? 12.379  -10.442 1.308   1.00 19.50  ? 33  HIS A N   1 
ATOM   246  C  CA  . HIS A  1 33  ? 11.413  -11.516 1.120   1.00 24.07  ? 33  HIS A CA  1 
ATOM   247  C  C   . HIS A  1 33  ? 11.544  -12.116 -0.185  1.00 21.75  ? 33  HIS A C   1 
ATOM   248  O  O   . HIS A  1 33  ? 12.136  -11.535 -1.097  1.00 19.02  ? 33  HIS A O   1 
ATOM   249  C  CB  . HIS A  1 33  ? 10.099  -11.004 1.489   1.00 25.12  ? 33  HIS A CB  1 
ATOM   250  C  CG  . HIS A  1 33  ? 9.620   -10.001 0.533   1.00 20.84  ? 33  HIS A CG  1 
ATOM   251  N  ND1 . HIS A  1 33  ? 9.886   -8.637  0.542   1.00 29.09  ? 33  HIS A ND1 1 
ATOM   252  C  CD2 . HIS A  1 33  ? 8.751   -10.214 -0.492  1.00 32.78  ? 33  HIS A CD2 1 
ATOM   253  C  CE1 . HIS A  1 33  ? 9.240   -8.079  -0.501  1.00 30.91  ? 33  HIS A CE1 1 
ATOM   254  N  NE2 . HIS A  1 33  ? 8.531   -9.008  -1.110  1.00 37.80  ? 33  HIS A NE2 1 
ATOM   255  N  N   . SER A  1 34  ? 10.975  -13.281 -0.325  1.00 24.31  ? 34  SER A N   1 
ATOM   256  C  CA  . SER A  1 34  ? 11.386  -14.203 -1.338  1.00 29.19  ? 34  SER A CA  1 
ATOM   257  C  C   . SER A  1 34  ? 11.080  -13.609 -2.718  1.00 26.31  ? 34  SER A C   1 
ATOM   258  O  O   . SER A  1 34  ? 11.874  -13.899 -3.637  1.00 33.18  ? 34  SER A O   1 
ATOM   259  C  CB  . SER A  1 34  ? 10.901  -15.619 -1.067  1.00 41.79  ? 34  SER A CB  1 
ATOM   260  O  OG  . SER A  1 34  ? 9.533   -15.552 -1.168  1.00 49.59  ? 34  SER A OG  1 
ATOM   261  N  N   . ASP A  1 35  ? 9.981   -12.851 -2.916  1.00 23.61  ? 35  ASP A N   1 
ATOM   262  C  CA  . ASP A  1 35  ? 9.677   -12.375 -4.283  1.00 29.99  ? 35  ASP A CA  1 
ATOM   263  C  C   . ASP A  1 35  ? 10.653  -11.384 -4.872  1.00 26.44  ? 35  ASP A C   1 
ATOM   264  O  O   . ASP A  1 35  ? 10.569  -11.081 -6.053  1.00 34.06  ? 35  ASP A O   1 
ATOM   265  C  CB  . ASP A  1 35  ? 8.293   -11.761 -4.282  1.00 37.69  ? 35  ASP A CB  1 
ATOM   266  C  CG  . ASP A  1 35  ? 7.190   -12.742 -3.846  1.00 59.05  ? 35  ASP A CG  1 
ATOM   267  O  OD1 . ASP A  1 35  ? 7.417   -13.998 -3.828  1.00 75.65  ? 35  ASP A OD1 1 
ATOM   268  O  OD2 . ASP A  1 35  ? 6.038   -12.269 -3.541  1.00 59.41  ? 35  ASP A OD2 1 
ATOM   269  N  N   . ILE A  1 36  ? 11.513  -10.793 -4.038  1.00 23.13  ? 36  ILE A N   1 
ATOM   270  C  CA  . ILE A  1 36  ? 12.419  -9.806  -4.496  1.00 20.34  ? 36  ILE A CA  1 
ATOM   271  C  C   . ILE A  1 36  ? 13.850  -10.272 -4.478  1.00 18.51  ? 36  ILE A C   1 
ATOM   272  O  O   . ILE A  1 36  ? 14.768  -9.446  -4.767  1.00 21.44  ? 36  ILE A O   1 
ATOM   273  C  CB  . ILE A  1 36  ? 12.227  -8.436  -3.788  1.00 23.31  ? 36  ILE A CB  1 
ATOM   274  C  CG1 . ILE A  1 36  ? 12.603  -8.634  -2.310  1.00 23.93  ? 36  ILE A CG1 1 
ATOM   275  C  CG2 . ILE A  1 36  ? 10.911  -7.756  -4.156  1.00 25.80  ? 36  ILE A CG2 1 
ATOM   276  C  CD1 . ILE A  1 36  ? 12.855  -7.354  -1.584  1.00 24.31  ? 36  ILE A CD1 1 
ATOM   277  N  N   . LEU A  1 37  ? 14.083  -11.532 -4.205  1.00 20.36  ? 37  LEU A N   1 
ATOM   278  C  CA  . LEU A  1 37  ? 15.493  -12.083 -4.166  1.00 19.35  ? 37  LEU A CA  1 
ATOM   279  C  C   . LEU A  1 37  ? 15.869  -12.600 -5.447  1.00 20.16  ? 37  LEU A C   1 
ATOM   280  O  O   . LEU A  1 37  ? 15.036  -13.193 -6.216  1.00 24.42  ? 37  LEU A O   1 
ATOM   281  C  CB  . LEU A  1 37  ? 15.612  -13.229 -3.179  1.00 20.22  ? 37  LEU A CB  1 
ATOM   282  C  CG  . LEU A  1 37  ? 15.186  -12.960 -1.711  1.00 22.13  ? 37  LEU A CG  1 
ATOM   283  C  CD1 . LEU A  1 37  ? 15.423  -14.229 -0.846  1.00 23.66  ? 37  LEU A CD1 1 
ATOM   284  C  CD2 . LEU A  1 37  ? 15.960  -11.727 -1.122  1.00 19.22  ? 37  LEU A CD2 1 
ATOM   285  N  N   . GLN A  1 38  ? 17.102  -12.349 -5.816  1.00 18.89  ? 38  GLN A N   1 
ATOM   286  C  CA  . GLN A  1 38  ? 17.684  -12.899 -7.097  1.00 19.29  ? 38  GLN A CA  1 
ATOM   287  C  C   . GLN A  1 38  ? 19.079  -13.336 -6.924  1.00 17.98  ? 38  GLN A C   1 
ATOM   288  O  O   . GLN A  1 38  ? 19.962  -12.512 -6.523  1.00 17.37  ? 38  GLN A O   1 
ATOM   289  C  CB  . GLN A  1 38  ? 17.603  -11.856 -8.179  1.00 24.93  ? 38  GLN A CB  1 
ATOM   290  C  CG  . GLN A  1 38  ? 17.920  -12.472 -9.583  1.00 31.60  ? 38  GLN A CG  1 
ATOM   291  C  CD  . GLN A  1 38  ? 17.751  -11.480 -10.759 1.00 32.56  ? 38  GLN A CD  1 
ATOM   292  O  OE1 . GLN A  1 38  ? 16.691  -11.332 -11.357 1.00 46.40  ? 38  GLN A OE1 1 
ATOM   293  N  NE2 . GLN A  1 38  ? 18.778  -10.759 -11.002 1.00 35.44  ? 38  GLN A NE2 1 
ATOM   294  N  N   . TYR A  1 39  ? 19.387  -14.598 -7.174  1.00 19.97  ? 39  TYR A N   1 
ATOM   295  C  CA  . TYR A  1 39  ? 20.749  -15.081 -7.067  1.00 18.84  ? 39  TYR A CA  1 
ATOM   296  C  C   . TYR A  1 39  ? 21.576  -14.329 -8.115  1.00 18.85  ? 39  TYR A C   1 
ATOM   297  O  O   . TYR A  1 39  ? 21.192  -14.085 -9.283  1.00 21.55  ? 39  TYR A O   1 
ATOM   298  C  CB  . TYR A  1 39  ? 20.710  -16.592 -7.420  1.00 19.30  ? 39  TYR A CB  1 
ATOM   299  C  CG  . TYR A  1 39  ? 22.072  -17.184 -7.470  1.00 22.32  ? 39  TYR A CG  1 
ATOM   300  C  CD1 . TYR A  1 39  ? 22.926  -17.204 -6.395  1.00 25.56  ? 39  TYR A CD1 1 
ATOM   301  C  CD2 . TYR A  1 39  ? 22.506  -17.806 -8.654  1.00 24.11  ? 39  TYR A CD2 1 
ATOM   302  C  CE1 . TYR A  1 39  ? 24.203  -17.746 -6.465  1.00 26.60  ? 39  TYR A CE1 1 
ATOM   303  C  CE2 . TYR A  1 39  ? 23.771  -18.360 -8.734  1.00 29.22  ? 39  TYR A CE2 1 
ATOM   304  C  CZ  . TYR A  1 39  ? 24.624  -18.391 -7.634  1.00 31.00  ? 39  TYR A CZ  1 
ATOM   305  O  OH  . TYR A  1 39  ? 25.900  -18.936 -7.718  1.00 35.62  ? 39  TYR A OH  1 
ATOM   306  N  N   . ASP A  1 40  ? 22.801  -14.011 -7.702  1.00 17.54  ? 40  ASP A N   1 
ATOM   307  C  CA  . ASP A  1 40  ? 23.802  -13.312 -8.547  1.00 18.85  ? 40  ASP A CA  1 
ATOM   308  C  C   . ASP A  1 40  ? 25.132  -14.044 -8.274  1.00 21.62  ? 40  ASP A C   1 
ATOM   309  O  O   . ASP A  1 40  ? 25.713  -13.912 -7.164  1.00 20.22  ? 40  ASP A O   1 
ATOM   310  C  CB  . ASP A  1 40  ? 23.823  -11.837 -8.258  1.00 23.48  ? 40  ASP A CB  1 
ATOM   311  C  CG  . ASP A  1 40  ? 24.783  -11.088 -9.140  1.00 32.78  ? 40  ASP A CG  1 
ATOM   312  O  OD1 . ASP A  1 40  ? 25.604  -11.682 -9.744  1.00 28.88  ? 40  ASP A OD1 1 
ATOM   313  O  OD2 . ASP A  1 40  ? 24.791  -9.849  -9.053  1.00 47.24  ? 40  ASP A OD2 1 
ATOM   314  N  N   . ALA A  1 41  ? 25.568  -14.833 -9.267  1.00 25.71  ? 41  ALA A N   1 
ATOM   315  C  CA  . ALA A  1 41  ? 26.850  -15.612 -9.145  1.00 30.23  ? 41  ALA A CA  1 
ATOM   316  C  C   . ALA A  1 41  ? 28.066  -14.708 -9.015  1.00 24.09  ? 41  ALA A C   1 
ATOM   317  O  O   . ALA A  1 41  ? 29.168  -15.135 -8.625  1.00 36.45  ? 41  ALA A O   1 
ATOM   318  C  CB  . ALA A  1 41  ? 27.117  -16.561 -10.361 1.00 32.82  ? 41  ALA A CB  1 
ATOM   319  N  N   . SER A  1 42  ? 27.909  -13.436 -9.323  1.00 25.29  ? 42  SER A N   1 
ATOM   320  C  CA  . SER A  1 42  ? 29.024  -12.489 -9.107  1.00 28.37  ? 42  SER A CA  1 
ATOM   321  C  C   . SER A  1 42  ? 29.337  -12.192 -7.628  1.00 29.94  ? 42  SER A C   1 
ATOM   322  O  O   . SER A  1 42  ? 30.421  -11.644 -7.288  1.00 29.49  ? 42  SER A O   1 
ATOM   323  C  CB  . SER A  1 42  ? 28.822  -11.205 -9.950  1.00 35.71  ? 42  SER A CB  1 
ATOM   324  O  OG  . SER A  1 42  ? 28.098  -10.224 -9.272  1.00 40.58  ? 42  SER A OG  1 
ATOM   325  N  N   . LEU A  1 43  ? 28.448  -12.582 -6.747  1.00 20.67  ? 43  LEU A N   1 
ATOM   326  C  CA  . LEU A  1 43  ? 28.612  -12.189 -5.314  1.00 20.28  ? 43  LEU A CA  1 
ATOM   327  C  C   . LEU A  1 43  ? 29.490  -13.219 -4.631  1.00 19.33  ? 43  LEU A C   1 
ATOM   328  O  O   . LEU A  1 43  ? 28.995  -14.147 -3.957  1.00 21.04  ? 43  LEU A O   1 
ATOM   329  C  CB  . LEU A  1 43  ? 27.260  -12.090 -4.747  1.00 17.92  ? 43  LEU A CB  1 
ATOM   330  C  CG  . LEU A  1 43  ? 26.392  -10.899 -5.268  1.00 17.41  ? 43  LEU A CG  1 
ATOM   331  C  CD1 . LEU A  1 43  ? 24.991  -10.944 -4.628  1.00 17.58  ? 43  LEU A CD1 1 
ATOM   332  C  CD2 . LEU A  1 43  ? 27.047  -9.560  -5.096  1.00 19.60  ? 43  LEU A CD2 1 
ATOM   333  N  N   . THR A  1 44  ? 30.777  -12.989 -4.660  1.00 20.61  ? 44  THR A N   1 
ATOM   334  C  CA  . THR A  1 44  ? 31.752  -13.976 -4.119  1.00 21.62  ? 44  THR A CA  1 
ATOM   335  C  C   . THR A  1 44  ? 32.072  -13.600 -2.647  1.00 20.04  ? 44  THR A C   1 
ATOM   336  O  O   . THR A  1 44  ? 31.569  -12.623 -2.151  1.00 17.98  ? 44  THR A O   1 
ATOM   337  C  CB  . THR A  1 44  ? 33.041  -13.924 -4.943  1.00 27.65  ? 44  THR A CB  1 
ATOM   338  O  OG1 . THR A  1 44  ? 33.434  -12.550 -4.969  1.00 30.82  ? 44  THR A OG1 1 
ATOM   339  C  CG2 . THR A  1 44  ? 32.772  -14.487 -6.362  1.00 40.38  ? 44  THR A CG2 1 
ATOM   340  N  N   . PRO A  1 45  ? 32.745  -14.544 -1.944  1.00 19.35  ? 45  PRO A N   1 
ATOM   341  C  CA  . PRO A  1 45  ? 32.942  -14.221 -0.538  1.00 18.76  ? 45  PRO A CA  1 
ATOM   342  C  C   . PRO A  1 45  ? 33.812  -13.032 -0.272  1.00 18.10  ? 45  PRO A C   1 
ATOM   343  O  O   . PRO A  1 45  ? 34.861  -12.838 -0.903  1.00 22.88  ? 45  PRO A O   1 
ATOM   344  C  CB  . PRO A  1 45  ? 33.671  -15.496 -0.021  1.00 23.62  ? 45  PRO A CB  1 
ATOM   345  C  CG  . PRO A  1 45  ? 33.204  -16.596 -1.018  1.00 26.41  ? 45  PRO A CG  1 
ATOM   346  C  CD  . PRO A  1 45  ? 33.227  -15.925 -2.301  1.00 23.78  ? 45  PRO A CD  1 
ATOM   347  N  N   . LEU A  1 46  ? 33.405  -12.228 0.682   1.00 17.43  ? 46  LEU A N   1 
ATOM   348  C  CA  . LEU A  1 46  ? 34.236  -11.134 1.193   1.00 16.98  ? 46  LEU A CA  1 
ATOM   349  C  C   . LEU A  1 46  ? 35.361  -11.714 2.016   1.00 16.90  ? 46  LEU A C   1 
ATOM   350  O  O   . LEU A  1 46  ? 35.226  -12.791 2.625   1.00 19.98  ? 46  LEU A O   1 
ATOM   351  C  CB  . LEU A  1 46  ? 33.379  -10.167 2.063   1.00 16.35  ? 46  LEU A CB  1 
ATOM   352  C  CG  . LEU A  1 46  ? 32.262  -9.520  1.257   1.00 16.86  ? 46  LEU A CG  1 
ATOM   353  C  CD1 . LEU A  1 46  ? 31.494  -8.614  2.212   1.00 19.40  ? 46  LEU A CD1 1 
ATOM   354  C  CD2 . LEU A  1 46  ? 32.819  -8.704  0.093   1.00 22.68  ? 46  LEU A CD2 1 
ATOM   355  N  N   . GLU A  1 47  ? 36.435  -10.901 2.126   1.00 16.91  ? 47  GLU A N   1 
ATOM   356  C  CA  . GLU A  1 47  ? 37.535  -11.276 2.984   1.00 18.19  ? 47  GLU A CA  1 
ATOM   357  C  C   . GLU A  1 47  ? 37.640  -10.188 4.040   1.00 16.12  ? 47  GLU A C   1 
ATOM   358  O  O   . GLU A  1 47  ? 37.521  -8.970  3.744   1.00 19.50  ? 47  GLU A O   1 
ATOM   359  C  CB  . GLU A  1 47  ? 38.852  -11.348 2.182   1.00 24.13  ? 47  GLU A CB  1 
ATOM   360  C  CG  . GLU A  1 47  ? 38.735  -12.387 1.047   1.00 32.20  ? 47  GLU A CG  1 
ATOM   361  C  CD  . GLU A  1 47  ? 39.922  -12.545 0.135   1.00 49.06  ? 47  GLU A CD  1 
ATOM   362  O  OE1 . GLU A  1 47  ? 39.741  -12.591 -1.151  1.00 62.09  ? 47  GLU A OE1 1 
ATOM   363  O  OE2 . GLU A  1 47  ? 41.036  -12.735 0.703   1.00 57.99  ? 47  GLU A OE2 1 
ATOM   364  N  N   . PHE A  1 48  ? 37.828  -10.563 5.293   1.00 16.15  ? 48  PHE A N   1 
ATOM   365  C  CA  . PHE A  1 48  ? 37.806  -9.639  6.453   1.00 15.50  ? 48  PHE A CA  1 
ATOM   366  C  C   . PHE A  1 48  ? 39.221  -9.512  6.872   1.00 15.55  ? 48  PHE A C   1 
ATOM   367  O  O   . PHE A  1 48  ? 39.812  -10.474 7.365   1.00 21.16  ? 48  PHE A O   1 
ATOM   368  C  CB  . PHE A  1 48  ? 36.853  -10.207 7.545   1.00 16.29  ? 48  PHE A CB  1 
ATOM   369  C  CG  . PHE A  1 48  ? 35.501  -10.587 6.965   1.00 15.09  ? 48  PHE A CG  1 
ATOM   370  C  CD1 . PHE A  1 48  ? 34.656  -9.577  6.502   1.00 15.80  ? 48  PHE A CD1 1 
ATOM   371  C  CD2 . PHE A  1 48  ? 35.146  -11.910 6.786   1.00 17.66  ? 48  PHE A CD2 1 
ATOM   372  C  CE1 . PHE A  1 48  ? 33.419  -10.010 5.887   1.00 15.57  ? 48  PHE A CE1 1 
ATOM   373  C  CE2 . PHE A  1 48  ? 33.970  -12.313 6.182   1.00 17.81  ? 48  PHE A CE2 1 
ATOM   374  C  CZ  . PHE A  1 48  ? 33.083  -11.277 5.767   1.00 17.81  ? 48  PHE A CZ  1 
ATOM   375  N  N   . GLN A  1 49  ? 39.829  -8.418  6.614   1.00 15.98  ? 49  GLN A N   1 
ATOM   376  C  CA  . GLN A  1 49  ? 41.323  -8.243  6.824   1.00 16.68  ? 49  GLN A CA  1 
ATOM   377  C  C   . GLN A  1 49  ? 41.567  -7.284  7.958   1.00 13.61  ? 49  GLN A C   1 
ATOM   378  O  O   . GLN A  1 49  ? 40.851  -6.281  8.131   1.00 14.26  ? 49  GLN A O   1 
ATOM   379  C  CB  . GLN A  1 49  ? 41.921  -7.544  5.570   1.00 18.24  ? 49  GLN A CB  1 
ATOM   380  C  CG  . GLN A  1 49  ? 41.716  -8.422  4.340   1.00 22.91  ? 49  GLN A CG  1 
ATOM   381  C  CD  . GLN A  1 49  ? 42.786  -8.527  3.302   1.00 37.01  ? 49  GLN A CD  1 
ATOM   382  O  OE1 . GLN A  1 49  ? 43.105  -9.656  2.864   1.00 44.43  ? 49  GLN A OE1 1 
ATOM   383  N  NE2 . GLN A  1 49  ? 43.288  -7.337  2.800   1.00 45.22  ? 49  GLN A NE2 1 
ATOM   384  N  N   . GLY A  1 50  ? 42.478  -7.612  8.842   1.00 15.90  ? 50  GLY A N   1 
ATOM   385  C  CA  . GLY A  1 50  ? 42.751  -6.758  9.955   1.00 15.40  ? 50  GLY A CA  1 
ATOM   386  C  C   . GLY A  1 50  ? 41.635  -6.755  11.027  1.00 14.91  ? 50  GLY A C   1 
ATOM   387  O  O   . GLY A  1 50  ? 41.588  -5.833  11.832  1.00 15.62  ? 50  GLY A O   1 
ATOM   388  N  N   . TYR A  1 51  ? 40.791  -7.835  11.002  1.00 14.77  ? 51  TYR A N   1 
ATOM   389  C  CA  . TYR A  1 51  ? 39.678  -7.891  12.018  1.00 14.55  ? 51  TYR A CA  1 
ATOM   390  C  C   . TYR A  1 51  ? 40.201  -8.386  13.338  1.00 15.43  ? 51  TYR A C   1 
ATOM   391  O  O   . TYR A  1 51  ? 39.519  -8.248  14.352  1.00 15.98  ? 51  TYR A O   1 
ATOM   392  C  CB  . TYR A  1 51  ? 38.581  -8.797  11.479  1.00 13.63  ? 51  TYR A CB  1 
ATOM   393  C  CG  . TYR A  1 51  ? 37.552  -8.112  10.606  1.00 13.53  ? 51  TYR A CG  1 
ATOM   394  C  CD1 . TYR A  1 51  ? 37.903  -7.273  9.601   1.00 13.69  ? 51  TYR A CD1 1 
ATOM   395  C  CD2 . TYR A  1 51  ? 36.157  -8.344  10.869  1.00 13.40  ? 51  TYR A CD2 1 
ATOM   396  C  CE1 . TYR A  1 51  ? 36.920  -6.642  8.802   1.00 13.39  ? 51  TYR A CE1 1 
ATOM   397  C  CE2 . TYR A  1 51  ? 35.174  -7.742  10.078  1.00 13.41  ? 51  TYR A CE2 1 
ATOM   398  C  CZ  . TYR A  1 51  ? 35.552  -6.839  9.117   1.00 13.59  ? 51  TYR A CZ  1 
ATOM   399  O  OH  . TYR A  1 51  ? 34.565  -6.232  8.393   1.00 14.44  ? 51  TYR A OH  1 
ATOM   400  N  N   . ASN A  1 52  ? 41.396  -9.031  13.350  1.00 16.84  ? 52  ASN A N   1 
ATOM   401  C  CA  . ASN A  1 52  ? 41.918  -9.554  14.576  1.00 18.24  ? 52  ASN A CA  1 
ATOM   402  C  C   . ASN A  1 52  ? 42.646  -8.416  15.274  1.00 18.22  ? 52  ASN A C   1 
ATOM   403  O  O   . ASN A  1 52  ? 43.902  -8.255  15.124  1.00 22.69  ? 52  ASN A O   1 
ATOM   404  C  CB  . ASN A  1 52  ? 42.806  -10.764 14.317  1.00 19.88  ? 52  ASN A CB  1 
ATOM   405  C  CG  . ASN A  1 52  ? 43.245  -11.455 15.596  1.00 25.55  ? 52  ASN A CG  1 
ATOM   406  O  OD1 . ASN A  1 52  ? 42.507  -11.387 16.657  1.00 24.69  ? 52  ASN A OD1 1 
ATOM   407  N  ND2 . ASN A  1 52  ? 44.436  -12.046 15.576  1.00 29.83  ? 52  ASN A ND2 1 
ATOM   408  N  N   . LEU A  1 53  ? 41.916  -7.614  16.032  1.00 18.97  ? 53  LEU A N   1 
ATOM   409  C  CA  . LEU A  1 53  ? 42.487  -6.411  16.597  1.00 19.72  ? 53  LEU A CA  1 
ATOM   410  C  C   . LEU A  1 53  ? 43.426  -6.738  17.695  1.00 23.76  ? 53  LEU A C   1 
ATOM   411  O  O   . LEU A  1 53  ? 43.223  -7.664  18.559  1.00 26.69  ? 53  LEU A O   1 
ATOM   412  C  CB  . LEU A  1 53  ? 41.413  -5.474  17.179  1.00 16.58  ? 53  LEU A CB  1 
ATOM   413  C  CG  . LEU A  1 53  ? 40.285  -5.142  16.200  1.00 15.84  ? 53  LEU A CG  1 
ATOM   414  C  CD1 . LEU A  1 53  ? 39.296  -4.226  16.973  1.00 18.24  ? 53  LEU A CD1 1 
ATOM   415  C  CD2 . LEU A  1 53  ? 40.839  -4.481  14.963  1.00 19.39  ? 53  LEU A CD2 1 
ATOM   416  N  N   . SER A  1 54  ? 44.531  -5.939  17.720  1.00 23.96  ? 54  SER A N   1 
ATOM   417  C  CA  . SER A  1 54  ? 45.603  -6.187  18.717  1.00 30.93  ? 54  SER A CA  1 
ATOM   418  C  C   . SER A  1 54  ? 45.025  -6.219  20.114  1.00 27.99  ? 54  SER A C   1 
ATOM   419  O  O   . SER A  1 54  ? 44.419  -5.214  20.522  1.00 23.52  ? 54  SER A O   1 
ATOM   420  C  CB  . SER A  1 54  ? 46.558  -4.999  18.614  1.00 27.69  ? 54  SER A CB  1 
ATOM   421  O  OG  . SER A  1 54  ? 47.630  -5.142  19.539  1.00 33.80  ? 54  SER A OG  1 
ATOM   422  N  N   . ALA A  1 55  ? 45.252  -7.271  20.877  1.00 34.79  ? 55  ALA A N   1 
ATOM   423  C  CA  . ALA A  1 55  ? 44.904  -7.269  22.293  1.00 29.97  ? 55  ALA A CA  1 
ATOM   424  C  C   . ALA A  1 55  ? 45.663  -6.253  23.094  1.00 28.64  ? 55  ALA A C   1 
ATOM   425  O  O   . ALA A  1 55  ? 45.309  -6.054  24.252  1.00 33.19  ? 55  ALA A O   1 
ATOM   426  C  CB  . ALA A  1 55  ? 45.225  -8.663  22.917  1.00 47.50  ? 55  ALA A CB  1 
ATOM   427  N  N   . ASN A  1 56  ? 46.721  -5.662  22.485  1.00 31.51  ? 56  ASN A N   1 
ATOM   428  C  CA  . ASN A  1 56  ? 47.553  -4.638  23.187  1.00 27.39  ? 56  ASN A CA  1 
ATOM   429  C  C   . ASN A  1 56  ? 47.064  -3.252  22.859  1.00 26.43  ? 56  ASN A C   1 
ATOM   430  O  O   . ASN A  1 56  ? 47.640  -2.278  23.340  1.00 34.56  ? 56  ASN A O   1 
ATOM   431  C  CB  . ASN A  1 56  ? 49.030  -4.747  22.741  1.00 26.60  ? 56  ASN A CB  1 
ATOM   432  C  CG  . ASN A  1 56  ? 49.615  -6.039  23.141  1.00 35.98  ? 56  ASN A CG  1 
ATOM   433  O  OD1 . ASN A  1 56  ? 49.379  -6.437  24.287  1.00 37.00  ? 56  ASN A OD1 1 
ATOM   434  N  ND2 . ASN A  1 56  ? 50.195  -6.798  22.209  1.00 36.73  ? 56  ASN A ND2 1 
ATOM   435  N  N   . LYS A  1 57  ? 46.017  -3.158  21.998  1.00 22.96  ? 57  LYS A N   1 
ATOM   436  C  CA  . LYS A  1 57  ? 45.374  -1.819  21.700  1.00 19.39  ? 57  LYS A CA  1 
ATOM   437  C  C   . LYS A  1 57  ? 43.975  -1.775  22.372  1.00 18.87  ? 57  LYS A C   1 
ATOM   438  O  O   . LYS A  1 57  ? 43.421  -2.758  22.720  1.00 20.38  ? 57  LYS A O   1 
ATOM   439  C  CB  . LYS A  1 57  ? 45.179  -1.624  20.190  1.00 19.13  ? 57  LYS A CB  1 
ATOM   440  C  CG  . LYS A  1 57  ? 46.440  -1.214  19.389  1.00 22.67  ? 57  LYS A CG  1 
ATOM   441  C  CD  . LYS A  1 57  ? 46.052  -1.076  17.905  1.00 25.12  ? 57  LYS A CD  1 
ATOM   442  C  CE  . LYS A  1 57  ? 45.110  0.136   17.774  1.00 37.68  ? 57  LYS A CE  1 
ATOM   443  N  N   . GLN A  1 58  ? 43.547  -0.567  22.665  1.00 21.25  ? 58  GLN A N   1 
ATOM   444  C  CA  . GLN A  1 58  ? 42.166  -0.365  23.251  1.00 20.37  ? 58  GLN A CA  1 
ATOM   445  C  C   . GLN A  1 58  ? 41.349  0.435   22.304  1.00 19.73  ? 58  GLN A C   1 
ATOM   446  O  O   . GLN A  1 58  ? 41.847  1.371   21.703  1.00 24.84  ? 58  GLN A O   1 
ATOM   447  C  CB  . GLN A  1 58  ? 42.211  0.389   24.562  1.00 22.51  ? 58  GLN A CB  1 
ATOM   448  C  CG  . GLN A  1 58  ? 42.855  -0.514  25.580  1.00 25.49  ? 58  GLN A CG  1 
ATOM   449  C  CD  . GLN A  1 58  ? 43.039  0.077   26.883  1.00 23.52  ? 58  GLN A CD  1 
ATOM   450  O  OE1 . GLN A  1 58  ? 43.604  -0.631  27.762  1.00 33.10  ? 58  GLN A OE1 1 
ATOM   451  N  NE2 . GLN A  1 58  ? 42.685  1.343   27.024  1.00 32.95  ? 58  GLN A NE2 1 
ATOM   452  N  N   . PHE A  1 59  ? 40.066  0.126   22.250  1.00 17.71  ? 59  PHE A N   1 
ATOM   453  C  CA  . PHE A  1 59  ? 39.157  0.776   21.292  1.00 17.55  ? 59  PHE A CA  1 
ATOM   454  C  C   . PHE A  1 59  ? 38.031  1.495   22.008  1.00 16.24  ? 59  PHE A C   1 
ATOM   455  O  O   . PHE A  1 59  ? 37.501  0.925   23.016  1.00 17.87  ? 59  PHE A O   1 
ATOM   456  C  CB  . PHE A  1 59  ? 38.671  -0.356  20.346  1.00 17.75  ? 59  PHE A CB  1 
ATOM   457  C  CG  . PHE A  1 59  ? 39.859  -0.853  19.535  1.00 17.28  ? 59  PHE A CG  1 
ATOM   458  C  CD1 . PHE A  1 59  ? 40.254  -0.235  18.372  1.00 19.43  ? 59  PHE A CD1 1 
ATOM   459  C  CD2 . PHE A  1 59  ? 40.556  -1.947  20.019  1.00 17.17  ? 59  PHE A CD2 1 
ATOM   460  C  CE1 . PHE A  1 59  ? 41.397  -0.667  17.703  1.00 18.97  ? 59  PHE A CE1 1 
ATOM   461  C  CE2 . PHE A  1 59  ? 41.699  -2.390  19.322  1.00 17.25  ? 59  PHE A CE2 1 
ATOM   462  C  CZ  . PHE A  1 59  ? 42.123  -1.750  18.159  1.00 18.25  ? 59  PHE A CZ  1 
ATOM   463  N  N   . LEU A  1 60  ? 37.651  2.685   21.623  1.00 17.12  ? 60  LEU A N   1 
ATOM   464  C  CA  . LEU A  1 60  ? 36.724  3.505   22.357  1.00 16.50  ? 60  LEU A CA  1 
ATOM   465  C  C   . LEU A  1 60  ? 35.229  3.059   22.152  1.00 15.91  ? 60  LEU A C   1 
ATOM   466  O  O   . LEU A  1 60  ? 34.751  2.965   21.041  1.00 16.36  ? 60  LEU A O   1 
ATOM   467  C  CB  . LEU A  1 60  ? 36.823  4.925   21.948  1.00 19.31  ? 60  LEU A CB  1 
ATOM   468  C  CG  . LEU A  1 60  ? 36.004  6.009   22.600  1.00 20.61  ? 60  LEU A CG  1 
ATOM   469  C  CD1 . LEU A  1 60  ? 36.478  6.157   24.069  1.00 26.17  ? 60  LEU A CD1 1 
ATOM   470  C  CD2 . LEU A  1 60  ? 35.987  7.391   21.944  1.00 23.12  ? 60  LEU A CD2 1 
ATOM   471  N  N   . LEU A  1 61  ? 34.583  2.699   23.241  1.00 15.49  ? 61  LEU A N   1 
ATOM   472  C  CA  . LEU A  1 61  ? 33.155  2.355   23.290  1.00 15.40  ? 61  LEU A CA  1 
ATOM   473  C  C   . LEU A  1 61  ? 32.434  3.577   23.816  1.00 15.84  ? 61  LEU A C   1 
ATOM   474  O  O   . LEU A  1 61  ? 32.819  4.164   24.800  1.00 16.77  ? 61  LEU A O   1 
ATOM   475  C  CB  . LEU A  1 61  ? 32.967  1.231   24.250  1.00 17.70  ? 61  LEU A CB  1 
ATOM   476  C  CG  . LEU A  1 61  ? 31.562  0.565   24.215  1.00 18.48  ? 61  LEU A CG  1 
ATOM   477  C  CD1 . LEU A  1 61  ? 31.376  -0.335  22.928  1.00 17.35  ? 61  LEU A CD1 1 
ATOM   478  C  CD2 . LEU A  1 61  ? 31.390  -0.305  25.461  1.00 21.93  ? 61  LEU A CD2 1 
ATOM   479  N  N   A THR A  1 62  ? 31.350  3.965   23.113  0.50 14.13  ? 62  THR A N   1 
ATOM   480  N  N   B THR A  1 62  ? 31.343  3.969   23.127  0.50 14.49  ? 62  THR A N   1 
ATOM   481  C  CA  A THR A  1 62  ? 30.586  5.141   23.527  0.50 15.02  ? 62  THR A CA  1 
ATOM   482  C  CA  B THR A  1 62  ? 30.575  5.121   23.617  0.50 15.70  ? 62  THR A CA  1 
ATOM   483  C  C   A THR A  1 62  ? 29.104  4.787   23.548  0.50 14.13  ? 62  THR A C   1 
ATOM   484  C  C   B THR A  1 62  ? 29.093  4.962   23.451  0.50 17.40  ? 62  THR A C   1 
ATOM   485  O  O   A THR A  1 62  ? 28.626  3.976   22.745  0.50 14.63  ? 62  THR A O   1 
ATOM   486  O  O   B THR A  1 62  ? 28.597  4.436   22.466  0.50 15.68  ? 62  THR A O   1 
ATOM   487  C  CB  A THR A  1 62  ? 30.834  6.278   22.481  0.50 17.62  ? 62  THR A CB  1 
ATOM   488  C  CB  B THR A  1 62  ? 30.909  6.402   22.807  0.50 19.74  ? 62  THR A CB  1 
ATOM   489  O  OG1 A THR A  1 62  ? 32.248  6.486   22.255  0.50 19.99  ? 62  THR A OG1 1 
ATOM   490  O  OG1 B THR A  1 62  ? 30.675  6.190   21.389  0.50 20.21  ? 62  THR A OG1 1 
ATOM   491  C  CG2 A THR A  1 62  ? 30.115  7.634   22.864  0.50 21.42  ? 62  THR A CG2 1 
ATOM   492  C  CG2 B THR A  1 62  ? 32.328  6.889   23.011  0.50 23.94  ? 62  THR A CG2 1 
ATOM   493  N  N   . ASN A  1 63  ? 28.368  5.479   24.415  1.00 16.03  ? 63  ASN A N   1 
ATOM   494  C  CA  . ASN A  1 63  ? 26.898  5.564   24.307  1.00 15.30  ? 63  ASN A CA  1 
ATOM   495  C  C   . ASN A  1 63  ? 26.687  6.941   23.721  1.00 15.97  ? 63  ASN A C   1 
ATOM   496  O  O   . ASN A  1 63  ? 26.986  7.998   24.304  1.00 17.21  ? 63  ASN A O   1 
ATOM   497  C  CB  . ASN A  1 63  ? 26.328  5.471   25.683  1.00 16.06  ? 63  ASN A CB  1 
ATOM   498  C  CG  . ASN A  1 63  ? 24.847  5.759   25.755  1.00 14.61  ? 63  ASN A CG  1 
ATOM   499  O  OD1 . ASN A  1 63  ? 24.261  6.441   24.872  1.00 16.41  ? 63  ASN A OD1 1 
ATOM   500  N  ND2 . ASN A  1 63  ? 24.229  5.248   26.830  1.00 16.30  ? 63  ASN A ND2 1 
ATOM   501  N  N   . ASN A  1 64  ? 26.205  7.017   22.452  1.00 16.12  ? 64  ASN A N   1 
ATOM   502  C  CA  . ASN A  1 64  ? 25.986  8.286   21.786  1.00 16.70  ? 64  ASN A CA  1 
ATOM   503  C  C   . ASN A  1 64  ? 24.528  8.763   21.881  1.00 16.92  ? 64  ASN A C   1 
ATOM   504  O  O   . ASN A  1 64  ? 24.104  9.720   21.153  1.00 19.51  ? 64  ASN A O   1 
ATOM   505  C  CB  . ASN A  1 64  ? 26.430  8.236   20.297  1.00 17.92  ? 64  ASN A CB  1 
ATOM   506  C  CG  . ASN A  1 64  ? 25.713  7.158   19.497  1.00 17.38  ? 64  ASN A CG  1 
ATOM   507  O  OD1 . ASN A  1 64  ? 24.649  6.680   19.964  1.00 16.01  ? 64  ASN A OD1 1 
ATOM   508  N  ND2 . ASN A  1 64  ? 26.232  6.812   18.285  1.00 22.44  ? 64  ASN A ND2 1 
ATOM   509  N  N   . GLY A  1 65  ? 23.726  8.142   22.730  1.00 16.17  ? 65  GLY A N   1 
ATOM   510  C  CA  . GLY A  1 65  ? 22.338  8.530   22.912  1.00 18.21  ? 65  GLY A CA  1 
ATOM   511  C  C   . GLY A  1 65  ? 21.439  7.833   21.912  1.00 17.23  ? 65  GLY A C   1 
ATOM   512  O  O   . GLY A  1 65  ? 20.291  8.046   21.996  1.00 22.63  ? 65  GLY A O   1 
ATOM   513  N  N   . HIS A  1 66  ? 22.012  7.086   20.935  1.00 15.40  ? 66  HIS A N   1 
ATOM   514  C  CA  . HIS A  1 66  ? 21.222  6.361   19.879  1.00 14.47  ? 66  HIS A CA  1 
ATOM   515  C  C   . HIS A  1 66  ? 21.502  4.906   19.899  1.00 14.08  ? 66  HIS A C   1 
ATOM   516  O  O   . HIS A  1 66  ? 20.662  4.145   19.409  1.00 17.21  ? 66  HIS A O   1 
ATOM   517  C  CB  . HIS A  1 66  ? 21.431  7.028   18.541  1.00 16.69  ? 66  HIS A CB  1 
ATOM   518  C  CG  . HIS A  1 66  ? 21.147  8.517   18.522  1.00 18.08  ? 66  HIS A CG  1 
ATOM   519  N  ND1 . HIS A  1 66  ? 19.873  9.059   18.608  1.00 19.28  ? 66  HIS A ND1 1 
ATOM   520  C  CD2 . HIS A  1 66  ? 22.015  9.536   18.370  1.00 19.22  ? 66  HIS A CD2 1 
ATOM   521  C  CE1 . HIS A  1 66  ? 19.994  10.405  18.482  1.00 17.54  ? 66  HIS A CE1 1 
ATOM   522  N  NE2 . HIS A  1 66  ? 21.287  10.674  18.328  1.00 18.89  ? 66  HIS A NE2 1 
ATOM   523  N  N   . SER A  1 67  ? 22.732  4.499   20.239  1.00 13.96  ? 67  SER A N   1 
ATOM   524  C  CA  . SER A  1 67  ? 23.164  3.099   20.229  1.00 12.99  ? 67  SER A CA  1 
ATOM   525  C  C   . SER A  1 67  ? 24.402  3.054   21.178  1.00 13.21  ? 67  SER A C   1 
ATOM   526  O  O   . SER A  1 67  ? 24.760  4.054   21.783  1.00 15.34  ? 67  SER A O   1 
ATOM   527  C  CB  . SER A  1 67  ? 23.522  2.712   18.830  1.00 14.18  ? 67  SER A CB  1 
ATOM   528  O  OG  . SER A  1 67  ? 23.877  1.298   18.804  1.00 14.02  ? 67  SER A OG  1 
ATOM   529  N  N   . VAL A  1 68  ? 24.987  1.910   21.279  1.00 13.24  ? 68  VAL A N   1 
ATOM   530  C  CA  . VAL A  1 68  ? 26.328  1.724   21.802  1.00 12.68  ? 68  VAL A CA  1 
ATOM   531  C  C   . VAL A  1 68  ? 27.225  1.489   20.578  1.00 12.99  ? 68  VAL A C   1 
ATOM   532  O  O   . VAL A  1 68  ? 26.904  0.650   19.764  1.00 13.98  ? 68  VAL A O   1 
ATOM   533  C  CB  . VAL A  1 68  ? 26.408  0.578   22.848  1.00 14.94  ? 68  VAL A CB  1 
ATOM   534  C  CG1 . VAL A  1 68  ? 25.869  -0.780  22.435  1.00 17.33  ? 68  VAL A CG1 1 
ATOM   535  C  CG2 . VAL A  1 68  ? 27.828  0.530   23.318  1.00 19.37  ? 68  VAL A CG2 1 
ATOM   536  N  N   A LYS A  1 69  ? 28.304  2.269   20.484  0.50 14.59  ? 69  LYS A N   1 
ATOM   537  N  N   B LYS A  1 69  ? 28.322  2.239   20.501  0.50 13.21  ? 69  LYS A N   1 
ATOM   538  C  CA  A LYS A  1 69  ? 29.229  2.194   19.350  0.50 13.97  ? 69  LYS A CA  1 
ATOM   539  C  CA  B LYS A  1 69  ? 29.212  2.239   19.338  0.50 11.84  ? 69  LYS A CA  1 
ATOM   540  C  C   A LYS A  1 69  ? 30.649  1.939   19.769  0.50 12.55  ? 69  LYS A C   1 
ATOM   541  C  C   B LYS A  1 69  ? 30.641  1.937   19.765  0.50 13.04  ? 69  LYS A C   1 
ATOM   542  O  O   A LYS A  1 69  ? 31.107  2.447   20.786  0.50 13.63  ? 69  LYS A O   1 
ATOM   543  O  O   B LYS A  1 69  ? 31.102  2.454   20.783  0.50 15.59  ? 69  LYS A O   1 
ATOM   544  C  CB  A LYS A  1 69  ? 29.125  3.339   18.434  0.50 17.28  ? 69  LYS A CB  1 
ATOM   545  C  CB  B LYS A  1 69  ? 29.158  3.586   18.741  0.50 11.90  ? 69  LYS A CB  1 
ATOM   546  C  CG  A LYS A  1 69  ? 29.762  4.606   18.732  0.50 19.62  ? 69  LYS A CG  1 
ATOM   547  C  CG  B LYS A  1 69  ? 30.056  3.808   17.601  0.50 13.40  ? 69  LYS A CG  1 
ATOM   548  C  CD  A LYS A  1 69  ? 30.039  5.395   17.459  0.50 24.32  ? 69  LYS A CD  1 
ATOM   549  C  CD  B LYS A  1 69  ? 29.923  5.123   16.913  0.50 15.75  ? 69  LYS A CD  1 
ATOM   550  C  CE  A LYS A  1 69  ? 30.632  6.706   17.937  0.50 34.33  ? 69  LYS A CE  1 
ATOM   551  C  CE  B LYS A  1 69  ? 30.340  6.244   17.771  0.50 19.69  ? 69  LYS A CE  1 
ATOM   552  N  NZ  A LYS A  1 69  ? 30.612  7.723   16.864  0.50 33.30  ? 69  LYS A NZ  1 
ATOM   553  N  NZ  B LYS A  1 69  ? 30.498  7.502   16.931  0.50 19.29  ? 69  LYS A NZ  1 
ATOM   554  N  N   . LEU A  1 70  ? 31.314  1.078   19.033  1.00 11.89  ? 70  LEU A N   1 
ATOM   555  C  CA  . LEU A  1 70  ? 32.745  0.782   19.203  1.00 11.94  ? 70  LEU A CA  1 
ATOM   556  C  C   . LEU A  1 70  ? 33.503  1.324   18.031  1.00 11.76  ? 70  LEU A C   1 
ATOM   557  O  O   . LEU A  1 70  ? 33.226  0.990   16.901  1.00 12.81  ? 70  LEU A O   1 
ATOM   558  C  CB  . LEU A  1 70  ? 32.945  -0.728  19.318  1.00 12.90  ? 70  LEU A CB  1 
ATOM   559  C  CG  . LEU A  1 70  ? 34.411  -1.128  19.552  1.00 13.83  ? 70  LEU A CG  1 
ATOM   560  C  CD1 . LEU A  1 70  ? 34.911  -0.683  20.907  1.00 16.09  ? 70  LEU A CD1 1 
ATOM   561  C  CD2 . LEU A  1 70  ? 34.480  -2.668  19.425  1.00 16.55  ? 70  LEU A CD2 1 
ATOM   562  N  N   . ASN A  1 71  ? 34.476  2.215   18.298  1.00 12.82  ? 71  ASN A N   1 
ATOM   563  C  CA  . ASN A  1 71  ? 35.349  2.702   17.249  1.00 12.65  ? 71  ASN A CA  1 
ATOM   564  C  C   . ASN A  1 71  ? 36.261  1.602   16.746  1.00 13.13  ? 71  ASN A C   1 
ATOM   565  O  O   . ASN A  1 71  ? 36.775  0.821   17.573  1.00 15.85  ? 71  ASN A O   1 
ATOM   566  C  CB  . ASN A  1 71  ? 36.094  3.869   17.724  1.00 15.84  ? 71  ASN A CB  1 
ATOM   567  C  CG  . ASN A  1 71  ? 35.249  5.106   17.803  1.00 20.41  ? 71  ASN A CG  1 
ATOM   568  O  OD1 . ASN A  1 71  ? 34.030  5.087   17.463  1.00 24.64  ? 71  ASN A OD1 1 
ATOM   569  N  ND2 . ASN A  1 71  ? 35.849  6.238   18.226  1.00 26.79  ? 71  ASN A ND2 1 
ATOM   570  N  N   . LEU A  1 72  ? 36.533  1.630   15.468  1.00 12.99  ? 72  LEU A N   1 
ATOM   571  C  CA  . LEU A  1 72  ? 37.358  0.577   14.860  1.00 13.28  ? 72  LEU A CA  1 
ATOM   572  C  C   . LEU A  1 72  ? 38.472  1.268   14.068  1.00 13.96  ? 72  LEU A C   1 
ATOM   573  O  O   . LEU A  1 72  ? 38.276  2.385   13.558  1.00 15.32  ? 72  LEU A O   1 
ATOM   574  C  CB  . LEU A  1 72  ? 36.501  -0.244  13.890  1.00 12.71  ? 72  LEU A CB  1 
ATOM   575  C  CG  . LEU A  1 72  ? 35.412  -1.080  14.615  1.00 12.47  ? 72  LEU A CG  1 
ATOM   576  C  CD1 . LEU A  1 72  ? 34.482  -1.675  13.547  1.00 13.66  ? 72  LEU A CD1 1 
ATOM   577  C  CD2 . LEU A  1 72  ? 35.981  -2.125  15.541  1.00 15.35  ? 72  LEU A CD2 1 
ATOM   578  N  N   . PRO A  1 73  ? 39.651  0.578   13.892  1.00 14.45  ? 73  PRO A N   1 
ATOM   579  C  CA  . PRO A  1 73  ? 40.760  1.239   13.234  1.00 15.70  ? 73  PRO A CA  1 
ATOM   580  C  C   . PRO A  1 73  ? 40.689  1.134   11.680  1.00 16.35  ? 73  PRO A C   1 
ATOM   581  O  O   . PRO A  1 73  ? 40.205  0.104   11.191  1.00 15.29  ? 73  PRO A O   1 
ATOM   582  C  CB  . PRO A  1 73  ? 41.944  0.426   13.802  1.00 16.45  ? 73  PRO A CB  1 
ATOM   583  C  CG  . PRO A  1 73  ? 41.399  -0.975  13.972  1.00 15.82  ? 73  PRO A CG  1 
ATOM   584  C  CD  . PRO A  1 73  ? 39.906  -0.758  14.422  1.00 14.94  ? 73  PRO A CD  1 
ATOM   585  N  N   . SER A  1 74  ? 41.362  2.065   10.957  1.00 17.32  ? 74  SER A N   1 
ATOM   586  C  CA  . SER A  1 74  ? 41.154  2.091   9.518   1.00 19.42  ? 74  SER A CA  1 
ATOM   587  C  C   . SER A  1 74  ? 42.057  1.039   8.846   1.00 16.93  ? 74  SER A C   1 
ATOM   588  O  O   . SER A  1 74  ? 41.837  0.819   7.668   1.00 20.36  ? 74  SER A O   1 
ATOM   589  C  CB  . SER A  1 74  ? 41.375  3.480   9.000   1.00 26.88  ? 74  SER A CB  1 
ATOM   590  O  OG  . SER A  1 74  ? 42.776  3.769   9.291   1.00 27.55  ? 74  SER A OG  1 
ATOM   591  N  N   . ASP A  1 75  ? 42.934  0.294   9.575   1.00 16.46  ? 75  ASP A N   1 
ATOM   592  C  CA  . ASP A  1 75  ? 43.632  -0.811  8.908   1.00 19.23  ? 75  ASP A CA  1 
ATOM   593  C  C   . ASP A  1 75  ? 42.750  -2.072  8.811   1.00 16.37  ? 75  ASP A C   1 
ATOM   594  O  O   . ASP A  1 75  ? 43.019  -3.032  8.101   1.00 20.06  ? 75  ASP A O   1 
ATOM   595  C  CB  . ASP A  1 75  ? 44.980  -1.113  9.598   1.00 20.93  ? 75  ASP A CB  1 
ATOM   596  C  CG  . ASP A  1 75  ? 44.715  -1.484  11.048  1.00 22.09  ? 75  ASP A CG  1 
ATOM   597  O  OD1 . ASP A  1 75  ? 44.336  -0.593  11.859  1.00 27.62  ? 75  ASP A OD1 1 
ATOM   598  O  OD2 . ASP A  1 75  ? 45.007  -2.585  11.455  1.00 26.81  ? 75  ASP A OD2 1 
ATOM   599  N  N   . MET A  1 76  ? 41.627  -2.070  9.527   1.00 15.54  ? 76  MET A N   1 
ATOM   600  C  CA  . MET A  1 76  ? 40.650  -3.143  9.398   1.00 14.14  ? 76  MET A CA  1 
ATOM   601  C  C   . MET A  1 76  ? 39.823  -2.884  8.122   1.00 12.78  ? 76  MET A C   1 
ATOM   602  O  O   . MET A  1 76  ? 39.379  -1.714  7.970   1.00 14.08  ? 76  MET A O   1 
ATOM   603  C  CB  . MET A  1 76  ? 39.759  -3.045  10.634  1.00 16.54  ? 76  MET A CB  1 
ATOM   604  C  CG  . MET A  1 76  ? 38.644  -4.006  10.620  1.00 15.18  ? 76  MET A CG  1 
ATOM   605  S  SD  . MET A  1 76  ? 37.784  -3.946  12.272  1.00 15.70  ? 76  MET A SD  1 
ATOM   606  C  CE  . MET A  1 76  ? 36.165  -4.661  11.762  1.00 15.08  ? 76  MET A CE  1 
ATOM   607  N  N   . HIS A  1 77  ? 39.646  -3.848  7.268   1.00 12.96  ? 77  HIS A N   1 
ATOM   608  C  CA  . HIS A  1 77  ? 38.925  -3.531  6.013   1.00 13.86  ? 77  HIS A CA  1 
ATOM   609  C  C   . HIS A  1 77  ? 38.356  -4.809  5.437   1.00 12.76  ? 77  HIS A C   1 
ATOM   610  O  O   . HIS A  1 77  ? 38.650  -5.902  5.751   1.00 14.42  ? 77  HIS A O   1 
ATOM   611  C  CB  . HIS A  1 77  ? 39.862  -2.748  5.028   1.00 15.25  ? 77  HIS A CB  1 
ATOM   612  C  CG  . HIS A  1 77  ? 41.031  -3.612  4.575   1.00 16.60  ? 77  HIS A CG  1 
ATOM   613  N  ND1 . HIS A  1 77  ? 42.196  -3.583  5.213   1.00 19.96  ? 77  HIS A ND1 1 
ATOM   614  C  CD2 . HIS A  1 77  ? 41.195  -4.413  3.489   1.00 19.24  ? 77  HIS A CD2 1 
ATOM   615  C  CE1 . HIS A  1 77  ? 43.079  -4.291  4.518   1.00 18.58  ? 77  HIS A CE1 1 
ATOM   616  N  NE2 . HIS A  1 77  ? 42.491  -4.845  3.479   1.00 19.88  ? 77  HIS A NE2 1 
ATOM   617  N  N   . ILE A  1 78  ? 37.405  -4.551  4.494   1.00 13.82  ? 78  ILE A N   1 
ATOM   618  C  CA  . ILE A  1 78  ? 36.823  -5.568  3.604   1.00 14.56  ? 78  ILE A CA  1 
ATOM   619  C  C   . ILE A  1 78  ? 37.604  -5.580  2.323   1.00 14.81  ? 78  ILE A C   1 
ATOM   620  O  O   . ILE A  1 78  ? 37.765  -4.514  1.725   1.00 17.08  ? 78  ILE A O   1 
ATOM   621  C  CB  . ILE A  1 78  ? 35.270  -5.218  3.299   1.00 15.50  ? 78  ILE A CB  1 
ATOM   622  C  CG1 . ILE A  1 78  ? 34.429  -5.238  4.567   1.00 16.95  ? 78  ILE A CG1 1 
ATOM   623  C  CG2 . ILE A  1 78  ? 34.728  -6.159  2.214   1.00 18.92  ? 78  ILE A CG2 1 
ATOM   624  C  CD1 . ILE A  1 78  ? 33.097  -4.498  4.339   1.00 17.69  ? 78  ILE A CD1 1 
ATOM   625  N  N   . GLN A  1 79  ? 37.909  -6.781  1.871   1.00 15.83  ? 79  GLN A N   1 
ATOM   626  C  CA  . GLN A  1 79  ? 38.487  -6.949  0.554   1.00 18.59  ? 79  GLN A CA  1 
ATOM   627  C  C   . GLN A  1 79  ? 37.422  -7.797  -0.221  1.00 18.29  ? 79  GLN A C   1 
ATOM   628  O  O   . GLN A  1 79  ? 36.728  -8.695  0.303   1.00 19.87  ? 79  GLN A O   1 
ATOM   629  C  CB  . GLN A  1 79  ? 39.893  -7.668  0.654   1.00 23.03  ? 79  GLN A CB  1 
ATOM   630  C  CG  . GLN A  1 79  ? 40.500  -8.101  -0.642  1.00 28.97  ? 79  GLN A CG  1 
ATOM   631  C  CD  . GLN A  1 79  ? 41.842  -8.724  -0.357  1.00 41.06  ? 79  GLN A CD  1 
ATOM   632  O  OE1 . GLN A  1 79  ? 42.886  -8.324  -0.919  1.00 70.23  ? 79  GLN A OE1 1 
ATOM   633  N  NE2 . GLN A  1 79  ? 41.842  -9.745  0.512   1.00 49.59  ? 79  GLN A NE2 1 
ATOM   634  N  N   . GLY A  1 80  ? 37.300  -7.476  -1.472  1.00 21.08  ? 80  GLY A N   1 
ATOM   635  C  CA  . GLY A  1 80  ? 36.380  -8.203  -2.412  1.00 22.83  ? 80  GLY A CA  1 
ATOM   636  C  C   . GLY A  1 80  ? 35.348  -7.303  -3.117  1.00 20.37  ? 80  GLY A C   1 
ATOM   637  O  O   . GLY A  1 80  ? 34.712  -7.714  -4.103  1.00 25.20  ? 80  GLY A O   1 
ATOM   638  N  N   . LEU A  1 81  ? 35.180  -6.092  -2.658  1.00 17.87  ? 81  LEU A N   1 
ATOM   639  C  CA  . LEU A  1 81  ? 34.328  -5.090  -3.305  1.00 21.29  ? 81  LEU A CA  1 
ATOM   640  C  C   . LEU A  1 81  ? 35.164  -4.308  -4.323  1.00 22.42  ? 81  LEU A C   1 
ATOM   641  O  O   . LEU A  1 81  ? 36.462  -4.516  -4.399  1.00 25.83  ? 81  LEU A O   1 
ATOM   642  C  CB  . LEU A  1 81  ? 33.639  -4.129  -2.278  1.00 19.53  ? 81  LEU A CB  1 
ATOM   643  C  CG  . LEU A  1 81  ? 32.721  -4.858  -1.252  1.00 19.22  ? 81  LEU A CG  1 
ATOM   644  C  CD1 . LEU A  1 81  ? 32.275  -3.870  -0.140  1.00 21.10  ? 81  LEU A CD1 1 
ATOM   645  C  CD2 . LEU A  1 81  ? 31.521  -5.508  -1.989  1.00 21.94  ? 81  LEU A CD2 1 
ATOM   646  N  N   . GLN A  1 82  ? 34.493  -3.487  -5.120  1.00 28.19  ? 82  GLN A N   1 
ATOM   647  C  CA  . GLN A  1 82  ? 35.185  -2.704  -6.148  1.00 30.97  ? 82  GLN A CA  1 
ATOM   648  C  C   . GLN A  1 82  ? 36.368  -1.928  -5.573  1.00 28.56  ? 82  GLN A C   1 
ATOM   649  O  O   . GLN A  1 82  ? 37.456  -1.902  -6.149  1.00 28.55  ? 82  GLN A O   1 
ATOM   650  C  CB  . GLN A  1 82  ? 34.216  -1.749  -6.850  1.00 42.38  ? 82  GLN A CB  1 
ATOM   651  C  CG  . GLN A  1 82  ? 33.810  -2.194  -8.247  1.00 60.27  ? 82  GLN A CG  1 
ATOM   652  C  CD  . GLN A  1 82  ? 34.624  -1.524  -9.337  1.00 73.06  ? 82  GLN A CD  1 
ATOM   653  O  OE1 . GLN A  1 82  ? 34.881  -0.321  -9.288  1.00 53.76  ? 82  GLN A OE1 1 
ATOM   654  N  NE2 . GLN A  1 82  ? 35.031  -2.303  -10.333 1.00 60.93  ? 82  GLN A NE2 1 
ATOM   655  N  N   . SER A  1 83  ? 36.133  -1.295  -4.431  1.00 19.06  ? 83  SER A N   1 
ATOM   656  C  CA  . SER A  1 83  ? 37.112  -0.522  -3.740  1.00 16.37  ? 83  SER A CA  1 
ATOM   657  C  C   . SER A  1 83  ? 37.326  -1.154  -2.379  1.00 15.14  ? 83  SER A C   1 
ATOM   658  O  O   . SER A  1 83  ? 36.499  -1.932  -1.913  1.00 14.77  ? 83  SER A O   1 
ATOM   659  C  CB  . SER A  1 83  ? 36.563  0.860   -3.451  1.00 16.97  ? 83  SER A CB  1 
ATOM   660  O  OG  . SER A  1 83  ? 36.271  1.645   -4.617  1.00 19.68  ? 83  SER A OG  1 
ATOM   661  N  N   . ARG A  1 84  ? 38.425  -0.762  -1.744  1.00 14.71  ? 84  ARG A N   1 
ATOM   662  C  CA  . ARG A  1 84  ? 38.628  -1.190  -0.359  1.00 12.98  ? 84  ARG A CA  1 
ATOM   663  C  C   . ARG A  1 84  ? 37.710  -0.295  0.515   1.00 13.25  ? 84  ARG A C   1 
ATOM   664  O  O   . ARG A  1 84  ? 37.604  0.877   0.348   1.00 13.22  ? 84  ARG A O   1 
ATOM   665  C  CB  . ARG A  1 84  ? 40.085  -0.892  0.067   1.00 14.41  ? 84  ARG A CB  1 
ATOM   666  C  CG  . ARG A  1 84  ? 40.300  -1.211  1.573   1.00 13.81  ? 84  ARG A CG  1 
ATOM   667  C  CD  . ARG A  1 84  ? 41.714  -1.002  2.041   1.00 14.77  ? 84  ARG A CD  1 
ATOM   668  N  NE  . ARG A  1 84  ? 42.562  -2.054  1.524   1.00 14.27  ? 84  ARG A NE  1 
ATOM   669  C  CZ  . ARG A  1 84  ? 43.836  -2.162  1.838   1.00 13.86  ? 84  ARG A CZ  1 
ATOM   670  N  NH1 . ARG A  1 84  ? 44.379  -1.278  2.671   1.00 16.25  ? 84  ARG A NH1 1 
ATOM   671  N  NH2 . ARG A  1 84  ? 44.544  -3.156  1.329   1.00 16.82  ? 84  ARG A NH2 1 
ATOM   672  N  N   . TYR A  1 85  ? 37.016  -1.002  1.470   1.00 12.62  ? 85  TYR A N   1 
ATOM   673  C  CA  . TYR A  1 85  ? 36.218  -0.298  2.454   1.00 12.25  ? 85  TYR A CA  1 
ATOM   674  C  C   . TYR A  1 85  ? 36.831  -0.550  3.818   1.00 11.75  ? 85  TYR A C   1 
ATOM   675  O  O   . TYR A  1 85  ? 36.959  -1.708  4.223   1.00 13.36  ? 85  TYR A O   1 
ATOM   676  C  CB  . TYR A  1 85  ? 34.735  -0.747  2.415   1.00 12.26  ? 85  TYR A CB  1 
ATOM   677  C  CG  . TYR A  1 85  ? 33.997  -0.208  1.241   1.00 12.04  ? 85  TYR A CG  1 
ATOM   678  C  CD1 . TYR A  1 85  ? 34.084  -0.824  -0.017  1.00 15.06  ? 85  TYR A CD1 1 
ATOM   679  C  CD2 . TYR A  1 85  ? 33.206  0.932   1.380   1.00 12.63  ? 85  TYR A CD2 1 
ATOM   680  C  CE1 . TYR A  1 85  ? 33.351  -0.296  -1.140  1.00 14.58  ? 85  TYR A CE1 1 
ATOM   681  C  CE2 . TYR A  1 85  ? 32.458  1.497   0.284   1.00 13.59  ? 85  TYR A CE2 1 
ATOM   682  C  CZ  . TYR A  1 85  ? 32.625  0.893   -0.910  1.00 14.59  ? 85  TYR A CZ  1 
ATOM   683  O  OH  . TYR A  1 85  ? 31.909  1.419   -1.968  1.00 19.40  ? 85  TYR A OH  1 
ATOM   684  N  N   . SER A  1 86  ? 37.237  0.504   4.492   1.00 12.15  ? 86  SER A N   1 
ATOM   685  C  CA  . SER A  1 86  ? 37.952  0.376   5.773   1.00 11.84  ? 86  SER A CA  1 
ATOM   686  C  C   . SER A  1 86  ? 36.985  0.624   6.939   1.00 11.21  ? 86  SER A C   1 
ATOM   687  O  O   . SER A  1 86  ? 36.074  1.475   6.819   1.00 11.36  ? 86  SER A O   1 
ATOM   688  C  CB  . SER A  1 86  ? 39.058  1.436   5.810   1.00 13.68  ? 86  SER A CB  1 
ATOM   689  O  OG  . SER A  1 86  ? 40.051  1.157   4.863   1.00 14.84  ? 86  SER A OG  1 
ATOM   690  N  N   . ALA A  1 87  ? 37.162  -0.062  8.034   1.00 12.03  ? 87  ALA A N   1 
ATOM   691  C  CA  . ALA A  1 87  ? 36.229  0.041   9.142   1.00 11.71  ? 87  ALA A CA  1 
ATOM   692  C  C   . ALA A  1 87  ? 36.302  1.365   9.768   1.00 11.86  ? 87  ALA A C   1 
ATOM   693  O  O   . ALA A  1 87  ? 37.379  2.019   9.846   1.00 13.95  ? 87  ALA A O   1 
ATOM   694  C  CB  . ALA A  1 87  ? 36.537  -1.025  10.206  1.00 13.95  ? 87  ALA A CB  1 
ATOM   695  N  N   . THR A  1 88  ? 35.167  1.817   10.340  1.00 11.88  ? 88  THR A N   1 
ATOM   696  C  CA  . THR A  1 88  ? 35.136  2.996   11.174  1.00 11.73  ? 88  THR A CA  1 
ATOM   697  C  C   . THR A  1 88  ? 34.452  2.777   12.498  1.00 10.49  ? 88  THR A C   1 
ATOM   698  O  O   . THR A  1 88  ? 34.916  3.327   13.528  1.00 12.23  ? 88  THR A O   1 
ATOM   699  C  CB  . THR A  1 88  ? 34.483  4.197   10.424  1.00 12.72  ? 88  THR A CB  1 
ATOM   700  O  OG1 . THR A  1 88  ? 34.448  5.338   11.205  1.00 14.80  ? 88  THR A OG1 1 
ATOM   701  C  CG2 . THR A  1 88  ? 33.088  3.952   9.883   1.00 13.04  ? 88  THR A CG2 1 
ATOM   702  N  N   . GLN A  1 89  ? 33.364  1.998   12.593  1.00 11.07  ? 89  GLN A N   1 
ATOM   703  C  CA  . GLN A  1 89  ? 32.700  1.750   13.888  1.00 10.82  ? 89  GLN A CA  1 
ATOM   704  C  C   . GLN A  1 89  ? 31.761  0.588   13.719  1.00 10.53  ? 89  GLN A C   1 
ATOM   705  O  O   . GLN A  1 89  ? 31.334  0.271   12.618  1.00 11.06  ? 89  GLN A O   1 
ATOM   706  C  CB  . GLN A  1 89  ? 31.967  2.979   14.441  1.00 12.54  ? 89  GLN A CB  1 
ATOM   707  C  CG  . GLN A  1 89  ? 31.046  3.609   13.407  1.00 15.08  ? 89  GLN A CG  1 
ATOM   708  C  CD  . GLN A  1 89  ? 29.625  3.511   13.792  1.00 14.12  ? 89  GLN A CD  1 
ATOM   709  O  OE1 . GLN A  1 89  ? 29.158  2.357   14.121  1.00 14.18  ? 89  GLN A OE1 1 
ATOM   710  N  NE2 . GLN A  1 89  ? 28.852  4.504   13.612  1.00 18.65  ? 89  GLN A NE2 1 
ATOM   711  N  N   . LEU A  1 90  ? 31.394  -0.030  14.846  1.00 10.76  ? 90  LEU A N   1 
ATOM   712  C  CA  . LEU A  1 90  ? 30.255  -0.936  14.880  1.00 9.95   ? 90  LEU A CA  1 
ATOM   713  C  C   . LEU A  1 90  ? 29.298  -0.489  15.937  1.00 10.36  ? 90  LEU A C   1 
ATOM   714  O  O   . LEU A  1 90  ? 29.648  0.200   16.880  1.00 10.48  ? 90  LEU A O   1 
ATOM   715  C  CB  . LEU A  1 90  ? 30.674  -2.390  14.994  1.00 11.03  ? 90  LEU A CB  1 
ATOM   716  C  CG  . LEU A  1 90  ? 31.493  -2.866  16.248  1.00 11.32  ? 90  LEU A CG  1 
ATOM   717  C  CD1 . LEU A  1 90  ? 30.574  -2.929  17.489  1.00 12.98  ? 90  LEU A CD1 1 
ATOM   718  C  CD2 . LEU A  1 90  ? 32.130  -4.227  15.960  1.00 13.58  ? 90  LEU A CD2 1 
ATOM   719  N  N   . HIS A  1 91  ? 28.034  -0.920  15.816  1.00 10.49  ? 91  HIS A N   1 
ATOM   720  C  CA  . HIS A  1 91  ? 26.996  -0.589  16.782  1.00 9.74   ? 91  HIS A CA  1 
ATOM   721  C  C   . HIS A  1 91  ? 25.827  -1.552  16.616  1.00 9.45   ? 91  HIS A C   1 
ATOM   722  O  O   . HIS A  1 91  ? 25.850  -2.392  15.719  1.00 9.79   ? 91  HIS A O   1 
ATOM   723  C  CB  . HIS A  1 91  ? 26.497  0.878   16.593  1.00 10.38  ? 91  HIS A CB  1 
ATOM   724  C  CG  . HIS A  1 91  ? 25.891  1.081   15.265  1.00 9.55   ? 91  HIS A CG  1 
ATOM   725  N  ND1 . HIS A  1 91  ? 26.578  1.538   14.168  1.00 10.00  ? 91  HIS A ND1 1 
ATOM   726  C  CD2 . HIS A  1 91  ? 24.643  0.763   14.806  1.00 9.57   ? 91  HIS A CD2 1 
ATOM   727  C  CE1 . HIS A  1 91  ? 25.751  1.497   13.098  1.00 9.75   ? 91  HIS A CE1 1 
ATOM   728  N  NE2 . HIS A  1 91  ? 24.563  1.037   13.460  1.00 9.04   ? 91  HIS A NE2 1 
ATOM   729  N  N   . LEU A  1 92  ? 24.848  -1.454  17.510  1.00 10.33  ? 92  LEU A N   1 
ATOM   730  C  CA  . LEU A  1 92  ? 23.749  -2.393  17.485  1.00 9.42   ? 92  LEU A CA  1 
ATOM   731  C  C   . LEU A  1 92  ? 22.372  -1.697  17.512  1.00 9.10   ? 92  LEU A C   1 
ATOM   732  O  O   . LEU A  1 92  ? 22.240  -0.537  17.841  1.00 10.11  ? 92  LEU A O   1 
ATOM   733  C  CB  . LEU A  1 92  ? 23.807  -3.344  18.717  1.00 12.46  ? 92  LEU A CB  1 
ATOM   734  C  CG  . LEU A  1 92  ? 25.054  -4.263  18.703  1.00 10.99  ? 92  LEU A CG  1 
ATOM   735  C  CD1 . LEU A  1 92  ? 26.138  -3.745  19.596  1.00 21.62  ? 92  LEU A CD1 1 
ATOM   736  C  CD2 . LEU A  1 92  ? 24.638  -5.656  18.940  1.00 16.94  ? 92  LEU A CD2 1 
ATOM   737  N  N   . HIS A  1 93  ? 21.349  -2.480  17.153  1.00 9.26   ? 93  HIS A N   1 
ATOM   738  C  CA  . HIS A  1 93  ? 19.943  -2.029  17.253  1.00 9.61   ? 93  HIS A CA  1 
ATOM   739  C  C   . HIS A  1 93  ? 19.175  -3.167  17.905  1.00 8.75   ? 93  HIS A C   1 
ATOM   740  O  O   . HIS A  1 93  ? 19.436  -4.351  17.655  1.00 9.76   ? 93  HIS A O   1 
ATOM   741  C  CB  . HIS A  1 93  ? 19.361  -1.843  15.808  1.00 10.07  ? 93  HIS A CB  1 
ATOM   742  C  CG  . HIS A  1 93  ? 20.125  -0.818  15.012  1.00 9.04   ? 93  HIS A CG  1 
ATOM   743  N  ND1 . HIS A  1 93  ? 19.782  0.496   14.994  1.00 10.28  ? 93  HIS A ND1 1 
ATOM   744  C  CD2 . HIS A  1 93  ? 21.202  -0.932  14.213  1.00 8.84   ? 93  HIS A CD2 1 
ATOM   745  C  CE1 . HIS A  1 93  ? 20.627  1.181   14.178  1.00 9.32   ? 93  HIS A CE1 1 
ATOM   746  N  NE2 . HIS A  1 93  ? 21.522  0.345   13.713  1.00 9.31   ? 93  HIS A NE2 1 
ATOM   747  N  N   . TRP A  1 94  ? 18.200  -2.823  18.771  1.00 10.06  ? 94  TRP A N   1 
ATOM   748  C  CA  . TRP A  1 94  ? 17.450  -3.829  19.500  1.00 9.68   ? 94  TRP A CA  1 
ATOM   749  C  C   . TRP A  1 94  ? 16.074  -3.292  19.849  1.00 10.39  ? 94  TRP A C   1 
ATOM   750  O  O   . TRP A  1 94  ? 15.730  -2.127  19.590  1.00 10.33  ? 94  TRP A O   1 
ATOM   751  C  CB  . TRP A  1 94  ? 18.253  -4.212  20.789  1.00 10.82  ? 94  TRP A CB  1 
ATOM   752  C  CG  . TRP A  1 94  ? 18.506  -3.095  21.695  1.00 10.55  ? 94  TRP A CG  1 
ATOM   753  C  CD1 . TRP A  1 94  ? 17.665  -2.592  22.685  1.00 11.71  ? 94  TRP A CD1 1 
ATOM   754  C  CD2 . TRP A  1 94  ? 19.691  -2.247  21.707  1.00 10.59  ? 94  TRP A CD2 1 
ATOM   755  N  NE1 . TRP A  1 94  ? 18.307  -1.504  23.331  1.00 11.84  ? 94  TRP A NE1 1 
ATOM   756  C  CE2 . TRP A  1 94  ? 19.556  -1.315  22.763  1.00 11.23  ? 94  TRP A CE2 1 
ATOM   757  C  CE3 . TRP A  1 94  ? 20.855  -2.196  20.920  1.00 10.64  ? 94  TRP A CE3 1 
ATOM   758  C  CZ2 . TRP A  1 94  ? 20.536  -0.343  23.057  1.00 12.13  ? 94  TRP A CZ2 1 
ATOM   759  C  CZ3 . TRP A  1 94  ? 21.821  -1.278  21.217  1.00 11.09  ? 94  TRP A CZ3 1 
ATOM   760  C  CH2 . TRP A  1 94  ? 21.659  -0.365  22.252  1.00 11.79  ? 94  TRP A CH2 1 
ATOM   761  N  N   . GLY A  1 95  ? 15.241  -4.196  20.422  1.00 10.24  ? 95  GLY A N   1 
ATOM   762  C  CA  . GLY A  1 95  ? 13.845  -3.938  20.783  1.00 11.00  ? 95  GLY A CA  1 
ATOM   763  C  C   . GLY A  1 95  ? 13.751  -3.631  22.261  1.00 11.49  ? 95  GLY A C   1 
ATOM   764  O  O   . GLY A  1 95  ? 14.385  -2.738  22.821  1.00 11.58  ? 95  GLY A O   1 
ATOM   765  N  N   . ASN A  1 96  ? 12.924  -4.430  22.956  1.00 11.42  ? 96  ASN A N   1 
ATOM   766  C  CA  . ASN A  1 96  ? 12.780  -4.212  24.401  1.00 12.30  ? 96  ASN A CA  1 
ATOM   767  C  C   . ASN A  1 96  ? 12.253  -5.533  24.972  1.00 13.30  ? 96  ASN A C   1 
ATOM   768  O  O   . ASN A  1 96  ? 11.790  -6.399  24.239  1.00 12.84  ? 96  ASN A O   1 
ATOM   769  C  CB  . ASN A  1 96  ? 11.817  -3.070  24.724  1.00 14.19  ? 96  ASN A CB  1 
ATOM   770  C  CG  . ASN A  1 96  ? 10.383  -3.418  24.470  1.00 16.05  ? 96  ASN A CG  1 
ATOM   771  O  OD1 . ASN A  1 96  ? 9.711   -3.970  25.342  1.00 20.01  ? 96  ASN A OD1 1 
ATOM   772  N  ND2 . ASN A  1 96  ? 9.872   -3.131  23.272  1.00 17.14  ? 96  ASN A ND2 1 
ATOM   773  N  N   . PRO A  1 97  ? 12.321  -5.698  26.344  1.00 12.64  ? 97  PRO A N   1 
ATOM   774  C  CA  . PRO A  1 97  ? 12.010  -7.022  26.883  1.00 14.22  ? 97  PRO A CA  1 
ATOM   775  C  C   . PRO A  1 97  ? 10.570  -7.464  26.616  1.00 13.55  ? 97  PRO A C   1 
ATOM   776  O  O   . PRO A  1 97  ? 10.308  -8.640  26.639  1.00 16.45  ? 97  PRO A O   1 
ATOM   777  C  CB  . PRO A  1 97  ? 12.325  -6.841  28.349  1.00 16.25  ? 97  PRO A CB  1 
ATOM   778  C  CG  . PRO A  1 97  ? 13.390  -5.753  28.404  1.00 17.62  ? 97  PRO A CG  1 
ATOM   779  C  CD  . PRO A  1 97  ? 12.903  -4.832  27.320  1.00 15.05  ? 97  PRO A CD  1 
ATOM   780  N  N   . ASN A  1 98  ? 9.643   -6.503  26.481  1.00 13.88  ? 98  ASN A N   1 
ATOM   781  C  CA  . ASN A  1 98  ? 8.225   -6.910  26.202  1.00 15.47  ? 98  ASN A CA  1 
ATOM   782  C  C   . ASN A  1 98  ? 8.013   -7.221  24.742  1.00 15.03  ? 98  ASN A C   1 
ATOM   783  O  O   . ASN A  1 98  ? 6.961   -7.809  24.384  1.00 18.13  ? 98  ASN A O   1 
ATOM   784  C  CB  . ASN A  1 98  ? 7.285   -5.735  26.579  1.00 17.19  ? 98  ASN A CB  1 
ATOM   785  C  CG  . ASN A  1 98  ? 7.178   -5.569  28.075  1.00 25.63  ? 98  ASN A CG  1 
ATOM   786  O  OD1 . ASN A  1 98  ? 7.261   -6.463  28.893  1.00 32.40  ? 98  ASN A OD1 1 
ATOM   787  N  ND2 . ASN A  1 98  ? 6.750   -4.392  28.421  1.00 36.29  ? 98  ASN A ND2 1 
ATOM   788  N  N   . ASP A  1 99  ? 8.936   -6.872  23.844  1.00 14.12  ? 99  ASP A N   1 
ATOM   789  C  CA  . ASP A  1 99  ? 8.785   -7.188  22.465  1.00 14.74  ? 99  ASP A CA  1 
ATOM   790  C  C   . ASP A  1 99  ? 10.184  -7.276  21.882  1.00 13.03  ? 99  ASP A C   1 
ATOM   791  O  O   . ASP A  1 99  ? 10.725  -6.350  21.255  1.00 13.19  ? 99  ASP A O   1 
ATOM   792  C  CB  . ASP A  1 99  ? 7.925   -6.071  21.790  1.00 15.14  ? 99  ASP A CB  1 
ATOM   793  C  CG  . ASP A  1 99  ? 7.437   -6.485  20.396  1.00 15.33  ? 99  ASP A CG  1 
ATOM   794  O  OD1 . ASP A  1 99  ? 7.766   -7.541  19.875  1.00 20.28  ? 99  ASP A OD1 1 
ATOM   795  O  OD2 . ASP A  1 99  ? 6.607   -5.744  19.867  1.00 23.39  ? 99  ASP A OD2 1 
ATOM   796  N  N   . PRO A  1 100 ? 10.870  -8.395  22.109  1.00 12.52  ? 100 PRO A N   1 
ATOM   797  C  CA  . PRO A  1 100 ? 12.325  -8.497  21.922  1.00 12.63  ? 100 PRO A CA  1 
ATOM   798  C  C   . PRO A  1 100 ? 12.681  -8.848  20.462  1.00 12.58  ? 100 PRO A C   1 
ATOM   799  O  O   . PRO A  1 100 ? 13.257  -9.881  20.177  1.00 14.67  ? 100 PRO A O   1 
ATOM   800  C  CB  . PRO A  1 100 ? 12.767  -9.586  22.949  1.00 14.49  ? 100 PRO A CB  1 
ATOM   801  C  CG  . PRO A  1 100 ? 11.541  -10.495 22.869  1.00 14.71  ? 100 PRO A CG  1 
ATOM   802  C  CD  . PRO A  1 100 ? 10.351  -9.542  22.911  1.00 14.43  ? 100 PRO A CD  1 
ATOM   803  N  N   . HIS A  1 101 ? 12.245  -7.955  19.560  1.00 12.42  ? 101 HIS A N   1 
ATOM   804  C  CA  . HIS A  1 101 ? 12.305  -8.184  18.093  1.00 13.12  ? 101 HIS A CA  1 
ATOM   805  C  C   . HIS A  1 101 ? 12.704  -6.960  17.383  1.00 12.42  ? 101 HIS A C   1 
ATOM   806  O  O   . HIS A  1 101 ? 11.959  -6.384  16.636  1.00 17.39  ? 101 HIS A O   1 
ATOM   807  C  CB  . HIS A  1 101 ? 10.966  -8.727  17.560  1.00 15.86  ? 101 HIS A CB  1 
ATOM   808  C  CG  . HIS A  1 101 ? 10.460  -9.921  18.347  1.00 16.09  ? 101 HIS A CG  1 
ATOM   809  N  ND1 . HIS A  1 101 ? 10.924  -11.186 18.278  1.00 18.40  ? 101 HIS A ND1 1 
ATOM   810  C  CD2 . HIS A  1 101 ? 9.448   -9.933  19.246  1.00 16.95  ? 101 HIS A CD2 1 
ATOM   811  C  CE1 . HIS A  1 101 ? 10.222  -11.954 19.137  1.00 18.44  ? 101 HIS A CE1 1 
ATOM   812  N  NE2 . HIS A  1 101 ? 9.348   -11.179 19.747  1.00 18.28  ? 101 HIS A NE2 1 
ATOM   813  N  N   . GLY A  1 102 ? 13.929  -6.475  17.622  1.00 11.84  ? 102 GLY A N   1 
ATOM   814  C  CA  . GLY A  1 102 ? 14.371  -5.133  17.251  1.00 11.99  ? 102 GLY A CA  1 
ATOM   815  C  C   . GLY A  1 102 ? 15.445  -5.110  16.176  1.00 10.21  ? 102 GLY A C   1 
ATOM   816  O  O   . GLY A  1 102 ? 16.138  -4.102  16.065  1.00 11.57  ? 102 GLY A O   1 
ATOM   817  N  N   . SER A  1 103 ? 15.588  -6.157  15.327  1.00 10.07  ? 103 SER A N   1 
ATOM   818  C  CA  . SER A  1 103 ? 16.436  -5.988  14.144  1.00 9.93   ? 103 SER A CA  1 
ATOM   819  C  C   . SER A  1 103 ? 15.885  -4.897  13.248  1.00 9.83   ? 103 SER A C   1 
ATOM   820  O  O   . SER A  1 103 ? 14.666  -4.579  13.308  1.00 11.65  ? 103 SER A O   1 
ATOM   821  C  CB  . SER A  1 103 ? 16.634  -7.244  13.385  1.00 10.11  ? 103 SER A CB  1 
ATOM   822  O  OG  . SER A  1 103 ? 15.375  -7.709  12.776  1.00 10.47  ? 103 SER A OG  1 
ATOM   823  N  N   . GLU A  1 104 ? 16.705  -4.342  12.407  1.00 8.99   ? 104 GLU A N   1 
ATOM   824  C  CA  . GLU A  1 104 ? 16.201  -3.357  11.416  1.00 10.14  ? 104 GLU A CA  1 
ATOM   825  C  C   . GLU A  1 104 ? 15.752  -4.064  10.144  1.00 9.80   ? 104 GLU A C   1 
ATOM   826  O  O   . GLU A  1 104 ? 14.582  -3.857  9.709   1.00 9.84   ? 104 GLU A O   1 
ATOM   827  C  CB  . GLU A  1 104 ? 17.361  -2.374  11.050  1.00 9.97   ? 104 GLU A CB  1 
ATOM   828  C  CG  . GLU A  1 104 ? 17.869  -1.673  12.339  1.00 10.47  ? 104 GLU A CG  1 
ATOM   829  C  CD  . GLU A  1 104 ? 18.238  -0.281  12.022  1.00 9.50   ? 104 GLU A CD  1 
ATOM   830  O  OE1 . GLU A  1 104 ? 19.329  -0.096  11.415  1.00 10.54  ? 104 GLU A OE1 1 
ATOM   831  O  OE2 . GLU A  1 104 ? 17.453  0.662   12.303  1.00 11.01  ? 104 GLU A OE2 1 
ATOM   832  N  N   . HIS A  1 105 ? 16.588  -4.871  9.519   1.00 9.49   ? 105 HIS A N   1 
ATOM   833  C  CA  . HIS A  1 105 ? 16.095  -5.690  8.422   1.00 9.52   ? 105 HIS A CA  1 
ATOM   834  C  C   . HIS A  1 105 ? 15.180  -6.761  8.946   1.00 9.70   ? 105 HIS A C   1 
ATOM   835  O  O   . HIS A  1 105 ? 15.370  -7.267  10.076  1.00 10.67  ? 105 HIS A O   1 
ATOM   836  C  CB  . HIS A  1 105 ? 17.283  -6.307  7.678   1.00 9.54   ? 105 HIS A CB  1 
ATOM   837  C  CG  . HIS A  1 105 ? 18.077  -5.263  6.930   1.00 9.80   ? 105 HIS A CG  1 
ATOM   838  N  ND1 . HIS A  1 105 ? 19.125  -4.553  7.508   1.00 9.84   ? 105 HIS A ND1 1 
ATOM   839  C  CD2 . HIS A  1 105 ? 17.899  -4.716  5.694   1.00 9.95   ? 105 HIS A CD2 1 
ATOM   840  C  CE1 . HIS A  1 105 ? 19.541  -3.648  6.614   1.00 10.15  ? 105 HIS A CE1 1 
ATOM   841  N  NE2 . HIS A  1 105 ? 18.819  -3.729  5.500   1.00 10.60  ? 105 HIS A NE2 1 
ATOM   842  N  N   . THR A  1 106 ? 14.226  -7.176  8.131   1.00 9.75   ? 106 THR A N   1 
ATOM   843  C  CA  . THR A  1 106 ? 13.372  -8.337  8.415   1.00 10.61  ? 106 THR A CA  1 
ATOM   844  C  C   . THR A  1 106 ? 13.593  -9.318  7.283   1.00 10.10  ? 106 THR A C   1 
ATOM   845  O  O   . THR A  1 106 ? 14.023  -9.020  6.198   1.00 10.57  ? 106 THR A O   1 
ATOM   846  C  CB  . THR A  1 106 ? 11.892  -7.919  8.562   1.00 10.70  ? 106 THR A CB  1 
ATOM   847  O  OG1 . THR A  1 106 ? 11.449  -7.298  7.363   1.00 11.96  ? 106 THR A OG1 1 
ATOM   848  C  CG2 . THR A  1 106 ? 11.736  -6.937  9.682   1.00 12.71  ? 106 THR A CG2 1 
ATOM   849  N  N   . VAL A  1 107 ? 13.222  -10.622 7.574   1.00 11.18  ? 107 VAL A N   1 
ATOM   850  C  CA  . VAL A  1 107 ? 13.330  -11.658 6.621   1.00 11.37  ? 107 VAL A CA  1 
ATOM   851  C  C   . VAL A  1 107 ? 11.931  -12.315 6.491   1.00 11.16  ? 107 VAL A C   1 
ATOM   852  O  O   . VAL A  1 107 ? 11.426  -12.792 7.514   1.00 12.36  ? 107 VAL A O   1 
ATOM   853  C  CB  . VAL A  1 107 ? 14.383  -12.760 6.946   1.00 12.07  ? 107 VAL A CB  1 
ATOM   854  C  CG1 . VAL A  1 107 ? 14.341  -13.887 5.909   1.00 15.11  ? 107 VAL A CG1 1 
ATOM   855  C  CG2 . VAL A  1 107 ? 15.786  -12.124 7.047   1.00 14.67  ? 107 VAL A CG2 1 
ATOM   856  N  N   . SER A  1 108 ? 11.323  -12.196 5.317   1.00 12.84  ? 108 SER A N   1 
ATOM   857  C  CA  . SER A  1 108 ? 9.946   -12.700 5.138   1.00 13.53  ? 108 SER A CA  1 
ATOM   858  C  C   . SER A  1 108 ? 9.036   -12.140 6.221   1.00 12.48  ? 108 SER A C   1 
ATOM   859  O  O   . SER A  1 108 ? 8.175   -12.846 6.774   1.00 14.15  ? 108 SER A O   1 
ATOM   860  C  CB  . SER A  1 108 ? 9.946   -14.273 5.199   1.00 16.67  ? 108 SER A CB  1 
ATOM   861  O  OG  . SER A  1 108 ? 10.691  -14.774 4.139   1.00 20.66  ? 108 SER A OG  1 
ATOM   862  N  N   . GLY A  1 109 ? 9.212   -10.829 6.465   1.00 12.61  ? 109 GLY A N   1 
ATOM   863  C  CA  . GLY A  1 109 ? 8.367   -10.094 7.357   1.00 13.31  ? 109 GLY A CA  1 
ATOM   864  C  C   . GLY A  1 109 ? 8.744   -10.249 8.818   1.00 14.43  ? 109 GLY A C   1 
ATOM   865  O  O   . GLY A  1 109 ? 8.070   -9.609  9.623   1.00 16.84  ? 109 GLY A O   1 
ATOM   866  N  N   . GLN A  1 110 ? 9.705   -11.100 9.186   1.00 13.29  ? 110 GLN A N   1 
ATOM   867  C  CA  . GLN A  1 110 ? 10.048  -11.352 10.557  1.00 13.02  ? 110 GLN A CA  1 
ATOM   868  C  C   . GLN A  1 110 ? 11.299  -10.588 11.048  1.00 11.56  ? 110 GLN A C   1 
ATOM   869  O  O   . GLN A  1 110 ? 12.313  -10.624 10.384  1.00 11.69  ? 110 GLN A O   1 
ATOM   870  C  CB  . GLN A  1 110 ? 10.339  -12.827 10.759  1.00 14.36  ? 110 GLN A CB  1 
ATOM   871  C  CG  . GLN A  1 110 ? 9.212   -13.739 10.180  1.00 15.35  ? 110 GLN A CG  1 
ATOM   872  C  CD  . GLN A  1 110 ? 7.833   -13.285 10.602  1.00 16.95  ? 110 GLN A CD  1 
ATOM   873  O  OE1 . GLN A  1 110 ? 7.514   -13.265 11.811  1.00 18.17  ? 110 GLN A OE1 1 
ATOM   874  N  NE2 . GLN A  1 110 ? 6.993   -12.977 9.629   1.00 19.56  ? 110 GLN A NE2 1 
ATOM   875  N  N   . HIS A  1 111 ? 11.162  -9.932  12.205  1.00 11.71  ? 111 HIS A N   1 
ATOM   876  C  CA  . HIS A  1 111 ? 12.322  -9.383  12.874  1.00 12.24  ? 111 HIS A CA  1 
ATOM   877  C  C   . HIS A  1 111 ? 13.125  -10.434 13.549  1.00 12.43  ? 111 HIS A C   1 
ATOM   878  O  O   . HIS A  1 111 ? 12.587  -11.474 13.983  1.00 17.37  ? 111 HIS A O   1 
ATOM   879  C  CB  . HIS A  1 111 ? 11.960  -8.394  13.987  1.00 13.65  ? 111 HIS A CB  1 
ATOM   880  C  CG  . HIS A  1 111 ? 11.447  -7.081  13.470  1.00 12.80  ? 111 HIS A CG  1 
ATOM   881  N  ND1 . HIS A  1 111 ? 10.174  -6.753  13.087  1.00 16.53  ? 111 HIS A ND1 1 
ATOM   882  C  CD2 . HIS A  1 111 ? 12.228  -6.000  13.272  1.00 11.47  ? 111 HIS A CD2 1 
ATOM   883  C  CE1 . HIS A  1 111 ? 10.178  -5.498  12.676  1.00 14.49  ? 111 HIS A CE1 1 
ATOM   884  N  NE2 . HIS A  1 111 ? 11.415  -5.006  12.708  1.00 16.15  ? 111 HIS A NE2 1 
ATOM   885  N  N   . PHE A  1 112 ? 14.404  -10.196 13.688  1.00 11.37  ? 112 PHE A N   1 
ATOM   886  C  CA  . PHE A  1 112 ? 15.275  -10.950 14.619  1.00 10.96  ? 112 PHE A CA  1 
ATOM   887  C  C   . PHE A  1 112 ? 15.324  -10.120 15.904  1.00 10.30  ? 112 PHE A C   1 
ATOM   888  O  O   . PHE A  1 112 ? 14.807  -8.970  15.956  1.00 10.86  ? 112 PHE A O   1 
ATOM   889  C  CB  . PHE A  1 112 ? 16.639  -11.145 13.967  1.00 11.05  ? 112 PHE A CB  1 
ATOM   890  C  CG  . PHE A  1 112 ? 16.587  -12.266 12.929  1.00 12.49  ? 112 PHE A CG  1 
ATOM   891  C  CD1 . PHE A  1 112 ? 16.054  -12.036 11.619  1.00 16.83  ? 112 PHE A CD1 1 
ATOM   892  C  CD2 . PHE A  1 112 ? 17.056  -13.532 13.282  1.00 15.77  ? 112 PHE A CD2 1 
ATOM   893  C  CE1 . PHE A  1 112 ? 16.017  -13.167 10.741  1.00 21.07  ? 112 PHE A CE1 1 
ATOM   894  C  CE2 . PHE A  1 112 ? 17.030  -14.590 12.397  1.00 19.92  ? 112 PHE A CE2 1 
ATOM   895  C  CZ  . PHE A  1 112 ? 16.491  -14.402 11.212  1.00 22.44  ? 112 PHE A CZ  1 
ATOM   896  N  N   . ALA A  1 113 ? 15.951  -10.678 16.940  1.00 10.30  ? 113 ALA A N   1 
ATOM   897  C  CA  . ALA A  1 113 ? 15.986  -9.990  18.229  1.00 10.84  ? 113 ALA A CA  1 
ATOM   898  C  C   . ALA A  1 113 ? 16.751  -8.683  18.152  1.00 10.23  ? 113 ALA A C   1 
ATOM   899  O  O   . ALA A  1 113 ? 16.376  -7.706  18.803  1.00 10.75  ? 113 ALA A O   1 
ATOM   900  C  CB  . ALA A  1 113 ? 16.559  -10.879 19.301  1.00 12.75  ? 113 ALA A CB  1 
ATOM   901  N  N   . ALA A  1 114 ? 17.880  -8.683  17.390  1.00 10.26  ? 114 ALA A N   1 
ATOM   902  C  CA  . ALA A  1 114 ? 18.742  -7.472  17.356  1.00 9.84   ? 114 ALA A CA  1 
ATOM   903  C  C   . ALA A  1 114 ? 19.528  -7.554  16.053  1.00 9.31   ? 114 ALA A C   1 
ATOM   904  O  O   . ALA A  1 114 ? 19.460  -8.543  15.308  1.00 9.66   ? 114 ALA A O   1 
ATOM   905  C  CB  . ALA A  1 114 ? 19.621  -7.407  18.633  1.00 11.34  ? 114 ALA A CB  1 
ATOM   906  N  N   . GLU A  1 115 ? 20.328  -6.526  15.840  1.00 9.51   ? 115 GLU A N   1 
ATOM   907  C  CA  . GLU A  1 115 ? 21.138  -6.501  14.608  1.00 9.56   ? 115 GLU A CA  1 
ATOM   908  C  C   . GLU A  1 115 ? 22.424  -5.716  14.879  1.00 9.55   ? 115 GLU A C   1 
ATOM   909  O  O   . GLU A  1 115 ? 22.366  -4.643  15.525  1.00 10.72  ? 115 GLU A O   1 
ATOM   910  C  CB  . GLU A  1 115 ? 20.328  -5.845  13.463  1.00 10.15  ? 115 GLU A CB  1 
ATOM   911  C  CG  . GLU A  1 115 ? 20.969  -5.879  12.089  1.00 9.65   ? 115 GLU A CG  1 
ATOM   912  C  CD  . GLU A  1 115 ? 20.000  -5.496  10.968  1.00 9.62   ? 115 GLU A CD  1 
ATOM   913  O  OE1 . GLU A  1 115 ? 18.779  -5.732  11.140  1.00 10.18  ? 115 GLU A OE1 1 
ATOM   914  O  OE2 . GLU A  1 115 ? 20.474  -4.993  9.915   1.00 10.54  ? 115 GLU A OE2 1 
ATOM   915  N  N   . LEU A  1 116 ? 23.556  -6.267  14.442  1.00 9.34   ? 116 LEU A N   1 
ATOM   916  C  CA  . LEU A  1 116 ? 24.873  -5.595  14.538  1.00 9.63   ? 116 LEU A CA  1 
ATOM   917  C  C   . LEU A  1 116 ? 25.194  -5.037  13.163  1.00 8.71   ? 116 LEU A C   1 
ATOM   918  O  O   . LEU A  1 116 ? 25.043  -5.708  12.158  1.00 9.26   ? 116 LEU A O   1 
ATOM   919  C  CB  . LEU A  1 116 ? 25.922  -6.665  14.927  1.00 10.75  ? 116 LEU A CB  1 
ATOM   920  C  CG  . LEU A  1 116 ? 27.404  -6.219  14.814  1.00 10.76  ? 116 LEU A CG  1 
ATOM   921  C  CD1 . LEU A  1 116 ? 27.758  -5.283  15.952  1.00 13.43  ? 116 LEU A CD1 1 
ATOM   922  C  CD2 . LEU A  1 116 ? 28.337  -7.458  14.764  1.00 13.39  ? 116 LEU A CD2 1 
ATOM   923  N  N   . HIS A  1 117 ? 25.706  -3.792  13.170  1.00 8.67   ? 117 HIS A N   1 
ATOM   924  C  CA  . HIS A  1 117 ? 26.222  -3.163  11.937  1.00 8.82   ? 117 HIS A CA  1 
ATOM   925  C  C   . HIS A  1 117 ? 27.663  -2.828  12.116  1.00 8.55   ? 117 HIS A C   1 
ATOM   926  O  O   . HIS A  1 117 ? 28.038  -2.159  13.068  1.00 9.71   ? 117 HIS A O   1 
ATOM   927  C  CB  . HIS A  1 117 ? 25.424  -1.866  11.715  1.00 9.72   ? 117 HIS A CB  1 
ATOM   928  C  CG  . HIS A  1 117 ? 24.026  -2.134  11.319  1.00 8.70   ? 117 HIS A CG  1 
ATOM   929  N  ND1 . HIS A  1 117 ? 23.014  -1.198  11.467  1.00 8.86   ? 117 HIS A ND1 1 
ATOM   930  C  CD2 . HIS A  1 117 ? 23.490  -3.234  10.776  1.00 9.27   ? 117 HIS A CD2 1 
ATOM   931  C  CE1 . HIS A  1 117 ? 21.897  -1.769  10.985  1.00 8.77   ? 117 HIS A CE1 1 
ATOM   932  N  NE2 . HIS A  1 117 ? 22.143  -2.995  10.571  1.00 9.16   ? 117 HIS A NE2 1 
ATOM   933  N  N   . ILE A  1 118 ? 28.476  -3.289  11.179  1.00 9.08   ? 118 ILE A N   1 
ATOM   934  C  CA  . ILE A  1 118 ? 29.922  -2.949  11.152  1.00 8.95   ? 118 ILE A CA  1 
ATOM   935  C  C   . ILE A  1 118 ? 30.076  -2.015  9.918   1.00 9.25   ? 118 ILE A C   1 
ATOM   936  O  O   . ILE A  1 118 ? 29.941  -2.412  8.760   1.00 9.76   ? 118 ILE A O   1 
ATOM   937  C  CB  . ILE A  1 118 ? 30.816  -4.163  10.983  1.00 10.29  ? 118 ILE A CB  1 
ATOM   938  C  CG1 . ILE A  1 118 ? 30.451  -5.228  12.035  1.00 10.93  ? 118 ILE A CG1 1 
ATOM   939  C  CG2 . ILE A  1 118 ? 32.276  -3.691  11.171  1.00 12.99  ? 118 ILE A CG2 1 
ATOM   940  C  CD1 . ILE A  1 118 ? 31.283  -6.525  11.933  1.00 12.99  ? 118 ILE A CD1 1 
ATOM   941  N  N   . VAL A  1 119 ? 30.303  -0.737  10.246  1.00 9.19   ? 119 VAL A N   1 
ATOM   942  C  CA  . VAL A  1 119 ? 30.281  0.345   9.212   1.00 9.53   ? 119 VAL A CA  1 
ATOM   943  C  C   . VAL A  1 119 ? 31.707  0.516   8.696   1.00 9.57   ? 119 VAL A C   1 
ATOM   944  O  O   . VAL A  1 119 ? 32.666  0.668   9.493   1.00 11.29  ? 119 VAL A O   1 
ATOM   945  C  CB  . VAL A  1 119 ? 29.783  1.628   9.825   1.00 9.99   ? 119 VAL A CB  1 
ATOM   946  C  CG1 . VAL A  1 119 ? 29.686  2.739   8.766   1.00 11.94  ? 119 VAL A CG1 1 
ATOM   947  C  CG2 . VAL A  1 119 ? 28.404  1.494   10.512  1.00 10.81  ? 119 VAL A CG2 1 
ATOM   948  N  N   . HIS A  1 120 ? 31.823  0.583   7.372   1.00 10.90  ? 120 HIS A N   1 
ATOM   949  C  CA  . HIS A  1 120 ? 33.066  0.814   6.648   1.00 10.49  ? 120 HIS A CA  1 
ATOM   950  C  C   . HIS A  1 120 ? 32.881  1.940   5.686   1.00 10.14  ? 120 HIS A C   1 
ATOM   951  O  O   . HIS A  1 120 ? 31.769  2.222   5.220   1.00 11.28  ? 120 HIS A O   1 
ATOM   952  C  CB  . HIS A  1 120 ? 33.492  -0.483  5.886   1.00 11.05  ? 120 HIS A CB  1 
ATOM   953  C  CG  . HIS A  1 120 ? 33.663  -1.697  6.697   1.00 10.72  ? 120 HIS A CG  1 
ATOM   954  N  ND1 . HIS A  1 120 ? 32.569  -2.373  7.257   1.00 11.29  ? 120 HIS A ND1 1 
ATOM   955  C  CD2 . HIS A  1 120 ? 34.717  -2.464  6.946   1.00 12.06  ? 120 HIS A CD2 1 
ATOM   956  C  CE1 . HIS A  1 120 ? 33.035  -3.513  7.809   1.00 12.19  ? 120 HIS A CE1 1 
ATOM   957  N  NE2 . HIS A  1 120 ? 34.355  -3.595  7.661   1.00 12.06  ? 120 HIS A NE2 1 
ATOM   958  N  N   . TYR A  1 121 ? 33.996  2.602   5.312   1.00 11.48  ? 121 TYR A N   1 
ATOM   959  C  CA  . TYR A  1 121 ? 33.952  3.657   4.334   1.00 12.06  ? 121 TYR A CA  1 
ATOM   960  C  C   . TYR A  1 121 ? 34.950  3.447   3.210   1.00 12.09  ? 121 TYR A C   1 
ATOM   961  O  O   . TYR A  1 121 ? 35.921  2.701   3.370   1.00 12.14  ? 121 TYR A O   1 
ATOM   962  C  CB  . TYR A  1 121 ? 34.274  5.079   4.998   1.00 13.58  ? 121 TYR A CB  1 
ATOM   963  C  CG  . TYR A  1 121 ? 35.701  5.256   5.393   1.00 13.42  ? 121 TYR A CG  1 
ATOM   964  C  CD1 . TYR A  1 121 ? 36.122  4.726   6.591   1.00 14.27  ? 121 TYR A CD1 1 
ATOM   965  C  CD2 . TYR A  1 121 ? 36.573  5.951   4.594   1.00 15.25  ? 121 TYR A CD2 1 
ATOM   966  C  CE1 . TYR A  1 121 ? 37.417  4.865   7.031   1.00 17.39  ? 121 TYR A CE1 1 
ATOM   967  C  CE2 . TYR A  1 121 ? 37.945  6.082   5.034   1.00 17.04  ? 121 TYR A CE2 1 
ATOM   968  C  CZ  . TYR A  1 121 ? 38.354  5.510   6.252   1.00 18.07  ? 121 TYR A CZ  1 
ATOM   969  O  OH  . TYR A  1 121 ? 39.638  5.632   6.732   1.00 21.76  ? 121 TYR A OH  1 
ATOM   970  N  N   . ASN A  1 122 ? 34.660  4.034   2.035   1.00 12.35  ? 122 ASN A N   1 
ATOM   971  C  CA  . ASN A  1 122 ? 35.523  3.782   0.842   1.00 13.56  ? 122 ASN A CA  1 
ATOM   972  C  C   . ASN A  1 122 ? 36.804  4.611   0.967   1.00 13.01  ? 122 ASN A C   1 
ATOM   973  O  O   . ASN A  1 122 ? 36.806  5.821   0.708   1.00 14.00  ? 122 ASN A O   1 
ATOM   974  C  CB  . ASN A  1 122 ? 34.749  4.240   -0.391  1.00 13.52  ? 122 ASN A CB  1 
ATOM   975  C  CG  . ASN A  1 122 ? 35.418  3.801   -1.651  1.00 14.72  ? 122 ASN A CG  1 
ATOM   976  O  OD1 . ASN A  1 122 ? 36.689  3.782   -1.729  1.00 14.93  ? 122 ASN A OD1 1 
ATOM   977  N  ND2 . ASN A  1 122 ? 34.629  3.513   -2.687  1.00 17.27  ? 122 ASN A ND2 1 
ATOM   978  N  N   . SER A  1 123 ? 37.837  4.004   1.510   1.00 12.79  ? 123 SER A N   1 
ATOM   979  C  CA  . SER A  1 123 ? 39.094  4.608   1.750   1.00 14.02  ? 123 SER A CA  1 
ATOM   980  C  C   . SER A  1 123 ? 39.905  4.766   0.447   1.00 14.15  ? 123 SER A C   1 
ATOM   981  O  O   . SER A  1 123 ? 40.919  5.475   0.460   1.00 16.26  ? 123 SER A O   1 
ATOM   982  C  CB  . SER A  1 123 ? 39.860  3.801   2.855   1.00 13.54  ? 123 SER A CB  1 
ATOM   983  O  OG  . SER A  1 123 ? 39.888  2.486   2.532   1.00 14.54  ? 123 SER A OG  1 
ATOM   984  N  N   . ASP A  1 124 ? 39.554  4.070   -0.620  1.00 14.24  ? 124 ASP A N   1 
ATOM   985  C  CA  . ASP A  1 124 ? 40.267  4.306   -1.923  1.00 16.40  ? 124 ASP A CA  1 
ATOM   986  C  C   . ASP A  1 124 ? 39.855  5.642   -2.456  1.00 17.75  ? 124 ASP A C   1 
ATOM   987  O  O   . ASP A  1 124 ? 40.675  6.275   -3.163  1.00 21.90  ? 124 ASP A O   1 
ATOM   988  C  CB  . ASP A  1 124 ? 39.896  3.186   -2.888  1.00 18.28  ? 124 ASP A CB  1 
ATOM   989  C  CG  . ASP A  1 124 ? 40.618  1.920   -2.617  1.00 15.42  ? 124 ASP A CG  1 
ATOM   990  O  OD1 . ASP A  1 124 ? 41.695  1.922   -1.841  1.00 16.54  ? 124 ASP A OD1 1 
ATOM   991  O  OD2 . ASP A  1 124 ? 40.172  0.878   -3.131  1.00 17.04  ? 124 ASP A OD2 1 
ATOM   992  N  N   . LEU A  1 125 ? 38.622  6.058   -2.233  1.00 15.89  ? 125 LEU A N   1 
ATOM   993  C  CA  . LEU A  1 125 ? 38.061  7.298   -2.886  1.00 16.54  ? 125 LEU A CA  1 
ATOM   994  C  C   . LEU A  1 125 ? 38.068  8.442   -1.940  1.00 15.13  ? 125 LEU A C   1 
ATOM   995  O  O   . LEU A  1 125 ? 38.159  9.650   -2.382  1.00 20.55  ? 125 LEU A O   1 
ATOM   996  C  CB  . LEU A  1 125 ? 36.604  7.073   -3.434  1.00 16.25  ? 125 LEU A CB  1 
ATOM   997  C  CG  . LEU A  1 125 ? 36.533  5.983   -4.548  1.00 19.55  ? 125 LEU A CG  1 
ATOM   998  C  CD1 . LEU A  1 125 ? 35.135  5.903   -5.094  1.00 21.93  ? 125 LEU A CD1 1 
ATOM   999  C  CD2 . LEU A  1 125 ? 37.611  6.136   -5.640  1.00 27.41  ? 125 LEU A CD2 1 
ATOM   1000 N  N   . TYR A  1 126 ? 37.972  8.200   -0.607  1.00 16.14  ? 126 TYR A N   1 
ATOM   1001 C  CA  . TYR A  1 126 ? 37.827  9.253   0.363   1.00 15.13  ? 126 TYR A CA  1 
ATOM   1002 C  C   . TYR A  1 126 ? 38.766  9.190   1.567   1.00 18.28  ? 126 TYR A C   1 
ATOM   1003 O  O   . TYR A  1 126 ? 39.191  8.098   1.954   1.00 17.97  ? 126 TYR A O   1 
ATOM   1004 C  CB  . TYR A  1 126 ? 36.320  9.271   0.907   1.00 18.48  ? 126 TYR A CB  1 
ATOM   1005 C  CG  . TYR A  1 126 ? 35.290  9.299   -0.234  1.00 17.45  ? 126 TYR A CG  1 
ATOM   1006 C  CD1 . TYR A  1 126 ? 35.215  10.383  -1.090  1.00 22.02  ? 126 TYR A CD1 1 
ATOM   1007 C  CD2 . TYR A  1 126 ? 34.498  8.177   -0.459  1.00 17.77  ? 126 TYR A CD2 1 
ATOM   1008 C  CE1 . TYR A  1 126 ? 34.372  10.329  -2.205  1.00 21.47  ? 126 TYR A CE1 1 
ATOM   1009 C  CE2 . TYR A  1 126 ? 33.617  8.113   -1.615  1.00 17.69  ? 126 TYR A CE2 1 
ATOM   1010 C  CZ  . TYR A  1 126 ? 33.560  9.223   -2.416  1.00 19.85  ? 126 TYR A CZ  1 
ATOM   1011 O  OH  . TYR A  1 126 ? 32.795  9.229   -3.558  1.00 22.46  ? 126 TYR A OH  1 
ATOM   1012 N  N   . PRO A  1 127 ? 39.032  10.303  2.229   1.00 19.34  ? 127 PRO A N   1 
ATOM   1013 C  CA  . PRO A  1 127 ? 40.087  10.367  3.239   1.00 20.62  ? 127 PRO A CA  1 
ATOM   1014 C  C   . PRO A  1 127 ? 39.670  9.891   4.556   1.00 19.69  ? 127 PRO A C   1 
ATOM   1015 O  O   . PRO A  1 127 ? 40.540  9.407   5.359   1.00 25.13  ? 127 PRO A O   1 
ATOM   1016 C  CB  . PRO A  1 127 ? 40.453  11.865  3.314   1.00 24.24  ? 127 PRO A CB  1 
ATOM   1017 C  CG  . PRO A  1 127 ? 39.176  12.540  2.784   1.00 22.19  ? 127 PRO A CG  1 
ATOM   1018 C  CD  . PRO A  1 127 ? 38.664  11.657  1.699   1.00 21.36  ? 127 PRO A CD  1 
ATOM   1019 N  N   . ASP A  1 128 ? 38.328  9.893   4.864   1.00 18.87  ? 128 ASP A N   1 
ATOM   1020 C  CA  . ASP A  1 128 ? 37.862  9.476   6.122   1.00 19.12  ? 128 ASP A CA  1 
ATOM   1021 C  C   . ASP A  1 128 ? 36.314  9.210   6.027   1.00 18.07  ? 128 ASP A C   1 
ATOM   1022 O  O   . ASP A  1 128 ? 35.736  9.525   5.020   1.00 16.34  ? 128 ASP A O   1 
ATOM   1023 C  CB  . ASP A  1 128 ? 38.118  10.541  7.206   1.00 22.42  ? 128 ASP A CB  1 
ATOM   1024 C  CG  . ASP A  1 128 ? 37.794  11.912  6.741   1.00 23.06  ? 128 ASP A CG  1 
ATOM   1025 O  OD1 . ASP A  1 128 ? 36.597  12.137  6.489   1.00 26.71  ? 128 ASP A OD1 1 
ATOM   1026 O  OD2 . ASP A  1 128 ? 38.678  12.801  6.826   1.00 35.34  ? 128 ASP A OD2 1 
ATOM   1027 N  N   . ALA A  1 129 ? 35.770  8.615   7.093   1.00 16.95  ? 129 ALA A N   1 
ATOM   1028 C  CA  . ALA A  1 129 ? 34.430  8.177   7.044   1.00 16.19  ? 129 ALA A CA  1 
ATOM   1029 C  C   . ALA A  1 129 ? 33.430  9.366   6.957   1.00 18.20  ? 129 ALA A C   1 
ATOM   1030 O  O   . ALA A  1 129 ? 32.399  9.284   6.255   1.00 19.33  ? 129 ALA A O   1 
ATOM   1031 C  CB  . ALA A  1 129 ? 34.068  7.288   8.225   1.00 19.86  ? 129 ALA A CB  1 
ATOM   1032 N  N   . SER A  1 130 ? 33.746  10.395  7.711   1.00 19.96  ? 130 SER A N   1 
ATOM   1033 C  CA  . SER A  1 130 ? 32.837  11.553  7.666   1.00 22.27  ? 130 SER A CA  1 
ATOM   1034 C  C   . SER A  1 130 ? 32.676  12.119  6.227   1.00 19.92  ? 130 SER A C   1 
ATOM   1035 O  O   . SER A  1 130 ? 31.534  12.379  5.763   1.00 23.54  ? 130 SER A O   1 
ATOM   1036 C  CB  . SER A  1 130 ? 33.347  12.617  8.676   1.00 27.93  ? 130 SER A CB  1 
ATOM   1037 O  OG  . SER A  1 130 ? 32.561  13.819  8.598   1.00 40.66  ? 130 SER A OG  1 
ATOM   1038 N  N   . THR A  1 131 ? 33.830  12.255  5.584   1.00 19.27  ? 131 THR A N   1 
ATOM   1039 C  CA  . THR A  1 131 ? 33.799  12.830  4.211   1.00 22.01  ? 131 THR A CA  1 
ATOM   1040 C  C   . THR A  1 131 ? 33.052  11.809  3.309   1.00 18.58  ? 131 THR A C   1 
ATOM   1041 O  O   . THR A  1 131 ? 32.381  12.245  2.371   1.00 19.80  ? 131 THR A O   1 
ATOM   1042 C  CB  . THR A  1 131 ? 35.274  13.011  3.688   1.00 21.30  ? 131 THR A CB  1 
ATOM   1043 O  OG1 . THR A  1 131 ? 35.881  13.892  4.628   1.00 24.15  ? 131 THR A OG1 1 
ATOM   1044 C  CG2 . THR A  1 131 ? 35.306  13.615  2.335   1.00 23.42  ? 131 THR A CG2 1 
ATOM   1045 N  N   . ALA A  1 132 ? 33.307  10.500  3.477   1.00 17.40  ? 132 ALA A N   1 
ATOM   1046 C  CA  . ALA A  1 132 ? 32.675  9.496   2.543   1.00 14.59  ? 132 ALA A CA  1 
ATOM   1047 C  C   . ALA A  1 132 ? 31.176  9.451   2.703   1.00 16.06  ? 132 ALA A C   1 
ATOM   1048 O  O   . ALA A  1 132 ? 30.484  9.021   1.757   1.00 15.31  ? 132 ALA A O   1 
ATOM   1049 C  CB  . ALA A  1 132 ? 33.204  8.136   2.957   1.00 16.23  ? 132 ALA A CB  1 
ATOM   1050 N  N   . SER A  1 133 ? 30.682  9.779   3.865   1.00 15.53  ? 133 SER A N   1 
ATOM   1051 C  CA  . SER A  1 133 ? 29.268  9.355   4.173   1.00 16.40  ? 133 SER A CA  1 
ATOM   1052 C  C   . SER A  1 133 ? 28.209  9.937   3.336   1.00 15.08  ? 133 SER A C   1 
ATOM   1053 O  O   . SER A  1 133 ? 27.138  9.313   3.231   1.00 16.58  ? 133 SER A O   1 
ATOM   1054 C  CB  . SER A  1 133 ? 29.033  9.648   5.682   1.00 17.50  ? 133 SER A CB  1 
ATOM   1055 O  OG  . SER A  1 133 ? 28.886  11.051  5.975   1.00 21.22  ? 133 SER A OG  1 
ATOM   1056 N  N   . ASN A  1 134 ? 28.424  11.088  2.710   1.00 16.46  ? 134 ASN A N   1 
ATOM   1057 C  CA  . ASN A  1 134 ? 27.434  11.736  1.877   1.00 17.42  ? 134 ASN A CA  1 
ATOM   1058 C  C   . ASN A  1 134 ? 27.835  11.642  0.387   1.00 17.49  ? 134 ASN A C   1 
ATOM   1059 O  O   . ASN A  1 134 ? 27.275  12.320  -0.519  1.00 24.36  ? 134 ASN A O   1 
ATOM   1060 C  CB  . ASN A  1 134 ? 26.983  13.146  2.373   1.00 20.19  ? 134 ASN A CB  1 
ATOM   1061 C  CG  . ASN A  1 134 ? 28.100  14.115  2.320   1.00 29.66  ? 134 ASN A CG  1 
ATOM   1062 O  OD1 . ASN A  1 134 ? 29.261  13.741  2.001   1.00 25.69  ? 134 ASN A OD1 1 
ATOM   1063 N  ND2 . ASN A  1 134 ? 27.828  15.426  2.556   1.00 31.95  ? 134 ASN A ND2 1 
ATOM   1064 N  N   . LYS A  1 135 ? 28.733  10.740  0.044   1.00 17.44  ? 135 LYS A N   1 
ATOM   1065 C  CA  . LYS A  1 135 ? 29.301  10.667  -1.319  1.00 18.10  ? 135 LYS A CA  1 
ATOM   1066 C  C   . LYS A  1 135 ? 29.027  9.351   -1.976  1.00 17.34  ? 135 LYS A C   1 
ATOM   1067 O  O   . LYS A  1 135 ? 28.792  8.313   -1.319  1.00 17.35  ? 135 LYS A O   1 
ATOM   1068 C  CB  . LYS A  1 135 ? 30.839  10.978  -1.316  1.00 21.91  ? 135 LYS A CB  1 
ATOM   1069 C  CG  . LYS A  1 135 ? 31.002  12.534  -0.930  1.00 25.54  ? 135 LYS A CG  1 
ATOM   1070 C  CD  . LYS A  1 135 ? 32.481  13.008  -0.837  1.00 27.00  ? 135 LYS A CD  1 
ATOM   1071 C  CE  . LYS A  1 135 ? 32.677  14.432  -0.478  1.00 26.31  ? 135 LYS A CE  1 
ATOM   1072 N  NZ  . LYS A  1 135 ? 31.958  14.658  0.845   1.00 23.93  ? 135 LYS A NZ  1 
ATOM   1073 N  N   . SER A  1 136 ? 29.021  9.380   -3.279  1.00 20.58  ? 136 SER A N   1 
ATOM   1074 C  CA  . SER A  1 136 ? 28.854  8.175   -4.137  1.00 23.00  ? 136 SER A CA  1 
ATOM   1075 C  C   . SER A  1 136 ? 29.834  7.047   -3.678  1.00 16.91  ? 136 SER A C   1 
ATOM   1076 O  O   . SER A  1 136 ? 31.018  7.222   -3.497  1.00 19.53  ? 136 SER A O   1 
ATOM   1077 C  CB  . SER A  1 136 ? 29.191  8.488   -5.624  1.00 26.46  ? 136 SER A CB  1 
ATOM   1078 O  OG  . SER A  1 136 ? 28.783  7.448   -6.452  1.00 36.62  ? 136 SER A OG  1 
ATOM   1079 N  N   . GLU A  1 137 ? 29.245  5.875   -3.545  1.00 17.62  ? 137 GLU A N   1 
ATOM   1080 C  CA  . GLU A  1 137 ? 30.027  4.675   -3.122  1.00 15.84  ? 137 GLU A CA  1 
ATOM   1081 C  C   . GLU A  1 137 ? 30.733  4.831   -1.797  1.00 14.99  ? 137 GLU A C   1 
ATOM   1082 O  O   . GLU A  1 137 ? 31.756  4.214   -1.512  1.00 16.69  ? 137 GLU A O   1 
ATOM   1083 C  CB  . GLU A  1 137 ? 31.022  4.189   -4.244  1.00 21.83  ? 137 GLU A CB  1 
ATOM   1084 C  CG  . GLU A  1 137 ? 30.294  3.912   -5.572  1.00 30.40  ? 137 GLU A CG  1 
ATOM   1085 C  CD  . GLU A  1 137 ? 30.881  2.755   -6.411  1.00 47.87  ? 137 GLU A CD  1 
ATOM   1086 O  OE1 . GLU A  1 137 ? 31.429  3.052   -7.496  1.00 67.23  ? 137 GLU A OE1 1 
ATOM   1087 O  OE2 . GLU A  1 137 ? 30.701  1.569   -5.945  1.00 60.28  ? 137 GLU A OE2 1 
ATOM   1088 N  N   . GLY A  1 138 ? 30.153  5.693   -0.936  1.00 13.75  ? 138 GLY A N   1 
ATOM   1089 C  CA  . GLY A  1 138 ? 30.883  6.118   0.245   1.00 14.33  ? 138 GLY A CA  1 
ATOM   1090 C  C   . GLY A  1 138 ? 31.008  5.069   1.320   1.00 11.92  ? 138 GLY A C   1 
ATOM   1091 O  O   . GLY A  1 138 ? 32.047  5.047   2.037   1.00 12.98  ? 138 GLY A O   1 
ATOM   1092 N  N   . LEU A  1 139 ? 29.966  4.251   1.563   1.00 12.34  ? 139 LEU A N   1 
ATOM   1093 C  CA  . LEU A  1 139 ? 29.919  3.372   2.754   1.00 11.68  ? 139 LEU A CA  1 
ATOM   1094 C  C   . LEU A  1 139 ? 29.522  1.949   2.386   1.00 10.88  ? 139 LEU A C   1 
ATOM   1095 O  O   . LEU A  1 139 ? 28.857  1.720   1.390   1.00 11.32  ? 139 LEU A O   1 
ATOM   1096 C  CB  . LEU A  1 139 ? 28.915  3.893   3.814   1.00 11.29  ? 139 LEU A CB  1 
ATOM   1097 C  CG  . LEU A  1 139 ? 29.155  5.335   4.332   1.00 12.08  ? 139 LEU A CG  1 
ATOM   1098 C  CD1 . LEU A  1 139 ? 27.921  5.719   5.152   1.00 15.00  ? 139 LEU A CD1 1 
ATOM   1099 C  CD2 . LEU A  1 139 ? 30.459  5.422   5.100   1.00 13.91  ? 139 LEU A CD2 1 
ATOM   1100 N  N   . ALA A  1 140 ? 29.965  1.014   3.241   1.00 11.05  ? 140 ALA A N   1 
ATOM   1101 C  CA  . ALA A  1 140 ? 29.549  -0.372  3.138   1.00 10.84  ? 140 ALA A CA  1 
ATOM   1102 C  C   . ALA A  1 140 ? 29.315  -0.823  4.573   1.00 10.51  ? 140 ALA A C   1 
ATOM   1103 O  O   . ALA A  1 140 ? 30.179  -0.617  5.436   1.00 11.53  ? 140 ALA A O   1 
ATOM   1104 C  CB  . ALA A  1 140 ? 30.624  -1.195  2.430   1.00 11.28  ? 140 ALA A CB  1 
ATOM   1105 N  N   . VAL A  1 141 ? 28.184  -1.496  4.786   1.00 9.90   ? 141 VAL A N   1 
ATOM   1106 C  CA  . VAL A  1 141 ? 27.860  -2.001  6.138   1.00 9.94   ? 141 VAL A CA  1 
ATOM   1107 C  C   . VAL A  1 141 ? 27.706  -3.489  6.038   1.00 9.76   ? 141 VAL A C   1 
ATOM   1108 O  O   . VAL A  1 141 ? 27.094  -4.023  5.102   1.00 10.59  ? 141 VAL A O   1 
ATOM   1109 C  CB  . VAL A  1 141 ? 26.617  -1.360  6.713   1.00 10.05  ? 141 VAL A CB  1 
ATOM   1110 C  CG1 . VAL A  1 141 ? 26.287  -1.937  8.121   1.00 11.36  ? 141 VAL A CG1 1 
ATOM   1111 C  CG2 . VAL A  1 141 ? 26.774  0.176   6.778   1.00 12.25  ? 141 VAL A CG2 1 
ATOM   1112 N  N   . LEU A  1 142 ? 28.304  -4.190  7.057   1.00 9.86   ? 142 LEU A N   1 
ATOM   1113 C  CA  . LEU A  1 142 ? 28.025  -5.636  7.248   1.00 10.65  ? 142 LEU A CA  1 
ATOM   1114 C  C   . LEU A  1 142 ? 26.966  -5.702  8.344   1.00 9.44   ? 142 LEU A C   1 
ATOM   1115 O  O   . LEU A  1 142 ? 27.166  -5.141  9.440   1.00 10.59  ? 142 LEU A O   1 
ATOM   1116 C  CB  . LEU A  1 142 ? 29.251  -6.376  7.697   1.00 10.94  ? 142 LEU A CB  1 
ATOM   1117 C  CG  . LEU A  1 142 ? 30.466  -6.281  6.760   1.00 11.69  ? 142 LEU A CG  1 
ATOM   1118 C  CD1 . LEU A  1 142 ? 31.601  -7.099  7.407   1.00 14.35  ? 142 LEU A CD1 1 
ATOM   1119 C  CD2 . LEU A  1 142 ? 30.119  -6.744  5.342   1.00 13.60  ? 142 LEU A CD2 1 
ATOM   1120 N  N   . ALA A  1 143 ? 25.885  -6.419  8.060   1.00 10.13  ? 143 ALA A N   1 
ATOM   1121 C  CA  . ALA A  1 143 ? 24.778  -6.558  9.081   1.00 9.53   ? 143 ALA A CA  1 
ATOM   1122 C  C   . ALA A  1 143 ? 24.703  -8.017  9.474   1.00 9.42   ? 143 ALA A C   1 
ATOM   1123 O  O   . ALA A  1 143 ? 24.624  -8.935  8.629   1.00 10.41  ? 143 ALA A O   1 
ATOM   1124 C  CB  . ALA A  1 143 ? 23.482  -6.116  8.466   1.00 9.95   ? 143 ALA A CB  1 
ATOM   1125 N  N   . VAL A  1 144 ? 24.690  -8.232  10.800  1.00 9.47   ? 144 VAL A N   1 
ATOM   1126 C  CA  . VAL A  1 144 ? 24.509  -9.560  11.357  1.00 10.34  ? 144 VAL A CA  1 
ATOM   1127 C  C   . VAL A  1 144 ? 23.206  -9.559  12.144  1.00 9.34   ? 144 VAL A C   1 
ATOM   1128 O  O   . VAL A  1 144 ? 22.994  -8.747  13.059  1.00 10.36  ? 144 VAL A O   1 
ATOM   1129 C  CB  . VAL A  1 144 ? 25.668  -9.867  12.336  1.00 10.99  ? 144 VAL A CB  1 
ATOM   1130 C  CG1 . VAL A  1 144 ? 25.461  -11.300 12.888  1.00 13.23  ? 144 VAL A CG1 1 
ATOM   1131 C  CG2 . VAL A  1 144 ? 27.021  -9.799  11.580  1.00 12.29  ? 144 VAL A CG2 1 
ATOM   1132 N  N   . LEU A  1 145 ? 22.329  -10.499 11.804  1.00 9.91   ? 145 LEU A N   1 
ATOM   1133 C  CA  . LEU A  1 145 ? 21.090  -10.690 12.523  1.00 10.41  ? 145 LEU A CA  1 
ATOM   1134 C  C   . LEU A  1 145 ? 21.350  -11.528 13.763  1.00 10.03  ? 145 LEU A C   1 
ATOM   1135 O  O   . LEU A  1 145 ? 22.133  -12.486 13.718  1.00 11.51  ? 145 LEU A O   1 
ATOM   1136 C  CB  . LEU A  1 145 ? 20.100  -11.416 11.577  1.00 11.72  ? 145 LEU A CB  1 
ATOM   1137 C  CG  . LEU A  1 145 ? 19.818  -10.650 10.263  1.00 12.56  ? 145 LEU A CG  1 
ATOM   1138 C  CD1 . LEU A  1 145 ? 19.151  -11.548 9.205   1.00 14.66  ? 145 LEU A CD1 1 
ATOM   1139 C  CD2 . LEU A  1 145 ? 18.954  -9.391  10.608  1.00 14.64  ? 145 LEU A CD2 1 
ATOM   1140 N  N   . ILE A  1 146 ? 20.714  -11.167 14.866  1.00 10.12  ? 146 ILE A N   1 
ATOM   1141 C  CA  . ILE A  1 146 ? 20.991  -11.785 16.168  1.00 10.46  ? 146 ILE A CA  1 
ATOM   1142 C  C   . ILE A  1 146 ? 19.678  -12.346 16.712  1.00 10.71  ? 146 ILE A C   1 
ATOM   1143 O  O   . ILE A  1 146 ? 18.644  -11.670 16.738  1.00 11.41  ? 146 ILE A O   1 
ATOM   1144 C  CB  . ILE A  1 146 ? 21.500  -10.718 17.162  1.00 10.47  ? 146 ILE A CB  1 
ATOM   1145 C  CG1 . ILE A  1 146 ? 22.828  -10.116 16.653  1.00 11.84  ? 146 ILE A CG1 1 
ATOM   1146 C  CG2 . ILE A  1 146 ? 21.693  -11.305 18.578  1.00 11.62  ? 146 ILE A CG2 1 
ATOM   1147 C  CD1 . ILE A  1 146 ? 23.252  -8.846  17.381  1.00 11.99  ? 146 ILE A CD1 1 
ATOM   1148 N  N   . GLU A  1 147 ? 19.739  -13.587 17.201  1.00 12.02  ? 147 GLU A N   1 
ATOM   1149 C  CA  . GLU A  1 147 ? 18.579  -14.249 17.809  1.00 13.52  ? 147 GLU A CA  1 
ATOM   1150 C  C   . GLU A  1 147 ? 19.014  -14.790 19.160  1.00 12.37  ? 147 GLU A C   1 
ATOM   1151 O  O   . GLU A  1 147 ? 20.186  -14.990 19.462  1.00 12.93  ? 147 GLU A O   1 
ATOM   1152 C  CB  . GLU A  1 147 ? 18.020  -15.359 16.934  1.00 15.50  ? 147 GLU A CB  1 
ATOM   1153 C  CG  . GLU A  1 147 ? 18.921  -16.518 16.744  1.00 15.69  ? 147 GLU A CG  1 
ATOM   1154 C  CD  . GLU A  1 147 ? 18.482  -17.512 15.729  1.00 18.54  ? 147 GLU A CD  1 
ATOM   1155 O  OE1 . GLU A  1 147 ? 17.495  -17.285 14.970  1.00 20.51  ? 147 GLU A OE1 1 
ATOM   1156 O  OE2 . GLU A  1 147 ? 19.156  -18.542 15.578  1.00 22.33  ? 147 GLU A OE2 1 
ATOM   1157 N  N   A MET A  1 148 ? 18.049  -15.008 20.075  0.50 13.12  ? 148 MET A N   1 
ATOM   1158 N  N   B MET A  1 148 ? 17.961  -15.178 19.916  0.50 14.82  ? 148 MET A N   1 
ATOM   1159 C  CA  A MET A  1 148 ? 18.370  -15.574 21.376  0.50 12.91  ? 148 MET A CA  1 
ATOM   1160 C  CA  B MET A  1 148 ? 18.177  -15.751 21.197  0.50 17.85  ? 148 MET A CA  1 
ATOM   1161 C  C   A MET A  1 148 ? 18.655  -17.097 21.177  0.50 14.43  ? 148 MET A C   1 
ATOM   1162 C  C   B MET A  1 148 ? 18.691  -17.218 21.049  0.50 16.63  ? 148 MET A C   1 
ATOM   1163 O  O   A MET A  1 148 ? 17.959  -17.772 20.425  0.50 15.52  ? 148 MET A O   1 
ATOM   1164 O  O   B MET A  1 148 ? 18.288  -17.951 20.116  0.50 17.71  ? 148 MET A O   1 
ATOM   1165 C  CB  A MET A  1 148 ? 17.141  -15.487 22.295  0.50 12.88  ? 148 MET A CB  1 
ATOM   1166 C  CB  B MET A  1 148 ? 16.804  -15.839 21.925  0.50 18.64  ? 148 MET A CB  1 
ATOM   1167 C  CG  A MET A  1 148 ? 17.407  -16.046 23.678  0.50 16.32  ? 148 MET A CG  1 
ATOM   1168 C  CG  B MET A  1 148 ? 16.211  -14.525 22.444  0.50 20.55  ? 148 MET A CG  1 
ATOM   1169 S  SD  A MET A  1 148 ? 16.085  -15.834 24.883  0.50 19.57  ? 148 MET A SD  1 
ATOM   1170 S  SD  B MET A  1 148 ? 14.611  -14.905 23.216  0.50 33.54  ? 148 MET A SD  1 
ATOM   1171 C  CE  A MET A  1 148 ? 15.784  -14.064 24.992  0.50 14.73  ? 148 MET A CE  1 
ATOM   1172 C  CE  B MET A  1 148 ? 13.762  -13.358 23.569  0.50 18.74  ? 148 MET A CE  1 
ATOM   1173 N  N   . GLY A  1 149 ? 19.668  -17.624 21.865  1.00 15.79  ? 149 GLY A N   1 
ATOM   1174 C  CA  . GLY A  1 149 ? 20.058  -19.058 21.847  1.00 16.92  ? 149 GLY A CA  1 
ATOM   1175 C  C   . GLY A  1 149 ? 21.157  -19.228 22.844  1.00 16.13  ? 149 GLY A C   1 
ATOM   1176 O  O   . GLY A  1 149 ? 20.991  -18.804 23.997  1.00 16.92  ? 149 GLY A O   1 
ATOM   1177 N  N   A SER A  1 150 ? 22.257  -19.777 22.362  0.50 16.40  ? 150 SER A N   1 
ATOM   1178 N  N   B SER A  1 150 ? 22.220  -19.956 22.520  0.50 17.74  ? 150 SER A N   1 
ATOM   1179 C  CA  A SER A  1 150 ? 23.440  -20.005 23.158  0.50 18.22  ? 150 SER A CA  1 
ATOM   1180 C  CA  B SER A  1 150 ? 23.276  -20.201 23.486  0.50 17.35  ? 150 SER A CA  1 
ATOM   1181 C  C   A SER A  1 150 ? 24.149  -18.750 23.708  0.50 16.28  ? 150 SER A C   1 
ATOM   1182 C  C   B SER A  1 150 ? 24.066  -18.930 23.729  0.50 18.68  ? 150 SER A C   1 
ATOM   1183 O  O   A SER A  1 150 ? 24.277  -17.727 23.025  0.50 15.27  ? 150 SER A O   1 
ATOM   1184 O  O   B SER A  1 150 ? 24.193  -18.102 22.796  0.50 17.03  ? 150 SER A O   1 
ATOM   1185 C  CB  A SER A  1 150 ? 24.415  -20.918 22.348  0.50 19.54  ? 150 SER A CB  1 
ATOM   1186 C  CB  B SER A  1 150 ? 24.294  -21.211 22.928  0.50 20.11  ? 150 SER A CB  1 
ATOM   1187 O  OG  A SER A  1 150 ? 23.688  -22.175 22.241  0.50 26.86  ? 150 SER A OG  1 
ATOM   1188 O  OG  B SER A  1 150 ? 24.644  -20.805 21.570  0.50 24.58  ? 150 SER A OG  1 
ATOM   1189 N  N   . PHE A  1 151 ? 24.692  -18.870 24.928  1.00 18.78  ? 151 PHE A N   1 
ATOM   1190 C  CA  . PHE A  1 151 ? 25.668  -17.799 25.314  1.00 17.80  ? 151 PHE A CA  1 
ATOM   1191 C  C   . PHE A  1 151 ? 26.738  -17.618 24.257  1.00 17.36  ? 151 PHE A C   1 
ATOM   1192 O  O   . PHE A  1 151 ? 27.350  -18.606 23.780  1.00 18.25  ? 151 PHE A O   1 
ATOM   1193 C  CB  . PHE A  1 151 ? 26.243  -18.133 26.713  1.00 18.39  ? 151 PHE A CB  1 
ATOM   1194 C  CG  . PHE A  1 151 ? 27.231  -17.136 27.193  1.00 18.73  ? 151 PHE A CG  1 
ATOM   1195 C  CD1 . PHE A  1 151 ? 26.807  -15.850 27.723  1.00 21.36  ? 151 PHE A CD1 1 
ATOM   1196 C  CD2 . PHE A  1 151 ? 28.557  -17.420 27.121  1.00 21.39  ? 151 PHE A CD2 1 
ATOM   1197 C  CE1 . PHE A  1 151 ? 27.736  -14.895 28.120  1.00 21.28  ? 151 PHE A CE1 1 
ATOM   1198 C  CE2 . PHE A  1 151 ? 29.456  -16.510 27.531  1.00 20.87  ? 151 PHE A CE2 1 
ATOM   1199 C  CZ  . PHE A  1 151 ? 29.121  -15.246 28.052  1.00 19.66  ? 151 PHE A CZ  1 
ATOM   1200 N  N   . ASN A  1 152 ? 27.109  -16.348 24.020  1.00 15.46  ? 152 ASN A N   1 
ATOM   1201 C  CA  . ASN A  1 152 ? 28.104  -16.098 22.980  1.00 15.78  ? 152 ASN A CA  1 
ATOM   1202 C  C   . ASN A  1 152 ? 29.256  -15.305 23.691  1.00 16.97  ? 152 ASN A C   1 
ATOM   1203 O  O   . ASN A  1 152 ? 29.195  -14.078 23.945  1.00 15.79  ? 152 ASN A O   1 
ATOM   1204 C  CB  . ASN A  1 152 ? 27.426  -15.170 21.926  1.00 15.23  ? 152 ASN A CB  1 
ATOM   1205 C  CG  . ASN A  1 152 ? 28.256  -15.096 20.713  1.00 14.16  ? 152 ASN A CG  1 
ATOM   1206 O  OD1 . ASN A  1 152 ? 29.499  -14.761 20.789  1.00 15.77  ? 152 ASN A OD1 1 
ATOM   1207 N  ND2 . ASN A  1 152 ? 27.692  -15.328 19.549  1.00 14.45  ? 152 ASN A ND2 1 
ATOM   1208 N  N   . PRO A  1 153 ? 30.426  -15.998 23.922  1.00 17.27  ? 153 PRO A N   1 
ATOM   1209 C  CA  . PRO A  1 153 ? 31.534  -15.334 24.585  1.00 18.14  ? 153 PRO A CA  1 
ATOM   1210 C  C   . PRO A  1 153 ? 32.083  -14.154 23.777  1.00 16.15  ? 153 PRO A C   1 
ATOM   1211 O  O   . PRO A  1 153 ? 32.534  -13.145 24.368  1.00 19.04  ? 153 PRO A O   1 
ATOM   1212 C  CB  . PRO A  1 153 ? 32.619  -16.469 24.696  1.00 22.98  ? 153 PRO A CB  1 
ATOM   1213 C  CG  . PRO A  1 153 ? 31.878  -17.735 24.535  1.00 25.34  ? 153 PRO A CG  1 
ATOM   1214 C  CD  . PRO A  1 153 ? 30.573  -17.475 23.730  1.00 19.42  ? 153 PRO A CD  1 
ATOM   1215 N  N   . SER A  1 154 ? 31.964  -14.216 22.435  1.00 15.81  ? 154 SER A N   1 
ATOM   1216 C  CA  . SER A  1 154 ? 32.559  -13.127 21.640  1.00 16.34  ? 154 SER A CA  1 
ATOM   1217 C  C   . SER A  1 154 ? 31.733  -11.821 21.781  1.00 14.13  ? 154 SER A C   1 
ATOM   1218 O  O   . SER A  1 154 ? 32.287  -10.766 21.967  1.00 15.56  ? 154 SER A O   1 
ATOM   1219 C  CB  . SER A  1 154 ? 32.647  -13.535 20.177  1.00 18.30  ? 154 SER A CB  1 
ATOM   1220 O  OG  . SER A  1 154 ? 33.519  -14.681 20.125  1.00 22.27  ? 154 SER A OG  1 
ATOM   1221 N  N   . TYR A  1 155 ? 30.387  -11.955 21.721  1.00 14.61  ? 155 TYR A N   1 
ATOM   1222 C  CA  . TYR A  1 155 ? 29.603  -10.727 21.993  1.00 14.02  ? 155 TYR A CA  1 
ATOM   1223 C  C   . TYR A  1 155 ? 29.756  -10.238 23.376  1.00 14.48  ? 155 TYR A C   1 
ATOM   1224 O  O   . TYR A  1 155 ? 29.637  -9.026  23.608  1.00 14.73  ? 155 TYR A O   1 
ATOM   1225 C  CB  . TYR A  1 155 ? 28.117  -10.942 21.688  1.00 14.20  ? 155 TYR A CB  1 
ATOM   1226 C  CG  . TYR A  1 155 ? 27.809  -10.823 20.158  1.00 13.28  ? 155 TYR A CG  1 
ATOM   1227 C  CD1 . TYR A  1 155 ? 28.148  -11.819 19.238  1.00 13.10  ? 155 TYR A CD1 1 
ATOM   1228 C  CD2 . TYR A  1 155 ? 27.244  -9.674  19.661  1.00 13.22  ? 155 TYR A CD2 1 
ATOM   1229 C  CE1 . TYR A  1 155 ? 27.947  -11.688 17.897  1.00 12.12  ? 155 TYR A CE1 1 
ATOM   1230 C  CE2 . TYR A  1 155 ? 27.043  -9.513  18.265  1.00 12.50  ? 155 TYR A CE2 1 
ATOM   1231 C  CZ  . TYR A  1 155 ? 27.385  -10.520 17.404  1.00 11.50  ? 155 TYR A CZ  1 
ATOM   1232 O  OH  . TYR A  1 155 ? 27.156  -10.302 16.058  1.00 12.92  ? 155 TYR A OH  1 
ATOM   1233 N  N   . ASP A  1 156 ? 30.100  -11.133 24.307  1.00 14.44  ? 156 ASP A N   1 
ATOM   1234 C  CA  . ASP A  1 156 ? 30.321  -10.717 25.713  1.00 16.78  ? 156 ASP A CA  1 
ATOM   1235 C  C   . ASP A  1 156 ? 31.573  -9.779  25.822  1.00 15.49  ? 156 ASP A C   1 
ATOM   1236 O  O   . ASP A  1 156 ? 31.666  -9.001  26.800  1.00 18.22  ? 156 ASP A O   1 
ATOM   1237 C  CB  . ASP A  1 156 ? 30.292  -11.788 26.704  1.00 20.17  ? 156 ASP A CB  1 
ATOM   1238 C  CG  . ASP A  1 156 ? 29.287  -11.452 27.828  1.00 20.83  ? 156 ASP A CG  1 
ATOM   1239 O  OD1 . ASP A  1 156 ? 28.121  -11.052 27.531  1.00 19.33  ? 156 ASP A OD1 1 
ATOM   1240 O  OD2 . ASP A  1 156 ? 29.678  -11.503 28.997  1.00 25.48  ? 156 ASP A OD2 1 
ATOM   1241 N  N   . LYS A  1 157 ? 32.474  -9.843  24.839  1.00 16.25  ? 157 LYS A N   1 
ATOM   1242 C  CA  . LYS A  1 157 ? 33.673  -8.950  24.851  1.00 17.60  ? 157 LYS A CA  1 
ATOM   1243 C  C   . LYS A  1 157 ? 33.211  -7.520  24.682  1.00 17.20  ? 157 LYS A C   1 
ATOM   1244 O  O   . LYS A  1 157 ? 33.930  -6.595  25.133  1.00 21.38  ? 157 LYS A O   1 
ATOM   1245 C  CB  . LYS A  1 157 ? 34.700  -9.389  23.762  1.00 17.43  ? 157 LYS A CB  1 
ATOM   1246 C  CG  . LYS A  1 157 ? 35.208  -10.807 24.102  1.00 21.12  ? 157 LYS A CG  1 
ATOM   1247 C  CD  . LYS A  1 157 ? 36.218  -11.303 23.039  1.00 20.09  ? 157 LYS A CD  1 
ATOM   1248 C  CE  . LYS A  1 157 ? 36.501  -12.747 23.332  1.00 25.06  ? 157 LYS A CE  1 
ATOM   1249 N  NZ  . LYS A  1 157 ? 37.450  -13.310 22.284  1.00 25.95  ? 157 LYS A NZ  1 
ATOM   1250 N  N   . ILE A  1 158 ? 32.004  -7.295  24.098  1.00 17.19  ? 158 ILE A N   1 
ATOM   1251 C  CA  . ILE A  1 158 ? 31.417  -5.924  24.083  1.00 16.68  ? 158 ILE A CA  1 
ATOM   1252 C  C   . ILE A  1 158 ? 30.510  -5.782  25.303  1.00 16.23  ? 158 ILE A C   1 
ATOM   1253 O  O   . ILE A  1 158 ? 30.555  -4.776  26.002  1.00 16.78  ? 158 ILE A O   1 
ATOM   1254 C  CB  . ILE A  1 158 ? 30.654  -5.685  22.788  1.00 17.94  ? 158 ILE A CB  1 
ATOM   1255 C  CG1 . ILE A  1 158 ? 31.586  -5.742  21.569  1.00 22.19  ? 158 ILE A CG1 1 
ATOM   1256 C  CG2 . ILE A  1 158 ? 29.909  -4.349  22.913  1.00 19.19  ? 158 ILE A CG2 1 
ATOM   1257 C  CD1 . ILE A  1 158 ? 30.866  -5.855  20.221  1.00 23.75  ? 158 ILE A CD1 1 
ATOM   1258 N  N   . PHE A  1 159 ? 29.549  -6.723  25.403  1.00 14.91  ? 159 PHE A N   1 
ATOM   1259 C  CA  . PHE A  1 159 ? 28.534  -6.569  26.481  1.00 16.53  ? 159 PHE A CA  1 
ATOM   1260 C  C   . PHE A  1 159 ? 28.989  -6.430  27.864  1.00 16.06  ? 159 PHE A C   1 
ATOM   1261 O  O   . PHE A  1 159 ? 28.355  -5.762  28.660  1.00 16.94  ? 159 PHE A O   1 
ATOM   1262 C  CB  . PHE A  1 159 ? 27.451  -7.627  26.386  1.00 14.65  ? 159 PHE A CB  1 
ATOM   1263 C  CG  . PHE A  1 159 ? 26.740  -7.776  25.068  1.00 15.18  ? 159 PHE A CG  1 
ATOM   1264 C  CD1 . PHE A  1 159 ? 26.616  -6.745  24.142  1.00 18.60  ? 159 PHE A CD1 1 
ATOM   1265 C  CD2 . PHE A  1 159 ? 26.105  -8.986  24.763  1.00 17.44  ? 159 PHE A CD2 1 
ATOM   1266 C  CE1 . PHE A  1 159 ? 25.931  -6.920  22.972  1.00 18.86  ? 159 PHE A CE1 1 
ATOM   1267 C  CE2 . PHE A  1 159 ? 25.422  -9.165  23.584  1.00 17.62  ? 159 PHE A CE2 1 
ATOM   1268 C  CZ  . PHE A  1 159 ? 25.336  -8.119  22.687  1.00 18.09  ? 159 PHE A CZ  1 
ATOM   1269 N  N   . SER A  1 160 ? 30.174  -7.005  28.180  1.00 16.87  ? 160 SER A N   1 
ATOM   1270 C  CA  . SER A  1 160 ? 30.706  -6.857  29.608  1.00 18.70  ? 160 SER A CA  1 
ATOM   1271 C  C   . SER A  1 160 ? 31.105  -5.426  29.898  1.00 19.71  ? 160 SER A C   1 
ATOM   1272 O  O   . SER A  1 160 ? 31.340  -5.165  31.059  1.00 21.16  ? 160 SER A O   1 
ATOM   1273 C  CB  . SER A  1 160 ? 31.816  -7.877  29.741  1.00 20.54  ? 160 SER A CB  1 
ATOM   1274 O  OG  . SER A  1 160 ? 32.959  -7.473  28.955  1.00 22.47  ? 160 SER A OG  1 
ATOM   1275 N  N   . HIS A  1 161 ? 31.207  -4.531  28.874  1.00 17.39  ? 161 HIS A N   1 
ATOM   1276 C  CA  . HIS A  1 161 ? 31.516  -3.147  29.118  1.00 17.59  ? 161 HIS A CA  1 
ATOM   1277 C  C   . HIS A  1 161 ? 30.293  -2.246  29.147  1.00 18.77  ? 161 HIS A C   1 
ATOM   1278 O  O   . HIS A  1 161 ? 30.460  -1.042  29.400  1.00 18.92  ? 161 HIS A O   1 
ATOM   1279 C  CB  . HIS A  1 161 ? 32.534  -2.683  28.118  1.00 17.67  ? 161 HIS A CB  1 
ATOM   1280 C  CG  . HIS A  1 161 ? 33.830  -3.457  28.181  1.00 18.32  ? 161 HIS A CG  1 
ATOM   1281 N  ND1 . HIS A  1 161 ? 34.922  -3.007  28.946  1.00 24.95  ? 161 HIS A ND1 1 
ATOM   1282 C  CD2 . HIS A  1 161 ? 34.253  -4.564  27.510  1.00 20.68  ? 161 HIS A CD2 1 
ATOM   1283 C  CE1 . HIS A  1 161 ? 35.964  -3.809  28.756  1.00 25.28  ? 161 HIS A CE1 1 
ATOM   1284 N  NE2 . HIS A  1 161 ? 35.569  -4.793  27.949  1.00 22.43  ? 161 HIS A NE2 1 
ATOM   1285 N  N   . LEU A  1 162 ? 29.074  -2.807  28.954  1.00 17.35  ? 162 LEU A N   1 
ATOM   1286 C  CA  . LEU A  1 162 ? 27.931  -1.902  28.899  1.00 16.81  ? 162 LEU A CA  1 
ATOM   1287 C  C   . LEU A  1 162 ? 27.725  -1.146  30.191  1.00 18.87  ? 162 LEU A C   1 
ATOM   1288 O  O   . LEU A  1 162 ? 27.218  -0.006  30.150  1.00 18.16  ? 162 LEU A O   1 
ATOM   1289 C  CB  . LEU A  1 162 ? 26.609  -2.717  28.608  1.00 19.78  ? 162 LEU A CB  1 
ATOM   1290 C  CG  . LEU A  1 162 ? 26.563  -3.320  27.201  1.00 18.05  ? 162 LEU A CG  1 
ATOM   1291 C  CD1 . LEU A  1 162 ? 25.329  -4.312  27.126  1.00 22.76  ? 162 LEU A CD1 1 
ATOM   1292 C  CD2 . LEU A  1 162 ? 26.652  -2.365  26.056  1.00 26.99  ? 162 LEU A CD2 1 
ATOM   1293 N  N   . GLN A  1 163 ? 28.099  -1.750  31.356  1.00 19.55  ? 163 GLN A N   1 
ATOM   1294 C  CA  . GLN A  1 163 ? 28.040  -1.103  32.673  1.00 21.73  ? 163 GLN A CA  1 
ATOM   1295 C  C   . GLN A  1 163 ? 28.699  0.241   32.693  1.00 24.21  ? 163 GLN A C   1 
ATOM   1296 O  O   . GLN A  1 163 ? 28.327  1.112   33.481  1.00 35.20  ? 163 GLN A O   1 
ATOM   1297 C  CB  . GLN A  1 163 ? 28.642  -2.084  33.777  1.00 28.38  ? 163 GLN A CB  1 
ATOM   1298 C  CG  . GLN A  1 163 ? 30.079  -2.582  33.445  1.00 28.70  ? 163 GLN A CG  1 
ATOM   1299 C  CD  . GLN A  1 163 ? 30.730  -3.318  34.575  1.00 40.61  ? 163 GLN A CD  1 
ATOM   1300 O  OE1 . GLN A  1 163 ? 30.302  -3.183  35.732  1.00 33.21  ? 163 GLN A OE1 1 
ATOM   1301 N  NE2 . GLN A  1 163 ? 31.808  -4.076  34.267  1.00 45.49  ? 163 GLN A NE2 1 
ATOM   1302 N  N   . HIS A  1 164 ? 29.728  0.414   31.903  1.00 18.62  ? 164 HIS A N   1 
ATOM   1303 C  CA  . HIS A  1 164 ? 30.552  1.685   31.956  1.00 19.07  ? 164 HIS A CA  1 
ATOM   1304 C  C   . HIS A  1 164 ? 30.097  2.662   30.953  1.00 18.69  ? 164 HIS A C   1 
ATOM   1305 O  O   . HIS A  1 164 ? 30.742  3.721   30.845  1.00 21.47  ? 164 HIS A O   1 
ATOM   1306 C  CB  . HIS A  1 164 ? 31.996  1.348   31.766  1.00 20.08  ? 164 HIS A CB  1 
ATOM   1307 C  CG  . HIS A  1 164 ? 32.590  0.444   32.803  1.00 18.44  ? 164 HIS A CG  1 
ATOM   1308 N  ND1 . HIS A  1 164 ? 32.301  0.419   34.143  1.00 20.10  ? 164 HIS A ND1 1 
ATOM   1309 C  CD2 . HIS A  1 164 ? 33.624  -0.403  32.656  1.00 21.25  ? 164 HIS A CD2 1 
ATOM   1310 C  CE1 . HIS A  1 164 ? 33.074  -0.458  34.790  1.00 19.20  ? 164 HIS A CE1 1 
ATOM   1311 N  NE2 . HIS A  1 164 ? 33.851  -1.013  33.879  1.00 32.80  ? 164 HIS A NE2 1 
ATOM   1312 N  N   . VAL A  1 165 ? 29.093  2.325   30.096  1.00 17.20  ? 165 VAL A N   1 
ATOM   1313 C  CA  . VAL A  1 165 ? 28.588  3.302   29.129  1.00 16.98  ? 165 VAL A CA  1 
ATOM   1314 C  C   . VAL A  1 165 ? 27.049  3.458   29.263  1.00 15.89  ? 165 VAL A C   1 
ATOM   1315 O  O   . VAL A  1 165 ? 26.349  3.692   28.278  1.00 16.47  ? 165 VAL A O   1 
ATOM   1316 C  CB  . VAL A  1 165 ? 28.995  3.004   27.650  1.00 19.05  ? 165 VAL A CB  1 
ATOM   1317 C  CG1 . VAL A  1 165 ? 30.524  3.143   27.514  1.00 19.54  ? 165 VAL A CG1 1 
ATOM   1318 C  CG2 . VAL A  1 165 ? 28.567  1.577   27.219  1.00 18.09  ? 165 VAL A CG2 1 
ATOM   1319 N  N   . LYS A  1 166 ? 26.558  3.419   30.520  1.00 17.15  ? 166 LYS A N   1 
ATOM   1320 C  CA  . LYS A  1 166 ? 25.184  3.448   30.790  1.00 17.31  ? 166 LYS A CA  1 
ATOM   1321 C  C   . LYS A  1 166 ? 24.454  4.697   30.221  1.00 15.27  ? 166 LYS A C   1 
ATOM   1322 O  O   . LYS A  1 166 ? 23.332  4.554   29.753  1.00 17.46  ? 166 LYS A O   1 
ATOM   1323 C  CB  . LYS A  1 166 ? 24.960  3.350   32.337  1.00 18.52  ? 166 LYS A CB  1 
ATOM   1324 C  CG  . LYS A  1 166 ? 23.529  3.379   32.798  1.00 19.39  ? 166 LYS A CG  1 
ATOM   1325 C  CD  . LYS A  1 166 ? 23.497  2.963   34.324  1.00 23.07  ? 166 LYS A CD  1 
ATOM   1326 C  CE  . LYS A  1 166 ? 24.235  1.596   34.539  1.00 31.80  ? 166 LYS A CE  1 
ATOM   1327 N  NZ  . LYS A  1 166 ? 23.420  0.550   33.879  1.00 57.21  ? 166 LYS A NZ  1 
ATOM   1328 N  N   . TYR A  1 167 ? 25.062  5.879   30.279  1.00 16.50  ? 167 TYR A N   1 
ATOM   1329 C  CA  . TYR A  1 167 ? 24.367  7.166   29.930  1.00 16.57  ? 167 TYR A CA  1 
ATOM   1330 C  C   . TYR A  1 167 ? 24.979  7.853   28.751  1.00 16.02  ? 167 TYR A C   1 
ATOM   1331 O  O   . TYR A  1 167 ? 26.180  7.615   28.395  1.00 17.03  ? 167 TYR A O   1 
ATOM   1332 C  CB  . TYR A  1 167 ? 24.440  8.159   31.096  1.00 17.53  ? 167 TYR A CB  1 
ATOM   1333 C  CG  . TYR A  1 167 ? 23.676  7.622   32.305  1.00 16.34  ? 167 TYR A CG  1 
ATOM   1334 C  CD1 . TYR A  1 167 ? 22.277  7.683   32.338  1.00 18.17  ? 167 TYR A CD1 1 
ATOM   1335 C  CD2 . TYR A  1 167 ? 24.351  7.137   33.400  1.00 18.22  ? 167 TYR A CD2 1 
ATOM   1336 C  CE1 . TYR A  1 167 ? 21.546  7.169   33.390  1.00 19.40  ? 167 TYR A CE1 1 
ATOM   1337 C  CE2 . TYR A  1 167 ? 23.653  6.612   34.494  1.00 22.34  ? 167 TYR A CE2 1 
ATOM   1338 C  CZ  . TYR A  1 167 ? 22.235  6.659   34.471  1.00 20.01  ? 167 TYR A CZ  1 
ATOM   1339 O  OH  . TYR A  1 167 ? 21.524  6.224   35.588  1.00 23.17  ? 167 TYR A OH  1 
ATOM   1340 N  N   . LYS A  1 168 ? 24.161  8.668   28.085  1.00 17.23  ? 168 LYS A N   1 
ATOM   1341 C  CA  . LYS A  1 168 ? 24.671  9.299   26.867  1.00 19.08  ? 168 LYS A CA  1 
ATOM   1342 C  C   . LYS A  1 168 ? 25.932  10.084  27.189  1.00 19.74  ? 168 LYS A C   1 
ATOM   1343 O  O   . LYS A  1 168 ? 26.014  10.799  28.180  1.00 19.85  ? 168 LYS A O   1 
ATOM   1344 C  CB  . LYS A  1 168 ? 23.582  10.284  26.446  1.00 19.35  ? 168 LYS A CB  1 
ATOM   1345 C  CG  . LYS A  1 168 ? 23.903  11.056  25.127  1.00 19.91  ? 168 LYS A CG  1 
ATOM   1346 C  CD  . LYS A  1 168 ? 22.776  11.922  24.643  1.00 24.91  ? 168 LYS A CD  1 
ATOM   1347 C  CE  . LYS A  1 168 ? 23.261  12.600  23.331  1.00 38.41  ? 168 LYS A CE  1 
ATOM   1348 N  NZ  . LYS A  1 168 ? 22.209  13.479  22.771  1.00 38.46  ? 168 LYS A NZ  1 
ATOM   1349 N  N   . GLY A  1 169 ? 26.929  9.945   26.313  1.00 19.05  ? 169 GLY A N   1 
ATOM   1350 C  CA  . GLY A  1 169 ? 28.160  10.654  26.523  1.00 21.62  ? 169 GLY A CA  1 
ATOM   1351 C  C   . GLY A  1 169 ? 29.258  9.857   27.179  1.00 22.75  ? 169 GLY A C   1 
ATOM   1352 O  O   . GLY A  1 169 ? 30.404  10.236  27.089  1.00 27.29  ? 169 GLY A O   1 
ATOM   1353 N  N   . GLN A  1 170 ? 28.925  8.798   27.873  1.00 18.15  ? 170 GLN A N   1 
ATOM   1354 C  CA  . GLN A  1 170 ? 29.877  8.066   28.623  1.00 17.76  ? 170 GLN A CA  1 
ATOM   1355 C  C   . GLN A  1 170 ? 30.697  7.202   27.619  1.00 18.25  ? 170 GLN A C   1 
ATOM   1356 O  O   . GLN A  1 170 ? 30.179  6.830   26.532  1.00 19.00  ? 170 GLN A O   1 
ATOM   1357 C  CB  . GLN A  1 170 ? 29.205  7.199   29.725  1.00 16.99  ? 170 GLN A CB  1 
ATOM   1358 C  CG  . GLN A  1 170 ? 28.651  8.066   30.816  1.00 18.21  ? 170 GLN A CG  1 
ATOM   1359 C  CD  . GLN A  1 170 ? 28.083  7.303   31.954  1.00 18.55  ? 170 GLN A CD  1 
ATOM   1360 O  OE1 . GLN A  1 170 ? 27.548  6.258   31.766  1.00 18.45  ? 170 GLN A OE1 1 
ATOM   1361 N  NE2 . GLN A  1 170 ? 28.251  7.781   33.193  1.00 23.29  ? 170 GLN A NE2 1 
ATOM   1362 N  N   A GLU A  1 171 ? 31.960  6.895   27.993  0.50 19.09  ? 171 GLU A N   1 
ATOM   1363 N  N   B GLU A  1 171 ? 31.896  6.784   28.096  0.50 18.96  ? 171 GLU A N   1 
ATOM   1364 C  CA  A GLU A  1 171 ? 32.995  6.325   27.120  0.50 17.59  ? 171 GLU A CA  1 
ATOM   1365 C  CA  B GLU A  1 171 ? 32.865  6.040   27.309  0.50 18.58  ? 171 GLU A CA  1 
ATOM   1366 C  C   A GLU A  1 171 ? 33.764  5.327   27.923  0.50 16.97  ? 171 GLU A C   1 
ATOM   1367 C  C   B GLU A  1 171 ? 33.491  4.989   28.104  0.50 16.65  ? 171 GLU A C   1 
ATOM   1368 O  O   A GLU A  1 171 ? 33.996  5.631   29.128  0.50 18.81  ? 171 GLU A O   1 
ATOM   1369 O  O   B GLU A  1 171 ? 33.601  4.964   29.375  0.50 17.97  ? 171 GLU A O   1 
ATOM   1370 C  CB  A GLU A  1 171 ? 33.897  7.459   26.584  0.50 21.48  ? 171 GLU A CB  1 
ATOM   1371 C  CB  B GLU A  1 171 ? 33.954  6.926   26.636  0.50 21.28  ? 171 GLU A CB  1 
ATOM   1372 C  CG  A GLU A  1 171 ? 33.204  8.249   25.492  0.50 27.30  ? 171 GLU A CG  1 
ATOM   1373 C  CG  B GLU A  1 171 ? 34.739  7.826   27.575  0.50 22.05  ? 171 GLU A CG  1 
ATOM   1374 C  CD  A GLU A  1 171 ? 34.043  9.428   24.985  0.50 24.43  ? 171 GLU A CD  1 
ATOM   1375 C  CD  B GLU A  1 171 ? 35.849  8.567   26.823  0.50 25.88  ? 171 GLU A CD  1 
ATOM   1376 O  OE1 A GLU A  1 171 ? 35.166  9.595   25.457  0.50 31.30  ? 171 GLU A OE1 1 
ATOM   1377 O  OE1 B GLU A  1 171 ? 35.571  9.003   25.703  0.50 24.42  ? 171 GLU A OE1 1 
ATOM   1378 O  OE2 A GLU A  1 171 ? 33.524  10.161  24.127  0.50 26.02  ? 171 GLU A OE2 1 
ATOM   1379 O  OE2 B GLU A  1 171 ? 36.995  8.676   27.400  0.50 24.72  ? 171 GLU A OE2 1 
ATOM   1380 N  N   . ALA A  1 172 ? 34.096  4.121   27.375  1.00 18.80  ? 172 ALA A N   1 
ATOM   1381 C  CA  . ALA A  1 172 ? 34.913  3.108   28.027  1.00 18.31  ? 172 ALA A CA  1 
ATOM   1382 C  C   . ALA A  1 172 ? 35.890  2.589   26.943  1.00 18.86  ? 172 ALA A C   1 
ATOM   1383 O  O   . ALA A  1 172 ? 35.727  2.843   25.775  1.00 20.08  ? 172 ALA A O   1 
ATOM   1384 C  CB  . ALA A  1 172 ? 34.091  1.934   28.474  1.00 20.89  ? 172 ALA A CB  1 
ATOM   1385 N  N   . PHE A  1 173 ? 36.838  1.777   27.369  1.00 19.45  ? 173 PHE A N   1 
ATOM   1386 C  CA  . PHE A  1 173 ? 37.850  1.173   26.472  1.00 19.15  ? 173 PHE A CA  1 
ATOM   1387 C  C   . PHE A  1 173 ? 37.727  -0.336  26.419  1.00 20.51  ? 173 PHE A C   1 
ATOM   1388 O  O   . PHE A  1 173 ? 37.695  -1.005  27.467  1.00 26.11  ? 173 PHE A O   1 
ATOM   1389 C  CB  . PHE A  1 173 ? 39.222  1.651   26.906  1.00 22.60  ? 173 PHE A CB  1 
ATOM   1390 C  CG  . PHE A  1 173 ? 39.492  3.060   26.477  1.00 22.62  ? 173 PHE A CG  1 
ATOM   1391 C  CD1 . PHE A  1 173 ? 39.748  3.393   25.099  1.00 27.50  ? 173 PHE A CD1 1 
ATOM   1392 C  CD2 . PHE A  1 173 ? 39.342  4.092   27.370  1.00 34.43  ? 173 PHE A CD2 1 
ATOM   1393 C  CE1 . PHE A  1 173 ? 39.956  4.711   24.694  1.00 25.52  ? 173 PHE A CE1 1 
ATOM   1394 C  CE2 . PHE A  1 173 ? 39.571  5.409   27.004  1.00 32.79  ? 173 PHE A CE2 1 
ATOM   1395 C  CZ  . PHE A  1 173 ? 39.902  5.723   25.668  1.00 35.81  ? 173 PHE A CZ  1 
ATOM   1396 N  N   . VAL A  1 174 ? 37.651  -0.865  25.220  1.00 18.62  ? 174 VAL A N   1 
ATOM   1397 C  CA  . VAL A  1 174 ? 37.579  -2.291  25.035  1.00 17.81  ? 174 VAL A CA  1 
ATOM   1398 C  C   . VAL A  1 174 ? 38.887  -2.788  24.428  1.00 18.73  ? 174 VAL A C   1 
ATOM   1399 O  O   . VAL A  1 174 ? 39.302  -2.293  23.423  1.00 20.20  ? 174 VAL A O   1 
ATOM   1400 C  CB  . VAL A  1 174 ? 36.414  -2.630  24.099  1.00 18.48  ? 174 VAL A CB  1 
ATOM   1401 C  CG1 . VAL A  1 174 ? 36.337  -4.128  23.811  1.00 21.34  ? 174 VAL A CG1 1 
ATOM   1402 C  CG2 . VAL A  1 174 ? 35.096  -2.031  24.678  1.00 20.77  ? 174 VAL A CG2 1 
ATOM   1403 N  N   . PRO A  1 175 ? 39.546  -3.781  25.038  1.00 19.50  ? 175 PRO A N   1 
ATOM   1404 C  CA  . PRO A  1 175 ? 40.764  -4.294  24.442  1.00 19.33  ? 175 PRO A CA  1 
ATOM   1405 C  C   . PRO A  1 175 ? 40.477  -4.953  23.107  1.00 18.14  ? 175 PRO A C   1 
ATOM   1406 O  O   . PRO A  1 175 ? 39.419  -5.685  22.983  1.00 18.96  ? 175 PRO A O   1 
ATOM   1407 C  CB  . PRO A  1 175 ? 41.304  -5.311  25.475  1.00 23.29  ? 175 PRO A CB  1 
ATOM   1408 C  CG  . PRO A  1 175 ? 40.627  -4.901  26.762  1.00 26.66  ? 175 PRO A CG  1 
ATOM   1409 C  CD  . PRO A  1 175 ? 39.224  -4.417  26.316  1.00 20.96  ? 175 PRO A CD  1 
ATOM   1410 N  N   . GLY A  1 176 ? 41.415  -4.935  22.214  1.00 19.18  ? 176 GLY A N   1 
ATOM   1411 C  CA  . GLY A  1 176 ? 41.209  -5.539  20.959  1.00 17.25  ? 176 GLY A CA  1 
ATOM   1412 C  C   . GLY A  1 176 ? 40.842  -6.974  21.071  1.00 18.29  ? 176 GLY A C   1 
ATOM   1413 O  O   . GLY A  1 176 ? 41.418  -7.707  21.889  1.00 21.08  ? 176 GLY A O   1 
ATOM   1414 N  N   . PHE A  1 177 ? 39.934  -7.417  20.204  1.00 17.54  ? 177 PHE A N   1 
ATOM   1415 C  CA  . PHE A  1 177 ? 39.651  -8.823  20.028  1.00 17.50  ? 177 PHE A CA  1 
ATOM   1416 C  C   . PHE A  1 177 ? 39.287  -9.089  18.585  1.00 15.90  ? 177 PHE A C   1 
ATOM   1417 O  O   . PHE A  1 177 ? 39.261  -8.128  17.768  1.00 17.25  ? 177 PHE A O   1 
ATOM   1418 C  CB  . PHE A  1 177 ? 38.543  -9.321  20.961  1.00 19.28  ? 177 PHE A CB  1 
ATOM   1419 C  CG  . PHE A  1 177 ? 37.143  -8.695  20.642  1.00 17.77  ? 177 PHE A CG  1 
ATOM   1420 C  CD1 . PHE A  1 177 ? 36.820  -7.436  21.039  1.00 17.20  ? 177 PHE A CD1 1 
ATOM   1421 C  CD2 . PHE A  1 177 ? 36.207  -9.427  19.880  1.00 18.95  ? 177 PHE A CD2 1 
ATOM   1422 C  CE1 . PHE A  1 177 ? 35.516  -6.899  20.764  1.00 19.41  ? 177 PHE A CE1 1 
ATOM   1423 C  CE2 . PHE A  1 177 ? 34.943  -8.937  19.567  1.00 18.65  ? 177 PHE A CE2 1 
ATOM   1424 C  CZ  . PHE A  1 177 ? 34.639  -7.677  20.023  1.00 17.33  ? 177 PHE A CZ  1 
ATOM   1425 N  N   . ASN A  1 178 ? 39.124  -10.338 18.204  1.00 18.21  ? 178 ASN A N   1 
ATOM   1426 C  CA  . ASN A  1 178 ? 38.918  -10.650 16.749  1.00 16.59  ? 178 ASN A CA  1 
ATOM   1427 C  C   . ASN A  1 178 ? 37.421  -10.379 16.399  1.00 16.34  ? 178 ASN A C   1 
ATOM   1428 O  O   . ASN A  1 178 ? 36.515  -11.159 16.743  1.00 15.70  ? 178 ASN A O   1 
ATOM   1429 C  CB  . ASN A  1 178 ? 39.248  -12.112 16.479  1.00 18.48  ? 178 ASN A CB  1 
ATOM   1430 C  CG  . ASN A  1 178 ? 39.114  -12.535 15.037  1.00 18.05  ? 178 ASN A CG  1 
ATOM   1431 O  OD1 . ASN A  1 178 ? 38.784  -11.694 14.126  1.00 19.08  ? 178 ASN A OD1 1 
ATOM   1432 N  ND2 . ASN A  1 178 ? 39.272  -13.768 14.773  1.00 23.64  ? 178 ASN A ND2 1 
ATOM   1433 N  N   . ILE A  1 179 ? 37.158  -9.288  15.716  1.00 14.59  ? 179 ILE A N   1 
ATOM   1434 C  CA  . ILE A  1 179 ? 35.805  -8.870  15.378  1.00 14.32  ? 179 ILE A CA  1 
ATOM   1435 C  C   . ILE A  1 179 ? 35.171  -9.926  14.446  1.00 13.20  ? 179 ILE A C   1 
ATOM   1436 O  O   . ILE A  1 179 ? 33.941  -10.013 14.395  1.00 13.14  ? 179 ILE A O   1 
ATOM   1437 C  CB  . ILE A  1 179 ? 35.890  -7.492  14.634  1.00 14.14  ? 179 ILE A CB  1 
ATOM   1438 C  CG1 . ILE A  1 179 ? 36.498  -6.436  15.507  1.00 15.17  ? 179 ILE A CG1 1 
ATOM   1439 C  CG2 . ILE A  1 179 ? 34.494  -6.994  14.212  1.00 15.47  ? 179 ILE A CG2 1 
ATOM   1440 C  CD1 . ILE A  1 179 ? 35.902  -6.261  16.913  1.00 16.05  ? 179 ILE A CD1 1 
ATOM   1441 N  N   . GLU A  1 180 ? 35.928  -10.752 13.745  1.00 14.19  ? 180 GLU A N   1 
ATOM   1442 C  CA  . GLU A  1 180 ? 35.350  -11.764 12.887  1.00 14.58  ? 180 GLU A CA  1 
ATOM   1443 C  C   . GLU A  1 180 ? 34.523  -12.773 13.754  1.00 14.93  ? 180 GLU A C   1 
ATOM   1444 O  O   . GLU A  1 180 ? 33.637  -13.448 13.184  1.00 15.96  ? 180 GLU A O   1 
ATOM   1445 C  CB  . GLU A  1 180 ? 36.379  -12.408 12.023  1.00 16.84  ? 180 GLU A CB  1 
ATOM   1446 C  CG  . GLU A  1 180 ? 35.800  -13.201 10.874  1.00 20.86  ? 180 GLU A CG  1 
ATOM   1447 C  CD  . GLU A  1 180 ? 36.837  -13.728 9.889   1.00 21.05  ? 180 GLU A CD  1 
ATOM   1448 O  OE1 . GLU A  1 180 ? 38.034  -13.400 10.034  1.00 26.45  ? 180 GLU A OE1 1 
ATOM   1449 O  OE2 . GLU A  1 180 ? 36.424  -14.474 8.968   1.00 26.47  ? 180 GLU A OE2 1 
ATOM   1450 N  N   . GLU A  1 181 ? 34.858  -12.849 15.041  1.00 14.76  ? 181 GLU A N   1 
ATOM   1451 C  CA  . GLU A  1 181 ? 34.061  -13.736 15.904  1.00 15.24  ? 181 GLU A CA  1 
ATOM   1452 C  C   . GLU A  1 181 ? 32.626  -13.329 16.044  1.00 13.10  ? 181 GLU A C   1 
ATOM   1453 O  O   . GLU A  1 181 ? 31.801  -14.081 16.537  1.00 15.53  ? 181 GLU A O   1 
ATOM   1454 C  CB  . GLU A  1 181 ? 34.690  -13.823 17.296  1.00 17.84  ? 181 GLU A CB  1 
ATOM   1455 C  CG  . GLU A  1 181 ? 36.117  -14.403 17.379  1.00 18.42  ? 181 GLU A CG  1 
ATOM   1456 C  CD  . GLU A  1 181 ? 36.764  -14.135 18.763  1.00 22.22  ? 181 GLU A CD  1 
ATOM   1457 O  OE1 . GLU A  1 181 ? 36.076  -13.709 19.765  1.00 25.20  ? 181 GLU A OE1 1 
ATOM   1458 O  OE2 . GLU A  1 181 ? 37.972  -14.423 18.877  1.00 25.56  ? 181 GLU A OE2 1 
ATOM   1459 N  N   . LEU A  1 182 ? 32.306  -12.053 15.711  1.00 12.50  ? 182 LEU A N   1 
ATOM   1460 C  CA  . LEU A  1 182 ? 30.944  -11.549 15.777  1.00 11.76  ? 182 LEU A CA  1 
ATOM   1461 C  C   . LEU A  1 182 ? 30.135  -11.955 14.547  1.00 12.45  ? 182 LEU A C   1 
ATOM   1462 O  O   . LEU A  1 182 ? 28.897  -11.756 14.521  1.00 12.74  ? 182 LEU A O   1 
ATOM   1463 C  CB  . LEU A  1 182 ? 30.920  -10.035 15.913  1.00 11.70  ? 182 LEU A CB  1 
ATOM   1464 C  CG  . LEU A  1 182 ? 31.709  -9.508  17.085  1.00 11.97  ? 182 LEU A CG  1 
ATOM   1465 C  CD1 . LEU A  1 182 ? 31.628  -7.974  17.084  1.00 13.88  ? 182 LEU A CD1 1 
ATOM   1466 C  CD2 . LEU A  1 182 ? 31.152  -10.013 18.393  1.00 14.44  ? 182 LEU A CD2 1 
ATOM   1467 N  N   . LEU A  1 183 ? 30.775  -12.468 13.499  1.00 13.09  ? 183 LEU A N   1 
ATOM   1468 C  CA  . LEU A  1 183 ? 30.100  -12.843 12.294  1.00 13.40  ? 183 LEU A CA  1 
ATOM   1469 C  C   . LEU A  1 183 ? 29.531  -14.220 12.362  1.00 13.18  ? 183 LEU A C   1 
ATOM   1470 O  O   . LEU A  1 183 ? 30.055  -15.052 13.128  1.00 15.13  ? 183 LEU A O   1 
ATOM   1471 C  CB  . LEU A  1 183 ? 31.051  -12.715 11.076  1.00 14.91  ? 183 LEU A CB  1 
ATOM   1472 C  CG  . LEU A  1 183 ? 31.733  -11.355 10.889  1.00 14.86  ? 183 LEU A CG  1 
ATOM   1473 C  CD1 . LEU A  1 183 ? 32.557  -11.359 9.601   1.00 18.74  ? 183 LEU A CD1 1 
ATOM   1474 C  CD2 . LEU A  1 183 ? 30.691  -10.217 10.810  1.00 16.17  ? 183 LEU A CD2 1 
ATOM   1475 N  N   . PRO A  1 184 ? 28.480  -14.524 11.637  1.00 13.36  ? 184 PRO A N   1 
ATOM   1476 C  CA  . PRO A  1 184 ? 27.885  -15.829 11.674  1.00 14.78  ? 184 PRO A CA  1 
ATOM   1477 C  C   . PRO A  1 184 ? 28.597  -16.826 10.924  1.00 19.00  ? 184 PRO A C   1 
ATOM   1478 O  O   . PRO A  1 184 ? 29.710  -16.513 10.273  1.00 18.37  ? 184 PRO A O   1 
ATOM   1479 C  CB  . PRO A  1 184 ? 26.415  -15.466 11.098  1.00 18.81  ? 184 PRO A CB  1 
ATOM   1480 C  CG  . PRO A  1 184 ? 26.818  -14.430 10.010  1.00 16.40  ? 184 PRO A CG  1 
ATOM   1481 C  CD  . PRO A  1 184 ? 27.782  -13.593 10.737  1.00 14.19  ? 184 PRO A CD  1 
ATOM   1482 N  N   . GLU A  1 185 ? 27.969  -18.028 10.918  1.00 19.49  ? 185 GLU A N   1 
ATOM   1483 C  CA  . GLU A  1 185 ? 28.422  -19.119 10.000  1.00 20.36  ? 185 GLU A CA  1 
ATOM   1484 C  C   . GLU A  1 185 ? 28.164  -18.774 8.576   1.00 19.87  ? 185 GLU A C   1 
ATOM   1485 O  O   . GLU A  1 185 ? 27.168  -18.094 8.255   1.00 20.73  ? 185 GLU A O   1 
ATOM   1486 C  CB  . GLU A  1 185 ? 27.595  -20.430 10.346  1.00 26.05  ? 185 GLU A CB  1 
ATOM   1487 C  CG  . GLU A  1 185 ? 27.936  -20.920 11.762  1.00 35.95  ? 185 GLU A CG  1 
ATOM   1488 C  CD  . GLU A  1 185 ? 29.472  -20.960 11.992  1.00 48.48  ? 185 GLU A CD  1 
ATOM   1489 O  OE1 . GLU A  1 185 ? 30.205  -21.708 11.284  1.00 61.46  ? 185 GLU A OE1 1 
ATOM   1490 O  OE2 . GLU A  1 185 ? 29.961  -20.263 12.880  1.00 51.06  ? 185 GLU A OE2 1 
ATOM   1491 N  N   . ARG A  1 186 ? 29.060  -19.346 7.764   1.00 18.52  ? 186 ARG A N   1 
ATOM   1492 C  CA  . ARG A  1 186 ? 28.897  -19.231 6.353   1.00 21.56  ? 186 ARG A CA  1 
ATOM   1493 C  C   . ARG A  1 186 ? 28.715  -17.845 5.903   1.00 19.73  ? 186 ARG A C   1 
ATOM   1494 O  O   . ARG A  1 186 ? 27.709  -17.458 5.225   1.00 17.77  ? 186 ARG A O   1 
ATOM   1495 C  CB  . ARG A  1 186 ? 27.782  -20.214 5.804   1.00 23.55  ? 186 ARG A CB  1 
ATOM   1496 C  CG  . ARG A  1 186 ? 28.053  -21.635 6.230   1.00 34.22  ? 186 ARG A CG  1 
ATOM   1497 C  CD  . ARG A  1 186 ? 27.090  -22.668 5.663   1.00 32.30  ? 186 ARG A CD  1 
ATOM   1498 N  NE  . ARG A  1 186 ? 25.706  -22.496 6.104   1.00 38.42  ? 186 ARG A NE  1 
ATOM   1499 C  CZ  . ARG A  1 186 ? 25.217  -22.735 7.325   1.00 39.74  ? 186 ARG A CZ  1 
ATOM   1500 N  NH1 . ARG A  1 186 ? 25.998  -23.127 8.333   1.00 45.65  ? 186 ARG A NH1 1 
ATOM   1501 N  NH2 . ARG A  1 186 ? 23.922  -22.521 7.542   1.00 42.85  ? 186 ARG A NH2 1 
ATOM   1502 N  N   . THR A  1 187 ? 29.699  -17.049 6.158   1.00 15.78  ? 187 THR A N   1 
ATOM   1503 C  CA  . THR A  1 187 ? 29.596  -15.678 5.674   1.00 15.67  ? 187 THR A CA  1 
ATOM   1504 C  C   . THR A  1 187 ? 29.581  -15.588 4.164   1.00 16.82  ? 187 THR A C   1 
ATOM   1505 O  O   . THR A  1 187 ? 29.257  -14.530 3.667   1.00 16.53  ? 187 THR A O   1 
ATOM   1506 C  CB  . THR A  1 187 ? 30.716  -14.818 6.230   1.00 15.85  ? 187 THR A CB  1 
ATOM   1507 O  OG1 . THR A  1 187 ? 31.950  -15.447 6.033   1.00 18.89  ? 187 THR A OG1 1 
ATOM   1508 C  CG2 . THR A  1 187 ? 30.519  -14.500 7.752   1.00 17.01  ? 187 THR A CG2 1 
ATOM   1509 N  N   . ALA A  1 188 ? 29.884  -16.654 3.444   1.00 18.02  ? 188 ALA A N   1 
ATOM   1510 C  CA  . ALA A  1 188 ? 29.680  -16.642 1.994   1.00 18.13  ? 188 ALA A CA  1 
ATOM   1511 C  C   . ALA A  1 188 ? 28.250  -16.394 1.566   1.00 16.03  ? 188 ALA A C   1 
ATOM   1512 O  O   . ALA A  1 188 ? 28.035  -15.938 0.434   1.00 16.24  ? 188 ALA A O   1 
ATOM   1513 C  CB  . ALA A  1 188 ? 30.148  -18.027 1.361   1.00 21.68  ? 188 ALA A CB  1 
ATOM   1514 N  N   . GLU A  1 189 ? 27.290  -16.685 2.446   1.00 15.75  ? 189 GLU A N   1 
ATOM   1515 C  CA  . GLU A  1 189 ? 25.861  -16.599 2.127   1.00 15.62  ? 189 GLU A CA  1 
ATOM   1516 C  C   . GLU A  1 189 ? 25.354  -15.176 2.660   1.00 13.44  ? 189 GLU A C   1 
ATOM   1517 O  O   . GLU A  1 189 ? 25.318  -14.969 3.889   1.00 13.42  ? 189 GLU A O   1 
ATOM   1518 C  CB  . GLU A  1 189 ? 25.066  -17.709 2.806   1.00 18.62  ? 189 GLU A CB  1 
ATOM   1519 C  CG  . GLU A  1 189 ? 25.449  -19.129 2.280   1.00 25.83  ? 189 GLU A CG  1 
ATOM   1520 C  CD  . GLU A  1 189 ? 24.991  -20.286 3.213   1.00 26.61  ? 189 GLU A CD  1 
ATOM   1521 O  OE1 . GLU A  1 189 ? 24.328  -20.095 4.218   1.00 26.03  ? 189 GLU A OE1 1 
ATOM   1522 O  OE2 . GLU A  1 189 ? 25.451  -21.476 2.983   1.00 34.99  ? 189 GLU A OE2 1 
ATOM   1523 N  N   . TYR A  1 190 ? 24.923  -14.326 1.722   1.00 13.36  ? 190 TYR A N   1 
ATOM   1524 C  CA  . TYR A  1 190 ? 24.466  -12.982 2.115   1.00 11.85  ? 190 TYR A CA  1 
ATOM   1525 C  C   . TYR A  1 190 ? 23.544  -12.397 1.096   1.00 11.88  ? 190 TYR A C   1 
ATOM   1526 O  O   . TYR A  1 190 ? 23.445  -12.840 -0.075  1.00 13.45  ? 190 TYR A O   1 
ATOM   1527 C  CB  . TYR A  1 190 ? 25.675  -12.030 2.335   1.00 11.85  ? 190 TYR A CB  1 
ATOM   1528 C  CG  . TYR A  1 190 ? 26.588  -11.883 1.148   1.00 11.90  ? 190 TYR A CG  1 
ATOM   1529 C  CD1 . TYR A  1 190 ? 26.302  -10.986 0.122   1.00 13.02  ? 190 TYR A CD1 1 
ATOM   1530 C  CD2 . TYR A  1 190 ? 27.789  -12.616 1.085   1.00 14.46  ? 190 TYR A CD2 1 
ATOM   1531 C  CE1 . TYR A  1 190 ? 27.175  -10.817 -0.971  1.00 13.29  ? 190 TYR A CE1 1 
ATOM   1532 C  CE2 . TYR A  1 190 ? 28.686  -12.456 0.010   1.00 14.88  ? 190 TYR A CE2 1 
ATOM   1533 C  CZ  . TYR A  1 190 ? 28.355  -11.571 -0.975  1.00 14.06  ? 190 TYR A CZ  1 
ATOM   1534 O  OH  . TYR A  1 190 ? 29.201  -11.352 -2.087  1.00 15.48  ? 190 TYR A OH  1 
ATOM   1535 N  N   . TYR A  1 191 ? 22.771  -11.390 1.570   1.00 11.54  ? 191 TYR A N   1 
ATOM   1536 C  CA  . TYR A  1 191 ? 21.951  -10.534 0.769   1.00 11.45  ? 191 TYR A CA  1 
ATOM   1537 C  C   . TYR A  1 191 ? 22.689  -9.214  0.472   1.00 10.69  ? 191 TYR A C   1 
ATOM   1538 O  O   . TYR A  1 191 ? 23.440  -8.751  1.340   1.00 11.90  ? 191 TYR A O   1 
ATOM   1539 C  CB  . TYR A  1 191 ? 20.674  -10.127 1.577   1.00 12.25  ? 191 TYR A CB  1 
ATOM   1540 C  CG  . TYR A  1 191 ? 19.871  -11.263 2.146   1.00 12.39  ? 191 TYR A CG  1 
ATOM   1541 C  CD1 . TYR A  1 191 ? 18.815  -11.807 1.418   1.00 13.57  ? 191 TYR A CD1 1 
ATOM   1542 C  CD2 . TYR A  1 191 ? 20.090  -11.662 3.462   1.00 12.59  ? 191 TYR A CD2 1 
ATOM   1543 C  CE1 . TYR A  1 191 ? 17.998  -12.781 1.990   1.00 14.76  ? 191 TYR A CE1 1 
ATOM   1544 C  CE2 . TYR A  1 191 ? 19.280  -12.649 4.066   1.00 13.55  ? 191 TYR A CE2 1 
ATOM   1545 C  CZ  . TYR A  1 191 ? 18.262  -13.190 3.325   1.00 13.32  ? 191 TYR A CZ  1 
ATOM   1546 O  OH  . TYR A  1 191 ? 17.437  -14.178 3.863   1.00 16.42  ? 191 TYR A OH  1 
ATOM   1547 N  N   . ARG A  1 192 ? 22.525  -8.660  -0.701  1.00 11.44  ? 192 ARG A N   1 
ATOM   1548 C  CA  . ARG A  1 192 ? 23.235  -7.443  -1.083  1.00 11.48  ? 192 ARG A CA  1 
ATOM   1549 C  C   . ARG A  1 192 ? 22.317  -6.498  -1.781  1.00 10.99  ? 192 ARG A C   1 
ATOM   1550 O  O   . ARG A  1 192 ? 21.598  -6.882  -2.699  1.00 12.34  ? 192 ARG A O   1 
ATOM   1551 C  CB  . ARG A  1 192 ? 24.343  -7.885  -2.092  1.00 13.44  ? 192 ARG A CB  1 
ATOM   1552 C  CG  . ARG A  1 192 ? 24.983  -6.770  -2.937  1.00 14.21  ? 192 ARG A CG  1 
ATOM   1553 C  CD  . ARG A  1 192 ? 25.812  -5.814  -2.042  1.00 15.23  ? 192 ARG A CD  1 
ATOM   1554 N  NE  . ARG A  1 192 ? 26.800  -6.425  -1.127  1.00 15.60  ? 192 ARG A NE  1 
ATOM   1555 C  CZ  . ARG A  1 192 ? 27.908  -7.029  -1.547  1.00 14.30  ? 192 ARG A CZ  1 
ATOM   1556 N  NH1 . ARG A  1 192 ? 28.283  -6.997  -2.871  1.00 16.87  ? 192 ARG A NH1 1 
ATOM   1557 N  NH2 . ARG A  1 192 ? 28.717  -7.611  -0.683  1.00 16.35  ? 192 ARG A NH2 1 
ATOM   1558 N  N   . TYR A  1 193 ? 22.326  -5.230  -1.377  1.00 10.40  ? 193 TYR A N   1 
ATOM   1559 C  CA  . TYR A  1 193 ? 21.511  -4.203  -2.104  1.00 10.94  ? 193 TYR A CA  1 
ATOM   1560 C  C   . TYR A  1 193 ? 22.105  -2.858  -1.780  1.00 11.00  ? 193 TYR A C   1 
ATOM   1561 O  O   . TYR A  1 193 ? 22.807  -2.656  -0.766  1.00 11.98  ? 193 TYR A O   1 
ATOM   1562 C  CB  . TYR A  1 193 ? 20.025  -4.269  -1.732  1.00 11.71  ? 193 TYR A CB  1 
ATOM   1563 C  CG  . TYR A  1 193 ? 19.633  -3.733  -0.349  1.00 11.27  ? 193 TYR A CG  1 
ATOM   1564 C  CD1 . TYR A  1 193 ? 19.849  -4.470  0.821   1.00 10.63  ? 193 TYR A CD1 1 
ATOM   1565 C  CD2 . TYR A  1 193 ? 19.090  -2.487  -0.232  1.00 12.08  ? 193 TYR A CD2 1 
ATOM   1566 C  CE1 . TYR A  1 193 ? 19.551  -3.995  2.061   1.00 10.00  ? 193 TYR A CE1 1 
ATOM   1567 C  CE2 . TYR A  1 193 ? 18.800  -1.963  1.021   1.00 11.45  ? 193 TYR A CE2 1 
ATOM   1568 C  CZ  . TYR A  1 193 ? 19.050  -2.727  2.166   1.00 10.40  ? 193 TYR A CZ  1 
ATOM   1569 O  OH  . TYR A  1 193 ? 18.722  -2.139  3.364   1.00 10.22  ? 193 TYR A OH  1 
ATOM   1570 N  N   . ARG A  1 194 ? 21.772  -1.884  -2.622  1.00 11.35  ? 194 ARG A N   1 
ATOM   1571 C  CA  . ARG A  1 194 ? 22.179  -0.480  -2.382  1.00 11.06  ? 194 ARG A CA  1 
ATOM   1572 C  C   . ARG A  1 194 ? 21.124  0.233   -1.567  1.00 11.70  ? 194 ARG A C   1 
ATOM   1573 O  O   . ARG A  1 194 ? 19.907  0.219   -1.929  1.00 12.96  ? 194 ARG A O   1 
ATOM   1574 C  CB  . ARG A  1 194 ? 22.358  0.240   -3.723  1.00 15.27  ? 194 ARG A CB  1 
ATOM   1575 C  CG  . ARG A  1 194 ? 23.495  -0.316  -4.527  1.00 18.17  ? 194 ARG A CG  1 
ATOM   1576 C  CD  . ARG A  1 194 ? 24.822  0.168   -4.029  1.00 28.99  ? 194 ARG A CD  1 
ATOM   1577 N  NE  . ARG A  1 194 ? 25.949  -0.438  -4.805  1.00 51.17  ? 194 ARG A NE  1 
ATOM   1578 C  CZ  . ARG A  1 194 ? 27.096  0.161   -5.022  1.00 40.97  ? 194 ARG A CZ  1 
ATOM   1579 N  NH1 . ARG A  1 194 ? 27.274  1.408   -4.570  1.00 55.44  ? 194 ARG A NH1 1 
ATOM   1580 N  NH2 . ARG A  1 194 ? 28.036  -0.490  -5.727  1.00 43.33  ? 194 ARG A NH2 1 
ATOM   1581 N  N   . GLY A  1 195 ? 21.508  0.849   -0.478  1.00 10.62  ? 195 GLY A N   1 
ATOM   1582 C  CA  . GLY A  1 195 ? 20.567  1.572   0.362   1.00 10.72  ? 195 GLY A CA  1 
ATOM   1583 C  C   . GLY A  1 195 ? 21.164  2.728   1.047   1.00 10.37  ? 195 GLY A C   1 
ATOM   1584 O  O   . GLY A  1 195 ? 22.030  3.455   0.489   1.00 10.82  ? 195 GLY A O   1 
ATOM   1585 N  N   . SER A  1 196 ? 20.768  2.960   2.294   1.00 10.07  ? 196 SER A N   1 
ATOM   1586 C  CA  . SER A  1 196 ? 21.049  4.174   2.982   1.00 10.16  ? 196 SER A CA  1 
ATOM   1587 C  C   . SER A  1 196 ? 21.482  3.915   4.418   1.00 9.95   ? 196 SER A C   1 
ATOM   1588 O  O   . SER A  1 196 ? 21.325  2.799   4.928   1.00 10.03  ? 196 SER A O   1 
ATOM   1589 C  CB  . SER A  1 196 ? 19.805  5.105   3.051   1.00 10.74  ? 196 SER A CB  1 
ATOM   1590 O  OG  . SER A  1 196 ? 18.837  4.635   3.990   1.00 10.10  ? 196 SER A OG  1 
ATOM   1591 N  N   . LEU A  1 197 ? 21.996  4.964   5.078   1.00 9.77   ? 197 LEU A N   1 
ATOM   1592 C  CA  . LEU A  1 197 ? 22.039  4.952   6.522   1.00 10.12  ? 197 LEU A CA  1 
ATOM   1593 C  C   . LEU A  1 197 ? 20.613  4.689   7.044   1.00 8.96   ? 197 LEU A C   1 
ATOM   1594 O  O   . LEU A  1 197 ? 19.659  5.297   6.510   1.00 9.85   ? 197 LEU A O   1 
ATOM   1595 C  CB  . LEU A  1 197 ? 22.528  6.248   7.125   1.00 11.08  ? 197 LEU A CB  1 
ATOM   1596 C  CG  . LEU A  1 197 ? 24.028  6.517   7.151   1.00 13.15  ? 197 LEU A CG  1 
ATOM   1597 C  CD1 . LEU A  1 197 ? 24.565  6.843   5.776   1.00 16.84  ? 197 LEU A CD1 1 
ATOM   1598 C  CD2 . LEU A  1 197 ? 24.273  7.694   8.115   1.00 15.44  ? 197 LEU A CD2 1 
ATOM   1599 N  N   . THR A  1 198 ? 20.452  3.941   8.131   1.00 9.66   ? 198 THR A N   1 
ATOM   1600 C  CA  . THR A  1 198 ? 19.161  3.742   8.735   1.00 9.95   ? 198 THR A CA  1 
ATOM   1601 C  C   . THR A  1 198 ? 18.894  4.749   9.828   1.00 9.38   ? 198 THR A C   1 
ATOM   1602 O  O   . THR A  1 198 ? 17.823  4.704   10.461  1.00 10.46  ? 198 THR A O   1 
ATOM   1603 C  CB  . THR A  1 198 ? 19.010  2.335   9.295   1.00 9.27   ? 198 THR A CB  1 
ATOM   1604 O  OG1 . THR A  1 198 ? 19.882  2.255   10.412  1.00 9.46   ? 198 THR A OG1 1 
ATOM   1605 C  CG2 . THR A  1 198 ? 19.264  1.243   8.319   1.00 10.30  ? 198 THR A CG2 1 
ATOM   1606 N  N   . THR A  1 199 ? 19.819  5.671   10.066  1.00 9.94   ? 199 THR A N   1 
ATOM   1607 C  CA  . THR A  1 199 ? 19.667  6.737   11.012  1.00 10.40  ? 199 THR A CA  1 
ATOM   1608 C  C   . THR A  1 199 ? 19.857  8.073   10.208  1.00 10.53  ? 199 THR A C   1 
ATOM   1609 O  O   . THR A  1 199 ? 20.525  8.009   9.176   1.00 10.64  ? 199 THR A O   1 
ATOM   1610 C  CB  . THR A  1 199 ? 20.698  6.739   12.147  1.00 10.97  ? 199 THR A CB  1 
ATOM   1611 O  OG1 . THR A  1 199 ? 22.004  6.964   11.574  1.00 12.22  ? 199 THR A OG1 1 
ATOM   1612 C  CG2 . THR A  1 199 ? 20.704  5.405   12.828  1.00 11.96  ? 199 THR A CG2 1 
ATOM   1613 N  N   . PRO A  1 200 ? 19.376  9.187   10.752  1.00 10.07  ? 200 PRO A N   1 
ATOM   1614 C  CA  . PRO A  1 200 ? 19.813  10.481  10.186  1.00 11.50  ? 200 PRO A CA  1 
ATOM   1615 C  C   . PRO A  1 200 ? 21.330  10.493  10.043  1.00 11.96  ? 200 PRO A C   1 
ATOM   1616 O  O   . PRO A  1 200 ? 22.020  9.977   10.917  1.00 12.29  ? 200 PRO A O   1 
ATOM   1617 C  CB  . PRO A  1 200 ? 19.305  11.470  11.203  1.00 12.14  ? 200 PRO A CB  1 
ATOM   1618 C  CG  . PRO A  1 200 ? 18.056  10.818  11.761  1.00 11.17  ? 200 PRO A CG  1 
ATOM   1619 C  CD  . PRO A  1 200 ? 18.484  9.391   11.898  1.00 11.02  ? 200 PRO A CD  1 
ATOM   1620 N  N   . PRO A  1 201 ? 21.864  11.098  8.986   1.00 11.35  ? 201 PRO A N   1 
ATOM   1621 C  CA  . PRO A  1 201 ? 21.097  11.843  7.944   1.00 11.85  ? 201 PRO A CA  1 
ATOM   1622 C  C   . PRO A  1 201 ? 20.522  10.989  6.820   1.00 11.14  ? 201 PRO A C   1 
ATOM   1623 O  O   . PRO A  1 201 ? 20.032  11.572  5.881   1.00 12.49  ? 201 PRO A O   1 
ATOM   1624 C  CB  . PRO A  1 201 ? 22.162  12.831  7.346   1.00 12.83  ? 201 PRO A CB  1 
ATOM   1625 C  CG  . PRO A  1 201 ? 23.268  12.801  8.281   1.00 18.02  ? 201 PRO A CG  1 
ATOM   1626 C  CD  . PRO A  1 201 ? 23.279  11.379  8.938   1.00 13.05  ? 201 PRO A CD  1 
ATOM   1627 N  N   . CYS A  1 202 ? 20.527  9.657   6.902   1.00 10.49  ? 202 CYS A N   1 
ATOM   1628 C  CA  . CYS A  1 202 ? 19.852  8.788   5.957   1.00 10.50  ? 202 CYS A CA  1 
ATOM   1629 C  C   . CYS A  1 202 ? 20.421  8.853   4.572   1.00 10.16  ? 202 CYS A C   1 
ATOM   1630 O  O   . CYS A  1 202 ? 19.731  8.576   3.569   1.00 11.10  ? 202 CYS A O   1 
ATOM   1631 C  CB  . CYS A  1 202 ? 18.346  9.017   5.855   1.00 11.14  ? 202 CYS A CB  1 
ATOM   1632 S  SG  . CYS A  1 202 ? 17.441  8.949   7.464   1.00 11.03  ? 202 CYS A SG  1 
ATOM   1633 N  N   . ASN A  1 203 ? 21.733  9.224   4.448   1.00 11.22  ? 203 ASN A N   1 
ATOM   1634 C  CA  . ASN A  1 203 ? 22.267  9.328   3.127   1.00 12.07  ? 203 ASN A CA  1 
ATOM   1635 C  C   . ASN A  1 203 ? 22.174  8.071   2.338   1.00 11.28  ? 203 ASN A C   1 
ATOM   1636 O  O   . ASN A  1 203 ? 22.460  6.974   2.867   1.00 11.05  ? 203 ASN A O   1 
ATOM   1637 C  CB  . ASN A  1 203 ? 23.749  9.782   3.155   1.00 14.69  ? 203 ASN A CB  1 
ATOM   1638 C  CG  . ASN A  1 203 ? 23.890  10.981  4.073   1.00 16.34  ? 203 ASN A CG  1 
ATOM   1639 O  OD1 . ASN A  1 203 ? 23.928  10.836  5.292   1.00 20.26  ? 203 ASN A OD1 1 
ATOM   1640 N  ND2 . ASN A  1 203 ? 23.931  12.139  3.491   1.00 23.02  ? 203 ASN A ND2 1 
ATOM   1641 N  N   . PRO A  1 204 ? 21.863  8.133   1.030   1.00 11.41  ? 204 PRO A N   1 
ATOM   1642 C  CA  . PRO A  1 204 ? 21.685  6.950   0.172   1.00 11.42  ? 204 PRO A CA  1 
ATOM   1643 C  C   . PRO A  1 204 ? 22.981  6.417   -0.373  1.00 11.22  ? 204 PRO A C   1 
ATOM   1644 O  O   . PRO A  1 204 ? 23.162  6.235   -1.604  1.00 13.43  ? 204 PRO A O   1 
ATOM   1645 C  CB  . PRO A  1 204 ? 20.707  7.393   -0.904  1.00 13.62  ? 204 PRO A CB  1 
ATOM   1646 C  CG  . PRO A  1 204 ? 21.134  8.851   -1.093  1.00 16.01  ? 204 PRO A CG  1 
ATOM   1647 C  CD  . PRO A  1 204 ? 21.346  9.354   0.314   1.00 13.94  ? 204 PRO A CD  1 
ATOM   1648 N  N   . THR A  1 205 ? 23.965  6.154   0.514   1.00 12.03  ? 205 THR A N   1 
ATOM   1649 C  CA  . THR A  1 205 ? 25.353  5.967   0.130   1.00 11.67  ? 205 THR A CA  1 
ATOM   1650 C  C   . THR A  1 205 ? 25.904  4.610   0.667   1.00 11.34  ? 205 THR A C   1 
ATOM   1651 O  O   . THR A  1 205 ? 27.131  4.439   0.656   1.00 13.02  ? 205 THR A O   1 
ATOM   1652 C  CB  . THR A  1 205 ? 26.213  7.073   0.681   1.00 13.34  ? 205 THR A CB  1 
ATOM   1653 O  OG1 . THR A  1 205 ? 25.946  7.106   2.089   1.00 13.08  ? 205 THR A OG1 1 
ATOM   1654 C  CG2 . THR A  1 205 ? 25.774  8.419   0.055   1.00 14.45  ? 205 THR A CG2 1 
ATOM   1655 N  N   . VAL A  1 206 ? 25.003  3.689   1.070   1.00 10.91  ? 206 VAL A N   1 
ATOM   1656 C  CA  . VAL A  1 206 ? 25.460  2.423   1.687   1.00 11.43  ? 206 VAL A CA  1 
ATOM   1657 C  C   . VAL A  1 206 ? 25.301  1.254   0.798   1.00 11.15  ? 206 VAL A C   1 
ATOM   1658 O  O   . VAL A  1 206 ? 24.170  0.946   0.329   1.00 12.04  ? 206 VAL A O   1 
ATOM   1659 C  CB  . VAL A  1 206 ? 24.718  2.203   3.037   1.00 10.74  ? 206 VAL A CB  1 
ATOM   1660 C  CG1 . VAL A  1 206 ? 25.177  0.891   3.674   1.00 11.91  ? 206 VAL A CG1 1 
ATOM   1661 C  CG2 . VAL A  1 206 ? 24.956  3.357   3.988   1.00 11.74  ? 206 VAL A CG2 1 
ATOM   1662 N  N   . LEU A  1 207 ? 26.349  0.474   0.602   1.00 10.98  ? 207 LEU A N   1 
ATOM   1663 C  CA  . LEU A  1 207 ? 26.252  -0.850  0.055   1.00 11.90  ? 207 LEU A CA  1 
ATOM   1664 C  C   . LEU A  1 207 ? 26.028  -1.817  1.183   1.00 10.89  ? 207 LEU A C   1 
ATOM   1665 O  O   . LEU A  1 207 ? 26.919  -1.990  2.053   1.00 10.79  ? 207 LEU A O   1 
ATOM   1666 C  CB  . LEU A  1 207 ? 27.536  -1.165  -0.706  1.00 13.72  ? 207 LEU A CB  1 
ATOM   1667 C  CG  . LEU A  1 207 ? 27.468  -2.488  -1.555  1.00 15.92  ? 207 LEU A CG  1 
ATOM   1668 C  CD1 . LEU A  1 207 ? 26.309  -2.333  -2.694  1.00 21.13  ? 207 LEU A CD1 1 
ATOM   1669 C  CD2 . LEU A  1 207 ? 28.813  -2.727  -2.164  1.00 24.51  ? 207 LEU A CD2 1 
ATOM   1670 N  N   . TRP A  1 208 ? 24.837  -2.400  1.246   1.00 10.39  ? 208 TRP A N   1 
ATOM   1671 C  CA  . TRP A  1 208 ? 24.487  -3.313  2.362   1.00 9.71   ? 208 TRP A CA  1 
ATOM   1672 C  C   . TRP A  1 208 ? 24.849  -4.739  2.043   1.00 9.35   ? 208 TRP A C   1 
ATOM   1673 O  O   . TRP A  1 208 ? 24.563  -5.228  0.928   1.00 11.47  ? 208 TRP A O   1 
ATOM   1674 C  CB  . TRP A  1 208 ? 22.960  -3.241  2.609   1.00 10.54  ? 208 TRP A CB  1 
ATOM   1675 C  CG  . TRP A  1 208 ? 22.579  -2.042  3.390   1.00 9.36   ? 208 TRP A CG  1 
ATOM   1676 C  CD1 . TRP A  1 208 ? 22.129  -0.811  2.974   1.00 9.71   ? 208 TRP A CD1 1 
ATOM   1677 C  CD2 . TRP A  1 208 ? 22.719  -1.915  4.829   1.00 9.47   ? 208 TRP A CD2 1 
ATOM   1678 N  NE1 . TRP A  1 208 ? 21.992  0.062   3.998   1.00 10.09  ? 208 TRP A NE1 1 
ATOM   1679 C  CE2 . TRP A  1 208 ? 22.338  -0.579  5.169   1.00 9.55   ? 208 TRP A CE2 1 
ATOM   1680 C  CE3 . TRP A  1 208 ? 23.057  -2.795  5.866   1.00 9.46   ? 208 TRP A CE3 1 
ATOM   1681 C  CZ2 . TRP A  1 208 ? 22.340  -0.089  6.487   1.00 10.14  ? 208 TRP A CZ2 1 
ATOM   1682 C  CZ3 . TRP A  1 208 ? 23.053  -2.339  7.151   1.00 10.04  ? 208 TRP A CZ3 1 
ATOM   1683 C  CH2 . TRP A  1 208 ? 22.742  -0.999  7.483   1.00 10.29  ? 208 TRP A CH2 1 
ATOM   1684 N  N   . THR A  1 209 ? 25.407  -5.411  3.042   1.00 9.40   ? 209 THR A N   1 
ATOM   1685 C  CA  . THR A  1 209 ? 25.626  -6.867  3.017   1.00 10.33  ? 209 THR A CA  1 
ATOM   1686 C  C   . THR A  1 209 ? 25.000  -7.398  4.285   1.00 10.13  ? 209 THR A C   1 
ATOM   1687 O  O   . THR A  1 209 ? 25.459  -7.061  5.366   1.00 10.97  ? 209 THR A O   1 
ATOM   1688 C  CB  . THR A  1 209 ? 27.097  -7.239  2.942   1.00 10.72  ? 209 THR A CB  1 
ATOM   1689 O  OG1 . THR A  1 209 ? 27.665  -6.683  1.753   1.00 11.87  ? 209 THR A OG1 1 
ATOM   1690 C  CG2 . THR A  1 209 ? 27.307  -8.740  2.907   1.00 12.95  ? 209 THR A CG2 1 
ATOM   1691 N  N   . VAL A  1 210 ? 23.893  -8.165  4.139   1.00 9.92   ? 210 VAL A N   1 
ATOM   1692 C  CA  . VAL A  1 210 ? 23.216  -8.722  5.314   1.00 10.17  ? 210 VAL A CA  1 
ATOM   1693 C  C   . VAL A  1 210 ? 23.482  -10.218 5.288   1.00 9.58   ? 210 VAL A C   1 
ATOM   1694 O  O   . VAL A  1 210 ? 23.119  -10.886 4.305   1.00 10.79  ? 210 VAL A O   1 
ATOM   1695 C  CB  . VAL A  1 210 ? 21.697  -8.430  5.295   1.00 10.48  ? 210 VAL A CB  1 
ATOM   1696 C  CG1 . VAL A  1 210 ? 21.059  -9.058  6.544   1.00 11.11  ? 210 VAL A CG1 1 
ATOM   1697 C  CG2 . VAL A  1 210 ? 21.392  -6.957  5.189   1.00 11.24  ? 210 VAL A CG2 1 
ATOM   1698 N  N   . PHE A  1 211 ? 24.181  -10.741 6.260   1.00 9.95   ? 211 PHE A N   1 
ATOM   1699 C  CA  . PHE A  1 211 ? 24.467  -12.197 6.230   1.00 10.81  ? 211 PHE A CA  1 
ATOM   1700 C  C   . PHE A  1 211 ? 23.212  -12.997 6.352   1.00 10.72  ? 211 PHE A C   1 
ATOM   1701 O  O   . PHE A  1 211 ? 22.289  -12.693 7.094   1.00 11.58  ? 211 PHE A O   1 
ATOM   1702 C  CB  . PHE A  1 211 ? 25.488  -12.599 7.275   1.00 10.92  ? 211 PHE A CB  1 
ATOM   1703 C  CG  . PHE A  1 211 ? 26.827  -11.960 6.987   1.00 11.16  ? 211 PHE A CG  1 
ATOM   1704 C  CD1 . PHE A  1 211 ? 27.613  -12.378 5.919   1.00 12.26  ? 211 PHE A CD1 1 
ATOM   1705 C  CD2 . PHE A  1 211 ? 27.312  -10.898 7.803   1.00 11.87  ? 211 PHE A CD2 1 
ATOM   1706 C  CE1 . PHE A  1 211 ? 28.844  -11.759 5.608   1.00 14.49  ? 211 PHE A CE1 1 
ATOM   1707 C  CE2 . PHE A  1 211 ? 28.585  -10.321 7.514   1.00 12.96  ? 211 PHE A CE2 1 
ATOM   1708 C  CZ  . PHE A  1 211 ? 29.302  -10.711 6.406   1.00 14.15  ? 211 PHE A CZ  1 
ATOM   1709 N  N   . ARG A  1 212 ? 23.128  -14.117 5.602   1.00 11.40  ? 212 ARG A N   1 
ATOM   1710 C  CA  . ARG A  1 212 ? 21.939  -14.937 5.659   1.00 11.78  ? 212 ARG A CA  1 
ATOM   1711 C  C   . ARG A  1 212 ? 21.713  -15.580 7.010   1.00 11.79  ? 212 ARG A C   1 
ATOM   1712 O  O   . ARG A  1 212 ? 20.542  -15.676 7.437   1.00 13.34  ? 212 ARG A O   1 
ATOM   1713 C  CB  . ARG A  1 212 ? 22.075  -16.063 4.618   1.00 13.66  ? 212 ARG A CB  1 
ATOM   1714 C  CG  . ARG A  1 212 ? 20.839  -16.900 4.493   1.00 16.43  ? 212 ARG A CG  1 
ATOM   1715 C  CD  . ARG A  1 212 ? 21.108  -18.079 3.567   1.00 19.53  ? 212 ARG A CD  1 
ATOM   1716 N  NE  . ARG A  1 212 ? 19.834  -18.815 3.293   1.00 28.41  ? 212 ARG A NE  1 
ATOM   1717 C  CZ  . ARG A  1 212 ? 19.631  -19.716 2.338   1.00 34.99  ? 212 ARG A CZ  1 
ATOM   1718 N  NH1 . ARG A  1 212 ? 20.668  -20.178 1.674   1.00 31.69  ? 212 ARG A NH1 1 
ATOM   1719 N  NH2 . ARG A  1 212 ? 18.402  -20.195 2.118   1.00 44.94  ? 212 ARG A NH2 1 
ATOM   1720 N  N   . ASN A  1 213 ? 22.779  -16.031 7.640   1.00 12.48  ? 213 ASN A N   1 
ATOM   1721 C  CA  . ASN A  1 213 ? 22.575  -16.806 8.891   1.00 13.40  ? 213 ASN A CA  1 
ATOM   1722 C  C   . ASN A  1 213 ? 22.717  -15.901 10.080  1.00 13.66  ? 213 ASN A C   1 
ATOM   1723 O  O   . ASN A  1 213 ? 23.646  -15.104 10.153  1.00 12.75  ? 213 ASN A O   1 
ATOM   1724 C  CB  . ASN A  1 213 ? 23.650  -17.896 8.937   1.00 14.73  ? 213 ASN A CB  1 
ATOM   1725 C  CG  . ASN A  1 213 ? 23.524  -18.810 7.728   1.00 17.30  ? 213 ASN A CG  1 
ATOM   1726 O  OD1 . ASN A  1 213 ? 24.488  -18.966 6.966   1.00 21.58  ? 213 ASN A OD1 1 
ATOM   1727 N  ND2 . ASN A  1 213 ? 22.368  -19.252 7.440   1.00 18.91  ? 213 ASN A ND2 1 
ATOM   1728 N  N   . PRO A  1 214 ? 21.867  -16.048 11.116  1.00 12.26  ? 214 PRO A N   1 
ATOM   1729 C  CA  . PRO A  1 214 ? 21.987  -15.247 12.305  1.00 13.25  ? 214 PRO A CA  1 
ATOM   1730 C  C   . PRO A  1 214 ? 23.114  -15.792 13.267  1.00 11.80  ? 214 PRO A C   1 
ATOM   1731 O  O   . PRO A  1 214 ? 23.505  -16.974 13.113  1.00 14.49  ? 214 PRO A O   1 
ATOM   1732 C  CB  . PRO A  1 214 ? 20.580  -15.390 12.977  1.00 15.10  ? 214 PRO A CB  1 
ATOM   1733 C  CG  . PRO A  1 214 ? 20.233  -16.852 12.563  1.00 16.06  ? 214 PRO A CG  1 
ATOM   1734 C  CD  . PRO A  1 214 ? 20.665  -16.932 11.097  1.00 15.80  ? 214 PRO A CD  1 
ATOM   1735 N  N   . VAL A  1 215 ? 23.472  -15.008 14.243  1.00 12.05  ? 215 VAL A N   1 
ATOM   1736 C  CA  . VAL A  1 215 ? 24.210  -15.499 15.377  1.00 12.45  ? 215 VAL A CA  1 
ATOM   1737 C  C   . VAL A  1 215 ? 23.241  -15.615 16.556  1.00 11.88  ? 215 VAL A C   1 
ATOM   1738 O  O   . VAL A  1 215 ? 22.158  -15.032 16.533  1.00 12.93  ? 215 VAL A O   1 
ATOM   1739 C  CB  . VAL A  1 215 ? 25.371  -14.569 15.748  1.00 12.75  ? 215 VAL A CB  1 
ATOM   1740 C  CG1 . VAL A  1 215 ? 26.393  -14.473 14.629  1.00 15.28  ? 215 VAL A CG1 1 
ATOM   1741 C  CG2 . VAL A  1 215 ? 24.917  -13.184 16.183  1.00 13.25  ? 215 VAL A CG2 1 
ATOM   1742 N  N   A GLN A  1 216 ? 23.636  -16.433 17.553  0.50 13.11  ? 216 GLN A N   1 
ATOM   1743 N  N   B GLN A  1 216 ? 23.750  -16.196 17.642  0.50 12.65  ? 216 GLN A N   1 
ATOM   1744 C  CA  A GLN A  1 216 ? 22.988  -16.417 18.919  0.50 13.45  ? 216 GLN A CA  1 
ATOM   1745 C  CA  B GLN A  1 216 ? 22.908  -16.426 18.828  0.50 13.22  ? 216 GLN A CA  1 
ATOM   1746 C  C   A GLN A  1 216 ? 23.659  -15.755 20.023  0.50 13.33  ? 216 GLN A C   1 
ATOM   1747 C  C   B GLN A  1 216 ? 23.588  -15.862 20.005  0.50 13.63  ? 216 GLN A C   1 
ATOM   1748 O  O   A GLN A  1 216 ? 24.878  -15.792 20.130  0.50 15.04  ? 216 GLN A O   1 
ATOM   1749 O  O   B GLN A  1 216 ? 24.812  -15.981 20.073  0.50 14.82  ? 216 GLN A O   1 
ATOM   1750 C  CB  A GLN A  1 216 ? 22.795  -17.876 19.395  0.50 14.28  ? 216 GLN A CB  1 
ATOM   1751 C  CB  B GLN A  1 216 ? 22.682  -17.997 19.004  0.50 14.23  ? 216 GLN A CB  1 
ATOM   1752 C  CG  A GLN A  1 216 ? 21.953  -18.580 18.374  0.50 15.28  ? 216 GLN A CG  1 
ATOM   1753 C  CG  B GLN A  1 216 ? 21.802  -18.666 17.932  0.50 16.04  ? 216 GLN A CG  1 
ATOM   1754 C  CD  A GLN A  1 216 ? 21.636  -19.999 18.645  0.50 19.23  ? 216 GLN A CD  1 
ATOM   1755 C  CD  B GLN A  1 216 ? 22.605  -19.099 16.680  0.50 16.46  ? 216 GLN A CD  1 
ATOM   1756 O  OE1 A GLN A  1 216 ? 22.069  -20.580 19.599  0.50 19.71  ? 216 GLN A OE1 1 
ATOM   1757 O  OE1 B GLN A  1 216 ? 23.765  -19.494 16.794  0.50 18.08  ? 216 GLN A OE1 1 
ATOM   1758 N  NE2 A GLN A  1 216 ? 20.889  -20.559 17.816  0.50 26.68  ? 216 GLN A NE2 1 
ATOM   1759 N  NE2 B GLN A  1 216 ? 22.021  -19.011 15.433  0.50 18.60  ? 216 GLN A NE2 1 
ATOM   1760 N  N   . ILE A  1 217 ? 22.829  -15.175 20.891  1.00 13.01  ? 217 ILE A N   1 
ATOM   1761 C  CA  . ILE A  1 217 ? 23.316  -14.729 22.206  1.00 13.15  ? 217 ILE A CA  1 
ATOM   1762 C  C   . ILE A  1 217 ? 22.318  -15.236 23.232  1.00 13.90  ? 217 ILE A C   1 
ATOM   1763 O  O   . ILE A  1 217 ? 21.173  -15.549 22.872  1.00 13.61  ? 217 ILE A O   1 
ATOM   1764 C  CB  . ILE A  1 217 ? 23.454  -13.181 22.237  1.00 12.62  ? 217 ILE A CB  1 
ATOM   1765 C  CG1 . ILE A  1 217 ? 22.087  -12.416 22.092  1.00 13.28  ? 217 ILE A CG1 1 
ATOM   1766 C  CG2 . ILE A  1 217 ? 24.461  -12.735 21.193  1.00 14.56  ? 217 ILE A CG2 1 
ATOM   1767 C  CD1 . ILE A  1 217 ? 22.154  -10.924 22.275  1.00 13.65  ? 217 ILE A CD1 1 
ATOM   1768 N  N   . SER A  1 218 ? 22.725  -15.302 24.502  1.00 14.18  ? 218 SER A N   1 
ATOM   1769 C  CA  . SER A  1 218 ? 21.806  -15.935 25.461  1.00 15.05  ? 218 SER A CA  1 
ATOM   1770 C  C   . SER A  1 218 ? 20.661  -14.969 25.790  1.00 14.33  ? 218 SER A C   1 
ATOM   1771 O  O   . SER A  1 218 ? 20.695  -13.756 25.586  1.00 13.75  ? 218 SER A O   1 
ATOM   1772 C  CB  . SER A  1 218 ? 22.434  -16.342 26.738  1.00 16.58  ? 218 SER A CB  1 
ATOM   1773 O  OG  . SER A  1 218 ? 22.944  -15.146 27.407  1.00 16.29  ? 218 SER A OG  1 
ATOM   1774 N  N   . GLN A  1 219 ? 19.651  -15.536 26.451  1.00 17.05  ? 219 GLN A N   1 
ATOM   1775 C  CA  . GLN A  1 219 ? 18.539  -14.716 26.939  1.00 17.07  ? 219 GLN A CA  1 
ATOM   1776 C  C   . GLN A  1 219 ? 19.068  -13.626 27.907  1.00 16.44  ? 219 GLN A C   1 
ATOM   1777 O  O   . GLN A  1 219 ? 18.594  -12.497 27.830  1.00 15.70  ? 219 GLN A O   1 
ATOM   1778 C  CB  . GLN A  1 219 ? 17.585  -15.653 27.722  1.00 24.92  ? 219 GLN A CB  1 
ATOM   1779 C  CG  . GLN A  1 219 ? 17.712  -15.664 29.277  1.00 41.59  ? 219 GLN A CG  1 
ATOM   1780 C  CD  . GLN A  1 219 ? 16.715  -14.835 30.212  1.00 48.05  ? 219 GLN A CD  1 
ATOM   1781 O  OE1 . GLN A  1 219 ? 16.939  -13.702 30.848  1.00 23.48  ? 219 GLN A OE1 1 
ATOM   1782 N  NE2 . GLN A  1 219 ? 15.590  -15.495 30.396  1.00 56.47  ? 219 GLN A NE2 1 
ATOM   1783 N  N   . GLU A  1 220 ? 20.017  -13.927 28.757  1.00 15.81  ? 220 GLU A N   1 
ATOM   1784 C  CA  . GLU A  1 220 ? 20.575  -12.989 29.686  1.00 17.00  ? 220 GLU A CA  1 
ATOM   1785 C  C   . GLU A  1 220 ? 21.360  -11.907 28.877  1.00 14.37  ? 220 GLU A C   1 
ATOM   1786 O  O   . GLU A  1 220 ? 21.244  -10.743 29.249  1.00 15.10  ? 220 GLU A O   1 
ATOM   1787 C  CB  . GLU A  1 220 ? 21.444  -13.576 30.745  1.00 18.04  ? 220 GLU A CB  1 
ATOM   1788 C  CG  . GLU A  1 220 ? 20.716  -14.549 31.673  1.00 24.78  ? 220 GLU A CG  1 
ATOM   1789 C  CD  . GLU A  1 220 ? 20.431  -15.911 31.050  1.00 30.18  ? 220 GLU A CD  1 
ATOM   1790 O  OE1 . GLU A  1 220 ? 21.014  -16.236 29.993  1.00 26.46  ? 220 GLU A OE1 1 
ATOM   1791 O  OE2 . GLU A  1 220 ? 19.620  -16.667 31.628  1.00 37.46  ? 220 GLU A OE2 1 
ATOM   1792 N  N   . GLN A  1 221 ? 22.114  -12.296 27.845  1.00 14.83  ? 221 GLN A N   1 
ATOM   1793 C  CA  . GLN A  1 221 ? 22.859  -11.270 27.076  1.00 13.66  ? 221 GLN A CA  1 
ATOM   1794 C  C   . GLN A  1 221 ? 21.892  -10.330 26.393  1.00 13.60  ? 221 GLN A C   1 
ATOM   1795 O  O   . GLN A  1 221 ? 22.116  -9.091  26.387  1.00 13.21  ? 221 GLN A O   1 
ATOM   1796 C  CB  . GLN A  1 221 ? 23.714  -11.924 26.054  1.00 13.17  ? 221 GLN A CB  1 
ATOM   1797 C  CG  . GLN A  1 221 ? 24.939  -12.687 26.690  1.00 15.03  ? 221 GLN A CG  1 
ATOM   1798 C  CD  . GLN A  1 221 ? 25.785  -13.285 25.588  1.00 14.15  ? 221 GLN A CD  1 
ATOM   1799 O  OE1 . GLN A  1 221 ? 25.374  -14.220 24.952  1.00 14.76  ? 221 GLN A OE1 1 
ATOM   1800 N  NE2 . GLN A  1 221 ? 27.035  -12.811 25.438  1.00 15.68  ? 221 GLN A NE2 1 
ATOM   1801 N  N   . LEU A  1 222 ? 20.848  -10.838 25.802  1.00 12.47  ? 222 LEU A N   1 
ATOM   1802 C  CA  . LEU A  1 222 ? 19.867  -9.978  25.075  1.00 12.71  ? 222 LEU A CA  1 
ATOM   1803 C  C   . LEU A  1 222 ? 19.198  -9.049  26.054  1.00 13.64  ? 222 LEU A C   1 
ATOM   1804 O  O   . LEU A  1 222 ? 19.044  -7.853  25.815  1.00 12.87  ? 222 LEU A O   1 
ATOM   1805 C  CB  . LEU A  1 222 ? 18.870  -10.873 24.338  1.00 13.21  ? 222 LEU A CB  1 
ATOM   1806 C  CG  . LEU A  1 222 ? 17.770  -10.082 23.661  1.00 13.09  ? 222 LEU A CG  1 
ATOM   1807 C  CD1 . LEU A  1 222 ? 18.308  -9.161  22.518  1.00 13.78  ? 222 LEU A CD1 1 
ATOM   1808 C  CD2 . LEU A  1 222 ? 16.771  -11.077 23.068  1.00 15.77  ? 222 LEU A CD2 1 
ATOM   1809 N  N   . LEU A  1 223 ? 18.846  -9.568  27.272  1.00 13.85  ? 223 LEU A N   1 
ATOM   1810 C  CA  . LEU A  1 223 ? 18.178  -8.710  28.241  1.00 13.95  ? 223 LEU A CA  1 
ATOM   1811 C  C   . LEU A  1 223 ? 19.168  -7.631  28.699  1.00 13.64  ? 223 LEU A C   1 
ATOM   1812 O  O   . LEU A  1 223 ? 18.730  -6.506  28.933  1.00 14.74  ? 223 LEU A O   1 
ATOM   1813 C  CB  . LEU A  1 223 ? 17.740  -9.579  29.407  1.00 15.43  ? 223 LEU A CB  1 
ATOM   1814 C  CG  . LEU A  1 223 ? 17.048  -8.873  30.561  1.00 18.02  ? 223 LEU A CG  1 
ATOM   1815 C  CD1 . LEU A  1 223 ? 15.706  -8.300  30.033  1.00 17.82  ? 223 LEU A CD1 1 
ATOM   1816 C  CD2 . LEU A  1 223 ? 16.758  -9.878  31.660  1.00 21.34  ? 223 LEU A CD2 1 
ATOM   1817 N  N   . ALA A  1 224 ? 20.479  -7.972  28.874  1.00 14.36  ? 224 ALA A N   1 
ATOM   1818 C  CA  . ALA A  1 224 ? 21.447  -6.944  29.299  1.00 16.77  ? 224 ALA A CA  1 
ATOM   1819 C  C   . ALA A  1 224 ? 21.518  -5.849  28.211  1.00 15.71  ? 224 ALA A C   1 
ATOM   1820 O  O   . ALA A  1 224 ? 21.465  -4.625  28.519  1.00 17.35  ? 224 ALA A O   1 
ATOM   1821 C  CB  . ALA A  1 224 ? 22.816  -7.537  29.508  1.00 18.89  ? 224 ALA A CB  1 
ATOM   1822 N  N   . LEU A  1 225 ? 21.535  -6.226  26.948  1.00 14.52  ? 225 LEU A N   1 
ATOM   1823 C  CA  . LEU A  1 225 ? 21.611  -5.209  25.903  1.00 14.30  ? 225 LEU A CA  1 
ATOM   1824 C  C   . LEU A  1 225 ? 20.368  -4.331  25.923  1.00 14.47  ? 225 LEU A C   1 
ATOM   1825 O  O   . LEU A  1 225 ? 20.482  -3.084  25.780  1.00 15.75  ? 225 LEU A O   1 
ATOM   1826 C  CB  . LEU A  1 225 ? 21.739  -5.931  24.557  1.00 12.98  ? 225 LEU A CB  1 
ATOM   1827 C  CG  . LEU A  1 225 ? 21.832  -4.950  23.370  1.00 14.24  ? 225 LEU A CG  1 
ATOM   1828 C  CD1 . LEU A  1 225 ? 23.077  -4.035  23.455  1.00 15.67  ? 225 LEU A CD1 1 
ATOM   1829 C  CD2 . LEU A  1 225 ? 21.821  -5.775  22.097  1.00 15.21  ? 225 LEU A CD2 1 
ATOM   1830 N  N   . GLU A  1 226 ? 19.191  -4.945  26.158  1.00 12.81  ? 226 GLU A N   1 
ATOM   1831 C  CA  . GLU A  1 226 ? 17.970  -4.179  26.143  1.00 13.67  ? 226 GLU A CA  1 
ATOM   1832 C  C   . GLU A  1 226 ? 17.759  -3.279  27.362  1.00 14.65  ? 226 GLU A C   1 
ATOM   1833 O  O   . GLU A  1 226 ? 16.891  -2.417  27.314  1.00 17.21  ? 226 GLU A O   1 
ATOM   1834 C  CB  . GLU A  1 226 ? 16.784  -5.158  26.059  1.00 13.12  ? 226 GLU A CB  1 
ATOM   1835 C  CG  . GLU A  1 226 ? 16.640  -5.927  24.772  1.00 13.37  ? 226 GLU A CG  1 
ATOM   1836 C  CD  . GLU A  1 226 ? 15.748  -7.111  24.843  1.00 13.47  ? 226 GLU A CD  1 
ATOM   1837 O  OE1 . GLU A  1 226 ? 15.526  -7.624  26.011  1.00 14.82  ? 226 GLU A OE1 1 
ATOM   1838 O  OE2 . GLU A  1 226 ? 15.272  -7.563  23.808  1.00 14.40  ? 226 GLU A OE2 1 
ATOM   1839 N  N   . THR A  1 227 ? 18.474  -3.555  28.474  1.00 14.23  ? 227 THR A N   1 
ATOM   1840 C  CA  . THR A  1 227 ? 18.132  -2.844  29.727  1.00 16.61  ? 227 THR A CA  1 
ATOM   1841 C  C   . THR A  1 227 ? 19.354  -2.091  30.282  1.00 16.23  ? 227 THR A C   1 
ATOM   1842 O  O   . THR A  1 227 ? 19.206  -1.415  31.306  1.00 19.87  ? 227 THR A O   1 
ATOM   1843 C  CB  . THR A  1 227 ? 17.670  -3.904  30.826  1.00 16.94  ? 227 THR A CB  1 
ATOM   1844 O  OG1 . THR A  1 227 ? 18.680  -4.859  31.066  1.00 18.21  ? 227 THR A OG1 1 
ATOM   1845 C  CG2 . THR A  1 227 ? 16.389  -4.531  30.363  1.00 21.14  ? 227 THR A CG2 1 
ATOM   1846 N  N   . ALA A  1 228 ? 20.550  -2.181  29.673  1.00 15.41  ? 228 ALA A N   1 
ATOM   1847 C  CA  . ALA A  1 228 ? 21.737  -1.580  30.277  1.00 16.05  ? 228 ALA A CA  1 
ATOM   1848 C  C   . ALA A  1 228 ? 21.828  -0.098  30.029  1.00 16.81  ? 228 ALA A C   1 
ATOM   1849 O  O   . ALA A  1 228 ? 22.495  0.586   30.823  1.00 18.91  ? 228 ALA A O   1 
ATOM   1850 C  CB  . ALA A  1 228 ? 23.006  -2.269  29.708  1.00 22.33  ? 228 ALA A CB  1 
ATOM   1851 N  N   . LEU A  1 229 ? 21.229  0.435   28.956  1.00 14.96  ? 229 LEU A N   1 
ATOM   1852 C  CA  . LEU A  1 229 ? 21.578  1.782   28.507  1.00 15.39  ? 229 LEU A CA  1 
ATOM   1853 C  C   . LEU A  1 229 ? 20.460  2.738   28.557  1.00 14.65  ? 229 LEU A C   1 
ATOM   1854 O  O   . LEU A  1 229 ? 19.297  2.349   28.389  1.00 15.80  ? 229 LEU A O   1 
ATOM   1855 C  CB  . LEU A  1 229 ? 22.121  1.727   27.060  1.00 15.92  ? 229 LEU A CB  1 
ATOM   1856 C  CG  . LEU A  1 229 ? 23.246  0.653   26.838  1.00 16.44  ? 229 LEU A CG  1 
ATOM   1857 C  CD1 . LEU A  1 229 ? 23.646  0.744   25.360  1.00 20.47  ? 229 LEU A CD1 1 
ATOM   1858 C  CD2 . LEU A  1 229 ? 24.431  0.918   27.748  1.00 18.86  ? 229 LEU A CD2 1 
ATOM   1859 N  N   . TYR A  1 230 ? 20.778  4.018   28.679  1.00 16.51  ? 230 TYR A N   1 
ATOM   1860 C  CA  . TYR A  1 230 ? 19.816  5.050   28.697  1.00 17.01  ? 230 TYR A CA  1 
ATOM   1861 C  C   . TYR A  1 230 ? 20.178  6.035   27.513  1.00 17.12  ? 230 TYR A C   1 
ATOM   1862 O  O   . TYR A  1 230 ? 21.379  6.242   27.164  1.00 18.48  ? 230 TYR A O   1 
ATOM   1863 C  CB  . TYR A  1 230 ? 19.908  5.852   29.961  1.00 17.95  ? 230 TYR A CB  1 
ATOM   1864 C  CG  . TYR A  1 230 ? 19.353  5.170   31.175  1.00 20.09  ? 230 TYR A CG  1 
ATOM   1865 C  CD1 . TYR A  1 230 ? 20.013  4.098   31.769  1.00 27.54  ? 230 TYR A CD1 1 
ATOM   1866 C  CD2 . TYR A  1 230 ? 18.180  5.621   31.752  1.00 24.54  ? 230 TYR A CD2 1 
ATOM   1867 C  CE1 . TYR A  1 230 ? 19.501  3.490   32.909  1.00 34.80  ? 230 TYR A CE1 1 
ATOM   1868 C  CE2 . TYR A  1 230 ? 17.659  5.024   32.888  1.00 27.75  ? 230 TYR A CE2 1 
ATOM   1869 C  CZ  . TYR A  1 230 ? 18.313  3.962   33.469  1.00 33.61  ? 230 TYR A CZ  1 
ATOM   1870 O  OH  . TYR A  1 230 ? 17.757  3.394   34.605  1.00 41.91  ? 230 TYR A OH  1 
ATOM   1871 N  N   . CYS A  1 231 ? 19.167  6.666   26.886  1.00 18.60  ? 231 CYS A N   1 
ATOM   1872 C  CA  . CYS A  1 231 ? 19.555  7.566   25.829  1.00 18.31  ? 231 CYS A CA  1 
ATOM   1873 C  C   . CYS A  1 231 ? 19.770  9.023   26.327  1.00 18.06  ? 231 CYS A C   1 
ATOM   1874 O  O   . CYS A  1 231 ? 20.122  9.905   25.595  1.00 20.54  ? 231 CYS A O   1 
ATOM   1875 C  CB  . CYS A  1 231 ? 18.554  7.527   24.667  1.00 25.24  ? 231 CYS A CB  1 
ATOM   1876 S  SG  . CYS A  1 231 ? 16.816  7.581   25.153  1.00 38.08  ? 231 CYS A SG  1 
ATOM   1877 N  N   . THR A  1 232 ? 19.540  9.201   27.621  1.00 18.42  ? 232 THR A N   1 
ATOM   1878 C  CA  . THR A  1 232 ? 19.679  10.471  28.286  1.00 18.40  ? 232 THR A CA  1 
ATOM   1879 C  C   . THR A  1 232 ? 21.072  10.552  29.042  1.00 17.27  ? 232 THR A C   1 
ATOM   1880 O  O   . THR A  1 232 ? 21.669  9.604   29.407  1.00 19.09  ? 232 THR A O   1 
ATOM   1881 C  CB  . THR A  1 232 ? 18.519  10.680  29.272  1.00 20.71  ? 232 THR A CB  1 
ATOM   1882 O  OG1 . THR A  1 232 ? 18.236  9.476   29.998  1.00 20.04  ? 232 THR A OG1 1 
ATOM   1883 C  CG2 . THR A  1 232 ? 17.177  11.083  28.588  1.00 21.54  ? 232 THR A CG2 1 
ATOM   1884 N  N   . HIS A  1 233 ? 21.484  11.795  29.292  1.00 19.18  ? 233 HIS A N   1 
ATOM   1885 C  CA  . HIS A  1 233 ? 22.678  12.076  30.084  1.00 19.12  ? 233 HIS A CA  1 
ATOM   1886 C  C   . HIS A  1 233 ? 22.367  11.727  31.566  1.00 18.95  ? 233 HIS A C   1 
ATOM   1887 O  O   . HIS A  1 233 ? 21.201  11.704  32.029  1.00 18.65  ? 233 HIS A O   1 
ATOM   1888 C  CB  . HIS A  1 233 ? 23.060  13.546  30.041  1.00 21.14  ? 233 HIS A CB  1 
ATOM   1889 C  CG  . HIS A  1 233 ? 23.685  13.976  28.713  1.00 29.59  ? 233 HIS A CG  1 
ATOM   1890 N  ND1 . HIS A  1 233 ? 23.060  14.828  27.784  1.00 38.94  ? 233 HIS A ND1 1 
ATOM   1891 C  CD2 . HIS A  1 233 ? 24.920  13.736  28.201  1.00 30.33  ? 233 HIS A CD2 1 
ATOM   1892 C  CE1 . HIS A  1 233 ? 23.864  15.045  26.761  1.00 36.72  ? 233 HIS A CE1 1 
ATOM   1893 N  NE2 . HIS A  1 233 ? 24.972  14.339  26.960  1.00 33.75  ? 233 HIS A NE2 1 
ATOM   1894 N  N   . MET A  1 234 ? 23.432  11.410  32.277  1.00 21.17  ? 234 MET A N   1 
ATOM   1895 C  CA  . MET A  1 234 ? 23.287  10.900  33.630  1.00 21.71  ? 234 MET A CA  1 
ATOM   1896 C  C   . MET A  1 234 ? 22.483  11.820  34.508  1.00 21.42  ? 234 MET A C   1 
ATOM   1897 O  O   . MET A  1 234 ? 21.746  11.307  35.352  1.00 22.76  ? 234 MET A O   1 
ATOM   1898 C  CB  . MET A  1 234 ? 24.636  10.676  34.271  1.00 23.25  ? 234 MET A CB  1 
ATOM   1899 C  CG  . MET A  1 234 ? 24.658  10.031  35.613  1.00 23.49  ? 234 MET A CG  1 
ATOM   1900 S  SD  . MET A  1 234 ? 26.342  9.730   36.145  1.00 36.45  ? 234 MET A SD  1 
ATOM   1901 C  CE  . MET A  1 234 ? 27.060  11.364  35.853  1.00 42.49  ? 234 MET A CE  1 
ATOM   1902 N  N   . ASP A  1 235 ? 22.645  13.139  34.369  1.00 23.76  ? 235 ASP A N   1 
ATOM   1903 C  CA  . ASP A  1 235 ? 21.984  14.006  35.383  1.00 27.98  ? 235 ASP A CA  1 
ATOM   1904 C  C   . ASP A  1 235 ? 20.670  14.537  34.795  1.00 27.77  ? 235 ASP A C   1 
ATOM   1905 O  O   . ASP A  1 235 ? 20.068  15.385  35.376  1.00 29.12  ? 235 ASP A O   1 
ATOM   1906 C  CB  . ASP A  1 235 ? 22.894  15.145  35.857  1.00 36.78  ? 235 ASP A CB  1 
ATOM   1907 C  CG  . ASP A  1 235 ? 23.287  16.034  34.697  1.00 61.75  ? 235 ASP A CG  1 
ATOM   1908 O  OD1 . ASP A  1 235 ? 22.642  15.906  33.580  1.00 55.40  ? 235 ASP A OD1 1 
ATOM   1909 O  OD2 . ASP A  1 235 ? 24.229  16.834  34.900  1.00 85.82  ? 235 ASP A OD2 1 
ATOM   1910 N  N   . ASP A  1 236 ? 20.124  13.940  33.732  1.00 23.91  ? 236 ASP A N   1 
ATOM   1911 C  CA  . ASP A  1 236 ? 18.794  14.340  33.227  1.00 22.64  ? 236 ASP A CA  1 
ATOM   1912 C  C   . ASP A  1 236 ? 17.787  13.975  34.306  1.00 22.85  ? 236 ASP A C   1 
ATOM   1913 O  O   . ASP A  1 236 ? 17.679  12.789  34.692  1.00 25.33  ? 236 ASP A O   1 
ATOM   1914 C  CB  . ASP A  1 236 ? 18.535  13.590  31.935  1.00 24.23  ? 236 ASP A CB  1 
ATOM   1915 C  CG  . ASP A  1 236 ? 17.350  14.154  31.159  1.00 25.38  ? 236 ASP A CG  1 
ATOM   1916 O  OD1 . ASP A  1 236 ? 16.358  14.552  31.792  1.00 31.49  ? 236 ASP A OD1 1 
ATOM   1917 O  OD2 . ASP A  1 236 ? 17.453  14.248  29.894  1.00 27.40  ? 236 ASP A OD2 1 
ATOM   1918 N  N   . PRO A  1 237 ? 16.937  14.921  34.716  1.00 24.40  ? 237 PRO A N   1 
ATOM   1919 C  CA  . PRO A  1 237 ? 15.990  14.514  35.693  1.00 26.63  ? 237 PRO A CA  1 
ATOM   1920 C  C   . PRO A  1 237 ? 14.810  13.663  35.145  1.00 26.78  ? 237 PRO A C   1 
ATOM   1921 O  O   . PRO A  1 237 ? 13.991  13.209  35.960  1.00 28.76  ? 237 PRO A O   1 
ATOM   1922 C  CB  . PRO A  1 237 ? 15.421  15.899  36.205  1.00 32.61  ? 237 PRO A CB  1 
ATOM   1923 C  CG  . PRO A  1 237 ? 15.636  16.832  35.126  1.00 36.20  ? 237 PRO A CG  1 
ATOM   1924 C  CD  . PRO A  1 237 ? 16.858  16.371  34.375  1.00 29.90  ? 237 PRO A CD  1 
ATOM   1925 N  N   . SER A  1 238 ? 14.716  13.459  33.798  1.00 24.90  ? 238 SER A N   1 
ATOM   1926 C  CA  . SER A  1 238 ? 13.633  12.620  33.170  1.00 24.17  ? 238 SER A CA  1 
ATOM   1927 C  C   . SER A  1 238 ? 14.361  11.533  32.338  1.00 25.86  ? 238 SER A C   1 
ATOM   1928 O  O   . SER A  1 238 ? 14.453  11.703  31.110  1.00 25.55  ? 238 SER A O   1 
ATOM   1929 C  CB  . SER A  1 238 ? 12.710  13.495  32.308  1.00 31.23  ? 238 SER A CB  1 
ATOM   1930 O  OG  . SER A  1 238 ? 12.115  14.340  33.223  1.00 39.53  ? 238 SER A OG  1 
ATOM   1931 N  N   . PRO A  1 239 ? 14.928  10.477  32.982  1.00 22.76  ? 239 PRO A N   1 
ATOM   1932 C  CA  . PRO A  1 239 ? 15.747  9.496   32.243  1.00 22.27  ? 239 PRO A CA  1 
ATOM   1933 C  C   . PRO A  1 239 ? 14.890  8.709   31.291  1.00 22.44  ? 239 PRO A C   1 
ATOM   1934 O  O   . PRO A  1 239 ? 13.649  8.503   31.543  1.00 24.69  ? 239 PRO A O   1 
ATOM   1935 C  CB  . PRO A  1 239 ? 16.272  8.594   33.375  1.00 24.50  ? 239 PRO A CB  1 
ATOM   1936 C  CG  . PRO A  1 239 ? 15.335  8.866   34.564  1.00 28.48  ? 239 PRO A CG  1 
ATOM   1937 C  CD  . PRO A  1 239 ? 14.951  10.292  34.455  1.00 25.88  ? 239 PRO A CD  1 
ATOM   1938 N  N   . ARG A  1 240 ? 15.485  8.267   30.197  1.00 21.83  ? 240 ARG A N   1 
ATOM   1939 C  CA  . ARG A  1 240 ? 14.759  7.439   29.175  1.00 21.21  ? 240 ARG A CA  1 
ATOM   1940 C  C   . ARG A  1 240 ? 15.667  6.271   28.840  1.00 19.40  ? 240 ARG A C   1 
ATOM   1941 O  O   . ARG A  1 240 ? 16.872  6.401   28.539  1.00 21.48  ? 240 ARG A O   1 
ATOM   1942 C  CB  . ARG A  1 240 ? 14.298  8.103   27.844  1.00 33.27  ? 240 ARG A CB  1 
ATOM   1943 C  CG  . ARG A  1 240 ? 13.472  9.425   27.984  1.00 46.89  ? 240 ARG A CG  1 
ATOM   1944 C  CD  . ARG A  1 240 ? 13.158  10.162  26.655  1.00 66.92  ? 240 ARG A CD  1 
ATOM   1945 N  NE  . ARG A  1 240 ? 14.203  11.084  26.127  1.00 59.65  ? 240 ARG A NE  1 
ATOM   1946 C  CZ  . ARG A  1 240 ? 15.011  10.826  25.072  1.00 59.40  ? 240 ARG A CZ  1 
ATOM   1947 N  NH1 . ARG A  1 240 ? 14.938  9.668   24.415  1.00 102.90 ? 240 ARG A NH1 1 
ATOM   1948 N  NH2 . ARG A  1 240 ? 15.912  11.716  24.664  1.00 57.47  ? 240 ARG A NH2 1 
ATOM   1949 N  N   . GLU A  1 241 ? 15.146  5.070   28.950  1.00 18.29  ? 241 GLU A N   1 
ATOM   1950 C  CA  . GLU A  1 241 ? 15.861  3.847   28.647  1.00 18.94  ? 241 GLU A CA  1 
ATOM   1951 C  C   . GLU A  1 241 ? 16.036  3.797   27.111  1.00 18.93  ? 241 GLU A C   1 
ATOM   1952 O  O   . GLU A  1 241 ? 15.097  4.087   26.362  1.00 21.42  ? 241 GLU A O   1 
ATOM   1953 C  CB  . GLU A  1 241 ? 14.995  2.634   29.036  1.00 24.48  ? 241 GLU A CB  1 
ATOM   1954 C  CG  . GLU A  1 241 ? 14.751  2.487   30.548  1.00 31.76  ? 241 GLU A CG  1 
ATOM   1955 C  CD  . GLU A  1 241 ? 13.807  1.296   30.847  1.00 43.89  ? 241 GLU A CD  1 
ATOM   1956 O  OE1 . GLU A  1 241 ? 13.320  0.606   29.900  1.00 65.54  ? 241 GLU A OE1 1 
ATOM   1957 O  OE2 . GLU A  1 241 ? 13.565  1.002   32.020  1.00 49.90  ? 241 GLU A OE2 1 
ATOM   1958 N  N   . MET A  1 242 ? 17.195  3.255   26.672  1.00 15.74  ? 242 MET A N   1 
ATOM   1959 C  CA  . MET A  1 242 ? 17.481  3.123   25.254  1.00 14.80  ? 242 MET A CA  1 
ATOM   1960 C  C   . MET A  1 242 ? 16.978  1.766   24.823  1.00 12.71  ? 242 MET A C   1 
ATOM   1961 O  O   . MET A  1 242 ? 17.590  0.701   25.048  1.00 14.10  ? 242 MET A O   1 
ATOM   1962 C  CB  . MET A  1 242 ? 19.019  3.192   25.018  1.00 14.59  ? 242 MET A CB  1 
ATOM   1963 C  CG  . MET A  1 242 ? 19.349  3.160   23.561  1.00 14.46  ? 242 MET A CG  1 
ATOM   1964 S  SD  . MET A  1 242 ? 21.131  3.148   23.234  1.00 16.18  ? 242 MET A SD  1 
ATOM   1965 C  CE  . MET A  1 242 ? 21.604  4.777   23.795  1.00 18.03  ? 242 MET A CE  1 
ATOM   1966 N  N   . ILE A  1 243 ? 15.821  1.781   24.163  1.00 12.59  ? 243 ILE A N   1 
ATOM   1967 C  CA  . ILE A  1 243 ? 15.107  0.632   23.676  1.00 11.77  ? 243 ILE A CA  1 
ATOM   1968 C  C   . ILE A  1 243 ? 14.535  0.917   22.293  1.00 12.03  ? 243 ILE A C   1 
ATOM   1969 O  O   . ILE A  1 243 ? 14.350  2.122   21.973  1.00 12.24  ? 243 ILE A O   1 
ATOM   1970 C  CB  . ILE A  1 243 ? 13.926  0.188   24.589  1.00 13.38  ? 243 ILE A CB  1 
ATOM   1971 C  CG1 . ILE A  1 243 ? 12.978  1.325   24.917  1.00 15.75  ? 243 ILE A CG1 1 
ATOM   1972 C  CG2 . ILE A  1 243 ? 14.525  -0.389  25.898  1.00 16.43  ? 243 ILE A CG2 1 
ATOM   1973 C  CD1 . ILE A  1 243 ? 11.748  0.877   25.748  1.00 19.33  ? 243 ILE A CD1 1 
ATOM   1974 N  N   . ASN A  1 244 ? 14.186  -0.126  21.543  1.00 11.36  ? 244 ASN A N   1 
ATOM   1975 C  CA  . ASN A  1 244 ? 13.469  0.065   20.274  1.00 10.70  ? 244 ASN A CA  1 
ATOM   1976 C  C   . ASN A  1 244 ? 14.206  1.067   19.359  1.00 11.05  ? 244 ASN A C   1 
ATOM   1977 O  O   . ASN A  1 244 ? 13.562  1.893   18.680  1.00 11.64  ? 244 ASN A O   1 
ATOM   1978 C  CB  . ASN A  1 244 ? 12.046  0.512   20.490  1.00 13.03  ? 244 ASN A CB  1 
ATOM   1979 C  CG  . ASN A  1 244 ? 11.305  -0.445  21.422  1.00 13.45  ? 244 ASN A CG  1 
ATOM   1980 O  OD1 . ASN A  1 244 ? 11.510  -1.651  21.365  1.00 15.11  ? 244 ASN A OD1 1 
ATOM   1981 N  ND2 . ASN A  1 244 ? 10.423  0.119   22.306  1.00 18.08  ? 244 ASN A ND2 1 
ATOM   1982 N  N   . ASN A  1 245 ? 15.532  0.951   19.260  1.00 10.40  ? 245 ASN A N   1 
ATOM   1983 C  CA  . ASN A  1 245 ? 16.349  1.896   18.499  1.00 10.04  ? 245 ASN A CA  1 
ATOM   1984 C  C   . ASN A  1 245 ? 16.564  1.335   17.096  1.00 9.62   ? 245 ASN A C   1 
ATOM   1985 O  O   . ASN A  1 245 ? 17.711  1.241   16.642  1.00 11.17  ? 245 ASN A O   1 
ATOM   1986 C  CB  . ASN A  1 245 ? 17.634  2.227   19.223  1.00 11.06  ? 245 ASN A CB  1 
ATOM   1987 C  CG  . ASN A  1 245 ? 18.496  1.054   19.502  1.00 9.83   ? 245 ASN A CG  1 
ATOM   1988 O  OD1 . ASN A  1 245 ? 18.067  -0.114  19.491  1.00 11.56  ? 245 ASN A OD1 1 
ATOM   1989 N  ND2 . ASN A  1 245 ? 19.763  1.295   19.738  1.00 12.48  ? 245 ASN A ND2 1 
ATOM   1990 N  N   . PHE A  1 246 ? 15.503  0.994   16.411  1.00 9.82   ? 246 PHE A N   1 
ATOM   1991 C  CA  . PHE A  1 246 ? 15.543  0.490   15.032  1.00 9.98   ? 246 PHE A CA  1 
ATOM   1992 C  C   . PHE A  1 246 ? 14.572  1.303   14.228  1.00 9.09   ? 246 PHE A C   1 
ATOM   1993 O  O   . PHE A  1 246 ? 13.536  1.748   14.752  1.00 10.33  ? 246 PHE A O   1 
ATOM   1994 C  CB  . PHE A  1 246 ? 15.185  -1.018  14.981  1.00 11.33  ? 246 PHE A CB  1 
ATOM   1995 C  CG  . PHE A  1 246 ? 13.819  -1.387  15.495  1.00 10.31  ? 246 PHE A CG  1 
ATOM   1996 C  CD1 . PHE A  1 246 ? 13.611  -1.587  16.834  1.00 11.15  ? 246 PHE A CD1 1 
ATOM   1997 C  CD2 . PHE A  1 246 ? 12.738  -1.462  14.650  1.00 12.13  ? 246 PHE A CD2 1 
ATOM   1998 C  CE1 . PHE A  1 246 ? 12.299  -1.899  17.345  1.00 11.78  ? 246 PHE A CE1 1 
ATOM   1999 C  CE2 . PHE A  1 246 ? 11.474  -1.769  15.102  1.00 13.49  ? 246 PHE A CE2 1 
ATOM   2000 C  CZ  . PHE A  1 246 ? 11.241  -2.017  16.460  1.00 11.82  ? 246 PHE A CZ  1 
ATOM   2001 N  N   . ARG A  1 247 ? 14.837  1.444   12.954  1.00 9.36   ? 247 ARG A N   1 
ATOM   2002 C  CA  . ARG A  1 247 ? 13.900  2.138   12.023  1.00 9.10   ? 247 ARG A CA  1 
ATOM   2003 C  C   . ARG A  1 247 ? 12.957  1.067   11.489  1.00 9.01   ? 247 ARG A C   1 
ATOM   2004 O  O   . ARG A  1 247 ? 13.350  -0.046  11.195  1.00 9.69   ? 247 ARG A O   1 
ATOM   2005 C  CB  . ARG A  1 247 ? 14.695  2.768   10.892  1.00 9.67   ? 247 ARG A CB  1 
ATOM   2006 C  CG  . ARG A  1 247 ? 13.927  3.795   10.051  1.00 9.51   ? 247 ARG A CG  1 
ATOM   2007 C  CD  . ARG A  1 247 ? 14.744  4.257   8.891   1.00 9.62   ? 247 ARG A CD  1 
ATOM   2008 N  NE  . ARG A  1 247 ? 14.118  5.422   8.245   1.00 9.50   ? 247 ARG A NE  1 
ATOM   2009 C  CZ  . ARG A  1 247 ? 14.615  5.994   7.137   1.00 9.72   ? 247 ARG A CZ  1 
ATOM   2010 N  NH1 . ARG A  1 247 ? 15.627  5.461   6.483   1.00 10.67  ? 247 ARG A NH1 1 
ATOM   2011 N  NH2 . ARG A  1 247 ? 14.064  7.122   6.688   1.00 10.64  ? 247 ARG A NH2 1 
ATOM   2012 N  N   . GLN A  1 248 ? 11.668  1.464   11.227  1.00 9.49   ? 248 GLN A N   1 
ATOM   2013 C  CA  . GLN A  1 248 ? 10.753  0.616   10.503  1.00 8.92   ? 248 GLN A CA  1 
ATOM   2014 C  C   . GLN A  1 248 ? 11.269  0.357   9.073   1.00 9.30   ? 248 GLN A C   1 
ATOM   2015 O  O   . GLN A  1 248 ? 11.967  1.189   8.480   1.00 9.66   ? 248 GLN A O   1 
ATOM   2016 C  CB  . GLN A  1 248 ? 9.367   1.291   10.407  1.00 10.07  ? 248 GLN A CB  1 
ATOM   2017 C  CG  . GLN A  1 248 ? 8.687   1.579   11.721  1.00 9.90   ? 248 GLN A CG  1 
ATOM   2018 C  CD  . GLN A  1 248 ? 8.366   0.381   12.533  1.00 9.80   ? 248 GLN A CD  1 
ATOM   2019 O  OE1 . GLN A  1 248 ? 9.095   -0.044  13.395  1.00 12.03  ? 248 GLN A OE1 1 
ATOM   2020 N  NE2 . GLN A  1 248 ? 7.234   -0.253  12.188  1.00 12.80  ? 248 GLN A NE2 1 
ATOM   2021 N  N   . VAL A  1 249 ? 10.830  -0.764  8.491   1.00 9.13   ? 249 VAL A N   1 
ATOM   2022 C  CA  . VAL A  1 249 ? 11.200  -1.047  7.111   1.00 9.80   ? 249 VAL A CA  1 
ATOM   2023 C  C   . VAL A  1 249 ? 10.564  -0.044  6.155   1.00 8.90   ? 249 VAL A C   1 
ATOM   2024 O  O   . VAL A  1 249 ? 9.452   0.470   6.381   1.00 10.09  ? 249 VAL A O   1 
ATOM   2025 C  CB  . VAL A  1 249 ? 10.875  -2.495  6.700   1.00 11.23  ? 249 VAL A CB  1 
ATOM   2026 C  CG1 . VAL A  1 249 ? 11.760  -3.490  7.484   1.00 11.53  ? 249 VAL A CG1 1 
ATOM   2027 C  CG2 . VAL A  1 249 ? 9.417   -2.802  6.788   1.00 13.25  ? 249 VAL A CG2 1 
ATOM   2028 N  N   . GLN A  1 250 ? 11.292  0.201   5.084   1.00 9.22   ? 250 GLN A N   1 
ATOM   2029 C  CA  . GLN A  1 250 ? 10.933  1.173   4.085   1.00 10.21  ? 250 GLN A CA  1 
ATOM   2030 C  C   . GLN A  1 250 ? 10.320  0.479   2.864   1.00 10.60  ? 250 GLN A C   1 
ATOM   2031 O  O   . GLN A  1 250 ? 10.659  -0.648  2.548   1.00 12.71  ? 250 GLN A O   1 
ATOM   2032 C  CB  . GLN A  1 250 ? 12.245  1.907   3.621   1.00 10.32  ? 250 GLN A CB  1 
ATOM   2033 C  CG  . GLN A  1 250 ? 13.041  2.513   4.804   1.00 10.32  ? 250 GLN A CG  1 
ATOM   2034 C  CD  . GLN A  1 250 ? 12.303  3.609   5.474   1.00 9.80   ? 250 GLN A CD  1 
ATOM   2035 O  OE1 . GLN A  1 250 ? 12.043  4.681   4.851   1.00 10.74  ? 250 GLN A OE1 1 
ATOM   2036 N  NE2 . GLN A  1 250 ? 11.918  3.451   6.710   1.00 9.58   ? 250 GLN A NE2 1 
ATOM   2037 N  N   . LYS A  1 251 ? 9.520   1.236   2.120   1.00 11.74  ? 251 LYS A N   1 
ATOM   2038 C  CA  . LYS A  1 251 ? 9.013   0.678   0.830   1.00 12.10  ? 251 LYS A CA  1 
ATOM   2039 C  C   . LYS A  1 251 ? 10.193  0.387   -0.072  1.00 12.12  ? 251 LYS A C   1 
ATOM   2040 O  O   . LYS A  1 251 ? 11.211  1.126   -0.090  1.00 13.51  ? 251 LYS A O   1 
ATOM   2041 C  CB  . LYS A  1 251 ? 8.098   1.670   0.166   1.00 14.67  ? 251 LYS A CB  1 
ATOM   2042 C  CG  . LYS A  1 251 ? 6.723   1.567   0.834   1.00 17.52  ? 251 LYS A CG  1 
ATOM   2043 C  CD  . LYS A  1 251 ? 5.760   2.451   0.227   1.00 17.46  ? 251 LYS A CD  1 
ATOM   2044 C  CE  . LYS A  1 251 ? 4.290   2.148   0.634   1.00 12.20  ? 251 LYS A CE  1 
ATOM   2045 N  NZ  . LYS A  1 251 ? 4.067   2.155   2.098   1.00 10.82  ? 251 LYS A NZ  1 
ATOM   2046 N  N   . PHE A  1 252 ? 10.123  -0.673  -0.872  1.00 14.55  ? 252 PHE A N   1 
ATOM   2047 C  CA  . PHE A  1 252 ? 11.202  -1.126  -1.775  1.00 14.80  ? 252 PHE A CA  1 
ATOM   2048 C  C   . PHE A  1 252 ? 10.469  -1.732  -3.005  1.00 17.75  ? 252 PHE A C   1 
ATOM   2049 O  O   . PHE A  1 252 ? 10.131  -2.942  -2.973  1.00 22.79  ? 252 PHE A O   1 
ATOM   2050 C  CB  . PHE A  1 252 ? 11.961  -2.240  -1.097  1.00 15.83  ? 252 PHE A CB  1 
ATOM   2051 C  CG  . PHE A  1 252 ? 13.223  -2.667  -1.750  1.00 15.59  ? 252 PHE A CG  1 
ATOM   2052 C  CD1 . PHE A  1 252 ? 14.406  -1.869  -1.694  1.00 16.29  ? 252 PHE A CD1 1 
ATOM   2053 C  CD2 . PHE A  1 252 ? 13.252  -3.922  -2.403  1.00 17.27  ? 252 PHE A CD2 1 
ATOM   2054 C  CE1 . PHE A  1 252 ? 15.596  -2.386  -2.272  1.00 17.76  ? 252 PHE A CE1 1 
ATOM   2055 C  CE2 . PHE A  1 252 ? 14.465  -4.411  -2.938  1.00 18.69  ? 252 PHE A CE2 1 
ATOM   2056 C  CZ  . PHE A  1 252 ? 15.583  -3.574  -2.912  1.00 18.86  ? 252 PHE A CZ  1 
ATOM   2057 N  N   . ASP A  1 253 ? 10.224  -0.937  -3.994  1.00 23.32  ? 253 ASP A N   1 
ATOM   2058 C  CA  . ASP A  1 253 ? 9.508   -1.371  -5.253  1.00 21.37  ? 253 ASP A CA  1 
ATOM   2059 C  C   . ASP A  1 253 ? 10.229  -1.206  -6.440  1.00 20.74  ? 253 ASP A C   1 
ATOM   2060 O  O   . ASP A  1 253 ? 10.985  -0.337  -6.667  1.00 22.47  ? 253 ASP A O   1 
ATOM   2061 C  CB  . ASP A  1 253 ? 8.173   -0.590  -5.347  1.00 27.22  ? 253 ASP A CB  1 
ATOM   2062 C  CG  . ASP A  1 253 ? 7.131   -1.266  -6.246  1.00 52.19  ? 253 ASP A CG  1 
ATOM   2063 O  OD1 . ASP A  1 253 ? 6.953   -2.500  -6.174  1.00 46.61  ? 253 ASP A OD1 1 
ATOM   2064 O  OD2 . ASP A  1 253 ? 6.463   -0.537  -7.013  1.00 58.54  ? 253 ASP A OD2 1 
ATOM   2065 N  N   . GLU A  1 254 ? 9.974   -2.175  -7.287  1.00 21.58  ? 254 GLU A N   1 
ATOM   2066 C  CA  . GLU A  1 254 ? 10.571  -2.314  -8.646  1.00 22.55  ? 254 GLU A CA  1 
ATOM   2067 C  C   . GLU A  1 254 ? 12.077  -2.510  -8.474  1.00 23.28  ? 254 GLU A C   1 
ATOM   2068 O  O   . GLU A  1 254 ? 12.885  -2.038  -9.299  1.00 26.03  ? 254 GLU A O   1 
ATOM   2069 C  CB  . GLU A  1 254 ? 10.242  -1.087  -9.488  1.00 25.21  ? 254 GLU A CB  1 
ATOM   2070 C  CG  . GLU A  1 254 ? 8.722   -1.139  -9.781  1.00 30.90  ? 254 GLU A CG  1 
ATOM   2071 C  CD  . GLU A  1 254 ? 8.311   -2.507  -10.473 1.00 39.65  ? 254 GLU A CD  1 
ATOM   2072 O  OE1 . GLU A  1 254 ? 9.117   -2.986  -11.346 1.00 62.33  ? 254 GLU A OE1 1 
ATOM   2073 O  OE2 . GLU A  1 254 ? 7.203   -3.082  -10.192 1.00 51.53  ? 254 GLU A OE2 1 
ATOM   2074 N  N   . ARG A  1 255 ? 12.460  -3.235  -7.394  1.00 21.04  ? 255 ARG A N   1 
ATOM   2075 C  CA  . ARG A  1 255 ? 13.942  -3.475  -7.095  1.00 21.12  ? 255 ARG A CA  1 
ATOM   2076 C  C   . ARG A  1 255 ? 14.150  -4.861  -6.636  1.00 22.46  ? 255 ARG A C   1 
ATOM   2077 O  O   . ARG A  1 255 ? 13.212  -5.499  -6.054  1.00 22.35  ? 255 ARG A O   1 
ATOM   2078 C  CB  . ARG A  1 255 ? 14.412  -2.500  -6.003  1.00 19.70  ? 255 ARG A CB  1 
ATOM   2079 C  CG  . ARG A  1 255 ? 14.387  -1.091  -6.507  1.00 20.94  ? 255 ARG A CG  1 
ATOM   2080 C  CD  . ARG A  1 255 ? 14.964  -0.125  -5.484  1.00 20.57  ? 255 ARG A CD  1 
ATOM   2081 N  NE  . ARG A  1 255 ? 16.360  -0.414  -5.311  1.00 21.75  ? 255 ARG A NE  1 
ATOM   2082 C  CZ  . ARG A  1 255 ? 17.040  -0.118  -4.185  1.00 19.17  ? 255 ARG A CZ  1 
ATOM   2083 N  NH1 . ARG A  1 255 ? 16.441  0.582   -3.181  1.00 20.06  ? 255 ARG A NH1 1 
ATOM   2084 N  NH2 . ARG A  1 255 ? 18.280  -0.526  -4.078  1.00 17.44  ? 255 ARG A NH2 1 
ATOM   2085 N  N   . LEU A  1 256 ? 15.366  -5.340  -6.776  1.00 22.66  ? 256 LEU A N   1 
ATOM   2086 C  CA  . LEU A  1 256 ? 15.727  -6.644  -6.261  1.00 21.22  ? 256 LEU A CA  1 
ATOM   2087 C  C   . LEU A  1 256 ? 16.799  -6.558  -5.153  1.00 18.79  ? 256 LEU A C   1 
ATOM   2088 O  O   . LEU A  1 256 ? 17.531  -5.606  -5.034  1.00 21.29  ? 256 LEU A O   1 
ATOM   2089 C  CB  . LEU A  1 256 ? 16.264  -7.529  -7.402  1.00 21.92  ? 256 LEU A CB  1 
ATOM   2090 C  CG  . LEU A  1 256 ? 15.314  -7.747  -8.539  1.00 24.41  ? 256 LEU A CG  1 
ATOM   2091 C  CD1 . LEU A  1 256 ? 16.130  -8.286  -9.691  1.00 30.43  ? 256 LEU A CD1 1 
ATOM   2092 C  CD2 . LEU A  1 256 ? 14.158  -8.678  -8.111  1.00 32.56  ? 256 LEU A CD2 1 
ATOM   2093 N  N   . VAL A  1 257 ? 16.795  -7.590  -4.338  1.00 17.07  ? 257 VAL A N   1 
ATOM   2094 C  CA  . VAL A  1 257 ? 17.936  -7.842  -3.472  1.00 16.93  ? 257 VAL A CA  1 
ATOM   2095 C  C   . VAL A  1 257 ? 18.669  -9.015  -4.040  1.00 15.13  ? 257 VAL A C   1 
ATOM   2096 O  O   . VAL A  1 257 ? 18.046  -10.109 -4.290  1.00 17.48  ? 257 VAL A O   1 
ATOM   2097 C  CB  . VAL A  1 257 ? 17.408  -8.114  -2.047  1.00 16.94  ? 257 VAL A CB  1 
ATOM   2098 C  CG1 . VAL A  1 257 ? 18.509  -8.688  -1.120  1.00 17.31  ? 257 VAL A CG1 1 
ATOM   2099 C  CG2 . VAL A  1 257 ? 16.742  -6.936  -1.414  1.00 19.73  ? 257 VAL A CG2 1 
ATOM   2100 N  N   . TYR A  1 258 ? 19.955  -8.837  -4.209  1.00 15.25  ? 258 TYR A N   1 
ATOM   2101 C  CA  . TYR A  1 258 ? 20.747  -9.950  -4.783  1.00 14.91  ? 258 TYR A CA  1 
ATOM   2102 C  C   . TYR A  1 258 ? 21.242  -10.838 -3.716  1.00 14.19  ? 258 TYR A C   1 
ATOM   2103 O  O   . TYR A  1 258 ? 21.583  -10.400 -2.618  1.00 16.38  ? 258 TYR A O   1 
ATOM   2104 C  CB  . TYR A  1 258 ? 21.845  -9.297  -5.651  1.00 15.85  ? 258 TYR A CB  1 
ATOM   2105 C  CG  . TYR A  1 258 ? 21.241  -8.375  -6.659  1.00 18.30  ? 258 TYR A CG  1 
ATOM   2106 C  CD1 . TYR A  1 258 ? 20.706  -8.913  -7.792  1.00 22.11  ? 258 TYR A CD1 1 
ATOM   2107 C  CD2 . TYR A  1 258 ? 21.123  -6.972  -6.432  1.00 20.93  ? 258 TYR A CD2 1 
ATOM   2108 C  CE1 . TYR A  1 258 ? 20.099  -8.061  -8.784  1.00 23.37  ? 258 TYR A CE1 1 
ATOM   2109 C  CE2 . TYR A  1 258 ? 20.440  -6.177  -7.312  1.00 26.69  ? 258 TYR A CE2 1 
ATOM   2110 C  CZ  . TYR A  1 258 ? 20.033  -6.690  -8.537  1.00 24.49  ? 258 TYR A CZ  1 
ATOM   2111 O  OH  . TYR A  1 258 ? 19.378  -5.872  -9.430  1.00 33.57  ? 258 TYR A OH  1 
ATOM   2112 N  N   . THR A  1 259 ? 21.332  -12.115 -4.020  1.00 14.79  ? 259 THR A N   1 
ATOM   2113 C  CA  . THR A  1 259 ? 21.790  -13.082 -3.059  1.00 14.45  ? 259 THR A CA  1 
ATOM   2114 C  C   . THR A  1 259 ? 22.989  -13.851 -3.562  1.00 13.98  ? 259 THR A C   1 
ATOM   2115 O  O   . THR A  1 259 ? 23.096  -14.168 -4.757  1.00 15.82  ? 259 THR A O   1 
ATOM   2116 C  CB  . THR A  1 259 ? 20.702  -14.090 -2.629  1.00 16.14  ? 259 THR A CB  1 
ATOM   2117 O  OG1 . THR A  1 259 ? 20.194  -14.773 -3.759  1.00 18.98  ? 259 THR A OG1 1 
ATOM   2118 C  CG2 . THR A  1 259 ? 19.582  -13.363 -1.993  1.00 17.04  ? 259 THR A CG2 1 
ATOM   2119 N  N   . SER A  1 260 ? 23.890  -14.192 -2.651  1.00 14.64  ? 260 SER A N   1 
ATOM   2120 C  CA  . SER A  1 260 ? 25.032  -15.026 -3.026  1.00 17.21  ? 260 SER A CA  1 
ATOM   2121 C  C   . SER A  1 260 ? 24.743  -16.508 -2.956  1.00 17.99  ? 260 SER A C   1 
ATOM   2122 O  O   . SER A  1 260 ? 25.639  -17.310 -3.307  1.00 23.83  ? 260 SER A O   1 
ATOM   2123 C  CB  . SER A  1 260 ? 26.246  -14.748 -2.165  1.00 16.92  ? 260 SER A CB  1 
ATOM   2124 O  OG  . SER A  1 260 ? 25.902  -15.096 -0.881  1.00 15.31  ? 260 SER A OG  1 
ATOM   2125 N  N   . PHE A  1 261 ? 23.507  -16.855 -2.589  1.00 18.31  ? 261 PHE A N   1 
ATOM   2126 C  CA  . PHE A  1 261 ? 23.201  -18.206 -2.400  1.00 20.52  ? 261 PHE A CA  1 
ATOM   2127 C  C   . PHE A  1 261 ? 21.984  -18.398 -3.252  1.00 20.62  ? 261 PHE A C   1 
ATOM   2128 O  O   . PHE A  1 261 ? 21.115  -17.533 -3.502  1.00 23.48  ? 261 PHE A O   1 
ATOM   2129 C  CB  . PHE A  1 261 ? 22.876  -18.520 -0.950  1.00 22.05  ? 261 PHE A CB  1 
ATOM   2130 C  CG  . PHE A  1 261 ? 21.865  -17.558 -0.355  1.00 20.41  ? 261 PHE A CG  1 
ATOM   2131 C  CD1 . PHE A  1 261 ? 20.485  -17.855 -0.256  1.00 22.41  ? 261 PHE A CD1 1 
ATOM   2132 C  CD2 . PHE A  1 261 ? 22.302  -16.400 0.180   1.00 17.83  ? 261 PHE A CD2 1 
ATOM   2133 C  CE1 . PHE A  1 261 ? 19.572  -16.984 0.291   1.00 25.00  ? 261 PHE A CE1 1 
ATOM   2134 C  CE2 . PHE A  1 261 ? 21.365  -15.519 0.798   1.00 16.98  ? 261 PHE A CE2 1 
ATOM   2135 C  CZ  . PHE A  1 261 ? 20.014  -15.817 0.857   1.00 18.73  ? 261 PHE A CZ  1 
ATOM   2136 N  N   . SER A  1 262 ? 21.867  -19.627 -3.818  1.00 28.01  ? 262 SER A N   1 
ATOM   2137 C  CA  . SER A  1 262 ? 20.554  -19.848 -4.522  1.00 30.35  ? 262 SER A CA  1 
ATOM   2138 C  C   . SER A  1 262 ? 19.752  -20.805 -3.702  1.00 42.00  ? 262 SER A C   1 
ATOM   2139 O  O   . SER A  1 262 ? 18.524  -20.667 -3.654  1.00 49.00  ? 262 SER A O   1 
ATOM   2140 C  CB  . SER A  1 262 ? 20.724  -20.406 -5.927  1.00 43.76  ? 262 SER A CB  1 
ATOM   2141 O  OG  . SER A  1 262 ? 21.542  -21.543 -5.839  1.00 54.12  ? 262 SER A OG  1 
ATOM   2142 N  N   . GLN A  1 263 ? 20.413  -21.764 -3.062  1.00 49.38  ? 263 GLN A N   1 
ATOM   2143 C  CA  . GLN A  1 263 ? 19.725  -22.749 -2.236  1.00 62.90  ? 263 GLN A CA  1 
ATOM   2144 C  C   . GLN A  1 263 ? 19.114  -22.101 -0.998  1.00 82.61  ? 263 GLN A C   1 
ATOM   2145 O  O   . GLN A  1 263 ? 19.486  -20.990 -0.620  1.00 70.64  ? 263 GLN A O   1 
ATOM   2146 C  CB  . GLN A  1 263 ? 20.684  -23.868 -1.824  1.00 75.82  ? 263 GLN A CB  1 
ATOM   2147 C  CG  . GLN A  1 263 ? 21.590  -24.353 -2.945  1.00 81.52  ? 263 GLN A CG  1 
ATOM   2148 C  CD  . GLN A  1 263 ? 22.023  -25.794 -2.761  1.00 49.82  ? 263 GLN A CD  1 
ATOM   2149 O  OE1 . GLN A  1 263 ? 23.046  -26.072 -2.135  1.00 45.21  ? 263 GLN A OE1 1 
ATOM   2150 N  NE2 . GLN A  1 263 ? 21.244  -26.720 -3.309  1.00 29.02  ? 263 GLN A NE2 1 
ATOM   2151 N  N   . LYS B  1 3   ? -1.376  17.312  -2.600  1.00 74.92  ? 3   LYS B N   1 
ATOM   2152 C  CA  . LYS B  1 3   ? 0.135   17.180  -2.651  1.00 41.39  ? 3   LYS B CA  1 
ATOM   2153 C  C   . LYS B  1 3   ? 0.670   15.766  -2.187  1.00 36.19  ? 3   LYS B C   1 
ATOM   2154 O  O   . LYS B  1 3   ? 1.542   15.144  -2.878  1.00 33.61  ? 3   LYS B O   1 
ATOM   2155 C  CB  . LYS B  1 3   ? 0.711   18.130  -1.637  1.00 76.32  ? 3   LYS B CB  1 
ATOM   2156 C  CG  . LYS B  1 3   ? -0.190  18.446  -0.368  1.00 58.60  ? 3   LYS B CG  1 
ATOM   2157 C  CD  . LYS B  1 3   ? -1.055  19.722  -0.448  1.00 53.31  ? 3   LYS B CD  1 
ATOM   2158 C  CE  . LYS B  1 3   ? -0.371  20.870  0.322   1.00 39.86  ? 3   LYS B CE  1 
ATOM   2159 N  NZ  . LYS B  1 3   ? -0.852  22.251  0.214   1.00 53.77  ? 3   LYS B NZ  1 
ATOM   2160 N  N   . TRP B  1 4   ? 0.209   15.310  -0.998  1.00 17.19  ? 4   TRP B N   1 
ATOM   2161 C  CA  . TRP B  1 4   ? 0.870   14.146  -0.450  1.00 14.68  ? 4   TRP B CA  1 
ATOM   2162 C  C   . TRP B  1 4   ? 0.632   12.945  -1.299  1.00 13.21  ? 4   TRP B C   1 
ATOM   2163 O  O   . TRP B  1 4   ? -0.382  12.880  -2.009  1.00 14.95  ? 4   TRP B O   1 
ATOM   2164 C  CB  . TRP B  1 4   ? 0.358   13.923  0.987   1.00 12.84  ? 4   TRP B CB  1 
ATOM   2165 C  CG  . TRP B  1 4   ? -1.138  13.604  1.145   1.00 12.18  ? 4   TRP B CG  1 
ATOM   2166 C  CD1 . TRP B  1 4   ? -2.171  14.474  1.363   1.00 14.32  ? 4   TRP B CD1 1 
ATOM   2167 C  CD2 . TRP B  1 4   ? -1.727  12.283  1.139   1.00 11.11  ? 4   TRP B CD2 1 
ATOM   2168 N  NE1 . TRP B  1 4   ? -3.333  13.772  1.497   1.00 13.66  ? 4   TRP B NE1 1 
ATOM   2169 C  CE2 . TRP B  1 4   ? -3.093  12.446  1.376   1.00 12.26  ? 4   TRP B CE2 1 
ATOM   2170 C  CE3 . TRP B  1 4   ? -1.169  10.965  1.022   1.00 12.05  ? 4   TRP B CE3 1 
ATOM   2171 C  CZ2 . TRP B  1 4   ? -3.964  11.345  1.422   1.00 13.48  ? 4   TRP B CZ2 1 
ATOM   2172 C  CZ3 . TRP B  1 4   ? -2.056  9.916   1.129   1.00 12.15  ? 4   TRP B CZ3 1 
ATOM   2173 C  CH2 . TRP B  1 4   ? -3.380  10.076  1.339   1.00 11.96  ? 4   TRP B CH2 1 
ATOM   2174 N  N   . THR B  1 5   ? 1.540   12.010  -1.268  1.00 13.33  ? 5   THR B N   1 
ATOM   2175 C  CA  . THR B  1 5   ? 1.475   10.781  -2.076  1.00 14.43  ? 5   THR B CA  1 
ATOM   2176 C  C   . THR B  1 5   ? 1.924   9.586   -1.224  1.00 11.72  ? 5   THR B C   1 
ATOM   2177 O  O   . THR B  1 5   ? 2.304   9.755   -0.100  1.00 12.10  ? 5   THR B O   1 
ATOM   2178 C  CB  . THR B  1 5   ? 2.432   10.888  -3.364  1.00 15.50  ? 5   THR B CB  1 
ATOM   2179 O  OG1 . THR B  1 5   ? 3.747   10.860  -2.795  1.00 16.78  ? 5   THR B OG1 1 
ATOM   2180 C  CG2 . THR B  1 5   ? 2.127   12.241  -4.191  1.00 17.28  ? 5   THR B CG2 1 
ATOM   2181 N  N   . TYR B  1 6   ? 2.026   8.466   -1.884  1.00 12.89  ? 6   TYR B N   1 
ATOM   2182 C  CA  . TYR B  1 6   ? 2.591   7.288   -1.286  1.00 13.56  ? 6   TYR B CA  1 
ATOM   2183 C  C   . TYR B  1 6   ? 3.984   6.933   -1.868  1.00 13.61  ? 6   TYR B C   1 
ATOM   2184 O  O   . TYR B  1 6   ? 4.531   5.852   -1.563  1.00 14.38  ? 6   TYR B O   1 
ATOM   2185 C  CB  . TYR B  1 6   ? 1.660   6.069   -1.461  1.00 13.43  ? 6   TYR B CB  1 
ATOM   2186 C  CG  . TYR B  1 6   ? 0.431   6.173   -0.615  1.00 11.10  ? 6   TYR B CG  1 
ATOM   2187 C  CD1 . TYR B  1 6   ? -0.752  6.728   -1.092  1.00 11.94  ? 6   TYR B CD1 1 
ATOM   2188 C  CD2 . TYR B  1 6   ? 0.483   5.686   0.688   1.00 11.21  ? 6   TYR B CD2 1 
ATOM   2189 C  CE1 . TYR B  1 6   ? -1.928  6.700   -0.327  1.00 11.55  ? 6   TYR B CE1 1 
ATOM   2190 C  CE2 . TYR B  1 6   ? -0.659  5.670   1.487   1.00 10.33  ? 6   TYR B CE2 1 
ATOM   2191 C  CZ  . TYR B  1 6   ? -1.884  6.182   0.998   1.00 10.60  ? 6   TYR B CZ  1 
ATOM   2192 O  OH  . TYR B  1 6   ? -3.016  6.189   1.690   1.00 11.63  ? 6   TYR B OH  1 
ATOM   2193 N  N   . PHE B  1 7   ? 4.547   7.762   -2.736  1.00 15.16  ? 7   PHE B N   1 
ATOM   2194 C  CA  . PHE B  1 7   ? 5.798   7.365   -3.398  1.00 17.40  ? 7   PHE B CA  1 
ATOM   2195 C  C   . PHE B  1 7   ? 6.495   8.645   -3.796  1.00 21.83  ? 7   PHE B C   1 
ATOM   2196 O  O   . PHE B  1 7   ? 5.882   9.517   -4.452  1.00 23.31  ? 7   PHE B O   1 
ATOM   2197 C  CB  . PHE B  1 7   ? 5.468   6.571   -4.741  1.00 22.75  ? 7   PHE B CB  1 
ATOM   2198 C  CG  . PHE B  1 7   ? 6.680   6.213   -5.522  1.00 24.17  ? 7   PHE B CG  1 
ATOM   2199 C  CD1 . PHE B  1 7   ? 7.616   5.202   -5.046  1.00 28.95  ? 7   PHE B CD1 1 
ATOM   2200 C  CD2 . PHE B  1 7   ? 6.984   6.948   -6.686  1.00 38.35  ? 7   PHE B CD2 1 
ATOM   2201 C  CE1 . PHE B  1 7   ? 8.783   4.895   -5.815  1.00 34.44  ? 7   PHE B CE1 1 
ATOM   2202 C  CE2 . PHE B  1 7   ? 8.126   6.649   -7.398  1.00 49.00  ? 7   PHE B CE2 1 
ATOM   2203 C  CZ  . PHE B  1 7   ? 9.011   5.643   -6.983  1.00 48.50  ? 7   PHE B CZ  1 
ATOM   2204 N  N   . GLY B  1 8   ? 7.795   8.670   -3.547  1.00 22.96  ? 8   GLY B N   1 
ATOM   2205 C  CA  . GLY B  1 8   ? 8.639   9.766   -4.071  1.00 20.94  ? 8   GLY B CA  1 
ATOM   2206 C  C   . GLY B  1 8   ? 8.734   10.849  -3.041  1.00 18.84  ? 8   GLY B C   1 
ATOM   2207 O  O   . GLY B  1 8   ? 8.549   10.636  -1.769  1.00 19.43  ? 8   GLY B O   1 
ATOM   2208 N  N   . PRO B  1 9   ? 9.097   12.086  -3.435  1.00 19.68  ? 9   PRO B N   1 
ATOM   2209 C  CA  . PRO B  1 9   ? 9.395   13.138  -2.492  1.00 21.42  ? 9   PRO B CA  1 
ATOM   2210 C  C   . PRO B  1 9   ? 8.325   13.509  -1.513  1.00 18.43  ? 9   PRO B C   1 
ATOM   2211 O  O   . PRO B  1 9   ? 8.639   13.984  -0.487  1.00 18.84  ? 9   PRO B O   1 
ATOM   2212 C  CB  . PRO B  1 9   ? 9.759   14.366  -3.367  1.00 25.38  ? 9   PRO B CB  1 
ATOM   2213 C  CG  . PRO B  1 9   ? 9.823   13.872  -4.687  1.00 27.90  ? 9   PRO B CG  1 
ATOM   2214 C  CD  . PRO B  1 9   ? 9.347   12.494  -4.841  1.00 24.88  ? 9   PRO B CD  1 
ATOM   2215 N  N   . ASP B  1 10  ? 7.062   13.337  -1.925  1.00 18.02  ? 10  ASP B N   1 
ATOM   2216 C  CA  . ASP B  1 10  ? 5.944   13.722  -1.070  1.00 15.61  ? 10  ASP B CA  1 
ATOM   2217 C  C   . ASP B  1 10  ? 5.293   12.504  -0.377  1.00 14.24  ? 10  ASP B C   1 
ATOM   2218 O  O   . ASP B  1 10  ? 4.167   12.609  0.112   1.00 14.65  ? 10  ASP B O   1 
ATOM   2219 C  CB  . ASP B  1 10  ? 4.907   14.463  -1.934  1.00 16.99  ? 10  ASP B CB  1 
ATOM   2220 C  CG  . ASP B  1 10  ? 5.434   15.751  -2.470  1.00 22.49  ? 10  ASP B CG  1 
ATOM   2221 O  OD1 . ASP B  1 10  ? 6.117   16.498  -1.803  1.00 24.31  ? 10  ASP B OD1 1 
ATOM   2222 O  OD2 . ASP B  1 10  ? 5.224   16.056  -3.653  1.00 30.96  ? 10  ASP B OD2 1 
ATOM   2223 N  N   . GLY B  1 11  ? 6.023   11.396  -0.364  1.00 14.68  ? 11  GLY B N   1 
ATOM   2224 C  CA  . GLY B  1 11  ? 5.549   10.161  0.289   1.00 12.86  ? 11  GLY B CA  1 
ATOM   2225 C  C   . GLY B  1 11  ? 5.589   10.189  1.780   1.00 11.28  ? 11  GLY B C   1 
ATOM   2226 O  O   . GLY B  1 11  ? 5.817   11.217  2.429   1.00 11.37  ? 11  GLY B O   1 
ATOM   2227 N  N   . GLU B  1 12  ? 5.342   8.997   2.404   1.00 10.63  ? 12  GLU B N   1 
ATOM   2228 C  CA  . GLU B  1 12  ? 4.909   8.989   3.792   1.00 9.84   ? 12  GLU B CA  1 
ATOM   2229 C  C   . GLU B  1 12  ? 5.966   9.462   4.767   1.00 9.57   ? 12  GLU B C   1 
ATOM   2230 O  O   . GLU B  1 12  ? 5.613   9.907   5.854   1.00 10.24  ? 12  GLU B O   1 
ATOM   2231 C  CB  . GLU B  1 12  ? 4.462   7.545   4.171   1.00 10.36  ? 12  GLU B CB  1 
ATOM   2232 C  CG  . GLU B  1 12  ? 5.598   6.561   4.237   1.00 10.39  ? 12  GLU B CG  1 
ATOM   2233 C  CD  . GLU B  1 12  ? 4.998   5.148   4.159   1.00 9.98   ? 12  GLU B CD  1 
ATOM   2234 O  OE1 . GLU B  1 12  ? 4.631   4.635   5.290   1.00 10.21  ? 12  GLU B OE1 1 
ATOM   2235 O  OE2 . GLU B  1 12  ? 4.881   4.600   3.056   1.00 11.62  ? 12  GLU B OE2 1 
ATOM   2236 N  N   . ASN B  1 13  ? 7.278   9.349   4.442   1.00 10.06  ? 13  ASN B N   1 
ATOM   2237 C  CA  . ASN B  1 13  ? 8.288   9.850   5.408   1.00 10.21  ? 13  ASN B CA  1 
ATOM   2238 C  C   . ASN B  1 13  ? 8.270   11.369  5.456   1.00 10.56  ? 13  ASN B C   1 
ATOM   2239 O  O   . ASN B  1 13  ? 8.887   11.943  6.339   1.00 11.93  ? 13  ASN B O   1 
ATOM   2240 C  CB  . ASN B  1 13  ? 9.673   9.371   5.053   1.00 11.09  ? 13  ASN B CB  1 
ATOM   2241 C  CG  . ASN B  1 13  ? 9.885   7.871   5.283   1.00 10.37  ? 13  ASN B CG  1 
ATOM   2242 O  OD1 . ASN B  1 13  ? 8.973   7.201   5.807   1.00 11.06  ? 13  ASN B OD1 1 
ATOM   2243 N  ND2 . ASN B  1 13  ? 11.059  7.380   5.017   1.00 11.29  ? 13  ASN B ND2 1 
ATOM   2244 N  N   . SER B  1 14  ? 7.610   12.026  4.525   1.00 10.12  ? 14  SER B N   1 
ATOM   2245 C  CA  . SER B  1 14  ? 7.536   13.487  4.433   1.00 10.89  ? 14  SER B CA  1 
ATOM   2246 C  C   . SER B  1 14  ? 6.185   13.989  4.873   1.00 9.93   ? 14  SER B C   1 
ATOM   2247 O  O   . SER B  1 14  ? 6.055   15.245  4.971   1.00 11.05  ? 14  SER B O   1 
ATOM   2248 C  CB  . SER B  1 14  ? 7.845   13.944  3.023   1.00 12.34  ? 14  SER B CB  1 
ATOM   2249 O  OG  . SER B  1 14  ? 9.207   13.691  2.741   1.00 13.55  ? 14  SER B OG  1 
ATOM   2250 N  N   . TRP B  1 15  ? 5.170   13.202  5.121   1.00 9.78   ? 15  TRP B N   1 
ATOM   2251 C  CA  . TRP B  1 15  ? 3.847   13.743  5.494   1.00 10.37  ? 15  TRP B CA  1 
ATOM   2252 C  C   . TRP B  1 15  ? 3.945   14.622  6.680   1.00 10.38  ? 15  TRP B C   1 
ATOM   2253 O  O   . TRP B  1 15  ? 3.189   15.637  6.729   1.00 11.15  ? 15  TRP B O   1 
ATOM   2254 C  CB  . TRP B  1 15  ? 2.870   12.566  5.803   1.00 10.12  ? 15  TRP B CB  1 
ATOM   2255 C  CG  . TRP B  1 15  ? 2.528   11.711  4.647   1.00 9.68   ? 15  TRP B CG  1 
ATOM   2256 C  CD1 . TRP B  1 15  ? 2.799   11.902  3.329   1.00 10.98  ? 15  TRP B CD1 1 
ATOM   2257 C  CD2 . TRP B  1 15  ? 1.762   10.482  4.753   1.00 9.09   ? 15  TRP B CD2 1 
ATOM   2258 N  NE1 . TRP B  1 15  ? 2.243   10.838  2.572   1.00 10.12  ? 15  TRP B NE1 1 
ATOM   2259 C  CE2 . TRP B  1 15  ? 1.627   9.997   3.473   1.00 9.89   ? 15  TRP B CE2 1 
ATOM   2260 C  CE3 . TRP B  1 15  ? 1.188   9.794   5.869   1.00 9.96   ? 15  TRP B CE3 1 
ATOM   2261 C  CZ2 . TRP B  1 15  ? 0.891   8.778   3.220   1.00 10.65  ? 15  TRP B CZ2 1 
ATOM   2262 C  CZ3 . TRP B  1 15  ? 0.508   8.589   5.557   1.00 10.28  ? 15  TRP B CZ3 1 
ATOM   2263 C  CH2 . TRP B  1 15  ? 0.376   8.136   4.294   1.00 10.42  ? 15  TRP B CH2 1 
ATOM   2264 N  N   . SER B  1 16  ? 4.742   14.333  7.678   1.00 10.59  ? 16  SER B N   1 
ATOM   2265 C  CA  . SER B  1 16  ? 4.795   15.098  8.871   1.00 11.83  ? 16  SER B CA  1 
ATOM   2266 C  C   . SER B  1 16  ? 5.327   16.559  8.651   1.00 11.00  ? 16  SER B C   1 
ATOM   2267 O  O   . SER B  1 16  ? 5.088   17.367  9.568   1.00 12.99  ? 16  SER B O   1 
ATOM   2268 C  CB  . SER B  1 16  ? 5.731   14.450  9.894   1.00 13.36  ? 16  SER B CB  1 
ATOM   2269 O  OG  . SER B  1 16  ? 7.052   14.567  9.435   1.00 17.03  ? 16  SER B OG  1 
ATOM   2270 N  N   . LYS B  1 17  ? 5.916   16.830  7.552   1.00 11.19  ? 17  LYS B N   1 
ATOM   2271 C  CA  . LYS B  1 17  ? 6.342   18.218  7.233   1.00 11.39  ? 17  LYS B CA  1 
ATOM   2272 C  C   . LYS B  1 17  ? 5.162   19.132  7.109   1.00 12.38  ? 17  LYS B C   1 
ATOM   2273 O  O   . LYS B  1 17  ? 5.289   20.339  7.443   1.00 13.84  ? 17  LYS B O   1 
ATOM   2274 C  CB  . LYS B  1 17  ? 7.143   18.243  5.947   1.00 12.69  ? 17  LYS B CB  1 
ATOM   2275 C  CG  . LYS B  1 17  ? 8.407   17.416  5.873   1.00 12.60  ? 17  LYS B CG  1 
ATOM   2276 C  CD  . LYS B  1 17  ? 9.014   17.393  4.462   1.00 12.82  ? 17  LYS B CD  1 
ATOM   2277 C  CE  . LYS B  1 17  ? 10.225  16.496  4.336   1.00 12.49  ? 17  LYS B CE  1 
ATOM   2278 N  NZ  . LYS B  1 17  ? 10.785  16.630  3.004   1.00 13.44  ? 17  LYS B NZ  1 
ATOM   2279 N  N   . LYS B  1 18  ? 4.006   18.663  6.614   1.00 12.30  ? 18  LYS B N   1 
ATOM   2280 C  CA  . LYS B  1 18  ? 2.817   19.460  6.415   1.00 12.88  ? 18  LYS B CA  1 
ATOM   2281 C  C   . LYS B  1 18  ? 1.714   19.057  7.410   1.00 12.52  ? 18  LYS B C   1 
ATOM   2282 O  O   . LYS B  1 18  ? 0.787   19.854  7.597   1.00 15.51  ? 18  LYS B O   1 
ATOM   2283 C  CB  . LYS B  1 18  ? 2.261   19.307  4.991   1.00 14.81  ? 18  LYS B CB  1 
ATOM   2284 C  CG  . LYS B  1 18  ? 3.224   19.935  3.983   1.00 22.37  ? 18  LYS B CG  1 
ATOM   2285 C  CD  . LYS B  1 18  ? 2.615   19.854  2.532   1.00 27.73  ? 18  LYS B CD  1 
ATOM   2286 C  CE  . LYS B  1 18  ? 3.297   20.849  1.524   1.00 34.71  ? 18  LYS B CE  1 
ATOM   2287 N  NZ  . LYS B  1 18  ? 2.652   20.499  0.200   1.00 50.58  ? 18  LYS B NZ  1 
ATOM   2288 N  N   . TYR B  1 19  ? 1.760   17.837  7.950   1.00 12.26  ? 19  TYR B N   1 
ATOM   2289 C  CA  . TYR B  1 19  ? 0.673   17.272  8.739   1.00 12.70  ? 19  TYR B CA  1 
ATOM   2290 C  C   . TYR B  1 19  ? 1.254   16.781  10.033  1.00 11.29  ? 19  TYR B C   1 
ATOM   2291 O  O   . TYR B  1 19  ? 1.705   15.632  10.128  1.00 12.35  ? 19  TYR B O   1 
ATOM   2292 C  CB  . TYR B  1 19  ? -0.023  16.134  7.982   1.00 12.35  ? 19  TYR B CB  1 
ATOM   2293 C  CG  . TYR B  1 19  ? -0.599  16.542  6.667   1.00 11.24  ? 19  TYR B CG  1 
ATOM   2294 C  CD1 . TYR B  1 19  ? -1.857  17.190  6.635   1.00 14.59  ? 19  TYR B CD1 1 
ATOM   2295 C  CD2 . TYR B  1 19  ? 0.064   16.342  5.512   1.00 12.71  ? 19  TYR B CD2 1 
ATOM   2296 C  CE1 . TYR B  1 19  ? -2.414  17.552  5.369   1.00 16.15  ? 19  TYR B CE1 1 
ATOM   2297 C  CE2 . TYR B  1 19  ? -0.460  16.706  4.272   1.00 15.07  ? 19  TYR B CE2 1 
ATOM   2298 C  CZ  . TYR B  1 19  ? -1.719  17.342  4.226   1.00 16.98  ? 19  TYR B CZ  1 
ATOM   2299 O  OH  . TYR B  1 19  ? -2.249  17.697  3.006   1.00 21.67  ? 19  TYR B OH  1 
ATOM   2300 N  N   . PRO B  1 20  ? 1.391   17.668  11.050  1.00 13.25  ? 20  PRO B N   1 
ATOM   2301 C  CA  . PRO B  1 20  ? 2.165   17.285  12.218  1.00 13.61  ? 20  PRO B CA  1 
ATOM   2302 C  C   . PRO B  1 20  ? 1.711   16.036  12.890  1.00 12.51  ? 20  PRO B C   1 
ATOM   2303 O  O   . PRO B  1 20  ? 2.528   15.322  13.538  1.00 13.19  ? 20  PRO B O   1 
ATOM   2304 C  CB  . PRO B  1 20  ? 2.037   18.520  13.195  1.00 17.08  ? 20  PRO B CB  1 
ATOM   2305 C  CG  . PRO B  1 20  ? 1.807   19.620  12.281  1.00 21.21  ? 20  PRO B CG  1 
ATOM   2306 C  CD  . PRO B  1 20  ? 0.959   19.102  11.083  1.00 15.73  ? 20  PRO B CD  1 
ATOM   2307 N  N   . SER B  1 21  ? 0.392   15.711  12.893  1.00 12.16  ? 21  SER B N   1 
ATOM   2308 C  CA  . SER B  1 21  ? -0.017  14.526  13.592  1.00 12.32  ? 21  SER B CA  1 
ATOM   2309 C  C   . SER B  1 21  ? 0.564   13.241  12.960  1.00 10.11  ? 21  SER B C   1 
ATOM   2310 O  O   . SER B  1 21  ? 0.595   12.228  13.670  1.00 12.07  ? 21  SER B O   1 
ATOM   2311 C  CB  . SER B  1 21  ? -1.538  14.408  13.654  1.00 12.91  ? 21  SER B CB  1 
ATOM   2312 O  OG  . SER B  1 21  ? -2.096  15.479  14.438  1.00 15.91  ? 21  SER B OG  1 
ATOM   2313 N  N   . CYS B  1 22  ? 0.990   13.253  11.746  1.00 10.28  ? 22  CYS B N   1 
ATOM   2314 C  CA  . CYS B  1 22  ? 1.574   12.100  11.116  1.00 10.81  ? 22  CYS B CA  1 
ATOM   2315 C  C   . CYS B  1 22  ? 2.886   11.734  11.770  1.00 11.83  ? 22  CYS B C   1 
ATOM   2316 O  O   . CYS B  1 22  ? 3.359   10.600  11.601  1.00 12.55  ? 22  CYS B O   1 
ATOM   2317 C  CB  . CYS B  1 22  ? 1.773   12.310  9.585   1.00 10.96  ? 22  CYS B CB  1 
ATOM   2318 S  SG  . CYS B  1 22  ? 0.220   12.598  8.711   1.00 11.57  ? 22  CYS B SG  1 
ATOM   2319 N  N   . GLY B  1 23  ? 3.520   12.653  12.562  1.00 12.21  ? 23  GLY B N   1 
ATOM   2320 C  CA  . GLY B  1 23  ? 4.664   12.413  13.340  1.00 13.38  ? 23  GLY B CA  1 
ATOM   2321 C  C   . GLY B  1 23  ? 4.397   12.268  14.788  1.00 13.14  ? 23  GLY B C   1 
ATOM   2322 O  O   . GLY B  1 23  ? 5.342   12.270  15.617  1.00 16.42  ? 23  GLY B O   1 
ATOM   2323 N  N   . GLY B  1 24  ? 3.123   12.199  15.197  1.00 14.44  ? 24  GLY B N   1 
ATOM   2324 C  CA  . GLY B  1 24  ? 2.812   12.158  16.558  1.00 16.58  ? 24  GLY B CA  1 
ATOM   2325 C  C   . GLY B  1 24  ? 2.516   10.801  17.075  1.00 16.92  ? 24  GLY B C   1 
ATOM   2326 O  O   . GLY B  1 24  ? 2.986   9.826   16.510  1.00 19.81  ? 24  GLY B O   1 
ATOM   2327 N  N   . LEU B  1 25  ? 1.820   10.759  18.179  1.00 20.30  ? 25  LEU B N   1 
ATOM   2328 C  CA  . LEU B  1 25  ? 1.605   9.432   18.772  1.00 23.83  ? 25  LEU B CA  1 
ATOM   2329 C  C   . LEU B  1 25  ? 0.373   8.729   18.196  1.00 19.49  ? 25  LEU B C   1 
ATOM   2330 O  O   . LEU B  1 25  ? -0.433  9.350   17.396  1.00 17.04  ? 25  LEU B O   1 
ATOM   2331 C  CB  . LEU B  1 25  ? 1.774   9.369   20.251  1.00 26.26  ? 25  LEU B CB  1 
ATOM   2332 C  CG  . LEU B  1 25  ? 3.167   9.812   20.885  1.00 25.21  ? 25  LEU B CG  1 
ATOM   2333 C  CD1 . LEU B  1 25  ? 3.035   10.022  22.364  1.00 36.58  ? 25  LEU B CD1 1 
ATOM   2334 C  CD2 . LEU B  1 25  ? 4.355   8.896   20.525  1.00 35.32  ? 25  LEU B CD2 1 
ATOM   2335 N  N   . LEU B  1 26  ? 0.211   7.439   18.517  1.00 19.62  ? 26  LEU B N   1 
ATOM   2336 C  CA  . LEU B  1 26  ? -0.970  6.660   18.284  1.00 18.72  ? 26  LEU B CA  1 
ATOM   2337 C  C   . LEU B  1 26  ? -1.170  6.420   16.798  1.00 13.55  ? 26  LEU B C   1 
ATOM   2338 O  O   . LEU B  1 26  ? -2.357  6.364   16.345  1.00 14.11  ? 26  LEU B O   1 
ATOM   2339 C  CB  . LEU B  1 26  ? -2.254  7.262   18.898  1.00 19.58  ? 26  LEU B CB  1 
ATOM   2340 C  CG  . LEU B  1 26  ? -2.250  7.435   20.472  1.00 27.64  ? 26  LEU B CG  1 
ATOM   2341 C  CD1 . LEU B  1 26  ? -3.601  7.991   20.960  1.00 38.66  ? 26  LEU B CD1 1 
ATOM   2342 C  CD2 . LEU B  1 26  ? -2.015  6.109   21.171  1.00 27.80  ? 26  LEU B CD2 1 
ATOM   2343 N  N   . GLN B  1 27  ? -0.129  6.302   16.012  1.00 12.73  ? 27  GLN B N   1 
ATOM   2344 C  CA  . GLN B  1 27  ? -0.291  6.144   14.573  1.00 10.71  ? 27  GLN B CA  1 
ATOM   2345 C  C   . GLN B  1 27  ? -0.664  4.736   14.159  1.00 10.31  ? 27  GLN B C   1 
ATOM   2346 O  O   . GLN B  1 27  ? -0.217  3.728   14.719  1.00 12.82  ? 27  GLN B O   1 
ATOM   2347 C  CB  . GLN B  1 27  ? 0.928   6.657   13.859  1.00 11.90  ? 27  GLN B CB  1 
ATOM   2348 C  CG  . GLN B  1 27  ? 1.241   8.146   14.095  1.00 12.20  ? 27  GLN B CG  1 
ATOM   2349 C  CD  . GLN B  1 27  ? 0.143   8.972   13.393  1.00 10.53  ? 27  GLN B CD  1 
ATOM   2350 O  OE1 . GLN B  1 27  ? 0.133   9.093   12.181  1.00 11.33  ? 27  GLN B OE1 1 
ATOM   2351 N  NE2 . GLN B  1 27  ? -0.768  9.493   14.190  1.00 11.21  ? 27  GLN B NE2 1 
ATOM   2352 N  N   . SER B  1 28  ? -1.407  4.700   13.067  1.00 9.81   ? 28  SER B N   1 
ATOM   2353 C  CA  . SER B  1 28  ? -1.801  3.454   12.390  1.00 9.22   ? 28  SER B CA  1 
ATOM   2354 C  C   . SER B  1 28  ? -1.220  3.442   10.975  1.00 9.22   ? 28  SER B C   1 
ATOM   2355 O  O   . SER B  1 28  ? -0.963  4.553   10.444  1.00 10.17  ? 28  SER B O   1 
ATOM   2356 C  CB  . SER B  1 28  ? -3.327  3.413   12.343  1.00 9.76   ? 28  SER B CB  1 
ATOM   2357 O  OG  . SER B  1 28  ? -3.881  3.330   13.648  1.00 10.16  ? 28  SER B OG  1 
ATOM   2358 N  N   . PRO B  1 29  ? -1.121  2.295   10.302  1.00 8.70   ? 29  PRO B N   1 
ATOM   2359 C  CA  . PRO B  1 29  ? -1.454  0.921   10.782  1.00 8.89   ? 29  PRO B CA  1 
ATOM   2360 C  C   . PRO B  1 29  ? -0.301  0.361   11.554  1.00 8.98   ? 29  PRO B C   1 
ATOM   2361 O  O   . PRO B  1 29  ? 0.751   0.990   11.789  1.00 9.55   ? 29  PRO B O   1 
ATOM   2362 C  CB  . PRO B  1 29  ? -1.673  0.227   9.444   1.00 9.17   ? 29  PRO B CB  1 
ATOM   2363 C  CG  . PRO B  1 29  ? -0.556  0.812   8.579   1.00 9.62   ? 29  PRO B CG  1 
ATOM   2364 C  CD  . PRO B  1 29  ? -0.587  2.290   8.947   1.00 9.46   ? 29  PRO B CD  1 
ATOM   2365 N  N   . ILE B  1 30  ? -0.529  -0.864  12.078  1.00 9.46   ? 30  ILE B N   1 
ATOM   2366 C  CA  . ILE B  1 30  ? 0.467   -1.604  12.891  1.00 9.13   ? 30  ILE B CA  1 
ATOM   2367 C  C   . ILE B  1 30  ? 0.489   -3.012  12.459  1.00 9.71   ? 30  ILE B C   1 
ATOM   2368 O  O   . ILE B  1 30  ? -0.413  -3.533  11.794  1.00 10.01  ? 30  ILE B O   1 
ATOM   2369 C  CB  . ILE B  1 30  ? 0.138   -1.457  14.399  1.00 10.66  ? 30  ILE B CB  1 
ATOM   2370 C  CG1 . ILE B  1 30  ? -1.299  -2.031  14.728  1.00 12.24  ? 30  ILE B CG1 1 
ATOM   2371 C  CG2 . ILE B  1 30  ? 0.255   0.000   14.856  1.00 13.07  ? 30  ILE B CG2 1 
ATOM   2372 C  CD1 . ILE B  1 30  ? -1.621  -2.127  16.186  1.00 14.85  ? 30  ILE B CD1 1 
ATOM   2373 N  N   . ASP B  1 31  ? 1.571   -3.720  12.880  1.00 9.75   ? 31  ASP B N   1 
ATOM   2374 C  CA  . ASP B  1 31  ? 1.686   -5.159  12.737  1.00 10.22  ? 31  ASP B CA  1 
ATOM   2375 C  C   . ASP B  1 31  ? 1.043   -5.817  13.894  1.00 10.69  ? 31  ASP B C   1 
ATOM   2376 O  O   . ASP B  1 31  ? 1.444   -5.638  15.055  1.00 13.52  ? 31  ASP B O   1 
ATOM   2377 C  CB  . ASP B  1 31  ? 3.177   -5.517  12.665  1.00 11.58  ? 31  ASP B CB  1 
ATOM   2378 C  CG  . ASP B  1 31  ? 3.302   -7.044  12.524  1.00 12.73  ? 31  ASP B CG  1 
ATOM   2379 O  OD1 . ASP B  1 31  ? 2.763   -7.641  11.568  1.00 13.18  ? 31  ASP B OD1 1 
ATOM   2380 O  OD2 . ASP B  1 31  ? 3.993   -7.585  13.386  1.00 16.37  ? 31  ASP B OD2 1 
ATOM   2381 N  N   . LEU B  1 32  ? 0.118   -6.701  13.665  1.00 11.05  ? 32  LEU B N   1 
ATOM   2382 C  CA  . LEU B  1 32  ? -0.645  -7.425  14.719  1.00 12.54  ? 32  LEU B CA  1 
ATOM   2383 C  C   . LEU B  1 32  ? 0.161   -8.690  14.968  1.00 12.80  ? 32  LEU B C   1 
ATOM   2384 O  O   . LEU B  1 32  ? 0.193   -9.565  14.154  1.00 14.76  ? 32  LEU B O   1 
ATOM   2385 C  CB  . LEU B  1 32  ? -2.047  -7.740  14.170  1.00 13.59  ? 32  LEU B CB  1 
ATOM   2386 C  CG  . LEU B  1 32  ? -2.814  -6.500  13.792  1.00 12.56  ? 32  LEU B CG  1 
ATOM   2387 C  CD1 . LEU B  1 32  ? -4.085  -6.790  13.006  1.00 14.83  ? 32  LEU B CD1 1 
ATOM   2388 C  CD2 . LEU B  1 32  ? -3.117  -5.595  15.015  1.00 17.13  ? 32  LEU B CD2 1 
ATOM   2389 N  N   . HIS B  1 33  ? 0.876   -8.777  16.109  1.00 13.33  ? 33  HIS B N   1 
ATOM   2390 C  CA  . HIS B  1 33  ? 1.762   -9.986  16.358  1.00 13.72  ? 33  HIS B CA  1 
ATOM   2391 C  C   . HIS B  1 33  ? 1.660   -10.252 17.836  1.00 13.70  ? 33  HIS B C   1 
ATOM   2392 O  O   . HIS B  1 33  ? 1.302   -9.438  18.658  1.00 13.66  ? 33  HIS B O   1 
ATOM   2393 C  CB  . HIS B  1 33  ? 3.230   -9.667  15.975  1.00 15.40  ? 33  HIS B CB  1 
ATOM   2394 C  CG  . HIS B  1 33  ? 3.873   -8.499  16.739  1.00 16.24  ? 33  HIS B CG  1 
ATOM   2395 N  ND1 . HIS B  1 33  ? 3.633   -7.200  16.449  1.00 19.58  ? 33  HIS B ND1 1 
ATOM   2396 C  CD2 . HIS B  1 33  ? 4.832   -8.454  17.719  1.00 15.56  ? 33  HIS B CD2 1 
ATOM   2397 C  CE1 . HIS B  1 33  ? 4.307   -6.399  17.276  1.00 21.86  ? 33  HIS B CE1 1 
ATOM   2398 N  NE2 . HIS B  1 33  ? 5.062   -7.136  18.030  1.00 18.86  ? 33  HIS B NE2 1 
ATOM   2399 N  N   . SER B  1 34  ? 2.026   -11.498 18.193  1.00 14.86  ? 34  SER B N   1 
ATOM   2400 C  CA  . SER B  1 34  ? 1.681   -12.132 19.530  1.00 16.60  ? 34  SER B CA  1 
ATOM   2401 C  C   . SER B  1 34  ? 2.149   -11.259 20.668  1.00 14.23  ? 34  SER B C   1 
ATOM   2402 O  O   . SER B  1 34  ? 1.426   -11.132 21.660  1.00 15.63  ? 34  SER B O   1 
ATOM   2403 C  CB  . SER B  1 34  ? 2.189   -13.575 19.554  1.00 21.43  ? 34  SER B CB  1 
ATOM   2404 O  OG  . SER B  1 34  ? 3.614   -13.486 19.558  1.00 22.35  ? 34  SER B OG  1 
ATOM   2405 N  N   . ASP B  1 35  ? 3.356   -10.646 20.604  1.00 15.24  ? 35  ASP B N   1 
ATOM   2406 C  CA  . ASP B  1 35  ? 3.867   -9.954  21.807  1.00 15.11  ? 35  ASP B CA  1 
ATOM   2407 C  C   . ASP B  1 35  ? 3.068   -8.849  22.257  1.00 15.54  ? 35  ASP B C   1 
ATOM   2408 O  O   . ASP B  1 35  ? 3.177   -8.399  23.424  1.00 19.14  ? 35  ASP B O   1 
ATOM   2409 C  CB  . ASP B  1 35  ? 5.301   -9.345  21.503  1.00 17.81  ? 35  ASP B CB  1 
ATOM   2410 C  CG  . ASP B  1 35  ? 6.227   -10.330 20.913  1.00 16.62  ? 35  ASP B CG  1 
ATOM   2411 O  OD1 . ASP B  1 35  ? 5.930   -10.798 19.801  1.00 18.45  ? 35  ASP B OD1 1 
ATOM   2412 O  OD2 . ASP B  1 35  ? 7.235   -10.728 21.587  1.00 19.71  ? 35  ASP B OD2 1 
ATOM   2413 N  N   . ILE B  1 36  ? 2.207   -8.274  21.381  1.00 14.17  ? 36  ILE B N   1 
ATOM   2414 C  CA  . ILE B  1 36  ? 1.475   -7.120  21.747  1.00 14.82  ? 36  ILE B CA  1 
ATOM   2415 C  C   . ILE B  1 36  ? -0.066  -7.360  21.838  1.00 14.20  ? 36  ILE B C   1 
ATOM   2416 O  O   . ILE B  1 36  ? -0.823  -6.368  21.991  1.00 16.39  ? 36  ILE B O   1 
ATOM   2417 C  CB  . ILE B  1 36  ? 1.755   -5.846  20.872  1.00 16.62  ? 36  ILE B CB  1 
ATOM   2418 C  CG1 . ILE B  1 36  ? 1.666   -6.096  19.401  1.00 19.27  ? 36  ILE B CG1 1 
ATOM   2419 C  CG2 . ILE B  1 36  ? 3.200   -5.330  21.146  1.00 21.18  ? 36  ILE B CG2 1 
ATOM   2420 C  CD1 . ILE B  1 36  ? 0.411   -6.307  18.794  1.00 20.20  ? 36  ILE B CD1 1 
ATOM   2421 N  N   . LEU B  1 37  ? -0.460  -8.613  21.733  1.00 13.10  ? 37  LEU B N   1 
ATOM   2422 C  CA  . LEU B  1 37  ? -1.907  -9.003  21.765  1.00 13.53  ? 37  LEU B CA  1 
ATOM   2423 C  C   . LEU B  1 37  ? -2.287  -9.333  23.191  1.00 14.70  ? 37  LEU B C   1 
ATOM   2424 O  O   . LEU B  1 37  ? -1.506  -9.973  23.912  1.00 19.02  ? 37  LEU B O   1 
ATOM   2425 C  CB  . LEU B  1 37  ? -2.173  -10.204 20.866  1.00 14.14  ? 37  LEU B CB  1 
ATOM   2426 C  CG  . LEU B  1 37  ? -1.899  -9.961  19.406  1.00 16.09  ? 37  LEU B CG  1 
ATOM   2427 C  CD1 . LEU B  1 37  ? -2.172  -11.195 18.542  1.00 19.81  ? 37  LEU B CD1 1 
ATOM   2428 C  CD2 . LEU B  1 37  ? -2.683  -8.788  18.809  1.00 17.03  ? 37  LEU B CD2 1 
ATOM   2429 N  N   . GLN B  1 38  ? -3.522  -8.995  23.582  1.00 14.29  ? 38  GLN B N   1 
ATOM   2430 C  CA  . GLN B  1 38  ? -4.044  -9.461  24.857  1.00 15.33  ? 38  GLN B CA  1 
ATOM   2431 C  C   . GLN B  1 38  ? -5.544  -9.673  24.757  1.00 13.49  ? 38  GLN B C   1 
ATOM   2432 O  O   . GLN B  1 38  ? -6.287  -8.790  24.304  1.00 13.31  ? 38  GLN B O   1 
ATOM   2433 C  CB  . GLN B  1 38  ? -3.813  -8.417  25.942  1.00 19.21  ? 38  GLN B CB  1 
ATOM   2434 C  CG  . GLN B  1 38  ? -4.282  -8.842  27.383  1.00 24.39  ? 38  GLN B CG  1 
ATOM   2435 C  CD  . GLN B  1 38  ? -3.875  -7.873  28.372  1.00 28.01  ? 38  GLN B CD  1 
ATOM   2436 O  OE1 . GLN B  1 38  ? -2.684  -7.630  28.491  1.00 46.00  ? 38  GLN B OE1 1 
ATOM   2437 N  NE2 . GLN B  1 38  ? -4.760  -7.393  29.187  1.00 44.75  ? 38  GLN B NE2 1 
ATOM   2438 N  N   . TYR B  1 39  ? -5.996  -10.840 25.144  1.00 12.98  ? 39  TYR B N   1 
ATOM   2439 C  CA  . TYR B  1 39  ? -7.402  -11.107 25.092  1.00 12.68  ? 39  TYR B CA  1 
ATOM   2440 C  C   . TYR B  1 39  ? -8.146  -10.200 26.094  1.00 13.29  ? 39  TYR B C   1 
ATOM   2441 O  O   . TYR B  1 39  ? -7.680  -9.936  27.211  1.00 14.80  ? 39  TYR B O   1 
ATOM   2442 C  CB  . TYR B  1 39  ? -7.591  -12.584 25.541  1.00 15.21  ? 39  TYR B CB  1 
ATOM   2443 C  CG  . TYR B  1 39  ? -9.024  -12.970 25.720  1.00 14.21  ? 39  TYR B CG  1 
ATOM   2444 C  CD1 . TYR B  1 39  ? -9.894  -12.961 24.660  1.00 15.11  ? 39  TYR B CD1 1 
ATOM   2445 C  CD2 . TYR B  1 39  ? -9.503  -13.344 26.963  1.00 16.99  ? 39  TYR B CD2 1 
ATOM   2446 C  CE1 . TYR B  1 39  ? -11.222 -13.323 24.799  1.00 15.50  ? 39  TYR B CE1 1 
ATOM   2447 C  CE2 . TYR B  1 39  ? -10.832 -13.713 27.134  1.00 18.93  ? 39  TYR B CE2 1 
ATOM   2448 C  CZ  . TYR B  1 39  ? -11.677 -13.696 26.041  1.00 17.14  ? 39  TYR B CZ  1 
ATOM   2449 O  OH  . TYR B  1 39  ? -13.006 -14.055 26.170  1.00 19.93  ? 39  TYR B OH  1 
ATOM   2450 N  N   . ASP B  1 40  ? -9.290  -9.730  25.681  1.00 12.55  ? 40  ASP B N   1 
ATOM   2451 C  CA  . ASP B  1 40  ? -10.176 -8.933  26.508  1.00 13.64  ? 40  ASP B CA  1 
ATOM   2452 C  C   . ASP B  1 40  ? -11.555 -9.437  26.375  1.00 13.05  ? 40  ASP B C   1 
ATOM   2453 O  O   . ASP B  1 40  ? -12.230 -9.223  25.340  1.00 13.96  ? 40  ASP B O   1 
ATOM   2454 C  CB  . ASP B  1 40  ? -10.062 -7.436  26.055  1.00 14.62  ? 40  ASP B CB  1 
ATOM   2455 C  CG  . ASP B  1 40  ? -10.862 -6.526  26.882  1.00 17.72  ? 40  ASP B CG  1 
ATOM   2456 O  OD1 . ASP B  1 40  ? -11.667 -6.952  27.699  1.00 18.72  ? 40  ASP B OD1 1 
ATOM   2457 O  OD2 . ASP B  1 40  ? -10.593 -5.260  26.764  1.00 24.20  ? 40  ASP B OD2 1 
ATOM   2458 N  N   . ALA B  1 41  ? -12.084 -10.113 27.420  1.00 14.68  ? 41  ALA B N   1 
ATOM   2459 C  CA  . ALA B  1 41  ? -13.413 -10.672 27.356  1.00 16.45  ? 41  ALA B CA  1 
ATOM   2460 C  C   . ALA B  1 41  ? -14.506 -9.604  27.295  1.00 16.87  ? 41  ALA B C   1 
ATOM   2461 O  O   . ALA B  1 41  ? -15.683 -10.002 26.913  1.00 18.78  ? 41  ALA B O   1 
ATOM   2462 C  CB  . ALA B  1 41  ? -13.608 -11.536 28.616  1.00 19.60  ? 41  ALA B CB  1 
ATOM   2463 N  N   A SER B  1 42  ? -14.224 -8.280  27.526  0.50 14.11  ? 42  SER B N   1 
ATOM   2464 N  N   B SER B  1 42  ? -14.277 -8.320  27.556  0.50 16.47  ? 42  SER B N   1 
ATOM   2465 C  CA  A SER B  1 42  ? -15.189 -7.222  27.356  0.50 13.58  ? 42  SER B CA  1 
ATOM   2466 C  CA  B SER B  1 42  ? -15.340 -7.437  27.394  0.50 18.60  ? 42  SER B CA  1 
ATOM   2467 C  C   A SER B  1 42  ? -15.414 -6.797  25.910  0.50 13.69  ? 42  SER B C   1 
ATOM   2468 C  C   B SER B  1 42  ? -15.629 -7.087  25.930  0.50 16.16  ? 42  SER B C   1 
ATOM   2469 O  O   A SER B  1 42  ? -16.246 -5.910  25.627  0.50 13.68  ? 42  SER B O   1 
ATOM   2470 O  O   B SER B  1 42  ? -16.687 -6.471  25.642  0.50 18.77  ? 42  SER B O   1 
ATOM   2471 C  CB  A SER B  1 42  ? -14.775 -5.979  28.156  0.50 17.67  ? 42  SER B CB  1 
ATOM   2472 C  CB  B SER B  1 42  ? -14.954 -6.211  28.154  0.50 30.67  ? 42  SER B CB  1 
ATOM   2473 O  OG  A SER B  1 42  ? -13.848 -5.203  27.520  0.50 17.63  ? 42  SER B OG  1 
ATOM   2474 O  OG  B SER B  1 42  ? -14.841 -6.663  29.503  0.50 25.82  ? 42  SER B OG  1 
ATOM   2475 N  N   . LEU B  1 43  ? -14.710 -7.443  24.997  1.00 13.90  ? 43  LEU B N   1 
ATOM   2476 C  CA  . LEU B  1 43  ? -14.894 -7.130  23.538  1.00 14.77  ? 43  LEU B CA  1 
ATOM   2477 C  C   . LEU B  1 43  ? -15.966 -7.986  22.975  1.00 14.49  ? 43  LEU B C   1 
ATOM   2478 O  O   . LEU B  1 43  ? -15.737 -9.084  22.358  1.00 15.82  ? 43  LEU B O   1 
ATOM   2479 C  CB  . LEU B  1 43  ? -13.598 -7.287  22.844  1.00 13.24  ? 43  LEU B CB  1 
ATOM   2480 C  CG  . LEU B  1 43  ? -12.530 -6.288  23.184  1.00 13.09  ? 43  LEU B CG  1 
ATOM   2481 C  CD1 . LEU B  1 43  ? -11.269 -6.630  22.420  1.00 15.56  ? 43  LEU B CD1 1 
ATOM   2482 C  CD2 . LEU B  1 43  ? -12.920 -4.884  22.928  1.00 15.15  ? 43  LEU B CD2 1 
ATOM   2483 N  N   . THR B  1 44  ? -17.219 -7.550  23.198  1.00 15.06  ? 44  THR B N   1 
ATOM   2484 C  CA  . THR B  1 44  ? -18.399 -8.329  22.796  1.00 16.70  ? 44  THR B CA  1 
ATOM   2485 C  C   . THR B  1 44  ? -18.750 -8.071  21.313  1.00 14.55  ? 44  THR B C   1 
ATOM   2486 O  O   . THR B  1 44  ? -18.162 -7.187  20.661  1.00 14.14  ? 44  THR B O   1 
ATOM   2487 C  CB  . THR B  1 44  ? -19.597 -7.927  23.717  1.00 19.69  ? 44  THR B CB  1 
ATOM   2488 O  OG1 . THR B  1 44  ? -19.610 -6.513  23.810  1.00 23.33  ? 44  THR B OG1 1 
ATOM   2489 C  CG2 . THR B  1 44  ? -19.277 -8.401  25.171  1.00 21.42  ? 44  THR B CG2 1 
ATOM   2490 N  N   . PRO B  1 45  ? -19.615 -8.850  20.714  1.00 14.85  ? 45  PRO B N   1 
ATOM   2491 C  CA  . PRO B  1 45  ? -19.858 -8.710  19.237  1.00 15.30  ? 45  PRO B CA  1 
ATOM   2492 C  C   . PRO B  1 45  ? -20.448 -7.392  18.818  1.00 14.26  ? 45  PRO B C   1 
ATOM   2493 O  O   . PRO B  1 45  ? -21.336 -6.879  19.505  1.00 18.07  ? 45  PRO B O   1 
ATOM   2494 C  CB  . PRO B  1 45  ? -20.778 -9.896  18.903  1.00 18.63  ? 45  PRO B CB  1 
ATOM   2495 C  CG  . PRO B  1 45  ? -20.466 -10.866 20.037  1.00 18.28  ? 45  PRO B CG  1 
ATOM   2496 C  CD  . PRO B  1 45  ? -20.342 -9.987  21.244  1.00 19.22  ? 45  PRO B CD  1 
ATOM   2497 N  N   . LEU B  1 46  ? -20.012 -6.863  17.682  1.00 13.39  ? 46  LEU B N   1 
ATOM   2498 C  CA  . LEU B  1 46  ? -20.692 -5.763  17.091  1.00 13.30  ? 46  LEU B CA  1 
ATOM   2499 C  C   . LEU B  1 46  ? -21.913 -6.180  16.277  1.00 12.83  ? 46  LEU B C   1 
ATOM   2500 O  O   . LEU B  1 46  ? -21.924 -7.286  15.762  1.00 14.56  ? 46  LEU B O   1 
ATOM   2501 C  CB  . LEU B  1 46  ? -19.705 -4.983  16.205  1.00 14.78  ? 46  LEU B CB  1 
ATOM   2502 C  CG  . LEU B  1 46  ? -18.458 -4.386  16.947  1.00 17.03  ? 46  LEU B CG  1 
ATOM   2503 C  CD1 . LEU B  1 46  ? -17.563 -3.771  15.820  1.00 18.37  ? 46  LEU B CD1 1 
ATOM   2504 C  CD2 . LEU B  1 46  ? -18.906 -3.399  18.030  1.00 20.83  ? 46  LEU B CD2 1 
ATOM   2505 N  N   . GLU B  1 47  ? -22.874 -5.275  16.178  1.00 13.56  ? 47  GLU B N   1 
ATOM   2506 C  CA  . GLU B  1 47  ? -24.004 -5.516  15.302  1.00 14.74  ? 47  GLU B CA  1 
ATOM   2507 C  C   . GLU B  1 47  ? -23.996 -4.394  14.200  1.00 13.35  ? 47  GLU B C   1 
ATOM   2508 O  O   . GLU B  1 47  ? -23.725 -3.227  14.523  1.00 15.73  ? 47  GLU B O   1 
ATOM   2509 C  CB  . GLU B  1 47  ? -25.315 -5.419  16.136  1.00 17.79  ? 47  GLU B CB  1 
ATOM   2510 C  CG  . GLU B  1 47  ? -25.313 -6.533  17.234  1.00 23.36  ? 47  GLU B CG  1 
ATOM   2511 C  CD  . GLU B  1 47  ? -26.472 -6.450  18.193  1.00 30.01  ? 47  GLU B CD  1 
ATOM   2512 O  OE1 . GLU B  1 47  ? -26.214 -6.326  19.436  1.00 50.91  ? 47  GLU B OE1 1 
ATOM   2513 O  OE2 . GLU B  1 47  ? -27.613 -6.561  17.833  1.00 40.31  ? 47  GLU B OE2 1 
ATOM   2514 N  N   . PHE B  1 48  ? -24.290 -4.819  13.009  1.00 12.85  ? 48  PHE B N   1 
ATOM   2515 C  CA  . PHE B  1 48  ? -24.186 -3.940  11.826  1.00 12.91  ? 48  PHE B CA  1 
ATOM   2516 C  C   . PHE B  1 48  ? -25.600 -3.603  11.408  1.00 13.18  ? 48  PHE B C   1 
ATOM   2517 O  O   . PHE B  1 48  ? -26.293 -4.526  10.933  1.00 16.76  ? 48  PHE B O   1 
ATOM   2518 C  CB  . PHE B  1 48  ? -23.381 -4.674  10.754  1.00 14.86  ? 48  PHE B CB  1 
ATOM   2519 C  CG  . PHE B  1 48  ? -22.047 -5.161  11.295  1.00 13.51  ? 48  PHE B CG  1 
ATOM   2520 C  CD1 . PHE B  1 48  ? -21.049 -4.290  11.705  1.00 15.77  ? 48  PHE B CD1 1 
ATOM   2521 C  CD2 . PHE B  1 48  ? -21.877 -6.547  11.455  1.00 14.86  ? 48  PHE B CD2 1 
ATOM   2522 C  CE1 . PHE B  1 48  ? -19.864 -4.828  12.321  1.00 14.85  ? 48  PHE B CE1 1 
ATOM   2523 C  CE2 . PHE B  1 48  ? -20.758 -7.099  12.085  1.00 15.42  ? 48  PHE B CE2 1 
ATOM   2524 C  CZ  . PHE B  1 48  ? -19.795 -6.223  12.484  1.00 14.97  ? 48  PHE B CZ  1 
ATOM   2525 N  N   . GLN B  1 49  ? -26.006 -2.379  11.601  1.00 13.16  ? 49  GLN B N   1 
ATOM   2526 C  CA  . GLN B  1 49  ? -27.409 -1.988  11.381  1.00 13.98  ? 49  GLN B CA  1 
ATOM   2527 C  C   . GLN B  1 49  ? -27.526 -1.103  10.168  1.00 12.89  ? 49  GLN B C   1 
ATOM   2528 O  O   . GLN B  1 49  ? -26.713 -0.176  9.975   1.00 13.09  ? 49  GLN B O   1 
ATOM   2529 C  CB  . GLN B  1 49  ? -27.905 -1.209  12.631  1.00 16.54  ? 49  GLN B CB  1 
ATOM   2530 C  CG  . GLN B  1 49  ? -27.729 -1.983  13.922  1.00 18.98  ? 49  GLN B CG  1 
ATOM   2531 C  CD  . GLN B  1 49  ? -28.543 -3.281  13.941  1.00 20.91  ? 49  GLN B CD  1 
ATOM   2532 O  OE1 . GLN B  1 49  ? -28.009 -4.405  14.160  1.00 31.36  ? 49  GLN B OE1 1 
ATOM   2533 N  NE2 . GLN B  1 49  ? -29.840 -3.182  13.746  1.00 26.98  ? 49  GLN B NE2 1 
ATOM   2534 N  N   . GLY B  1 50  ? -28.524 -1.363  9.330   1.00 14.22  ? 50  GLY B N   1 
ATOM   2535 C  CA  . GLY B  1 50  ? -28.760 -0.509  8.154   1.00 14.19  ? 50  GLY B CA  1 
ATOM   2536 C  C   . GLY B  1 50  ? -27.641 -0.699  7.118   1.00 12.64  ? 50  GLY B C   1 
ATOM   2537 O  O   . GLY B  1 50  ? -27.495 0.150   6.268   1.00 14.39  ? 50  GLY B O   1 
ATOM   2538 N  N   . TYR B  1 51  ? -26.922 -1.826  7.167   1.00 12.12  ? 51  TYR B N   1 
ATOM   2539 C  CA  . TYR B  1 51  ? -25.918 -2.094  6.142   1.00 12.12  ? 51  TYR B CA  1 
ATOM   2540 C  C   . TYR B  1 51  ? -26.483 -2.670  4.829   1.00 11.63  ? 51  TYR B C   1 
ATOM   2541 O  O   . TYR B  1 51  ? -25.821 -2.646  3.828   1.00 11.42  ? 51  TYR B O   1 
ATOM   2542 C  CB  . TYR B  1 51  ? -24.892 -3.156  6.681   1.00 11.44  ? 51  TYR B CB  1 
ATOM   2543 C  CG  . TYR B  1 51  ? -23.758 -2.620  7.513   1.00 10.55  ? 51  TYR B CG  1 
ATOM   2544 C  CD1 . TYR B  1 51  ? -23.945 -1.696  8.506   1.00 11.55  ? 51  TYR B CD1 1 
ATOM   2545 C  CD2 . TYR B  1 51  ? -22.422 -3.093  7.250   1.00 10.61  ? 51  TYR B CD2 1 
ATOM   2546 C  CE1 . TYR B  1 51  ? -22.875 -1.143  9.229   1.00 11.36  ? 51  TYR B CE1 1 
ATOM   2547 C  CE2 . TYR B  1 51  ? -21.375 -2.561  8.013   1.00 10.85  ? 51  TYR B CE2 1 
ATOM   2548 C  CZ  . TYR B  1 51  ? -21.566 -1.606  8.914   1.00 11.50  ? 51  TYR B CZ  1 
ATOM   2549 O  OH  . TYR B  1 51  ? -20.462 -1.100  9.599   1.00 13.30  ? 51  TYR B OH  1 
ATOM   2550 N  N   . ASN B  1 52  ? -27.766 -3.109  4.885   1.00 12.72  ? 52  ASN B N   1 
ATOM   2551 C  CA  . ASN B  1 52  ? -28.361 -3.649  3.660   1.00 12.61  ? 52  ASN B CA  1 
ATOM   2552 C  C   . ASN B  1 52  ? -28.989 -2.512  2.897   1.00 13.42  ? 52  ASN B C   1 
ATOM   2553 O  O   . ASN B  1 52  ? -30.145 -2.148  3.066   1.00 17.02  ? 52  ASN B O   1 
ATOM   2554 C  CB  . ASN B  1 52  ? -29.414 -4.750  4.038   1.00 15.25  ? 52  ASN B CB  1 
ATOM   2555 C  CG  . ASN B  1 52  ? -29.894 -5.474  2.858   1.00 19.14  ? 52  ASN B CG  1 
ATOM   2556 O  OD1 . ASN B  1 52  ? -29.571 -5.215  1.755   1.00 29.18  ? 52  ASN B OD1 1 
ATOM   2557 N  ND2 . ASN B  1 52  ? -30.941 -6.238  3.050   1.00 25.98  ? 52  ASN B ND2 1 
ATOM   2558 N  N   . LEU B  1 53  ? -28.170 -1.869  2.098   1.00 12.23  ? 53  LEU B N   1 
ATOM   2559 C  CA  . LEU B  1 53  ? -28.629 -0.608  1.424   1.00 12.76  ? 53  LEU B CA  1 
ATOM   2560 C  C   . LEU B  1 53  ? -29.547 -1.025  0.235   1.00 11.80  ? 53  LEU B C   1 
ATOM   2561 O  O   . LEU B  1 53  ? -29.329 -2.021  -0.481  1.00 14.30  ? 53  LEU B O   1 
ATOM   2562 C  CB  . LEU B  1 53  ? -27.414 0.098   0.791   1.00 12.41  ? 53  LEU B CB  1 
ATOM   2563 C  CG  . LEU B  1 53  ? -26.351 0.469   1.818   1.00 13.94  ? 53  LEU B CG  1 
ATOM   2564 C  CD1 . LEU B  1 53  ? -25.197 1.167   1.008   1.00 16.61  ? 53  LEU B CD1 1 
ATOM   2565 C  CD2 . LEU B  1 53  ? -26.877 1.327   2.982   1.00 18.59  ? 53  LEU B CD2 1 
ATOM   2566 N  N   . SER B  1 54  ? -30.587 -0.235  0.041   1.00 12.48  ? 54  SER B N   1 
ATOM   2567 C  CA  . SER B  1 54  ? -31.554 -0.589  -0.998  1.00 14.82  ? 54  SER B CA  1 
ATOM   2568 C  C   . SER B  1 54  ? -30.929 -0.565  -2.381  1.00 13.10  ? 54  SER B C   1 
ATOM   2569 O  O   . SER B  1 54  ? -30.298 0.461   -2.760  1.00 13.24  ? 54  SER B O   1 
ATOM   2570 C  CB  . SER B  1 54  ? -32.685 0.364   -0.933  1.00 15.22  ? 54  SER B CB  1 
ATOM   2571 O  OG  . SER B  1 54  ? -33.560 0.093   -2.052  1.00 16.45  ? 54  SER B OG  1 
ATOM   2572 N  N   . ALA B  1 55  ? -31.144 -1.634  -3.198  1.00 14.79  ? 55  ALA B N   1 
ATOM   2573 C  CA  . ALA B  1 55  ? -30.698 -1.711  -4.601  1.00 15.45  ? 55  ALA B CA  1 
ATOM   2574 C  C   . ALA B  1 55  ? -31.399 -0.684  -5.472  1.00 14.71  ? 55  ALA B C   1 
ATOM   2575 O  O   . ALA B  1 55  ? -30.945 -0.452  -6.576  1.00 17.08  ? 55  ALA B O   1 
ATOM   2576 C  CB  . ALA B  1 55  ? -30.881 -3.094  -5.215  1.00 20.63  ? 55  ALA B CB  1 
ATOM   2577 N  N   . ASN B  1 56  ? -32.487 -0.057  -4.984  1.00 14.17  ? 56  ASN B N   1 
ATOM   2578 C  CA  . ASN B  1 56  ? -33.194 0.913   -5.775  1.00 15.24  ? 56  ASN B CA  1 
ATOM   2579 C  C   . ASN B  1 56  ? -32.687 2.320   -5.470  1.00 14.80  ? 56  ASN B C   1 
ATOM   2580 O  O   . ASN B  1 56  ? -33.103 3.285   -6.127  1.00 18.35  ? 56  ASN B O   1 
ATOM   2581 C  CB  . ASN B  1 56  ? -34.676 0.857   -5.508  1.00 16.27  ? 56  ASN B CB  1 
ATOM   2582 C  CG  . ASN B  1 56  ? -35.319 -0.484  -5.936  1.00 19.35  ? 56  ASN B CG  1 
ATOM   2583 O  OD1 . ASN B  1 56  ? -34.780 -1.196  -6.754  1.00 20.54  ? 56  ASN B OD1 1 
ATOM   2584 N  ND2 . ASN B  1 56  ? -36.394 -0.836  -5.375  1.00 31.65  ? 56  ASN B ND2 1 
ATOM   2585 N  N   . LYS B  1 57  ? -31.781 2.478   -4.509  1.00 13.70  ? 57  LYS B N   1 
ATOM   2586 C  CA  . LYS B  1 57  ? -31.119 3.714   -4.216  1.00 13.49  ? 57  LYS B CA  1 
ATOM   2587 C  C   . LYS B  1 57  ? -29.675 3.662   -4.777  1.00 12.85  ? 57  LYS B C   1 
ATOM   2588 O  O   . LYS B  1 57  ? -29.211 2.579   -5.167  1.00 13.90  ? 57  LYS B O   1 
ATOM   2589 C  CB  . LYS B  1 57  ? -31.087 3.973   -2.692  1.00 16.12  ? 57  LYS B CB  1 
ATOM   2590 C  CG  . LYS B  1 57  ? -32.479 4.148   -2.129  1.00 19.97  ? 57  LYS B CG  1 
ATOM   2591 C  CD  . LYS B  1 57  ? -32.385 4.518   -0.568  1.00 30.37  ? 57  LYS B CD  1 
ATOM   2592 C  CE  . LYS B  1 57  ? -33.387 5.503   -0.141  1.00 43.89  ? 57  LYS B CE  1 
ATOM   2593 N  NZ  . LYS B  1 57  ? -33.404 6.732   -1.024  1.00 47.69  ? 57  LYS B NZ  1 
ATOM   2594 N  N   . GLN B  1 58  ? -29.056 4.846   -4.869  1.00 14.04  ? 58  GLN B N   1 
ATOM   2595 C  CA  . GLN B  1 58  ? -27.651 4.991   -5.427  1.00 14.45  ? 58  GLN B CA  1 
ATOM   2596 C  C   . GLN B  1 58  ? -26.832 5.651   -4.378  1.00 13.15  ? 58  GLN B C   1 
ATOM   2597 O  O   . GLN B  1 58  ? -27.297 6.543   -3.712  1.00 14.56  ? 58  GLN B O   1 
ATOM   2598 C  CB  . GLN B  1 58  ? -27.534 5.436   -6.856  1.00 19.22  ? 58  GLN B CB  1 
ATOM   2599 C  CG  . GLN B  1 58  ? -28.515 6.495   -7.188  1.00 27.68  ? 58  GLN B CG  1 
ATOM   2600 C  CD  . GLN B  1 58  ? -28.565 6.714   -8.667  1.00 33.75  ? 58  GLN B CD  1 
ATOM   2601 O  OE1 . GLN B  1 58  ? -28.202 5.839   -9.450  1.00 29.21  ? 58  GLN B OE1 1 
ATOM   2602 N  NE2 . GLN B  1 58  ? -29.009 7.891   -9.051  1.00 36.69  ? 58  GLN B NE2 1 
ATOM   2603 N  N   . PHE B  1 59  ? -25.544 5.350   -4.474  1.00 11.99  ? 59  PHE B N   1 
ATOM   2604 C  CA  . PHE B  1 59  ? -24.568 5.863   -3.513  1.00 11.68  ? 59  PHE B CA  1 
ATOM   2605 C  C   . PHE B  1 59  ? -23.343 6.325   -4.308  1.00 10.94  ? 59  PHE B C   1 
ATOM   2606 O  O   . PHE B  1 59  ? -22.942 5.717   -5.288  1.00 11.99  ? 59  PHE B O   1 
ATOM   2607 C  CB  . PHE B  1 59  ? -24.219 4.765   -2.507  1.00 12.16  ? 59  PHE B CB  1 
ATOM   2608 C  CG  . PHE B  1 59  ? -25.437 4.401   -1.744  1.00 11.24  ? 59  PHE B CG  1 
ATOM   2609 C  CD1 . PHE B  1 59  ? -26.304 3.405   -2.224  1.00 12.69  ? 59  PHE B CD1 1 
ATOM   2610 C  CD2 . PHE B  1 59  ? -25.773 5.089   -0.583  1.00 12.57  ? 59  PHE B CD2 1 
ATOM   2611 C  CE1 . PHE B  1 59  ? -27.525 3.178   -1.553  1.00 12.56  ? 59  PHE B CE1 1 
ATOM   2612 C  CE2 . PHE B  1 59  ? -26.988 4.871   0.101   1.00 13.80  ? 59  PHE B CE2 1 
ATOM   2613 C  CZ  . PHE B  1 59  ? -27.822 3.896   -0.421  1.00 13.56  ? 59  PHE B CZ  1 
ATOM   2614 N  N   . LEU B  1 60  ? -22.801 7.462   -3.885  1.00 11.14  ? 60  LEU B N   1 
ATOM   2615 C  CA  . LEU B  1 60  ? -21.766 8.099   -4.734  1.00 11.41  ? 60  LEU B CA  1 
ATOM   2616 C  C   . LEU B  1 60  ? -20.399 7.531   -4.482  1.00 10.49  ? 60  LEU B C   1 
ATOM   2617 O  O   . LEU B  1 60  ? -19.898 7.513   -3.345  1.00 11.85  ? 60  LEU B O   1 
ATOM   2618 C  CB  . LEU B  1 60  ? -21.722 9.593   -4.288  1.00 13.68  ? 60  LEU B CB  1 
ATOM   2619 C  CG  . LEU B  1 60  ? -20.929 10.519  -5.183  1.00 18.52  ? 60  LEU B CG  1 
ATOM   2620 C  CD1 . LEU B  1 60  ? -21.650 10.649  -6.536  1.00 21.81  ? 60  LEU B CD1 1 
ATOM   2621 C  CD2 . LEU B  1 60  ? -20.809 11.879  -4.570  1.00 25.68  ? 60  LEU B CD2 1 
ATOM   2622 N  N   . LEU B  1 61  ? -19.765 7.075   -5.570  1.00 11.46  ? 61  LEU B N   1 
ATOM   2623 C  CA  . LEU B  1 61  ? -18.449 6.565   -5.648  1.00 11.72  ? 61  LEU B CA  1 
ATOM   2624 C  C   . LEU B  1 61  ? -17.524 7.692   -6.159  1.00 11.72  ? 61  LEU B C   1 
ATOM   2625 O  O   . LEU B  1 61  ? -17.885 8.308   -7.187  1.00 14.58  ? 61  LEU B O   1 
ATOM   2626 C  CB  . LEU B  1 61  ? -18.370 5.354   -6.584  1.00 12.82  ? 61  LEU B CB  1 
ATOM   2627 C  CG  . LEU B  1 61  ? -17.124 4.560   -6.556  1.00 13.17  ? 61  LEU B CG  1 
ATOM   2628 C  CD1 . LEU B  1 61  ? -16.978 3.732   -5.224  1.00 15.70  ? 61  LEU B CD1 1 
ATOM   2629 C  CD2 . LEU B  1 61  ? -17.060 3.588   -7.734  1.00 16.04  ? 61  LEU B CD2 1 
ATOM   2630 N  N   . THR B  1 62  ? -16.384 7.943   -5.523  1.00 11.45  ? 62  THR B N   1 
ATOM   2631 C  CA  . THR B  1 62  ? -15.543 9.063   -5.996  1.00 13.83  ? 62  THR B CA  1 
ATOM   2632 C  C   . THR B  1 62  ? -14.065 8.559   -5.933  1.00 12.83  ? 62  THR B C   1 
ATOM   2633 O  O   . THR B  1 62  ? -13.613 7.858   -4.967  1.00 14.68  ? 62  THR B O   1 
ATOM   2634 C  CB  . THR B  1 62  ? -15.612 10.214  -4.961  1.00 20.37  ? 62  THR B CB  1 
ATOM   2635 O  OG1 . THR B  1 62  ? -16.952 10.657  -4.764  1.00 21.17  ? 62  THR B OG1 1 
ATOM   2636 C  CG2 . THR B  1 62  ? -14.743 11.415  -5.467  1.00 24.46  ? 62  THR B CG2 1 
ATOM   2637 N  N   . ASN B  1 63  ? -13.250 9.018   -6.897  1.00 12.82  ? 63  ASN B N   1 
ATOM   2638 C  CA  . ASN B  1 63  ? -11.811 8.969   -6.820  1.00 12.94  ? 63  ASN B CA  1 
ATOM   2639 C  C   . ASN B  1 63  ? -11.305 10.212  -6.201  1.00 12.49  ? 63  ASN B C   1 
ATOM   2640 O  O   . ASN B  1 63  ? -11.556 11.320  -6.765  1.00 13.12  ? 63  ASN B O   1 
ATOM   2641 C  CB  . ASN B  1 63  ? -11.275 8.806   -8.239  1.00 13.83  ? 63  ASN B CB  1 
ATOM   2642 C  CG  . ASN B  1 63  ? -9.789  8.841   -8.333  1.00 11.93  ? 63  ASN B CG  1 
ATOM   2643 O  OD1 . ASN B  1 63  ? -9.106  9.401   -7.475  1.00 13.84  ? 63  ASN B OD1 1 
ATOM   2644 N  ND2 . ASN B  1 63  ? -9.287  8.241   -9.396  1.00 13.84  ? 63  ASN B ND2 1 
ATOM   2645 N  N   . ASN B  1 64  ? -10.824 10.132  -4.999  1.00 12.21  ? 64  ASN B N   1 
ATOM   2646 C  CA  . ASN B  1 64  ? -10.425 11.330  -4.312  1.00 13.89  ? 64  ASN B CA  1 
ATOM   2647 C  C   . ASN B  1 64  ? -8.907  11.646  -4.454  1.00 13.94  ? 64  ASN B C   1 
ATOM   2648 O  O   . ASN B  1 64  ? -8.360  12.514  -3.717  1.00 15.13  ? 64  ASN B O   1 
ATOM   2649 C  CB  . ASN B  1 64  ? -10.823 11.246  -2.781  1.00 14.19  ? 64  ASN B CB  1 
ATOM   2650 C  CG  . ASN B  1 64  ? -10.071 10.181  -2.062  1.00 14.59  ? 64  ASN B CG  1 
ATOM   2651 O  OD1 . ASN B  1 64  ? -9.105  9.564   -2.580  1.00 14.01  ? 64  ASN B OD1 1 
ATOM   2652 N  ND2 . ASN B  1 64  ? -10.488 9.878   -0.836  1.00 18.65  ? 64  ASN B ND2 1 
ATOM   2653 N  N   . GLY B  1 65  ? -8.238  11.012  -5.405  1.00 13.52  ? 65  GLY B N   1 
ATOM   2654 C  CA  . GLY B  1 65  ? -6.819  11.251  -5.645  1.00 14.56  ? 65  GLY B CA  1 
ATOM   2655 C  C   . GLY B  1 65  ? -5.955  10.342  -4.785  1.00 13.42  ? 65  GLY B C   1 
ATOM   2656 O  O   . GLY B  1 65  ? -4.738  10.411  -4.964  1.00 18.54  ? 65  GLY B O   1 
ATOM   2657 N  N   . HIS B  1 66  ? -6.515  9.599   -3.831  1.00 12.85  ? 66  HIS B N   1 
ATOM   2658 C  CA  . HIS B  1 66  ? -5.736  8.725   -2.922  1.00 13.76  ? 66  HIS B CA  1 
ATOM   2659 C  C   . HIS B  1 66  ? -6.277  7.352   -2.744  1.00 12.52  ? 66  HIS B C   1 
ATOM   2660 O  O   . HIS B  1 66  ? -5.501  6.443   -2.397  1.00 13.69  ? 66  HIS B O   1 
ATOM   2661 C  CB  . HIS B  1 66  ? -5.595  9.366   -1.568  1.00 15.83  ? 66  HIS B CB  1 
ATOM   2662 C  CG  . HIS B  1 66  ? -5.067  10.788  -1.632  1.00 14.75  ? 66  HIS B CG  1 
ATOM   2663 N  ND1 . HIS B  1 66  ? -3.707  11.105  -1.849  1.00 16.67  ? 66  HIS B ND1 1 
ATOM   2664 C  CD2 . HIS B  1 66  ? -5.705  11.921  -1.497  1.00 15.67  ? 66  HIS B CD2 1 
ATOM   2665 C  CE1 . HIS B  1 66  ? -3.586  12.434  -1.840  1.00 14.45  ? 66  HIS B CE1 1 
ATOM   2666 N  NE2 . HIS B  1 66  ? -4.814  12.928  -1.638  1.00 17.39  ? 66  HIS B NE2 1 
ATOM   2667 N  N   . SER B  1 67  ? -7.574  7.151   -3.049  1.00 12.29  ? 67  SER B N   1 
ATOM   2668 C  CA  . SER B  1 67  ? -8.254  5.838   -3.005  1.00 11.86  ? 67  SER B CA  1 
ATOM   2669 C  C   . SER B  1 67  ? -9.508  6.011   -3.811  1.00 11.57  ? 67  SER B C   1 
ATOM   2670 O  O   . SER B  1 67  ? -9.751  7.074   -4.434  1.00 12.78  ? 67  SER B O   1 
ATOM   2671 C  CB  . SER B  1 67  ? -8.556  5.548   -1.528  1.00 12.43  ? 67  SER B CB  1 
ATOM   2672 O  OG  . SER B  1 67  ? -9.165  4.220   -1.416  1.00 12.29  ? 67  SER B OG  1 
ATOM   2673 N  N   . VAL B  1 68  ? -10.310 4.963   -3.840  1.00 11.83  ? 68  VAL B N   1 
ATOM   2674 C  CA  . VAL B  1 68  ? -11.665 5.056   -4.315  1.00 11.94  ? 68  VAL B CA  1 
ATOM   2675 C  C   . VAL B  1 68  ? -12.551 4.936   -3.046  1.00 10.99  ? 68  VAL B C   1 
ATOM   2676 O  O   . VAL B  1 68  ? -12.358 3.994   -2.279  1.00 11.85  ? 68  VAL B O   1 
ATOM   2677 C  CB  . VAL B  1 68  ? -11.977 3.988   -5.387  1.00 13.91  ? 68  VAL B CB  1 
ATOM   2678 C  CG1 . VAL B  1 68  ? -11.720 2.504   -4.929  1.00 14.84  ? 68  VAL B CG1 1 
ATOM   2679 C  CG2 . VAL B  1 68  ? -13.335 4.189   -5.959  1.00 18.54  ? 68  VAL B CG2 1 
ATOM   2680 N  N   . LYS B  1 69  ? -13.484 5.882   -2.942  1.00 12.51  ? 69  LYS B N   1 
ATOM   2681 C  CA  . LYS B  1 69  ? -14.379 5.859   -1.799  1.00 11.81  ? 69  LYS B CA  1 
ATOM   2682 C  C   . LYS B  1 69  ? -15.876 5.889   -2.173  1.00 10.15  ? 69  LYS B C   1 
ATOM   2683 O  O   . LYS B  1 69  ? -16.280 6.499   -3.143  1.00 12.89  ? 69  LYS B O   1 
ATOM   2684 C  CB  . LYS B  1 69  ? -14.062 7.014   -0.857  1.00 16.90  ? 69  LYS B CB  1 
ATOM   2685 C  CG  . LYS B  1 69  ? -14.661 8.332   -1.306  1.00 23.19  ? 69  LYS B CG  1 
ATOM   2686 C  CD  . LYS B  1 69  ? -14.582 9.377   -0.211  1.00 26.53  ? 69  LYS B CD  1 
ATOM   2687 C  CE  . LYS B  1 69  ? -14.922 10.751  -0.762  1.00 25.26  ? 69  LYS B CE  1 
ATOM   2688 N  NZ  . LYS B  1 69  ? -14.820 11.796  0.292   1.00 28.45  ? 69  LYS B NZ  1 
ATOM   2689 N  N   . LEU B  1 70  ? -16.633 5.160   -1.384  1.00 9.98   ? 70  LEU B N   1 
ATOM   2690 C  CA  . LEU B  1 70  ? -18.102 5.053   -1.557  1.00 9.40   ? 70  LEU B CA  1 
ATOM   2691 C  C   . LEU B  1 70  ? -18.699 5.793   -0.377  1.00 9.63   ? 70  LEU B C   1 
ATOM   2692 O  O   . LEU B  1 70  ? -18.432 5.465   0.801   1.00 9.92   ? 70  LEU B O   1 
ATOM   2693 C  CB  . LEU B  1 70  ? -18.531 3.602   -1.533  1.00 9.99   ? 70  LEU B CB  1 
ATOM   2694 C  CG  . LEU B  1 70  ? -20.028 3.366   -1.754  1.00 10.82  ? 70  LEU B CG  1 
ATOM   2695 C  CD1 . LEU B  1 70  ? -20.487 3.827   -3.137  1.00 12.71  ? 70  LEU B CD1 1 
ATOM   2696 C  CD2 . LEU B  1 70  ? -20.393 1.934   -1.530  1.00 12.85  ? 70  LEU B CD2 1 
ATOM   2697 N  N   . ASN B  1 71  ? -19.533 6.805   -0.651  1.00 10.06  ? 71  ASN B N   1 
ATOM   2698 C  CA  . ASN B  1 71  ? -20.252 7.519   0.467   1.00 11.12  ? 71  ASN B CA  1 
ATOM   2699 C  C   . ASN B  1 71  ? -21.351 6.611   1.002   1.00 11.89  ? 71  ASN B C   1 
ATOM   2700 O  O   . ASN B  1 71  ? -22.024 5.886   0.246   1.00 14.51  ? 71  ASN B O   1 
ATOM   2701 C  CB  . ASN B  1 71  ? -20.872 8.810   -0.078  1.00 13.97  ? 71  ASN B CB  1 
ATOM   2702 C  CG  . ASN B  1 71  ? -19.887 9.836   -0.315  1.00 17.06  ? 71  ASN B CG  1 
ATOM   2703 O  OD1 . ASN B  1 71  ? -18.690 9.741   -0.015  1.00 21.01  ? 71  ASN B OD1 1 
ATOM   2704 N  ND2 . ASN B  1 71  ? -20.455 11.036  -0.717  1.00 23.99  ? 71  ASN B ND2 1 
ATOM   2705 N  N   . LEU B  1 72  ? -21.527 6.629   2.294   1.00 11.31  ? 72  LEU B N   1 
ATOM   2706 C  CA  . LEU B  1 72  ? -22.488 5.777   2.984   1.00 10.78  ? 72  LEU B CA  1 
ATOM   2707 C  C   . LEU B  1 72  ? -23.469 6.654   3.764   1.00 12.22  ? 72  LEU B C   1 
ATOM   2708 O  O   . LEU B  1 72  ? -23.106 7.770   4.228   1.00 13.93  ? 72  LEU B O   1 
ATOM   2709 C  CB  . LEU B  1 72  ? -21.747 4.855   3.955   1.00 10.92  ? 72  LEU B CB  1 
ATOM   2710 C  CG  . LEU B  1 72  ? -20.803 3.849   3.231   1.00 11.18  ? 72  LEU B CG  1 
ATOM   2711 C  CD1 . LEU B  1 72  ? -19.920 3.169   4.291   1.00 10.79  ? 72  LEU B CD1 1 
ATOM   2712 C  CD2 . LEU B  1 72  ? -21.530 2.851   2.368   1.00 11.65  ? 72  LEU B CD2 1 
ATOM   2713 N  N   . PRO B  1 73  ? -24.724 6.146   3.945   1.00 11.34  ? 73  PRO B N   1 
ATOM   2714 C  CA  . PRO B  1 73  ? -25.730 6.962   4.582   1.00 13.74  ? 73  PRO B CA  1 
ATOM   2715 C  C   . PRO B  1 73  ? -25.589 6.867   6.137   1.00 14.48  ? 73  PRO B C   1 
ATOM   2716 O  O   . PRO B  1 73  ? -25.172 5.853   6.686   1.00 14.83  ? 73  PRO B O   1 
ATOM   2717 C  CB  . PRO B  1 73  ? -27.028 6.311   4.113   1.00 15.12  ? 73  PRO B CB  1 
ATOM   2718 C  CG  . PRO B  1 73  ? -26.652 4.815   3.971   1.00 14.07  ? 73  PRO B CG  1 
ATOM   2719 C  CD  . PRO B  1 73  ? -25.253 4.900   3.429   1.00 12.66  ? 73  PRO B CD  1 
ATOM   2720 N  N   . SER B  1 74  ? -26.005 7.911   6.786   1.00 18.34  ? 74  SER B N   1 
ATOM   2721 C  CA  . SER B  1 74  ? -25.776 7.924   8.246   1.00 17.60  ? 74  SER B CA  1 
ATOM   2722 C  C   . SER B  1 74  ? -26.765 7.081   8.999   1.00 16.12  ? 74  SER B C   1 
ATOM   2723 O  O   . SER B  1 74  ? -26.529 6.924   10.216  1.00 17.44  ? 74  SER B O   1 
ATOM   2724 C  CB  . SER B  1 74  ? -25.801 9.325   8.835   1.00 22.12  ? 74  SER B CB  1 
ATOM   2725 O  OG  . SER B  1 74  ? -27.098 9.944   8.529   1.00 27.20  ? 74  SER B OG  1 
ATOM   2726 N  N   . ASP B  1 75  ? -27.793 6.505   8.379   1.00 15.86  ? 75  ASP B N   1 
ATOM   2727 C  CA  . ASP B  1 75  ? -28.679 5.602   9.099   1.00 16.03  ? 75  ASP B CA  1 
ATOM   2728 C  C   . ASP B  1 75  ? -27.900 4.265   9.260   1.00 16.04  ? 75  ASP B C   1 
ATOM   2729 O  O   . ASP B  1 75  ? -28.344 3.435   10.088  1.00 18.74  ? 75  ASP B O   1 
ATOM   2730 C  CB  . ASP B  1 75  ? -30.055 5.410   8.493   1.00 22.37  ? 75  ASP B CB  1 
ATOM   2731 C  CG  . ASP B  1 75  ? -30.036 4.876   7.055   1.00 29.95  ? 75  ASP B CG  1 
ATOM   2732 O  OD1 . ASP B  1 75  ? -29.300 5.355   6.157   1.00 38.52  ? 75  ASP B OD1 1 
ATOM   2733 O  OD2 . ASP B  1 75  ? -30.870 3.997   6.795   1.00 67.08  ? 75  ASP B OD2 1 
ATOM   2734 N  N   . MET B  1 76  ? -26.875 3.994   8.478   1.00 14.53  ? 76  MET B N   1 
ATOM   2735 C  CA  . MET B  1 76  ? -26.040 2.788   8.640   1.00 13.21  ? 76  MET B CA  1 
ATOM   2736 C  C   . MET B  1 76  ? -25.182 2.972   9.836   1.00 11.87  ? 76  MET B C   1 
ATOM   2737 O  O   . MET B  1 76  ? -24.535 4.060   9.977   1.00 12.98  ? 76  MET B O   1 
ATOM   2738 C  CB  . MET B  1 76  ? -25.289 2.646   7.320   1.00 15.87  ? 76  MET B CB  1 
ATOM   2739 C  CG  . MET B  1 76  ? -24.319 1.534   7.372   1.00 14.25  ? 76  MET B CG  1 
ATOM   2740 S  SD  . MET B  1 76  ? -23.524 1.459   5.693   1.00 14.58  ? 76  MET B SD  1 
ATOM   2741 C  CE  . MET B  1 76  ? -22.089 0.531   6.153   1.00 12.58  ? 76  MET B CE  1 
ATOM   2742 N  N   . HIS B  1 77  ? -25.146 2.043   10.778  1.00 12.05  ? 77  HIS B N   1 
ATOM   2743 C  CA  . HIS B  1 77  ? -24.403 2.251   12.008  1.00 12.74  ? 77  HIS B CA  1 
ATOM   2744 C  C   . HIS B  1 77  ? -23.952 0.960   12.633  1.00 11.25  ? 77  HIS B C   1 
ATOM   2745 O  O   . HIS B  1 77  ? -24.448 -0.087  12.334  1.00 12.65  ? 77  HIS B O   1 
ATOM   2746 C  CB  . HIS B  1 77  ? -25.135 3.167   13.015  1.00 15.73  ? 77  HIS B CB  1 
ATOM   2747 C  CG  . HIS B  1 77  ? -26.372 2.586   13.545  1.00 16.35  ? 77  HIS B CG  1 
ATOM   2748 N  ND1 . HIS B  1 77  ? -27.577 2.565   12.850  1.00 17.97  ? 77  HIS B ND1 1 
ATOM   2749 C  CD2 . HIS B  1 77  ? -26.635 1.959   14.715  1.00 17.79  ? 77  HIS B CD2 1 
ATOM   2750 C  CE1 . HIS B  1 77  ? -28.541 2.047   13.635  1.00 18.24  ? 77  HIS B CE1 1 
ATOM   2751 N  NE2 . HIS B  1 77  ? -27.990 1.597   14.758  1.00 20.57  ? 77  HIS B NE2 1 
ATOM   2752 N  N   . ILE B  1 78  ? -22.992 1.162   13.547  1.00 13.15  ? 78  ILE B N   1 
ATOM   2753 C  CA  . ILE B  1 78  ? -22.558 0.035   14.402  1.00 13.81  ? 78  ILE B CA  1 
ATOM   2754 C  C   . ILE B  1 78  ? -23.285 0.207   15.722  1.00 13.87  ? 78  ILE B C   1 
ATOM   2755 O  O   . ILE B  1 78  ? -23.294 1.282   16.295  1.00 15.75  ? 78  ILE B O   1 
ATOM   2756 C  CB  . ILE B  1 78  ? -21.010 0.156   14.641  1.00 14.89  ? 78  ILE B CB  1 
ATOM   2757 C  CG1 . ILE B  1 78  ? -20.190 -0.009  13.415  1.00 16.27  ? 78  ILE B CG1 1 
ATOM   2758 C  CG2 . ILE B  1 78  ? -20.558 -0.818  15.739  1.00 17.49  ? 78  ILE B CG2 1 
ATOM   2759 C  CD1 . ILE B  1 78  ? -18.745 0.520   13.563  1.00 16.02  ? 78  ILE B CD1 1 
ATOM   2760 N  N   . GLN B  1 79  ? -23.732 -0.958  16.194  1.00 14.36  ? 79  GLN B N   1 
ATOM   2761 C  CA  . GLN B  1 79  ? -24.315 -1.027  17.601  1.00 15.66  ? 79  GLN B CA  1 
ATOM   2762 C  C   . GLN B  1 79  ? -23.342 -1.883  18.380  1.00 16.53  ? 79  GLN B C   1 
ATOM   2763 O  O   . GLN B  1 79  ? -22.869 -2.938  17.876  1.00 17.32  ? 79  GLN B O   1 
ATOM   2764 C  CB  . GLN B  1 79  ? -25.725 -1.732  17.462  1.00 20.15  ? 79  GLN B CB  1 
ATOM   2765 C  CG  . GLN B  1 79  ? -26.431 -2.219  18.711  1.00 26.40  ? 79  GLN B CG  1 
ATOM   2766 C  CD  . GLN B  1 79  ? -26.812 -1.104  19.669  1.00 29.69  ? 79  GLN B CD  1 
ATOM   2767 O  OE1 . GLN B  1 79  ? -27.256 -0.044  19.232  1.00 29.29  ? 79  GLN B OE1 1 
ATOM   2768 N  NE2 . GLN B  1 79  ? -26.606 -1.311  21.006  1.00 43.64  ? 79  GLN B NE2 1 
ATOM   2769 N  N   . GLY B  1 80  ? -22.994 -1.446  19.596  1.00 18.07  ? 80  GLY B N   1 
ATOM   2770 C  CA  . GLY B  1 80  ? -22.157 -2.277  20.457  1.00 18.29  ? 80  GLY B CA  1 
ATOM   2771 C  C   . GLY B  1 80  ? -21.005 -1.531  21.017  1.00 18.13  ? 80  GLY B C   1 
ATOM   2772 O  O   . GLY B  1 80  ? -20.397 -2.017  22.004  1.00 22.13  ? 80  GLY B O   1 
ATOM   2773 N  N   . LEU B  1 81  ? -20.654 -0.354  20.466  1.00 17.07  ? 81  LEU B N   1 
ATOM   2774 C  CA  . LEU B  1 81  ? -19.634 0.488   21.038  1.00 18.04  ? 81  LEU B CA  1 
ATOM   2775 C  C   . LEU B  1 81  ? -20.261 1.392   22.119  1.00 19.39  ? 81  LEU B C   1 
ATOM   2776 O  O   . LEU B  1 81  ? -21.472 1.310   22.342  1.00 19.89  ? 81  LEU B O   1 
ATOM   2777 C  CB  . LEU B  1 81  ? -18.883 1.303   19.979  1.00 19.76  ? 81  LEU B CB  1 
ATOM   2778 C  CG  . LEU B  1 81  ? -18.153 0.402   18.965  1.00 18.48  ? 81  LEU B CG  1 
ATOM   2779 C  CD1 . LEU B  1 81  ? -17.756 1.230   17.737  1.00 20.08  ? 81  LEU B CD1 1 
ATOM   2780 C  CD2 . LEU B  1 81  ? -16.963 -0.224  19.694  1.00 22.36  ? 81  LEU B CD2 1 
ATOM   2781 N  N   . GLN B  1 82  ? -19.493 2.217   22.802  1.00 23.17  ? 82  GLN B N   1 
ATOM   2782 C  CA  . GLN B  1 82  ? -20.108 3.025   23.877  1.00 24.01  ? 82  GLN B CA  1 
ATOM   2783 C  C   . GLN B  1 82  ? -20.937 4.250   23.408  1.00 27.28  ? 82  GLN B C   1 
ATOM   2784 O  O   . GLN B  1 82  ? -21.612 4.867   24.207  1.00 28.14  ? 82  GLN B O   1 
ATOM   2785 C  CB  . GLN B  1 82  ? -19.078 3.486   24.818  1.00 29.49  ? 82  GLN B CB  1 
ATOM   2786 C  CG  . GLN B  1 82  ? -18.608 2.316   25.732  1.00 26.86  ? 82  GLN B CG  1 
ATOM   2787 C  CD  . GLN B  1 82  ? -17.495 2.764   26.614  1.00 43.91  ? 82  GLN B CD  1 
ATOM   2788 O  OE1 . GLN B  1 82  ? -17.581 2.688   27.854  1.00 42.91  ? 82  GLN B OE1 1 
ATOM   2789 N  NE2 . GLN B  1 82  ? -16.456 3.299   25.990  1.00 32.06  ? 82  GLN B NE2 1 
ATOM   2790 N  N   . SER B  1 83  ? -20.814 4.639   22.115  1.00 21.68  ? 83  SER B N   1 
ATOM   2791 C  CA  . SER B  1 83  ? -21.718 5.598   21.464  1.00 19.04  ? 83  SER B CA  1 
ATOM   2792 C  C   . SER B  1 83  ? -22.172 4.875   20.207  1.00 18.75  ? 83  SER B C   1 
ATOM   2793 O  O   . SER B  1 83  ? -21.475 3.912   19.750  1.00 17.55  ? 83  SER B O   1 
ATOM   2794 C  CB  . SER B  1 83  ? -21.001 6.854   21.107  1.00 22.04  ? 83  SER B CB  1 
ATOM   2795 O  OG  . SER B  1 83  ? -20.648 7.494   22.311  1.00 28.19  ? 83  SER B OG  1 
ATOM   2796 N  N   . ARG B  1 84  ? -23.191 5.370   19.541  1.00 18.89  ? 84  ARG B N   1 
ATOM   2797 C  CA  . ARG B  1 84  ? -23.546 4.977   18.209  1.00 17.43  ? 84  ARG B CA  1 
ATOM   2798 C  C   . ARG B  1 84  ? -22.473 5.614   17.269  1.00 16.29  ? 84  ARG B C   1 
ATOM   2799 O  O   . ARG B  1 84  ? -22.195 6.839   17.315  1.00 16.90  ? 84  ARG B O   1 
ATOM   2800 C  CB  . ARG B  1 84  ? -24.929 5.560   17.835  1.00 21.37  ? 84  ARG B CB  1 
ATOM   2801 C  CG  . ARG B  1 84  ? -25.184 5.407   16.345  1.00 20.72  ? 84  ARG B CG  1 
ATOM   2802 C  CD  . ARG B  1 84  ? -26.596 5.686   16.000  1.00 23.75  ? 84  ARG B CD  1 
ATOM   2803 N  NE  . ARG B  1 84  ? -26.819 5.787   14.559  1.00 22.64  ? 84  ARG B NE  1 
ATOM   2804 C  CZ  . ARG B  1 84  ? -27.961 5.736   13.881  1.00 25.31  ? 84  ARG B CZ  1 
ATOM   2805 N  NH1 . ARG B  1 84  ? -29.107 5.472   14.514  1.00 35.64  ? 84  ARG B NH1 1 
ATOM   2806 N  NH2 . ARG B  1 84  ? -27.901 5.756   12.530  1.00 28.95  ? 84  ARG B NH2 1 
ATOM   2807 N  N   . TYR B  1 85  ? -21.978 4.768   16.355  1.00 14.17  ? 85  TYR B N   1 
ATOM   2808 C  CA  . TYR B  1 85  ? -21.049 5.277   15.320  1.00 12.51  ? 85  TYR B CA  1 
ATOM   2809 C  C   . TYR B  1 85  ? -21.770 5.038   13.999  1.00 12.39  ? 85  TYR B C   1 
ATOM   2810 O  O   . TYR B  1 85  ? -22.091 3.932   13.624  1.00 14.10  ? 85  TYR B O   1 
ATOM   2811 C  CB  . TYR B  1 85  ? -19.695 4.538   15.377  1.00 13.67  ? 85  TYR B CB  1 
ATOM   2812 C  CG  . TYR B  1 85  ? -18.822 5.068   16.481  1.00 12.29  ? 85  TYR B CG  1 
ATOM   2813 C  CD1 . TYR B  1 85  ? -18.960 4.583   17.787  1.00 14.62  ? 85  TYR B CD1 1 
ATOM   2814 C  CD2 . TYR B  1 85  ? -17.810 5.977   16.226  1.00 12.60  ? 85  TYR B CD2 1 
ATOM   2815 C  CE1 . TYR B  1 85  ? -18.159 5.077   18.771  1.00 15.58  ? 85  TYR B CE1 1 
ATOM   2816 C  CE2 . TYR B  1 85  ? -16.959 6.454   17.198  1.00 13.40  ? 85  TYR B CE2 1 
ATOM   2817 C  CZ  . TYR B  1 85  ? -17.149 5.972   18.501  1.00 14.26  ? 85  TYR B CZ  1 
ATOM   2818 O  OH  . TYR B  1 85  ? -16.329 6.386   19.511  1.00 17.88  ? 85  TYR B OH  1 
ATOM   2819 N  N   . SER B  1 86  ? -22.012 6.121   13.242  1.00 12.46  ? 86  SER B N   1 
ATOM   2820 C  CA  . SER B  1 86  ? -22.733 6.043   11.963  1.00 12.84  ? 86  SER B CA  1 
ATOM   2821 C  C   . SER B  1 86  ? -21.732 6.105   10.829  1.00 11.00  ? 86  SER B C   1 
ATOM   2822 O  O   . SER B  1 86  ? -20.700 6.742   10.887  1.00 11.02  ? 86  SER B O   1 
ATOM   2823 C  CB  . SER B  1 86  ? -23.672 7.307   11.849  1.00 15.33  ? 86  SER B CB  1 
ATOM   2824 O  OG  . SER B  1 86  ? -24.687 7.220   12.876  1.00 16.94  ? 86  SER B OG  1 
ATOM   2825 N  N   . ALA B  1 87  ? -22.101 5.346   9.792   1.00 11.17  ? 87  ALA B N   1 
ATOM   2826 C  CA  . ALA B  1 87  ? -21.180 5.255   8.620   1.00 10.88  ? 87  ALA B CA  1 
ATOM   2827 C  C   . ALA B  1 87  ? -21.066 6.575   7.915   1.00 10.65  ? 87  ALA B C   1 
ATOM   2828 O  O   . ALA B  1 87  ? -22.045 7.373   7.856   1.00 12.62  ? 87  ALA B O   1 
ATOM   2829 C  CB  . ALA B  1 87  ? -21.670 4.198   7.690   1.00 13.20  ? 87  ALA B CB  1 
ATOM   2830 N  N   . THR B  1 88  ? -19.921 6.816   7.312   1.00 10.18  ? 88  THR B N   1 
ATOM   2831 C  CA  . THR B  1 88  ? -19.715 7.965   6.428   1.00 10.88  ? 88  THR B CA  1 
ATOM   2832 C  C   . THR B  1 88  ? -19.137 7.552   5.088   1.00 10.30  ? 88  THR B C   1 
ATOM   2833 O  O   . THR B  1 88  ? -19.579 8.098   4.052   1.00 10.19  ? 88  THR B O   1 
ATOM   2834 C  CB  . THR B  1 88  ? -18.871 9.095   7.134   1.00 12.97  ? 88  THR B CB  1 
ATOM   2835 O  OG1 . THR B  1 88  ? -18.742 10.228  6.236   1.00 16.65  ? 88  THR B OG1 1 
ATOM   2836 C  CG2 . THR B  1 88  ? -17.517 8.663   7.566   1.00 13.82  ? 88  THR B CG2 1 
ATOM   2837 N  N   . GLN B  1 89  ? -18.181 6.622   5.019   1.00 9.42   ? 89  GLN B N   1 
ATOM   2838 C  CA  . GLN B  1 89  ? -17.621 6.233   3.718   1.00 9.03   ? 89  GLN B CA  1 
ATOM   2839 C  C   . GLN B  1 89  ? -16.867 4.928   3.885   1.00 8.70   ? 89  GLN B C   1 
ATOM   2840 O  O   . GLN B  1 89  ? -16.464 4.611   5.034   1.00 9.26   ? 89  GLN B O   1 
ATOM   2841 C  CB  . GLN B  1 89  ? -16.694 7.328   3.127   1.00 10.29  ? 89  GLN B CB  1 
ATOM   2842 C  CG  . GLN B  1 89  ? -15.613 7.769   4.063   1.00 12.24  ? 89  GLN B CG  1 
ATOM   2843 C  CD  . GLN B  1 89  ? -14.231 7.468   3.600   1.00 12.04  ? 89  GLN B CD  1 
ATOM   2844 O  OE1 . GLN B  1 89  ? -14.035 6.229   3.334   1.00 12.78  ? 89  GLN B OE1 1 
ATOM   2845 N  NE2 . GLN B  1 89  ? -13.275 8.309   3.642   1.00 18.05  ? 89  GLN B NE2 1 
ATOM   2846 N  N   . LEU B  1 90  ? -16.655 4.230   2.795   1.00 8.27   ? 90  LEU B N   1 
ATOM   2847 C  CA  . LEU B  1 90  ? -15.707 3.124   2.782   1.00 7.92   ? 90  LEU B CA  1 
ATOM   2848 C  C   . LEU B  1 90  ? -14.713 3.385   1.656   1.00 7.87   ? 90  LEU B C   1 
ATOM   2849 O  O   . LEU B  1 90  ? -15.015 4.081   0.688   1.00 8.70   ? 90  LEU B O   1 
ATOM   2850 C  CB  . LEU B  1 90  ? -16.372 1.737   2.763   1.00 8.43   ? 90  LEU B CB  1 
ATOM   2851 C  CG  . LEU B  1 90  ? -17.273 1.424   1.562   1.00 8.94   ? 90  LEU B CG  1 
ATOM   2852 C  CD1 . LEU B  1 90  ? -16.516 1.131   0.280   1.00 10.41  ? 90  LEU B CD1 1 
ATOM   2853 C  CD2 . LEU B  1 90  ? -18.174 0.242   1.950   1.00 10.57  ? 90  LEU B CD2 1 
ATOM   2854 N  N   . HIS B  1 91  ? -13.548 2.755   1.774   1.00 8.11   ? 91  HIS B N   1 
ATOM   2855 C  CA  . HIS B  1 91  ? -12.509 2.890   0.704   1.00 8.17   ? 91  HIS B CA  1 
ATOM   2856 C  C   . HIS B  1 91  ? -11.555 1.716   0.887   1.00 7.78   ? 91  HIS B C   1 
ATOM   2857 O  O   . HIS B  1 91  ? -11.640 0.937   1.844   1.00 8.10   ? 91  HIS B O   1 
ATOM   2858 C  CB  . HIS B  1 91  ? -11.820 4.265   0.834   1.00 8.63   ? 91  HIS B CB  1 
ATOM   2859 C  CG  . HIS B  1 91  ? -11.064 4.413   2.105   1.00 7.59   ? 91  HIS B CG  1 
ATOM   2860 N  ND1 . HIS B  1 91  ? -11.591 4.988   3.216   1.00 8.43   ? 91  HIS B ND1 1 
ATOM   2861 C  CD2 . HIS B  1 91  ? -9.840  3.880   2.509   1.00 8.49   ? 91  HIS B CD2 1 
ATOM   2862 C  CE1 . HIS B  1 91  ? -10.738 4.883   4.242   1.00 8.36   ? 91  HIS B CE1 1 
ATOM   2863 N  NE2 . HIS B  1 91  ? -9.676  4.208   3.826   1.00 7.97   ? 91  HIS B NE2 1 
ATOM   2864 N  N   . LEU B  1 92  ? -10.586 1.648   -0.037  1.00 8.12   ? 92  LEU B N   1 
ATOM   2865 C  CA  . LEU B  1 92  ? -9.649  0.520   -0.037  1.00 8.67   ? 92  LEU B CA  1 
ATOM   2866 C  C   . LEU B  1 92  ? -8.205  0.991   -0.131  1.00 8.17   ? 92  LEU B C   1 
ATOM   2867 O  O   . LEU B  1 92  ? -7.873  2.143   -0.504  1.00 8.93   ? 92  LEU B O   1 
ATOM   2868 C  CB  . LEU B  1 92  ? -9.918  -0.435  -1.205  1.00 10.81  ? 92  LEU B CB  1 
ATOM   2869 C  CG  . LEU B  1 92  ? -11.323 -1.133  -1.126  1.00 10.96  ? 92  LEU B CG  1 
ATOM   2870 C  CD1 . LEU B  1 92  ? -12.297 -0.477  -1.931  1.00 17.30  ? 92  LEU B CD1 1 
ATOM   2871 C  CD2 . LEU B  1 92  ? -11.196 -2.597  -1.360  1.00 14.52  ? 92  LEU B CD2 1 
ATOM   2872 N  N   . HIS B  1 93  ? -7.295  0.058   0.173   1.00 8.04   ? 93  HIS B N   1 
ATOM   2873 C  CA  . HIS B  1 93  ? -5.851  0.203   -0.021  1.00 7.99   ? 93  HIS B CA  1 
ATOM   2874 C  C   . HIS B  1 93  ? -5.337  -1.026  -0.674  1.00 8.13   ? 93  HIS B C   1 
ATOM   2875 O  O   . HIS B  1 93  ? -5.809  -2.149  -0.373  1.00 8.87   ? 93  HIS B O   1 
ATOM   2876 C  CB  . HIS B  1 93  ? -5.170  0.358   1.343   1.00 9.05   ? 93  HIS B CB  1 
ATOM   2877 C  CG  . HIS B  1 93  ? -5.672  1.559   2.132   1.00 8.02   ? 93  HIS B CG  1 
ATOM   2878 N  ND1 . HIS B  1 93  ? -5.075  2.812   2.114   1.00 8.62   ? 93  HIS B ND1 1 
ATOM   2879 C  CD2 . HIS B  1 93  ? -6.726  1.683   3.001   1.00 8.08   ? 93  HIS B CD2 1 
ATOM   2880 C  CE1 . HIS B  1 93  ? -5.765  3.635   2.916   1.00 8.71   ? 93  HIS B CE1 1 
ATOM   2881 N  NE2 . HIS B  1 93  ? -6.773  2.985   3.472   1.00 7.66   ? 93  HIS B NE2 1 
ATOM   2882 N  N   . TRP B  1 94  ? -4.377  -0.889  -1.591  1.00 8.87   ? 94  TRP B N   1 
ATOM   2883 C  CA  . TRP B  1 94  ? -3.934  -2.030  -2.394  1.00 9.06   ? 94  TRP B CA  1 
ATOM   2884 C  C   . TRP B  1 94  ? -2.517  -1.772  -2.858  1.00 9.46   ? 94  TRP B C   1 
ATOM   2885 O  O   . TRP B  1 94  ? -1.892  -0.728  -2.641  1.00 9.53   ? 94  TRP B O   1 
ATOM   2886 C  CB  . TRP B  1 94  ? -4.893  -2.266  -3.558  1.00 9.54   ? 94  TRP B CB  1 
ATOM   2887 C  CG  . TRP B  1 94  ? -5.004  -1.070  -4.523  1.00 9.70   ? 94  TRP B CG  1 
ATOM   2888 C  CD1 . TRP B  1 94  ? -4.156  -0.743  -5.563  1.00 10.68  ? 94  TRP B CD1 1 
ATOM   2889 C  CD2 . TRP B  1 94  ? -5.966  -0.019  -4.426  1.00 9.45   ? 94  TRP B CD2 1 
ATOM   2890 N  NE1 . TRP B  1 94  ? -4.601  0.396   -6.155  1.00 11.22  ? 94  TRP B NE1 1 
ATOM   2891 C  CE2 . TRP B  1 94  ? -5.709  0.878   -5.524  1.00 9.61   ? 94  TRP B CE2 1 
ATOM   2892 C  CE3 . TRP B  1 94  ? -7.072  0.242   -3.590  1.00 9.60   ? 94  TRP B CE3 1 
ATOM   2893 C  CZ2 . TRP B  1 94  ? -6.510  2.012   -5.773  1.00 11.09  ? 94  TRP B CZ2 1 
ATOM   2894 C  CZ3 . TRP B  1 94  ? -7.847  1.404   -3.852  1.00 10.25  ? 94  TRP B CZ3 1 
ATOM   2895 C  CH2 . TRP B  1 94  ? -7.566  2.251   -4.948  1.00 10.43  ? 94  TRP B CH2 1 
ATOM   2896 N  N   . GLY B  1 95  ? -1.981  -2.828  -3.529  1.00 10.25  ? 95  GLY B N   1 
ATOM   2897 C  CA  . GLY B  1 95  ? -0.571  -2.871  -4.014  1.00 11.16  ? 95  GLY B CA  1 
ATOM   2898 C  C   . GLY B  1 95  ? -0.514  -2.535  -5.476  1.00 10.62  ? 95  GLY B C   1 
ATOM   2899 O  O   . GLY B  1 95  ? -0.998  -1.519  -5.953  1.00 11.47  ? 95  GLY B O   1 
ATOM   2900 N  N   . ASN B  1 96  ? 0.008   -3.472  -6.290  1.00 11.69  ? 96  ASN B N   1 
ATOM   2901 C  CA  . ASN B  1 96  ? 0.185   -3.209  -7.746  1.00 13.62  ? 96  ASN B CA  1 
ATOM   2902 C  C   . ASN B  1 96  ? 0.173   -4.521  -8.457  1.00 13.02  ? 96  ASN B C   1 
ATOM   2903 O  O   . ASN B  1 96  ? 0.266   -5.540  -7.851  1.00 13.10  ? 96  ASN B O   1 
ATOM   2904 C  CB  . ASN B  1 96  ? 1.422   -2.339  -8.014  1.00 16.38  ? 96  ASN B CB  1 
ATOM   2905 C  CG  . ASN B  1 96  ? 2.720   -3.114  -7.819  1.00 17.73  ? 96  ASN B CG  1 
ATOM   2906 O  OD1 . ASN B  1 96  ? 3.073   -3.961  -8.708  1.00 21.97  ? 96  ASN B OD1 1 
ATOM   2907 N  ND2 . ASN B  1 96  ? 3.363   -2.967  -6.674  1.00 19.31  ? 96  ASN B ND2 1 
ATOM   2908 N  N   . PRO B  1 97  ? 0.044   -4.488  -9.829  1.00 13.77  ? 97  PRO B N   1 
ATOM   2909 C  CA  . PRO B  1 97  ? -0.188  -5.710  -10.541 1.00 16.00  ? 97  PRO B CA  1 
ATOM   2910 C  C   . PRO B  1 97  ? 0.910   -6.710  -10.370 1.00 14.35  ? 97  PRO B C   1 
ATOM   2911 O  O   . PRO B  1 97  ? 0.669   -7.926  -10.480 1.00 17.34  ? 97  PRO B O   1 
ATOM   2912 C  CB  . PRO B  1 97  ? -0.320  -5.214  -12.019 1.00 19.23  ? 97  PRO B CB  1 
ATOM   2913 C  CG  . PRO B  1 97  ? -0.907  -3.921  -11.857 1.00 19.53  ? 97  PRO B CG  1 
ATOM   2914 C  CD  . PRO B  1 97  ? -0.180  -3.303  -10.657 1.00 17.22  ? 97  PRO B CD  1 
ATOM   2915 N  N   . ASN B  1 98  ? 2.158   -6.273  -10.205 1.00 13.54  ? 98  ASN B N   1 
ATOM   2916 C  CA  . ASN B  1 98  ? 3.308   -7.243  -10.165 1.00 15.75  ? 98  ASN B CA  1 
ATOM   2917 C  C   . ASN B  1 98  ? 3.541   -7.528  -8.714  1.00 19.23  ? 98  ASN B C   1 
ATOM   2918 O  O   . ASN B  1 98  ? 4.400   -8.347  -8.476  1.00 28.92  ? 98  ASN B O   1 
ATOM   2919 C  CB  . ASN B  1 98  ? 4.478   -6.504  -10.770 1.00 18.27  ? 98  ASN B CB  1 
ATOM   2920 C  CG  . ASN B  1 98  ? 4.281   -6.296  -12.302 1.00 17.58  ? 98  ASN B CG  1 
ATOM   2921 O  OD1 . ASN B  1 98  ? 3.922   -7.252  -13.058 1.00 18.06  ? 98  ASN B OD1 1 
ATOM   2922 N  ND2 . ASN B  1 98  ? 4.181   -5.029  -12.663 1.00 22.21  ? 98  ASN B ND2 1 
ATOM   2923 N  N   . ASP B  1 99  ? 2.888   -6.896  -7.718  1.00 17.04  ? 99  ASP B N   1 
ATOM   2924 C  CA  . ASP B  1 99  ? 3.147   -7.193  -6.267  1.00 17.77  ? 99  ASP B CA  1 
ATOM   2925 C  C   . ASP B  1 99  ? 1.777   -6.913  -5.580  1.00 14.73  ? 99  ASP B C   1 
ATOM   2926 O  O   . ASP B  1 99  ? 1.581   -5.830  -5.018  1.00 15.34  ? 99  ASP B O   1 
ATOM   2927 C  CB  . ASP B  1 99  ? 4.253   -6.355  -5.684  1.00 23.62  ? 99  ASP B CB  1 
ATOM   2928 C  CG  . ASP B  1 99  ? 4.419   -6.597  -4.208  1.00 32.69  ? 99  ASP B CG  1 
ATOM   2929 O  OD1 . ASP B  1 99  ? 4.130   -7.744  -3.841  1.00 48.20  ? 99  ASP B OD1 1 
ATOM   2930 O  OD2 . ASP B  1 99  ? 4.843   -5.683  -3.449  1.00 149.77 ? 99  ASP B OD2 1 
ATOM   2931 N  N   . PRO B  1 100 ? 0.866   -7.876  -5.579  1.00 14.09  ? 100 PRO B N   1 
ATOM   2932 C  CA  . PRO B  1 100 ? -0.498  -7.644  -4.983  1.00 14.33  ? 100 PRO B CA  1 
ATOM   2933 C  C   . PRO B  1 100 ? -0.499  -7.884  -3.475  1.00 13.02  ? 100 PRO B C   1 
ATOM   2934 O  O   . PRO B  1 100 ? -1.055  -8.815  -2.968  1.00 15.88  ? 100 PRO B O   1 
ATOM   2935 C  CB  . PRO B  1 100 ? -1.358  -8.585  -5.815  1.00 16.13  ? 100 PRO B CB  1 
ATOM   2936 C  CG  . PRO B  1 100 ? -0.400  -9.716  -6.217  1.00 19.25  ? 100 PRO B CG  1 
ATOM   2937 C  CD  . PRO B  1 100 ? 0.924   -9.123  -6.410  1.00 18.53  ? 100 PRO B CD  1 
ATOM   2938 N  N   . HIS B  1 101 ? 0.215   -7.027  -2.744  1.00 14.00  ? 101 HIS B N   1 
ATOM   2939 C  CA  . HIS B  1 101 ? 0.467   -7.125  -1.289  1.00 13.78  ? 101 HIS B CA  1 
ATOM   2940 C  C   . HIS B  1 101 ? 0.339   -5.778  -0.618  1.00 14.01  ? 101 HIS B C   1 
ATOM   2941 O  O   . HIS B  1 101 ? 1.309   -5.384  0.190   1.00 18.94  ? 101 HIS B O   1 
ATOM   2942 C  CB  . HIS B  1 101 ? 1.784   -7.757  -0.946  1.00 18.14  ? 101 HIS B CB  1 
ATOM   2943 C  CG  . HIS B  1 101 ? 1.761   -9.180  -1.397  1.00 21.43  ? 101 HIS B CG  1 
ATOM   2944 N  ND1 . HIS B  1 101 ? 1.218   -10.244 -0.722  1.00 31.55  ? 101 HIS B ND1 1 
ATOM   2945 C  CD2 . HIS B  1 101 ? 2.282   -9.707  -2.550  1.00 24.05  ? 101 HIS B CD2 1 
ATOM   2946 C  CE1 . HIS B  1 101 ? 1.358   -11.359 -1.444  1.00 36.98  ? 101 HIS B CE1 1 
ATOM   2947 N  NE2 . HIS B  1 101 ? 2.024   -11.069 -2.557  1.00 34.85  ? 101 HIS B NE2 1 
ATOM   2948 N  N   . GLY B  1 102 ? -0.818  -5.187  -0.629  1.00 11.53  ? 102 GLY B N   1 
ATOM   2949 C  CA  . GLY B  1 102 ? -1.002  -3.781  -0.272  1.00 10.47  ? 102 GLY B CA  1 
ATOM   2950 C  C   . GLY B  1 102 ? -1.931  -3.557  0.914   1.00 9.70   ? 102 GLY B C   1 
ATOM   2951 O  O   . GLY B  1 102 ? -2.458  -2.439  1.026   1.00 10.48  ? 102 GLY B O   1 
ATOM   2952 N  N   . SER B  1 103 ? -2.159  -4.542  1.824   1.00 9.61   ? 103 SER B N   1 
ATOM   2953 C  CA  . SER B  1 103 ? -2.844  -4.181  3.029   1.00 9.49   ? 103 SER B CA  1 
ATOM   2954 C  C   . SER B  1 103 ? -2.072  -3.175  3.855   1.00 9.41   ? 103 SER B C   1 
ATOM   2955 O  O   . SER B  1 103 ? -0.844  -3.057  3.691   1.00 11.62  ? 103 SER B O   1 
ATOM   2956 C  CB  . SER B  1 103 ? -3.187  -5.429  3.874   1.00 9.88   ? 103 SER B CB  1 
ATOM   2957 O  OG  . SER B  1 103 ? -2.019  -6.004  4.419   1.00 10.17  ? 103 SER B OG  1 
ATOM   2958 N  N   . GLU B  1 104 ? -2.755  -2.467  4.749   1.00 8.95   ? 104 GLU B N   1 
ATOM   2959 C  CA  . GLU B  1 104 ? -2.095  -1.528  5.677   1.00 9.12   ? 104 GLU B CA  1 
ATOM   2960 C  C   . GLU B  1 104 ? -1.680  -2.288  6.933   1.00 8.29   ? 104 GLU B C   1 
ATOM   2961 O  O   . GLU B  1 104 ? -0.524  -2.303  7.300   1.00 9.42   ? 104 GLU B O   1 
ATOM   2962 C  CB  . GLU B  1 104 ? -3.030  -0.379  5.985   1.00 9.44   ? 104 GLU B CB  1 
ATOM   2963 C  CG  . GLU B  1 104 ? -3.475  0.368   4.697   1.00 9.47   ? 104 GLU B CG  1 
ATOM   2964 C  CD  . GLU B  1 104 ? -3.547  1.835   4.979   1.00 8.61   ? 104 GLU B CD  1 
ATOM   2965 O  OE1 . GLU B  1 104 ? -4.544  2.253   5.597   1.00 9.54   ? 104 GLU B OE1 1 
ATOM   2966 O  OE2 . GLU B  1 104 ? -2.592  2.574   4.622   1.00 10.19  ? 104 GLU B OE2 1 
ATOM   2967 N  N   . HIS B  1 105 ? -2.654  -2.903  7.628   1.00 9.37   ? 105 HIS B N   1 
ATOM   2968 C  CA  . HIS B  1 105 ? -2.287  -3.768  8.742   1.00 9.21   ? 105 HIS B CA  1 
ATOM   2969 C  C   . HIS B  1 105 ? -1.615  -5.031  8.205   1.00 8.78   ? 105 HIS B C   1 
ATOM   2970 O  O   . HIS B  1 105 ? -1.925  -5.487  7.130   1.00 9.86   ? 105 HIS B O   1 
ATOM   2971 C  CB  . HIS B  1 105 ? -3.497  -4.111  9.585   1.00 9.53   ? 105 HIS B CB  1 
ATOM   2972 C  CG  . HIS B  1 105 ? -4.065  -2.934  10.270  1.00 9.20   ? 105 HIS B CG  1 
ATOM   2973 N  ND1 . HIS B  1 105 ? -4.997  -2.080  9.731   1.00 9.65   ? 105 HIS B ND1 1 
ATOM   2974 C  CD2 . HIS B  1 105 ? -3.772  -2.392  11.481  1.00 9.34   ? 105 HIS B CD2 1 
ATOM   2975 C  CE1 . HIS B  1 105 ? -5.221  -1.062  10.603  1.00 10.37  ? 105 HIS B CE1 1 
ATOM   2976 N  NE2 . HIS B  1 105 ? -4.482  -1.221  11.684  1.00 9.82   ? 105 HIS B NE2 1 
ATOM   2977 N  N   . THR B  1 106 ? -0.685  -5.515  9.015   1.00 9.67   ? 106 THR B N   1 
ATOM   2978 C  CA  . THR B  1 106 ? -0.040  -6.823  8.714   1.00 10.30  ? 106 THR B CA  1 
ATOM   2979 C  C   . THR B  1 106 ? -0.349  -7.724  9.891   1.00 10.70  ? 106 THR B C   1 
ATOM   2980 O  O   . THR B  1 106 ? -0.635  -7.252  10.995  1.00 10.75  ? 106 THR B O   1 
ATOM   2981 C  CB  . THR B  1 106 ? 1.435   -6.611  8.431   1.00 10.95  ? 106 THR B CB  1 
ATOM   2982 O  OG1 . THR B  1 106 ? 2.084   -6.054  9.554   1.00 11.97  ? 106 THR B OG1 1 
ATOM   2983 C  CG2 . THR B  1 106 ? 1.662   -5.768  7.247   1.00 13.07  ? 106 THR B CG2 1 
ATOM   2984 N  N   . VAL B  1 107 ? -0.222  -9.048  9.645   1.00 11.30  ? 107 VAL B N   1 
ATOM   2985 C  CA  . VAL B  1 107 ? -0.478  -10.004 10.729  1.00 13.09  ? 107 VAL B CA  1 
ATOM   2986 C  C   . VAL B  1 107 ? 0.784   -10.921 10.774  1.00 12.44  ? 107 VAL B C   1 
ATOM   2987 O  O   . VAL B  1 107 ? 1.167   -11.512 9.760   1.00 14.72  ? 107 VAL B O   1 
ATOM   2988 C  CB  . VAL B  1 107 ? -1.733  -10.870 10.469  1.00 14.09  ? 107 VAL B CB  1 
ATOM   2989 C  CG1 . VAL B  1 107 ? -1.824  -11.984 11.579  1.00 18.24  ? 107 VAL B CG1 1 
ATOM   2990 C  CG2 . VAL B  1 107 ? -3.014  -9.988  10.513  1.00 14.66  ? 107 VAL B CG2 1 
ATOM   2991 N  N   . SER B  1 108 ? 1.477   -10.824 11.938  1.00 13.75  ? 108 SER B N   1 
ATOM   2992 C  CA  . SER B  1 108 ? 2.755   -11.580 12.115  1.00 14.38  ? 108 SER B CA  1 
ATOM   2993 C  C   . SER B  1 108 ? 3.683   -11.307 10.920  1.00 15.50  ? 108 SER B C   1 
ATOM   2994 O  O   . SER B  1 108 ? 4.319   -12.188 10.342  1.00 16.03  ? 108 SER B O   1 
ATOM   2995 C  CB  . SER B  1 108 ? 2.458   -13.070 12.208  1.00 17.84  ? 108 SER B CB  1 
ATOM   2996 O  OG  . SER B  1 108 ? 1.699   -13.231 13.409  1.00 19.46  ? 108 SER B OG  1 
ATOM   2997 N  N   . GLY B  1 109 ? 3.767   -10.017 10.597  1.00 14.07  ? 109 GLY B N   1 
ATOM   2998 C  CA  . GLY B  1 109 ? 4.649   -9.554  9.587   1.00 14.59  ? 109 GLY B CA  1 
ATOM   2999 C  C   . GLY B  1 109 ? 4.271   -9.727  8.154   1.00 16.65  ? 109 GLY B C   1 
ATOM   3000 O  O   . GLY B  1 109 ? 5.055   -9.229  7.229   1.00 21.87  ? 109 GLY B O   1 
ATOM   3001 N  N   . GLN B  1 110 ? 3.113   -10.264 7.874   1.00 14.90  ? 110 GLN B N   1 
ATOM   3002 C  CA  . GLN B  1 110 ? 2.730   -10.525 6.432   1.00 15.56  ? 110 GLN B CA  1 
ATOM   3003 C  C   . GLN B  1 110 ? 1.605   -9.562  6.022   1.00 13.51  ? 110 GLN B C   1 
ATOM   3004 O  O   . GLN B  1 110 ? 0.626   -9.331  6.780   1.00 12.31  ? 110 GLN B O   1 
ATOM   3005 C  CB  . GLN B  1 110 ? 2.135   -11.878 6.406   1.00 18.02  ? 110 GLN B CB  1 
ATOM   3006 C  CG  . GLN B  1 110 ? 3.007   -12.989 7.036   1.00 19.96  ? 110 GLN B CG  1 
ATOM   3007 C  CD  . GLN B  1 110 ? 4.419   -12.962 6.443   1.00 24.18  ? 110 GLN B CD  1 
ATOM   3008 O  OE1 . GLN B  1 110 ? 4.589   -13.190 5.254   1.00 31.19  ? 110 GLN B OE1 1 
ATOM   3009 N  NE2 . GLN B  1 110 ? 5.420   -12.703 7.306   1.00 30.98  ? 110 GLN B NE2 1 
ATOM   3010 N  N   . HIS B  1 111 ? 1.779   -9.020  4.849   1.00 13.58  ? 111 HIS B N   1 
ATOM   3011 C  CA  . HIS B  1 111 ? 0.746   -8.292  4.213   1.00 12.67  ? 111 HIS B CA  1 
ATOM   3012 C  C   . HIS B  1 111 ? -0.287  -9.153  3.564   1.00 12.25  ? 111 HIS B C   1 
ATOM   3013 O  O   . HIS B  1 111 ? 0.038   -10.269 3.070   1.00 18.36  ? 111 HIS B O   1 
ATOM   3014 C  CB  . HIS B  1 111 ? 1.201   -7.392  2.990   1.00 14.96  ? 111 HIS B CB  1 
ATOM   3015 C  CG  . HIS B  1 111 ? 1.956   -6.182  3.401   1.00 12.53  ? 111 HIS B CG  1 
ATOM   3016 N  ND1 . HIS B  1 111 ? 1.357   -4.945  3.611   1.00 14.95  ? 111 HIS B ND1 1 
ATOM   3017 C  CD2 . HIS B  1 111 ? 3.256   -6.009  3.713   1.00 15.11  ? 111 HIS B CD2 1 
ATOM   3018 C  CE1 . HIS B  1 111 ? 2.282   -4.066  4.061   1.00 14.97  ? 111 HIS B CE1 1 
ATOM   3019 N  NE2 . HIS B  1 111 ? 3.444   -4.692  4.037   1.00 18.75  ? 111 HIS B NE2 1 
ATOM   3020 N  N   . PHE B  1 112 ? -1.485  -8.663  3.509   1.00 10.36  ? 112 PHE B N   1 
ATOM   3021 C  CA  . PHE B  1 112 ? -2.566  -9.255  2.767   1.00 10.38  ? 112 PHE B CA  1 
ATOM   3022 C  C   . PHE B  1 112 ? -2.600  -8.522  1.404   1.00 9.62   ? 112 PHE B C   1 
ATOM   3023 O  O   . PHE B  1 112 ? -1.870  -7.507  1.234   1.00 10.98  ? 112 PHE B O   1 
ATOM   3024 C  CB  . PHE B  1 112 ? -3.896  -9.185  3.470   1.00 11.63  ? 112 PHE B CB  1 
ATOM   3025 C  CG  . PHE B  1 112 ? -3.952  -10.158 4.609   1.00 13.77  ? 112 PHE B CG  1 
ATOM   3026 C  CD1 . PHE B  1 112 ? -3.289  -9.938  5.828   1.00 18.06  ? 112 PHE B CD1 1 
ATOM   3027 C  CD2 . PHE B  1 112 ? -4.613  -11.358 4.407   1.00 18.32  ? 112 PHE B CD2 1 
ATOM   3028 C  CE1 . PHE B  1 112 ? -3.328  -10.905 6.801   1.00 22.81  ? 112 PHE B CE1 1 
ATOM   3029 C  CE2 . PHE B  1 112 ? -4.666  -12.308 5.371   1.00 22.10  ? 112 PHE B CE2 1 
ATOM   3030 C  CZ  . PHE B  1 112 ? -4.015  -12.088 6.566   1.00 25.00  ? 112 PHE B CZ  1 
ATOM   3031 N  N   . ALA B  1 113 ? -3.378  -8.971  0.446   1.00 9.49   ? 113 ALA B N   1 
ATOM   3032 C  CA  . ALA B  1 113 ? -3.435  -8.371  -0.872  1.00 10.57  ? 113 ALA B CA  1 
ATOM   3033 C  C   . ALA B  1 113 ? -3.925  -6.914  -0.791  1.00 9.24   ? 113 ALA B C   1 
ATOM   3034 O  O   . ALA B  1 113 ? -3.469  -6.066  -1.546  1.00 10.21  ? 113 ALA B O   1 
ATOM   3035 C  CB  . ALA B  1 113 ? -4.260  -9.162  -1.822  1.00 12.36  ? 113 ALA B CB  1 
ATOM   3036 N  N   . ALA B  1 114 ? -4.966  -6.667  0.015   1.00 8.90   ? 114 ALA B N   1 
ATOM   3037 C  CA  . ALA B  1 114 ? -5.608  -5.348  0.037   1.00 8.39   ? 114 ALA B CA  1 
ATOM   3038 C  C   . ALA B  1 114 ? -6.311  -5.206  1.382   1.00 7.87   ? 114 ALA B C   1 
ATOM   3039 O  O   . ALA B  1 114 ? -6.311  -6.142  2.198   1.00 8.36   ? 114 ALA B O   1 
ATOM   3040 C  CB  . ALA B  1 114 ? -6.540  -5.174  -1.152  1.00 9.39   ? 114 ALA B CB  1 
ATOM   3041 N  N   . GLU B  1 115 ? -6.945  -4.055  1.610   1.00 8.29   ? 115 GLU B N   1 
ATOM   3042 C  CA  . GLU B  1 115 ? -7.657  -3.819  2.868   1.00 8.09   ? 115 GLU B CA  1 
ATOM   3043 C  C   . GLU B  1 115 ? -8.812  -2.886  2.584   1.00 7.78   ? 115 GLU B C   1 
ATOM   3044 O  O   . GLU B  1 115 ? -8.656  -1.878  1.883   1.00 9.08   ? 115 GLU B O   1 
ATOM   3045 C  CB  . GLU B  1 115 ? -6.702  -3.305  3.933   1.00 8.52   ? 115 GLU B CB  1 
ATOM   3046 C  CG  . GLU B  1 115 ? -7.242  -3.157  5.306   1.00 8.55   ? 115 GLU B CG  1 
ATOM   3047 C  CD  . GLU B  1 115 ? -6.168  -2.900  6.378   1.00 8.66   ? 115 GLU B CD  1 
ATOM   3048 O  OE1 . GLU B  1 115 ? -5.006  -3.350  6.164   1.00 9.81   ? 115 GLU B OE1 1 
ATOM   3049 O  OE2 . GLU B  1 115 ? -6.473  -2.304  7.420   1.00 9.32   ? 115 GLU B OE2 1 
ATOM   3050 N  N   . LEU B  1 116 ? -9.976  -3.199  3.174   1.00 7.43   ? 116 LEU B N   1 
ATOM   3051 C  CA  . LEU B  1 116 ? -11.151 -2.328  3.138   1.00 7.54   ? 116 LEU B CA  1 
ATOM   3052 C  C   . LEU B  1 116 ? -11.301 -1.645  4.477   1.00 7.46   ? 116 LEU B C   1 
ATOM   3053 O  O   . LEU B  1 116 ? -11.182 -2.291  5.525   1.00 7.74   ? 116 LEU B O   1 
ATOM   3054 C  CB  . LEU B  1 116 ? -12.393 -3.224  2.925   1.00 8.66   ? 116 LEU B CB  1 
ATOM   3055 C  CG  . LEU B  1 116 ? -13.767 -2.510  3.035   1.00 8.92   ? 116 LEU B CG  1 
ATOM   3056 C  CD1 . LEU B  1 116 ? -13.999 -1.641  1.854   1.00 10.89  ? 116 LEU B CD1 1 
ATOM   3057 C  CD2 . LEU B  1 116 ? -14.864 -3.498  3.212   1.00 11.04  ? 116 LEU B CD2 1 
ATOM   3058 N  N   . HIS B  1 117 ? -11.584 -0.326  4.450   1.00 7.09   ? 117 HIS B N   1 
ATOM   3059 C  CA  . HIS B  1 117 ? -11.901 0.436   5.644   1.00 7.20   ? 117 HIS B CA  1 
ATOM   3060 C  C   . HIS B  1 117 ? -13.280 0.999   5.531   1.00 7.17   ? 117 HIS B C   1 
ATOM   3061 O  O   . HIS B  1 117 ? -13.589 1.700   4.553   1.00 8.31   ? 117 HIS B O   1 
ATOM   3062 C  CB  . HIS B  1 117 ? -10.886 1.601   5.788   1.00 7.83   ? 117 HIS B CB  1 
ATOM   3063 C  CG  . HIS B  1 117 ? -9.504  1.112   6.105   1.00 7.25   ? 117 HIS B CG  1 
ATOM   3064 N  ND1 . HIS B  1 117 ? -8.363  1.855   5.822   1.00 7.12   ? 117 HIS B ND1 1 
ATOM   3065 C  CD2 . HIS B  1 117 ? -9.133  -0.050  6.704   1.00 7.71   ? 117 HIS B CD2 1 
ATOM   3066 C  CE1 . HIS B  1 117 ? -7.356  1.102   6.274   1.00 7.91   ? 117 HIS B CE1 1 
ATOM   3067 N  NE2 . HIS B  1 117 ? -7.787  -0.035  6.804   1.00 7.95   ? 117 HIS B NE2 1 
ATOM   3068 N  N   . ILE B  1 118 ? -14.121 0.704   6.539   1.00 7.45   ? 118 ILE B N   1 
ATOM   3069 C  CA  . ILE B  1 118 ? -15.491 1.305   6.618   1.00 8.36   ? 118 ILE B CA  1 
ATOM   3070 C  C   . ILE B  1 118 ? -15.453 2.269   7.733   1.00 8.26   ? 118 ILE B C   1 
ATOM   3071 O  O   . ILE B  1 118 ? -15.334 1.916   8.921   1.00 8.72   ? 118 ILE B O   1 
ATOM   3072 C  CB  . ILE B  1 118 ? -16.588 0.219   6.818   1.00 8.82   ? 118 ILE B CB  1 
ATOM   3073 C  CG1 . ILE B  1 118 ? -16.425 -0.932  5.814   1.00 9.61   ? 118 ILE B CG1 1 
ATOM   3074 C  CG2 . ILE B  1 118 ? -17.933 0.951   6.705   1.00 10.69  ? 118 ILE B CG2 1 
ATOM   3075 C  CD1 . ILE B  1 118 ? -17.465 -2.045  6.029   1.00 11.51  ? 118 ILE B CD1 1 
ATOM   3076 N  N   . VAL B  1 119 ? -15.480 3.569   7.409   1.00 8.26   ? 119 VAL B N   1 
ATOM   3077 C  CA  . VAL B  1 119 ? -15.263 4.663   8.347   1.00 8.33   ? 119 VAL B CA  1 
ATOM   3078 C  C   . VAL B  1 119 ? -16.624 5.105   8.950   1.00 8.80   ? 119 VAL B C   1 
ATOM   3079 O  O   . VAL B  1 119 ? -17.559 5.358   8.181   1.00 9.88   ? 119 VAL B O   1 
ATOM   3080 C  CB  . VAL B  1 119 ? -14.566 5.862   7.680   1.00 9.08   ? 119 VAL B CB  1 
ATOM   3081 C  CG1 . VAL B  1 119 ? -14.260 6.946   8.699   1.00 11.37  ? 119 VAL B CG1 1 
ATOM   3082 C  CG2 . VAL B  1 119 ? -13.277 5.432   6.962   1.00 9.64   ? 119 VAL B CG2 1 
ATOM   3083 N  N   . HIS B  1 120 ? -16.679 5.199   10.271  1.00 9.14   ? 120 HIS B N   1 
ATOM   3084 C  CA  . HIS B  1 120 ? -17.862 5.638   10.965  1.00 10.36  ? 120 HIS B CA  1 
ATOM   3085 C  C   . HIS B  1 120 ? -17.441 6.766   11.917  1.00 10.63  ? 120 HIS B C   1 
ATOM   3086 O  O   . HIS B  1 120 ? -16.262 6.901   12.298  1.00 10.83  ? 120 HIS B O   1 
ATOM   3087 C  CB  . HIS B  1 120 ? -18.435 4.474   11.826  1.00 9.87   ? 120 HIS B CB  1 
ATOM   3088 C  CG  . HIS B  1 120 ? -18.807 3.263   11.116  1.00 9.43   ? 120 HIS B CG  1 
ATOM   3089 N  ND1 . HIS B  1 120 ? -17.870 2.393   10.548  1.00 10.02  ? 120 HIS B ND1 1 
ATOM   3090 C  CD2 . HIS B  1 120 ? -19.979 2.690   10.887  1.00 10.88  ? 120 HIS B CD2 1 
ATOM   3091 C  CE1 . HIS B  1 120 ? -18.527 1.347   10.032  1.00 10.94  ? 120 HIS B CE1 1 
ATOM   3092 N  NE2 . HIS B  1 120 ? -19.838 1.484   10.248  1.00 10.55  ? 120 HIS B NE2 1 
ATOM   3093 N  N   . TYR B  1 121 ? -18.424 7.582   12.314  1.00 11.73  ? 121 TYR B N   1 
ATOM   3094 C  CA  . TYR B  1 121 ? -18.136 8.665   13.237  1.00 13.00  ? 121 TYR B CA  1 
ATOM   3095 C  C   . TYR B  1 121 ? -19.138 8.650   14.364  1.00 12.85  ? 121 TYR B C   1 
ATOM   3096 O  O   . TYR B  1 121 ? -20.228 8.146   14.256  1.00 12.92  ? 121 TYR B O   1 
ATOM   3097 C  CB  . TYR B  1 121 ? -18.170 10.056  12.536  1.00 14.07  ? 121 TYR B CB  1 
ATOM   3098 C  CG  . TYR B  1 121 ? -19.566 10.500  12.084  1.00 13.78  ? 121 TYR B CG  1 
ATOM   3099 C  CD1 . TYR B  1 121 ? -20.161 10.023  10.899  1.00 15.02  ? 121 TYR B CD1 1 
ATOM   3100 C  CD2 . TYR B  1 121 ? -20.266 11.475  12.889  1.00 16.21  ? 121 TYR B CD2 1 
ATOM   3101 C  CE1 . TYR B  1 121 ? -21.434 10.463  10.534  1.00 17.21  ? 121 TYR B CE1 1 
ATOM   3102 C  CE2 . TYR B  1 121 ? -21.555 11.918  12.454  1.00 19.80  ? 121 TYR B CE2 1 
ATOM   3103 C  CZ  . TYR B  1 121 ? -22.133 11.335  11.331  1.00 20.33  ? 121 TYR B CZ  1 
ATOM   3104 O  OH  . TYR B  1 121 ? -23.363 11.781  11.014  1.00 27.87  ? 121 TYR B OH  1 
ATOM   3105 N  N   . ASN B  1 122 ? -18.749 9.264   15.479  1.00 13.48  ? 122 ASN B N   1 
ATOM   3106 C  CA  . ASN B  1 122 ? -19.642 9.322   16.659  1.00 14.61  ? 122 ASN B CA  1 
ATOM   3107 C  C   . ASN B  1 122 ? -20.772 10.326  16.447  1.00 15.34  ? 122 ASN B C   1 
ATOM   3108 O  O   . ASN B  1 122 ? -20.557 11.558  16.656  1.00 16.00  ? 122 ASN B O   1 
ATOM   3109 C  CB  . ASN B  1 122 ? -18.816 9.650   17.877  1.00 14.95  ? 122 ASN B CB  1 
ATOM   3110 C  CG  . ASN B  1 122 ? -19.677 9.527   19.155  1.00 19.80  ? 122 ASN B CG  1 
ATOM   3111 O  OD1 . ASN B  1 122 ? -20.890 9.696   19.110  1.00 19.42  ? 122 ASN B OD1 1 
ATOM   3112 N  ND2 . ASN B  1 122 ? -19.012 9.270   20.257  1.00 24.30  ? 122 ASN B ND2 1 
ATOM   3113 N  N   . SER B  1 123 ? -21.904 9.835   15.930  1.00 16.46  ? 123 SER B N   1 
ATOM   3114 C  CA  . SER B  1 123 ? -23.074 10.719  15.595  1.00 18.52  ? 123 SER B CA  1 
ATOM   3115 C  C   . SER B  1 123 ? -23.836 11.118  16.843  1.00 22.26  ? 123 SER B C   1 
ATOM   3116 O  O   . SER B  1 123 ? -24.709 12.015  16.771  1.00 20.81  ? 123 SER B O   1 
ATOM   3117 C  CB  . SER B  1 123 ? -23.927 10.096  14.512  1.00 17.64  ? 123 SER B CB  1 
ATOM   3118 O  OG  . SER B  1 123 ? -24.225 8.775   14.968  1.00 19.44  ? 123 SER B OG  1 
ATOM   3119 N  N   . ASP B  1 124 ? -23.645 10.424  17.977  1.00 18.54  ? 124 ASP B N   1 
ATOM   3120 C  CA  . ASP B  1 124 ? -24.227 10.934  19.213  1.00 20.46  ? 124 ASP B CA  1 
ATOM   3121 C  C   . ASP B  1 124 ? -23.615 12.240  19.633  1.00 23.18  ? 124 ASP B C   1 
ATOM   3122 O  O   . ASP B  1 124 ? -24.393 13.075  20.193  1.00 22.79  ? 124 ASP B O   1 
ATOM   3123 C  CB  . ASP B  1 124 ? -23.964 9.969   20.363  1.00 23.31  ? 124 ASP B CB  1 
ATOM   3124 C  CG  . ASP B  1 124 ? -24.828 8.672   20.224  1.00 24.27  ? 124 ASP B CG  1 
ATOM   3125 O  OD1 . ASP B  1 124 ? -25.795 8.686   19.431  1.00 25.65  ? 124 ASP B OD1 1 
ATOM   3126 O  OD2 . ASP B  1 124 ? -24.589 7.635   20.866  1.00 26.86  ? 124 ASP B OD2 1 
ATOM   3127 N  N   . LEU B  1 125 ? -22.352 12.514  19.376  1.00 19.42  ? 125 LEU B N   1 
ATOM   3128 C  CA  . LEU B  1 125 ? -21.669 13.674  19.882  1.00 20.21  ? 125 LEU B CA  1 
ATOM   3129 C  C   . LEU B  1 125 ? -21.470 14.730  18.774  1.00 20.52  ? 125 LEU B C   1 
ATOM   3130 O  O   . LEU B  1 125 ? -21.381 15.943  19.083  1.00 24.77  ? 125 LEU B O   1 
ATOM   3131 C  CB  . LEU B  1 125 ? -20.317 13.335  20.435  1.00 20.58  ? 125 LEU B CB  1 
ATOM   3132 C  CG  . LEU B  1 125 ? -20.322 12.410  21.640  1.00 22.94  ? 125 LEU B CG  1 
ATOM   3133 C  CD1 . LEU B  1 125 ? -18.955 12.118  22.180  1.00 22.72  ? 125 LEU B CD1 1 
ATOM   3134 C  CD2 . LEU B  1 125 ? -21.156 12.971  22.853  1.00 26.64  ? 125 LEU B CD2 1 
ATOM   3135 N  N   . TYR B  1 126 ? -21.292 14.329  17.502  1.00 19.74  ? 126 TYR B N   1 
ATOM   3136 C  CA  . TYR B  1 126 ? -20.984 15.262  16.445  1.00 20.29  ? 126 TYR B CA  1 
ATOM   3137 C  C   . TYR B  1 126 ? -21.919 15.259  15.333  1.00 20.76  ? 126 TYR B C   1 
ATOM   3138 O  O   . TYR B  1 126 ? -22.493 14.203  15.054  1.00 22.49  ? 126 TYR B O   1 
ATOM   3139 C  CB  . TYR B  1 126 ? -19.529 14.920  15.962  1.00 21.08  ? 126 TYR B CB  1 
ATOM   3140 C  CG  . TYR B  1 126 ? -18.579 14.782  17.119  1.00 19.37  ? 126 TYR B CG  1 
ATOM   3141 C  CD1 . TYR B  1 126 ? -18.314 15.904  17.911  1.00 23.66  ? 126 TYR B CD1 1 
ATOM   3142 C  CD2 . TYR B  1 126 ? -18.033 13.538  17.505  1.00 20.33  ? 126 TYR B CD2 1 
ATOM   3143 C  CE1 . TYR B  1 126 ? -17.474 15.822  19.050  1.00 21.55  ? 126 TYR B CE1 1 
ATOM   3144 C  CE2 . TYR B  1 126 ? -17.173 13.403  18.571  1.00 19.92  ? 126 TYR B CE2 1 
ATOM   3145 C  CZ  . TYR B  1 126 ? -16.929 14.559  19.395  1.00 24.96  ? 126 TYR B CZ  1 
ATOM   3146 O  OH  . TYR B  1 126 ? -16.070 14.483  20.530  1.00 27.96  ? 126 TYR B OH  1 
ATOM   3147 N  N   . PRO B  1 127 ? -22.025 16.406  14.625  1.00 22.96  ? 127 PRO B N   1 
ATOM   3148 C  CA  . PRO B  1 127 ? -23.038 16.477  13.563  1.00 28.54  ? 127 PRO B CA  1 
ATOM   3149 C  C   . PRO B  1 127 ? -22.576 16.043  12.232  1.00 26.81  ? 127 PRO B C   1 
ATOM   3150 O  O   . PRO B  1 127 ? -23.401 15.971  11.353  1.00 28.81  ? 127 PRO B O   1 
ATOM   3151 C  CB  . PRO B  1 127 ? -23.338 17.993  13.486  1.00 34.78  ? 127 PRO B CB  1 
ATOM   3152 C  CG  . PRO B  1 127 ? -22.041 18.677  13.905  1.00 26.95  ? 127 PRO B CG  1 
ATOM   3153 C  CD  . PRO B  1 127 ? -21.537 17.780  15.017  1.00 24.60  ? 127 PRO B CD  1 
ATOM   3154 N  N   . ASP B  1 128 ? -21.275 15.601  12.113  1.00 21.16  ? 128 ASP B N   1 
ATOM   3155 C  CA  . ASP B  1 128 ? -20.738 15.159  10.857  1.00 20.54  ? 128 ASP B CA  1 
ATOM   3156 C  C   . ASP B  1 128 ? -19.391 14.584  11.163  1.00 18.80  ? 128 ASP B C   1 
ATOM   3157 O  O   . ASP B  1 128 ? -18.756 14.851  12.190  1.00 18.34  ? 128 ASP B O   1 
ATOM   3158 C  CB  . ASP B  1 128 ? -20.557 16.355  9.826   1.00 21.85  ? 128 ASP B CB  1 
ATOM   3159 C  CG  . ASP B  1 128 ? -19.666 17.372  10.348  1.00 24.09  ? 128 ASP B CG  1 
ATOM   3160 O  OD1 . ASP B  1 128 ? -20.048 18.261  11.175  1.00 30.05  ? 128 ASP B OD1 1 
ATOM   3161 O  OD2 . ASP B  1 128 ? -18.496 17.360  9.947   1.00 24.39  ? 128 ASP B OD2 1 
ATOM   3162 N  N   . ALA B  1 129 ? -18.946 13.759  10.213  1.00 19.26  ? 129 ALA B N   1 
ATOM   3163 C  CA  . ALA B  1 129 ? -17.708 13.040  10.380  1.00 17.52  ? 129 ALA B CA  1 
ATOM   3164 C  C   . ALA B  1 129 ? -16.438 13.948  10.376  1.00 16.37  ? 129 ALA B C   1 
ATOM   3165 O  O   . ALA B  1 129 ? -15.485 13.700  11.073  1.00 17.78  ? 129 ALA B O   1 
ATOM   3166 C  CB  . ALA B  1 129 ? -17.601 12.004  9.217   1.00 21.05  ? 129 ALA B CB  1 
ATOM   3167 N  N   A SER B  1 130 ? -16.530 15.083  9.644   0.50 19.00  ? 130 SER B N   1 
ATOM   3168 N  N   B SER B  1 130 ? -16.407 15.039  9.596   0.50 18.17  ? 130 SER B N   1 
ATOM   3169 C  CA  A SER B  1 130 ? -15.387 15.990  9.527   0.50 20.17  ? 130 SER B CA  1 
ATOM   3170 C  CA  B SER B  1 130 ? -15.186 15.887  9.625   0.50 18.08  ? 130 SER B CA  1 
ATOM   3171 C  C   A SER B  1 130 ? -15.073 16.587  10.909  0.50 20.11  ? 130 SER B C   1 
ATOM   3172 C  C   B SER B  1 130 ? -15.048 16.498  11.053  0.50 17.14  ? 130 SER B C   1 
ATOM   3173 O  O   A SER B  1 130 ? -13.889 16.666  11.328  0.50 21.04  ? 130 SER B O   1 
ATOM   3174 O  O   B SER B  1 130 ? -13.959 16.511  11.682  0.50 17.00  ? 130 SER B O   1 
ATOM   3175 C  CB  A SER B  1 130 ? -15.681 17.142  8.538   0.50 22.75  ? 130 SER B CB  1 
ATOM   3176 C  CB  B SER B  1 130 ? -15.278 17.021  8.557   0.50 18.37  ? 130 SER B CB  1 
ATOM   3177 O  OG  A SER B  1 130 ? -15.521 16.634  7.232   0.50 27.97  ? 130 SER B OG  1 
ATOM   3178 O  OG  B SER B  1 130 ? -14.200 17.884  8.604   0.50 22.71  ? 130 SER B OG  1 
ATOM   3179 N  N   . THR B  1 131 ? -16.135 17.070  11.567  1.00 20.48  ? 131 THR B N   1 
ATOM   3180 C  CA  . THR B  1 131 ? -16.016 17.534  13.000  1.00 19.80  ? 131 THR B CA  1 
ATOM   3181 C  C   . THR B  1 131 ? -15.532 16.448  13.939  1.00 21.18  ? 131 THR B C   1 
ATOM   3182 O  O   . THR B  1 131 ? -14.617 16.700  14.754  1.00 21.69  ? 131 THR B O   1 
ATOM   3183 C  CB  . THR B  1 131 ? -17.396 17.931  13.481  1.00 24.01  ? 131 THR B CB  1 
ATOM   3184 O  OG1 . THR B  1 131 ? -17.857 19.014  12.655  1.00 26.02  ? 131 THR B OG1 1 
ATOM   3185 C  CG2 . THR B  1 131 ? -17.407 18.446  15.020  1.00 26.29  ? 131 THR B CG2 1 
ATOM   3186 N  N   . ALA B  1 132 ? -16.078 15.217  13.816  1.00 17.69  ? 132 ALA B N   1 
ATOM   3187 C  CA  . ALA B  1 132 ? -15.693 14.099  14.717  1.00 17.90  ? 132 ALA B CA  1 
ATOM   3188 C  C   . ALA B  1 132 ? -14.202 13.781  14.504  1.00 16.76  ? 132 ALA B C   1 
ATOM   3189 O  O   . ALA B  1 132 ? -13.587 13.229  15.467  1.00 16.73  ? 132 ALA B O   1 
ATOM   3190 C  CB  . ALA B  1 132 ? -16.526 12.861  14.369  1.00 16.75  ? 132 ALA B CB  1 
ATOM   3191 N  N   . SER B  1 133 ? -13.695 13.995  13.276  1.00 16.21  ? 133 SER B N   1 
ATOM   3192 C  CA  . SER B  1 133 ? -12.319 13.444  12.936  1.00 15.47  ? 133 SER B CA  1 
ATOM   3193 C  C   . SER B  1 133 ? -11.201 14.033  13.698  1.00 15.95  ? 133 SER B C   1 
ATOM   3194 O  O   . SER B  1 133 ? -10.117 13.465  13.799  1.00 18.00  ? 133 SER B O   1 
ATOM   3195 C  CB  . SER B  1 133 ? -12.009 13.591  11.463  1.00 18.10  ? 133 SER B CB  1 
ATOM   3196 O  OG  . SER B  1 133 ? -11.800 14.928  11.089  1.00 18.11  ? 133 SER B OG  1 
ATOM   3197 N  N   . ASN B  1 134 ? -11.446 15.144  14.351  1.00 19.82  ? 134 ASN B N   1 
ATOM   3198 C  CA  . ASN B  1 134 ? -10.338 15.655  15.153  1.00 21.02  ? 134 ASN B CA  1 
ATOM   3199 C  C   . ASN B  1 134 ? -10.594 15.630  16.664  1.00 20.81  ? 134 ASN B C   1 
ATOM   3200 O  O   . ASN B  1 134 ? -9.916  16.309  17.432  1.00 26.51  ? 134 ASN B O   1 
ATOM   3201 C  CB  . ASN B  1 134 ? -9.657  16.930  14.609  1.00 31.54  ? 134 ASN B CB  1 
ATOM   3202 C  CG  . ASN B  1 134 ? -10.592 18.107  14.481  1.00 37.37  ? 134 ASN B CG  1 
ATOM   3203 O  OD1 . ASN B  1 134 ? -11.797 17.993  14.687  1.00 37.80  ? 134 ASN B OD1 1 
ATOM   3204 N  ND2 . ASN B  1 134 ? -10.030 19.261  14.134  1.00 36.90  ? 134 ASN B ND2 1 
ATOM   3205 N  N   . LYS B  1 135 ? -11.587 14.830  17.063  1.00 19.49  ? 135 LYS B N   1 
ATOM   3206 C  CA  . LYS B  1 135 ? -11.912 14.572  18.534  1.00 23.41  ? 135 LYS B CA  1 
ATOM   3207 C  C   . LYS B  1 135 ? -11.564 13.200  18.997  1.00 25.10  ? 135 LYS B C   1 
ATOM   3208 O  O   . LYS B  1 135 ? -11.702 12.282  18.279  1.00 20.01  ? 135 LYS B O   1 
ATOM   3209 C  CB  . LYS B  1 135 ? -13.378 14.741  18.825  1.00 28.36  ? 135 LYS B CB  1 
ATOM   3210 C  CG  . LYS B  1 135 ? -13.934 15.979  18.075  1.00 35.43  ? 135 LYS B CG  1 
ATOM   3211 C  CD  . LYS B  1 135 ? -14.008 17.282  18.786  1.00 56.81  ? 135 LYS B CD  1 
ATOM   3212 C  CE  . LYS B  1 135 ? -13.557 18.516  17.958  1.00 63.93  ? 135 LYS B CE  1 
ATOM   3213 N  NZ  . LYS B  1 135 ? -14.245 18.829  16.636  1.00 47.49  ? 135 LYS B NZ  1 
ATOM   3214 N  N   . SER B  1 136 ? -11.268 13.082  20.334  1.00 36.76  ? 136 SER B N   1 
ATOM   3215 C  CA  . SER B  1 136 ? -10.814 11.737  20.880  1.00 39.83  ? 136 SER B CA  1 
ATOM   3216 C  C   . SER B  1 136 ? -11.825 10.633  20.577  1.00 25.45  ? 136 SER B C   1 
ATOM   3217 O  O   . SER B  1 136 ? -12.912 10.886  20.814  1.00 22.87  ? 136 SER B O   1 
ATOM   3218 C  CB  . SER B  1 136 ? -10.528 11.841  22.449  1.00 53.27  ? 136 SER B CB  1 
ATOM   3219 N  N   . GLU B  1 137 ? -11.483 9.467   20.016  1.00 24.81  ? 137 GLU B N   1 
ATOM   3220 C  CA  . GLU B  1 137 ? -12.505 8.395   19.712  1.00 23.94  ? 137 GLU B CA  1 
ATOM   3221 C  C   . GLU B  1 137 ? -13.682 8.961   18.810  1.00 20.49  ? 137 GLU B C   1 
ATOM   3222 O  O   . GLU B  1 137 ? -14.754 8.371   18.926  1.00 22.43  ? 137 GLU B O   1 
ATOM   3223 C  CB  . GLU B  1 137 ? -13.090 7.792   21.006  1.00 33.27  ? 137 GLU B CB  1 
ATOM   3224 N  N   . GLY B  1 138 ? -13.498 10.104  18.073  1.00 15.73  ? 138 GLY B N   1 
ATOM   3225 C  CA  . GLY B  1 138 ? -14.468 10.603  17.139  1.00 14.13  ? 138 GLY B CA  1 
ATOM   3226 C  C   . GLY B  1 138 ? -14.811 9.623   16.040  1.00 12.79  ? 138 GLY B C   1 
ATOM   3227 O  O   . GLY B  1 138 ? -15.913 9.704   15.477  1.00 14.40  ? 138 GLY B O   1 
ATOM   3228 N  N   . LEU B  1 139 ? -13.888 8.753   15.671  1.00 11.27  ? 139 LEU B N   1 
ATOM   3229 C  CA  . LEU B  1 139 ? -14.084 7.856   14.526  1.00 10.84  ? 139 LEU B CA  1 
ATOM   3230 C  C   . LEU B  1 139 ? -13.945 6.411   14.948  1.00 10.35  ? 139 LEU B C   1 
ATOM   3231 O  O   . LEU B  1 139 ? -13.202 6.095   15.892  1.00 11.27  ? 139 LEU B O   1 
ATOM   3232 C  CB  . LEU B  1 139 ? -13.043 8.123   13.414  1.00 11.55  ? 139 LEU B CB  1 
ATOM   3233 C  CG  . LEU B  1 139 ? -13.096 9.544   12.841  1.00 11.77  ? 139 LEU B CG  1 
ATOM   3234 C  CD1 . LEU B  1 139 ? -11.949 9.702   11.849  1.00 14.73  ? 139 LEU B CD1 1 
ATOM   3235 C  CD2 . LEU B  1 139 ? -14.430 9.913   12.176  1.00 13.57  ? 139 LEU B CD2 1 
ATOM   3236 N  N   . ALA B  1 140 ? -14.612 5.514   14.251  1.00 10.89  ? 140 ALA B N   1 
ATOM   3237 C  CA  . ALA B  1 140 ? -14.436 4.075   14.447  1.00 9.74   ? 140 ALA B CA  1 
ATOM   3238 C  C   . ALA B  1 140 ? -14.350 3.497   13.053  1.00 10.09  ? 140 ALA B C   1 
ATOM   3239 O  O   . ALA B  1 140 ? -15.222 3.771   12.188  1.00 11.10  ? 140 ALA B O   1 
ATOM   3240 C  CB  . ALA B  1 140 ? -15.588 3.468   15.191  1.00 12.04  ? 140 ALA B CB  1 
ATOM   3241 N  N   . VAL B  1 141 ? -13.307 2.722   12.763  1.00 8.99   ? 141 VAL B N   1 
ATOM   3242 C  CA  . VAL B  1 141 ? -13.125 2.134   11.463  1.00 8.17   ? 141 VAL B CA  1 
ATOM   3243 C  C   . VAL B  1 141 ? -13.219 0.622   11.612  1.00 8.49   ? 141 VAL B C   1 
ATOM   3244 O  O   . VAL B  1 141 ? -12.604 0.041   12.546  1.00 9.56   ? 141 VAL B O   1 
ATOM   3245 C  CB  . VAL B  1 141 ? -11.780 2.534   10.832  1.00 9.61   ? 141 VAL B CB  1 
ATOM   3246 C  CG1 . VAL B  1 141 ? -11.617 1.829   9.424   1.00 11.16  ? 141 VAL B CG1 1 
ATOM   3247 C  CG2 . VAL B  1 141 ? -11.711 4.056   10.665  1.00 11.44  ? 141 VAL B CG2 1 
ATOM   3248 N  N   . LEU B  1 142 ? -13.929 -0.031  10.674  1.00 7.97   ? 142 LEU B N   1 
ATOM   3249 C  CA  . LEU B  1 142 ? -13.881 -1.490  10.514  1.00 8.32   ? 142 LEU B CA  1 
ATOM   3250 C  C   . LEU B  1 142 ? -12.938 -1.781  9.429   1.00 7.72   ? 142 LEU B C   1 
ATOM   3251 O  O   . LEU B  1 142 ? -13.071 -1.251  8.294   1.00 9.77   ? 142 LEU B O   1 
ATOM   3252 C  CB  . LEU B  1 142 ? -15.234 -2.040  10.187  1.00 9.84   ? 142 LEU B CB  1 
ATOM   3253 C  CG  . LEU B  1 142 ? -16.375 -1.737  11.125  1.00 10.39  ? 142 LEU B CG  1 
ATOM   3254 C  CD1 . LEU B  1 142 ? -17.654 -2.433  10.572  1.00 13.04  ? 142 LEU B CD1 1 
ATOM   3255 C  CD2 . LEU B  1 142 ? -16.064 -2.137  12.555  1.00 11.65  ? 142 LEU B CD2 1 
ATOM   3256 N  N   . ALA B  1 143 ? -11.922 -2.655  9.683   1.00 8.20   ? 143 ALA B N   1 
ATOM   3257 C  CA  . ALA B  1 143 ? -10.956 -3.040  8.668   1.00 7.67   ? 143 ALA B CA  1 
ATOM   3258 C  C   . ALA B  1 143 ? -11.120 -4.505  8.336   1.00 7.47   ? 143 ALA B C   1 
ATOM   3259 O  O   . ALA B  1 143 ? -11.167 -5.367  9.211   1.00 8.50   ? 143 ALA B O   1 
ATOM   3260 C  CB  . ALA B  1 143 ? -9.530  -2.801  9.202   1.00 9.22   ? 143 ALA B CB  1 
ATOM   3261 N  N   . VAL B  1 144 ? -11.207 -4.767  7.015   1.00 7.95   ? 144 VAL B N   1 
ATOM   3262 C  CA  . VAL B  1 144 ? -11.296 -6.138  6.500   1.00 7.89   ? 144 VAL B CA  1 
ATOM   3263 C  C   . VAL B  1 144 ? -10.027 -6.365  5.691   1.00 7.97   ? 144 VAL B C   1 
ATOM   3264 O  O   . VAL B  1 144 ? -9.747  -5.661  4.703   1.00 8.45   ? 144 VAL B O   1 
ATOM   3265 C  CB  . VAL B  1 144 ? -12.547 -6.342  5.602   1.00 8.45   ? 144 VAL B CB  1 
ATOM   3266 C  CG1 . VAL B  1 144 ? -12.613 -7.767  5.117   1.00 10.11  ? 144 VAL B CG1 1 
ATOM   3267 C  CG2 . VAL B  1 144 ? -13.842 -5.942  6.333   1.00 9.66   ? 144 VAL B CG2 1 
ATOM   3268 N  N   . LEU B  1 145 ? -9.304  -7.420  6.036   1.00 7.96   ? 145 LEU B N   1 
ATOM   3269 C  CA  . LEU B  1 145 ? -8.130  -7.861  5.338   1.00 8.45   ? 145 LEU B CA  1 
ATOM   3270 C  C   . LEU B  1 145 ? -8.594  -8.678  4.125   1.00 8.07   ? 145 LEU B C   1 
ATOM   3271 O  O   . LEU B  1 145 ? -9.518  -9.496  4.243   1.00 9.11   ? 145 LEU B O   1 
ATOM   3272 C  CB  . LEU B  1 145 ? -7.263  -8.714  6.247   1.00 10.14  ? 145 LEU B CB  1 
ATOM   3273 C  CG  . LEU B  1 145 ? -6.744  -7.985  7.491   1.00 10.95  ? 145 LEU B CG  1 
ATOM   3274 C  CD1 . LEU B  1 145 ? -6.203  -8.989  8.506   1.00 13.60  ? 145 LEU B CD1 1 
ATOM   3275 C  CD2 . LEU B  1 145 ? -5.700  -6.979  7.063   1.00 14.63  ? 145 LEU B CD2 1 
ATOM   3276 N  N   . ILE B  1 146 ? -7.972  -8.427  2.955   1.00 8.83   ? 146 ILE B N   1 
ATOM   3277 C  CA  . ILE B  1 146 ? -8.416  -9.070  1.706   1.00 8.95   ? 146 ILE B CA  1 
ATOM   3278 C  C   . ILE B  1 146 ? -7.278  -9.890  1.157   1.00 9.14   ? 146 ILE B C   1 
ATOM   3279 O  O   . ILE B  1 146 ? -6.157  -9.389  0.975   1.00 9.98   ? 146 ILE B O   1 
ATOM   3280 C  CB  . ILE B  1 146 ? -8.850  -8.013  0.678   1.00 9.02   ? 146 ILE B CB  1 
ATOM   3281 C  CG1 . ILE B  1 146 ? -9.981  -7.150  1.227   1.00 9.90   ? 146 ILE B CG1 1 
ATOM   3282 C  CG2 . ILE B  1 146 ? -9.131  -8.633  -0.659  1.00 10.54  ? 146 ILE B CG2 1 
ATOM   3283 C  CD1 . ILE B  1 146 ? -10.247 -5.880  0.434   1.00 10.82  ? 146 ILE B CD1 1 
ATOM   3284 N  N   . GLU B  1 147 ? -7.546  -11.151 0.853   1.00 9.47   ? 147 GLU B N   1 
ATOM   3285 C  CA  . GLU B  1 147 ? -6.544  -12.023 0.290   1.00 10.67  ? 147 GLU B CA  1 
ATOM   3286 C  C   . GLU B  1 147 ? -6.941  -12.468 -1.095  1.00 9.66   ? 147 GLU B C   1 
ATOM   3287 O  O   . GLU B  1 147 ? -8.117  -12.436 -1.475  1.00 10.80  ? 147 GLU B O   1 
ATOM   3288 C  CB  . GLU B  1 147 ? -6.449  -13.330 1.194   1.00 17.04  ? 147 GLU B CB  1 
ATOM   3289 C  CG  . GLU B  1 147 ? -7.442  -14.397 1.129   1.00 25.54  ? 147 GLU B CG  1 
ATOM   3290 C  CD  . GLU B  1 147 ? -7.265  -15.464 2.217   1.00 29.88  ? 147 GLU B CD  1 
ATOM   3291 O  OE1 . GLU B  1 147 ? -6.254  -15.376 2.946   1.00 25.32  ? 147 GLU B OE1 1 
ATOM   3292 O  OE2 . GLU B  1 147 ? -8.087  -16.393 2.383   1.00 37.20  ? 147 GLU B OE2 1 
ATOM   3293 N  N   . MET B  1 148 ? -5.993  -12.787 -1.949  1.00 9.68   ? 148 MET B N   1 
ATOM   3294 C  CA  . MET B  1 148 ? -6.243  -13.280 -3.260  1.00 10.13  ? 148 MET B CA  1 
ATOM   3295 C  C   . MET B  1 148 ? -6.849  -14.674 -3.190  1.00 10.47  ? 148 MET B C   1 
ATOM   3296 O  O   . MET B  1 148 ? -6.302  -15.561 -2.543  1.00 11.98  ? 148 MET B O   1 
ATOM   3297 C  CB  . MET B  1 148 ? -4.955  -13.321 -4.058  1.00 11.11  ? 148 MET B CB  1 
ATOM   3298 C  CG  . MET B  1 148 ? -5.157  -13.710 -5.530  1.00 12.98  ? 148 MET B CG  1 
ATOM   3299 S  SD  . MET B  1 148 ? -3.649  -13.819 -6.498  1.00 15.53  ? 148 MET B SD  1 
ATOM   3300 C  CE  . MET B  1 148 ? -3.200  -12.146 -6.493  1.00 15.87  ? 148 MET B CE  1 
ATOM   3301 N  N   . GLY B  1 149 ? -8.013  -14.876 -3.790  1.00 9.91   ? 149 GLY B N   1 
ATOM   3302 C  CA  . GLY B  1 149 ? -8.736  -16.145 -3.672  1.00 10.66  ? 149 GLY B CA  1 
ATOM   3303 C  C   . GLY B  1 149 ? -9.826  -16.196 -4.723  1.00 9.56   ? 149 GLY B C   1 
ATOM   3304 O  O   . GLY B  1 149 ? -9.642  -15.898 -5.894  1.00 10.29  ? 149 GLY B O   1 
ATOM   3305 N  N   . SER B  1 150 ? -11.004 -16.606 -4.253  1.00 9.95   ? 150 SER B N   1 
ATOM   3306 C  CA  . SER B  1 150 ? -12.197 -16.701 -5.124  1.00 9.99   ? 150 SER B CA  1 
ATOM   3307 C  C   . SER B  1 150 ? -12.706 -15.365 -5.505  1.00 10.31  ? 150 SER B C   1 
ATOM   3308 O  O   . SER B  1 150 ? -12.654 -14.368 -4.737  1.00 11.15  ? 150 SER B O   1 
ATOM   3309 C  CB  . SER B  1 150 ? -13.297 -17.453 -4.417  1.00 10.92  ? 150 SER B CB  1 
ATOM   3310 O  OG  . SER B  1 150 ? -12.922 -18.820 -4.229  1.00 11.77  ? 150 SER B OG  1 
ATOM   3311 N  N   . PHE B  1 151 ? -13.343 -15.313 -6.695  1.00 10.49  ? 151 PHE B N   1 
ATOM   3312 C  CA  . PHE B  1 151 ? -14.142 -14.139 -7.116  1.00 10.29  ? 151 PHE B CA  1 
ATOM   3313 C  C   . PHE B  1 151 ? -15.167 -13.822 -6.105  1.00 10.89  ? 151 PHE B C   1 
ATOM   3314 O  O   . PHE B  1 151 ? -15.865 -14.710 -5.576  1.00 12.85  ? 151 PHE B O   1 
ATOM   3315 C  CB  . PHE B  1 151 ? -14.736 -14.465 -8.437  1.00 11.70  ? 151 PHE B CB  1 
ATOM   3316 C  CG  . PHE B  1 151 ? -15.611 -13.329 -8.984  1.00 11.99  ? 151 PHE B CG  1 
ATOM   3317 C  CD1 . PHE B  1 151 ? -15.006 -12.232 -9.629  1.00 12.54  ? 151 PHE B CD1 1 
ATOM   3318 C  CD2 . PHE B  1 151 ? -17.014 -13.330 -8.829  1.00 13.04  ? 151 PHE B CD2 1 
ATOM   3319 C  CE1 . PHE B  1 151 ? -15.760 -11.157 -10.132 1.00 14.20  ? 151 PHE B CE1 1 
ATOM   3320 C  CE2 . PHE B  1 151 ? -17.773 -12.274 -9.327  1.00 14.79  ? 151 PHE B CE2 1 
ATOM   3321 C  CZ  . PHE B  1 151 ? -17.121 -11.210 -9.948  1.00 14.55  ? 151 PHE B CZ  1 
ATOM   3322 N  N   . ASN B  1 152 ? -15.353 -12.515 -5.808  1.00 9.98   ? 152 ASN B N   1 
ATOM   3323 C  CA  . ASN B  1 152 ? -16.258 -12.085 -4.794  1.00 9.50   ? 152 ASN B CA  1 
ATOM   3324 C  C   . ASN B  1 152 ? -17.334 -11.174 -5.415  1.00 9.92   ? 152 ASN B C   1 
ATOM   3325 O  O   . ASN B  1 152 ? -17.014 -9.995  -5.755  1.00 9.90   ? 152 ASN B O   1 
ATOM   3326 C  CB  . ASN B  1 152 ? -15.455 -11.325 -3.687  1.00 10.05  ? 152 ASN B CB  1 
ATOM   3327 C  CG  . ASN B  1 152 ? -16.268 -11.060 -2.489  1.00 10.11  ? 152 ASN B CG  1 
ATOM   3328 O  OD1 . ASN B  1 152 ? -17.391 -10.531 -2.590  1.00 12.12  ? 152 ASN B OD1 1 
ATOM   3329 N  ND2 . ASN B  1 152 ? -15.682 -11.382 -1.332  1.00 11.06  ? 152 ASN B ND2 1 
ATOM   3330 N  N   . PRO B  1 153 ? -18.552 -11.664 -5.610  1.00 10.55  ? 153 PRO B N   1 
ATOM   3331 C  CA  . PRO B  1 153 ? -19.543 -10.845 -6.338  1.00 11.15  ? 153 PRO B CA  1 
ATOM   3332 C  C   . PRO B  1 153 ? -19.847 -9.590  -5.558  1.00 11.59  ? 153 PRO B C   1 
ATOM   3333 O  O   . PRO B  1 153 ? -20.242 -8.589  -6.184  1.00 13.47  ? 153 PRO B O   1 
ATOM   3334 C  CB  . PRO B  1 153 ? -20.778 -11.807 -6.435  1.00 15.62  ? 153 PRO B CB  1 
ATOM   3335 C  CG  . PRO B  1 153 ? -20.228 -13.179 -6.298  1.00 18.72  ? 153 PRO B CG  1 
ATOM   3336 C  CD  . PRO B  1 153 ? -18.978 -13.065 -5.383  1.00 13.70  ? 153 PRO B CD  1 
ATOM   3337 N  N   . SER B  1 154 ? -19.802 -9.579  -4.239  1.00 10.99  ? 154 SER B N   1 
ATOM   3338 C  CA  . SER B  1 154 ? -20.130 -8.400  -3.457  1.00 12.21  ? 154 SER B CA  1 
ATOM   3339 C  C   . SER B  1 154 ? -19.124 -7.311  -3.650  1.00 10.44  ? 154 SER B C   1 
ATOM   3340 O  O   . SER B  1 154 ? -19.500 -6.135  -3.911  1.00 11.04  ? 154 SER B O   1 
ATOM   3341 C  CB  . SER B  1 154 ? -20.273 -8.751  -1.957  1.00 13.62  ? 154 SER B CB  1 
ATOM   3342 O  OG  . SER B  1 154 ? -21.274 -9.770  -1.818  1.00 20.83  ? 154 SER B OG  1 
ATOM   3343 N  N   . TYR B  1 155 ? -17.831 -7.608  -3.585  1.00 9.77   ? 155 TYR B N   1 
ATOM   3344 C  CA  . TYR B  1 155 ? -16.832 -6.591  -3.904  1.00 9.67   ? 155 TYR B CA  1 
ATOM   3345 C  C   . TYR B  1 155 ? -16.965 -6.136  -5.330  1.00 9.65   ? 155 TYR B C   1 
ATOM   3346 O  O   . TYR B  1 155 ? -16.644 -4.961  -5.654  1.00 10.48  ? 155 TYR B O   1 
ATOM   3347 C  CB  . TYR B  1 155 ? -15.410 -7.062  -3.589  1.00 9.66   ? 155 TYR B CB  1 
ATOM   3348 C  CG  . TYR B  1 155 ? -15.059 -6.978  -2.111  1.00 9.51   ? 155 TYR B CG  1 
ATOM   3349 C  CD1 . TYR B  1 155 ? -15.443 -7.946  -1.223  1.00 9.81   ? 155 TYR B CD1 1 
ATOM   3350 C  CD2 . TYR B  1 155 ? -14.334 -5.846  -1.633  1.00 9.97   ? 155 TYR B CD2 1 
ATOM   3351 C  CE1 . TYR B  1 155 ? -15.144 -7.812  0.145   1.00 10.27  ? 155 TYR B CE1 1 
ATOM   3352 C  CE2 . TYR B  1 155 ? -14.016 -5.729  -0.303  1.00 10.29  ? 155 TYR B CE2 1 
ATOM   3353 C  CZ  . TYR B  1 155 ? -14.460 -6.723  0.597   1.00 10.01  ? 155 TYR B CZ  1 
ATOM   3354 O  OH  . TYR B  1 155 ? -14.142 -6.552  1.919   1.00 10.48  ? 155 TYR B OH  1 
ATOM   3355 N  N   . ASP B  1 156 ? -17.381 -7.001  -6.242  1.00 10.02  ? 156 ASP B N   1 
ATOM   3356 C  CA  . ASP B  1 156 ? -17.532 -6.570  -7.606  1.00 10.60  ? 156 ASP B CA  1 
ATOM   3357 C  C   . ASP B  1 156 ? -18.620 -5.528  -7.764  1.00 10.81  ? 156 ASP B C   1 
ATOM   3358 O  O   . ASP B  1 156 ? -18.600 -4.832  -8.816  1.00 12.12  ? 156 ASP B O   1 
ATOM   3359 C  CB  . ASP B  1 156 ? -17.741 -7.749  -8.603  1.00 14.12  ? 156 ASP B CB  1 
ATOM   3360 C  CG  . ASP B  1 156 ? -16.761 -7.597  -9.794  1.00 13.45  ? 156 ASP B CG  1 
ATOM   3361 O  OD1 . ASP B  1 156 ? -15.521 -7.375  -9.588  1.00 13.08  ? 156 ASP B OD1 1 
ATOM   3362 O  OD2 . ASP B  1 156 ? -17.312 -7.664  -10.932 1.00 17.75  ? 156 ASP B OD2 1 
ATOM   3363 N  N   . LYS B  1 157 ? -19.556 -5.384  -6.834  1.00 11.24  ? 157 LYS B N   1 
ATOM   3364 C  CA  . LYS B  1 157 ? -20.550 -4.327  -6.928  1.00 13.45  ? 157 LYS B CA  1 
ATOM   3365 C  C   . LYS B  1 157 ? -19.824 -2.957  -6.881  1.00 12.20  ? 157 LYS B C   1 
ATOM   3366 O  O   . LYS B  1 157 ? -20.330 -1.995  -7.464  1.00 15.87  ? 157 LYS B O   1 
ATOM   3367 C  CB  . LYS B  1 157 ? -21.571 -4.473  -5.840  1.00 13.64  ? 157 LYS B CB  1 
ATOM   3368 C  CG  . LYS B  1 157 ? -22.464 -5.745  -6.080  1.00 18.45  ? 157 LYS B CG  1 
ATOM   3369 C  CD  . LYS B  1 157 ? -23.521 -6.035  -5.090  1.00 23.47  ? 157 LYS B CD  1 
ATOM   3370 C  CE  . LYS B  1 157 ? -24.211 -7.324  -5.515  1.00 27.35  ? 157 LYS B CE  1 
ATOM   3371 N  NZ  . LYS B  1 157 ? -25.139 -7.729  -4.409  1.00 36.84  ? 157 LYS B NZ  1 
ATOM   3372 N  N   . ILE B  1 158 ? -18.647 -2.863  -6.280  1.00 10.82  ? 158 ILE B N   1 
ATOM   3373 C  CA  . ILE B  1 158 ? -17.806 -1.645  -6.296  1.00 11.82  ? 158 ILE B CA  1 
ATOM   3374 C  C   . ILE B  1 158 ? -16.939 -1.723  -7.506  1.00 11.61  ? 158 ILE B C   1 
ATOM   3375 O  O   . ILE B  1 158 ? -16.889 -0.753  -8.314  1.00 12.99  ? 158 ILE B O   1 
ATOM   3376 C  CB  . ILE B  1 158 ? -16.985 -1.540  -5.036  1.00 12.80  ? 158 ILE B CB  1 
ATOM   3377 C  CG1 . ILE B  1 158 ? -17.910 -1.360  -3.811  1.00 15.40  ? 158 ILE B CG1 1 
ATOM   3378 C  CG2 . ILE B  1 158 ? -16.025 -0.347  -5.169  1.00 14.09  ? 158 ILE B CG2 1 
ATOM   3379 C  CD1 . ILE B  1 158 ? -17.249 -1.543  -2.500  1.00 19.76  ? 158 ILE B CD1 1 
ATOM   3380 N  N   . PHE B  1 159 ? -16.193 -2.820  -7.708  1.00 11.52  ? 159 PHE B N   1 
ATOM   3381 C  CA  . PHE B  1 159 ? -15.173 -2.847  -8.729  1.00 12.98  ? 159 PHE B CA  1 
ATOM   3382 C  C   . PHE B  1 159 ? -15.703 -2.647  -10.117 1.00 13.91  ? 159 PHE B C   1 
ATOM   3383 O  O   . PHE B  1 159 ? -14.946 -2.170  -11.003 1.00 16.32  ? 159 PHE B O   1 
ATOM   3384 C  CB  . PHE B  1 159 ? -14.301 -4.090  -8.644  1.00 12.93  ? 159 PHE B CB  1 
ATOM   3385 C  CG  . PHE B  1 159 ? -13.629 -4.321  -7.332  1.00 12.26  ? 159 PHE B CG  1 
ATOM   3386 C  CD1 . PHE B  1 159 ? -13.262 -3.317  -6.474  1.00 13.34  ? 159 PHE B CD1 1 
ATOM   3387 C  CD2 . PHE B  1 159 ? -13.360 -5.663  -6.959  1.00 14.38  ? 159 PHE B CD2 1 
ATOM   3388 C  CE1 . PHE B  1 159 ? -12.625 -3.585  -5.262  1.00 14.33  ? 159 PHE B CE1 1 
ATOM   3389 C  CE2 . PHE B  1 159 ? -12.703 -5.932  -5.779  1.00 14.85  ? 159 PHE B CE2 1 
ATOM   3390 C  CZ  . PHE B  1 159 ? -12.308 -4.888  -4.949  1.00 13.82  ? 159 PHE B CZ  1 
ATOM   3391 N  N   . SER B  1 160 ? -16.883 -3.106  -10.377 1.00 14.04  ? 160 SER B N   1 
ATOM   3392 C  CA  . SER B  1 160 ? -17.444 -2.975  -11.725 1.00 15.30  ? 160 SER B CA  1 
ATOM   3393 C  C   . SER B  1 160 ? -17.708 -1.558  -12.122 1.00 16.68  ? 160 SER B C   1 
ATOM   3394 O  O   . SER B  1 160 ? -17.871 -1.279  -13.331 1.00 19.28  ? 160 SER B O   1 
ATOM   3395 C  CB  . SER B  1 160 ? -18.715 -3.837  -11.782 1.00 18.55  ? 160 SER B CB  1 
ATOM   3396 O  OG  . SER B  1 160 ? -19.687 -3.235  -10.988 1.00 18.22  ? 160 SER B OG  1 
ATOM   3397 N  N   . HIS B  1 161 ? -17.544 -0.550  -11.257 1.00 15.38  ? 161 HIS B N   1 
ATOM   3398 C  CA  . HIS B  1 161 ? -17.658 0.843   -11.595 1.00 16.56  ? 161 HIS B CA  1 
ATOM   3399 C  C   . HIS B  1 161 ? -16.366 1.622   -11.720 1.00 17.72  ? 161 HIS B C   1 
ATOM   3400 O  O   . HIS B  1 161 ? -16.375 2.866   -12.002 1.00 21.54  ? 161 HIS B O   1 
ATOM   3401 C  CB  . HIS B  1 161 ? -18.506 1.560   -10.586 1.00 17.40  ? 161 HIS B CB  1 
ATOM   3402 C  CG  . HIS B  1 161 ? -19.837 1.090   -10.547 1.00 17.55  ? 161 HIS B CG  1 
ATOM   3403 N  ND1 . HIS B  1 161 ? -20.815 1.662   -11.348 1.00 20.98  ? 161 HIS B ND1 1 
ATOM   3404 C  CD2 . HIS B  1 161 ? -20.444 0.096   -9.913  1.00 18.07  ? 161 HIS B CD2 1 
ATOM   3405 C  CE1 . HIS B  1 161 ? -21.949 0.983   -11.243 1.00 20.64  ? 161 HIS B CE1 1 
ATOM   3406 N  NE2 . HIS B  1 161 ? -21.757 0.058   -10.311 1.00 19.81  ? 161 HIS B NE2 1 
ATOM   3407 N  N   . LEU B  1 162 ? -15.253 0.955   -11.496 1.00 18.95  ? 162 LEU B N   1 
ATOM   3408 C  CA  . LEU B  1 162 ? -13.904 1.665   -11.446 1.00 20.52  ? 162 LEU B CA  1 
ATOM   3409 C  C   . LEU B  1 162 ? -13.510 2.336   -12.738 1.00 22.26  ? 162 LEU B C   1 
ATOM   3410 O  O   . LEU B  1 162 ? -12.914 3.397   -12.624 1.00 25.53  ? 162 LEU B O   1 
ATOM   3411 C  CB  . LEU B  1 162 ? -12.834 0.711   -11.089 1.00 21.64  ? 162 LEU B CB  1 
ATOM   3412 C  CG  . LEU B  1 162 ? -13.005 0.115   -9.732  1.00 24.88  ? 162 LEU B CG  1 
ATOM   3413 C  CD1 . LEU B  1 162 ? -11.938 -0.890  -9.651  1.00 28.18  ? 162 LEU B CD1 1 
ATOM   3414 C  CD2 . LEU B  1 162 ? -12.919 1.155   -8.619  1.00 27.17  ? 162 LEU B CD2 1 
ATOM   3415 N  N   . GLN B  1 163 ? -13.781 1.804   -13.930 1.00 22.69  ? 163 GLN B N   1 
ATOM   3416 C  CA  . GLN B  1 163 ? -13.431 2.410   -15.178 1.00 23.62  ? 163 GLN B CA  1 
ATOM   3417 C  C   . GLN B  1 163 ? -14.090 3.733   -15.360 1.00 22.38  ? 163 GLN B C   1 
ATOM   3418 O  O   . GLN B  1 163 ? -13.863 4.482   -16.359 1.00 30.14  ? 163 GLN B O   1 
ATOM   3419 C  CB  . GLN B  1 163 ? -13.639 1.406   -16.422 1.00 25.29  ? 163 GLN B CB  1 
ATOM   3420 C  CG  . GLN B  1 163 ? -12.663 0.170   -16.365 1.00 30.57  ? 163 GLN B CG  1 
ATOM   3421 C  CD  . GLN B  1 163 ? -11.174 0.562   -16.415 1.00 30.89  ? 163 GLN B CD  1 
ATOM   3422 O  OE1 . GLN B  1 163 ? -10.791 1.640   -16.927 1.00 32.38  ? 163 GLN B OE1 1 
ATOM   3423 N  NE2 . GLN B  1 163 ? -10.315 -0.330  -15.914 1.00 28.94  ? 163 GLN B NE2 1 
ATOM   3424 N  N   . HIS B  1 164 ? -14.972 4.111   -14.483 1.00 22.61  ? 164 HIS B N   1 
ATOM   3425 C  CA  . HIS B  1 164 ? -15.810 5.232   -14.383 1.00 19.96  ? 164 HIS B CA  1 
ATOM   3426 C  C   . HIS B  1 164 ? -15.434 6.399   -13.389 1.00 18.92  ? 164 HIS B C   1 
ATOM   3427 O  O   . HIS B  1 164 ? -16.015 7.574   -13.294 1.00 20.91  ? 164 HIS B O   1 
ATOM   3428 C  CB  . HIS B  1 164 ? -17.235 4.913   -14.522 1.00 26.29  ? 164 HIS B CB  1 
ATOM   3429 C  CG  . HIS B  1 164 ? -17.441 3.778   -15.520 1.00 28.07  ? 164 HIS B CG  1 
ATOM   3430 N  ND1 . HIS B  1 164 ? -17.084 3.890   -16.872 1.00 29.89  ? 164 HIS B ND1 1 
ATOM   3431 C  CD2 . HIS B  1 164 ? -17.879 2.477   -15.361 1.00 28.12  ? 164 HIS B CD2 1 
ATOM   3432 C  CE1 . HIS B  1 164 ? -17.349 2.743   -17.495 1.00 33.05  ? 164 HIS B CE1 1 
ATOM   3433 N  NE2 . HIS B  1 164 ? -17.854 1.877   -16.614 1.00 31.83  ? 164 HIS B NE2 1 
ATOM   3434 N  N   . VAL B  1 165 ? -14.485 6.057   -12.592 1.00 15.38  ? 165 VAL B N   1 
ATOM   3435 C  CA  . VAL B  1 165 ? -13.931 6.968   -11.638 1.00 14.86  ? 165 VAL B CA  1 
ATOM   3436 C  C   . VAL B  1 165 ? -12.424 6.911   -11.753 1.00 12.93  ? 165 VAL B C   1 
ATOM   3437 O  O   . VAL B  1 165 ? -11.693 6.986   -10.786 1.00 13.67  ? 165 VAL B O   1 
ATOM   3438 C  CB  . VAL B  1 165 ? -14.368 6.712   -10.175 1.00 15.72  ? 165 VAL B CB  1 
ATOM   3439 C  CG1 . VAL B  1 165 ? -15.857 7.097   -10.006 1.00 17.96  ? 165 VAL B CG1 1 
ATOM   3440 C  CG2 . VAL B  1 165 ? -14.148 5.302   -9.759  1.00 16.42  ? 165 VAL B CG2 1 
ATOM   3441 N  N   A LYS B  1 166 ? -11.824 6.737   -12.979 0.50 13.35  ? 166 LYS B N   1 
ATOM   3442 N  N   B LYS B  1 166 ? -12.121 6.896   -13.023 0.50 14.70  ? 166 LYS B N   1 
ATOM   3443 C  CA  A LYS B  1 166 ? -10.335 6.565   -13.161 0.50 14.69  ? 166 LYS B CA  1 
ATOM   3444 C  CA  B LYS B  1 166 ? -10.839 6.615   -13.333 0.50 11.56  ? 166 LYS B CA  1 
ATOM   3445 C  C   A LYS B  1 166 ? -9.521  7.796   -12.676 0.50 12.97  ? 166 LYS B C   1 
ATOM   3446 C  C   B LYS B  1 166 ? -9.837  7.720   -12.852 0.50 12.11  ? 166 LYS B C   1 
ATOM   3447 O  O   A LYS B  1 166 ? -8.330  7.564   -12.205 0.50 12.27  ? 166 LYS B O   1 
ATOM   3448 O  O   B LYS B  1 166 ? -8.793  7.375   -12.490 0.50 10.88  ? 166 LYS B O   1 
ATOM   3449 C  CB  A LYS B  1 166 ? -9.959  6.351   -14.623 0.50 13.54  ? 166 LYS B CB  1 
ATOM   3450 C  CB  B LYS B  1 166 ? -10.746 6.500   -14.824 0.50 12.65  ? 166 LYS B CB  1 
ATOM   3451 C  CG  A LYS B  1 166 ? -10.674 5.173   -15.317 0.50 12.97  ? 166 LYS B CG  1 
ATOM   3452 C  CG  B LYS B  1 166 ? -9.342  6.210   -15.239 0.50 16.19  ? 166 LYS B CG  1 
ATOM   3453 C  CD  A LYS B  1 166 ? -10.225 5.060   -16.778 0.50 16.04  ? 166 LYS B CD  1 
ATOM   3454 C  CD  B LYS B  1 166 ? -9.280  5.852   -16.732 0.50 18.85  ? 166 LYS B CD  1 
ATOM   3455 C  CE  A LYS B  1 166 ? -8.681  4.723   -16.898 0.50 15.34  ? 166 LYS B CE  1 
ATOM   3456 C  CE  B LYS B  1 166 ? -9.596  4.387   -17.042 0.50 22.31  ? 166 LYS B CE  1 
ATOM   3457 N  NZ  A LYS B  1 166 ? -8.327  3.338   -16.315 0.50 17.48  ? 166 LYS B NZ  1 
ATOM   3458 N  NZ  B LYS B  1 166 ? -8.850  3.266   -16.347 0.50 18.59  ? 166 LYS B NZ  1 
ATOM   3459 N  N   . TYR B  1 167 ? -10.166 9.012   -12.820 1.00 13.57  ? 167 TYR B N   1 
ATOM   3460 C  CA  . TYR B  1 167 ? -9.344  10.116  -12.410 1.00 13.10  ? 167 TYR B CA  1 
ATOM   3461 C  C   . TYR B  1 167 ? -9.809  10.855  -11.211 1.00 12.04  ? 167 TYR B C   1 
ATOM   3462 O  O   . TYR B  1 167 ? -11.034 10.844  -10.898 1.00 12.73  ? 167 TYR B O   1 
ATOM   3463 C  CB  . TYR B  1 167 ? -9.288  11.103  -13.681 1.00 15.14  ? 167 TYR B CB  1 
ATOM   3464 C  CG  . TYR B  1 167 ? -8.982  10.341  -15.005 1.00 18.57  ? 167 TYR B CG  1 
ATOM   3465 C  CD1 . TYR B  1 167 ? -7.685  9.949   -15.303 1.00 24.41  ? 167 TYR B CD1 1 
ATOM   3466 C  CD2 . TYR B  1 167 ? -9.986  10.021  -15.955 1.00 21.93  ? 167 TYR B CD2 1 
ATOM   3467 C  CE1 . TYR B  1 167 ? -7.388  9.260   -16.474 1.00 19.22  ? 167 TYR B CE1 1 
ATOM   3468 C  CE2 . TYR B  1 167 ? -9.704  9.318   -17.119 1.00 20.25  ? 167 TYR B CE2 1 
ATOM   3469 C  CZ  . TYR B  1 167 ? -8.405  8.953   -17.382 1.00 20.25  ? 167 TYR B CZ  1 
ATOM   3470 O  OH  . TYR B  1 167 ? -8.153  8.274   -18.536 1.00 24.00  ? 167 TYR B OH  1 
ATOM   3471 N  N   . LYS B  1 168 ? -8.851  11.587  -10.622 1.00 13.43  ? 168 LYS B N   1 
ATOM   3472 C  CA  . LYS B  1 168 ? -9.156  12.368  -9.451  1.00 13.42  ? 168 LYS B CA  1 
ATOM   3473 C  C   . LYS B  1 168 ? -10.323 13.245  -9.647  1.00 13.65  ? 168 LYS B C   1 
ATOM   3474 O  O   . LYS B  1 168 ? -10.382 13.982  -10.697 1.00 16.44  ? 168 LYS B O   1 
ATOM   3475 C  CB  . LYS B  1 168 ? -7.914  13.245  -9.067  1.00 16.06  ? 168 LYS B CB  1 
ATOM   3476 C  CG  . LYS B  1 168 ? -8.166  13.985  -7.810  1.00 16.95  ? 168 LYS B CG  1 
ATOM   3477 C  CD  . LYS B  1 168 ? -6.859  14.636  -7.346  1.00 20.51  ? 168 LYS B CD  1 
ATOM   3478 C  CE  . LYS B  1 168 ? -7.154  15.282  -5.944  1.00 27.79  ? 168 LYS B CE  1 
ATOM   3479 N  NZ  . LYS B  1 168 ? -5.875  15.904  -5.403  1.00 37.43  ? 168 LYS B NZ  1 
ATOM   3480 N  N   . GLY B  1 169 ? -11.308 13.243  -8.767  1.00 13.83  ? 169 GLY B N   1 
ATOM   3481 C  CA  . GLY B  1 169 ? -12.425 14.102  -8.803  1.00 17.69  ? 169 GLY B CA  1 
ATOM   3482 C  C   . GLY B  1 169 ? -13.639 13.531  -9.531  1.00 16.54  ? 169 GLY B C   1 
ATOM   3483 O  O   . GLY B  1 169 ? -14.739 14.042  -9.407  1.00 21.86  ? 169 GLY B O   1 
ATOM   3484 N  N   . GLN B  1 170 ? -13.467 12.432  -10.261 1.00 14.86  ? 170 GLN B N   1 
ATOM   3485 C  CA  . GLN B  1 170 ? -14.621 11.861  -10.965 1.00 15.72  ? 170 GLN B CA  1 
ATOM   3486 C  C   . GLN B  1 170 ? -15.512 11.131  -9.924  1.00 14.40  ? 170 GLN B C   1 
ATOM   3487 O  O   . GLN B  1 170 ? -15.001 10.545  -8.926  1.00 15.45  ? 170 GLN B O   1 
ATOM   3488 C  CB  . GLN B  1 170 ? -14.150 10.946  -12.044 1.00 15.55  ? 170 GLN B CB  1 
ATOM   3489 C  CG  . GLN B  1 170 ? -13.479 11.794  -13.182 1.00 17.29  ? 170 GLN B CG  1 
ATOM   3490 C  CD  . GLN B  1 170 ? -13.063 10.905  -14.324 1.00 20.48  ? 170 GLN B CD  1 
ATOM   3491 O  OE1 . GLN B  1 170 ? -12.650 9.719   -14.209 1.00 18.88  ? 170 GLN B OE1 1 
ATOM   3492 N  NE2 . GLN B  1 170 ? -12.993 11.594  -15.467 1.00 25.38  ? 170 GLN B NE2 1 
ATOM   3493 N  N   . GLU B  1 171 ? -16.791 11.079  -10.261 1.00 15.93  ? 171 GLU B N   1 
ATOM   3494 C  CA  . GLU B  1 171 ? -17.865 10.514  -9.446  1.00 17.29  ? 171 GLU B CA  1 
ATOM   3495 C  C   . GLU B  1 171 ? -18.723 9.531   -10.289 1.00 18.38  ? 171 GLU B C   1 
ATOM   3496 O  O   . GLU B  1 171 ? -18.954 9.768   -11.530 1.00 21.35  ? 171 GLU B O   1 
ATOM   3497 C  CB  . GLU B  1 171 ? -18.719 11.653  -8.866  1.00 22.49  ? 171 GLU B CB  1 
ATOM   3498 C  CG  . GLU B  1 171 ? -17.961 12.530  -7.880  1.00 23.63  ? 171 GLU B CG  1 
ATOM   3499 C  CD  . GLU B  1 171 ? -18.790 13.741  -7.394  1.00 30.19  ? 171 GLU B CD  1 
ATOM   3500 O  OE1 . GLU B  1 171 ? -19.963 13.936  -7.862  1.00 42.08  ? 171 GLU B OE1 1 
ATOM   3501 O  OE2 . GLU B  1 171 ? -18.257 14.386  -6.456  1.00 36.61  ? 171 GLU B OE2 1 
ATOM   3502 N  N   . ALA B  1 172 ? -19.283 8.529   -9.656  1.00 16.38  ? 172 ALA B N   1 
ATOM   3503 C  CA  . ALA B  1 172 ? -20.173 7.576   -10.326 1.00 17.09  ? 172 ALA B CA  1 
ATOM   3504 C  C   . ALA B  1 172 ? -21.209 7.161   -9.248  1.00 16.17  ? 172 ALA B C   1 
ATOM   3505 O  O   . ALA B  1 172 ? -20.930 7.258   -8.079  1.00 17.63  ? 172 ALA B O   1 
ATOM   3506 C  CB  . ALA B  1 172 ? -19.404 6.346   -10.853 1.00 21.16  ? 172 ALA B CB  1 
ATOM   3507 N  N   . PHE B  1 173 ? -22.317 6.602   -9.632  1.00 15.72  ? 173 PHE B N   1 
ATOM   3508 C  CA  . PHE B  1 173 ? -23.347 6.117   -8.749  1.00 14.37  ? 173 PHE B CA  1 
ATOM   3509 C  C   . PHE B  1 173 ? -23.268 4.585   -8.751  1.00 15.95  ? 173 PHE B C   1 
ATOM   3510 O  O   . PHE B  1 173 ? -23.274 3.944   -9.819  1.00 22.37  ? 173 PHE B O   1 
ATOM   3511 C  CB  . PHE B  1 173 ? -24.704 6.630   -9.131  1.00 18.01  ? 173 PHE B CB  1 
ATOM   3512 C  CG  . PHE B  1 173 ? -24.939 7.998   -8.611  1.00 19.40  ? 173 PHE B CG  1 
ATOM   3513 C  CD1 . PHE B  1 173 ? -24.982 8.244   -7.200  1.00 22.89  ? 173 PHE B CD1 1 
ATOM   3514 C  CD2 . PHE B  1 173 ? -25.106 9.047   -9.486  1.00 27.01  ? 173 PHE B CD2 1 
ATOM   3515 C  CE1 . PHE B  1 173 ? -25.179 9.484   -6.695  1.00 26.44  ? 173 PHE B CE1 1 
ATOM   3516 C  CE2 . PHE B  1 173 ? -25.339 10.342  -8.988  1.00 30.46  ? 173 PHE B CE2 1 
ATOM   3517 C  CZ  . PHE B  1 173 ? -25.397 10.582  -7.605  1.00 30.02  ? 173 PHE B CZ  1 
ATOM   3518 N  N   . VAL B  1 174 ? -23.372 4.024   -7.563  1.00 14.09  ? 174 VAL B N   1 
ATOM   3519 C  CA  . VAL B  1 174 ? -23.324 2.574   -7.339  1.00 14.41  ? 174 VAL B CA  1 
ATOM   3520 C  C   . VAL B  1 174 ? -24.737 2.241   -6.710  1.00 13.59  ? 174 VAL B C   1 
ATOM   3521 O  O   . VAL B  1 174 ? -25.093 2.793   -5.693  1.00 14.36  ? 174 VAL B O   1 
ATOM   3522 C  CB  . VAL B  1 174 ? -22.204 2.189   -6.338  1.00 13.46  ? 174 VAL B CB  1 
ATOM   3523 C  CG1 . VAL B  1 174 ? -22.280 0.627   -6.052  1.00 14.97  ? 174 VAL B CG1 1 
ATOM   3524 C  CG2 . VAL B  1 174 ? -20.851 2.538   -6.999  1.00 16.15  ? 174 VAL B CG2 1 
ATOM   3525 N  N   . PRO B  1 175 ? -25.501 1.331   -7.341  1.00 11.97  ? 175 PRO B N   1 
ATOM   3526 C  CA  . PRO B  1 175 ? -26.753 0.916   -6.674  1.00 12.08  ? 175 PRO B CA  1 
ATOM   3527 C  C   . PRO B  1 175 ? -26.407 0.346   -5.285  1.00 11.77  ? 175 PRO B C   1 
ATOM   3528 O  O   . PRO B  1 175 ? -25.398 -0.355  -5.107  1.00 13.66  ? 175 PRO B O   1 
ATOM   3529 C  CB  . PRO B  1 175 ? -27.275 -0.163  -7.587  1.00 14.76  ? 175 PRO B CB  1 
ATOM   3530 C  CG  . PRO B  1 175 ? -26.687 0.137   -8.967  1.00 15.54  ? 175 PRO B CG  1 
ATOM   3531 C  CD  . PRO B  1 175 ? -25.287 0.712   -8.643  1.00 13.37  ? 175 PRO B CD  1 
ATOM   3532 N  N   . GLY B  1 176 ? -27.348 0.474   -4.355  1.00 12.62  ? 176 GLY B N   1 
ATOM   3533 C  CA  . GLY B  1 176 ? -27.129 -0.102  -3.049  1.00 12.44  ? 176 GLY B CA  1 
ATOM   3534 C  C   . GLY B  1 176 ? -26.991 -1.577  -3.093  1.00 12.50  ? 176 GLY B C   1 
ATOM   3535 O  O   . GLY B  1 176 ? -27.627 -2.289  -3.907  1.00 13.62  ? 176 GLY B O   1 
ATOM   3536 N  N   . PHE B  1 177 ? -26.251 -2.115  -2.085  1.00 11.61  ? 177 PHE B N   1 
ATOM   3537 C  CA  . PHE B  1 177 ? -26.157 -3.526  -1.911  1.00 12.87  ? 177 PHE B CA  1 
ATOM   3538 C  C   . PHE B  1 177 ? -25.870 -3.732  -0.421  1.00 12.98  ? 177 PHE B C   1 
ATOM   3539 O  O   . PHE B  1 177 ? -25.706 -2.743  0.323   1.00 12.90  ? 177 PHE B O   1 
ATOM   3540 C  CB  . PHE B  1 177 ? -25.054 -4.153  -2.807  1.00 14.06  ? 177 PHE B CB  1 
ATOM   3541 C  CG  . PHE B  1 177 ? -23.693 -3.700  -2.533  1.00 12.78  ? 177 PHE B CG  1 
ATOM   3542 C  CD1 . PHE B  1 177 ? -23.193 -2.466  -3.017  1.00 13.70  ? 177 PHE B CD1 1 
ATOM   3543 C  CD2 . PHE B  1 177 ? -22.805 -4.481  -1.706  1.00 13.98  ? 177 PHE B CD2 1 
ATOM   3544 C  CE1 . PHE B  1 177 ? -21.854 -2.030  -2.763  1.00 14.98  ? 177 PHE B CE1 1 
ATOM   3545 C  CE2 . PHE B  1 177 ? -21.517 -4.045  -1.467  1.00 14.55  ? 177 PHE B CE2 1 
ATOM   3546 C  CZ  . PHE B  1 177 ? -21.048 -2.899  -1.999  1.00 14.80  ? 177 PHE B CZ  1 
ATOM   3547 N  N   . ASN B  1 178 ? -25.827 -4.996  -0.001  1.00 13.94  ? 178 ASN B N   1 
ATOM   3548 C  CA  . ASN B  1 178 ? -25.604 -5.250  1.435   1.00 13.53  ? 178 ASN B CA  1 
ATOM   3549 C  C   . ASN B  1 178 ? -24.150 -5.170  1.799   1.00 11.11  ? 178 ASN B C   1 
ATOM   3550 O  O   . ASN B  1 178 ? -23.389 -6.093  1.474   1.00 12.94  ? 178 ASN B O   1 
ATOM   3551 C  CB  . ASN B  1 178 ? -26.194 -6.673  1.752   1.00 15.76  ? 178 ASN B CB  1 
ATOM   3552 C  CG  . ASN B  1 178 ? -26.167 -6.940  3.223   1.00 14.35  ? 178 ASN B CG  1 
ATOM   3553 O  OD1 . ASN B  1 178 ? -25.743 -6.123  4.058   1.00 14.66  ? 178 ASN B OD1 1 
ATOM   3554 N  ND2 . ASN B  1 178 ? -26.525 -8.186  3.566   1.00 17.65  ? 178 ASN B ND2 1 
ATOM   3555 N  N   . ILE B  1 179 ? -23.784 -4.097  2.407   1.00 10.88  ? 179 ILE B N   1 
ATOM   3556 C  CA  . ILE B  1 179 ? -22.395 -3.890  2.827   1.00 10.67  ? 179 ILE B CA  1 
ATOM   3557 C  C   . ILE B  1 179 ? -21.894 -4.954  3.734   1.00 10.44  ? 179 ILE B C   1 
ATOM   3558 O  O   . ILE B  1 179 ? -20.676 -5.207  3.814   1.00 11.15  ? 179 ILE B O   1 
ATOM   3559 C  CB  . ILE B  1 179 ? -22.248 -2.458  3.418   1.00 10.79  ? 179 ILE B CB  1 
ATOM   3560 C  CG1 . ILE B  1 179 ? -22.758 -1.364  2.495   1.00 11.85  ? 179 ILE B CG1 1 
ATOM   3561 C  CG2 . ILE B  1 179 ? -20.799 -2.203  3.842   1.00 12.00  ? 179 ILE B CG2 1 
ATOM   3562 C  CD1 . ILE B  1 179 ? -22.131 -1.325  1.075   1.00 13.76  ? 179 ILE B CD1 1 
ATOM   3563 N  N   . GLU B  1 180 ? -22.785 -5.603  4.521   1.00 11.16  ? 180 GLU B N   1 
ATOM   3564 C  CA  . GLU B  1 180 ? -22.313 -6.675  5.383   1.00 12.20  ? 180 GLU B CA  1 
ATOM   3565 C  C   . GLU B  1 180 ? -21.734 -7.791  4.578   1.00 11.89  ? 180 GLU B C   1 
ATOM   3566 O  O   . GLU B  1 180 ? -20.913 -8.589  5.143   1.00 12.96  ? 180 GLU B O   1 
ATOM   3567 C  CB  . GLU B  1 180 ? -23.504 -7.176  6.245   1.00 14.19  ? 180 GLU B CB  1 
ATOM   3568 C  CG  . GLU B  1 180 ? -22.990 -7.895  7.515   1.00 20.53  ? 180 GLU B CG  1 
ATOM   3569 C  CD  . GLU B  1 180 ? -24.086 -8.159  8.468   1.00 19.31  ? 180 GLU B CD  1 
ATOM   3570 O  OE1 . GLU B  1 180 ? -25.232 -7.736  8.305   1.00 22.55  ? 180 GLU B OE1 1 
ATOM   3571 O  OE2 . GLU B  1 180 ? -23.761 -8.807  9.458   1.00 25.41  ? 180 GLU B OE2 1 
ATOM   3572 N  N   . GLU B  1 181 ? -22.027 -7.934  3.281   1.00 11.46  ? 181 GLU B N   1 
ATOM   3573 C  CA  . GLU B  1 181 ? -21.482 -8.980  2.420   1.00 12.54  ? 181 GLU B CA  1 
ATOM   3574 C  C   . GLU B  1 181 ? -19.972 -8.717  2.204   1.00 11.50  ? 181 GLU B C   1 
ATOM   3575 O  O   . GLU B  1 181 ? -19.287 -9.594  1.683   1.00 13.04  ? 181 GLU B O   1 
ATOM   3576 C  CB  . GLU B  1 181 ? -22.169 -9.057  1.133   1.00 15.45  ? 181 GLU B CB  1 
ATOM   3577 C  CG  . GLU B  1 181 ? -23.628 -9.431  1.099   1.00 20.57  ? 181 GLU B CG  1 
ATOM   3578 C  CD  . GLU B  1 181 ? -24.267 -9.098  -0.271  1.00 26.42  ? 181 GLU B CD  1 
ATOM   3579 O  OE1 . GLU B  1 181 ? -23.563 -8.699  -1.246  1.00 35.08  ? 181 GLU B OE1 1 
ATOM   3580 O  OE2 . GLU B  1 181 ? -25.490 -9.249  -0.401  1.00 29.07  ? 181 GLU B OE2 1 
ATOM   3581 N  N   . LEU B  1 182 ? -19.464 -7.496  2.538   1.00 10.19  ? 182 LEU B N   1 
ATOM   3582 C  CA  . LEU B  1 182 ? -18.015 -7.234  2.391   1.00 9.77   ? 182 LEU B CA  1 
ATOM   3583 C  C   . LEU B  1 182 ? -17.264 -7.704  3.587   1.00 9.51   ? 182 LEU B C   1 
ATOM   3584 O  O   . LEU B  1 182 ? -16.011 -7.693  3.593   1.00 10.43  ? 182 LEU B O   1 
ATOM   3585 C  CB  . LEU B  1 182 ? -17.797 -5.710  2.194   1.00 10.08  ? 182 LEU B CB  1 
ATOM   3586 C  CG  . LEU B  1 182 ? -18.516 -5.069  1.011   1.00 9.60   ? 182 LEU B CG  1 
ATOM   3587 C  CD1 . LEU B  1 182 ? -18.230 -3.566  0.980   1.00 10.44  ? 182 LEU B CD1 1 
ATOM   3588 C  CD2 . LEU B  1 182 ? -18.139 -5.759  -0.313  1.00 11.26  ? 182 LEU B CD2 1 
ATOM   3589 N  N   . LEU B  1 183 ? -17.956 -8.075  4.684   1.00 10.81  ? 183 LEU B N   1 
ATOM   3590 C  CA  . LEU B  1 183 ? -17.296 -8.466  5.928   1.00 10.52  ? 183 LEU B CA  1 
ATOM   3591 C  C   . LEU B  1 183 ? -17.035 -9.963  5.903   1.00 10.63  ? 183 LEU B C   1 
ATOM   3592 O  O   . LEU B  1 183 ? -17.718 -10.711 5.198   1.00 12.29  ? 183 LEU B O   1 
ATOM   3593 C  CB  . LEU B  1 183 ? -18.217 -8.150  7.115   1.00 11.62  ? 183 LEU B CB  1 
ATOM   3594 C  CG  . LEU B  1 183 ? -18.655 -6.700  7.246   1.00 13.09  ? 183 LEU B CG  1 
ATOM   3595 C  CD1 . LEU B  1 183 ? -19.442 -6.486  8.561   1.00 16.80  ? 183 LEU B CD1 1 
ATOM   3596 C  CD2 . LEU B  1 183 ? -17.469 -5.757  7.231   1.00 15.87  ? 183 LEU B CD2 1 
ATOM   3597 N  N   . PRO B  1 184 ? -16.046 -10.414 6.679   1.00 10.54  ? 184 PRO B N   1 
ATOM   3598 C  CA  . PRO B  1 184 ? -15.729 -11.862 6.699   1.00 12.17  ? 184 PRO B CA  1 
ATOM   3599 C  C   . PRO B  1 184 ? -16.593 -12.559 7.606   1.00 16.62  ? 184 PRO B C   1 
ATOM   3600 O  O   . PRO B  1 184 ? -17.633 -12.053 8.187   1.00 18.36  ? 184 PRO B O   1 
ATOM   3601 C  CB  . PRO B  1 184 ? -14.314 -11.820 7.340   1.00 16.07  ? 184 PRO B CB  1 
ATOM   3602 C  CG  . PRO B  1 184 ? -14.389 -10.649 8.285   1.00 14.40  ? 184 PRO B CG  1 
ATOM   3603 C  CD  . PRO B  1 184 ? -15.161 -9.628  7.539   1.00 10.83  ? 184 PRO B CD  1 
ATOM   3604 N  N   . GLU B  1 185 ? -16.157 -13.884 7.653   1.00 16.58  ? 185 GLU B N   1 
ATOM   3605 C  CA  . GLU B  1 185 ? -16.769 -14.835 8.626   1.00 16.54  ? 185 GLU B CA  1 
ATOM   3606 C  C   . GLU B  1 185 ? -16.278 -14.502 10.056  1.00 15.52  ? 185 GLU B C   1 
ATOM   3607 O  O   . GLU B  1 185 ? -15.237 -13.926 10.335  1.00 18.81  ? 185 GLU B O   1 
ATOM   3608 C  CB  . GLU B  1 185 ? -16.240 -16.209 8.245   1.00 22.56  ? 185 GLU B CB  1 
ATOM   3609 C  CG  . GLU B  1 185 ? -16.740 -16.698 6.832   1.00 30.30  ? 185 GLU B CG  1 
ATOM   3610 C  CD  . GLU B  1 185 ? -18.270 -16.995 6.627   1.00 51.42  ? 185 GLU B CD  1 
ATOM   3611 O  OE1 . GLU B  1 185 ? -19.158 -16.202 7.030   1.00 41.11  ? 185 GLU B OE1 1 
ATOM   3612 O  OE2 . GLU B  1 185 ? -18.553 -18.090 6.025   1.00 80.74  ? 185 GLU B OE2 1 
ATOM   3613 N  N   . ARG B  1 186 ? -17.227 -14.900 10.980  1.00 16.15  ? 186 ARG B N   1 
ATOM   3614 C  CA  . ARG B  1 186 ? -16.958 -14.696 12.427  1.00 17.32  ? 186 ARG B CA  1 
ATOM   3615 C  C   . ARG B  1 186 ? -16.579 -13.332 12.804  1.00 16.32  ? 186 ARG B C   1 
ATOM   3616 O  O   . ARG B  1 186 ? -15.490 -13.037 13.345  1.00 16.42  ? 186 ARG B O   1 
ATOM   3617 C  CB  . ARG B  1 186 ? -15.980 -15.811 12.910  1.00 19.57  ? 186 ARG B CB  1 
ATOM   3618 C  CG  . ARG B  1 186 ? -16.515 -17.238 12.643  1.00 31.14  ? 186 ARG B CG  1 
ATOM   3619 C  CD  . ARG B  1 186 ? -15.602 -18.342 13.195  1.00 34.75  ? 186 ARG B CD  1 
ATOM   3620 N  NE  . ARG B  1 186 ? -14.342 -18.392 12.453  1.00 31.76  ? 186 ARG B NE  1 
ATOM   3621 C  CZ  . ARG B  1 186 ? -14.278 -18.618 11.144  1.00 45.62  ? 186 ARG B CZ  1 
ATOM   3622 N  NH1 . ARG B  1 186 ? -15.400 -18.839 10.481  1.00 59.16  ? 186 ARG B NH1 1 
ATOM   3623 N  NH2 . ARG B  1 186 ? -13.117 -18.630 10.494  1.00 56.73  ? 186 ARG B NH2 1 
ATOM   3624 N  N   . THR B  1 187 ? -17.424 -12.388 12.394  1.00 12.59  ? 187 THR B N   1 
ATOM   3625 C  CA  . THR B  1 187 ? -17.089 -11.049 12.773  1.00 11.38  ? 187 THR B CA  1 
ATOM   3626 C  C   . THR B  1 187 ? -16.900 -10.840 14.296  1.00 12.61  ? 187 THR B C   1 
ATOM   3627 O  O   . THR B  1 187 ? -16.396 -9.832  14.685  1.00 12.70  ? 187 THR B O   1 
ATOM   3628 C  CB  . THR B  1 187 ? -18.047 -10.035 12.223  1.00 11.90  ? 187 THR B CB  1 
ATOM   3629 O  OG1 . THR B  1 187 ? -19.384 -10.413 12.598  1.00 15.07  ? 187 THR B OG1 1 
ATOM   3630 C  CG2 . THR B  1 187 ? -17.956 -9.918  10.700  1.00 14.64  ? 187 THR B CG2 1 
ATOM   3631 N  N   . ALA B  1 188 ? -17.407 -11.791 15.125  1.00 13.91  ? 188 ALA B N   1 
ATOM   3632 C  CA  . ALA B  1 188 ? -17.164 -11.690 16.543  1.00 13.10  ? 188 ALA B CA  1 
ATOM   3633 C  C   . ALA B  1 188 ? -15.720 -11.721 16.917  1.00 10.98  ? 188 ALA B C   1 
ATOM   3634 O  O   . ALA B  1 188 ? -15.402 -11.241 17.995  1.00 12.42  ? 188 ALA B O   1 
ATOM   3635 C  CB  . ALA B  1 188 ? -17.904 -12.842 17.244  1.00 17.50  ? 188 ALA B CB  1 
ATOM   3636 N  N   . GLU B  1 189 ? -14.838 -12.239 16.050  1.00 11.44  ? 189 GLU B N   1 
ATOM   3637 C  CA  . GLU B  1 189 ? -13.398 -12.311 16.325  1.00 10.72  ? 189 GLU B CA  1 
ATOM   3638 C  C   . GLU B  1 189 ? -12.692 -11.156 15.672  1.00 9.76   ? 189 GLU B C   1 
ATOM   3639 O  O   . GLU B  1 189 ? -12.673 -11.024 14.422  1.00 10.51  ? 189 GLU B O   1 
ATOM   3640 C  CB  . GLU B  1 189 ? -12.859 -13.603 15.749  1.00 13.18  ? 189 GLU B CB  1 
ATOM   3641 C  CG  . GLU B  1 189 ? -13.573 -14.839 16.489  1.00 17.25  ? 189 GLU B CG  1 
ATOM   3642 C  CD  . GLU B  1 189 ? -13.116 -16.180 16.109  1.00 27.48  ? 189 GLU B CD  1 
ATOM   3643 O  OE1 . GLU B  1 189 ? -11.963 -16.363 15.773  1.00 25.02  ? 189 GLU B OE1 1 
ATOM   3644 O  OE2 . GLU B  1 189 ? -13.968 -17.115 16.262  1.00 39.16  ? 189 GLU B OE2 1 
ATOM   3645 N  N   . TYR B  1 190 ? -12.123 -10.295 16.479  1.00 9.38   ? 190 TYR B N   1 
ATOM   3646 C  CA  . TYR B  1 190 ? -11.466 -9.066  15.982  1.00 9.04   ? 190 TYR B CA  1 
ATOM   3647 C  C   . TYR B  1 190 ? -10.394 -8.609  16.947  1.00 9.33   ? 190 TYR B C   1 
ATOM   3648 O  O   . TYR B  1 190 ? -10.337 -8.987  18.112  1.00 9.97   ? 190 TYR B O   1 
ATOM   3649 C  CB  . TYR B  1 190 ? -12.524 -7.945  15.720  1.00 9.54   ? 190 TYR B CB  1 
ATOM   3650 C  CG  . TYR B  1 190 ? -13.337 -7.554  16.960  1.00 9.59   ? 190 TYR B CG  1 
ATOM   3651 C  CD1 . TYR B  1 190 ? -12.834 -6.657  17.903  1.00 9.68   ? 190 TYR B CD1 1 
ATOM   3652 C  CD2 . TYR B  1 190 ? -14.641 -8.062  17.137  1.00 10.58  ? 190 TYR B CD2 1 
ATOM   3653 C  CE1 . TYR B  1 190 ? -13.624 -6.292  18.971  1.00 10.50  ? 190 TYR B CE1 1 
ATOM   3654 C  CE2 . TYR B  1 190 ? -15.412 -7.708  18.256  1.00 10.58  ? 190 TYR B CE2 1 
ATOM   3655 C  CZ  . TYR B  1 190 ? -14.929 -6.820  19.160  1.00 11.12  ? 190 TYR B CZ  1 
ATOM   3656 O  OH  . TYR B  1 190 ? -15.652 -6.399  20.252  1.00 12.45  ? 190 TYR B OH  1 
ATOM   3657 N  N   . TYR B  1 191 ? -9.528  -7.749  16.370  1.00 9.44   ? 191 TYR B N   1 
ATOM   3658 C  CA  . TYR B  1 191 ? -8.545  -6.993  17.062  1.00 9.15   ? 191 TYR B CA  1 
ATOM   3659 C  C   . TYR B  1 191 ? -9.048  -5.567  17.279  1.00 9.23   ? 191 TYR B C   1 
ATOM   3660 O  O   . TYR B  1 191 ? -9.695  -4.998  16.387  1.00 10.55  ? 191 TYR B O   1 
ATOM   3661 C  CB  . TYR B  1 191 ? -7.267  -6.841  16.176  1.00 10.10  ? 191 TYR B CB  1 
ATOM   3662 C  CG  . TYR B  1 191 ? -6.640  -8.132  15.660  1.00 9.82   ? 191 TYR B CG  1 
ATOM   3663 C  CD1 . TYR B  1 191 ? -5.630  -8.812  16.387  1.00 10.99  ? 191 TYR B CD1 1 
ATOM   3664 C  CD2 . TYR B  1 191 ? -7.021  -8.661  14.446  1.00 10.00  ? 191 TYR B CD2 1 
ATOM   3665 C  CE1 . TYR B  1 191 ? -5.018  -9.932  15.856  1.00 11.48  ? 191 TYR B CE1 1 
ATOM   3666 C  CE2 . TYR B  1 191 ? -6.411  -9.754  13.871  1.00 11.50  ? 191 TYR B CE2 1 
ATOM   3667 C  CZ  . TYR B  1 191 ? -5.401  -10.401 14.647  1.00 11.64  ? 191 TYR B CZ  1 
ATOM   3668 O  OH  . TYR B  1 191 ? -4.762  -11.523 14.078  1.00 15.48  ? 191 TYR B OH  1 
ATOM   3669 N  N   . ARG B  1 192 ? -8.790  -4.976  18.441  1.00 9.51   ? 192 ARG B N   1 
ATOM   3670 C  CA  . ARG B  1 192 ? -9.200  -3.644  18.805  1.00 9.52   ? 192 ARG B CA  1 
ATOM   3671 C  C   . ARG B  1 192 ? -8.053  -2.841  19.306  1.00 10.25  ? 192 ARG B C   1 
ATOM   3672 O  O   . ARG B  1 192 ? -7.360  -3.298  20.231  1.00 11.25  ? 192 ARG B O   1 
ATOM   3673 C  CB  . ARG B  1 192 ? -10.319 -3.734  19.894  1.00 11.31  ? 192 ARG B CB  1 
ATOM   3674 C  CG  . ARG B  1 192 ? -10.693 -2.480  20.576  1.00 12.25  ? 192 ARG B CG  1 
ATOM   3675 C  CD  . ARG B  1 192 ? -11.299 -1.423  19.704  1.00 13.76  ? 192 ARG B CD  1 
ATOM   3676 N  NE  . ARG B  1 192 ? -12.442 -1.929  18.911  1.00 13.05  ? 192 ARG B NE  1 
ATOM   3677 C  CZ  . ARG B  1 192 ? -13.625 -2.270  19.402  1.00 12.66  ? 192 ARG B CZ  1 
ATOM   3678 N  NH1 . ARG B  1 192 ? -13.877 -2.089  20.718  1.00 13.99  ? 192 ARG B NH1 1 
ATOM   3679 N  NH2 . ARG B  1 192 ? -14.539 -2.809  18.625  1.00 13.94  ? 192 ARG B NH2 1 
ATOM   3680 N  N   . TYR B  1 193 ? -7.846  -1.616  18.823  1.00 10.12  ? 193 TYR B N   1 
ATOM   3681 C  CA  . TYR B  1 193 ? -6.802  -0.757  19.407  1.00 11.43  ? 193 TYR B CA  1 
ATOM   3682 C  C   . TYR B  1 193 ? -7.119  0.664   19.074  1.00 10.99  ? 193 TYR B C   1 
ATOM   3683 O  O   . TYR B  1 193 ? -7.927  0.976   18.171  1.00 10.83  ? 193 TYR B O   1 
ATOM   3684 C  CB  . TYR B  1 193 ? -5.379  -1.196  18.933  1.00 12.04  ? 193 TYR B CB  1 
ATOM   3685 C  CG  . TYR B  1 193 ? -5.040  -0.776  17.522  1.00 10.63  ? 193 TYR B CG  1 
ATOM   3686 C  CD1 . TYR B  1 193 ? -5.464  -1.519  16.427  1.00 10.53  ? 193 TYR B CD1 1 
ATOM   3687 C  CD2 . TYR B  1 193 ? -4.275  0.394   17.311  1.00 11.16  ? 193 TYR B CD2 1 
ATOM   3688 C  CE1 . TYR B  1 193 ? -5.114  -1.113  15.109  1.00 10.03  ? 193 TYR B CE1 1 
ATOM   3689 C  CE2 . TYR B  1 193 ? -3.960  0.768   16.023  1.00 9.79   ? 193 TYR B CE2 1 
ATOM   3690 C  CZ  . TYR B  1 193 ? -4.398  0.074   14.945  1.00 9.46   ? 193 TYR B CZ  1 
ATOM   3691 O  OH  . TYR B  1 193 ? -4.052  0.488   13.697  1.00 10.21  ? 193 TYR B OH  1 
ATOM   3692 N  N   . ARG B  1 194 ? -6.493  1.554   19.822  1.00 13.14  ? 194 ARG B N   1 
ATOM   3693 C  CA  . ARG B  1 194 ? -6.579  3.022   19.583  1.00 12.42  ? 194 ARG B CA  1 
ATOM   3694 C  C   . ARG B  1 194 ? -5.490  3.488   18.657  1.00 11.57  ? 194 ARG B C   1 
ATOM   3695 O  O   . ARG B  1 194 ? -4.286  3.235   18.858  1.00 14.24  ? 194 ARG B O   1 
ATOM   3696 C  CB  . ARG B  1 194 ? -6.317  3.730   20.931  1.00 19.64  ? 194 ARG B CB  1 
ATOM   3697 C  CG  . ARG B  1 194 ? -7.528  3.488   21.841  1.00 27.42  ? 194 ARG B CG  1 
ATOM   3698 C  CD  . ARG B  1 194 ? -8.661  4.502   21.741  1.00 47.23  ? 194 ARG B CD  1 
ATOM   3699 N  N   . GLY B  1 195 ? -5.893  4.139   17.559  1.00 11.48  ? 195 GLY B N   1 
ATOM   3700 C  CA  . GLY B  1 195 ? -4.946  4.576   16.572  1.00 10.88  ? 195 GLY B CA  1 
ATOM   3701 C  C   . GLY B  1 195 ? -5.417  5.832   15.876  1.00 9.64   ? 195 GLY B C   1 
ATOM   3702 O  O   . GLY B  1 195 ? -6.057  6.729   16.479  1.00 11.23  ? 195 GLY B O   1 
ATOM   3703 N  N   . SER B  1 196 ? -5.047  5.917   14.600  1.00 9.95   ? 196 SER B N   1 
ATOM   3704 C  CA  . SER B  1 196 ? -5.160  7.140   13.878  1.00 9.75   ? 196 SER B CA  1 
ATOM   3705 C  C   . SER B  1 196 ? -5.698  6.889   12.478  1.00 9.05   ? 196 SER B C   1 
ATOM   3706 O  O   . SER B  1 196 ? -5.786  5.757   11.992  1.00 9.90   ? 196 SER B O   1 
ATOM   3707 C  CB  . SER B  1 196 ? -3.740  7.827   13.696  1.00 10.83  ? 196 SER B CB  1 
ATOM   3708 O  OG  . SER B  1 196 ? -2.941  7.136   12.744  1.00 10.16  ? 196 SER B OG  1 
ATOM   3709 N  N   . LEU B  1 197 ? -6.023  7.997   11.817  1.00 9.45   ? 197 LEU B N   1 
ATOM   3710 C  CA  . LEU B  1 197 ? -6.120  7.929   10.330  1.00 9.32   ? 197 LEU B CA  1 
ATOM   3711 C  C   . LEU B  1 197 ? -4.813  7.403   9.804   1.00 8.74   ? 197 LEU B C   1 
ATOM   3712 O  O   . LEU B  1 197 ? -3.707  7.849   10.231  1.00 9.87   ? 197 LEU B O   1 
ATOM   3713 C  CB  . LEU B  1 197 ? -6.343  9.326   9.702   1.00 9.44   ? 197 LEU B CB  1 
ATOM   3714 C  CG  . LEU B  1 197 ? -7.765  9.813   9.622   1.00 11.45  ? 197 LEU B CG  1 
ATOM   3715 C  CD1 . LEU B  1 197 ? -8.366  10.104  10.943  1.00 16.73  ? 197 LEU B CD1 1 
ATOM   3716 C  CD2 . LEU B  1 197 ? -7.808  11.118  8.762   1.00 13.81  ? 197 LEU B CD2 1 
ATOM   3717 N  N   . THR B  1 198 ? -4.835  6.561   8.765   1.00 9.28   ? 198 THR B N   1 
ATOM   3718 C  CA  . THR B  1 198 ? -3.630  6.086   8.142   1.00 9.35   ? 198 THR B CA  1 
ATOM   3719 C  C   . THR B  1 198 ? -3.166  7.018   7.018   1.00 9.60   ? 198 THR B C   1 
ATOM   3720 O  O   . THR B  1 198 ? -2.144  6.690   6.355   1.00 9.75   ? 198 THR B O   1 
ATOM   3721 C  CB  . THR B  1 198 ? -3.757  4.679   7.640   1.00 9.26   ? 198 THR B CB  1 
ATOM   3722 O  OG1 . THR B  1 198 ? -4.671  4.721   6.520   1.00 8.87   ? 198 THR B OG1 1 
ATOM   3723 C  CG2 . THR B  1 198 ? -4.204  3.684   8.663   1.00 10.01  ? 198 THR B CG2 1 
ATOM   3724 N  N   . THR B  1 199 ? -3.920  8.084   6.746   1.00 9.72   ? 199 THR B N   1 
ATOM   3725 C  CA  . THR B  1 199 ? -3.558  9.057   5.730   1.00 9.23   ? 199 THR B CA  1 
ATOM   3726 C  C   . THR B  1 199 ? -3.499  10.379  6.416   1.00 10.07  ? 199 THR B C   1 
ATOM   3727 O  O   . THR B  1 199 ? -4.132  10.589  7.444   1.00 10.56  ? 199 THR B O   1 
ATOM   3728 C  CB  . THR B  1 199 ? -4.696  9.166   4.646   1.00 10.03  ? 199 THR B CB  1 
ATOM   3729 O  OG1 . THR B  1 199 ? -5.899  9.633   5.242   1.00 12.11  ? 199 THR B OG1 1 
ATOM   3730 C  CG2 . THR B  1 199 ? -4.984  7.836   4.025   1.00 11.61  ? 199 THR B CG2 1 
ATOM   3731 N  N   . PRO B  1 200 ? -2.780  11.373  5.822   1.00 9.72   ? 200 PRO B N   1 
ATOM   3732 C  CA  . PRO B  1 200 ? -2.931  12.767  6.303   1.00 10.25  ? 200 PRO B CA  1 
ATOM   3733 C  C   . PRO B  1 200 ? -4.390  13.127  6.460   1.00 11.01  ? 200 PRO B C   1 
ATOM   3734 O  O   . PRO B  1 200 ? -5.218  12.703  5.609   1.00 12.38  ? 200 PRO B O   1 
ATOM   3735 C  CB  . PRO B  1 200 ? -2.235  13.546  5.216   1.00 11.42  ? 200 PRO B CB  1 
ATOM   3736 C  CG  . PRO B  1 200 ? -1.146  12.615  4.690   1.00 11.51  ? 200 PRO B CG  1 
ATOM   3737 C  CD  . PRO B  1 200 ? -1.876  11.284  4.680   1.00 10.50  ? 200 PRO B CD  1 
ATOM   3738 N  N   A PRO B  1 201 ? -4.760  13.908  7.502   0.50 11.05  ? 201 PRO B N   1 
ATOM   3739 N  N   B PRO B  1 201 ? -4.766  13.843  7.484   0.50 10.75  ? 201 PRO B N   1 
ATOM   3740 C  CA  A PRO B  1 201 ? -3.926  14.497  8.593   0.50 10.16  ? 201 PRO B CA  1 
ATOM   3741 C  CA  B PRO B  1 201 ? -3.847  14.490  8.375   0.50 10.17  ? 201 PRO B CA  1 
ATOM   3742 C  C   A PRO B  1 201 ? -3.544  13.614  9.733   0.50 10.77  ? 201 PRO B C   1 
ATOM   3743 C  C   B PRO B  1 201 ? -3.400  13.614  9.542   0.50 10.25  ? 201 PRO B C   1 
ATOM   3744 O  O   A PRO B  1 201 ? -2.965  14.107  10.741  0.50 10.36  ? 201 PRO B O   1 
ATOM   3745 O  O   B PRO B  1 201 ? -2.649  14.127  10.410  0.50 10.13  ? 201 PRO B O   1 
ATOM   3746 C  CB  A PRO B  1 201 ? -4.794  15.658  9.165   0.50 13.00  ? 201 PRO B CB  1 
ATOM   3747 C  CB  B PRO B  1 201 ? -4.671  15.687  8.834   0.50 12.34  ? 201 PRO B CB  1 
ATOM   3748 C  CG  A PRO B  1 201 ? -5.828  15.914  8.120   0.50 15.87  ? 201 PRO B CG  1 
ATOM   3749 C  CG  B PRO B  1 201 ? -6.126  15.108  8.849   0.50 11.51  ? 201 PRO B CG  1 
ATOM   3750 C  CD  A PRO B  1 201 ? -6.106  14.556  7.436   0.50 12.01  ? 201 PRO B CD  1 
ATOM   3751 C  CD  B PRO B  1 201 ? -6.197  14.207  7.710   0.50 11.65  ? 201 PRO B CD  1 
ATOM   3752 N  N   . CYS B  1 202 ? -3.756  12.303  9.621   1.00 10.40  ? 202 CYS B N   1 
ATOM   3753 C  CA  . CYS B  1 202 ? -3.205  11.329  10.607  1.00 11.05  ? 202 CYS B CA  1 
ATOM   3754 C  C   . CYS B  1 202 ? -3.703  11.571  12.017  1.00 10.15  ? 202 CYS B C   1 
ATOM   3755 O  O   . CYS B  1 202 ? -3.075  11.188  12.991  1.00 11.27  ? 202 CYS B O   1 
ATOM   3756 C  CB  . CYS B  1 202 ? -1.677  11.306  10.648  1.00 11.65  ? 202 CYS B CB  1 
ATOM   3757 S  SG  . CYS B  1 202 ? -0.883  10.927  9.035   1.00 10.92  ? 202 CYS B SG  1 
ATOM   3758 N  N   A ASN B  1 203 ? -4.925  12.109  12.137  0.50 11.37  ? 203 ASN B N   1 
ATOM   3759 N  N   B ASN B  1 203 ? -4.908  12.148  12.148  0.50 11.75  ? 203 ASN B N   1 
ATOM   3760 C  CA  A ASN B  1 203 ? -5.509  12.402  13.467  0.50 12.21  ? 203 ASN B CA  1 
ATOM   3761 C  CA  B ASN B  1 203 ? -5.374  12.490  13.510  0.50 12.31  ? 203 ASN B CA  1 
ATOM   3762 C  C   A ASN B  1 203 ? -5.554  11.172  14.341  0.50 10.85  ? 203 ASN B C   1 
ATOM   3763 C  C   B ASN B  1 203 ? -5.440  11.212  14.316  0.50 10.42  ? 203 ASN B C   1 
ATOM   3764 O  O   A ASN B  1 203 ? -6.115  10.170  13.937  0.50 10.03  ? 203 ASN B O   1 
ATOM   3765 O  O   B ASN B  1 203 ? -5.870  10.207  13.817  0.50 10.84  ? 203 ASN B O   1 
ATOM   3766 C  CB  A ASN B  1 203 ? -6.919  12.946  13.316  0.50 13.04  ? 203 ASN B CB  1 
ATOM   3767 C  CB  B ASN B  1 203 ? -6.756  13.160  13.551  0.50 13.66  ? 203 ASN B CB  1 
ATOM   3768 C  CG  A ASN B  1 203 ? -6.950  14.109  12.401  0.50 14.35  ? 203 ASN B CG  1 
ATOM   3769 C  CG  B ASN B  1 203 ? -6.881  14.340  12.592  0.50 16.32  ? 203 ASN B CG  1 
ATOM   3770 O  OD1 A ASN B  1 203 ? -6.952  13.936  11.201  0.50 16.04  ? 203 ASN B OD1 1 
ATOM   3771 O  OD1 B ASN B  1 203 ? -5.905  14.891  12.150  0.50 17.85  ? 203 ASN B OD1 1 
ATOM   3772 N  ND2 A ASN B  1 203 ? -6.981  15.302  12.964  0.50 19.53  ? 203 ASN B ND2 1 
ATOM   3773 N  ND2 B ASN B  1 203 ? -8.124  14.688  12.230  0.50 18.53  ? 203 ASN B ND2 1 
ATOM   3774 N  N   . PRO B  1 204 ? -5.094  11.278  15.623  1.00 12.23  ? 204 PRO B N   1 
ATOM   3775 C  CA  . PRO B  1 204 ? -5.057  10.063  16.501  1.00 12.69  ? 204 PRO B CA  1 
ATOM   3776 C  C   . PRO B  1 204 ? -6.444  9.831   17.128  1.00 12.54  ? 204 PRO B C   1 
ATOM   3777 O  O   . PRO B  1 204 ? -6.529  9.846   18.401  1.00 16.03  ? 204 PRO B O   1 
ATOM   3778 C  CB  . PRO B  1 204 ? -3.929  10.391  17.462  1.00 14.55  ? 204 PRO B CB  1 
ATOM   3779 C  CG  . PRO B  1 204 ? -4.046  11.904  17.630  1.00 16.43  ? 204 PRO B CG  1 
ATOM   3780 C  CD  . PRO B  1 204 ? -4.306  12.417  16.170  1.00 15.30  ? 204 PRO B CD  1 
ATOM   3781 N  N   . THR B  1 205 ? -7.473  9.686   16.364  1.00 11.79  ? 205 THR B N   1 
ATOM   3782 C  CA  . THR B  1 205 ? -8.857  9.793   16.841  1.00 13.53  ? 205 THR B CA  1 
ATOM   3783 C  C   . THR B  1 205 ? -9.673  8.597   16.408  1.00 12.20  ? 205 THR B C   1 
ATOM   3784 O  O   . THR B  1 205 ? -10.915 8.672   16.462  1.00 13.20  ? 205 THR B O   1 
ATOM   3785 C  CB  . THR B  1 205 ? -9.497  11.101  16.228  1.00 14.28  ? 205 THR B CB  1 
ATOM   3786 O  OG1 . THR B  1 205 ? -9.305  10.975  14.816  1.00 14.47  ? 205 THR B OG1 1 
ATOM   3787 C  CG2 . THR B  1 205 ? -8.772  12.375  16.804  1.00 15.86  ? 205 THR B CG2 1 
ATOM   3788 N  N   . VAL B  1 206 ? -9.013  7.481   16.093  1.00 10.76  ? 206 VAL B N   1 
ATOM   3789 C  CA  . VAL B  1 206 ? -9.744  6.320   15.568  1.00 10.61  ? 206 VAL B CA  1 
ATOM   3790 C  C   . VAL B  1 206 ? -9.723  5.152   16.539  1.00 10.03  ? 206 VAL B C   1 
ATOM   3791 O  O   . VAL B  1 206 ? -8.642  4.720   16.965  1.00 11.94  ? 206 VAL B O   1 
ATOM   3792 C  CB  . VAL B  1 206 ? -9.119  5.831   14.206  1.00 10.02  ? 206 VAL B CB  1 
ATOM   3793 C  CG1 . VAL B  1 206 ? -9.870  4.597   13.711  1.00 10.95  ? 206 VAL B CG1 1 
ATOM   3794 C  CG2 . VAL B  1 206 ? -9.152  6.971   13.182  1.00 11.34  ? 206 VAL B CG2 1 
ATOM   3795 N  N   . LEU B  1 207 ? -10.888 4.580   16.792  1.00 9.44   ? 207 LEU B N   1 
ATOM   3796 C  CA  . LEU B  1 207 ? -11.000 3.275   17.416  1.00 10.46  ? 207 LEU B CA  1 
ATOM   3797 C  C   . LEU B  1 207 ? -11.010 2.236   16.315  1.00 9.14   ? 207 LEU B C   1 
ATOM   3798 O  O   . LEU B  1 207 ? -11.957 2.186   15.496  1.00 9.98   ? 207 LEU B O   1 
ATOM   3799 C  CB  . LEU B  1 207 ? -12.326 3.195   18.175  1.00 12.10  ? 207 LEU B CB  1 
ATOM   3800 C  CG  . LEU B  1 207 ? -12.454 2.084   19.185  1.00 18.65  ? 207 LEU B CG  1 
ATOM   3801 C  CD1 . LEU B  1 207 ? -11.386 2.195   20.297  1.00 25.58  ? 207 LEU B CD1 1 
ATOM   3802 C  CD2 . LEU B  1 207 ? -13.723 2.164   19.915  1.00 29.45  ? 207 LEU B CD2 1 
ATOM   3803 N  N   . TRP B  1 208 ? -9.937  1.479   16.188  1.00 9.37   ? 208 TRP B N   1 
ATOM   3804 C  CA  . TRP B  1 208 ? -9.792  0.444   15.121  1.00 9.12   ? 208 TRP B CA  1 
ATOM   3805 C  C   . TRP B  1 208 ? -10.415 -0.872  15.560  1.00 8.86   ? 208 TRP B C   1 
ATOM   3806 O  O   . TRP B  1 208 ? -10.163 -1.348  16.676  1.00 10.09  ? 208 TRP B O   1 
ATOM   3807 C  CB  . TRP B  1 208 ? -8.307  0.257   14.794  1.00 9.57   ? 208 TRP B CB  1 
ATOM   3808 C  CG  . TRP B  1 208 ? -7.811  1.354   13.905  1.00 8.89   ? 208 TRP B CG  1 
ATOM   3809 C  CD1 . TRP B  1 208 ? -7.154  2.505   14.244  1.00 9.38   ? 208 TRP B CD1 1 
ATOM   3810 C  CD2 . TRP B  1 208 ? -7.941  1.386   12.490  1.00 8.67   ? 208 TRP B CD2 1 
ATOM   3811 N  NE1 . TRP B  1 208 ? -6.903  3.272   13.146  1.00 9.38   ? 208 TRP B NE1 1 
ATOM   3812 C  CE2 . TRP B  1 208 ? -7.385  2.634   12.037  1.00 8.42   ? 208 TRP B CE2 1 
ATOM   3813 C  CE3 . TRP B  1 208 ? -8.490  0.533   11.519  1.00 8.86   ? 208 TRP B CE3 1 
ATOM   3814 C  CZ2 . TRP B  1 208 ? -7.412  3.032   10.713  1.00 9.43   ? 208 TRP B CZ2 1 
ATOM   3815 C  CZ3 . TRP B  1 208 ? -8.458  0.909   10.185  1.00 9.75   ? 208 TRP B CZ3 1 
ATOM   3816 C  CH2 . TRP B  1 208 ? -7.929  2.117   9.796   1.00 9.35   ? 208 TRP B CH2 1 
ATOM   3817 N  N   . THR B  1 209 ? -11.097 -1.504  14.607  1.00 8.68   ? 209 THR B N   1 
ATOM   3818 C  CA  . THR B  1 209 ? -11.530 -2.904  14.731  1.00 8.72   ? 209 THR B CA  1 
ATOM   3819 C  C   . THR B  1 209 ? -11.039 -3.576  13.475  1.00 8.49   ? 209 THR B C   1 
ATOM   3820 O  O   . THR B  1 209 ? -11.490 -3.222  12.390  1.00 9.99   ? 209 THR B O   1 
ATOM   3821 C  CB  . THR B  1 209 ? -13.054 -2.984  14.875  1.00 9.31   ? 209 THR B CB  1 
ATOM   3822 O  OG1 . THR B  1 209 ? -13.469 -2.263  16.034  1.00 10.30  ? 209 THR B OG1 1 
ATOM   3823 C  CG2 . THR B  1 209 ? -13.534 -4.457  14.938  1.00 10.45  ? 209 THR B CG2 1 
ATOM   3824 N  N   . VAL B  1 210 ? -10.123 -4.544  13.589  1.00 8.65   ? 210 VAL B N   1 
ATOM   3825 C  CA  . VAL B  1 210 ? -9.624  -5.270  12.448  1.00 8.89   ? 210 VAL B CA  1 
ATOM   3826 C  C   . VAL B  1 210 ? -10.171 -6.689  12.564  1.00 8.66   ? 210 VAL B C   1 
ATOM   3827 O  O   . VAL B  1 210 ? -9.882  -7.357  13.592  1.00 9.36   ? 210 VAL B O   1 
ATOM   3828 C  CB  . VAL B  1 210 ? -8.082  -5.277  12.365  1.00 9.19   ? 210 VAL B CB  1 
ATOM   3829 C  CG1 . VAL B  1 210 ? -7.612  -6.052  11.133  1.00 9.78   ? 210 VAL B CG1 1 
ATOM   3830 C  CG2 . VAL B  1 210 ? -7.509  -3.880  12.424  1.00 10.01  ? 210 VAL B CG2 1 
ATOM   3831 N  N   . PHE B  1 211 ? -10.976 -7.157  11.649  1.00 8.86   ? 211 PHE B N   1 
ATOM   3832 C  CA  . PHE B  1 211 ? -11.516 -8.519  11.781  1.00 8.89   ? 211 PHE B CA  1 
ATOM   3833 C  C   . PHE B  1 211 ? -10.424 -9.535  11.662  1.00 9.14   ? 211 PHE B C   1 
ATOM   3834 O  O   . PHE B  1 211 ? -9.469  -9.409  10.894  1.00 9.66   ? 211 PHE B O   1 
ATOM   3835 C  CB  . PHE B  1 211 ? -12.629 -8.788  10.757  1.00 9.40   ? 211 PHE B CB  1 
ATOM   3836 C  CG  . PHE B  1 211 ? -13.818 -7.926  11.086  1.00 8.87   ? 211 PHE B CG  1 
ATOM   3837 C  CD1 . PHE B  1 211 ? -14.615 -8.116  12.234  1.00 10.24  ? 211 PHE B CD1 1 
ATOM   3838 C  CD2 . PHE B  1 211 ? -14.156 -6.854  10.258  1.00 10.12  ? 211 PHE B CD2 1 
ATOM   3839 C  CE1 . PHE B  1 211 ? -15.696 -7.338  12.524  1.00 10.99  ? 211 PHE B CE1 1 
ATOM   3840 C  CE2 . PHE B  1 211 ? -15.241 -6.024  10.525  1.00 11.43  ? 211 PHE B CE2 1 
ATOM   3841 C  CZ  . PHE B  1 211 ? -16.021 -6.292  11.661  1.00 12.75  ? 211 PHE B CZ  1 
ATOM   3842 N  N   . ARG B  1 212 ? -10.521 -10.621 12.458  1.00 9.86   ? 212 ARG B N   1 
ATOM   3843 C  CA  . ARG B  1 212 ? -9.489  -11.693 12.441  1.00 9.76   ? 212 ARG B CA  1 
ATOM   3844 C  C   . ARG B  1 212 ? -9.429  -12.342 11.098  1.00 10.09  ? 212 ARG B C   1 
ATOM   3845 O  O   . ARG B  1 212 ? -8.318  -12.715 10.682  1.00 12.10  ? 212 ARG B O   1 
ATOM   3846 C  CB  . ARG B  1 212 ? -9.801  -12.674 13.523  1.00 10.92  ? 212 ARG B CB  1 
ATOM   3847 C  CG  . ARG B  1 212 ? -8.678  -13.715 13.686  1.00 11.99  ? 212 ARG B CG  1 
ATOM   3848 C  CD  . ARG B  1 212 ? -9.151  -14.805 14.686  1.00 13.51  ? 212 ARG B CD  1 
ATOM   3849 N  NE  . ARG B  1 212 ? -8.003  -15.694 14.918  1.00 15.06  ? 212 ARG B NE  1 
ATOM   3850 C  CZ  . ARG B  1 212 ? -8.009  -16.615 15.855  1.00 17.88  ? 212 ARG B CZ  1 
ATOM   3851 N  NH1 . ARG B  1 212 ? -9.151  -16.969 16.419  1.00 18.87  ? 212 ARG B NH1 1 
ATOM   3852 N  NH2 . ARG B  1 212 ? -6.893  -17.284 16.180  1.00 20.37  ? 212 ARG B NH2 1 
ATOM   3853 N  N   . ASN B  1 213 ? -10.572 -12.646 10.487  1.00 9.66   ? 213 ASN B N   1 
ATOM   3854 C  CA  . ASN B  1 213 ? -10.565 -13.480 9.309   1.00 11.01  ? 213 ASN B CA  1 
ATOM   3855 C  C   . ASN B  1 213 ? -10.604 -12.603 8.068   1.00 10.06  ? 213 ASN B C   1 
ATOM   3856 O  O   . ASN B  1 213 ? -11.363 -11.612 7.995   1.00 10.87  ? 213 ASN B O   1 
ATOM   3857 C  CB  . ASN B  1 213 ? -11.856 -14.301 9.325   1.00 14.40  ? 213 ASN B CB  1 
ATOM   3858 C  CG  . ASN B  1 213 ? -11.785 -15.284 10.488  1.00 17.64  ? 213 ASN B CG  1 
ATOM   3859 O  OD1 . ASN B  1 213 ? -10.784 -15.938 10.676  1.00 25.08  ? 213 ASN B OD1 1 
ATOM   3860 N  ND2 . ASN B  1 213 ? -12.742 -15.300 11.289  1.00 25.10  ? 213 ASN B ND2 1 
ATOM   3861 N  N   . PRO B  1 214 ? -9.826  -12.923 7.062   1.00 10.49  ? 214 PRO B N   1 
ATOM   3862 C  CA  . PRO B  1 214 ? -9.874  -12.178 5.776   1.00 10.39  ? 214 PRO B CA  1 
ATOM   3863 C  C   . PRO B  1 214 ? -11.049 -12.611 4.923   1.00 9.25   ? 214 PRO B C   1 
ATOM   3864 O  O   . PRO B  1 214 ? -11.648 -13.655 5.116   1.00 11.48  ? 214 PRO B O   1 
ATOM   3865 C  CB  . PRO B  1 214 ? -8.558  -12.569 5.111   1.00 12.05  ? 214 PRO B CB  1 
ATOM   3866 C  CG  . PRO B  1 214 ? -8.345  -13.980 5.533   1.00 15.08  ? 214 PRO B CG  1 
ATOM   3867 C  CD  . PRO B  1 214 ? -8.784  -13.999 7.051   1.00 14.21  ? 214 PRO B CD  1 
ATOM   3868 N  N   . VAL B  1 215 ? -11.311 -11.814 3.897   1.00 9.42   ? 215 VAL B N   1 
ATOM   3869 C  CA  . VAL B  1 215 ? -12.161 -12.200 2.773   1.00 9.14   ? 215 VAL B CA  1 
ATOM   3870 C  C   . VAL B  1 215 ? -11.296 -12.441 1.584   1.00 8.75   ? 215 VAL B C   1 
ATOM   3871 O  O   . VAL B  1 215 ? -10.101 -12.112 1.580   1.00 10.46  ? 215 VAL B O   1 
ATOM   3872 C  CB  . VAL B  1 215 ? -13.205 -11.101 2.476   1.00 9.56   ? 215 VAL B CB  1 
ATOM   3873 C  CG1 . VAL B  1 215 ? -14.142 -10.875 3.638   1.00 13.33  ? 215 VAL B CG1 1 
ATOM   3874 C  CG2 . VAL B  1 215 ? -12.581 -9.824  1.948   1.00 11.20  ? 215 VAL B CG2 1 
ATOM   3875 N  N   . GLN B  1 216 ? -11.861 -13.027 0.546   1.00 8.98   ? 216 GLN B N   1 
ATOM   3876 C  CA  . GLN B  1 216 ? -11.149 -13.262 -0.712  1.00 9.50   ? 216 GLN B CA  1 
ATOM   3877 C  C   . GLN B  1 216 ? -11.746 -12.442 -1.862  1.00 8.93   ? 216 GLN B C   1 
ATOM   3878 O  O   . GLN B  1 216 ? -12.972 -12.321 -1.943  1.00 10.37  ? 216 GLN B O   1 
ATOM   3879 C  CB  . GLN B  1 216 ? -11.224 -14.737 -1.130  1.00 10.71  ? 216 GLN B CB  1 
ATOM   3880 C  CG  . GLN B  1 216 ? -10.449 -15.617 -0.161  1.00 12.45  ? 216 GLN B CG  1 
ATOM   3881 C  CD  . GLN B  1 216 ? -10.457 -17.103 -0.573  1.00 13.11  ? 216 GLN B CD  1 
ATOM   3882 O  OE1 . GLN B  1 216 ? -11.027 -17.525 -1.583  1.00 12.91  ? 216 GLN B OE1 1 
ATOM   3883 N  NE2 . GLN B  1 216 ? -9.745  -17.844 0.180   1.00 19.69  ? 216 GLN B NE2 1 
ATOM   3884 N  N   . ILE B  1 217 ? -10.880 -11.952 -2.746  1.00 8.92   ? 217 ILE B N   1 
ATOM   3885 C  CA  . ILE B  1 217 ? -11.299 -11.486 -4.060  1.00 9.26   ? 217 ILE B CA  1 
ATOM   3886 C  C   . ILE B  1 217 ? -10.320 -12.112 -5.060  1.00 8.99   ? 217 ILE B C   1 
ATOM   3887 O  O   . ILE B  1 217 ? -9.228  -12.541 -4.666  1.00 9.50   ? 217 ILE B O   1 
ATOM   3888 C  CB  . ILE B  1 217 ? -11.278 -9.926  -4.161  1.00 9.75   ? 217 ILE B CB  1 
ATOM   3889 C  CG1 . ILE B  1 217 ? -9.888  -9.365  -4.102  1.00 10.09  ? 217 ILE B CG1 1 
ATOM   3890 C  CG2 . ILE B  1 217 ? -12.217 -9.341  -3.075  1.00 10.46  ? 217 ILE B CG2 1 
ATOM   3891 C  CD1 . ILE B  1 217 ? -9.865  -7.841  -4.285  1.00 12.22  ? 217 ILE B CD1 1 
ATOM   3892 N  N   . SER B  1 218 ? -10.682 -12.158 -6.330  1.00 9.07   ? 218 SER B N   1 
ATOM   3893 C  CA  . SER B  1 218 ? -9.846  -12.917 -7.257  1.00 9.74   ? 218 SER B CA  1 
ATOM   3894 C  C   . SER B  1 218 ? -8.676  -12.115 -7.753  1.00 10.09  ? 218 SER B C   1 
ATOM   3895 O  O   . SER B  1 218 ? -8.647  -10.860 -7.666  1.00 10.50  ? 218 SER B O   1 
ATOM   3896 C  CB  . SER B  1 218 ? -10.638 -13.425 -8.446  1.00 10.83  ? 218 SER B CB  1 
ATOM   3897 O  OG  . SER B  1 218 ? -11.046 -12.292 -9.242  1.00 11.64  ? 218 SER B OG  1 
ATOM   3898 N  N   . GLN B  1 219 ? -7.717  -12.810 -8.344  1.00 10.99  ? 219 GLN B N   1 
ATOM   3899 C  CA  . GLN B  1 219 ? -6.609  -12.158 -9.042  1.00 12.67  ? 219 GLN B CA  1 
ATOM   3900 C  C   . GLN B  1 219 ? -7.102  -11.153 -10.047 1.00 11.94  ? 219 GLN B C   1 
ATOM   3901 O  O   . GLN B  1 219 ? -6.532  -10.065 -10.190 1.00 12.35  ? 219 GLN B O   1 
ATOM   3902 C  CB  . GLN B  1 219 ? -5.748  -13.207 -9.726  1.00 15.91  ? 219 GLN B CB  1 
ATOM   3903 C  CG  . GLN B  1 219 ? -4.424  -12.548 -10.303 1.00 21.16  ? 219 GLN B CG  1 
ATOM   3904 C  CD  . GLN B  1 219 ? -4.425  -11.911 -11.618 1.00 31.19  ? 219 GLN B CD  1 
ATOM   3905 O  OE1 . GLN B  1 219 ? -3.575  -10.983 -11.945 1.00 28.90  ? 219 GLN B OE1 1 
ATOM   3906 N  NE2 . GLN B  1 219 ? -5.397  -12.335 -12.416 1.00 24.43  ? 219 GLN B NE2 1 
ATOM   3907 N  N   . GLU B  1 220 ? -8.159  -11.484 -10.801 1.00 12.10  ? 220 GLU B N   1 
ATOM   3908 C  CA  . GLU B  1 220 ? -8.669  -10.544 -11.838 1.00 13.28  ? 220 GLU B CA  1 
ATOM   3909 C  C   . GLU B  1 220 ? -9.267  -9.353  -11.172 1.00 11.70  ? 220 GLU B C   1 
ATOM   3910 O  O   . GLU B  1 220 ? -9.119  -8.216  -11.703 1.00 12.49  ? 220 GLU B O   1 
ATOM   3911 C  CB  . GLU B  1 220 ? -9.663  -11.276 -12.721 1.00 14.94  ? 220 GLU B CB  1 
ATOM   3912 C  CG  . GLU B  1 220 ? -9.005  -12.420 -13.579 1.00 16.30  ? 220 GLU B CG  1 
ATOM   3913 C  CD  . GLU B  1 220 ? -8.820  -13.711 -12.852 1.00 16.70  ? 220 GLU B CD  1 
ATOM   3914 O  OE1 . GLU B  1 220 ? -9.189  -13.933 -11.710 1.00 17.35  ? 220 GLU B OE1 1 
ATOM   3915 O  OE2 . GLU B  1 220 ? -8.271  -14.645 -13.472 1.00 27.35  ? 220 GLU B OE2 1 
ATOM   3916 N  N   . GLN B  1 221 ? -9.952  -9.510  -10.037 1.00 10.95  ? 221 GLN B N   1 
ATOM   3917 C  CA  . GLN B  1 221 ? -10.518 -8.335  -9.378  1.00 10.26  ? 221 GLN B CA  1 
ATOM   3918 C  C   . GLN B  1 221 ? -9.399  -7.462  -8.816  1.00 10.55  ? 221 GLN B C   1 
ATOM   3919 O  O   . GLN B  1 221 ? -9.468  -6.198  -8.957  1.00 11.37  ? 221 GLN B O   1 
ATOM   3920 C  CB  . GLN B  1 221 ? -11.411 -8.793  -8.202  1.00 10.71  ? 221 GLN B CB  1 
ATOM   3921 C  CG  . GLN B  1 221 ? -12.724 -9.401  -8.685  1.00 11.09  ? 221 GLN B CG  1 
ATOM   3922 C  CD  . GLN B  1 221 ? -13.585 -9.830  -7.567  1.00 9.21   ? 221 GLN B CD  1 
ATOM   3923 O  OE1 . GLN B  1 221 ? -13.287 -10.777 -6.823  1.00 10.27  ? 221 GLN B OE1 1 
ATOM   3924 N  NE2 . GLN B  1 221 ? -14.737 -9.151  -7.412  1.00 10.96  ? 221 GLN B NE2 1 
ATOM   3925 N  N   . LEU B  1 222 ? -8.371  -8.043  -8.231  1.00 10.02  ? 222 LEU B N   1 
ATOM   3926 C  CA  . LEU B  1 222 ? -7.239  -7.269  -7.808  1.00 10.82  ? 222 LEU B CA  1 
ATOM   3927 C  C   . LEU B  1 222 ? -6.601  -6.541  -8.951  1.00 11.27  ? 222 LEU B C   1 
ATOM   3928 O  O   . LEU B  1 222 ? -6.243  -5.363  -8.835  1.00 11.49  ? 222 LEU B O   1 
ATOM   3929 C  CB  . LEU B  1 222 ? -6.228  -8.168  -7.097  1.00 11.54  ? 222 LEU B CB  1 
ATOM   3930 C  CG  . LEU B  1 222 ? -6.595  -8.536  -5.700  1.00 11.18  ? 222 LEU B CG  1 
ATOM   3931 C  CD1 . LEU B  1 222 ? -5.874  -9.792  -5.194  1.00 13.24  ? 222 LEU B CD1 1 
ATOM   3932 C  CD2 . LEU B  1 222 ? -6.214  -7.356  -4.689  1.00 13.90  ? 222 LEU B CD2 1 
ATOM   3933 N  N   . LEU B  1 223 ? -6.398  -7.201  -10.076 1.00 11.47  ? 223 LEU B N   1 
ATOM   3934 C  CA  . LEU B  1 223 ? -5.762  -6.532  -11.170 1.00 12.55  ? 223 LEU B CA  1 
ATOM   3935 C  C   . LEU B  1 223 ? -6.629  -5.366  -11.695 1.00 12.83  ? 223 LEU B C   1 
ATOM   3936 O  O   . LEU B  1 223 ? -6.075  -4.292  -12.056 1.00 14.20  ? 223 LEU B O   1 
ATOM   3937 C  CB  . LEU B  1 223 ? -5.600  -7.583  -12.397 1.00 14.02  ? 223 LEU B CB  1 
ATOM   3938 C  CG  . LEU B  1 223 ? -4.874  -7.046  -13.616 1.00 16.13  ? 223 LEU B CG  1 
ATOM   3939 C  CD1 . LEU B  1 223 ? -3.469  -6.654  -13.260 1.00 18.25  ? 223 LEU B CD1 1 
ATOM   3940 C  CD2 . LEU B  1 223 ? -4.840  -8.092  -14.710 1.00 20.39  ? 223 LEU B CD2 1 
ATOM   3941 N  N   . ALA B  1 224 ? -7.968  -5.551  -11.744 1.00 13.44  ? 224 ALA B N   1 
ATOM   3942 C  CA  . ALA B  1 224 ? -8.837  -4.425  -12.149 1.00 14.10  ? 224 ALA B CA  1 
ATOM   3943 C  C   . ALA B  1 224 ? -8.656  -3.253  -11.182 1.00 15.13  ? 224 ALA B C   1 
ATOM   3944 O  O   . ALA B  1 224 ? -8.485  -2.104  -11.633 1.00 16.50  ? 224 ALA B O   1 
ATOM   3945 C  CB  . ALA B  1 224 ? -10.256 -4.870  -12.224 1.00 16.74  ? 224 ALA B CB  1 
ATOM   3946 N  N   . LEU B  1 225 ? -8.650  -3.514  -9.880  1.00 13.03  ? 225 LEU B N   1 
ATOM   3947 C  CA  . LEU B  1 225 ? -8.449  -2.472  -8.886  1.00 11.90  ? 225 LEU B CA  1 
ATOM   3948 C  C   . LEU B  1 225 ? -7.129  -1.788  -9.028  1.00 12.38  ? 225 LEU B C   1 
ATOM   3949 O  O   . LEU B  1 225 ? -7.055  -0.539  -8.919  1.00 15.46  ? 225 LEU B O   1 
ATOM   3950 C  CB  . LEU B  1 225 ? -8.634  -3.098  -7.493  1.00 12.24  ? 225 LEU B CB  1 
ATOM   3951 C  CG  . LEU B  1 225 ? -8.463  -2.137  -6.321  1.00 12.87  ? 225 LEU B CG  1 
ATOM   3952 C  CD1 . LEU B  1 225 ? -9.492  -1.032  -6.326  1.00 14.82  ? 225 LEU B CD1 1 
ATOM   3953 C  CD2 . LEU B  1 225 ? -8.484  -2.922  -4.997  1.00 14.15  ? 225 LEU B CD2 1 
ATOM   3954 N  N   . GLU B  1 226 ? -6.094  -2.534  -9.320  1.00 12.04  ? 226 GLU B N   1 
ATOM   3955 C  CA  . GLU B  1 226 ? -4.761  -2.019  -9.385  1.00 12.96  ? 226 GLU B CA  1 
ATOM   3956 C  C   . GLU B  1 226 ? -4.436  -1.353  -10.726 1.00 12.23  ? 226 GLU B C   1 
ATOM   3957 O  O   . GLU B  1 226 ? -3.368  -0.711  -10.769 1.00 16.38  ? 226 GLU B O   1 
ATOM   3958 C  CB  . GLU B  1 226 ? -3.739  -3.247  -9.224  1.00 13.32  ? 226 GLU B CB  1 
ATOM   3959 C  CG  . GLU B  1 226 ? -3.758  -3.870  -7.829  1.00 12.75  ? 226 GLU B CG  1 
ATOM   3960 C  CD  . GLU B  1 226 ? -3.403  -5.301  -7.813  1.00 13.27  ? 226 GLU B CD  1 
ATOM   3961 O  OE1 . GLU B  1 226 ? -3.083  -5.870  -8.937  1.00 13.17  ? 226 GLU B OE1 1 
ATOM   3962 O  OE2 . GLU B  1 226 ? -3.460  -5.987  -6.764  1.00 14.45  ? 226 GLU B OE2 1 
ATOM   3963 N  N   . THR B  1 227 ? -5.281  -1.468  -11.716 1.00 12.56  ? 227 THR B N   1 
ATOM   3964 C  CA  . THR B  1 227 ? -4.963  -0.862  -13.027 1.00 14.31  ? 227 THR B CA  1 
ATOM   3965 C  C   . THR B  1 227 ? -6.048  0.151   -13.406 1.00 15.53  ? 227 THR B C   1 
ATOM   3966 O  O   . THR B  1 227 ? -5.823  0.871   -14.421 1.00 20.04  ? 227 THR B O   1 
ATOM   3967 C  CB  . THR B  1 227 ? -4.954  -1.905  -14.179 1.00 15.46  ? 227 THR B CB  1 
ATOM   3968 O  OG1 . THR B  1 227 ? -6.170  -2.614  -14.253 1.00 15.28  ? 227 THR B OG1 1 
ATOM   3969 C  CG2 . THR B  1 227 ? -3.787  -2.858  -13.974 1.00 16.29  ? 227 THR B CG2 1 
ATOM   3970 N  N   . ALA B  1 228 ? -7.059  0.378   -12.648 1.00 13.59  ? 228 ALA B N   1 
ATOM   3971 C  CA  . ALA B  1 228 ? -8.106  1.227   -13.171 1.00 16.15  ? 228 ALA B CA  1 
ATOM   3972 C  C   . ALA B  1 228 ? -7.835  2.732   -12.890 1.00 16.11  ? 228 ALA B C   1 
ATOM   3973 O  O   . ALA B  1 228 ? -8.326  3.589   -13.605 1.00 18.80  ? 228 ALA B O   1 
ATOM   3974 C  CB  . ALA B  1 228 ? -9.376  0.882   -12.569 1.00 19.77  ? 228 ALA B CB  1 
ATOM   3975 N  N   . LEU B  1 229 ? -7.183  3.034   -11.794 1.00 14.29  ? 229 LEU B N   1 
ATOM   3976 C  CA  . LEU B  1 229 ? -7.293  4.383   -11.213 1.00 12.72  ? 229 LEU B CA  1 
ATOM   3977 C  C   . LEU B  1 229 ? -6.007  5.114   -11.258 1.00 13.35  ? 229 LEU B C   1 
ATOM   3978 O  O   . LEU B  1 229 ? -4.889  4.567   -11.209 1.00 13.41  ? 229 LEU B O   1 
ATOM   3979 C  CB  . LEU B  1 229 ? -7.783  4.280   -9.738  1.00 14.41  ? 229 LEU B CB  1 
ATOM   3980 C  CG  . LEU B  1 229 ? -9.044  3.443   -9.540  1.00 14.49  ? 229 LEU B CG  1 
ATOM   3981 C  CD1 . LEU B  1 229 ? -9.304  3.290   -8.042  1.00 18.18  ? 229 LEU B CD1 1 
ATOM   3982 C  CD2 . LEU B  1 229 ? -10.229 4.007   -10.283 1.00 19.82  ? 229 LEU B CD2 1 
ATOM   3983 N  N   . TYR B  1 230 ? -6.115  6.458   -11.246 1.00 13.92  ? 230 TYR B N   1 
ATOM   3984 C  CA  . TYR B  1 230 ? -5.018  7.441   -11.248 1.00 13.98  ? 230 TYR B CA  1 
ATOM   3985 C  C   . TYR B  1 230 ? -5.204  8.434   -10.123 1.00 13.85  ? 230 TYR B C   1 
ATOM   3986 O  O   . TYR B  1 230 ? -6.375  8.795   -9.817  1.00 14.11  ? 230 TYR B O   1 
ATOM   3987 C  CB  . TYR B  1 230 ? -5.049  8.169   -12.633 1.00 15.22  ? 230 TYR B CB  1 
ATOM   3988 C  CG  . TYR B  1 230 ? -4.597  7.228   -13.727 1.00 14.17  ? 230 TYR B CG  1 
ATOM   3989 C  CD1 . TYR B  1 230 ? -5.482  6.329   -14.273 1.00 16.80  ? 230 TYR B CD1 1 
ATOM   3990 C  CD2 . TYR B  1 230 ? -3.279  7.158   -14.111 1.00 16.73  ? 230 TYR B CD2 1 
ATOM   3991 C  CE1 . TYR B  1 230 ? -5.072  5.393   -15.190 1.00 17.83  ? 230 TYR B CE1 1 
ATOM   3992 C  CE2 . TYR B  1 230 ? -2.851  6.175   -15.075 1.00 19.00  ? 230 TYR B CE2 1 
ATOM   3993 C  CZ  . TYR B  1 230 ? -3.793  5.305   -15.539 1.00 18.80  ? 230 TYR B CZ  1 
ATOM   3994 O  OH  . TYR B  1 230 ? -3.438  4.313   -16.449 1.00 22.93  ? 230 TYR B OH  1 
ATOM   3995 N  N   . CYS B  1 231 ? -4.084  8.845   -9.514  1.00 15.20  ? 231 CYS B N   1 
ATOM   3996 C  CA  . CYS B  1 231 ? -4.214  9.846   -8.510  1.00 14.68  ? 231 CYS B CA  1 
ATOM   3997 C  C   . CYS B  1 231 ? -4.421  11.244  -9.084  1.00 15.07  ? 231 CYS B C   1 
ATOM   3998 O  O   . CYS B  1 231 ? -4.756  12.180  -8.365  1.00 16.28  ? 231 CYS B O   1 
ATOM   3999 C  CB  . CYS B  1 231 ? -2.804  9.972   -7.761  1.00 20.09  ? 231 CYS B CB  1 
ATOM   4000 S  SG  . CYS B  1 231 ? -2.197  8.487   -7.032  1.00 25.08  ? 231 CYS B SG  1 
ATOM   4001 N  N   . THR B  1 232 ? -4.243  11.406  -10.378 1.00 14.97  ? 232 THR B N   1 
ATOM   4002 C  CA  . THR B  1 232 ? -4.207  12.689  -11.048 1.00 13.71  ? 232 THR B CA  1 
ATOM   4003 C  C   . THR B  1 232 ? -5.538  12.932  -11.802 1.00 15.13  ? 232 THR B C   1 
ATOM   4004 O  O   . THR B  1 232 ? -6.309  12.045  -12.076 1.00 15.38  ? 232 THR B O   1 
ATOM   4005 C  CB  . THR B  1 232 ? -3.014  12.660  -12.040 1.00 14.40  ? 232 THR B CB  1 
ATOM   4006 O  OG1 . THR B  1 232 ? -2.945  11.393  -12.726 1.00 13.99  ? 232 THR B OG1 1 
ATOM   4007 C  CG2 . THR B  1 232 ? -1.746  12.919  -11.277 1.00 16.60  ? 232 THR B CG2 1 
ATOM   4008 N  N   . HIS B  1 233 ? -5.780  14.214  -12.118 1.00 15.19  ? 233 HIS B N   1 
ATOM   4009 C  CA  . HIS B  1 233 ? -6.935  14.574  -12.901 1.00 15.62  ? 233 HIS B CA  1 
ATOM   4010 C  C   . HIS B  1 233 ? -6.853  14.045  -14.345 1.00 14.82  ? 233 HIS B C   1 
ATOM   4011 O  O   . HIS B  1 233 ? -5.744  13.858  -14.839 1.00 17.27  ? 233 HIS B O   1 
ATOM   4012 C  CB  . HIS B  1 233 ? -7.046  16.094  -12.896 1.00 20.03  ? 233 HIS B CB  1 
ATOM   4013 C  CG  . HIS B  1 233 ? -7.483  16.604  -11.559 1.00 20.48  ? 233 HIS B CG  1 
ATOM   4014 N  ND1 . HIS B  1 233 ? -6.657  17.336  -10.725 1.00 35.34  ? 233 HIS B ND1 1 
ATOM   4015 C  CD2 . HIS B  1 233 ? -8.660  16.541  -10.909 1.00 24.12  ? 233 HIS B CD2 1 
ATOM   4016 C  CE1 . HIS B  1 233 ? -7.313  17.744  -9.654  1.00 34.53  ? 233 HIS B CE1 1 
ATOM   4017 N  NE2 . HIS B  1 233 ? -8.518  17.227  -9.721  1.00 26.82  ? 233 HIS B NE2 1 
ATOM   4018 N  N   . MET B  1 234 ? -7.993  13.941  -15.030 1.00 16.14  ? 234 MET B N   1 
ATOM   4019 C  CA  . MET B  1 234 ? -8.055  13.408  -16.411 1.00 16.65  ? 234 MET B CA  1 
ATOM   4020 C  C   . MET B  1 234 ? -7.133  14.195  -17.327 1.00 17.46  ? 234 MET B C   1 
ATOM   4021 O  O   . MET B  1 234 ? -6.581  13.596  -18.267 1.00 19.38  ? 234 MET B O   1 
ATOM   4022 C  CB  . MET B  1 234 ? -9.533  13.473  -16.940 1.00 18.38  ? 234 MET B CB  1 
ATOM   4023 C  CG  . MET B  1 234 ? -9.806  12.887  -18.394 1.00 21.79  ? 234 MET B CG  1 
ATOM   4024 S  SD  . MET B  1 234 ? -11.547 12.783  -18.682 1.00 27.82  ? 234 MET B SD  1 
ATOM   4025 C  CE  . MET B  1 234 ? -11.491 12.041  -20.280 1.00 29.10  ? 234 MET B CE  1 
ATOM   4026 N  N   . ASP B  1 235 ? -6.953  15.526  -17.109 1.00 16.62  ? 235 ASP B N   1 
ATOM   4027 C  CA  . ASP B  1 235 ? -6.216  16.283  -18.077 1.00 18.46  ? 235 ASP B CA  1 
ATOM   4028 C  C   . ASP B  1 235 ? -4.794  16.531  -17.624 1.00 17.04  ? 235 ASP B C   1 
ATOM   4029 O  O   . ASP B  1 235 ? -4.058  17.283  -18.257 1.00 21.51  ? 235 ASP B O   1 
ATOM   4030 C  CB  . ASP B  1 235 ? -6.976  17.637  -18.397 1.00 24.99  ? 235 ASP B CB  1 
ATOM   4031 C  CG  . ASP B  1 235 ? -6.974  18.564  -17.213 1.00 30.66  ? 235 ASP B CG  1 
ATOM   4032 O  OD1 . ASP B  1 235 ? -6.541  18.158  -16.080 1.00 36.07  ? 235 ASP B OD1 1 
ATOM   4033 O  OD2 . ASP B  1 235 ? -7.389  19.699  -17.347 1.00 49.06  ? 235 ASP B OD2 1 
ATOM   4034 N  N   . ASP B  1 236 ? -4.303  15.854  -16.606 1.00 16.04  ? 236 ASP B N   1 
ATOM   4035 C  CA  . ASP B  1 236 ? -2.968  16.129  -16.105 1.00 15.11  ? 236 ASP B CA  1 
ATOM   4036 C  C   . ASP B  1 236 ? -1.921  15.606  -17.128 1.00 15.17  ? 236 ASP B C   1 
ATOM   4037 O  O   . ASP B  1 236 ? -1.936  14.442  -17.506 1.00 15.89  ? 236 ASP B O   1 
ATOM   4038 C  CB  . ASP B  1 236 ? -2.791  15.419  -14.760 1.00 17.15  ? 236 ASP B CB  1 
ATOM   4039 C  CG  . ASP B  1 236 ? -1.553  15.949  -13.995 1.00 17.11  ? 236 ASP B CG  1 
ATOM   4040 O  OD1 . ASP B  1 236 ? -0.478  16.116  -14.536 1.00 17.98  ? 236 ASP B OD1 1 
ATOM   4041 O  OD2 . ASP B  1 236 ? -1.658  16.189  -12.743 1.00 21.44  ? 236 ASP B OD2 1 
ATOM   4042 N  N   . PRO B  1 237 ? -0.961  16.447  -17.556 1.00 15.24  ? 237 PRO B N   1 
ATOM   4043 C  CA  . PRO B  1 237 ? 0.101   15.975  -18.457 1.00 15.85  ? 237 PRO B CA  1 
ATOM   4044 C  C   . PRO B  1 237 ? 1.164   15.068  -17.772 1.00 15.53  ? 237 PRO B C   1 
ATOM   4045 O  O   . PRO B  1 237 ? 2.011   14.555  -18.504 1.00 17.29  ? 237 PRO B O   1 
ATOM   4046 C  CB  . PRO B  1 237 ? 0.732   17.280  -18.979 1.00 18.28  ? 237 PRO B CB  1 
ATOM   4047 C  CG  . PRO B  1 237 ? 0.545   18.228  -17.803 1.00 20.25  ? 237 PRO B CG  1 
ATOM   4048 C  CD  . PRO B  1 237 ? -0.914  17.920  -17.318 1.00 17.21  ? 237 PRO B CD  1 
ATOM   4049 N  N   A SER B  1 238 ? 1.100   14.823  -16.464 0.50 14.66  ? 238 SER B N   1 
ATOM   4050 N  N   B SER B  1 238 ? 1.033   14.882  -16.454 0.50 14.73  ? 238 SER B N   1 
ATOM   4051 C  CA  A SER B  1 238 ? 2.050   13.886  -15.819 0.50 15.54  ? 238 SER B CA  1 
ATOM   4052 C  CA  B SER B  1 238 ? 1.912   13.980  -15.692 0.50 15.09  ? 238 SER B CA  1 
ATOM   4053 C  C   A SER B  1 238 ? 1.271   12.882  -14.983 0.50 13.06  ? 238 SER B C   1 
ATOM   4054 C  C   B SER B  1 238 ? 1.042   12.993  -14.927 0.50 13.52  ? 238 SER B C   1 
ATOM   4055 O  O   A SER B  1 238 ? 1.325   12.928  -13.730 0.50 14.45  ? 238 SER B O   1 
ATOM   4056 O  O   B SER B  1 238 ? 0.808   13.165  -13.703 0.50 13.74  ? 238 SER B O   1 
ATOM   4057 C  CB  A SER B  1 238 ? 2.988   14.647  -14.896 0.50 18.36  ? 238 SER B CB  1 
ATOM   4058 C  CB  B SER B  1 238 ? 2.806   14.788  -14.755 0.50 21.27  ? 238 SER B CB  1 
ATOM   4059 O  OG  A SER B  1 238 ? 4.011   13.824  -14.442 0.50 23.01  ? 238 SER B OG  1 
ATOM   4060 O  OG  B SER B  1 238 ? 3.725   15.503  -15.567 0.50 22.53  ? 238 SER B OG  1 
ATOM   4061 N  N   . PRO B  1 239 ? 0.484   12.017  -15.616 1.00 14.04  ? 239 PRO B N   1 
ATOM   4062 C  CA  . PRO B  1 239 ? -0.410  11.085  -14.856 1.00 14.43  ? 239 PRO B CA  1 
ATOM   4063 C  C   . PRO B  1 239 ? 0.317   10.230  -13.877 1.00 14.64  ? 239 PRO B C   1 
ATOM   4064 O  O   . PRO B  1 239 ? 1.490   9.867   -14.096 1.00 16.47  ? 239 PRO B O   1 
ATOM   4065 C  CB  . PRO B  1 239 ? -0.991  10.170  -15.954 1.00 17.12  ? 239 PRO B CB  1 
ATOM   4066 C  CG  . PRO B  1 239 ? -0.567  10.767  -17.217 1.00 19.81  ? 239 PRO B CG  1 
ATOM   4067 C  CD  . PRO B  1 239 ? 0.458   11.816  -17.058 1.00 15.16  ? 239 PRO B CD  1 
ATOM   4068 N  N   . ARG B  1 240 ? -0.376  9.848   -12.804 1.00 14.58  ? 240 ARG B N   1 
ATOM   4069 C  CA  . ARG B  1 240 ? 0.278   8.950   -11.832 1.00 16.38  ? 240 ARG B CA  1 
ATOM   4070 C  C   . ARG B  1 240 ? -0.746  7.824   -11.511 1.00 14.85  ? 240 ARG B C   1 
ATOM   4071 O  O   . ARG B  1 240 ? -1.889  8.128   -11.207 1.00 15.44  ? 240 ARG B O   1 
ATOM   4072 C  CB  . ARG B  1 240 ? 0.586   9.715   -10.492 1.00 18.67  ? 240 ARG B CB  1 
ATOM   4073 C  CG  . ARG B  1 240 ? 1.755   10.698  -10.681 1.00 23.76  ? 240 ARG B CG  1 
ATOM   4074 C  CD  . ARG B  1 240 ? 2.057   11.422  -9.384  1.00 28.57  ? 240 ARG B CD  1 
ATOM   4075 N  NE  . ARG B  1 240 ? 1.063   12.440  -8.843  1.00 39.80  ? 240 ARG B NE  1 
ATOM   4076 C  CZ  . ARG B  1 240 ? 0.223   12.217  -7.791  1.00 30.55  ? 240 ARG B CZ  1 
ATOM   4077 N  NH1 . ARG B  1 240 ? 0.122   11.030  -7.193  1.00 42.24  ? 240 ARG B NH1 1 
ATOM   4078 N  NH2 . ARG B  1 240 ? -0.625  13.161  -7.346  1.00 38.71  ? 240 ARG B NH2 1 
ATOM   4079 N  N   . GLU B  1 241 ? -0.361  6.578   -11.738 1.00 16.33  ? 241 GLU B N   1 
ATOM   4080 C  CA  . GLU B  1 241 ? -1.198  5.428   -11.396 1.00 17.29  ? 241 GLU B CA  1 
ATOM   4081 C  C   . GLU B  1 241 ? -1.425  5.360   -9.878  1.00 16.20  ? 241 GLU B C   1 
ATOM   4082 O  O   . GLU B  1 241 ? -0.504  5.479   -9.087  1.00 17.90  ? 241 GLU B O   1 
ATOM   4083 C  CB  . GLU B  1 241 ? -0.451  4.117   -11.825 1.00 19.47  ? 241 GLU B CB  1 
ATOM   4084 C  CG  . GLU B  1 241 ? -0.393  4.050   -13.329 1.00 20.79  ? 241 GLU B CG  1 
ATOM   4085 C  CD  . GLU B  1 241 ? 0.368   2.845   -13.808 1.00 29.43  ? 241 GLU B CD  1 
ATOM   4086 O  OE1 . GLU B  1 241 ? 1.305   2.456   -13.106 1.00 33.54  ? 241 GLU B OE1 1 
ATOM   4087 O  OE2 . GLU B  1 241 ? -0.005  2.281   -14.859 1.00 37.55  ? 241 GLU B OE2 1 
ATOM   4088 N  N   . MET B  1 242 ? -2.661  5.019   -9.489  1.00 14.34  ? 242 MET B N   1 
ATOM   4089 C  CA  . MET B  1 242 ? -2.987  4.841   -8.051  1.00 13.78  ? 242 MET B CA  1 
ATOM   4090 C  C   . MET B  1 242 ? -2.736  3.371   -7.719  1.00 11.87  ? 242 MET B C   1 
ATOM   4091 O  O   . MET B  1 242 ? -3.595  2.481   -7.903  1.00 12.83  ? 242 MET B O   1 
ATOM   4092 C  CB  . MET B  1 242 ? -4.452  5.190   -7.866  1.00 14.20  ? 242 MET B CB  1 
ATOM   4093 C  CG  . MET B  1 242 ? -4.766  5.217   -6.338  1.00 15.55  ? 242 MET B CG  1 
ATOM   4094 S  SD  . MET B  1 242 ? -6.533  5.534   -6.038  1.00 13.91  ? 242 MET B SD  1 
ATOM   4095 C  CE  . MET B  1 242 ? -6.665  7.243   -6.569  1.00 15.87  ? 242 MET B CE  1 
ATOM   4096 N  N   . ILE B  1 243 ? -1.514  3.171   -7.219  1.00 12.17  ? 243 ILE B N   1 
ATOM   4097 C  CA  . ILE B  1 243 ? -1.012  1.878   -6.808  1.00 12.22  ? 243 ILE B CA  1 
ATOM   4098 C  C   . ILE B  1 243 ? -0.266  2.065   -5.486  1.00 10.99  ? 243 ILE B C   1 
ATOM   4099 O  O   . ILE B  1 243 ? 0.194   3.171   -5.141  1.00 11.88  ? 243 ILE B O   1 
ATOM   4100 C  CB  . ILE B  1 243 ? -0.110  1.266   -7.911  1.00 13.99  ? 243 ILE B CB  1 
ATOM   4101 C  CG1 . ILE B  1 243 ? 1.087   2.160   -8.208  1.00 16.19  ? 243 ILE B CG1 1 
ATOM   4102 C  CG2 . ILE B  1 243 ? -0.899  0.802   -9.108  1.00 15.93  ? 243 ILE B CG2 1 
ATOM   4103 C  CD1 . ILE B  1 243 ? 2.157   1.588   -9.118  1.00 20.66  ? 243 ILE B CD1 1 
ATOM   4104 N  N   . ASN B  1 244 ? -0.135  0.968   -4.753  1.00 10.97  ? 244 ASN B N   1 
ATOM   4105 C  CA  . ASN B  1 244 ? 0.694   1.020   -3.543  1.00 10.98  ? 244 ASN B CA  1 
ATOM   4106 C  C   . ASN B  1 244 ? 0.239   2.073   -2.571  1.00 10.12  ? 244 ASN B C   1 
ATOM   4107 O  O   . ASN B  1 244 ? 1.082   2.749   -1.956  1.00 10.93  ? 244 ASN B O   1 
ATOM   4108 C  CB  . ASN B  1 244 ? 2.184   1.091   -3.818  1.00 12.88  ? 244 ASN B CB  1 
ATOM   4109 C  CG  . ASN B  1 244 ? 2.593   -0.007  -4.769  1.00 15.20  ? 244 ASN B CG  1 
ATOM   4110 O  OD1 . ASN B  1 244 ? 2.236   -1.161  -4.726  1.00 16.04  ? 244 ASN B OD1 1 
ATOM   4111 N  ND2 . ASN B  1 244 ? 3.485   0.435   -5.711  1.00 20.33  ? 244 ASN B ND2 1 
ATOM   4112 N  N   . ASN B  1 245 ? -1.071  2.220   -2.382  1.00 9.37   ? 245 ASN B N   1 
ATOM   4113 C  CA  . ASN B  1 245 ? -1.634  3.308   -1.594  1.00 8.98   ? 245 ASN B CA  1 
ATOM   4114 C  C   . ASN B  1 245 ? -1.856  2.846   -0.162  1.00 8.75   ? 245 ASN B C   1 
ATOM   4115 O  O   . ASN B  1 245 ? -2.968  2.943   0.355   1.00 10.08  ? 245 ASN B O   1 
ATOM   4116 C  CB  . ASN B  1 245 ? -2.868  3.920   -2.218  1.00 9.49   ? 245 ASN B CB  1 
ATOM   4117 C  CG  . ASN B  1 245 ? -3.979  2.931   -2.410  1.00 9.31   ? 245 ASN B CG  1 
ATOM   4118 O  OD1 . ASN B  1 245 ? -3.782  1.721   -2.436  1.00 10.49  ? 245 ASN B OD1 1 
ATOM   4119 N  ND2 . ASN B  1 245 ? -5.221  3.458   -2.591  1.00 10.94  ? 245 ASN B ND2 1 
ATOM   4120 N  N   . PHE B  1 246 ? -0.812  2.329   0.455   1.00 9.60   ? 246 PHE B N   1 
ATOM   4121 C  CA  . PHE B  1 246 ? -0.889  1.896   1.859   1.00 8.79   ? 246 PHE B CA  1 
ATOM   4122 C  C   . PHE B  1 246 ? 0.286   2.488   2.555   1.00 9.04   ? 246 PHE B C   1 
ATOM   4123 O  O   . PHE B  1 246 ? 1.384   2.670   1.985   1.00 9.13   ? 246 PHE B O   1 
ATOM   4124 C  CB  . PHE B  1 246 ? -0.807  0.316   1.943   1.00 9.92   ? 246 PHE B CB  1 
ATOM   4125 C  CG  . PHE B  1 246 ? 0.415   -0.291  1.330   1.00 9.36   ? 246 PHE B CG  1 
ATOM   4126 C  CD1 . PHE B  1 246 ? 0.516   -0.570  -0.028  1.00 9.83   ? 246 PHE B CD1 1 
ATOM   4127 C  CD2 . PHE B  1 246 ? 1.528   -0.621  2.182   1.00 11.57  ? 246 PHE B CD2 1 
ATOM   4128 C  CE1 . PHE B  1 246 ? 1.708   -1.157  -0.596  1.00 11.52  ? 246 PHE B CE1 1 
ATOM   4129 C  CE2 . PHE B  1 246 ? 2.684   -1.161  1.632   1.00 12.15  ? 246 PHE B CE2 1 
ATOM   4130 C  CZ  . PHE B  1 246 ? 2.766   -1.433  0.264   1.00 12.23  ? 246 PHE B CZ  1 
ATOM   4131 N  N   . ARG B  1 247 ? 0.125   2.774   3.827   1.00 8.48   ? 247 ARG B N   1 
ATOM   4132 C  CA  . ARG B  1 247 ? 1.202   3.268   4.742   1.00 8.63   ? 247 ARG B CA  1 
ATOM   4133 C  C   . ARG B  1 247 ? 1.955   2.089   5.320   1.00 8.40   ? 247 ARG B C   1 
ATOM   4134 O  O   . ARG B  1 247 ? 1.330   1.074   5.653   1.00 9.15   ? 247 ARG B O   1 
ATOM   4135 C  CB  . ARG B  1 247 ? 0.581   4.137   5.829   1.00 9.48   ? 247 ARG B CB  1 
ATOM   4136 C  CG  . ARG B  1 247 ? 1.566   5.016   6.552   1.00 9.58   ? 247 ARG B CG  1 
ATOM   4137 C  CD  . ARG B  1 247 ? 0.872   5.681   7.734   1.00 9.49   ? 247 ARG B CD  1 
ATOM   4138 N  NE  . ARG B  1 247 ? 1.722   6.755   8.315   1.00 9.54   ? 247 ARG B NE  1 
ATOM   4139 C  CZ  . ARG B  1 247 ? 1.360   7.461   9.379   1.00 9.09   ? 247 ARG B CZ  1 
ATOM   4140 N  NH1 . ARG B  1 247 ? 0.268   7.186   10.085  1.00 10.34  ? 247 ARG B NH1 1 
ATOM   4141 N  NH2 . ARG B  1 247 ? 2.136   8.492   9.751   1.00 10.33  ? 247 ARG B NH2 1 
ATOM   4142 N  N   . GLN B  1 248 ? 3.265   2.243   5.529   1.00 8.74   ? 248 GLN B N   1 
ATOM   4143 C  CA  . GLN B  1 248 ? 4.010   1.235   6.314   1.00 8.86   ? 248 GLN B CA  1 
ATOM   4144 C  C   . GLN B  1 248 ? 3.504   1.154   7.709   1.00 8.50   ? 248 GLN B C   1 
ATOM   4145 O  O   . GLN B  1 248 ? 2.954   2.143   8.270   1.00 9.19   ? 248 GLN B O   1 
ATOM   4146 C  CB  . GLN B  1 248 ? 5.510   1.627   6.345   1.00 8.93   ? 248 GLN B CB  1 
ATOM   4147 C  CG  . GLN B  1 248 ? 6.218   1.659   4.975   1.00 10.19  ? 248 GLN B CG  1 
ATOM   4148 C  CD  . GLN B  1 248 ? 6.249   0.302   4.302   1.00 9.72   ? 248 GLN B CD  1 
ATOM   4149 O  OE1 . GLN B  1 248 ? 5.355   -0.037  3.499   1.00 10.23  ? 248 GLN B OE1 1 
ATOM   4150 N  NE2 . GLN B  1 248 ? 7.232   -0.501  4.613   1.00 11.31  ? 248 GLN B NE2 1 
ATOM   4151 N  N   . VAL B  1 249 ? 3.716   0.023   8.368   1.00 8.72   ? 249 VAL B N   1 
ATOM   4152 C  CA  . VAL B  1 249 ? 3.328   -0.094  9.807   1.00 9.50   ? 249 VAL B CA  1 
ATOM   4153 C  C   . VAL B  1 249 ? 4.161   0.823   10.677  1.00 9.24   ? 249 VAL B C   1 
ATOM   4154 O  O   . VAL B  1 249 ? 5.340   1.108   10.368  1.00 10.13  ? 249 VAL B O   1 
ATOM   4155 C  CB  . VAL B  1 249 ? 3.379   -1.568  10.274  1.00 10.10  ? 249 VAL B CB  1 
ATOM   4156 C  CG1 . VAL B  1 249 ? 2.349   -2.397  9.540   1.00 10.72  ? 249 VAL B CG1 1 
ATOM   4157 C  CG2 . VAL B  1 249 ? 4.784   -2.165  10.140  1.00 12.40  ? 249 VAL B CG2 1 
ATOM   4158 N  N   . GLN B  1 250 ? 3.584   1.216   11.790  1.00 9.50   ? 250 GLN B N   1 
ATOM   4159 C  CA  . GLN B  1 250 ? 4.105   2.219   12.706  1.00 8.96   ? 250 GLN B CA  1 
ATOM   4160 C  C   . GLN B  1 250 ? 4.607   1.578   13.966  1.00 10.11  ? 250 GLN B C   1 
ATOM   4161 O  O   . GLN B  1 250 ? 4.169   0.508   14.347  1.00 11.34  ? 250 GLN B O   1 
ATOM   4162 C  CB  . GLN B  1 250 ? 2.996   3.199   13.067  1.00 9.97   ? 250 GLN B CB  1 
ATOM   4163 C  CG  . GLN B  1 250 ? 2.310   3.830   11.865  1.00 11.05  ? 250 GLN B CG  1 
ATOM   4164 C  CD  . GLN B  1 250 ? 3.237   4.737   11.065  1.00 9.63   ? 250 GLN B CD  1 
ATOM   4165 O  OE1 . GLN B  1 250 ? 3.648   5.814   11.651  1.00 10.62  ? 250 GLN B OE1 1 
ATOM   4166 N  NE2 . GLN B  1 250 ? 3.547   4.448   9.849   1.00 10.14  ? 250 GLN B NE2 1 
ATOM   4167 N  N   . LYS B  1 251 ? 5.521   2.267   14.674  1.00 10.65  ? 251 LYS B N   1 
ATOM   4168 C  CA  . LYS B  1 251 ? 5.934   1.803   16.015  1.00 11.76  ? 251 LYS B CA  1 
ATOM   4169 C  C   . LYS B  1 251 ? 4.701   1.742   16.912  1.00 10.82  ? 251 LYS B C   1 
ATOM   4170 O  O   . LYS B  1 251 ? 3.795   2.560   16.831  1.00 12.26  ? 251 LYS B O   1 
ATOM   4171 C  CB  . LYS B  1 251 ? 6.907   2.779   16.623  1.00 14.20  ? 251 LYS B CB  1 
ATOM   4172 C  CG  . LYS B  1 251 ? 8.300   2.894   15.971  1.00 16.64  ? 251 LYS B CG  1 
ATOM   4173 C  CD  . LYS B  1 251 ? 9.153   1.792   16.432  1.00 17.65  ? 251 LYS B CD  1 
ATOM   4174 C  CE  . LYS B  1 251 ? 10.653  1.892   16.073  1.00 14.93  ? 251 LYS B CE  1 
ATOM   4175 N  NZ  . LYS B  1 251 ? 10.857  1.827   14.615  1.00 11.85  ? 251 LYS B NZ  1 
ATOM   4176 N  N   . PHE B  1 252 ? 4.695   0.752   17.783  1.00 12.40  ? 252 PHE B N   1 
ATOM   4177 C  CA  . PHE B  1 252 ? 3.549   0.640   18.670  1.00 14.44  ? 252 PHE B CA  1 
ATOM   4178 C  C   . PHE B  1 252 ? 3.400   1.745   19.849  1.00 26.46  ? 252 PHE B C   1 
ATOM   4179 O  O   . PHE B  1 252 ? 2.354   1.888   20.385  1.00 25.26  ? 252 PHE B O   1 
ATOM   4180 C  CB  . PHE B  1 252 ? 3.030   -0.766  19.090  1.00 18.22  ? 252 PHE B CB  1 
ATOM   4181 C  CG  . PHE B  1 252 ? 1.532   -0.764  19.422  1.00 15.92  ? 252 PHE B CG  1 
ATOM   4182 C  CD1 . PHE B  1 252 ? 0.943   -1.765  20.169  1.00 18.48  ? 252 PHE B CD1 1 
ATOM   4183 C  CD2 . PHE B  1 252 ? 0.723   0.255   18.940  1.00 17.72  ? 252 PHE B CD2 1 
ATOM   4184 C  CE1 . PHE B  1 252 ? -0.424  -1.755  20.423  1.00 22.10  ? 252 PHE B CE1 1 
ATOM   4185 C  CE2 . PHE B  1 252 ? -0.645  0.265   19.195  1.00 22.00  ? 252 PHE B CE2 1 
ATOM   4186 C  CZ  . PHE B  1 252 ? -1.211  -0.745  19.952  1.00 22.65  ? 252 PHE B CZ  1 
ATOM   4187 N  N   . ASP B  1 253 ? 4.484   2.482   20.176  1.00 22.13  ? 253 ASP B N   1 
ATOM   4188 C  CA  . ASP B  1 253 ? 4.452   3.509   21.240  1.00 22.58  ? 253 ASP B CA  1 
ATOM   4189 C  C   . ASP B  1 253 ? 3.838   2.941   22.567  1.00 28.24  ? 253 ASP B C   1 
ATOM   4190 O  O   . ASP B  1 253 ? 3.044   3.621   23.176  1.00 37.56  ? 253 ASP B O   1 
ATOM   4191 C  CB  . ASP B  1 253 ? 3.653   4.782   20.797  1.00 36.62  ? 253 ASP B CB  1 
ATOM   4192 C  CG  . ASP B  1 253 ? 4.194   5.454   19.536  1.00 42.56  ? 253 ASP B CG  1 
ATOM   4193 O  OD1 . ASP B  1 253 ? 5.422   5.481   19.364  1.00 38.37  ? 253 ASP B OD1 1 
ATOM   4194 O  OD2 . ASP B  1 253 ? 3.376   6.012   18.755  1.00 47.01  ? 253 ASP B OD2 1 
ATOM   4195 N  N   . GLU B  1 254 ? 4.225   1.714   22.948  1.00 25.14  ? 254 GLU B N   1 
ATOM   4196 C  CA  . GLU B  1 254 ? 3.754   0.989   24.062  1.00 28.54  ? 254 GLU B CA  1 
ATOM   4197 C  C   . GLU B  1 254 ? 2.229   0.565   24.066  1.00 27.33  ? 254 GLU B C   1 
ATOM   4198 O  O   . GLU B  1 254 ? 1.824   -0.099  25.020  1.00 29.70  ? 254 GLU B O   1 
ATOM   4199 N  N   . ARG B  1 255 ? 1.525   0.747   22.944  1.00 25.89  ? 255 ARG B N   1 
ATOM   4200 C  CA  . ARG B  1 255 ? 0.227   0.258   23.013  1.00 19.03  ? 255 ARG B CA  1 
ATOM   4201 C  C   . ARG B  1 255 ? 0.145   -1.348  22.921  1.00 22.17  ? 255 ARG B C   1 
ATOM   4202 O  O   . ARG B  1 255 ? 1.111   -2.060  22.504  1.00 26.05  ? 255 ARG B O   1 
ATOM   4203 C  CB  . ARG B  1 255 ? -0.435  0.758   21.621  1.00 23.28  ? 255 ARG B CB  1 
ATOM   4204 C  CG  . ARG B  1 255 ? -0.787  2.254   21.535  1.00 25.51  ? 255 ARG B CG  1 
ATOM   4205 C  CD  . ARG B  1 255 ? -1.229  2.673   20.120  1.00 21.46  ? 255 ARG B CD  1 
ATOM   4206 N  NE  . ARG B  1 255 ? -0.143  2.711   19.153  1.00 22.84  ? 255 ARG B NE  1 
ATOM   4207 C  CZ  . ARG B  1 255 ? -0.266  3.010   17.874  1.00 22.22  ? 255 ARG B CZ  1 
ATOM   4208 N  NH1 . ARG B  1 255 ? -1.504  3.219   17.367  1.00 16.41  ? 255 ARG B NH1 1 
ATOM   4209 N  NH2 . ARG B  1 255 ? 0.876   3.099   17.110  1.00 17.66  ? 255 ARG B NH2 1 
ATOM   4210 N  N   . LEU B  1 256 ? -1.066  -1.822  23.309  1.00 21.71  ? 256 LEU B N   1 
ATOM   4211 C  CA  . LEU B  1 256 ? -1.390  -3.246  23.166  1.00 21.07  ? 256 LEU B CA  1 
ATOM   4212 C  C   . LEU B  1 256 ? -2.608  -3.296  22.328  1.00 17.58  ? 256 LEU B C   1 
ATOM   4213 O  O   . LEU B  1 256 ? -3.322  -2.257  22.160  1.00 21.70  ? 256 LEU B O   1 
ATOM   4214 C  CB  . LEU B  1 256 ? -1.689  -3.967  24.412  1.00 21.37  ? 256 LEU B CB  1 
ATOM   4215 C  CG  . LEU B  1 256 ? -0.512  -4.055  25.376  1.00 21.03  ? 256 LEU B CG  1 
ATOM   4216 C  CD1 . LEU B  1 256 ? -1.168  -4.828  26.496  1.00 29.88  ? 256 LEU B CD1 1 
ATOM   4217 C  CD2 . LEU B  1 256 ? 0.651   -4.815  24.748  1.00 27.17  ? 256 LEU B CD2 1 
ATOM   4218 N  N   . VAL B  1 257 ? -2.751  -4.364  21.644  1.00 16.68  ? 257 VAL B N   1 
ATOM   4219 C  CA  . VAL B  1 257 ? -3.913  -4.615  20.805  1.00 13.85  ? 257 VAL B CA  1 
ATOM   4220 C  C   . VAL B  1 257 ? -4.722  -5.649  21.574  1.00 14.32  ? 257 VAL B C   1 
ATOM   4221 O  O   . VAL B  1 257 ? -4.245  -6.706  21.978  1.00 15.81  ? 257 VAL B O   1 
ATOM   4222 C  CB  . VAL B  1 257 ? -3.487  -5.159  19.459  1.00 14.80  ? 257 VAL B CB  1 
ATOM   4223 C  CG1 . VAL B  1 257 ? -4.707  -5.539  18.684  1.00 15.64  ? 257 VAL B CG1 1 
ATOM   4224 C  CG2 . VAL B  1 257 ? -2.731  -4.098  18.670  1.00 15.75  ? 257 VAL B CG2 1 
ATOM   4225 N  N   . TYR B  1 258 ? -6.006  -5.390  21.708  1.00 12.94  ? 258 TYR B N   1 
ATOM   4226 C  CA  . TYR B  1 258 ? -6.910  -6.309  22.465  1.00 12.31  ? 258 TYR B CA  1 
ATOM   4227 C  C   . TYR B  1 258 ? -7.683  -7.203  21.529  1.00 11.69  ? 258 TYR B C   1 
ATOM   4228 O  O   . TYR B  1 258 ? -8.092  -6.722  20.475  1.00 14.33  ? 258 TYR B O   1 
ATOM   4229 C  CB  . TYR B  1 258 ? -7.781  -5.483  23.342  1.00 15.69  ? 258 TYR B CB  1 
ATOM   4230 C  CG  . TYR B  1 258 ? -6.981  -4.586  24.245  1.00 18.22  ? 258 TYR B CG  1 
ATOM   4231 C  CD1 . TYR B  1 258 ? -6.340  -5.148  25.347  1.00 20.60  ? 258 TYR B CD1 1 
ATOM   4232 C  CD2 . TYR B  1 258 ? -6.693  -3.213  23.917  1.00 19.10  ? 258 TYR B CD2 1 
ATOM   4233 C  CE1 . TYR B  1 258 ? -5.586  -4.325  26.216  1.00 26.48  ? 258 TYR B CE1 1 
ATOM   4234 C  CE2 . TYR B  1 258 ? -5.904  -2.438  24.725  1.00 24.02  ? 258 TYR B CE2 1 
ATOM   4235 C  CZ  . TYR B  1 258 ? -5.293  -3.000  25.829  1.00 26.01  ? 258 TYR B CZ  1 
ATOM   4236 O  OH  . TYR B  1 258 ? -4.485  -2.152  26.554  1.00 30.24  ? 258 TYR B OH  1 
ATOM   4237 N  N   . THR B  1 259 ? -7.837  -8.451  21.859  1.00 11.40  ? 259 THR B N   1 
ATOM   4238 C  CA  . THR B  1 259 ? -8.502  -9.375  20.993  1.00 11.75  ? 259 THR B CA  1 
ATOM   4239 C  C   . THR B  1 259 ? -9.766  -9.918  21.620  1.00 10.81  ? 259 THR B C   1 
ATOM   4240 O  O   . THR B  1 259 ? -9.839  -10.152 22.844  1.00 12.74  ? 259 THR B O   1 
ATOM   4241 C  CB  . THR B  1 259 ? -7.602  -10.557 20.598  1.00 12.21  ? 259 THR B CB  1 
ATOM   4242 O  OG1 . THR B  1 259 ? -7.171  -11.275 21.758  1.00 13.76  ? 259 THR B OG1 1 
ATOM   4243 C  CG2 . THR B  1 259 ? -6.355  -10.046 19.844  1.00 13.79  ? 259 THR B CG2 1 
ATOM   4244 N  N   . SER B  1 260 ? -10.787 -10.121 20.815  1.00 10.83  ? 260 SER B N   1 
ATOM   4245 C  CA  . SER B  1 260 ? -12.049 -10.723 21.319  1.00 11.25  ? 260 SER B CA  1 
ATOM   4246 C  C   . SER B  1 260 ? -11.993 -12.215 21.256  1.00 11.81  ? 260 SER B C   1 
ATOM   4247 O  O   . SER B  1 260 ? -12.961 -12.859 21.678  1.00 15.73  ? 260 SER B O   1 
ATOM   4248 C  CB  . SER B  1 260 ? -13.211 -10.245 20.459  1.00 12.07  ? 260 SER B CB  1 
ATOM   4249 O  OG  . SER B  1 260 ? -13.058 -10.769 19.129  1.00 11.55  ? 260 SER B OG  1 
ATOM   4250 N  N   . PHE B  1 261 ? -10.858 -12.815 20.897  1.00 11.99  ? 261 PHE B N   1 
ATOM   4251 C  CA  . PHE B  1 261 ? -10.653 -14.244 20.790  1.00 13.01  ? 261 PHE B CA  1 
ATOM   4252 C  C   . PHE B  1 261 ? -9.427  -14.527 21.616  1.00 13.23  ? 261 PHE B C   1 
ATOM   4253 O  O   . PHE B  1 261 ? -8.463  -13.764 21.721  1.00 14.00  ? 261 PHE B O   1 
ATOM   4254 C  CB  . PHE B  1 261 ? -10.508 -14.689 19.308  1.00 13.72  ? 261 PHE B CB  1 
ATOM   4255 C  CG  . PHE B  1 261 ? -9.417  -13.933 18.549  1.00 13.85  ? 261 PHE B CG  1 
ATOM   4256 C  CD1 . PHE B  1 261 ? -9.762  -12.688 17.955  1.00 12.57  ? 261 PHE B CD1 1 
ATOM   4257 C  CD2 . PHE B  1 261 ? -8.121  -14.426 18.449  1.00 15.20  ? 261 PHE B CD2 1 
ATOM   4258 C  CE1 . PHE B  1 261 ? -8.799  -11.987 17.257  1.00 14.18  ? 261 PHE B CE1 1 
ATOM   4259 C  CE2 . PHE B  1 261 ? -7.157  -13.683 17.774  1.00 16.84  ? 261 PHE B CE2 1 
ATOM   4260 C  CZ  . PHE B  1 261 ? -7.500  -12.497 17.087  1.00 15.13  ? 261 PHE B CZ  1 
ATOM   4261 N  N   . SER B  1 262 ? -9.429  -15.718 22.237  1.00 18.57  ? 262 SER B N   1 
ATOM   4262 C  CA  . SER B  1 262 ? -8.318  -15.988 23.092  1.00 21.42  ? 262 SER B CA  1 
ATOM   4263 C  C   . SER B  1 262 ? -7.129  -16.380 22.348  1.00 27.37  ? 262 SER B C   1 
ATOM   4264 O  O   . SER B  1 262 ? -5.977  -16.221 22.916  1.00 32.91  ? 262 SER B O   1 
ATOM   4265 C  CB  . SER B  1 262 ? -8.666  -16.754 24.412  1.00 31.30  ? 262 SER B CB  1 
ATOM   4266 O  OG  . SER B  1 262 ? -9.614  -17.718 24.299  1.00 37.93  ? 262 SER B OG  1 
ATOM   4267 N  N   . GLN B  1 263 ? -7.401  -17.106 21.299  1.00 56.76  ? 263 GLN B N   1 
ATOM   4268 C  CA  . GLN B  1 263 ? -6.697  -18.297 20.673  1.00 37.52  ? 263 GLN B CA  1 
ATOM   4269 C  C   . GLN B  1 263 ? -7.495  -18.634 19.368  1.00 55.78  ? 263 GLN B C   1 
ATOM   4270 O  O   . GLN B  1 263 ? -6.954  -19.290 18.370  1.00 42.97  ? 263 GLN B O   1 
ATOM   4271 C  CB  . GLN B  1 263 ? -6.518  -19.545 21.639  1.00 61.77  ? 263 GLN B CB  1 
ATOM   4272 C  CG  . GLN B  1 263 ? -7.831  -20.113 22.193  1.00 73.71  ? 263 GLN B CG  1 
ATOM   4273 C  CD  . GLN B  1 263 ? -7.555  -20.848 23.545  1.00 83.22  ? 263 GLN B CD  1 
ATOM   4274 O  OE1 . GLN B  1 263 ? -7.614  -22.121 23.495  1.00 43.95  ? 263 GLN B OE1 1 
ATOM   4275 N  NE2 . GLN B  1 263 ? -7.259  -20.076 24.696  1.00 102.94 ? 263 GLN B NE2 1 
ATOM   4276 O  OXT . GLN B  1 263 ? -8.681  -18.090 19.269  1.00 24.00  ? 263 GLN B OXT 1 
ATOM   4277 N  N   . LYS C  1 3   ? 33.309  18.145  -25.608 1.00 84.69  ? 3   LYS C N   1 
ATOM   4278 C  CA  . LYS C  1 3   ? 32.209  17.838  -24.624 1.00 51.15  ? 3   LYS C CA  1 
ATOM   4279 C  C   . LYS C  1 3   ? 31.161  16.890  -25.162 1.00 39.13  ? 3   LYS C C   1 
ATOM   4280 O  O   . LYS C  1 3   ? 29.999  16.914  -24.666 1.00 75.36  ? 3   LYS C O   1 
ATOM   4281 C  CB  . LYS C  1 3   ? 31.486  19.108  -24.233 1.00 48.01  ? 3   LYS C CB  1 
ATOM   4282 N  N   . TRP C  1 4   ? 31.557  16.173  -26.229 1.00 26.53  ? 4   TRP C N   1 
ATOM   4283 C  CA  . TRP C  1 4   ? 30.715  15.073  -26.836 1.00 20.17  ? 4   TRP C CA  1 
ATOM   4284 C  C   . TRP C  1 4   ? 30.664  13.888  -25.836 1.00 20.57  ? 4   TRP C C   1 
ATOM   4285 O  O   . TRP C  1 4   ? 31.598  13.602  -25.016 1.00 21.49  ? 4   TRP C O   1 
ATOM   4286 C  CB  . TRP C  1 4   ? 31.219  14.626  -28.246 1.00 19.26  ? 4   TRP C CB  1 
ATOM   4287 C  CG  . TRP C  1 4   ? 32.546  14.044  -28.235 1.00 17.15  ? 4   TRP C CG  1 
ATOM   4288 C  CD1 . TRP C  1 4   ? 33.794  14.660  -28.404 1.00 18.81  ? 4   TRP C CD1 1 
ATOM   4289 C  CD2 . TRP C  1 4   ? 32.845  12.653  -28.057 1.00 16.18  ? 4   TRP C CD2 1 
ATOM   4290 N  NE1 . TRP C  1 4   ? 34.762  13.737  -28.417 1.00 18.82  ? 4   TRP C NE1 1 
ATOM   4291 C  CE2 . TRP C  1 4   ? 34.237  12.473  -28.180 1.00 17.42  ? 4   TRP C CE2 1 
ATOM   4292 C  CE3 . TRP C  1 4   ? 32.009  11.492  -27.935 1.00 16.60  ? 4   TRP C CE3 1 
ATOM   4293 C  CZ2 . TRP C  1 4   ? 34.880  11.170  -28.095 1.00 18.31  ? 4   TRP C CZ2 1 
ATOM   4294 C  CZ3 . TRP C  1 4   ? 32.613  10.179  -27.870 1.00 15.62  ? 4   TRP C CZ3 1 
ATOM   4295 C  CH2 . TRP C  1 4   ? 34.044  9.997   -27.953 1.00 18.23  ? 4   TRP C CH2 1 
ATOM   4296 N  N   . THR C  1 5   ? 29.531  13.220  -25.907 1.00 18.88  ? 5   THR C N   1 
ATOM   4297 C  CA  . THR C  1 5   ? 29.302  12.020  -25.019 1.00 18.71  ? 5   THR C CA  1 
ATOM   4298 C  C   . THR C  1 5   ? 28.616  10.883  -25.822 1.00 17.98  ? 5   THR C C   1 
ATOM   4299 O  O   . THR C  1 5   ? 28.366  10.985  -27.019 1.00 17.68  ? 5   THR C O   1 
ATOM   4300 C  CB  . THR C  1 5   ? 28.307  12.455  -23.856 1.00 23.73  ? 5   THR C CB  1 
ATOM   4301 O  OG1 . THR C  1 5   ? 26.998  12.730  -24.513 1.00 22.73  ? 5   THR C OG1 1 
ATOM   4302 C  CG2 . THR C  1 5   ? 28.852  13.661  -23.038 1.00 26.97  ? 5   THR C CG2 1 
ATOM   4303 N  N   . TYR C  1 6   ? 28.183  9.855   -25.115 1.00 19.28  ? 6   TYR C N   1 
ATOM   4304 C  CA  . TYR C  1 6   ? 27.318  8.829   -25.656 1.00 18.60  ? 6   TYR C CA  1 
ATOM   4305 C  C   . TYR C  1 6   ? 25.936  8.864   -25.137 1.00 19.67  ? 6   TYR C C   1 
ATOM   4306 O  O   . TYR C  1 6   ? 25.184  7.877   -25.232 1.00 23.41  ? 6   TYR C O   1 
ATOM   4307 C  CB  . TYR C  1 6   ? 27.969  7.434   -25.430 1.00 19.32  ? 6   TYR C CB  1 
ATOM   4308 C  CG  . TYR C  1 6   ? 29.247  7.178   -26.171 1.00 17.06  ? 6   TYR C CG  1 
ATOM   4309 C  CD1 . TYR C  1 6   ? 29.261  6.628   -27.483 1.00 16.40  ? 6   TYR C CD1 1 
ATOM   4310 C  CD2 . TYR C  1 6   ? 30.492  7.406   -25.583 1.00 17.67  ? 6   TYR C CD2 1 
ATOM   4311 C  CE1 . TYR C  1 6   ? 30.431  6.350   -28.146 1.00 15.40  ? 6   TYR C CE1 1 
ATOM   4312 C  CE2 . TYR C  1 6   ? 31.665  7.108   -26.215 1.00 17.55  ? 6   TYR C CE2 1 
ATOM   4313 C  CZ  . TYR C  1 6   ? 31.611  6.618   -27.559 1.00 15.29  ? 6   TYR C CZ  1 
ATOM   4314 O  OH  . TYR C  1 6   ? 32.811  6.257   -28.188 1.00 18.12  ? 6   TYR C OH  1 
ATOM   4315 N  N   . PHE C  1 7   ? 25.494  9.967   -24.594 1.00 27.21  ? 7   PHE C N   1 
ATOM   4316 C  CA  . PHE C  1 7   ? 24.037  10.116  -24.198 1.00 29.39  ? 7   PHE C CA  1 
ATOM   4317 C  C   . PHE C  1 7   ? 23.475  11.527  -24.207 1.00 43.03  ? 7   PHE C C   1 
ATOM   4318 O  O   . PHE C  1 7   ? 24.076  12.451  -24.778 1.00 28.79  ? 7   PHE C O   1 
ATOM   4319 C  CB  . PHE C  1 7   ? 23.848  9.648   -22.797 1.00 34.34  ? 7   PHE C CB  1 
ATOM   4320 C  CG  . PHE C  1 7   ? 24.548  10.542  -21.827 1.00 32.30  ? 7   PHE C CG  1 
ATOM   4321 C  CD1 . PHE C  1 7   ? 23.825  11.599  -21.266 1.00 42.52  ? 7   PHE C CD1 1 
ATOM   4322 C  CD2 . PHE C  1 7   ? 25.894  10.391  -21.506 1.00 45.36  ? 7   PHE C CD2 1 
ATOM   4323 C  CE1 . PHE C  1 7   ? 24.433  12.556  -20.392 1.00 35.12  ? 7   PHE C CE1 1 
ATOM   4324 C  CE2 . PHE C  1 7   ? 26.551  11.305  -20.626 1.00 38.05  ? 7   PHE C CE2 1 
ATOM   4325 C  CZ  . PHE C  1 7   ? 25.824  12.399  -20.075 1.00 46.58  ? 7   PHE C CZ  1 
ATOM   4326 N  N   . GLY C  1 8   ? 22.409  11.726  -23.442 1.00 40.48  ? 8   GLY C N   1 
ATOM   4327 C  CA  . GLY C  1 8   ? 21.803  13.034  -23.285 1.00 34.30  ? 8   GLY C CA  1 
ATOM   4328 C  C   . GLY C  1 8   ? 21.734  13.913  -24.515 1.00 31.52  ? 8   GLY C C   1 
ATOM   4329 O  O   . GLY C  1 8   ? 21.318  13.455  -25.579 1.00 38.24  ? 8   GLY C O   1 
ATOM   4330 N  N   . PRO C  1 9   ? 22.141  15.187  -24.384 1.00 31.39  ? 9   PRO C N   1 
ATOM   4331 C  CA  . PRO C  1 9   ? 21.957  15.946  -25.623 1.00 28.37  ? 9   PRO C CA  1 
ATOM   4332 C  C   . PRO C  1 9   ? 23.251  16.043  -26.427 1.00 21.51  ? 9   PRO C C   1 
ATOM   4333 O  O   . PRO C  1 9   ? 23.190  16.740  -27.459 1.00 26.24  ? 9   PRO C O   1 
ATOM   4334 C  CB  . PRO C  1 9   ? 21.451  17.414  -25.167 1.00 29.79  ? 9   PRO C CB  1 
ATOM   4335 C  CG  . PRO C  1 9   ? 22.176  17.468  -23.827 1.00 36.53  ? 9   PRO C CG  1 
ATOM   4336 C  CD  . PRO C  1 9   ? 22.086  16.083  -23.181 1.00 37.60  ? 9   PRO C CD  1 
ATOM   4337 N  N   . ASP C  1 10  ? 24.414  15.599  -25.846 1.00 23.96  ? 10  ASP C N   1 
ATOM   4338 C  CA  . ASP C  1 10  ? 25.711  15.706  -26.488 1.00 22.99  ? 10  ASP C CA  1 
ATOM   4339 C  C   . ASP C  1 10  ? 26.112  14.411  -27.095 1.00 20.37  ? 10  ASP C C   1 
ATOM   4340 O  O   . ASP C  1 10  ? 27.325  14.228  -27.478 1.00 21.49  ? 10  ASP C O   1 
ATOM   4341 C  CB  . ASP C  1 10  ? 26.784  16.232  -25.526 1.00 26.73  ? 10  ASP C CB  1 
ATOM   4342 C  CG  . ASP C  1 10  ? 26.528  17.625  -25.160 1.00 36.63  ? 10  ASP C CG  1 
ATOM   4343 O  OD1 . ASP C  1 10  ? 26.106  18.424  -25.979 1.00 36.94  ? 10  ASP C OD1 1 
ATOM   4344 O  OD2 . ASP C  1 10  ? 26.637  17.969  -24.007 1.00 38.93  ? 10  ASP C OD2 1 
ATOM   4345 N  N   . GLY C  1 11  ? 25.170  13.459  -27.153 1.00 23.29  ? 11  GLY C N   1 
ATOM   4346 C  CA  . GLY C  1 11  ? 25.374  12.057  -27.663 1.00 19.15  ? 11  GLY C CA  1 
ATOM   4347 C  C   . GLY C  1 11  ? 25.416  12.021  -29.182 1.00 14.12  ? 11  GLY C C   1 
ATOM   4348 O  O   . GLY C  1 11  ? 25.497  13.015  -29.922 1.00 15.61  ? 11  GLY C O   1 
ATOM   4349 N  N   . GLU C  1 12  ? 25.474  10.737  -29.662 1.00 14.13  ? 12  GLU C N   1 
ATOM   4350 C  CA  . GLU C  1 12  ? 25.934  10.560  -31.033 1.00 12.27  ? 12  GLU C CA  1 
ATOM   4351 C  C   . GLU C  1 12  ? 25.055  11.195  -32.083 1.00 12.61  ? 12  GLU C C   1 
ATOM   4352 O  O   . GLU C  1 12  ? 25.607  11.510  -33.149 1.00 13.01  ? 12  GLU C O   1 
ATOM   4353 C  CB  . GLU C  1 12  ? 26.112  9.030   -31.255 1.00 13.60  ? 12  GLU C CB  1 
ATOM   4354 C  CG  . GLU C  1 12  ? 24.812  8.253   -31.342 1.00 13.10  ? 12  GLU C CG  1 
ATOM   4355 C  CD  . GLU C  1 12  ? 25.062  6.770   -31.178 1.00 12.67  ? 12  GLU C CD  1 
ATOM   4356 O  OE1 . GLU C  1 12  ? 25.340  6.050   -32.146 1.00 12.41  ? 12  GLU C OE1 1 
ATOM   4357 O  OE2 . GLU C  1 12  ? 25.072  6.327   -29.968 1.00 15.55  ? 12  GLU C OE2 1 
ATOM   4358 N  N   . ASN C  1 13  ? 23.760  11.335  -31.861 1.00 12.28  ? 13  ASN C N   1 
ATOM   4359 C  CA  . ASN C  1 13  ? 22.973  11.988  -32.914 1.00 12.65  ? 13  ASN C CA  1 
ATOM   4360 C  C   . ASN C  1 13  ? 23.303  13.479  -33.079 1.00 11.73  ? 13  ASN C C   1 
ATOM   4361 O  O   . ASN C  1 13  ? 22.928  14.038  -34.076 1.00 13.12  ? 13  ASN C O   1 
ATOM   4362 C  CB  . ASN C  1 13  ? 21.481  11.822  -32.609 1.00 13.15  ? 13  ASN C CB  1 
ATOM   4363 C  CG  . ASN C  1 13  ? 20.998  10.392  -32.704 1.00 11.76  ? 13  ASN C CG  1 
ATOM   4364 O  OD1 . ASN C  1 13  ? 21.707  9.504   -33.232 1.00 12.79  ? 13  ASN C OD1 1 
ATOM   4365 N  ND2 . ASN C  1 13  ? 19.796  10.168  -32.239 1.00 12.37  ? 13  ASN C ND2 1 
ATOM   4366 N  N   . SER C  1 14  ? 23.985  14.057  -32.087 1.00 12.57  ? 14  SER C N   1 
ATOM   4367 C  CA  . SER C  1 14  ? 24.350  15.488  -32.152 1.00 13.33  ? 14  SER C CA  1 
ATOM   4368 C  C   . SER C  1 14  ? 25.812  15.702  -32.482 1.00 12.62  ? 14  SER C C   1 
ATOM   4369 O  O   . SER C  1 14  ? 26.206  16.841  -32.656 1.00 14.20  ? 14  SER C O   1 
ATOM   4370 C  CB  . SER C  1 14  ? 24.097  16.134  -30.752 1.00 17.86  ? 14  SER C CB  1 
ATOM   4371 O  OG  . SER C  1 14  ? 22.702  16.142  -30.524 1.00 21.81  ? 14  SER C OG  1 
ATOM   4372 N  N   . TRP C  1 15  ? 26.582  14.643  -32.655 1.00 12.78  ? 15  TRP C N   1 
ATOM   4373 C  CA  . TRP C  1 15  ? 28.032  14.820  -32.978 1.00 13.30  ? 15  TRP C CA  1 
ATOM   4374 C  C   . TRP C  1 15  ? 28.207  15.678  -34.236 1.00 13.88  ? 15  TRP C C   1 
ATOM   4375 O  O   . TRP C  1 15  ? 29.163  16.470  -34.323 1.00 13.83  ? 15  TRP C O   1 
ATOM   4376 C  CB  . TRP C  1 15  ? 28.702  13.543  -33.193 1.00 13.06  ? 15  TRP C CB  1 
ATOM   4377 C  CG  . TRP C  1 15  ? 28.841  12.693  -31.912 1.00 12.33  ? 15  TRP C CG  1 
ATOM   4378 C  CD1 . TRP C  1 15  ? 28.562  13.028  -30.608 1.00 13.74  ? 15  TRP C CD1 1 
ATOM   4379 C  CD2 . TRP C  1 15  ? 29.315  11.363  -31.870 1.00 11.80  ? 15  TRP C CD2 1 
ATOM   4380 N  NE1 . TRP C  1 15  ? 28.848  11.961  -29.779 1.00 13.02  ? 15  TRP C NE1 1 
ATOM   4381 C  CE2 . TRP C  1 15  ? 29.302  10.895  -30.513 1.00 12.80  ? 15  TRP C CE2 1 
ATOM   4382 C  CE3 . TRP C  1 15  ? 29.743  10.466  -32.898 1.00 12.60  ? 15  TRP C CE3 1 
ATOM   4383 C  CZ2 . TRP C  1 15  ? 29.688  9.643   -30.162 1.00 12.54  ? 15  TRP C CZ2 1 
ATOM   4384 C  CZ3 . TRP C  1 15  ? 30.095  9.167   -32.539 1.00 11.65  ? 15  TRP C CZ3 1 
ATOM   4385 C  CH2 . TRP C  1 15  ? 30.122  8.743   -31.193 1.00 13.04  ? 15  TRP C CH2 1 
ATOM   4386 N  N   . SER C  1 16  ? 27.359  15.491  -35.256 1.00 11.96  ? 16  SER C N   1 
ATOM   4387 C  CA  . SER C  1 16  ? 27.538  16.163  -36.532 1.00 12.68  ? 16  SER C CA  1 
ATOM   4388 C  C   . SER C  1 16  ? 27.460  17.683  -36.463 1.00 13.36  ? 16  SER C C   1 
ATOM   4389 O  O   . SER C  1 16  ? 27.919  18.309  -37.374 1.00 13.89  ? 16  SER C O   1 
ATOM   4390 C  CB  . SER C  1 16  ? 26.505  15.634  -37.511 1.00 13.79  ? 16  SER C CB  1 
ATOM   4391 O  OG  . SER C  1 16  ? 25.205  16.012  -37.098 1.00 14.75  ? 16  SER C OG  1 
ATOM   4392 N  N   A LYS C  1 17  ? 26.899  18.224  -35.386 0.50 12.88  ? 17  LYS C N   1 
ATOM   4393 N  N   B LYS C  1 17  ? 26.919  18.217  -35.380 0.50 13.41  ? 17  LYS C N   1 
ATOM   4394 C  CA  A LYS C  1 17  ? 26.948  19.703  -35.211 0.50 13.35  ? 17  LYS C CA  1 
ATOM   4395 C  CA  B LYS C  1 17  ? 26.795  19.690  -35.364 0.50 13.89  ? 17  LYS C CA  1 
ATOM   4396 C  C   A LYS C  1 17  ? 28.392  20.230  -35.216 0.50 13.07  ? 17  LYS C C   1 
ATOM   4397 C  C   B LYS C  1 17  ? 28.146  20.353  -35.154 0.50 14.63  ? 17  LYS C C   1 
ATOM   4398 O  O   A LYS C  1 17  ? 28.817  21.022  -36.064 0.50 13.81  ? 17  LYS C O   1 
ATOM   4399 O  O   B LYS C  1 17  ? 28.442  21.385  -35.698 0.50 15.54  ? 17  LYS C O   1 
ATOM   4400 C  CB  A LYS C  1 17  ? 26.266  20.035  -33.863 0.50 14.72  ? 17  LYS C CB  1 
ATOM   4401 C  CB  B LYS C  1 17  ? 25.838  20.081  -34.238 0.50 12.83  ? 17  LYS C CB  1 
ATOM   4402 C  CG  A LYS C  1 17  ? 24.766  19.766  -33.902 0.50 15.73  ? 17  LYS C CG  1 
ATOM   4403 C  CG  B LYS C  1 17  ? 24.355  19.928  -34.490 0.50 17.80  ? 17  LYS C CG  1 
ATOM   4404 C  CD  A LYS C  1 17  ? 24.245  19.637  -32.464 0.50 18.39  ? 17  LYS C CD  1 
ATOM   4405 C  CD  B LYS C  1 17  ? 23.593  20.282  -33.221 0.50 19.19  ? 17  LYS C CD  1 
ATOM   4406 C  CE  A LYS C  1 17  ? 22.819  19.151  -32.337 0.50 19.59  ? 17  LYS C CE  1 
ATOM   4407 C  CE  B LYS C  1 17  ? 23.863  21.754  -32.844 0.50 23.53  ? 17  LYS C CE  1 
ATOM   4408 N  NZ  A LYS C  1 17  ? 22.229  19.441  -31.014 0.50 19.73  ? 17  LYS C NZ  1 
ATOM   4409 N  NZ  B LYS C  1 17  ? 22.890  21.904  -31.783 0.50 28.20  ? 17  LYS C NZ  1 
ATOM   4410 N  N   A LYS C  1 18  ? 29.168  19.766  -34.248 0.50 14.39  ? 18  LYS C N   1 
ATOM   4411 N  N   B LYS C  1 18  ? 29.024  19.696  -34.397 0.50 13.83  ? 18  LYS C N   1 
ATOM   4412 C  CA  A LYS C  1 18  ? 30.557  20.234  -34.182 0.50 16.06  ? 18  LYS C CA  1 
ATOM   4413 C  CA  B LYS C  1 18  ? 30.377  20.237  -34.228 0.50 15.58  ? 18  LYS C CA  1 
ATOM   4414 C  C   A LYS C  1 18  ? 31.528  19.386  -34.926 0.50 17.59  ? 18  LYS C C   1 
ATOM   4415 C  C   B LYS C  1 18  ? 31.370  19.506  -35.145 0.50 14.86  ? 18  LYS C C   1 
ATOM   4416 O  O   A LYS C  1 18  ? 32.709  19.765  -35.039 0.50 18.64  ? 18  LYS C O   1 
ATOM   4417 O  O   B LYS C  1 18  ? 32.394  20.075  -35.541 0.50 16.40  ? 18  LYS C O   1 
ATOM   4418 C  CB  A LYS C  1 18  ? 30.960  20.396  -32.686 0.50 20.84  ? 18  LYS C CB  1 
ATOM   4419 C  CB  B LYS C  1 18  ? 30.896  20.018  -32.762 0.50 15.17  ? 18  LYS C CB  1 
ATOM   4420 C  CG  A LYS C  1 18  ? 30.193  21.513  -32.027 0.50 21.23  ? 18  LYS C CG  1 
ATOM   4421 C  CG  B LYS C  1 18  ? 32.348  20.436  -32.496 0.50 17.79  ? 18  LYS C CG  1 
ATOM   4422 C  CD  A LYS C  1 18  ? 31.034  22.780  -31.985 0.50 26.49  ? 18  LYS C CD  1 
ATOM   4423 C  CD  B LYS C  1 18  ? 32.634  20.538  -30.993 0.50 19.77  ? 18  LYS C CD  1 
ATOM   4424 C  CE  A LYS C  1 18  ? 30.261  23.853  -31.247 0.50 28.26  ? 18  LYS C CE  1 
ATOM   4425 C  CE  B LYS C  1 18  ? 34.111  20.779  -30.714 0.50 24.78  ? 18  LYS C CE  1 
ATOM   4426 N  NZ  A LYS C  1 18  ? 28.838  23.763  -31.676 0.50 32.75  ? 18  LYS C NZ  1 
ATOM   4427 N  NZ  B LYS C  1 18  ? 34.218  21.399  -29.369 0.50 32.11  ? 18  LYS C NZ  1 
ATOM   4428 N  N   . TYR C  1 19  ? 31.076  18.240  -35.433 1.00 15.31  ? 19  TYR C N   1 
ATOM   4429 C  CA  . TYR C  1 19  ? 32.005  17.392  -36.144 1.00 14.34  ? 19  TYR C CA  1 
ATOM   4430 C  C   . TYR C  1 19  ? 31.335  16.935  -37.462 1.00 12.75  ? 19  TYR C C   1 
ATOM   4431 O  O   . TYR C  1 19  ? 30.691  15.825  -37.452 1.00 14.18  ? 19  TYR C O   1 
ATOM   4432 C  CB  . TYR C  1 19  ? 32.378  16.141  -35.283 1.00 15.24  ? 19  TYR C CB  1 
ATOM   4433 C  CG  . TYR C  1 19  ? 33.004  16.578  -33.952 1.00 14.99  ? 19  TYR C CG  1 
ATOM   4434 C  CD1 . TYR C  1 19  ? 34.343  16.940  -33.933 1.00 17.14  ? 19  TYR C CD1 1 
ATOM   4435 C  CD2 . TYR C  1 19  ? 32.234  16.533  -32.775 1.00 16.35  ? 19  TYR C CD2 1 
ATOM   4436 C  CE1 . TYR C  1 19  ? 34.951  17.288  -32.727 1.00 19.35  ? 19  TYR C CE1 1 
ATOM   4437 C  CE2 . TYR C  1 19  ? 32.851  16.880  -31.550 1.00 18.22  ? 19  TYR C CE2 1 
ATOM   4438 C  CZ  . TYR C  1 19  ? 34.145  17.251  -31.535 1.00 19.04  ? 19  TYR C CZ  1 
ATOM   4439 O  OH  . TYR C  1 19  ? 34.737  17.560  -30.324 1.00 23.58  ? 19  TYR C OH  1 
ATOM   4440 N  N   . PRO C  1 20  ? 31.396  17.733  -38.535 1.00 14.56  ? 20  PRO C N   1 
ATOM   4441 C  CA  . PRO C  1 20  ? 30.516  17.496  -39.663 1.00 14.29  ? 20  PRO C CA  1 
ATOM   4442 C  C   . PRO C  1 20  ? 30.746  16.125  -40.316 1.00 13.61  ? 20  PRO C C   1 
ATOM   4443 O  O   . PRO C  1 20  ? 29.828  15.591  -40.922 1.00 13.08  ? 20  PRO C O   1 
ATOM   4444 C  CB  . PRO C  1 20  ? 30.819  18.629  -40.678 1.00 16.49  ? 20  PRO C CB  1 
ATOM   4445 C  CG  . PRO C  1 20  ? 31.610  19.601  -39.888 1.00 23.98  ? 20  PRO C CG  1 
ATOM   4446 C  CD  . PRO C  1 20  ? 32.164  18.991  -38.632 1.00 15.86  ? 20  PRO C CD  1 
ATOM   4447 N  N   . SER C  1 21  ? 31.936  15.537  -40.197 1.00 12.64  ? 21  SER C N   1 
ATOM   4448 C  CA  . SER C  1 21  ? 32.125  14.213  -40.834 1.00 12.60  ? 21  SER C CA  1 
ATOM   4449 C  C   . SER C  1 21  ? 31.305  13.140  -40.200 1.00 12.07  ? 21  SER C C   1 
ATOM   4450 O  O   . SER C  1 21  ? 31.041  12.114  -40.839 1.00 12.86  ? 21  SER C O   1 
ATOM   4451 C  CB  . SER C  1 21  ? 33.602  13.777  -40.764 1.00 13.20  ? 21  SER C CB  1 
ATOM   4452 O  OG  . SER C  1 21  ? 34.412  14.610  -41.608 1.00 15.90  ? 21  SER C OG  1 
ATOM   4453 N  N   . CYS C  1 22  ? 30.775  13.365  -38.967 1.00 12.69  ? 22  CYS C N   1 
ATOM   4454 C  CA  . CYS C  1 22  ? 29.951  12.345  -38.358 1.00 12.11  ? 22  CYS C CA  1 
ATOM   4455 C  C   . CYS C  1 22  ? 28.615  12.165  -39.050 1.00 12.46  ? 22  CYS C C   1 
ATOM   4456 O  O   . CYS C  1 22  ? 27.925  11.156  -38.853 1.00 13.54  ? 22  CYS C O   1 
ATOM   4457 C  CB  . CYS C  1 22  ? 29.691  12.718  -36.866 1.00 13.10  ? 22  CYS C CB  1 
ATOM   4458 S  SG  . CYS C  1 22  ? 31.229  12.743  -35.871 1.00 13.88  ? 22  CYS C SG  1 
ATOM   4459 N  N   . GLY C  1 23  ? 28.235  13.136  -39.931 1.00 12.90  ? 23  GLY C N   1 
ATOM   4460 C  CA  . GLY C  1 23  ? 27.045  13.021  -40.783 1.00 13.43  ? 23  GLY C CA  1 
ATOM   4461 C  C   . GLY C  1 23  ? 27.382  12.759  -42.268 1.00 13.23  ? 23  GLY C C   1 
ATOM   4462 O  O   . GLY C  1 23  ? 26.488  12.856  -43.108 1.00 14.66  ? 23  GLY C O   1 
ATOM   4463 N  N   . GLY C  1 24  ? 28.657  12.437  -42.530 1.00 13.68  ? 24  GLY C N   1 
ATOM   4464 C  CA  . GLY C  1 24  ? 29.131  12.278  -43.903 1.00 15.31  ? 24  GLY C CA  1 
ATOM   4465 C  C   . GLY C  1 24  ? 29.219  10.839  -44.319 1.00 14.17  ? 24  GLY C C   1 
ATOM   4466 O  O   . GLY C  1 24  ? 28.542  9.940   -43.802 1.00 15.77  ? 24  GLY C O   1 
ATOM   4467 N  N   . LEU C  1 25  ? 30.068  10.607  -45.338 1.00 14.66  ? 25  LEU C N   1 
ATOM   4468 C  CA  . LEU C  1 25  ? 30.251  9.281   -45.940 1.00 14.95  ? 25  LEU C CA  1 
ATOM   4469 C  C   . LEU C  1 25  ? 31.118  8.363   -45.090 1.00 13.25  ? 25  LEU C C   1 
ATOM   4470 O  O   . LEU C  1 25  ? 31.881  8.807   -44.205 1.00 14.02  ? 25  LEU C O   1 
ATOM   4471 C  CB  . LEU C  1 25  ? 30.944  9.516   -47.358 1.00 19.95  ? 25  LEU C CB  1 
ATOM   4472 C  CG  . LEU C  1 25  ? 30.206  10.336  -48.322 1.00 22.66  ? 25  LEU C CG  1 
ATOM   4473 C  CD1 . LEU C  1 25  ? 30.911  10.552  -49.658 1.00 30.04  ? 25  LEU C CD1 1 
ATOM   4474 C  CD2 . LEU C  1 25  ? 28.817  9.770   -48.434 1.00 35.37  ? 25  LEU C CD2 1 
ATOM   4475 N  N   . LEU C  1 26  ? 31.032  7.085   -45.411 1.00 14.15  ? 26  LEU C N   1 
ATOM   4476 C  CA  . LEU C  1 26  ? 31.942  6.044   -44.983 1.00 12.76  ? 26  LEU C CA  1 
ATOM   4477 C  C   . LEU C  1 26  ? 31.891  5.854   -43.468 1.00 12.75  ? 26  LEU C C   1 
ATOM   4478 O  O   . LEU C  1 26  ? 32.935  5.498   -42.884 1.00 15.04  ? 26  LEU C O   1 
ATOM   4479 C  CB  . LEU C  1 26  ? 33.421  6.264   -45.466 1.00 16.30  ? 26  LEU C CB  1 
ATOM   4480 C  CG  . LEU C  1 26  ? 33.635  6.252   -47.033 1.00 20.69  ? 26  LEU C CG  1 
ATOM   4481 C  CD1 . LEU C  1 26  ? 35.180  6.263   -47.234 1.00 25.82  ? 26  LEU C CD1 1 
ATOM   4482 C  CD2 . LEU C  1 26  ? 32.947  5.130   -47.762 1.00 23.58  ? 26  LEU C CD2 1 
ATOM   4483 N  N   . GLN C  1 27  ? 30.745  6.026   -42.801 1.00 12.08  ? 27  GLN C N   1 
ATOM   4484 C  CA  . GLN C  1 27  ? 30.757  5.958   -41.323 1.00 10.54  ? 27  GLN C CA  1 
ATOM   4485 C  C   . GLN C  1 27  ? 30.761  4.538   -40.828 1.00 10.95  ? 27  GLN C C   1 
ATOM   4486 O  O   . GLN C  1 27  ? 30.140  3.596   -41.366 1.00 13.68  ? 27  GLN C O   1 
ATOM   4487 C  CB  . GLN C  1 27  ? 29.545  6.725   -40.802 1.00 11.38  ? 27  GLN C CB  1 
ATOM   4488 C  CG  . GLN C  1 27  ? 29.574  8.254   -41.086 1.00 11.58  ? 27  GLN C CG  1 
ATOM   4489 C  CD  . GLN C  1 27  ? 30.731  8.853   -40.376 1.00 10.89  ? 27  GLN C CD  1 
ATOM   4490 O  OE1 . GLN C  1 27  ? 30.714  9.048   -39.164 1.00 11.86  ? 27  GLN C OE1 1 
ATOM   4491 N  NE2 . GLN C  1 27  ? 31.836  9.148   -41.119 1.00 11.77  ? 27  GLN C NE2 1 
ATOM   4492 N  N   . SER C  1 28  ? 31.494  4.375   -39.710 1.00 10.56  ? 28  SER C N   1 
ATOM   4493 C  CA  . SER C  1 28  ? 31.586  3.136   -38.964 1.00 10.10  ? 28  SER C CA  1 
ATOM   4494 C  C   . SER C  1 28  ? 31.001  3.345   -37.559 1.00 10.03  ? 28  SER C C   1 
ATOM   4495 O  O   . SER C  1 28  ? 30.869  4.472   -37.099 1.00 10.86  ? 28  SER C O   1 
ATOM   4496 C  CB  . SER C  1 28  ? 33.054  2.820   -38.784 1.00 11.15  ? 28  SER C CB  1 
ATOM   4497 O  OG  . SER C  1 28  ? 33.661  2.542   -40.057 1.00 11.24  ? 28  SER C OG  1 
ATOM   4498 N  N   . PRO C  1 29  ? 30.633  2.246   -36.858 1.00 10.10  ? 29  PRO C N   1 
ATOM   4499 C  CA  . PRO C  1 29  ? 30.737  0.852   -37.209 1.00 9.88   ? 29  PRO C CA  1 
ATOM   4500 C  C   . PRO C  1 29  ? 29.504  0.440   -38.045 1.00 9.60   ? 29  PRO C C   1 
ATOM   4501 O  O   . PRO C  1 29  ? 28.576  1.186   -38.307 1.00 10.00  ? 29  PRO C O   1 
ATOM   4502 C  CB  . PRO C  1 29  ? 30.724  0.167   -35.821 1.00 10.84  ? 29  PRO C CB  1 
ATOM   4503 C  CG  . PRO C  1 29  ? 29.731  1.029   -35.083 1.00 10.99  ? 29  PRO C CG  1 
ATOM   4504 C  CD  . PRO C  1 29  ? 30.010  2.430   -35.519 1.00 11.02  ? 29  PRO C CD  1 
ATOM   4505 N  N   . ILE C  1 30  ? 29.534  -0.861  -38.431 1.00 10.58  ? 30  ILE C N   1 
ATOM   4506 C  CA  . ILE C  1 30  ? 28.499  -1.454  -39.331 1.00 10.73  ? 30  ILE C CA  1 
ATOM   4507 C  C   . ILE C  1 30  ? 28.179  -2.818  -38.830 1.00 10.82  ? 30  ILE C C   1 
ATOM   4508 O  O   . ILE C  1 30  ? 28.986  -3.469  -38.067 1.00 11.38  ? 30  ILE C O   1 
ATOM   4509 C  CB  . ILE C  1 30  ? 28.962  -1.489  -40.785 1.00 10.32  ? 30  ILE C CB  1 
ATOM   4510 C  CG1 . ILE C  1 30  ? 30.219  -2.385  -40.961 1.00 11.09  ? 30  ILE C CG1 1 
ATOM   4511 C  CG2 . ILE C  1 30  ? 29.165  -0.042  -41.276 1.00 12.03  ? 30  ILE C CG2 1 
ATOM   4512 C  CD1 . ILE C  1 30  ? 30.561  -2.572  -42.465 1.00 13.13  ? 30  ILE C CD1 1 
ATOM   4513 N  N   . ASP C  1 31  ? 27.045  -3.355  -39.300 1.00 10.67  ? 31  ASP C N   1 
ATOM   4514 C  CA  . ASP C  1 31  ? 26.697  -4.739  -39.146 1.00 11.48  ? 31  ASP C CA  1 
ATOM   4515 C  C   . ASP C  1 31  ? 27.330  -5.601  -40.247 1.00 11.57  ? 31  ASP C C   1 
ATOM   4516 O  O   . ASP C  1 31  ? 27.221  -5.312  -41.442 1.00 13.84  ? 31  ASP C O   1 
ATOM   4517 C  CB  . ASP C  1 31  ? 25.181  -4.888  -39.236 1.00 12.97  ? 31  ASP C CB  1 
ATOM   4518 C  CG  . ASP C  1 31  ? 24.735  -6.323  -38.998 1.00 13.35  ? 31  ASP C CG  1 
ATOM   4519 O  OD1 . ASP C  1 31  ? 25.251  -7.018  -38.070 1.00 14.00  ? 31  ASP C OD1 1 
ATOM   4520 O  OD2 . ASP C  1 31  ? 23.880  -6.821  -39.755 1.00 18.15  ? 31  ASP C OD2 1 
ATOM   4521 N  N   . LEU C  1 32  ? 28.040  -6.668  -39.866 1.00 13.39  ? 32  LEU C N   1 
ATOM   4522 C  CA  . LEU C  1 32  ? 28.736  -7.581  -40.782 1.00 13.52  ? 32  LEU C CA  1 
ATOM   4523 C  C   . LEU C  1 32  ? 27.856  -8.759  -40.969 1.00 14.76  ? 32  LEU C C   1 
ATOM   4524 O  O   . LEU C  1 32  ? 27.624  -9.570  -40.073 1.00 15.68  ? 32  LEU C O   1 
ATOM   4525 C  CB  . LEU C  1 32  ? 30.031  -8.011  -40.110 1.00 13.62  ? 32  LEU C CB  1 
ATOM   4526 C  CG  . LEU C  1 32  ? 30.981  -6.843  -39.686 1.00 13.39  ? 32  LEU C CG  1 
ATOM   4527 C  CD1 . LEU C  1 32  ? 32.161  -7.272  -38.818 1.00 16.96  ? 32  LEU C CD1 1 
ATOM   4528 C  CD2 . LEU C  1 32  ? 31.465  -6.074  -40.912 1.00 15.78  ? 32  LEU C CD2 1 
ATOM   4529 N  N   . HIS C  1 33  ? 27.201  -8.917  -42.105 1.00 18.08  ? 33  HIS C N   1 
ATOM   4530 C  CA  . HIS C  1 33  ? 26.230  -10.020 -42.335 1.00 21.12  ? 33  HIS C CA  1 
ATOM   4531 C  C   . HIS C  1 33  ? 26.423  -10.648 -43.657 1.00 19.95  ? 33  HIS C C   1 
ATOM   4532 O  O   . HIS C  1 33  ? 26.927  -9.933  -44.524 1.00 17.89  ? 33  HIS C O   1 
ATOM   4533 C  CB  . HIS C  1 33  ? 24.781  -9.521  -42.090 1.00 22.83  ? 33  HIS C CB  1 
ATOM   4534 C  CG  . HIS C  1 33  ? 24.318  -8.446  -42.970 1.00 21.69  ? 33  HIS C CG  1 
ATOM   4535 N  ND1 . HIS C  1 33  ? 23.625  -8.778  -44.135 1.00 28.91  ? 33  HIS C ND1 1 
ATOM   4536 C  CD2 . HIS C  1 33  ? 24.554  -7.120  -42.998 1.00 25.21  ? 33  HIS C CD2 1 
ATOM   4537 C  CE1 . HIS C  1 33  ? 23.351  -7.637  -44.769 1.00 29.20  ? 33  HIS C CE1 1 
ATOM   4538 N  NE2 . HIS C  1 33  ? 23.923  -6.620  -44.128 1.00 25.38  ? 33  HIS C NE2 1 
ATOM   4539 N  N   . SER C  1 34  ? 26.005  -11.929 -43.846 1.00 21.96  ? 34  SER C N   1 
ATOM   4540 C  CA  . SER C  1 34  ? 26.410  -12.755 -44.955 1.00 26.62  ? 34  SER C CA  1 
ATOM   4541 C  C   . SER C  1 34  ? 26.093  -12.117 -46.293 1.00 20.60  ? 34  SER C C   1 
ATOM   4542 O  O   . SER C  1 34  ? 26.893  -12.187 -47.235 1.00 23.41  ? 34  SER C O   1 
ATOM   4543 C  CB  . SER C  1 34  ? 25.748  -14.133 -44.761 1.00 31.22  ? 34  SER C CB  1 
ATOM   4544 O  OG  . SER C  1 34  ? 24.490  -13.733 -44.281 1.00 48.95  ? 34  SER C OG  1 
ATOM   4545 N  N   . ASP C  1 35  ? 24.927  -11.378 -46.380 1.00 23.39  ? 35  ASP C N   1 
ATOM   4546 C  CA  . ASP C  1 35  ? 24.535  -10.846 -47.694 1.00 24.55  ? 35  ASP C CA  1 
ATOM   4547 C  C   . ASP C  1 35  ? 25.427  -9.872  -48.293 1.00 19.95  ? 35  ASP C C   1 
ATOM   4548 O  O   . ASP C  1 35  ? 25.390  -9.611  -49.502 1.00 25.65  ? 35  ASP C O   1 
ATOM   4549 C  CB  . ASP C  1 35  ? 23.036  -10.314 -47.758 1.00 33.68  ? 35  ASP C CB  1 
ATOM   4550 C  CG  . ASP C  1 35  ? 21.978  -11.342 -47.379 1.00 51.78  ? 35  ASP C CG  1 
ATOM   4551 O  OD1 . ASP C  1 35  ? 22.215  -12.577 -47.446 1.00 51.45  ? 35  ASP C OD1 1 
ATOM   4552 O  OD2 . ASP C  1 35  ? 20.844  -10.880 -47.024 1.00 64.59  ? 35  ASP C OD2 1 
ATOM   4553 N  N   . ILE C  1 36  ? 26.282  -9.253  -47.467 1.00 17.79  ? 36  ILE C N   1 
ATOM   4554 C  CA  . ILE C  1 36  ? 27.162  -8.243  -47.995 1.00 15.96  ? 36  ILE C CA  1 
ATOM   4555 C  C   . ILE C  1 36  ? 28.642  -8.672  -47.985 1.00 14.71  ? 36  ILE C C   1 
ATOM   4556 O  O   . ILE C  1 36  ? 29.516  -7.863  -48.242 1.00 16.59  ? 36  ILE C O   1 
ATOM   4557 C  CB  . ILE C  1 36  ? 26.966  -6.885  -47.263 1.00 17.52  ? 36  ILE C CB  1 
ATOM   4558 C  CG1 . ILE C  1 36  ? 27.303  -7.047  -45.764 1.00 18.59  ? 36  ILE C CG1 1 
ATOM   4559 C  CG2 . ILE C  1 36  ? 25.637  -6.255  -47.609 1.00 22.18  ? 36  ILE C CG2 1 
ATOM   4560 C  CD1 . ILE C  1 36  ? 27.440  -5.759  -44.976 1.00 20.36  ? 36  ILE C CD1 1 
ATOM   4561 N  N   . LEU C  1 37  ? 28.981  -9.909  -47.669 1.00 16.45  ? 37  LEU C N   1 
ATOM   4562 C  CA  . LEU C  1 37  ? 30.360  -10.340 -47.645 1.00 16.16  ? 37  LEU C CA  1 
ATOM   4563 C  C   . LEU C  1 37  ? 30.818  -10.844 -48.967 1.00 17.07  ? 37  LEU C C   1 
ATOM   4564 O  O   . LEU C  1 37  ? 30.012  -11.472 -49.752 1.00 18.59  ? 37  LEU C O   1 
ATOM   4565 C  CB  . LEU C  1 37  ? 30.499  -11.498 -46.637 1.00 18.23  ? 37  LEU C CB  1 
ATOM   4566 C  CG  . LEU C  1 37  ? 29.996  -11.304 -45.236 1.00 18.85  ? 37  LEU C CG  1 
ATOM   4567 C  CD1 . LEU C  1 37  ? 30.202  -12.505 -44.337 1.00 21.17  ? 37  LEU C CD1 1 
ATOM   4568 C  CD2 . LEU C  1 37  ? 30.655  -9.979  -44.663 1.00 17.92  ? 37  LEU C CD2 1 
ATOM   4569 N  N   . GLN C  1 38  ? 32.072  -10.639 -49.292 1.00 15.65  ? 38  GLN C N   1 
ATOM   4570 C  CA  . GLN C  1 38  ? 32.609  -11.173 -50.542 1.00 16.43  ? 38  GLN C CA  1 
ATOM   4571 C  C   . GLN C  1 38  ? 34.069  -11.520 -50.275 1.00 14.99  ? 38  GLN C C   1 
ATOM   4572 O  O   . GLN C  1 38  ? 34.841  -10.681 -49.849 1.00 15.34  ? 38  GLN C O   1 
ATOM   4573 C  CB  . GLN C  1 38  ? 32.559  -10.107 -51.681 1.00 17.87  ? 38  GLN C CB  1 
ATOM   4574 C  CG  . GLN C  1 38  ? 33.043  -10.693 -53.066 1.00 19.13  ? 38  GLN C CG  1 
ATOM   4575 C  CD  . GLN C  1 38  ? 32.755  -9.699  -54.197 1.00 22.42  ? 38  GLN C CD  1 
ATOM   4576 O  OE1 . GLN C  1 38  ? 31.613  -9.630  -54.710 1.00 39.12  ? 38  GLN C OE1 1 
ATOM   4577 N  NE2 . GLN C  1 38  ? 33.643  -8.915  -54.460 1.00 23.49  ? 38  GLN C NE2 1 
ATOM   4578 N  N   . TYR C  1 39  ? 34.412  -12.766 -50.611 1.00 14.90  ? 39  TYR C N   1 
ATOM   4579 C  CA  . TYR C  1 39  ? 35.847  -13.158 -50.507 1.00 15.07  ? 39  TYR C CA  1 
ATOM   4580 C  C   . TYR C  1 39  ? 36.702  -12.364 -51.438 1.00 15.06  ? 39  TYR C C   1 
ATOM   4581 O  O   . TYR C  1 39  ? 36.343  -12.074 -52.624 1.00 16.10  ? 39  TYR C O   1 
ATOM   4582 C  CB  . TYR C  1 39  ? 35.894  -14.683 -50.878 1.00 17.49  ? 39  TYR C CB  1 
ATOM   4583 C  CG  . TYR C  1 39  ? 37.343  -15.151 -51.015 1.00 16.71  ? 39  TYR C CG  1 
ATOM   4584 C  CD1 . TYR C  1 39  ? 38.143  -15.288 -49.888 1.00 20.63  ? 39  TYR C CD1 1 
ATOM   4585 C  CD2 . TYR C  1 39  ? 37.889  -15.509 -52.275 1.00 18.73  ? 39  TYR C CD2 1 
ATOM   4586 C  CE1 . TYR C  1 39  ? 39.443  -15.676 -50.040 1.00 21.52  ? 39  TYR C CE1 1 
ATOM   4587 C  CE2 . TYR C  1 39  ? 39.182  -15.998 -52.417 1.00 19.84  ? 39  TYR C CE2 1 
ATOM   4588 C  CZ  . TYR C  1 39  ? 39.979  -16.005 -51.339 1.00 23.25  ? 39  TYR C CZ  1 
ATOM   4589 O  OH  . TYR C  1 39  ? 41.308  -16.424 -51.424 1.00 24.90  ? 39  TYR C OH  1 
ATOM   4590 N  N   . ASP C  1 40  ? 37.887  -11.979 -50.969 1.00 16.00  ? 40  ASP C N   1 
ATOM   4591 C  CA  . ASP C  1 40  ? 38.881  -11.191 -51.739 1.00 16.17  ? 40  ASP C CA  1 
ATOM   4592 C  C   . ASP C  1 40  ? 40.207  -11.813 -51.523 1.00 15.87  ? 40  ASP C C   1 
ATOM   4593 O  O   . ASP C  1 40  ? 40.732  -11.807 -50.411 1.00 16.31  ? 40  ASP C O   1 
ATOM   4594 C  CB  . ASP C  1 40  ? 38.772  -9.760  -51.218 1.00 16.98  ? 40  ASP C CB  1 
ATOM   4595 C  CG  . ASP C  1 40  ? 39.743  -8.809  -51.850 1.00 19.58  ? 40  ASP C CG  1 
ATOM   4596 O  OD1 . ASP C  1 40  ? 40.629  -9.210  -52.567 1.00 19.15  ? 40  ASP C OD1 1 
ATOM   4597 O  OD2 . ASP C  1 40  ? 39.623  -7.581  -51.512 1.00 25.07  ? 40  ASP C OD2 1 
ATOM   4598 N  N   . ALA C  1 41  ? 40.786  -12.377 -52.593 1.00 17.36  ? 41  ALA C N   1 
ATOM   4599 C  CA  . ALA C  1 41  ? 42.127  -13.087 -52.512 1.00 18.62  ? 41  ALA C CA  1 
ATOM   4600 C  C   . ALA C  1 41  ? 43.240  -12.170 -52.174 1.00 16.84  ? 41  ALA C C   1 
ATOM   4601 O  O   . ALA C  1 41  ? 44.334  -12.608 -51.852 1.00 18.58  ? 41  ALA C O   1 
ATOM   4602 C  CB  . ALA C  1 41  ? 42.348  -13.706 -53.873 1.00 22.18  ? 41  ALA C CB  1 
ATOM   4603 N  N   . SER C  1 42  ? 43.051  -10.856 -52.284 1.00 16.51  ? 42  SER C N   1 
ATOM   4604 C  CA  . SER C  1 42  ? 44.118  -9.943  -51.925 1.00 18.70  ? 42  SER C CA  1 
ATOM   4605 C  C   . SER C  1 42  ? 44.357  -9.883  -50.388 1.00 17.51  ? 42  SER C C   1 
ATOM   4606 O  O   . SER C  1 42  ? 45.349  -9.291  -49.979 1.00 19.39  ? 42  SER C O   1 
ATOM   4607 C  CB  . SER C  1 42  ? 43.888  -8.515  -52.396 1.00 20.26  ? 42  SER C CB  1 
ATOM   4608 O  OG  . SER C  1 42  ? 42.878  -7.806  -51.616 1.00 20.74  ? 42  SER C OG  1 
ATOM   4609 N  N   . LEU C  1 43  ? 43.372  -10.381 -49.607 1.00 16.88  ? 43  LEU C N   1 
ATOM   4610 C  CA  . LEU C  1 43  ? 43.396  -10.166 -48.158 1.00 17.49  ? 43  LEU C CA  1 
ATOM   4611 C  C   . LEU C  1 43  ? 44.294  -11.219 -47.504 1.00 19.14  ? 43  LEU C C   1 
ATOM   4612 O  O   . LEU C  1 43  ? 43.808  -12.220 -46.931 1.00 20.40  ? 43  LEU C O   1 
ATOM   4613 C  CB  . LEU C  1 43  ? 41.971  -10.189 -47.611 1.00 16.92  ? 43  LEU C CB  1 
ATOM   4614 C  CG  . LEU C  1 43  ? 41.162  -8.993  -48.151 1.00 14.77  ? 43  LEU C CG  1 
ATOM   4615 C  CD1 . LEU C  1 43  ? 39.754  -9.105  -47.524 1.00 15.46  ? 43  LEU C CD1 1 
ATOM   4616 C  CD2 . LEU C  1 43  ? 41.820  -7.687  -47.945 1.00 17.87  ? 43  LEU C CD2 1 
ATOM   4617 N  N   . THR C  1 44  ? 45.574  -11.104 -47.733 1.00 19.00  ? 44  THR C N   1 
ATOM   4618 C  CA  . THR C  1 44  ? 46.593  -12.008 -47.153 1.00 20.56  ? 44  THR C CA  1 
ATOM   4619 C  C   . THR C  1 44  ? 46.824  -11.755 -45.644 1.00 21.43  ? 44  THR C C   1 
ATOM   4620 O  O   . THR C  1 44  ? 46.375  -10.714 -45.100 1.00 20.80  ? 44  THR C O   1 
ATOM   4621 C  CB  . THR C  1 44  ? 47.897  -11.908 -47.982 1.00 22.83  ? 44  THR C CB  1 
ATOM   4622 O  OG1 . THR C  1 44  ? 48.171  -10.509 -48.105 1.00 26.25  ? 44  THR C OG1 1 
ATOM   4623 C  CG2 . THR C  1 44  ? 47.651  -12.541 -49.343 1.00 27.48  ? 44  THR C CG2 1 
ATOM   4624 N  N   . PRO C  1 45  ? 47.538  -12.615 -44.961 1.00 20.67  ? 45  PRO C N   1 
ATOM   4625 C  CA  . PRO C  1 45  ? 47.825  -12.405 -43.542 1.00 20.34  ? 45  PRO C CA  1 
ATOM   4626 C  C   . PRO C  1 45  ? 48.648  -11.118 -43.242 1.00 23.85  ? 45  PRO C C   1 
ATOM   4627 O  O   . PRO C  1 45  ? 49.678  -10.953 -43.878 1.00 29.18  ? 45  PRO C O   1 
ATOM   4628 C  CB  . PRO C  1 45  ? 48.542  -13.689 -43.123 1.00 24.68  ? 45  PRO C CB  1 
ATOM   4629 C  CG  . PRO C  1 45  ? 48.005  -14.744 -44.122 1.00 26.79  ? 45  PRO C CG  1 
ATOM   4630 C  CD  . PRO C  1 45  ? 47.933  -13.951 -45.442 1.00 24.99  ? 45  PRO C CD  1 
ATOM   4631 N  N   . LEU C  1 46  ? 48.278  -10.297 -42.254 1.00 19.86  ? 46  LEU C N   1 
ATOM   4632 C  CA  . LEU C  1 46  ? 49.004  -9.178  -41.788 1.00 20.92  ? 46  LEU C CA  1 
ATOM   4633 C  C   . LEU C  1 46  ? 50.111  -9.737  -40.902 1.00 25.45  ? 46  LEU C C   1 
ATOM   4634 O  O   . LEU C  1 46  ? 49.956  -10.791 -40.287 1.00 26.12  ? 46  LEU C O   1 
ATOM   4635 C  CB  . LEU C  1 46  ? 47.956  -8.398  -40.969 1.00 21.77  ? 46  LEU C CB  1 
ATOM   4636 C  CG  . LEU C  1 46  ? 46.877  -7.698  -41.804 1.00 24.16  ? 46  LEU C CG  1 
ATOM   4637 C  CD1 . LEU C  1 46  ? 45.989  -6.837  -40.862 1.00 23.24  ? 46  LEU C CD1 1 
ATOM   4638 C  CD2 . LEU C  1 46  ? 47.503  -6.867  -42.990 1.00 27.44  ? 46  LEU C CD2 1 
ATOM   4639 N  N   . GLU C  1 47  ? 51.167  -8.949  -40.785 1.00 24.91  ? 47  GLU C N   1 
ATOM   4640 C  CA  . GLU C  1 47  ? 52.205  -9.273  -39.764 1.00 23.69  ? 47  GLU C CA  1 
ATOM   4641 C  C   . GLU C  1 47  ? 52.239  -8.094  -38.760 1.00 23.95  ? 47  GLU C C   1 
ATOM   4642 O  O   . GLU C  1 47  ? 52.156  -6.887  -39.137 1.00 24.28  ? 47  GLU C O   1 
ATOM   4643 C  CB  . GLU C  1 47  ? 53.543  -9.402  -40.505 1.00 32.41  ? 47  GLU C CB  1 
ATOM   4644 C  CG  . GLU C  1 47  ? 53.544  -10.647 -41.368 1.00 40.21  ? 47  GLU C CG  1 
ATOM   4645 N  N   . PHE C  1 48  ? 52.463  -8.424  -37.477 1.00 19.75  ? 48  PHE C N   1 
ATOM   4646 C  CA  . PHE C  1 48  ? 52.439  -7.457  -36.457 1.00 22.23  ? 48  PHE C CA  1 
ATOM   4647 C  C   . PHE C  1 48  ? 53.844  -7.329  -36.015 1.00 21.22  ? 48  PHE C C   1 
ATOM   4648 O  O   . PHE C  1 48  ? 54.352  -8.181  -35.324 1.00 29.27  ? 48  PHE C O   1 
ATOM   4649 C  CB  . PHE C  1 48  ? 51.451  -7.963  -35.353 1.00 21.84  ? 48  PHE C CB  1 
ATOM   4650 C  CG  . PHE C  1 48  ? 50.090  -8.354  -35.969 1.00 21.27  ? 48  PHE C CG  1 
ATOM   4651 C  CD1 . PHE C  1 48  ? 49.263  -7.390  -36.522 1.00 22.81  ? 48  PHE C CD1 1 
ATOM   4652 C  CD2 . PHE C  1 48  ? 49.768  -9.745  -36.102 1.00 19.96  ? 48  PHE C CD2 1 
ATOM   4653 C  CE1 . PHE C  1 48  ? 48.045  -7.801  -37.139 1.00 21.54  ? 48  PHE C CE1 1 
ATOM   4654 C  CE2 . PHE C  1 48  ? 48.609  -10.149 -36.666 1.00 22.86  ? 48  PHE C CE2 1 
ATOM   4655 C  CZ  . PHE C  1 48  ? 47.738  -9.139  -37.220 1.00 20.15  ? 48  PHE C CZ  1 
ATOM   4656 N  N   . GLN C  1 49  ? 54.420  -6.138  -36.232 1.00 20.23  ? 49  GLN C N   1 
ATOM   4657 C  CA  . GLN C  1 49  ? 55.916  -5.978  -35.912 1.00 26.05  ? 49  GLN C CA  1 
ATOM   4658 C  C   . GLN C  1 49  ? 56.104  -5.028  -34.795 1.00 26.67  ? 49  GLN C C   1 
ATOM   4659 O  O   . GLN C  1 49  ? 55.415  -3.998  -34.678 1.00 23.40  ? 49  GLN C O   1 
ATOM   4660 C  CB  . GLN C  1 49  ? 56.604  -5.418  -37.221 1.00 30.25  ? 49  GLN C CB  1 
ATOM   4661 C  CG  . GLN C  1 49  ? 56.382  -6.419  -38.328 1.00 31.27  ? 49  GLN C CG  1 
ATOM   4662 C  CD  . GLN C  1 49  ? 57.372  -6.418  -39.482 1.00 52.79  ? 49  GLN C CD  1 
ATOM   4663 O  OE1 . GLN C  1 49  ? 57.852  -5.350  -39.900 1.00 74.59  ? 49  GLN C OE1 1 
ATOM   4664 N  NE2 . GLN C  1 49  ? 57.645  -7.615  -40.072 1.00 55.30  ? 49  GLN C NE2 1 
ATOM   4665 N  N   . GLY C  1 50  ? 57.075  -5.385  -33.921 1.00 24.10  ? 50  GLY C N   1 
ATOM   4666 C  CA  . GLY C  1 50  ? 57.317  -4.433  -32.839 1.00 23.92  ? 50  GLY C CA  1 
ATOM   4667 C  C   . GLY C  1 50  ? 56.281  -4.506  -31.726 1.00 19.60  ? 50  GLY C C   1 
ATOM   4668 O  O   . GLY C  1 50  ? 56.135  -3.527  -30.985 1.00 27.07  ? 50  GLY C O   1 
ATOM   4669 N  N   . TYR C  1 51  ? 55.397  -5.505  -31.747 1.00 22.85  ? 51  TYR C N   1 
ATOM   4670 C  CA  . TYR C  1 51  ? 54.245  -5.506  -30.793 1.00 20.38  ? 51  TYR C CA  1 
ATOM   4671 C  C   . TYR C  1 51  ? 54.684  -6.042  -29.420 1.00 25.05  ? 51  TYR C C   1 
ATOM   4672 O  O   . TYR C  1 51  ? 54.012  -5.829  -28.388 1.00 21.33  ? 51  TYR C O   1 
ATOM   4673 C  CB  . TYR C  1 51  ? 53.093  -6.419  -31.274 1.00 21.18  ? 51  TYR C CB  1 
ATOM   4674 C  CG  . TYR C  1 51  ? 52.084  -5.748  -32.221 1.00 20.55  ? 51  TYR C CG  1 
ATOM   4675 C  CD1 . TYR C  1 51  ? 52.466  -4.909  -33.274 1.00 17.62  ? 51  TYR C CD1 1 
ATOM   4676 C  CD2 . TYR C  1 51  ? 50.716  -5.978  -32.000 1.00 17.09  ? 51  TYR C CD2 1 
ATOM   4677 C  CE1 . TYR C  1 51  ? 51.494  -4.314  -34.078 1.00 19.84  ? 51  TYR C CE1 1 
ATOM   4678 C  CE2 . TYR C  1 51  ? 49.746  -5.450  -32.828 1.00 20.11  ? 51  TYR C CE2 1 
ATOM   4679 C  CZ  . TYR C  1 51  ? 50.122  -4.592  -33.819 1.00 17.94  ? 51  TYR C CZ  1 
ATOM   4680 O  OH  . TYR C  1 51  ? 49.157  -4.056  -34.589 1.00 19.28  ? 51  TYR C OH  1 
ATOM   4681 N  N   . ASN C  1 52  ? 55.896  -6.544  -29.322 1.00 25.13  ? 52  ASN C N   1 
ATOM   4682 C  CA  . ASN C  1 52  ? 56.388  -7.122  -28.068 1.00 26.99  ? 52  ASN C CA  1 
ATOM   4683 C  C   . ASN C  1 52  ? 57.098  -6.045  -27.328 1.00 27.88  ? 52  ASN C C   1 
ATOM   4684 O  O   . ASN C  1 52  ? 58.336  -5.874  -27.515 1.00 33.64  ? 52  ASN C O   1 
ATOM   4685 C  CB  . ASN C  1 52  ? 57.219  -8.372  -28.347 1.00 34.43  ? 52  ASN C CB  1 
ATOM   4686 C  CG  . ASN C  1 52  ? 57.557  -9.080  -27.104 1.00 40.90  ? 52  ASN C CG  1 
ATOM   4687 O  OD1 . ASN C  1 52  ? 56.870  -8.929  -26.090 1.00 48.86  ? 52  ASN C OD1 1 
ATOM   4688 N  ND2 . ASN C  1 52  ? 58.683  -9.812  -27.128 1.00 40.42  ? 52  ASN C ND2 1 
ATOM   4689 N  N   . LEU C  1 53  ? 56.321  -5.299  -26.528 1.00 26.42  ? 53  LEU C N   1 
ATOM   4690 C  CA  . LEU C  1 53  ? 56.860  -4.151  -25.826 1.00 25.94  ? 53  LEU C CA  1 
ATOM   4691 C  C   . LEU C  1 53  ? 57.623  -4.595  -24.567 1.00 31.30  ? 53  LEU C C   1 
ATOM   4692 O  O   . LEU C  1 53  ? 57.184  -5.516  -23.818 1.00 37.18  ? 53  LEU C O   1 
ATOM   4693 C  CB  . LEU C  1 53  ? 55.774  -3.134  -25.483 1.00 23.74  ? 53  LEU C CB  1 
ATOM   4694 C  CG  . LEU C  1 53  ? 54.716  -2.726  -26.619 1.00 21.92  ? 53  LEU C CG  1 
ATOM   4695 C  CD1 . LEU C  1 53  ? 53.701  -1.826  -25.987 1.00 23.34  ? 53  LEU C CD1 1 
ATOM   4696 C  CD2 . LEU C  1 53  ? 55.367  -2.080  -27.866 1.00 32.05  ? 53  LEU C CD2 1 
ATOM   4697 N  N   . SER C  1 54  ? 58.801  -4.005  -24.320 1.00 42.62  ? 54  SER C N   1 
ATOM   4698 C  CA  . SER C  1 54  ? 59.650  -4.496  -23.120 1.00 34.66  ? 54  SER C CA  1 
ATOM   4699 C  C   . SER C  1 54  ? 58.952  -4.178  -21.792 1.00 48.06  ? 54  SER C C   1 
ATOM   4700 O  O   . SER C  1 54  ? 58.360  -3.104  -21.659 1.00 52.32  ? 54  SER C O   1 
ATOM   4701 C  CB  . SER C  1 54  ? 61.119  -4.019  -23.101 1.00 52.98  ? 54  SER C CB  1 
ATOM   4702 O  OG  . SER C  1 54  ? 61.462  -3.329  -24.280 1.00 75.39  ? 54  SER C OG  1 
ATOM   4703 N  N   . ALA C  1 55  ? 59.088  -5.048  -20.783 1.00 36.33  ? 55  ALA C N   1 
ATOM   4704 C  CA  . ALA C  1 55  ? 58.514  -4.856  -19.435 1.00 55.96  ? 55  ALA C CA  1 
ATOM   4705 C  C   . ALA C  1 55  ? 59.304  -3.718  -18.730 1.00 60.86  ? 55  ALA C C   1 
ATOM   4706 O  O   . ALA C  1 55  ? 58.885  -3.193  -17.676 1.00 73.00  ? 55  ALA C O   1 
ATOM   4707 C  CB  . ALA C  1 55  ? 58.516  -6.209  -18.716 1.00 67.15  ? 55  ALA C CB  1 
ATOM   4708 N  N   . ASN C  1 56  ? 60.330  -3.240  -19.453 1.00 41.60  ? 56  ASN C N   1 
ATOM   4709 C  CA  . ASN C  1 56  ? 61.339  -2.195  -19.079 1.00 52.75  ? 56  ASN C CA  1 
ATOM   4710 C  C   . ASN C  1 56  ? 60.796  -0.829  -19.426 1.00 55.34  ? 56  ASN C C   1 
ATOM   4711 O  O   . ASN C  1 56  ? 61.131  0.154   -18.660 1.00 67.41  ? 56  ASN C O   1 
ATOM   4712 C  CB  . ASN C  1 56  ? 62.579  -2.299  -19.951 1.00 62.34  ? 56  ASN C CB  1 
ATOM   4713 C  CG  . ASN C  1 56  ? 63.620  -3.234  -19.406 1.00 68.02  ? 56  ASN C CG  1 
ATOM   4714 O  OD1 . ASN C  1 56  ? 63.880  -3.261  -18.190 1.00 46.05  ? 56  ASN C OD1 1 
ATOM   4715 N  ND2 . ASN C  1 56  ? 64.267  -3.984  -20.308 1.00 53.94  ? 56  ASN C ND2 1 
ATOM   4716 N  N   . LYS C  1 57  ? 60.029  -0.731  -20.539 1.00 58.53  ? 57  LYS C N   1 
ATOM   4717 C  CA  . LYS C  1 57  ? 59.461  0.498   -20.997 1.00 45.76  ? 57  LYS C CA  1 
ATOM   4718 C  C   . LYS C  1 57  ? 58.046  0.516   -20.306 1.00 26.89  ? 57  LYS C C   1 
ATOM   4719 O  O   . LYS C  1 57  ? 57.446  -0.539  -19.838 1.00 34.08  ? 57  LYS C O   1 
ATOM   4720 C  CB  . LYS C  1 57  ? 59.501  0.453   -22.576 1.00 42.78  ? 57  LYS C CB  1 
ATOM   4721 C  CG  . LYS C  1 57  ? 60.856  0.840   -23.180 1.00 52.07  ? 57  LYS C CG  1 
ATOM   4722 N  N   . GLN C  1 58  ? 57.486  1.716   -20.118 1.00 29.16  ? 58  GLN C N   1 
ATOM   4723 C  CA  . GLN C  1 58  ? 56.086  1.935   -19.802 1.00 28.60  ? 58  GLN C CA  1 
ATOM   4724 C  C   . GLN C  1 58  ? 55.326  2.878   -20.732 1.00 23.22  ? 58  GLN C C   1 
ATOM   4725 O  O   . GLN C  1 58  ? 55.954  3.627   -21.518 1.00 26.47  ? 58  GLN C O   1 
ATOM   4726 C  CB  . GLN C  1 58  ? 56.071  2.439   -18.350 1.00 27.84  ? 58  GLN C CB  1 
ATOM   4727 C  CG  . GLN C  1 58  ? 56.482  3.911   -18.171 1.00 32.66  ? 58  GLN C CG  1 
ATOM   4728 C  CD  . GLN C  1 58  ? 56.526  4.328   -16.675 1.00 28.13  ? 58  GLN C CD  1 
ATOM   4729 O  OE1 . GLN C  1 58  ? 56.174  3.544   -15.753 1.00 31.93  ? 58  GLN C OE1 1 
ATOM   4730 N  NE2 . GLN C  1 58  ? 56.691  5.616   -16.449 1.00 28.89  ? 58  GLN C NE2 1 
ATOM   4731 N  N   . PHE C  1 59  ? 53.990  2.707   -20.649 1.00 22.77  ? 59  PHE C N   1 
ATOM   4732 C  CA  . PHE C  1 59  ? 53.041  3.254   -21.628 1.00 23.25  ? 59  PHE C CA  1 
ATOM   4733 C  C   . PHE C  1 59  ? 51.909  3.986   -20.957 1.00 22.40  ? 59  PHE C C   1 
ATOM   4734 O  O   . PHE C  1 59  ? 51.368  3.534   -19.943 1.00 22.11  ? 59  PHE C O   1 
ATOM   4735 C  CB  . PHE C  1 59  ? 52.652  2.169   -22.631 1.00 21.49  ? 59  PHE C CB  1 
ATOM   4736 C  CG  . PHE C  1 59  ? 53.843  1.576   -23.357 1.00 24.16  ? 59  PHE C CG  1 
ATOM   4737 C  CD1 . PHE C  1 59  ? 54.384  2.245   -24.487 1.00 23.50  ? 59  PHE C CD1 1 
ATOM   4738 C  CD2 . PHE C  1 59  ? 54.573  0.462   -22.821 1.00 25.11  ? 59  PHE C CD2 1 
ATOM   4739 C  CE1 . PHE C  1 59  ? 55.558  1.783   -25.112 1.00 26.75  ? 59  PHE C CE1 1 
ATOM   4740 C  CE2 . PHE C  1 59  ? 55.774  0.038   -23.377 1.00 27.86  ? 59  PHE C CE2 1 
ATOM   4741 C  CZ  . PHE C  1 59  ? 56.278  0.699   -24.559 1.00 29.73  ? 59  PHE C CZ  1 
ATOM   4742 N  N   . LEU C  1 60  ? 51.594  5.200   -21.344 1.00 21.63  ? 60  LEU C N   1 
ATOM   4743 C  CA  . LEU C  1 60  ? 50.645  6.054   -20.611 1.00 20.24  ? 60  LEU C CA  1 
ATOM   4744 C  C   . LEU C  1 60  ? 49.222  5.561   -20.870 1.00 18.83  ? 60  LEU C C   1 
ATOM   4745 O  O   . LEU C  1 60  ? 48.810  5.412   -22.029 1.00 20.02  ? 60  LEU C O   1 
ATOM   4746 C  CB  . LEU C  1 60  ? 50.747  7.469   -21.177 1.00 19.29  ? 60  LEU C CB  1 
ATOM   4747 C  CG  . LEU C  1 60  ? 50.049  8.634   -20.508 1.00 24.66  ? 60  LEU C CG  1 
ATOM   4748 C  CD1 . LEU C  1 60  ? 50.610  8.740   -19.049 1.00 27.58  ? 60  LEU C CD1 1 
ATOM   4749 C  CD2 . LEU C  1 60  ? 50.095  9.906   -21.277 1.00 27.79  ? 60  LEU C CD2 1 
ATOM   4750 N  N   . LEU C  1 61  ? 48.510  5.252   -19.780 1.00 21.49  ? 61  LEU C N   1 
ATOM   4751 C  CA  . LEU C  1 61  ? 47.097  4.899   -19.737 1.00 19.90  ? 61  LEU C CA  1 
ATOM   4752 C  C   . LEU C  1 61  ? 46.352  6.221   -19.295 1.00 18.55  ? 61  LEU C C   1 
ATOM   4753 O  O   . LEU C  1 61  ? 46.661  6.744   -18.277 1.00 22.31  ? 61  LEU C O   1 
ATOM   4754 C  CB  . LEU C  1 61  ? 46.900  3.764   -18.775 1.00 25.61  ? 61  LEU C CB  1 
ATOM   4755 C  CG  . LEU C  1 61  ? 45.548  3.151   -18.779 1.00 23.38  ? 61  LEU C CG  1 
ATOM   4756 C  CD1 . LEU C  1 61  ? 45.338  2.248   -20.037 1.00 24.58  ? 61  LEU C CD1 1 
ATOM   4757 C  CD2 . LEU C  1 61  ? 45.468  2.326   -17.460 1.00 29.75  ? 61  LEU C CD2 1 
ATOM   4758 N  N   . THR C  1 62  ? 45.222  6.533   -19.975 1.00 18.18  ? 62  THR C N   1 
ATOM   4759 C  CA  . THR C  1 62  ? 44.485  7.800   -19.767 1.00 19.27  ? 62  THR C CA  1 
ATOM   4760 C  C   . THR C  1 62  ? 43.010  7.413   -19.792 1.00 23.67  ? 62  THR C C   1 
ATOM   4761 O  O   . THR C  1 62  ? 42.535  6.722   -20.718 1.00 22.48  ? 62  THR C O   1 
ATOM   4762 C  CB  . THR C  1 62  ? 44.776  8.785   -20.884 1.00 22.57  ? 62  THR C CB  1 
ATOM   4763 O  OG1 . THR C  1 62  ? 46.178  9.088   -20.972 1.00 25.93  ? 62  THR C OG1 1 
ATOM   4764 C  CG2 . THR C  1 62  ? 44.043  10.129  -20.659 1.00 30.01  ? 62  THR C CG2 1 
ATOM   4765 N  N   . ASN C  1 63  ? 42.273  7.994   -18.860 1.00 20.50  ? 63  ASN C N   1 
ATOM   4766 C  CA  . ASN C  1 63  ? 40.870  8.137   -18.953 1.00 17.49  ? 63  ASN C CA  1 
ATOM   4767 C  C   . ASN C  1 63  ? 40.599  9.485   -19.552 1.00 20.26  ? 63  ASN C C   1 
ATOM   4768 O  O   . ASN C  1 63  ? 40.828  10.516  -18.917 1.00 21.36  ? 63  ASN C O   1 
ATOM   4769 C  CB  . ASN C  1 63  ? 40.255  7.903   -17.530 1.00 21.35  ? 63  ASN C CB  1 
ATOM   4770 C  CG  . ASN C  1 63  ? 38.780  8.155   -17.540 1.00 21.12  ? 63  ASN C CG  1 
ATOM   4771 O  OD1 . ASN C  1 63  ? 38.195  8.839   -18.345 1.00 21.01  ? 63  ASN C OD1 1 
ATOM   4772 N  ND2 . ASN C  1 63  ? 38.137  7.717   -16.409 1.00 19.45  ? 63  ASN C ND2 1 
ATOM   4773 N  N   . ASN C  1 64  ? 40.157  9.464   -20.860 1.00 18.78  ? 64  ASN C N   1 
ATOM   4774 C  CA  . ASN C  1 64  ? 39.897  10.656  -21.538 1.00 23.24  ? 64  ASN C CA  1 
ATOM   4775 C  C   . ASN C  1 64  ? 38.462  11.001  -21.471 1.00 19.55  ? 64  ASN C C   1 
ATOM   4776 O  O   . ASN C  1 64  ? 38.055  11.963  -22.154 1.00 22.68  ? 64  ASN C O   1 
ATOM   4777 C  CB  . ASN C  1 64  ? 40.408  10.550  -22.990 1.00 24.49  ? 64  ASN C CB  1 
ATOM   4778 C  CG  . ASN C  1 64  ? 39.746  9.445   -23.751 1.00 22.78  ? 64  ASN C CG  1 
ATOM   4779 O  OD1 . ASN C  1 64  ? 38.719  8.879   -23.319 1.00 24.00  ? 64  ASN C OD1 1 
ATOM   4780 N  ND2 . ASN C  1 64  ? 40.372  9.046   -24.894 1.00 26.82  ? 64  ASN C ND2 1 
ATOM   4781 N  N   . GLY C  1 65  ? 37.671  10.381  -20.515 1.00 22.95  ? 65  GLY C N   1 
ATOM   4782 C  CA  . GLY C  1 65  ? 36.219  10.717  -20.426 1.00 25.37  ? 65  GLY C CA  1 
ATOM   4783 C  C   . GLY C  1 65  ? 35.418  9.930   -21.430 1.00 20.90  ? 65  GLY C C   1 
ATOM   4784 O  O   . GLY C  1 65  ? 34.246  10.108  -21.397 1.00 27.62  ? 65  GLY C O   1 
ATOM   4785 N  N   . HIS C  1 66  ? 36.083  9.267   -22.391 1.00 22.16  ? 66  HIS C N   1 
ATOM   4786 C  CA  . HIS C  1 66  ? 35.316  8.603   -23.450 1.00 22.50  ? 66  HIS C CA  1 
ATOM   4787 C  C   . HIS C  1 66  ? 35.570  7.133   -23.424 1.00 17.36  ? 66  HIS C C   1 
ATOM   4788 O  O   . HIS C  1 66  ? 34.842  6.341   -24.026 1.00 23.25  ? 66  HIS C O   1 
ATOM   4789 C  CB  . HIS C  1 66  ? 35.687  9.200   -24.813 1.00 20.88  ? 66  HIS C CB  1 
ATOM   4790 C  CG  . HIS C  1 66  ? 35.386  10.656  -24.910 1.00 23.05  ? 66  HIS C CG  1 
ATOM   4791 N  ND1 . HIS C  1 66  ? 36.353  11.634  -25.079 1.00 24.58  ? 66  HIS C ND1 1 
ATOM   4792 C  CD2 . HIS C  1 66  ? 34.190  11.298  -24.763 1.00 23.28  ? 66  HIS C CD2 1 
ATOM   4793 C  CE1 . HIS C  1 66  ? 35.758  12.815  -25.081 1.00 25.32  ? 66  HIS C CE1 1 
ATOM   4794 N  NE2 . HIS C  1 66  ? 34.448  12.639  -24.877 1.00 29.17  ? 66  HIS C NE2 1 
ATOM   4795 N  N   . SER C  1 67  ? 36.795  6.776   -23.054 1.00 22.34  ? 67  SER C N   1 
ATOM   4796 C  CA  . SER C  1 67  ? 37.247  5.449   -23.012 1.00 16.98  ? 67  SER C CA  1 
ATOM   4797 C  C   . SER C  1 67  ? 38.454  5.422   -22.100 1.00 21.58  ? 67  SER C C   1 
ATOM   4798 O  O   . SER C  1 67  ? 38.776  6.473   -21.426 1.00 21.07  ? 67  SER C O   1 
ATOM   4799 C  CB  . SER C  1 67  ? 37.642  4.967   -24.424 1.00 22.18  ? 67  SER C CB  1 
ATOM   4800 O  OG  . SER C  1 67  ? 38.078  3.593   -24.454 1.00 19.58  ? 67  SER C OG  1 
ATOM   4801 N  N   . VAL C  1 68  ? 39.061  4.243   -22.013 1.00 17.75  ? 68  VAL C N   1 
ATOM   4802 C  CA  . VAL C  1 68  ? 40.430  4.180   -21.460 1.00 18.62  ? 68  VAL C CA  1 
ATOM   4803 C  C   . VAL C  1 68  ? 41.380  3.834   -22.615 1.00 20.77  ? 68  VAL C C   1 
ATOM   4804 O  O   . VAL C  1 68  ? 41.088  2.925   -23.373 1.00 18.87  ? 68  VAL C O   1 
ATOM   4805 C  CB  . VAL C  1 68  ? 40.476  3.199   -20.284 1.00 20.54  ? 68  VAL C CB  1 
ATOM   4806 C  CG1 . VAL C  1 68  ? 40.207  1.711   -20.641 1.00 20.19  ? 68  VAL C CG1 1 
ATOM   4807 C  CG2 . VAL C  1 68  ? 41.840  3.152   -19.652 1.00 24.89  ? 68  VAL C CG2 1 
ATOM   4808 N  N   . LYS C  1 69  ? 42.438  4.604   -22.723 1.00 19.63  ? 69  LYS C N   1 
ATOM   4809 C  CA  . LYS C  1 69  ? 43.412  4.609   -23.937 1.00 16.38  ? 69  LYS C CA  1 
ATOM   4810 C  C   . LYS C  1 69  ? 44.761  4.351   -23.358 1.00 18.34  ? 69  LYS C C   1 
ATOM   4811 O  O   . LYS C  1 69  ? 45.151  4.812   -22.304 1.00 22.16  ? 69  LYS C O   1 
ATOM   4812 C  CB  . LYS C  1 69  ? 43.380  6.012   -24.610 1.00 29.74  ? 69  LYS C CB  1 
ATOM   4813 C  CG  . LYS C  1 69  ? 44.496  6.384   -25.565 1.00 30.69  ? 69  LYS C CG  1 
ATOM   4814 C  CD  . LYS C  1 69  ? 44.187  7.749   -26.121 1.00 32.47  ? 69  LYS C CD  1 
ATOM   4815 C  CE  . LYS C  1 69  ? 44.491  8.930   -25.238 1.00 33.66  ? 69  LYS C CE  1 
ATOM   4816 N  NZ  . LYS C  1 69  ? 44.530  10.096  -26.209 1.00 35.46  ? 69  LYS C NZ  1 
ATOM   4817 N  N   . LEU C  1 70  ? 45.476  3.403   -24.028 1.00 17.40  ? 70  LEU C N   1 
ATOM   4818 C  CA  . LEU C  1 70  ? 46.879  3.244   -23.864 1.00 16.91  ? 70  LEU C CA  1 
ATOM   4819 C  C   . LEU C  1 70  ? 47.720  3.716   -25.016 1.00 16.27  ? 70  LEU C C   1 
ATOM   4820 O  O   . LEU C  1 70  ? 47.487  3.318   -26.157 1.00 17.04  ? 70  LEU C O   1 
ATOM   4821 C  CB  . LEU C  1 70  ? 47.155  1.726   -23.704 1.00 16.29  ? 70  LEU C CB  1 
ATOM   4822 C  CG  . LEU C  1 70  ? 48.591  1.278   -23.363 1.00 19.40  ? 70  LEU C CG  1 
ATOM   4823 C  CD1 . LEU C  1 70  ? 48.998  1.742   -21.917 1.00 23.48  ? 70  LEU C CD1 1 
ATOM   4824 C  CD2 . LEU C  1 70  ? 48.737  -0.261  -23.518 1.00 19.99  ? 70  LEU C CD2 1 
ATOM   4825 N  N   . ASN C  1 71  ? 48.628  4.669   -24.802 1.00 17.37  ? 71  ASN C N   1 
ATOM   4826 C  CA  . ASN C  1 71  ? 49.507  5.110   -25.884 1.00 19.92  ? 71  ASN C CA  1 
ATOM   4827 C  C   . ASN C  1 71  ? 50.424  3.968   -26.274 1.00 17.99  ? 71  ASN C C   1 
ATOM   4828 O  O   . ASN C  1 71  ? 50.948  3.197   -25.454 1.00 23.55  ? 71  ASN C O   1 
ATOM   4829 C  CB  . ASN C  1 71  ? 50.255  6.297   -25.337 1.00 20.17  ? 71  ASN C CB  1 
ATOM   4830 C  CG  . ASN C  1 71  ? 49.362  7.578   -25.246 1.00 27.44  ? 71  ASN C CG  1 
ATOM   4831 O  OD1 . ASN C  1 71  ? 48.123  7.544   -25.618 1.00 25.20  ? 71  ASN C OD1 1 
ATOM   4832 N  ND2 . ASN C  1 71  ? 49.973  8.690   -24.816 1.00 27.90  ? 71  ASN C ND2 1 
ATOM   4833 N  N   . LEU C  1 72  ? 50.738  3.895   -27.570 1.00 18.52  ? 72  LEU C N   1 
ATOM   4834 C  CA  . LEU C  1 72  ? 51.640  2.873   -28.102 1.00 18.66  ? 72  LEU C CA  1 
ATOM   4835 C  C   . LEU C  1 72  ? 52.730  3.505   -29.026 1.00 19.40  ? 72  LEU C C   1 
ATOM   4836 O  O   . LEU C  1 72  ? 52.522  4.658   -29.438 1.00 20.73  ? 72  LEU C O   1 
ATOM   4837 C  CB  . LEU C  1 72  ? 50.870  2.001   -29.103 1.00 17.80  ? 72  LEU C CB  1 
ATOM   4838 C  CG  . LEU C  1 72  ? 49.764  1.179   -28.409 1.00 17.66  ? 72  LEU C CG  1 
ATOM   4839 C  CD1 . LEU C  1 72  ? 48.812  0.509   -29.416 1.00 19.71  ? 72  LEU C CD1 1 
ATOM   4840 C  CD2 . LEU C  1 72  ? 50.291  0.134   -27.377 1.00 19.80  ? 72  LEU C CD2 1 
ATOM   4841 N  N   . PRO C  1 73  ? 53.947  2.965   -29.067 1.00 21.52  ? 73  PRO C N   1 
ATOM   4842 C  CA  . PRO C  1 73  ? 55.134  3.584   -29.702 1.00 23.31  ? 73  PRO C CA  1 
ATOM   4843 C  C   . PRO C  1 73  ? 55.111  3.395   -31.217 1.00 24.52  ? 73  PRO C C   1 
ATOM   4844 O  O   . PRO C  1 73  ? 54.606  2.339   -31.698 1.00 24.77  ? 73  PRO C O   1 
ATOM   4845 C  CB  . PRO C  1 73  ? 56.293  2.796   -29.068 1.00 23.98  ? 73  PRO C CB  1 
ATOM   4846 C  CG  . PRO C  1 73  ? 55.799  1.334   -28.974 1.00 21.47  ? 73  PRO C CG  1 
ATOM   4847 C  CD  . PRO C  1 73  ? 54.272  1.519   -28.692 1.00 21.81  ? 73  PRO C CD  1 
ATOM   4848 N  N   . SER C  1 74  ? 55.688  4.346   -31.994 1.00 25.68  ? 74  SER C N   1 
ATOM   4849 C  CA  . SER C  1 74  ? 55.523  4.400   -33.460 1.00 28.30  ? 74  SER C CA  1 
ATOM   4850 C  C   . SER C  1 74  ? 56.372  3.356   -34.151 1.00 35.30  ? 74  SER C C   1 
ATOM   4851 O  O   . SER C  1 74  ? 56.180  2.983   -35.308 1.00 29.55  ? 74  SER C O   1 
ATOM   4852 C  CB  . SER C  1 74  ? 55.762  5.811   -33.936 1.00 39.84  ? 74  SER C CB  1 
ATOM   4853 O  OG  . SER C  1 74  ? 57.134  6.164   -33.642 1.00 39.95  ? 74  SER C OG  1 
ATOM   4854 N  N   . ASP C  1 75  ? 57.287  2.775   -33.424 1.00 30.54  ? 75  ASP C N   1 
ATOM   4855 C  CA  . ASP C  1 75  ? 58.061  1.693   -34.038 1.00 30.65  ? 75  ASP C CA  1 
ATOM   4856 C  C   . ASP C  1 75  ? 57.201  0.332   -34.067 1.00 29.40  ? 75  ASP C C   1 
ATOM   4857 O  O   . ASP C  1 75  ? 57.551  -0.732  -34.673 1.00 32.51  ? 75  ASP C O   1 
ATOM   4858 C  CB  . ASP C  1 75  ? 59.367  1.548   -33.444 1.00 30.02  ? 75  ASP C CB  1 
ATOM   4859 C  CG  . ASP C  1 75  ? 59.245  1.151   -32.019 1.00 29.02  ? 75  ASP C CG  1 
ATOM   4860 O  OD1 . ASP C  1 75  ? 58.873  1.978   -31.173 1.00 34.99  ? 75  ASP C OD1 1 
ATOM   4861 O  OD2 . ASP C  1 75  ? 59.397  -0.066  -31.814 1.00 38.50  ? 75  ASP C OD2 1 
ATOM   4862 N  N   . MET C  1 76  ? 56.029  0.313   -33.458 1.00 23.32  ? 76  MET C N   1 
ATOM   4863 C  CA  . MET C  1 76  ? 55.207  -0.857  -33.574 1.00 19.81  ? 76  MET C CA  1 
ATOM   4864 C  C   . MET C  1 76  ? 54.307  -0.603  -34.834 1.00 20.78  ? 76  MET C C   1 
ATOM   4865 O  O   . MET C  1 76  ? 53.858  0.525   -35.062 1.00 21.02  ? 76  MET C O   1 
ATOM   4866 C  CB  . MET C  1 76  ? 54.310  -0.731  -32.408 1.00 23.94  ? 76  MET C CB  1 
ATOM   4867 C  CG  . MET C  1 76  ? 53.181  -1.643  -32.319 1.00 22.48  ? 76  MET C CG  1 
ATOM   4868 S  SD  . MET C  1 76  ? 52.358  -1.580  -30.644 1.00 23.39  ? 76  MET C SD  1 
ATOM   4869 C  CE  . MET C  1 76  ? 50.799  -2.194  -31.162 1.00 22.76  ? 76  MET C CE  1 
ATOM   4870 N  N   . HIS C  1 77  ? 54.156  -1.601  -35.641 1.00 19.82  ? 77  HIS C N   1 
ATOM   4871 C  CA  . HIS C  1 77  ? 53.572  -1.400  -36.981 1.00 20.93  ? 77  HIS C CA  1 
ATOM   4872 C  C   . HIS C  1 77  ? 52.999  -2.655  -37.582 1.00 19.60  ? 77  HIS C C   1 
ATOM   4873 O  O   . HIS C  1 77  ? 53.276  -3.802  -37.243 1.00 21.60  ? 77  HIS C O   1 
ATOM   4874 C  CB  . HIS C  1 77  ? 54.490  -0.619  -37.909 1.00 26.22  ? 77  HIS C CB  1 
ATOM   4875 C  CG  . HIS C  1 77  ? 55.662  -1.394  -38.363 1.00 24.57  ? 77  HIS C CG  1 
ATOM   4876 N  ND1 . HIS C  1 77  ? 56.836  -1.343  -37.716 1.00 28.58  ? 77  HIS C ND1 1 
ATOM   4877 C  CD2 . HIS C  1 77  ? 55.848  -2.203  -39.427 1.00 25.06  ? 77  HIS C CD2 1 
ATOM   4878 C  CE1 . HIS C  1 77  ? 57.723  -2.091  -38.356 1.00 30.41  ? 77  HIS C CE1 1 
ATOM   4879 N  NE2 . HIS C  1 77  ? 57.148  -2.670  -39.393 1.00 28.33  ? 77  HIS C NE2 1 
ATOM   4880 N  N   . ILE C  1 78  ? 52.044  -2.441  -38.508 1.00 21.08  ? 78  ILE C N   1 
ATOM   4881 C  CA  . ILE C  1 78  ? 51.491  -3.502  -39.306 1.00 20.35  ? 78  ILE C CA  1 
ATOM   4882 C  C   . ILE C  1 78  ? 52.208  -3.562  -40.642 1.00 21.54  ? 78  ILE C C   1 
ATOM   4883 O  O   . ILE C  1 78  ? 52.369  -2.492  -41.236 1.00 23.62  ? 78  ILE C O   1 
ATOM   4884 C  CB  . ILE C  1 78  ? 49.939  -3.255  -39.677 1.00 20.34  ? 78  ILE C CB  1 
ATOM   4885 C  CG1 . ILE C  1 78  ? 49.048  -3.125  -38.416 1.00 22.22  ? 78  ILE C CG1 1 
ATOM   4886 C  CG2 . ILE C  1 78  ? 49.375  -4.257  -40.694 1.00 22.63  ? 78  ILE C CG2 1 
ATOM   4887 C  CD1 . ILE C  1 78  ? 47.722  -2.365  -38.702 1.00 20.92  ? 78  ILE C CD1 1 
ATOM   4888 N  N   . GLN C  1 79  ? 52.508  -4.758  -41.055 1.00 23.36  ? 79  GLN C N   1 
ATOM   4889 C  CA  . GLN C  1 79  ? 53.124  -5.004  -42.339 1.00 29.43  ? 79  GLN C CA  1 
ATOM   4890 C  C   . GLN C  1 79  ? 52.124  -5.880  -43.116 1.00 24.72  ? 79  GLN C C   1 
ATOM   4891 O  O   . GLN C  1 79  ? 51.447  -6.817  -42.627 1.00 28.56  ? 79  GLN C O   1 
ATOM   4892 C  CB  . GLN C  1 79  ? 54.543  -5.692  -42.209 1.00 32.49  ? 79  GLN C CB  1 
ATOM   4893 C  CG  . GLN C  1 79  ? 55.474  -5.389  -43.406 1.00 53.93  ? 79  GLN C CG  1 
ATOM   4894 C  CD  . GLN C  1 79  ? 57.043  -5.332  -43.102 1.00 63.78  ? 79  GLN C CD  1 
ATOM   4895 O  OE1 . GLN C  1 79  ? 57.808  -6.087  -43.706 1.00 70.73  ? 79  GLN C OE1 1 
ATOM   4896 N  NE2 . GLN C  1 79  ? 57.508  -4.408  -42.168 1.00 49.14  ? 79  GLN C NE2 1 
ATOM   4897 N  N   . GLY C  1 80  ? 51.992  -5.536  -44.387 1.00 27.91  ? 80  GLY C N   1 
ATOM   4898 C  CA  . GLY C  1 80  ? 51.150  -6.266  -45.232 1.00 30.73  ? 80  GLY C CA  1 
ATOM   4899 C  C   . GLY C  1 80  ? 50.093  -5.438  -45.918 1.00 26.22  ? 80  GLY C C   1 
ATOM   4900 O  O   . GLY C  1 80  ? 49.441  -6.004  -46.805 1.00 32.51  ? 80  GLY C O   1 
ATOM   4901 N  N   . LEU C  1 81  ? 49.889  -4.168  -45.566 1.00 24.66  ? 81  LEU C N   1 
ATOM   4902 C  CA  . LEU C  1 81  ? 48.913  -3.288  -46.208 1.00 26.04  ? 81  LEU C CA  1 
ATOM   4903 C  C   . LEU C  1 81  ? 49.639  -2.510  -47.317 1.00 28.09  ? 81  LEU C C   1 
ATOM   4904 O  O   . LEU C  1 81  ? 50.827  -2.706  -47.486 1.00 29.80  ? 81  LEU C O   1 
ATOM   4905 C  CB  . LEU C  1 81  ? 48.292  -2.323  -45.203 1.00 23.28  ? 81  LEU C CB  1 
ATOM   4906 C  CG  . LEU C  1 81  ? 47.450  -2.986  -44.073 1.00 23.46  ? 81  LEU C CG  1 
ATOM   4907 C  CD1 . LEU C  1 81  ? 46.985  -2.060  -42.957 1.00 27.92  ? 81  LEU C CD1 1 
ATOM   4908 C  CD2 . LEU C  1 81  ? 46.227  -3.594  -44.783 1.00 23.43  ? 81  LEU C CD2 1 
ATOM   4909 N  N   . GLN C  1 82  ? 48.942  -1.653  -48.020 1.00 27.21  ? 82  GLN C N   1 
ATOM   4910 C  CA  . GLN C  1 82  ? 49.655  -0.980  -49.132 1.00 32.41  ? 82  GLN C CA  1 
ATOM   4911 C  C   . GLN C  1 82  ? 50.678  0.135   -48.695 1.00 28.82  ? 82  GLN C C   1 
ATOM   4912 O  O   . GLN C  1 82  ? 51.468  0.710   -49.477 1.00 33.53  ? 82  GLN C O   1 
ATOM   4913 C  CB  . GLN C  1 82  ? 48.577  -0.364  -50.052 1.00 35.53  ? 82  GLN C CB  1 
ATOM   4914 N  N   . SER C  1 83  ? 50.601  0.512   -47.433 1.00 25.01  ? 83  SER C N   1 
ATOM   4915 C  CA  . SER C  1 83  ? 51.474  1.539   -46.768 1.00 21.11  ? 83  SER C CA  1 
ATOM   4916 C  C   . SER C  1 83  ? 51.832  0.963   -45.410 1.00 19.89  ? 83  SER C C   1 
ATOM   4917 O  O   . SER C  1 83  ? 51.063  0.077   -44.903 1.00 18.33  ? 83  SER C O   1 
ATOM   4918 C  CB  . SER C  1 83  ? 50.747  2.844   -46.457 1.00 24.05  ? 83  SER C CB  1 
ATOM   4919 O  OG  . SER C  1 83  ? 50.476  3.596   -47.563 1.00 28.23  ? 83  SER C OG  1 
ATOM   4920 N  N   . ARG C  1 84  ? 52.889  1.471   -44.801 1.00 18.85  ? 84  ARG C N   1 
ATOM   4921 C  CA  . ARG C  1 84  ? 53.150  1.021   -43.442 1.00 17.94  ? 84  ARG C CA  1 
ATOM   4922 C  C   . ARG C  1 84  ? 52.245  1.875   -42.523 1.00 15.61  ? 84  ARG C C   1 
ATOM   4923 O  O   . ARG C  1 84  ? 52.118  3.073   -42.661 1.00 18.31  ? 84  ARG C O   1 
ATOM   4924 C  CB  . ARG C  1 84  ? 54.601  1.341   -43.061 1.00 22.06  ? 84  ARG C CB  1 
ATOM   4925 C  CG  . ARG C  1 84  ? 54.814  1.043   -41.532 1.00 23.36  ? 84  ARG C CG  1 
ATOM   4926 C  CD  . ARG C  1 84  ? 56.213  1.236   -41.047 1.00 23.36  ? 84  ARG C CD  1 
ATOM   4927 N  NE  . ARG C  1 84  ? 57.057  0.186   -41.580 1.00 21.70  ? 84  ARG C NE  1 
ATOM   4928 C  CZ  . ARG C  1 84  ? 58.337  0.090   -41.288 1.00 21.37  ? 84  ARG C CZ  1 
ATOM   4929 N  NH1 . ARG C  1 84  ? 58.876  1.000   -40.487 1.00 24.72  ? 84  ARG C NH1 1 
ATOM   4930 N  NH2 . ARG C  1 84  ? 59.069  -0.890  -41.801 1.00 23.70  ? 84  ARG C NH2 1 
ATOM   4931 N  N   . TYR C  1 85  ? 51.567  1.140   -41.597 1.00 17.64  ? 85  TYR C N   1 
ATOM   4932 C  CA  . TYR C  1 85  ? 50.739  1.783   -40.557 1.00 17.85  ? 85  TYR C CA  1 
ATOM   4933 C  C   . TYR C  1 85  ? 51.401  1.554   -39.206 1.00 18.96  ? 85  TYR C C   1 
ATOM   4934 O  O   . TYR C  1 85  ? 51.611  0.400   -38.869 1.00 19.24  ? 85  TYR C O   1 
ATOM   4935 C  CB  . TYR C  1 85  ? 49.298  1.221   -40.583 1.00 18.30  ? 85  TYR C CB  1 
ATOM   4936 C  CG  . TYR C  1 85  ? 48.510  1.793   -41.777 1.00 15.31  ? 85  TYR C CG  1 
ATOM   4937 C  CD1 . TYR C  1 85  ? 48.584  1.177   -42.998 1.00 16.55  ? 85  TYR C CD1 1 
ATOM   4938 C  CD2 . TYR C  1 85  ? 47.745  2.965   -41.653 1.00 18.25  ? 85  TYR C CD2 1 
ATOM   4939 C  CE1 . TYR C  1 85  ? 47.822  1.682   -44.089 1.00 15.73  ? 85  TYR C CE1 1 
ATOM   4940 C  CE2 . TYR C  1 85  ? 47.034  3.466   -42.672 1.00 17.51  ? 85  TYR C CE2 1 
ATOM   4941 C  CZ  . TYR C  1 85  ? 47.110  2.799   -43.915 1.00 17.49  ? 85  TYR C CZ  1 
ATOM   4942 O  OH  . TYR C  1 85  ? 46.341  3.265   -44.984 1.00 19.52  ? 85  TYR C OH  1 
ATOM   4943 N  N   . SER C  1 86  ? 51.763  2.629   -38.534 1.00 17.30  ? 86  SER C N   1 
ATOM   4944 C  CA  . SER C  1 86  ? 52.426  2.537   -37.238 1.00 18.23  ? 86  SER C CA  1 
ATOM   4945 C  C   . SER C  1 86  ? 51.398  2.769   -36.117 1.00 18.28  ? 86  SER C C   1 
ATOM   4946 O  O   . SER C  1 86  ? 50.555  3.684   -36.189 1.00 17.92  ? 86  SER C O   1 
ATOM   4947 C  CB  . SER C  1 86  ? 53.553  3.515   -37.206 1.00 21.79  ? 86  SER C CB  1 
ATOM   4948 O  OG  . SER C  1 86  ? 54.554  3.242   -38.190 1.00 21.80  ? 86  SER C OG  1 
ATOM   4949 N  N   . ALA C  1 87  ? 51.655  2.136   -34.961 1.00 18.50  ? 87  ALA C N   1 
ATOM   4950 C  CA  . ALA C  1 87  ? 50.722  2.284   -33.828 1.00 16.33  ? 87  ALA C CA  1 
ATOM   4951 C  C   . ALA C  1 87  ? 50.735  3.657   -33.197 1.00 16.62  ? 87  ALA C C   1 
ATOM   4952 O  O   . ALA C  1 87  ? 51.820  4.290   -33.157 1.00 18.02  ? 87  ALA C O   1 
ATOM   4953 C  CB  . ALA C  1 87  ? 51.039  1.222   -32.830 1.00 19.67  ? 87  ALA C CB  1 
ATOM   4954 N  N   . THR C  1 88  ? 49.576  4.049   -32.662 1.00 16.77  ? 88  THR C N   1 
ATOM   4955 C  CA  . THR C  1 88  ? 49.398  5.265   -31.890 1.00 16.78  ? 88  THR C CA  1 
ATOM   4956 C  C   . THR C  1 88  ? 48.777  5.045   -30.554 1.00 15.69  ? 88  THR C C   1 
ATOM   4957 O  O   . THR C  1 88  ? 49.247  5.616   -29.517 1.00 17.07  ? 88  THR C O   1 
ATOM   4958 C  CB  . THR C  1 88  ? 48.895  6.451   -32.619 1.00 16.43  ? 88  THR C CB  1 
ATOM   4959 O  OG1 . THR C  1 88  ? 48.800  7.607   -31.839 1.00 20.34  ? 88  THR C OG1 1 
ATOM   4960 C  CG2 . THR C  1 88  ? 47.458  6.183   -33.157 1.00 17.72  ? 88  THR C CG2 1 
ATOM   4961 N  N   . GLN C  1 89  ? 47.746  4.209   -30.457 1.00 17.55  ? 89  GLN C N   1 
ATOM   4962 C  CA  . GLN C  1 89  ? 47.008  3.998   -29.146 1.00 15.22  ? 89  GLN C CA  1 
ATOM   4963 C  C   . GLN C  1 89  ? 46.050  2.823   -29.347 1.00 16.43  ? 89  GLN C C   1 
ATOM   4964 O  O   . GLN C  1 89  ? 45.691  2.480   -30.508 1.00 15.88  ? 89  GLN C O   1 
ATOM   4965 C  CB  . GLN C  1 89  ? 46.337  5.289   -28.654 1.00 18.41  ? 89  GLN C CB  1 
ATOM   4966 C  CG  . GLN C  1 89  ? 45.391  5.916   -29.708 1.00 20.07  ? 89  GLN C CG  1 
ATOM   4967 C  CD  . GLN C  1 89  ? 43.903  5.695   -29.368 1.00 17.30  ? 89  GLN C CD  1 
ATOM   4968 O  OE1 . GLN C  1 89  ? 43.529  4.597   -28.952 1.00 20.66  ? 89  GLN C OE1 1 
ATOM   4969 N  NE2 . GLN C  1 89  ? 43.119  6.673   -29.460 1.00 24.23  ? 89  GLN C NE2 1 
ATOM   4970 N  N   . LEU C  1 90  ? 45.684  2.173   -28.236 1.00 16.95  ? 90  LEU C N   1 
ATOM   4971 C  CA  . LEU C  1 90  ? 44.583  1.344   -28.176 1.00 14.26  ? 90  LEU C CA  1 
ATOM   4972 C  C   . LEU C  1 90  ? 43.559  1.789   -27.183 1.00 15.29  ? 90  LEU C C   1 
ATOM   4973 O  O   . LEU C  1 90  ? 43.909  2.525   -26.231 1.00 16.15  ? 90  LEU C O   1 
ATOM   4974 C  CB  . LEU C  1 90  ? 44.924  -0.111  -28.120 1.00 14.80  ? 90  LEU C CB  1 
ATOM   4975 C  CG  . LEU C  1 90  ? 45.776  -0.492  -26.766 1.00 15.92  ? 90  LEU C CG  1 
ATOM   4976 C  CD1 . LEU C  1 90  ? 44.873  -0.552  -25.552 1.00 17.28  ? 90  LEU C CD1 1 
ATOM   4977 C  CD2 . LEU C  1 90  ? 46.233  -1.850  -26.984 1.00 17.80  ? 90  LEU C CD2 1 
ATOM   4978 N  N   . HIS C  1 91  ? 42.327  1.305   -27.352 1.00 15.89  ? 91  HIS C N   1 
ATOM   4979 C  CA  . HIS C  1 91  ? 41.234  1.710   -26.434 1.00 13.44  ? 91  HIS C CA  1 
ATOM   4980 C  C   . HIS C  1 91  ? 40.169  0.614   -26.570 1.00 15.01  ? 91  HIS C C   1 
ATOM   4981 O  O   . HIS C  1 91  ? 40.226  -0.254  -27.423 1.00 15.86  ? 91  HIS C O   1 
ATOM   4982 C  CB  . HIS C  1 91  ? 40.869  3.123   -26.631 1.00 15.36  ? 91  HIS C CB  1 
ATOM   4983 C  CG  . HIS C  1 91  ? 40.171  3.245   -27.954 1.00 14.96  ? 91  HIS C CG  1 
ATOM   4984 N  ND1 . HIS C  1 91  ? 40.907  3.665   -29.060 1.00 14.66  ? 91  HIS C ND1 1 
ATOM   4985 C  CD2 . HIS C  1 91  ? 38.959  2.839   -28.410 1.00 14.50  ? 91  HIS C CD2 1 
ATOM   4986 C  CE1 . HIS C  1 91  ? 40.117  3.565   -30.118 1.00 15.04  ? 91  HIS C CE1 1 
ATOM   4987 N  NE2 . HIS C  1 91  ? 38.947  3.051   -29.761 1.00 15.34  ? 91  HIS C NE2 1 
ATOM   4988 N  N   . LEU C  1 92  ? 39.166  0.701   -25.709 1.00 15.87  ? 92  LEU C N   1 
ATOM   4989 C  CA  . LEU C  1 92  ? 38.077  -0.258  -25.677 1.00 17.91  ? 92  LEU C CA  1 
ATOM   4990 C  C   . LEU C  1 92  ? 36.689  0.440   -25.627 1.00 12.67  ? 92  LEU C C   1 
ATOM   4991 O  O   . LEU C  1 92  ? 36.534  1.605   -25.396 1.00 16.48  ? 92  LEU C O   1 
ATOM   4992 C  CB  . LEU C  1 92  ? 38.137  -1.165  -24.393 1.00 18.49  ? 92  LEU C CB  1 
ATOM   4993 C  CG  . LEU C  1 92  ? 39.379  -2.043  -24.414 1.00 18.19  ? 92  LEU C CG  1 
ATOM   4994 C  CD1 . LEU C  1 92  ? 40.316  -1.715  -23.406 1.00 34.20  ? 92  LEU C CD1 1 
ATOM   4995 C  CD2 . LEU C  1 92  ? 39.059  -3.423  -24.442 1.00 19.72  ? 92  LEU C CD2 1 
ATOM   4996 N  N   . HIS C  1 93  ? 35.723  -0.399  -26.085 1.00 15.53  ? 93  HIS C N   1 
ATOM   4997 C  CA  . HIS C  1 93  ? 34.291  0.021   -26.074 1.00 14.80  ? 93  HIS C CA  1 
ATOM   4998 C  C   . HIS C  1 93  ? 33.523  -1.095  -25.399 1.00 14.86  ? 93  HIS C C   1 
ATOM   4999 O  O   . HIS C  1 93  ? 33.727  -2.287  -25.614 1.00 14.56  ? 93  HIS C O   1 
ATOM   5000 C  CB  . HIS C  1 93  ? 33.744  0.155   -27.501 1.00 14.65  ? 93  HIS C CB  1 
ATOM   5001 C  CG  . HIS C  1 93  ? 34.478  1.245   -28.279 1.00 12.31  ? 93  HIS C CG  1 
ATOM   5002 N  ND1 . HIS C  1 93  ? 34.163  2.590   -28.321 1.00 14.07  ? 93  HIS C ND1 1 
ATOM   5003 C  CD2 . HIS C  1 93  ? 35.629  1.064   -29.115 1.00 13.74  ? 93  HIS C CD2 1 
ATOM   5004 C  CE1 . HIS C  1 93  ? 35.043  3.175   -29.112 1.00 13.16  ? 93  HIS C CE1 1 
ATOM   5005 N  NE2 . HIS C  1 93  ? 35.924  2.317   -29.591 1.00 13.70  ? 93  HIS C NE2 1 
ATOM   5006 N  N   . TRP C  1 94  ? 32.533  -0.772  -24.520 1.00 15.22  ? 94  TRP C N   1 
ATOM   5007 C  CA  . TRP C  1 94  ? 31.769  -1.768  -23.774 1.00 15.08  ? 94  TRP C CA  1 
ATOM   5008 C  C   . TRP C  1 94  ? 30.341  -1.240  -23.503 1.00 14.46  ? 94  TRP C C   1 
ATOM   5009 O  O   . TRP C  1 94  ? 30.028  -0.084  -23.723 1.00 14.94  ? 94  TRP C O   1 
ATOM   5010 C  CB  . TRP C  1 94  ? 32.535  -2.127  -22.500 1.00 16.69  ? 94  TRP C CB  1 
ATOM   5011 C  CG  . TRP C  1 94  ? 32.807  -0.987  -21.592 1.00 17.33  ? 94  TRP C CG  1 
ATOM   5012 C  CD1 . TRP C  1 94  ? 31.969  -0.537  -20.588 1.00 17.57  ? 94  TRP C CD1 1 
ATOM   5013 C  CD2 . TRP C  1 94  ? 33.961  -0.127  -21.546 1.00 17.44  ? 94  TRP C CD2 1 
ATOM   5014 N  NE1 . TRP C  1 94  ? 32.538  0.593   -19.940 1.00 17.62  ? 94  TRP C NE1 1 
ATOM   5015 C  CE2 . TRP C  1 94  ? 33.769  0.840   -20.526 1.00 18.31  ? 94  TRP C CE2 1 
ATOM   5016 C  CE3 . TRP C  1 94  ? 35.157  -0.073  -22.305 1.00 18.86  ? 94  TRP C CE3 1 
ATOM   5017 C  CZ2 . TRP C  1 94  ? 34.749  1.793   -20.177 1.00 17.66  ? 94  TRP C CZ2 1 
ATOM   5018 C  CZ3 . TRP C  1 94  ? 36.089  0.919   -21.994 1.00 18.88  ? 94  TRP C CZ3 1 
ATOM   5019 C  CH2 . TRP C  1 94  ? 35.881  1.859   -20.958 1.00 18.84  ? 94  TRP C CH2 1 
ATOM   5020 N  N   . GLY C  1 95  ? 29.587  -2.184  -22.899 1.00 16.40  ? 95  GLY C N   1 
ATOM   5021 C  CA  . GLY C  1 95  ? 28.172  -1.950  -22.588 1.00 16.90  ? 95  GLY C CA  1 
ATOM   5022 C  C   . GLY C  1 95  ? 28.016  -1.635  -21.097 1.00 18.14  ? 95  GLY C C   1 
ATOM   5023 O  O   . GLY C  1 95  ? 28.643  -0.668  -20.560 1.00 17.38  ? 95  GLY C O   1 
ATOM   5024 N  N   . ASN C  1 96  ? 27.122  -2.370  -20.456 1.00 19.68  ? 96  ASN C N   1 
ATOM   5025 C  CA  . ASN C  1 96  ? 26.905  -2.079  -18.953 1.00 20.24  ? 96  ASN C CA  1 
ATOM   5026 C  C   . ASN C  1 96  ? 26.492  -3.422  -18.358 1.00 18.47  ? 96  ASN C C   1 
ATOM   5027 O  O   . ASN C  1 96  ? 26.099  -4.366  -19.058 1.00 19.69  ? 96  ASN C O   1 
ATOM   5028 C  CB  . ASN C  1 96  ? 25.889  -0.918  -18.765 1.00 22.73  ? 96  ASN C CB  1 
ATOM   5029 C  CG  . ASN C  1 96  ? 24.462  -1.354  -19.123 1.00 25.35  ? 96  ASN C CG  1 
ATOM   5030 O  OD1 . ASN C  1 96  ? 23.799  -1.878  -18.297 1.00 32.88  ? 96  ASN C OD1 1 
ATOM   5031 N  ND2 . ASN C  1 96  ? 24.027  -1.134  -20.321 1.00 26.86  ? 96  ASN C ND2 1 
ATOM   5032 N  N   . PRO C  1 97  ? 26.534  -3.555  -17.000 1.00 20.91  ? 97  PRO C N   1 
ATOM   5033 C  CA  . PRO C  1 97  ? 26.200  -4.852  -16.442 1.00 23.18  ? 97  PRO C CA  1 
ATOM   5034 C  C   . PRO C  1 97  ? 24.780  -5.336  -16.696 1.00 21.36  ? 97  PRO C C   1 
ATOM   5035 O  O   . PRO C  1 97  ? 24.535  -6.549  -16.694 1.00 23.69  ? 97  PRO C O   1 
ATOM   5036 C  CB  . PRO C  1 97  ? 26.362  -4.607  -14.881 1.00 25.47  ? 97  PRO C CB  1 
ATOM   5037 C  CG  . PRO C  1 97  ? 27.406  -3.531  -14.853 1.00 26.59  ? 97  PRO C CG  1 
ATOM   5038 C  CD  . PRO C  1 97  ? 27.050  -2.586  -16.031 1.00 22.75  ? 97  PRO C CD  1 
ATOM   5039 N  N   . ASN C  1 98  ? 23.875  -4.399  -16.894 1.00 22.42  ? 98  ASN C N   1 
ATOM   5040 C  CA  . ASN C  1 98  ? 22.445  -4.833  -17.170 1.00 25.73  ? 98  ASN C CA  1 
ATOM   5041 C  C   . ASN C  1 98  ? 22.223  -5.222  -18.661 1.00 23.89  ? 98  ASN C C   1 
ATOM   5042 O  O   . ASN C  1 98  ? 21.235  -5.873  -18.974 1.00 26.53  ? 98  ASN C O   1 
ATOM   5043 C  CB  . ASN C  1 98  ? 21.457  -3.729  -16.856 1.00 25.15  ? 98  ASN C CB  1 
ATOM   5044 C  CG  . ASN C  1 98  ? 21.357  -3.491  -15.343 1.00 35.34  ? 98  ASN C CG  1 
ATOM   5045 O  OD1 . ASN C  1 98  ? 21.400  -4.428  -14.579 1.00 39.09  ? 98  ASN C OD1 1 
ATOM   5046 N  ND2 . ASN C  1 98  ? 21.279  -2.263  -14.938 1.00 44.57  ? 98  ASN C ND2 1 
ATOM   5047 N  N   . ASP C  1 99  ? 23.159  -4.848  -19.562 1.00 21.66  ? 99  ASP C N   1 
ATOM   5048 C  CA  . ASP C  1 99  ? 23.044  -5.143  -21.023 1.00 20.23  ? 99  ASP C CA  1 
ATOM   5049 C  C   . ASP C  1 99  ? 24.505  -5.236  -21.524 1.00 17.79  ? 99  ASP C C   1 
ATOM   5050 O  O   . ASP C  1 99  ? 25.019  -4.224  -22.098 1.00 19.76  ? 99  ASP C O   1 
ATOM   5051 C  CB  . ASP C  1 99  ? 22.301  -4.015  -21.732 1.00 21.20  ? 99  ASP C CB  1 
ATOM   5052 C  CG  . ASP C  1 99  ? 21.754  -4.429  -23.042 1.00 25.92  ? 99  ASP C CG  1 
ATOM   5053 O  OD1 . ASP C  1 99  ? 21.947  -5.566  -23.433 1.00 28.14  ? 99  ASP C OD1 1 
ATOM   5054 O  OD2 . ASP C  1 99  ? 21.196  -3.572  -23.697 1.00 29.88  ? 99  ASP C OD2 1 
ATOM   5055 N  N   . PRO C  1 100 ? 25.162  -6.367  -21.246 1.00 17.89  ? 100 PRO C N   1 
ATOM   5056 C  CA  . PRO C  1 100 ? 26.646  -6.428  -21.401 1.00 20.03  ? 100 PRO C CA  1 
ATOM   5057 C  C   . PRO C  1 100 ? 26.922  -6.763  -22.876 1.00 20.06  ? 100 PRO C C   1 
ATOM   5058 O  O   . PRO C  1 100 ? 27.518  -7.796  -23.152 1.00 19.44  ? 100 PRO C O   1 
ATOM   5059 C  CB  . PRO C  1 100 ? 27.042  -7.575  -20.450 1.00 21.06  ? 100 PRO C CB  1 
ATOM   5060 C  CG  . PRO C  1 100 ? 25.858  -8.501  -20.397 1.00 22.57  ? 100 PRO C CG  1 
ATOM   5061 C  CD  . PRO C  1 100 ? 24.640  -7.568  -20.507 1.00 22.33  ? 100 PRO C CD  1 
ATOM   5062 N  N   . HIS C  1 101 ? 26.524  -5.864  -23.794 1.00 16.84  ? 101 HIS C N   1 
ATOM   5063 C  CA  . HIS C  1 101 ? 26.660  -6.190  -25.266 1.00 16.81  ? 101 HIS C CA  1 
ATOM   5064 C  C   . HIS C  1 101 ? 27.068  -4.900  -25.914 1.00 19.15  ? 101 HIS C C   1 
ATOM   5065 O  O   . HIS C  1 101 ? 26.324  -4.408  -26.755 1.00 21.39  ? 101 HIS C O   1 
ATOM   5066 C  CB  . HIS C  1 101 ? 25.308  -6.681  -25.755 1.00 20.93  ? 101 HIS C CB  1 
ATOM   5067 C  CG  . HIS C  1 101 ? 24.756  -7.830  -25.039 1.00 21.29  ? 101 HIS C CG  1 
ATOM   5068 N  ND1 . HIS C  1 101 ? 25.244  -9.116  -25.146 1.00 23.86  ? 101 HIS C ND1 1 
ATOM   5069 C  CD2 . HIS C  1 101 ? 23.825  -7.848  -24.052 1.00 21.73  ? 101 HIS C CD2 1 
ATOM   5070 C  CE1 . HIS C  1 101 ? 24.584  -9.905  -24.309 1.00 28.12  ? 101 HIS C CE1 1 
ATOM   5071 N  NE2 . HIS C  1 101 ? 23.696  -9.158  -23.659 1.00 25.30  ? 101 HIS C NE2 1 
ATOM   5072 N  N   . GLY C  1 102 ? 28.289  -4.436  -25.763 1.00 16.30  ? 102 GLY C N   1 
ATOM   5073 C  CA  . GLY C  1 102 ? 28.752  -3.133  -26.121 1.00 16.00  ? 102 GLY C CA  1 
ATOM   5074 C  C   . GLY C  1 102 ? 29.895  -3.094  -27.137 1.00 14.15  ? 102 GLY C C   1 
ATOM   5075 O  O   . GLY C  1 102 ? 30.525  -2.051  -27.240 1.00 15.38  ? 102 GLY C O   1 
ATOM   5076 N  N   . SER C  1 103 ? 29.974  -4.163  -27.989 1.00 13.98  ? 103 SER C N   1 
ATOM   5077 C  CA  . SER C  1 103 ? 30.834  -3.955  -29.151 1.00 13.13  ? 103 SER C CA  1 
ATOM   5078 C  C   . SER C  1 103 ? 30.266  -2.936  -30.102 1.00 13.84  ? 103 SER C C   1 
ATOM   5079 O  O   . SER C  1 103 ? 29.086  -2.604  -30.020 1.00 14.62  ? 103 SER C O   1 
ATOM   5080 C  CB  . SER C  1 103 ? 30.994  -5.287  -29.911 1.00 13.74  ? 103 SER C CB  1 
ATOM   5081 O  OG  . SER C  1 103 ? 29.765  -5.741  -30.529 1.00 13.78  ? 103 SER C OG  1 
ATOM   5082 N  N   . GLU C  1 104 ? 31.153  -2.424  -30.954 1.00 12.15  ? 104 GLU C N   1 
ATOM   5083 C  CA  . GLU C  1 104 ? 30.737  -1.443  -31.994 1.00 12.13  ? 104 GLU C CA  1 
ATOM   5084 C  C   . GLU C  1 104 ? 30.220  -2.156  -33.212 1.00 11.19  ? 104 GLU C C   1 
ATOM   5085 O  O   . GLU C  1 104 ? 29.078  -1.957  -33.650 1.00 11.57  ? 104 GLU C O   1 
ATOM   5086 C  CB  . GLU C  1 104 ? 31.848  -0.468  -32.270 1.00 12.30  ? 104 GLU C CB  1 
ATOM   5087 C  CG  . GLU C  1 104 ? 32.354  0.248   -31.016 1.00 13.93  ? 104 GLU C CG  1 
ATOM   5088 C  CD  . GLU C  1 104 ? 32.713  1.679   -31.320 1.00 13.30  ? 104 GLU C CD  1 
ATOM   5089 O  OE1 . GLU C  1 104 ? 33.795  1.868   -31.890 1.00 13.80  ? 104 GLU C OE1 1 
ATOM   5090 O  OE2 . GLU C  1 104 ? 31.913  2.598   -31.031 1.00 13.78  ? 104 GLU C OE2 1 
ATOM   5091 N  N   . HIS C  1 105 ? 31.077  -2.955  -33.813 1.00 11.23  ? 105 HIS C N   1 
ATOM   5092 C  CA  . HIS C  1 105 ? 30.596  -3.810  -34.931 1.00 11.03  ? 105 HIS C CA  1 
ATOM   5093 C  C   . HIS C  1 105 ? 29.688  -4.913  -34.393 1.00 10.85  ? 105 HIS C C   1 
ATOM   5094 O  O   . HIS C  1 105 ? 29.846  -5.389  -33.256 1.00 13.35  ? 105 HIS C O   1 
ATOM   5095 C  CB  . HIS C  1 105 ? 31.802  -4.425  -35.620 1.00 11.64  ? 105 HIS C CB  1 
ATOM   5096 C  CG  . HIS C  1 105 ? 32.622  -3.404  -36.375 1.00 11.41  ? 105 HIS C CG  1 
ATOM   5097 N  ND1 . HIS C  1 105 ? 33.648  -2.699  -35.796 1.00 12.56  ? 105 HIS C ND1 1 
ATOM   5098 C  CD2 . HIS C  1 105 ? 32.488  -2.890  -37.612 1.00 11.20  ? 105 HIS C CD2 1 
ATOM   5099 C  CE1 . HIS C  1 105 ? 34.110  -1.784  -36.690 1.00 12.45  ? 105 HIS C CE1 1 
ATOM   5100 N  NE2 . HIS C  1 105 ? 33.381  -1.891  -37.813 1.00 11.86  ? 105 HIS C NE2 1 
ATOM   5101 N  N   . THR C  1 106 ? 28.750  -5.309  -35.218 1.00 11.26  ? 106 THR C N   1 
ATOM   5102 C  CA  . THR C  1 106 ? 27.882  -6.455  -34.961 1.00 12.00  ? 106 THR C CA  1 
ATOM   5103 C  C   . THR C  1 106 ? 28.066  -7.487  -36.044 1.00 11.81  ? 106 THR C C   1 
ATOM   5104 O  O   . THR C  1 106 ? 28.559  -7.179  -37.126 1.00 12.66  ? 106 THR C O   1 
ATOM   5105 C  CB  . THR C  1 106 ? 26.402  -6.006  -34.798 1.00 12.56  ? 106 THR C CB  1 
ATOM   5106 O  OG1 . THR C  1 106 ? 25.950  -5.424  -36.038 1.00 12.91  ? 106 THR C OG1 1 
ATOM   5107 C  CG2 . THR C  1 106 ? 26.179  -5.017  -33.712 1.00 14.08  ? 106 THR C CG2 1 
ATOM   5108 N  N   . VAL C  1 107 ? 27.702  -8.744  -35.716 1.00 12.83  ? 107 VAL C N   1 
ATOM   5109 C  CA  . VAL C  1 107 ? 27.818  -9.829  -36.687 1.00 13.47  ? 107 VAL C CA  1 
ATOM   5110 C  C   . VAL C  1 107 ? 26.442  -10.431 -36.811 1.00 13.62  ? 107 VAL C C   1 
ATOM   5111 O  O   . VAL C  1 107 ? 25.896  -10.879 -35.780 1.00 14.28  ? 107 VAL C O   1 
ATOM   5112 C  CB  . VAL C  1 107 ? 28.916  -10.888 -36.339 1.00 15.33  ? 107 VAL C CB  1 
ATOM   5113 C  CG1 . VAL C  1 107 ? 28.855  -12.042 -37.308 1.00 17.54  ? 107 VAL C CG1 1 
ATOM   5114 C  CG2 . VAL C  1 107 ? 30.299  -10.203 -36.191 1.00 17.44  ? 107 VAL C CG2 1 
ATOM   5115 N  N   . SER C  1 108 ? 25.822  -10.359 -37.993 1.00 14.22  ? 108 SER C N   1 
ATOM   5116 C  CA  . SER C  1 108 ? 24.474  -10.890 -38.153 1.00 15.93  ? 108 SER C CA  1 
ATOM   5117 C  C   . SER C  1 108 ? 23.526  -10.254 -37.134 1.00 14.53  ? 108 SER C C   1 
ATOM   5118 O  O   . SER C  1 108 ? 22.655  -10.972 -36.577 1.00 16.06  ? 108 SER C O   1 
ATOM   5119 C  CB  . SER C  1 108 ? 24.428  -12.475 -38.079 1.00 18.64  ? 108 SER C CB  1 
ATOM   5120 O  OG  . SER C  1 108 ? 25.220  -12.995 -39.125 1.00 23.43  ? 108 SER C OG  1 
ATOM   5121 N  N   . GLY C  1 109 ? 23.694  -8.946  -36.923 1.00 13.72  ? 109 GLY C N   1 
ATOM   5122 C  CA  . GLY C  1 109 ? 22.848  -8.197  -36.026 1.00 14.80  ? 109 GLY C CA  1 
ATOM   5123 C  C   . GLY C  1 109 ? 23.236  -8.294  -34.549 1.00 14.32  ? 109 GLY C C   1 
ATOM   5124 O  O   . GLY C  1 109 ? 22.544  -7.649  -33.751 1.00 17.01  ? 109 GLY C O   1 
ATOM   5125 N  N   . GLN C  1 110 ? 24.198  -9.143  -34.176 1.00 13.68  ? 110 GLN C N   1 
ATOM   5126 C  CA  . GLN C  1 110 ? 24.443  -9.376  -32.773 1.00 15.82  ? 110 GLN C CA  1 
ATOM   5127 C  C   . GLN C  1 110 ? 25.712  -8.667  -32.280 1.00 13.87  ? 110 GLN C C   1 
ATOM   5128 O  O   . GLN C  1 110 ? 26.769  -8.700  -32.966 1.00 13.32  ? 110 GLN C O   1 
ATOM   5129 C  CB  . GLN C  1 110 ? 24.747  -10.876 -32.497 1.00 16.89  ? 110 GLN C CB  1 
ATOM   5130 C  CG  . GLN C  1 110 ? 23.684  -11.805 -33.145 1.00 17.80  ? 110 GLN C CG  1 
ATOM   5131 C  CD  . GLN C  1 110 ? 22.251  -11.347 -32.745 1.00 18.26  ? 110 GLN C CD  1 
ATOM   5132 O  OE1 . GLN C  1 110 ? 21.932  -11.349 -31.550 1.00 20.76  ? 110 GLN C OE1 1 
ATOM   5133 N  NE2 . GLN C  1 110 ? 21.401  -11.019 -33.749 1.00 19.97  ? 110 GLN C NE2 1 
ATOM   5134 N  N   . HIS C  1 111 ? 25.578  -7.928  -31.167 1.00 13.94  ? 111 HIS C N   1 
ATOM   5135 C  CA  . HIS C  1 111 ? 26.757  -7.377  -30.520 1.00 14.43  ? 111 HIS C CA  1 
ATOM   5136 C  C   . HIS C  1 111 ? 27.552  -8.492  -29.774 1.00 16.32  ? 111 HIS C C   1 
ATOM   5137 O  O   . HIS C  1 111 ? 26.977  -9.471  -29.342 1.00 20.23  ? 111 HIS C O   1 
ATOM   5138 C  CB  . HIS C  1 111 ? 26.377  -6.366  -29.411 1.00 17.18  ? 111 HIS C CB  1 
ATOM   5139 C  CG  . HIS C  1 111 ? 25.840  -5.114  -29.954 1.00 14.74  ? 111 HIS C CG  1 
ATOM   5140 N  ND1 . HIS C  1 111 ? 26.627  -3.986  -30.130 1.00 15.78  ? 111 HIS C ND1 1 
ATOM   5141 C  CD2 . HIS C  1 111 ? 24.590  -4.813  -30.412 1.00 17.04  ? 111 HIS C CD2 1 
ATOM   5142 C  CE1 . HIS C  1 111 ? 25.870  -3.031  -30.699 1.00 15.56  ? 111 HIS C CE1 1 
ATOM   5143 N  NE2 . HIS C  1 111 ? 24.622  -3.486  -30.766 1.00 20.13  ? 111 HIS C NE2 1 
ATOM   5144 N  N   . PHE C  1 112 ? 28.817  -8.209  -29.657 1.00 15.30  ? 112 PHE C N   1 
ATOM   5145 C  CA  . PHE C  1 112 ? 29.679  -8.913  -28.689 1.00 15.00  ? 112 PHE C CA  1 
ATOM   5146 C  C   . PHE C  1 112 ? 29.702  -8.064  -27.392 1.00 15.52  ? 112 PHE C C   1 
ATOM   5147 O  O   . PHE C  1 112 ? 29.208  -6.984  -27.359 1.00 15.32  ? 112 PHE C O   1 
ATOM   5148 C  CB  . PHE C  1 112 ? 31.023  -9.159  -29.292 1.00 17.41  ? 112 PHE C CB  1 
ATOM   5149 C  CG  . PHE C  1 112 ? 30.967  -10.233 -30.284 1.00 19.73  ? 112 PHE C CG  1 
ATOM   5150 C  CD1 . PHE C  1 112 ? 30.468  -10.004 -31.630 1.00 22.18  ? 112 PHE C CD1 1 
ATOM   5151 C  CD2 . PHE C  1 112 ? 31.413  -11.499 -29.936 1.00 23.03  ? 112 PHE C CD2 1 
ATOM   5152 C  CE1 . PHE C  1 112 ? 30.413  -11.106 -32.560 1.00 26.65  ? 112 PHE C CE1 1 
ATOM   5153 C  CE2 . PHE C  1 112 ? 31.417  -12.519 -30.834 1.00 22.88  ? 112 PHE C CE2 1 
ATOM   5154 C  CZ  . PHE C  1 112 ? 30.903  -12.347 -32.134 1.00 30.09  ? 112 PHE C CZ  1 
ATOM   5155 N  N   . ALA C  1 113 ? 30.317  -8.653  -26.338 1.00 16.26  ? 113 ALA C N   1 
ATOM   5156 C  CA  . ALA C  1 113 ? 30.403  -7.928  -25.071 1.00 16.69  ? 113 ALA C CA  1 
ATOM   5157 C  C   . ALA C  1 113 ? 31.127  -6.623  -25.095 1.00 15.57  ? 113 ALA C C   1 
ATOM   5158 O  O   . ALA C  1 113 ? 30.693  -5.614  -24.485 1.00 17.24  ? 113 ALA C O   1 
ATOM   5159 C  CB  . ALA C  1 113 ? 30.935  -8.869  -24.005 1.00 18.70  ? 113 ALA C CB  1 
ATOM   5160 N  N   . ALA C  1 114 ? 32.275  -6.618  -25.896 1.00 16.95  ? 114 ALA C N   1 
ATOM   5161 C  CA  . ALA C  1 114 ? 33.102  -5.379  -25.927 1.00 15.82  ? 114 ALA C CA  1 
ATOM   5162 C  C   . ALA C  1 114 ? 34.000  -5.516  -27.172 1.00 14.79  ? 114 ALA C C   1 
ATOM   5163 O  O   . ALA C  1 114 ? 33.853  -6.504  -27.863 1.00 14.45  ? 114 ALA C O   1 
ATOM   5164 C  CB  . ALA C  1 114 ? 33.943  -5.412  -24.617 1.00 17.58  ? 114 ALA C CB  1 
ATOM   5165 N  N   . GLU C  1 115 ? 34.730  -4.452  -27.427 1.00 13.93  ? 115 GLU C N   1 
ATOM   5166 C  CA  . GLU C  1 115 ? 35.553  -4.456  -28.655 1.00 15.14  ? 115 GLU C CA  1 
ATOM   5167 C  C   . GLU C  1 115 ? 36.795  -3.627  -28.222 1.00 13.49  ? 115 GLU C C   1 
ATOM   5168 O  O   . GLU C  1 115 ? 36.744  -2.501  -27.665 1.00 15.83  ? 115 GLU C O   1 
ATOM   5169 C  CB  . GLU C  1 115 ? 34.709  -3.842  -29.781 1.00 14.15  ? 115 GLU C CB  1 
ATOM   5170 C  CG  . GLU C  1 115 ? 35.433  -3.962  -31.151 1.00 14.73  ? 115 GLU C CG  1 
ATOM   5171 C  CD  . GLU C  1 115 ? 34.502  -3.537  -32.271 1.00 13.43  ? 115 GLU C CD  1 
ATOM   5172 O  OE1 . GLU C  1 115 ? 34.956  -3.074  -33.342 1.00 13.33  ? 115 GLU C OE1 1 
ATOM   5173 O  OE2 . GLU C  1 115 ? 33.276  -3.804  -32.177 1.00 14.26  ? 115 GLU C OE2 1 
ATOM   5174 N  N   . LEU C  1 116 ? 37.946  -4.209  -28.741 1.00 15.69  ? 116 LEU C N   1 
ATOM   5175 C  CA  . LEU C  1 116 ? 39.239  -3.496  -28.595 1.00 15.26  ? 116 LEU C CA  1 
ATOM   5176 C  C   . LEU C  1 116 ? 39.747  -2.940  -29.995 1.00 12.14  ? 116 LEU C C   1 
ATOM   5177 O  O   . LEU C  1 116 ? 39.504  -3.655  -30.995 1.00 14.75  ? 116 LEU C O   1 
ATOM   5178 C  CB  . LEU C  1 116 ? 40.331  -4.552  -28.240 1.00 16.61  ? 116 LEU C CB  1 
ATOM   5179 C  CG  . LEU C  1 116 ? 41.823  -4.028  -28.232 1.00 17.50  ? 116 LEU C CG  1 
ATOM   5180 C  CD1 . LEU C  1 116 ? 42.129  -3.030  -27.104 1.00 20.45  ? 116 LEU C CD1 1 
ATOM   5181 C  CD2 . LEU C  1 116 ? 42.780  -5.186  -28.380 1.00 19.33  ? 116 LEU C CD2 1 
ATOM   5182 N  N   . HIS C  1 117 ? 40.096  -1.707  -30.017 1.00 13.95  ? 117 HIS C N   1 
ATOM   5183 C  CA  . HIS C  1 117 ? 40.581  -1.061  -31.244 1.00 13.96  ? 117 HIS C CA  1 
ATOM   5184 C  C   . HIS C  1 117 ? 42.092  -0.723  -31.011 1.00 14.66  ? 117 HIS C C   1 
ATOM   5185 O  O   . HIS C  1 117 ? 42.462  -0.019  -30.059 1.00 14.74  ? 117 HIS C O   1 
ATOM   5186 C  CB  . HIS C  1 117 ? 39.843  0.187   -31.489 1.00 14.26  ? 117 HIS C CB  1 
ATOM   5187 C  CG  . HIS C  1 117 ? 38.429  -0.079  -31.906 1.00 13.32  ? 117 HIS C CG  1 
ATOM   5188 N  ND1 . HIS C  1 117 ? 37.416  0.827   -31.795 1.00 15.18  ? 117 HIS C ND1 1 
ATOM   5189 C  CD2 . HIS C  1 117 ? 38.001  -1.238  -32.460 1.00 13.01  ? 117 HIS C CD2 1 
ATOM   5190 C  CE1 . HIS C  1 117 ? 36.318  0.233   -32.274 1.00 13.21  ? 117 HIS C CE1 1 
ATOM   5191 N  NE2 . HIS C  1 117 ? 36.633  -0.992  -32.696 1.00 12.18  ? 117 HIS C NE2 1 
ATOM   5192 N  N   . ILE C  1 118 ? 42.931  -1.211  -31.930 1.00 14.42  ? 118 ILE C N   1 
ATOM   5193 C  CA  . ILE C  1 118 ? 44.358  -0.849  -31.951 1.00 16.07  ? 118 ILE C CA  1 
ATOM   5194 C  C   . ILE C  1 118 ? 44.588  0.112   -33.098 1.00 11.69  ? 118 ILE C C   1 
ATOM   5195 O  O   . ILE C  1 118 ? 44.472  -0.366  -34.312 1.00 15.09  ? 118 ILE C O   1 
ATOM   5196 C  CB  . ILE C  1 118 ? 45.217  -2.039  -32.069 1.00 15.63  ? 118 ILE C CB  1 
ATOM   5197 C  CG1 . ILE C  1 118 ? 44.914  -3.059  -31.020 1.00 16.92  ? 118 ILE C CG1 1 
ATOM   5198 C  CG2 . ILE C  1 118 ? 46.742  -1.597  -31.860 1.00 17.40  ? 118 ILE C CG2 1 
ATOM   5199 C  CD1 . ILE C  1 118 ? 45.695  -4.327  -31.059 1.00 19.48  ? 118 ILE C CD1 1 
ATOM   5200 N  N   . VAL C  1 119 ? 44.753  1.363   -32.857 1.00 15.52  ? 119 VAL C N   1 
ATOM   5201 C  CA  . VAL C  1 119 ? 44.776  2.465   -33.823 1.00 15.43  ? 119 VAL C CA  1 
ATOM   5202 C  C   . VAL C  1 119 ? 46.164  2.661   -34.359 1.00 14.06  ? 119 VAL C C   1 
ATOM   5203 O  O   . VAL C  1 119 ? 47.104  2.807   -33.566 1.00 15.72  ? 119 VAL C O   1 
ATOM   5204 C  CB  . VAL C  1 119 ? 44.191  3.755   -33.270 1.00 14.93  ? 119 VAL C CB  1 
ATOM   5205 C  CG1 . VAL C  1 119 ? 44.124  4.854   -34.356 1.00 15.97  ? 119 VAL C CG1 1 
ATOM   5206 C  CG2 . VAL C  1 119 ? 42.840  3.523   -32.613 1.00 16.50  ? 119 VAL C CG2 1 
ATOM   5207 N  N   . HIS C  1 120 ? 46.288  2.646   -35.673 1.00 15.80  ? 120 HIS C N   1 
ATOM   5208 C  CA  . HIS C  1 120 ? 47.581  2.908   -36.387 1.00 15.65  ? 120 HIS C CA  1 
ATOM   5209 C  C   . HIS C  1 120 ? 47.387  4.093   -37.376 1.00 15.90  ? 120 HIS C C   1 
ATOM   5210 O  O   . HIS C  1 120 ? 46.263  4.302   -37.843 1.00 15.39  ? 120 HIS C O   1 
ATOM   5211 C  CB  . HIS C  1 120 ? 48.070  1.682   -37.161 1.00 16.08  ? 120 HIS C CB  1 
ATOM   5212 C  CG  . HIS C  1 120 ? 48.210  0.403   -36.450 1.00 16.11  ? 120 HIS C CG  1 
ATOM   5213 N  ND1 . HIS C  1 120 ? 47.154  -0.217  -35.820 1.00 15.80  ? 120 HIS C ND1 1 
ATOM   5214 C  CD2 . HIS C  1 120 ? 49.310  -0.279  -36.063 1.00 19.28  ? 120 HIS C CD2 1 
ATOM   5215 C  CE1 . HIS C  1 120 ? 47.548  -1.334  -35.273 1.00 16.88  ? 120 HIS C CE1 1 
ATOM   5216 N  NE2 . HIS C  1 120 ? 48.879  -1.435  -35.377 1.00 17.57  ? 120 HIS C NE2 1 
ATOM   5217 N  N   . TYR C  1 121 ? 48.520  4.733   -37.740 1.00 16.74  ? 121 TYR C N   1 
ATOM   5218 C  CA  . TYR C  1 121 ? 48.502  5.877   -38.677 1.00 17.66  ? 121 TYR C CA  1 
ATOM   5219 C  C   . TYR C  1 121 ? 49.473  5.528   -39.796 1.00 19.14  ? 121 TYR C C   1 
ATOM   5220 O  O   . TYR C  1 121 ? 50.401  4.784   -39.660 1.00 17.85  ? 121 TYR C O   1 
ATOM   5221 C  CB  . TYR C  1 121 ? 48.793  7.243   -38.008 1.00 18.51  ? 121 TYR C CB  1 
ATOM   5222 C  CG  . TYR C  1 121 ? 50.195  7.467   -37.570 1.00 16.94  ? 121 TYR C CG  1 
ATOM   5223 C  CD1 . TYR C  1 121 ? 50.632  6.850   -36.361 1.00 20.28  ? 121 TYR C CD1 1 
ATOM   5224 C  CD2 . TYR C  1 121 ? 51.079  8.126   -38.424 1.00 18.41  ? 121 TYR C CD2 1 
ATOM   5225 C  CE1 . TYR C  1 121 ? 51.959  7.000   -35.925 1.00 22.92  ? 121 TYR C CE1 1 
ATOM   5226 C  CE2 . TYR C  1 121 ? 52.456  8.241   -38.045 1.00 22.05  ? 121 TYR C CE2 1 
ATOM   5227 C  CZ  . TYR C  1 121 ? 52.835  7.748   -36.758 1.00 21.96  ? 121 TYR C CZ  1 
ATOM   5228 O  OH  . TYR C  1 121 ? 54.174  7.787   -36.346 1.00 28.18  ? 121 TYR C OH  1 
ATOM   5229 N  N   . ASN C  1 122 ? 49.167  6.119   -40.926 1.00 17.04  ? 122 ASN C N   1 
ATOM   5230 C  CA  . ASN C  1 122 ? 50.012  5.905   -42.139 1.00 17.04  ? 122 ASN C CA  1 
ATOM   5231 C  C   . ASN C  1 122 ? 51.292  6.778   -42.044 1.00 16.34  ? 122 ASN C C   1 
ATOM   5232 O  O   . ASN C  1 122 ? 51.286  7.981   -42.335 1.00 19.21  ? 122 ASN C O   1 
ATOM   5233 C  CB  . ASN C  1 122 ? 49.187  6.343   -43.364 1.00 18.75  ? 122 ASN C CB  1 
ATOM   5234 C  CG  . ASN C  1 122 ? 49.831  5.921   -44.616 1.00 19.41  ? 122 ASN C CG  1 
ATOM   5235 O  OD1 . ASN C  1 122 ? 51.060  5.902   -44.722 1.00 19.95  ? 122 ASN C OD1 1 
ATOM   5236 N  ND2 . ASN C  1 122 ? 49.009  5.616   -45.634 1.00 20.77  ? 122 ASN C ND2 1 
ATOM   5237 N  N   . SER C  1 123 ? 52.285  6.108   -41.548 1.00 18.23  ? 123 SER C N   1 
ATOM   5238 C  CA  . SER C  1 123 ? 53.588  6.773   -41.318 1.00 18.29  ? 123 SER C CA  1 
ATOM   5239 C  C   . SER C  1 123 ? 54.361  6.954   -42.594 1.00 17.21  ? 123 SER C C   1 
ATOM   5240 O  O   . SER C  1 123 ? 55.350  7.765   -42.581 1.00 21.58  ? 123 SER C O   1 
ATOM   5241 C  CB  . SER C  1 123 ? 54.367  5.996   -40.233 1.00 21.23  ? 123 SER C CB  1 
ATOM   5242 O  OG  . SER C  1 123 ? 54.474  4.595   -40.497 1.00 20.17  ? 123 SER C OG  1 
ATOM   5243 N  N   . ASP C  1 124 ? 54.017  6.295   -43.660 1.00 17.25  ? 124 ASP C N   1 
ATOM   5244 C  CA  . ASP C  1 124 ? 54.641  6.575   -44.938 1.00 17.50  ? 124 ASP C CA  1 
ATOM   5245 C  C   . ASP C  1 124 ? 54.182  7.930   -45.504 1.00 19.31  ? 124 ASP C C   1 
ATOM   5246 O  O   . ASP C  1 124 ? 55.035  8.668   -46.086 1.00 25.49  ? 124 ASP C O   1 
ATOM   5247 C  CB  . ASP C  1 124 ? 54.355  5.454   -45.933 1.00 19.31  ? 124 ASP C CB  1 
ATOM   5248 C  CG  . ASP C  1 124 ? 55.059  4.176   -45.667 1.00 20.55  ? 124 ASP C CG  1 
ATOM   5249 O  OD1 . ASP C  1 124 ? 56.122  4.160   -44.888 1.00 21.87  ? 124 ASP C OD1 1 
ATOM   5250 O  OD2 . ASP C  1 124 ? 54.646  3.156   -46.197 1.00 21.87  ? 124 ASP C OD2 1 
ATOM   5251 N  N   . LEU C  1 125 ? 52.958  8.294   -45.274 1.00 16.64  ? 125 LEU C N   1 
ATOM   5252 C  CA  . LEU C  1 125 ? 52.446  9.586   -45.787 1.00 20.23  ? 125 LEU C CA  1 
ATOM   5253 C  C   . LEU C  1 125 ? 52.582  10.687  -44.779 1.00 21.89  ? 125 LEU C C   1 
ATOM   5254 O  O   . LEU C  1 125 ? 52.635  11.884  -45.235 1.00 23.72  ? 125 LEU C O   1 
ATOM   5255 C  CB  . LEU C  1 125 ? 50.989  9.370   -46.244 1.00 19.10  ? 125 LEU C CB  1 
ATOM   5256 C  CG  . LEU C  1 125 ? 50.757  8.446   -47.402 1.00 20.84  ? 125 LEU C CG  1 
ATOM   5257 C  CD1 . LEU C  1 125 ? 49.272  8.409   -47.770 1.00 21.53  ? 125 LEU C CD1 1 
ATOM   5258 C  CD2 . LEU C  1 125 ? 51.612  8.808   -48.628 1.00 24.75  ? 125 LEU C CD2 1 
ATOM   5259 N  N   . TYR C  1 126 ? 52.405  10.367  -43.493 1.00 20.76  ? 126 TYR C N   1 
ATOM   5260 C  CA  . TYR C  1 126 ? 52.193  11.413  -42.508 1.00 20.33  ? 126 TYR C CA  1 
ATOM   5261 C  C   . TYR C  1 126 ? 53.170  11.306  -41.320 1.00 20.54  ? 126 TYR C C   1 
ATOM   5262 O  O   . TYR C  1 126 ? 53.588  10.218  -40.957 1.00 20.64  ? 126 TYR C O   1 
ATOM   5263 C  CB  . TYR C  1 126 ? 50.697  11.421  -41.998 1.00 19.84  ? 126 TYR C CB  1 
ATOM   5264 C  CG  . TYR C  1 126 ? 49.730  11.425  -43.161 1.00 20.37  ? 126 TYR C CG  1 
ATOM   5265 C  CD1 . TYR C  1 126 ? 49.658  12.530  -44.037 1.00 24.13  ? 126 TYR C CD1 1 
ATOM   5266 C  CD2 . TYR C  1 126 ? 48.882  10.290  -43.438 1.00 20.56  ? 126 TYR C CD2 1 
ATOM   5267 C  CE1 . TYR C  1 126 ? 48.787  12.540  -45.117 1.00 21.25  ? 126 TYR C CE1 1 
ATOM   5268 C  CE2 . TYR C  1 126 ? 48.004  10.315  -44.537 1.00 20.76  ? 126 TYR C CE2 1 
ATOM   5269 C  CZ  . TYR C  1 126 ? 47.969  11.428  -45.342 1.00 20.39  ? 126 TYR C CZ  1 
ATOM   5270 O  OH  . TYR C  1 126 ? 47.138  11.474  -46.429 1.00 20.76  ? 126 TYR C OH  1 
ATOM   5271 N  N   . PRO C  1 127 ? 53.484  12.464  -40.702 1.00 22.42  ? 127 PRO C N   1 
ATOM   5272 C  CA  . PRO C  1 127 ? 54.571  12.503  -39.700 1.00 22.40  ? 127 PRO C CA  1 
ATOM   5273 C  C   . PRO C  1 127 ? 54.098  11.995  -38.325 1.00 26.13  ? 127 PRO C C   1 
ATOM   5274 O  O   . PRO C  1 127 ? 54.909  11.595  -37.475 1.00 30.31  ? 127 PRO C O   1 
ATOM   5275 C  CB  . PRO C  1 127 ? 54.860  14.003  -39.583 1.00 29.60  ? 127 PRO C CB  1 
ATOM   5276 C  CG  . PRO C  1 127 ? 53.669  14.767  -40.064 1.00 28.33  ? 127 PRO C CG  1 
ATOM   5277 C  CD  . PRO C  1 127 ? 53.122  13.828  -41.147 1.00 26.27  ? 127 PRO C CD  1 
ATOM   5278 N  N   . ASP C  1 128 ? 52.792  11.981  -38.091 1.00 23.04  ? 128 ASP C N   1 
ATOM   5279 C  CA  . ASP C  1 128 ? 52.259  11.551  -36.778 1.00 24.30  ? 128 ASP C CA  1 
ATOM   5280 C  C   . ASP C  1 128 ? 50.775  11.290  -36.952 1.00 22.70  ? 128 ASP C C   1 
ATOM   5281 O  O   . ASP C  1 128 ? 50.149  11.719  -37.937 1.00 22.95  ? 128 ASP C O   1 
ATOM   5282 C  CB  . ASP C  1 128 ? 52.429  12.609  -35.649 1.00 29.42  ? 128 ASP C CB  1 
ATOM   5283 C  CG  . ASP C  1 128 ? 52.161  14.041  -36.111 1.00 33.63  ? 128 ASP C CG  1 
ATOM   5284 O  OD1 . ASP C  1 128 ? 51.085  14.341  -36.628 1.00 32.65  ? 128 ASP C OD1 1 
ATOM   5285 O  OD2 . ASP C  1 128 ? 53.052  14.945  -35.954 1.00 38.98  ? 128 ASP C OD2 1 
ATOM   5286 N  N   . ALA C  1 129 ? 50.229  10.696  -35.894 1.00 22.46  ? 129 ALA C N   1 
ATOM   5287 C  CA  . ALA C  1 129 ? 48.789  10.299  -35.970 1.00 21.29  ? 129 ALA C CA  1 
ATOM   5288 C  C   . ALA C  1 129 ? 47.800  11.469  -35.999 1.00 24.11  ? 129 ALA C C   1 
ATOM   5289 O  O   . ALA C  1 129 ? 46.820  11.430  -36.735 1.00 24.12  ? 129 ALA C O   1 
ATOM   5290 C  CB  . ALA C  1 129 ? 48.451  9.373   -34.847 1.00 26.73  ? 129 ALA C CB  1 
ATOM   5291 N  N   . SER C  1 130 ? 48.055  12.539  -35.251 1.00 26.16  ? 130 SER C N   1 
ATOM   5292 C  CA  . SER C  1 130 ? 47.139  13.707  -35.290 1.00 29.55  ? 130 SER C CA  1 
ATOM   5293 C  C   . SER C  1 130 ? 47.075  14.290  -36.719 1.00 29.66  ? 130 SER C C   1 
ATOM   5294 O  O   . SER C  1 130 ? 45.998  14.587  -37.213 1.00 30.46  ? 130 SER C O   1 
ATOM   5295 C  CB  . SER C  1 130 ? 47.393  14.698  -34.135 1.00 44.17  ? 130 SER C CB  1 
ATOM   5296 O  OG  . SER C  1 130 ? 48.422  15.564  -34.483 1.00 55.29  ? 130 SER C OG  1 
ATOM   5297 N  N   . THR C  1 131 ? 48.224  14.415  -37.404 1.00 25.08  ? 131 THR C N   1 
ATOM   5298 C  CA  . THR C  1 131 ? 48.258  14.954  -38.765 1.00 23.92  ? 131 THR C CA  1 
ATOM   5299 C  C   . THR C  1 131 ? 47.490  13.990  -39.712 1.00 19.91  ? 131 THR C C   1 
ATOM   5300 O  O   . THR C  1 131 ? 46.745  14.426  -40.572 1.00 22.24  ? 131 THR C O   1 
ATOM   5301 C  CB  . THR C  1 131 ? 49.739  15.097  -39.295 1.00 24.84  ? 131 THR C CB  1 
ATOM   5302 O  OG1 . THR C  1 131 ? 50.380  16.011  -38.377 1.00 30.00  ? 131 THR C OG1 1 
ATOM   5303 C  CG2 . THR C  1 131 ? 49.708  15.734  -40.753 1.00 25.75  ? 131 THR C CG2 1 
ATOM   5304 N  N   . ALA C  1 132 ? 47.746  12.693  -39.505 1.00 19.50  ? 132 ALA C N   1 
ATOM   5305 C  CA  . ALA C  1 132 ? 47.124  11.699  -40.386 1.00 21.27  ? 132 ALA C CA  1 
ATOM   5306 C  C   . ALA C  1 132 ? 45.620  11.577  -40.256 1.00 19.15  ? 132 ALA C C   1 
ATOM   5307 O  O   . ALA C  1 132 ? 44.959  11.143  -41.263 1.00 19.28  ? 132 ALA C O   1 
ATOM   5308 C  CB  . ALA C  1 132 ? 47.707  10.310  -40.017 1.00 18.47  ? 132 ALA C CB  1 
ATOM   5309 N  N   . SER C  1 133 ? 45.045  11.859  -39.089 1.00 21.21  ? 133 SER C N   1 
ATOM   5310 C  CA  . SER C  1 133 ? 43.700  11.345  -38.769 1.00 22.07  ? 133 SER C CA  1 
ATOM   5311 C  C   . SER C  1 133 ? 42.674  11.949  -39.694 1.00 16.99  ? 133 SER C C   1 
ATOM   5312 O  O   . SER C  1 133 ? 41.598  11.269  -39.825 1.00 18.87  ? 133 SER C O   1 
ATOM   5313 C  CB  . SER C  1 133 ? 43.401  11.662  -37.237 1.00 21.49  ? 133 SER C CB  1 
ATOM   5314 O  OG  . SER C  1 133 ? 43.266  13.094  -37.051 1.00 21.28  ? 133 SER C OG  1 
ATOM   5315 N  N   . ASN C  1 134 ? 42.804  13.140  -40.283 1.00 18.12  ? 134 ASN C N   1 
ATOM   5316 C  CA  . ASN C  1 134 ? 41.812  13.730  -41.144 1.00 18.89  ? 134 ASN C CA  1 
ATOM   5317 C  C   . ASN C  1 134 ? 42.231  13.686  -42.629 1.00 18.48  ? 134 ASN C C   1 
ATOM   5318 O  O   . ASN C  1 134 ? 41.613  14.381  -43.462 1.00 23.88  ? 134 ASN C O   1 
ATOM   5319 C  CB  . ASN C  1 134 ? 41.422  15.207  -40.731 1.00 21.76  ? 134 ASN C CB  1 
ATOM   5320 C  CG  . ASN C  1 134 ? 42.649  16.149  -40.718 1.00 25.35  ? 134 ASN C CG  1 
ATOM   5321 O  OD1 . ASN C  1 134 ? 43.756  15.748  -41.038 1.00 29.47  ? 134 ASN C OD1 1 
ATOM   5322 N  ND2 . ASN C  1 134 ? 42.430  17.424  -40.423 1.00 29.24  ? 134 ASN C ND2 1 
ATOM   5323 N  N   . LYS C  1 135 ? 43.208  12.840  -43.001 1.00 19.69  ? 135 LYS C N   1 
ATOM   5324 C  CA  . LYS C  1 135 ? 43.790  12.773  -44.330 1.00 19.50  ? 135 LYS C CA  1 
ATOM   5325 C  C   . LYS C  1 135 ? 43.561  11.428  -44.975 1.00 19.82  ? 135 LYS C C   1 
ATOM   5326 O  O   . LYS C  1 135 ? 43.362  10.410  -44.316 1.00 18.53  ? 135 LYS C O   1 
ATOM   5327 C  CB  . LYS C  1 135 ? 45.288  13.213  -44.238 1.00 23.00  ? 135 LYS C CB  1 
ATOM   5328 C  CG  . LYS C  1 135 ? 45.501  14.667  -43.875 1.00 26.77  ? 135 LYS C CG  1 
ATOM   5329 C  CD  . LYS C  1 135 ? 46.904  15.093  -43.870 1.00 27.83  ? 135 LYS C CD  1 
ATOM   5330 C  CE  . LYS C  1 135 ? 46.982  16.467  -43.326 1.00 25.61  ? 135 LYS C CE  1 
ATOM   5331 N  NZ  . LYS C  1 135 ? 46.357  16.790  -41.959 1.00 27.89  ? 135 LYS C NZ  1 
ATOM   5332 N  N   . SER C  1 136 ? 43.647  11.465  -46.308 1.00 22.56  ? 136 SER C N   1 
ATOM   5333 C  CA  . SER C  1 136 ? 43.418  10.309  -47.169 1.00 22.36  ? 136 SER C CA  1 
ATOM   5334 C  C   . SER C  1 136 ? 44.342  9.185   -46.668 1.00 18.37  ? 136 SER C C   1 
ATOM   5335 O  O   . SER C  1 136 ? 45.565  9.366   -46.443 1.00 19.88  ? 136 SER C O   1 
ATOM   5336 C  CB  . SER C  1 136 ? 43.841  10.768  -48.543 1.00 28.32  ? 136 SER C CB  1 
ATOM   5337 O  OG  . SER C  1 136 ? 43.785  9.625   -49.324 1.00 32.15  ? 136 SER C OG  1 
ATOM   5338 N  N   . GLU C  1 137 ? 43.761  7.994   -46.520 1.00 19.34  ? 137 GLU C N   1 
ATOM   5339 C  CA  . GLU C  1 137 ? 44.494  6.776   -46.124 1.00 17.58  ? 137 GLU C CA  1 
ATOM   5340 C  C   . GLU C  1 137 ? 45.245  7.022   -44.812 1.00 16.78  ? 137 GLU C C   1 
ATOM   5341 O  O   . GLU C  1 137 ? 46.288  6.339   -44.559 1.00 17.98  ? 137 GLU C O   1 
ATOM   5342 C  CB  . GLU C  1 137 ? 45.469  6.232   -47.196 1.00 19.52  ? 137 GLU C CB  1 
ATOM   5343 C  CG  . GLU C  1 137 ? 44.790  5.989   -48.518 1.00 24.44  ? 137 GLU C CG  1 
ATOM   5344 C  CD  . GLU C  1 137 ? 45.774  5.511   -49.625 1.00 27.74  ? 137 GLU C CD  1 
ATOM   5345 O  OE1 . GLU C  1 137 ? 47.039  5.787   -49.628 1.00 44.43  ? 137 GLU C OE1 1 
ATOM   5346 O  OE2 . GLU C  1 137 ? 45.257  4.904   -50.524 1.00 34.90  ? 137 GLU C OE2 1 
ATOM   5347 N  N   . GLY C  1 138 ? 44.653  7.785   -43.901 1.00 15.53  ? 138 GLY C N   1 
ATOM   5348 C  CA  . GLY C  1 138 ? 45.438  8.213   -42.721 1.00 16.85  ? 138 GLY C CA  1 
ATOM   5349 C  C   . GLY C  1 138 ? 45.536  7.162   -41.684 1.00 16.30  ? 138 GLY C C   1 
ATOM   5350 O  O   . GLY C  1 138 ? 46.552  7.165   -40.934 1.00 16.73  ? 138 GLY C O   1 
ATOM   5351 N  N   . LEU C  1 139 ? 44.532  6.285   -41.470 1.00 14.91  ? 139 LEU C N   1 
ATOM   5352 C  CA  . LEU C  1 139 ? 44.462  5.416   -40.320 1.00 14.21  ? 139 LEU C CA  1 
ATOM   5353 C  C   . LEU C  1 139 ? 44.139  3.986   -40.676 1.00 14.47  ? 139 LEU C C   1 
ATOM   5354 O  O   . LEU C  1 139 ? 43.465  3.697   -41.684 1.00 14.74  ? 139 LEU C O   1 
ATOM   5355 C  CB  . LEU C  1 139 ? 43.415  5.908   -39.272 1.00 16.42  ? 139 LEU C CB  1 
ATOM   5356 C  CG  . LEU C  1 139 ? 43.650  7.322   -38.724 1.00 16.33  ? 139 LEU C CG  1 
ATOM   5357 C  CD1 . LEU C  1 139 ? 42.432  7.801   -37.937 1.00 18.78  ? 139 LEU C CD1 1 
ATOM   5358 C  CD2 . LEU C  1 139 ? 44.918  7.508   -37.859 1.00 18.63  ? 139 LEU C CD2 1 
ATOM   5359 N  N   . ALA C  1 140 ? 44.530  3.042   -39.807 1.00 15.79  ? 140 ALA C N   1 
ATOM   5360 C  CA  . ALA C  1 140 ? 44.166  1.665   -39.938 1.00 14.04  ? 140 ALA C CA  1 
ATOM   5361 C  C   . ALA C  1 140 ? 43.868  1.135   -38.526 1.00 14.48  ? 140 ALA C C   1 
ATOM   5362 O  O   . ALA C  1 140 ? 44.678  1.326   -37.633 1.00 16.14  ? 140 ALA C O   1 
ATOM   5363 C  CB  . ALA C  1 140 ? 45.166  0.785   -40.659 1.00 15.28  ? 140 ALA C CB  1 
ATOM   5364 N  N   . VAL C  1 141 ? 42.769  0.392   -38.309 1.00 13.93  ? 141 VAL C N   1 
ATOM   5365 C  CA  . VAL C  1 141 ? 42.432  -0.018  -37.026 1.00 13.80  ? 141 VAL C CA  1 
ATOM   5366 C  C   . VAL C  1 141 ? 42.288  -1.479  -37.048 1.00 12.50  ? 141 VAL C C   1 
ATOM   5367 O  O   . VAL C  1 141 ? 41.711  -2.116  -38.014 1.00 14.79  ? 141 VAL C O   1 
ATOM   5368 C  CB  . VAL C  1 141 ? 41.170  0.630   -36.439 1.00 12.95  ? 141 VAL C CB  1 
ATOM   5369 C  CG1 . VAL C  1 141 ? 40.805  -0.053  -35.039 1.00 15.79  ? 141 VAL C CG1 1 
ATOM   5370 C  CG2 . VAL C  1 141 ? 41.235  2.152   -36.305 1.00 15.00  ? 141 VAL C CG2 1 
ATOM   5371 N  N   . LEU C  1 142 ? 42.881  -2.164  -36.038 1.00 13.90  ? 142 LEU C N   1 
ATOM   5372 C  CA  . LEU C  1 142 ? 42.628  -3.570  -35.846 1.00 12.40  ? 142 LEU C CA  1 
ATOM   5373 C  C   . LEU C  1 142 ? 41.522  -3.698  -34.786 1.00 14.50  ? 142 LEU C C   1 
ATOM   5374 O  O   . LEU C  1 142 ? 41.701  -3.134  -33.691 1.00 15.15  ? 142 LEU C O   1 
ATOM   5375 C  CB  . LEU C  1 142 ? 43.863  -4.313  -35.356 1.00 15.34  ? 142 LEU C CB  1 
ATOM   5376 C  CG  . LEU C  1 142 ? 45.071  -4.204  -36.254 1.00 15.41  ? 142 LEU C CG  1 
ATOM   5377 C  CD1 . LEU C  1 142 ? 46.244  -4.993  -35.580 1.00 18.64  ? 142 LEU C CD1 1 
ATOM   5378 C  CD2 . LEU C  1 142 ? 44.812  -4.741  -37.676 1.00 17.65  ? 142 LEU C CD2 1 
ATOM   5379 N  N   . ALA C  1 143 ? 40.467  -4.452  -35.074 1.00 14.09  ? 143 ALA C N   1 
ATOM   5380 C  CA  . ALA C  1 143 ? 39.345  -4.591  -34.146 1.00 13.30  ? 143 ALA C CA  1 
ATOM   5381 C  C   . ALA C  1 143 ? 39.184  -5.965  -33.728 1.00 13.20  ? 143 ALA C C   1 
ATOM   5382 O  O   . ALA C  1 143 ? 39.174  -6.974  -34.514 1.00 14.95  ? 143 ALA C O   1 
ATOM   5383 C  CB  . ALA C  1 143 ? 38.021  -4.092  -34.790 1.00 13.08  ? 143 ALA C CB  1 
ATOM   5384 N  N   . VAL C  1 144 ? 39.173  -6.153  -32.412 1.00 13.66  ? 144 VAL C N   1 
ATOM   5385 C  CA  . VAL C  1 144 ? 39.037  -7.487  -31.841 1.00 14.49  ? 144 VAL C CA  1 
ATOM   5386 C  C   . VAL C  1 144 ? 37.700  -7.517  -30.978 1.00 14.90  ? 144 VAL C C   1 
ATOM   5387 O  O   . VAL C  1 144 ? 37.432  -6.672  -30.131 1.00 16.02  ? 144 VAL C O   1 
ATOM   5388 C  CB  . VAL C  1 144 ? 40.157  -7.804  -30.809 1.00 15.79  ? 144 VAL C CB  1 
ATOM   5389 C  CG1 . VAL C  1 144 ? 39.921  -9.234  -30.295 1.00 18.79  ? 144 VAL C CG1 1 
ATOM   5390 C  CG2 . VAL C  1 144 ? 41.512  -7.728  -31.509 1.00 18.18  ? 144 VAL C CG2 1 
ATOM   5391 N  N   . LEU C  1 145 ? 36.858  -8.444  -31.402 1.00 14.89  ? 145 LEU C N   1 
ATOM   5392 C  CA  . LEU C  1 145 ? 35.562  -8.658  -30.733 1.00 15.45  ? 145 LEU C CA  1 
ATOM   5393 C  C   . LEU C  1 145 ? 35.829  -9.472  -29.455 1.00 17.02  ? 145 LEU C C   1 
ATOM   5394 O  O   . LEU C  1 145 ? 36.593  -10.418 -29.476 1.00 19.14  ? 145 LEU C O   1 
ATOM   5395 C  CB  . LEU C  1 145 ? 34.599  -9.406  -31.628 1.00 16.47  ? 145 LEU C CB  1 
ATOM   5396 C  CG  . LEU C  1 145 ? 34.275  -8.620  -32.927 1.00 17.39  ? 145 LEU C CG  1 
ATOM   5397 C  CD1 . LEU C  1 145 ? 33.611  -9.594  -33.938 1.00 17.99  ? 145 LEU C CD1 1 
ATOM   5398 C  CD2 . LEU C  1 145 ? 33.392  -7.419  -32.629 1.00 18.43  ? 145 LEU C CD2 1 
ATOM   5399 N  N   . ILE C  1 146 ? 35.155  -9.087  -28.340 1.00 16.31  ? 146 ILE C N   1 
ATOM   5400 C  CA  . ILE C  1 146 ? 35.411  -9.675  -26.960 1.00 16.25  ? 146 ILE C CA  1 
ATOM   5401 C  C   . ILE C  1 146 ? 34.091  -10.281 -26.490 1.00 18.23  ? 146 ILE C C   1 
ATOM   5402 O  O   . ILE C  1 146 ? 33.042  -9.602  -26.502 1.00 18.27  ? 146 ILE C O   1 
ATOM   5403 C  CB  . ILE C  1 146 ? 35.897  -8.606  -26.006 1.00 17.07  ? 146 ILE C CB  1 
ATOM   5404 C  CG1 . ILE C  1 146 ? 37.275  -8.000  -26.472 1.00 18.09  ? 146 ILE C CG1 1 
ATOM   5405 C  CG2 . ILE C  1 146 ? 36.034  -9.196  -24.603 1.00 17.52  ? 146 ILE C CG2 1 
ATOM   5406 C  CD1 . ILE C  1 146 ? 37.637  -6.677  -25.824 1.00 20.08  ? 146 ILE C CD1 1 
ATOM   5407 N  N   . GLU C  1 147 ? 34.140  -11.506 -26.064 1.00 20.27  ? 147 GLU C N   1 
ATOM   5408 C  CA  . GLU C  1 147 ? 33.021  -12.182 -25.478 1.00 21.39  ? 147 GLU C CA  1 
ATOM   5409 C  C   . GLU C  1 147 ? 33.394  -12.763 -24.100 1.00 21.41  ? 147 GLU C C   1 
ATOM   5410 O  O   . GLU C  1 147 ? 34.574  -12.910 -23.724 1.00 21.99  ? 147 GLU C O   1 
ATOM   5411 C  CB  . GLU C  1 147 ? 32.462  -13.367 -26.246 1.00 22.30  ? 147 GLU C CB  1 
ATOM   5412 C  CG  . GLU C  1 147 ? 33.463  -14.439 -26.518 1.00 23.35  ? 147 GLU C CG  1 
ATOM   5413 C  CD  . GLU C  1 147 ? 32.921  -15.489 -27.487 1.00 25.83  ? 147 GLU C CD  1 
ATOM   5414 O  OE1 . GLU C  1 147 ? 31.963  -15.254 -28.254 1.00 30.54  ? 147 GLU C OE1 1 
ATOM   5415 O  OE2 . GLU C  1 147 ? 33.506  -16.550 -27.597 1.00 33.01  ? 147 GLU C OE2 1 
ATOM   5416 N  N   . MET C  1 148 ? 32.366  -13.104 -23.301 1.00 24.79  ? 148 MET C N   1 
ATOM   5417 C  CA  . MET C  1 148 ? 32.625  -13.661 -22.005 1.00 26.07  ? 148 MET C CA  1 
ATOM   5418 C  C   . MET C  1 148 ? 33.059  -15.133 -22.152 1.00 28.31  ? 148 MET C C   1 
ATOM   5419 O  O   . MET C  1 148 ? 32.603  -15.932 -23.063 1.00 26.85  ? 148 MET C O   1 
ATOM   5420 C  CB  . MET C  1 148 ? 31.298  -13.742 -21.201 1.00 30.26  ? 148 MET C CB  1 
ATOM   5421 C  CG  . MET C  1 148 ? 30.522  -12.485 -20.812 1.00 38.90  ? 148 MET C CG  1 
ATOM   5422 S  SD  . MET C  1 148 ? 28.986  -13.085 -20.066 1.00 57.26  ? 148 MET C SD  1 
ATOM   5423 C  CE  . MET C  1 148 ? 29.695  -14.148 -18.810 1.00 73.96  ? 148 MET C CE  1 
ATOM   5424 N  N   . GLY C  1 149 ? 34.022  -15.522 -21.282 1.00 33.28  ? 149 GLY C N   1 
ATOM   5425 C  CA  . GLY C  1 149 ? 34.430  -16.921 -21.367 1.00 28.10  ? 149 GLY C CA  1 
ATOM   5426 C  C   . GLY C  1 149 ? 35.523  -17.063 -20.290 1.00 31.25  ? 149 GLY C C   1 
ATOM   5427 O  O   . GLY C  1 149 ? 35.421  -16.531 -19.156 1.00 27.80  ? 149 GLY C O   1 
ATOM   5428 N  N   . SER C  1 150 ? 36.662  -17.660 -20.737 1.00 33.59  ? 150 SER C N   1 
ATOM   5429 C  CA  . SER C  1 150 ? 37.840  -17.880 -19.894 1.00 27.87  ? 150 SER C CA  1 
ATOM   5430 C  C   . SER C  1 150 ? 38.497  -16.581 -19.434 1.00 31.35  ? 150 SER C C   1 
ATOM   5431 O  O   . SER C  1 150 ? 38.557  -15.652 -20.265 1.00 31.10  ? 150 SER C O   1 
ATOM   5432 C  CB  . SER C  1 150 ? 38.845  -18.708 -20.696 1.00 34.33  ? 150 SER C CB  1 
ATOM   5433 O  OG  . SER C  1 150 ? 38.415  -20.004 -20.693 1.00 48.00  ? 150 SER C OG  1 
ATOM   5434 N  N   . PHE C  1 151 ? 39.087  -16.610 -18.219 1.00 30.57  ? 151 PHE C N   1 
ATOM   5435 C  CA  . PHE C  1 151 ? 39.942  -15.507 -17.764 1.00 32.42  ? 151 PHE C CA  1 
ATOM   5436 C  C   . PHE C  1 151 ? 41.048  -15.292 -18.774 1.00 31.30  ? 151 PHE C C   1 
ATOM   5437 O  O   . PHE C  1 151 ? 41.576  -16.267 -19.265 1.00 33.76  ? 151 PHE C O   1 
ATOM   5438 C  CB  . PHE C  1 151 ? 40.514  -15.777 -16.295 1.00 32.30  ? 151 PHE C CB  1 
ATOM   5439 C  CG  . PHE C  1 151 ? 41.493  -14.728 -15.833 1.00 28.41  ? 151 PHE C CG  1 
ATOM   5440 C  CD1 . PHE C  1 151 ? 41.012  -13.513 -15.308 1.00 29.34  ? 151 PHE C CD1 1 
ATOM   5441 C  CD2 . PHE C  1 151 ? 42.881  -14.993 -15.809 1.00 34.73  ? 151 PHE C CD2 1 
ATOM   5442 C  CE1 . PHE C  1 151 ? 41.881  -12.487 -14.875 1.00 28.57  ? 151 PHE C CE1 1 
ATOM   5443 C  CE2 . PHE C  1 151 ? 43.763  -13.953 -15.445 1.00 29.62  ? 151 PHE C CE2 1 
ATOM   5444 C  CZ  . PHE C  1 151 ? 43.282  -12.711 -14.911 1.00 29.14  ? 151 PHE C CZ  1 
ATOM   5445 N  N   . ASN C  1 152 ? 41.413  -14.025 -18.968 1.00 24.82  ? 152 ASN C N   1 
ATOM   5446 C  CA  . ASN C  1 152 ? 42.450  -13.585 -19.909 1.00 23.09  ? 152 ASN C CA  1 
ATOM   5447 C  C   . ASN C  1 152 ? 43.540  -12.799 -19.336 1.00 22.64  ? 152 ASN C C   1 
ATOM   5448 O  O   . ASN C  1 152 ? 43.433  -11.556 -18.908 1.00 25.24  ? 152 ASN C O   1 
ATOM   5449 C  CB  . ASN C  1 152 ? 41.768  -12.822 -21.091 1.00 22.29  ? 152 ASN C CB  1 
ATOM   5450 C  CG  . ASN C  1 152 ? 42.680  -12.757 -22.285 1.00 26.02  ? 152 ASN C CG  1 
ATOM   5451 O  OD1 . ASN C  1 152 ? 43.819  -12.305 -22.091 1.00 26.19  ? 152 ASN C OD1 1 
ATOM   5452 N  ND2 . ASN C  1 152 ? 42.148  -12.887 -23.526 1.00 24.70  ? 152 ASN C ND2 1 
ATOM   5453 N  N   . PRO C  1 153 ? 44.713  -13.460 -19.031 1.00 23.90  ? 153 PRO C N   1 
ATOM   5454 C  CA  . PRO C  1 153 ? 45.867  -12.741 -18.419 1.00 25.75  ? 153 PRO C CA  1 
ATOM   5455 C  C   . PRO C  1 153 ? 46.407  -11.632 -19.174 1.00 20.99  ? 153 PRO C C   1 
ATOM   5456 O  O   . PRO C  1 153 ? 46.789  -10.604 -18.568 1.00 25.59  ? 153 PRO C O   1 
ATOM   5457 C  CB  . PRO C  1 153 ? 46.997  -13.878 -18.156 1.00 25.55  ? 153 PRO C CB  1 
ATOM   5458 C  CG  . PRO C  1 153 ? 46.377  -15.218 -18.624 1.00 30.86  ? 153 PRO C CG  1 
ATOM   5459 C  CD  . PRO C  1 153 ? 44.983  -14.900 -19.315 1.00 24.21  ? 153 PRO C CD  1 
ATOM   5460 N  N   . SER C  1 154 ? 46.354  -11.675 -20.512 1.00 23.73  ? 154 SER C N   1 
ATOM   5461 C  CA  . SER C  1 154 ? 46.807  -10.568 -21.341 1.00 24.97  ? 154 SER C CA  1 
ATOM   5462 C  C   . SER C  1 154 ? 45.982  -9.336  -21.152 1.00 19.31  ? 154 SER C C   1 
ATOM   5463 O  O   . SER C  1 154 ? 46.545  -8.222  -20.944 1.00 23.16  ? 154 SER C O   1 
ATOM   5464 C  CB  . SER C  1 154 ? 47.015  -11.048 -22.716 1.00 29.37  ? 154 SER C CB  1 
ATOM   5465 O  OG  . SER C  1 154 ? 47.783  -12.210 -22.668 1.00 32.49  ? 154 SER C OG  1 
ATOM   5466 N  N   . TYR C  1 155 ? 44.629  -9.420  -21.249 1.00 20.88  ? 155 TYR C N   1 
ATOM   5467 C  CA  . TYR C  1 155 ? 43.815  -8.232  -21.009 1.00 23.81  ? 155 TYR C CA  1 
ATOM   5468 C  C   . TYR C  1 155 ? 43.904  -7.788  -19.627 1.00 18.22  ? 155 TYR C C   1 
ATOM   5469 O  O   . TYR C  1 155 ? 43.730  -6.561  -19.332 1.00 20.62  ? 155 TYR C O   1 
ATOM   5470 C  CB  . TYR C  1 155 ? 42.334  -8.561  -21.305 1.00 22.24  ? 155 TYR C CB  1 
ATOM   5471 C  CG  . TYR C  1 155 ? 42.126  -8.443  -22.845 1.00 19.01  ? 155 TYR C CG  1 
ATOM   5472 C  CD1 . TYR C  1 155 ? 42.523  -9.499  -23.695 1.00 19.57  ? 155 TYR C CD1 1 
ATOM   5473 C  CD2 . TYR C  1 155 ? 41.545  -7.313  -23.405 1.00 18.72  ? 155 TYR C CD2 1 
ATOM   5474 C  CE1 . TYR C  1 155 ? 42.363  -9.389  -25.113 1.00 19.49  ? 155 TYR C CE1 1 
ATOM   5475 C  CE2 . TYR C  1 155 ? 41.337  -7.196  -24.794 1.00 20.95  ? 155 TYR C CE2 1 
ATOM   5476 C  CZ  . TYR C  1 155 ? 41.742  -8.252  -25.623 1.00 18.78  ? 155 TYR C CZ  1 
ATOM   5477 O  OH  . TYR C  1 155 ? 41.572  -8.097  -27.002 1.00 19.63  ? 155 TYR C OH  1 
ATOM   5478 N  N   . ASP C  1 156 ? 44.267  -8.594  -18.599 1.00 22.95  ? 156 ASP C N   1 
ATOM   5479 C  CA  . ASP C  1 156 ? 44.397  -8.208  -17.217 1.00 25.33  ? 156 ASP C CA  1 
ATOM   5480 C  C   . ASP C  1 156 ? 45.628  -7.223  -17.103 1.00 23.56  ? 156 ASP C C   1 
ATOM   5481 O  O   . ASP C  1 156 ? 45.742  -6.463  -16.113 1.00 24.22  ? 156 ASP C O   1 
ATOM   5482 C  CB  . ASP C  1 156 ? 44.442  -9.314  -16.218 1.00 28.84  ? 156 ASP C CB  1 
ATOM   5483 C  CG  . ASP C  1 156 ? 43.386  -9.133  -15.171 1.00 37.13  ? 156 ASP C CG  1 
ATOM   5484 O  OD1 . ASP C  1 156 ? 42.263  -8.682  -15.501 1.00 29.94  ? 156 ASP C OD1 1 
ATOM   5485 O  OD2 . ASP C  1 156 ? 43.680  -9.435  -14.010 1.00 41.24  ? 156 ASP C OD2 1 
ATOM   5486 N  N   . LYS C  1 157 ? 46.595  -7.273  -18.077 1.00 20.96  ? 157 LYS C N   1 
ATOM   5487 C  CA  . LYS C  1 157 ? 47.748  -6.344  -18.039 1.00 23.30  ? 157 LYS C CA  1 
ATOM   5488 C  C   . LYS C  1 157 ? 47.260  -4.991  -18.177 1.00 25.40  ? 157 LYS C C   1 
ATOM   5489 O  O   . LYS C  1 157 ? 47.947  -4.059  -17.650 1.00 32.38  ? 157 LYS C O   1 
ATOM   5490 C  CB  . LYS C  1 157 ? 48.870  -6.707  -19.065 1.00 29.55  ? 157 LYS C CB  1 
ATOM   5491 C  CG  . LYS C  1 157 ? 49.439  -8.099  -18.782 1.00 33.44  ? 157 LYS C CG  1 
ATOM   5492 C  CD  . LYS C  1 157 ? 50.342  -8.769  -19.801 1.00 30.03  ? 157 LYS C CD  1 
ATOM   5493 C  CE  . LYS C  1 157 ? 50.724  -10.081 -19.215 1.00 41.09  ? 157 LYS C CE  1 
ATOM   5494 N  NZ  . LYS C  1 157 ? 51.282  -11.001 -20.267 1.00 48.89  ? 157 LYS C NZ  1 
ATOM   5495 N  N   . ILE C  1 158 ? 46.078  -4.730  -18.844 1.00 25.05  ? 158 ILE C N   1 
ATOM   5496 C  CA  . ILE C  1 158 ? 45.519  -3.404  -18.904 1.00 22.50  ? 158 ILE C CA  1 
ATOM   5497 C  C   . ILE C  1 158 ? 44.638  -3.302  -17.635 1.00 21.20  ? 158 ILE C C   1 
ATOM   5498 O  O   . ILE C  1 158 ? 44.579  -2.207  -16.978 1.00 22.84  ? 158 ILE C O   1 
ATOM   5499 C  CB  . ILE C  1 158 ? 44.730  -3.143  -20.211 1.00 21.64  ? 158 ILE C CB  1 
ATOM   5500 C  CG1 . ILE C  1 158 ? 45.861  -3.115  -21.268 1.00 26.86  ? 158 ILE C CG1 1 
ATOM   5501 C  CG2 . ILE C  1 158 ? 44.021  -1.810  -20.131 1.00 24.95  ? 158 ILE C CG2 1 
ATOM   5502 C  CD1 . ILE C  1 158 ? 45.361  -3.162  -22.706 1.00 30.75  ? 158 ILE C CD1 1 
ATOM   5503 N  N   . PHE C  1 159 ? 43.693  -4.221  -17.622 1.00 24.24  ? 159 PHE C N   1 
ATOM   5504 C  CA  . PHE C  1 159 ? 42.588  -4.164  -16.589 1.00 20.01  ? 159 PHE C CA  1 
ATOM   5505 C  C   . PHE C  1 159 ? 42.955  -3.966  -15.109 1.00 24.25  ? 159 PHE C C   1 
ATOM   5506 O  O   . PHE C  1 159 ? 42.205  -3.339  -14.330 1.00 23.42  ? 159 PHE C O   1 
ATOM   5507 C  CB  . PHE C  1 159 ? 41.570  -5.319  -16.667 1.00 24.37  ? 159 PHE C CB  1 
ATOM   5508 C  CG  . PHE C  1 159 ? 40.865  -5.491  -17.997 1.00 20.44  ? 159 PHE C CG  1 
ATOM   5509 C  CD1 . PHE C  1 159 ? 40.700  -4.465  -18.926 1.00 23.11  ? 159 PHE C CD1 1 
ATOM   5510 C  CD2 . PHE C  1 159 ? 40.330  -6.731  -18.290 1.00 23.73  ? 159 PHE C CD2 1 
ATOM   5511 C  CE1 . PHE C  1 159 ? 40.034  -4.707  -20.127 1.00 23.28  ? 159 PHE C CE1 1 
ATOM   5512 C  CE2 . PHE C  1 159 ? 39.670  -6.977  -19.475 1.00 27.49  ? 159 PHE C CE2 1 
ATOM   5513 C  CZ  . PHE C  1 159 ? 39.519  -5.965  -20.398 1.00 22.91  ? 159 PHE C CZ  1 
ATOM   5514 N  N   . SER C  1 160 ? 44.186  -4.364  -14.800 1.00 22.41  ? 160 SER C N   1 
ATOM   5515 C  CA  . SER C  1 160 ? 44.675  -4.272  -13.475 1.00 24.32  ? 160 SER C CA  1 
ATOM   5516 C  C   . SER C  1 160 ? 45.113  -2.931  -13.067 1.00 25.83  ? 160 SER C C   1 
ATOM   5517 O  O   . SER C  1 160 ? 45.427  -2.763  -11.879 1.00 33.50  ? 160 SER C O   1 
ATOM   5518 C  CB  . SER C  1 160 ? 45.792  -5.260  -13.301 1.00 31.26  ? 160 SER C CB  1 
ATOM   5519 O  OG  . SER C  1 160 ? 46.992  -4.960  -14.068 1.00 30.21  ? 160 SER C OG  1 
ATOM   5520 N  N   . HIS C  1 161 ? 45.121  -2.008  -14.013 1.00 22.53  ? 161 HIS C N   1 
ATOM   5521 C  CA  . HIS C  1 161 ? 45.354  -0.590  -13.742 1.00 24.58  ? 161 HIS C CA  1 
ATOM   5522 C  C   . HIS C  1 161 ? 44.165  0.318   -13.660 1.00 21.97  ? 161 HIS C C   1 
ATOM   5523 O  O   . HIS C  1 161 ? 44.351  1.579   -13.476 1.00 22.55  ? 161 HIS C O   1 
ATOM   5524 C  CB  . HIS C  1 161 ? 46.502  -0.072  -14.718 1.00 24.37  ? 161 HIS C CB  1 
ATOM   5525 C  CG  . HIS C  1 161 ? 47.787  -0.824  -14.511 1.00 28.67  ? 161 HIS C CG  1 
ATOM   5526 N  ND1 . HIS C  1 161 ? 48.753  -0.419  -13.591 1.00 30.52  ? 161 HIS C ND1 1 
ATOM   5527 C  CD2 . HIS C  1 161 ? 48.154  -2.099  -14.912 1.00 31.42  ? 161 HIS C CD2 1 
ATOM   5528 C  CE1 . HIS C  1 161 ? 49.723  -1.316  -13.547 1.00 34.87  ? 161 HIS C CE1 1 
ATOM   5529 N  NE2 . HIS C  1 161 ? 49.349  -2.372  -14.273 1.00 37.40  ? 161 HIS C NE2 1 
ATOM   5530 N  N   . LEU C  1 162 ? 42.935  -0.151  -14.034 1.00 22.89  ? 162 LEU C N   1 
ATOM   5531 C  CA  . LEU C  1 162 ? 41.768  0.770   -14.170 1.00 22.34  ? 162 LEU C CA  1 
ATOM   5532 C  C   . LEU C  1 162 ? 41.415  1.485   -12.982 1.00 18.85  ? 162 LEU C C   1 
ATOM   5533 O  O   . LEU C  1 162 ? 40.977  2.665   -13.088 1.00 20.00  ? 162 LEU C O   1 
ATOM   5534 C  CB  . LEU C  1 162 ? 40.560  -0.123  -14.599 1.00 25.91  ? 162 LEU C CB  1 
ATOM   5535 C  CG  . LEU C  1 162 ? 40.710  -0.783  -15.943 1.00 22.87  ? 162 LEU C CG  1 
ATOM   5536 C  CD1 . LEU C  1 162 ? 39.473  -1.624  -16.278 1.00 31.21  ? 162 LEU C CD1 1 
ATOM   5537 C  CD2 . LEU C  1 162 ? 40.893  0.233   -17.090 1.00 29.62  ? 162 LEU C CD2 1 
ATOM   5538 N  N   . GLN C  1 163 ? 41.750  0.998   -11.739 1.00 21.68  ? 163 GLN C N   1 
ATOM   5539 C  CA  . GLN C  1 163 ? 41.388  1.739   -10.517 1.00 22.61  ? 163 GLN C CA  1 
ATOM   5540 C  C   . GLN C  1 163 ? 42.268  2.998   -10.319 1.00 22.51  ? 163 GLN C C   1 
ATOM   5541 O  O   . GLN C  1 163 ? 41.955  3.879   -9.429  1.00 25.72  ? 163 GLN C O   1 
ATOM   5542 C  CB  . GLN C  1 163 ? 41.298  0.820   -9.264  1.00 24.15  ? 163 GLN C CB  1 
ATOM   5543 C  CG  . GLN C  1 163 ? 40.247  -0.320  -9.386  1.00 27.45  ? 163 GLN C CG  1 
ATOM   5544 C  CD  . GLN C  1 163 ? 38.782  0.100   -9.439  1.00 27.72  ? 163 GLN C CD  1 
ATOM   5545 O  OE1 . GLN C  1 163 ? 38.319  1.121   -8.826  1.00 27.93  ? 163 GLN C OE1 1 
ATOM   5546 N  NE2 . GLN C  1 163 ? 38.055  -0.647  -10.194 1.00 39.58  ? 163 GLN C NE2 1 
ATOM   5547 N  N   . HIS C  1 164 ? 43.367  3.094   -11.115 1.00 20.58  ? 164 HIS C N   1 
ATOM   5548 C  CA  . HIS C  1 164 ? 44.308  4.284   -11.115 1.00 20.96  ? 164 HIS C CA  1 
ATOM   5549 C  C   . HIS C  1 164 ? 43.862  5.414   -12.024 1.00 21.82  ? 164 HIS C C   1 
ATOM   5550 O  O   . HIS C  1 164 ? 44.408  6.522   -11.960 1.00 26.51  ? 164 HIS C O   1 
ATOM   5551 C  CB  . HIS C  1 164 ? 45.771  3.881   -11.318 1.00 24.18  ? 164 HIS C CB  1 
ATOM   5552 C  CG  . HIS C  1 164 ? 46.207  2.834   -10.361 1.00 20.00  ? 164 HIS C CG  1 
ATOM   5553 N  ND1 . HIS C  1 164 ? 46.328  3.081   -8.988  1.00 23.58  ? 164 HIS C ND1 1 
ATOM   5554 C  CD2 . HIS C  1 164 ? 46.613  1.546   -10.568 1.00 23.57  ? 164 HIS C CD2 1 
ATOM   5555 C  CE1 . HIS C  1 164 ? 46.662  1.935   -8.396  1.00 25.12  ? 164 HIS C CE1 1 
ATOM   5556 N  NE2 . HIS C  1 164 ? 46.861  0.998   -9.326  1.00 30.82  ? 164 HIS C NE2 1 
ATOM   5557 N  N   . VAL C  1 165 ? 42.903  5.103   -12.892 1.00 23.89  ? 165 VAL C N   1 
ATOM   5558 C  CA  . VAL C  1 165 ? 42.411  6.142   -13.861 1.00 23.61  ? 165 VAL C CA  1 
ATOM   5559 C  C   . VAL C  1 165 ? 40.920  6.265   -13.761 1.00 19.75  ? 165 VAL C C   1 
ATOM   5560 O  O   . VAL C  1 165 ? 40.242  6.442   -14.808 1.00 20.63  ? 165 VAL C O   1 
ATOM   5561 C  CB  . VAL C  1 165 ? 42.970  5.945   -15.266 1.00 21.68  ? 165 VAL C CB  1 
ATOM   5562 C  CG1 . VAL C  1 165 ? 44.492  6.087   -15.296 1.00 24.56  ? 165 VAL C CG1 1 
ATOM   5563 C  CG2 . VAL C  1 165 ? 42.545  4.533   -15.715 1.00 23.27  ? 165 VAL C CG2 1 
ATOM   5564 N  N   . LYS C  1 166 ? 40.327  6.231   -12.544 1.00 22.35  ? 166 LYS C N   1 
ATOM   5565 C  CA  . LYS C  1 166 ? 38.904  6.218   -12.506 1.00 23.07  ? 166 LYS C CA  1 
ATOM   5566 C  C   . LYS C  1 166 ? 38.275  7.406   -12.972 1.00 23.28  ? 166 LYS C C   1 
ATOM   5567 O  O   . LYS C  1 166 ? 37.125  7.268   -13.474 1.00 23.85  ? 166 LYS C O   1 
ATOM   5568 C  CB  . LYS C  1 166 ? 38.406  6.009   -10.960 1.00 26.07  ? 166 LYS C CB  1 
ATOM   5569 C  CG  . LYS C  1 166 ? 38.562  4.613   -10.517 1.00 32.41  ? 166 LYS C CG  1 
ATOM   5570 C  CD  . LYS C  1 166 ? 38.101  4.494   -9.049  1.00 35.49  ? 166 LYS C CD  1 
ATOM   5571 C  CE  . LYS C  1 166 ? 36.606  4.282   -8.963  1.00 31.26  ? 166 LYS C CE  1 
ATOM   5572 N  NZ  . LYS C  1 166 ? 36.161  2.945   -9.505  1.00 30.09  ? 166 LYS C NZ  1 
ATOM   5573 N  N   . TYR C  1 167 ? 38.870  8.536   -12.940 1.00 21.46  ? 167 TYR C N   1 
ATOM   5574 C  CA  . TYR C  1 167 ? 38.173  9.739   -13.310 1.00 21.53  ? 167 TYR C CA  1 
ATOM   5575 C  C   . TYR C  1 167 ? 38.679  10.311  -14.585 1.00 20.97  ? 167 TYR C C   1 
ATOM   5576 O  O   . TYR C  1 167 ? 39.864  10.201  -14.807 1.00 21.86  ? 167 TYR C O   1 
ATOM   5577 C  CB  . TYR C  1 167 ? 38.328  10.697  -12.116 1.00 22.87  ? 167 TYR C CB  1 
ATOM   5578 C  CG  . TYR C  1 167 ? 37.636  10.222  -10.852 1.00 24.63  ? 167 TYR C CG  1 
ATOM   5579 C  CD1 . TYR C  1 167 ? 36.193  10.230  -10.736 1.00 27.59  ? 167 TYR C CD1 1 
ATOM   5580 C  CD2 . TYR C  1 167 ? 38.409  9.714   -9.803  1.00 23.29  ? 167 TYR C CD2 1 
ATOM   5581 C  CE1 . TYR C  1 167 ? 35.621  9.745   -9.525  1.00 38.14  ? 167 TYR C CE1 1 
ATOM   5582 C  CE2 . TYR C  1 167 ? 37.845  9.323   -8.591  1.00 32.37  ? 167 TYR C CE2 1 
ATOM   5583 C  CZ  . TYR C  1 167 ? 36.440  9.356   -8.436  1.00 31.69  ? 167 TYR C CZ  1 
ATOM   5584 O  OH  . TYR C  1 167 ? 35.893  8.866   -7.244  1.00 31.11  ? 167 TYR C OH  1 
ATOM   5585 N  N   . LYS C  1 168 ? 37.863  11.191  -15.177 1.00 20.62  ? 168 LYS C N   1 
ATOM   5586 C  CA  . LYS C  1 168 ? 38.249  11.851  -16.415 1.00 20.54  ? 168 LYS C CA  1 
ATOM   5587 C  C   . LYS C  1 168 ? 39.546  12.655  -16.199 1.00 24.20  ? 168 LYS C C   1 
ATOM   5588 O  O   . LYS C  1 168 ? 39.672  13.507  -15.230 1.00 25.08  ? 168 LYS C O   1 
ATOM   5589 C  CB  . LYS C  1 168 ? 37.174  12.831  -16.857 1.00 23.53  ? 168 LYS C CB  1 
ATOM   5590 C  CG  . LYS C  1 168 ? 37.501  13.476  -18.189 1.00 23.76  ? 168 LYS C CG  1 
ATOM   5591 C  CD  . LYS C  1 168 ? 36.345  14.367  -18.654 1.00 26.43  ? 168 LYS C CD  1 
ATOM   5592 C  CE  . LYS C  1 168 ? 36.896  14.933  -20.007 1.00 30.90  ? 168 LYS C CE  1 
ATOM   5593 N  NZ  . LYS C  1 168 ? 35.811  15.499  -20.854 1.00 48.64  ? 168 LYS C NZ  1 
ATOM   5594 N  N   . GLY C  1 169 ? 40.474  12.534  -17.143 1.00 21.43  ? 169 GLY C N   1 
ATOM   5595 C  CA  . GLY C  1 169 ? 41.823  13.243  -17.082 1.00 25.48  ? 169 GLY C CA  1 
ATOM   5596 C  C   . GLY C  1 169 ? 42.923  12.505  -16.379 1.00 25.07  ? 169 GLY C C   1 
ATOM   5597 O  O   . GLY C  1 169 ? 44.104  12.830  -16.525 1.00 31.71  ? 169 GLY C O   1 
ATOM   5598 N  N   . GLN C  1 170 ? 42.568  11.506  -15.554 1.00 21.58  ? 170 GLN C N   1 
ATOM   5599 C  CA  . GLN C  1 170 ? 43.614  10.793  -14.765 1.00 22.05  ? 170 GLN C CA  1 
ATOM   5600 C  C   . GLN C  1 170 ? 44.413  9.911   -15.683 1.00 23.10  ? 170 GLN C C   1 
ATOM   5601 O  O   . GLN C  1 170 ? 43.959  9.285   -16.680 1.00 22.22  ? 170 GLN C O   1 
ATOM   5602 C  CB  . GLN C  1 170 ? 43.043  9.959   -13.618 1.00 22.22  ? 170 GLN C CB  1 
ATOM   5603 C  CG  . GLN C  1 170 ? 42.380  10.911  -12.597 1.00 21.25  ? 170 GLN C CG  1 
ATOM   5604 C  CD  . GLN C  1 170 ? 41.963  10.119  -11.351 1.00 26.17  ? 170 GLN C CD  1 
ATOM   5605 O  OE1 . GLN C  1 170 ? 41.398  9.078   -11.439 1.00 22.95  ? 170 GLN C OE1 1 
ATOM   5606 N  NE2 . GLN C  1 170 ? 42.261  10.658  -10.186 1.00 29.24  ? 170 GLN C NE2 1 
ATOM   5607 N  N   . GLU C  1 171 ? 45.667  9.752   -15.289 1.00 22.79  ? 171 GLU C N   1 
ATOM   5608 C  CA  . GLU C  1 171 ? 46.690  8.987   -16.025 1.00 21.66  ? 171 GLU C CA  1 
ATOM   5609 C  C   . GLU C  1 171 ? 47.453  8.044   -15.131 1.00 23.56  ? 171 GLU C C   1 
ATOM   5610 O  O   . GLU C  1 171 ? 47.681  8.295   -13.938 1.00 24.52  ? 171 GLU C O   1 
ATOM   5611 C  CB  . GLU C  1 171 ? 47.713  9.972   -16.774 1.00 29.75  ? 171 GLU C CB  1 
ATOM   5612 C  CG  . GLU C  1 171 ? 47.017  10.949  -17.708 1.00 31.71  ? 171 GLU C CG  1 
ATOM   5613 C  CD  . GLU C  1 171 ? 47.970  11.913  -18.319 1.00 37.74  ? 171 GLU C CD  1 
ATOM   5614 O  OE1 . GLU C  1 171 ? 49.038  12.062  -17.767 1.00 33.77  ? 171 GLU C OE1 1 
ATOM   5615 O  OE2 . GLU C  1 171 ? 47.558  12.636  -19.250 1.00 46.88  ? 171 GLU C OE2 1 
ATOM   5616 N  N   . ALA C  1 172 ? 47.939  7.011   -15.737 1.00 21.39  ? 172 ALA C N   1 
ATOM   5617 C  CA  . ALA C  1 172 ? 48.811  6.025   -15.115 1.00 23.38  ? 172 ALA C CA  1 
ATOM   5618 C  C   . ALA C  1 172 ? 49.707  5.392   -16.094 1.00 24.90  ? 172 ALA C C   1 
ATOM   5619 O  O   . ALA C  1 172 ? 49.476  5.500   -17.235 1.00 40.58  ? 172 ALA C O   1 
ATOM   5620 C  CB  . ALA C  1 172 ? 48.026  4.991   -14.259 1.00 34.58  ? 172 ALA C CB  1 
ATOM   5621 N  N   . PHE C  1 173 ? 50.621  4.588   -15.692 1.00 30.88  ? 173 PHE C N   1 
ATOM   5622 C  CA  . PHE C  1 173 ? 51.557  3.921   -16.592 1.00 34.07  ? 173 PHE C CA  1 
ATOM   5623 C  C   . PHE C  1 173 ? 51.306  2.440   -16.489 1.00 35.14  ? 173 PHE C C   1 
ATOM   5624 O  O   . PHE C  1 173 ? 50.902  1.908   -15.418 1.00 31.13  ? 173 PHE C O   1 
ATOM   5625 C  CB  . PHE C  1 173 ? 53.060  4.255   -16.322 1.00 31.78  ? 173 PHE C CB  1 
ATOM   5626 C  CG  . PHE C  1 173 ? 53.495  5.585   -16.888 1.00 33.57  ? 173 PHE C CG  1 
ATOM   5627 C  CD1 . PHE C  1 173 ? 53.751  5.793   -18.294 1.00 32.10  ? 173 PHE C CD1 1 
ATOM   5628 C  CD2 . PHE C  1 173 ? 53.606  6.685   -16.044 1.00 40.75  ? 173 PHE C CD2 1 
ATOM   5629 C  CE1 . PHE C  1 173 ? 54.126  7.082   -18.744 1.00 32.17  ? 173 PHE C CE1 1 
ATOM   5630 C  CE2 . PHE C  1 173 ? 53.960  7.959   -16.523 1.00 41.08  ? 173 PHE C CE2 1 
ATOM   5631 C  CZ  . PHE C  1 173 ? 54.269  8.167   -17.870 1.00 32.41  ? 173 PHE C CZ  1 
ATOM   5632 N  N   . VAL C  1 174 ? 51.328  1.804   -17.649 1.00 29.19  ? 174 VAL C N   1 
ATOM   5633 C  CA  . VAL C  1 174 ? 51.361  0.324   -17.724 1.00 29.58  ? 174 VAL C CA  1 
ATOM   5634 C  C   . VAL C  1 174 ? 52.732  -0.138  -18.221 1.00 35.50  ? 174 VAL C C   1 
ATOM   5635 O  O   . VAL C  1 174 ? 53.224  0.371   -19.290 1.00 28.73  ? 174 VAL C O   1 
ATOM   5636 C  CB  . VAL C  1 174 ? 50.340  -0.166  -18.808 1.00 32.94  ? 174 VAL C CB  1 
ATOM   5637 C  CG1 . VAL C  1 174 ? 50.368  -1.684  -19.008 1.00 26.58  ? 174 VAL C CG1 1 
ATOM   5638 C  CG2 . VAL C  1 174 ? 48.923  0.258   -18.400 1.00 34.94  ? 174 VAL C CG2 1 
ATOM   5639 N  N   . PRO C  1 175 ? 53.281  -1.184  -17.621 1.00 29.50  ? 175 PRO C N   1 
ATOM   5640 C  CA  . PRO C  1 175 ? 54.541  -1.771  -18.209 1.00 28.14  ? 175 PRO C CA  1 
ATOM   5641 C  C   . PRO C  1 175 ? 54.318  -2.419  -19.522 1.00 26.28  ? 175 PRO C C   1 
ATOM   5642 O  O   . PRO C  1 175 ? 53.277  -2.963  -19.710 1.00 33.59  ? 175 PRO C O   1 
ATOM   5643 C  CB  . PRO C  1 175 ? 54.841  -2.925  -17.241 1.00 37.76  ? 175 PRO C CB  1 
ATOM   5644 C  CG  . PRO C  1 175 ? 54.050  -2.670  -16.017 1.00 33.31  ? 175 PRO C CG  1 
ATOM   5645 C  CD  . PRO C  1 175 ? 52.903  -1.817  -16.327 1.00 29.12  ? 175 PRO C CD  1 
ATOM   5646 N  N   . GLY C  1 176 ? 55.339  -2.336  -20.406 1.00 25.67  ? 176 GLY C N   1 
ATOM   5647 C  CA  . GLY C  1 176 ? 55.271  -3.053  -21.696 1.00 29.43  ? 176 GLY C CA  1 
ATOM   5648 C  C   . GLY C  1 176 ? 54.849  -4.503  -21.503 1.00 33.98  ? 176 GLY C C   1 
ATOM   5649 O  O   . GLY C  1 176 ? 55.211  -5.124  -20.488 1.00 34.55  ? 176 GLY C O   1 
ATOM   5650 N  N   . PHE C  1 177 ? 54.057  -4.951  -22.461 1.00 27.67  ? 177 PHE C N   1 
ATOM   5651 C  CA  . PHE C  1 177 ? 53.873  -6.433  -22.717 1.00 26.92  ? 177 PHE C CA  1 
ATOM   5652 C  C   . PHE C  1 177 ? 53.611  -6.621  -24.173 1.00 25.54  ? 177 PHE C C   1 
ATOM   5653 O  O   . PHE C  1 177 ? 53.646  -5.667  -24.936 1.00 24.87  ? 177 PHE C O   1 
ATOM   5654 C  CB  . PHE C  1 177 ? 52.707  -7.034  -21.912 1.00 30.19  ? 177 PHE C CB  1 
ATOM   5655 C  CG  . PHE C  1 177 ? 51.312  -6.420  -22.241 1.00 24.51  ? 177 PHE C CG  1 
ATOM   5656 C  CD1 . PHE C  1 177 ? 50.946  -5.121  -21.790 1.00 28.94  ? 177 PHE C CD1 1 
ATOM   5657 C  CD2 . PHE C  1 177 ? 50.395  -7.106  -22.995 1.00 29.82  ? 177 PHE C CD2 1 
ATOM   5658 C  CE1 . PHE C  1 177 ? 49.709  -4.551  -22.065 1.00 28.98  ? 177 PHE C CE1 1 
ATOM   5659 C  CE2 . PHE C  1 177 ? 49.092  -6.559  -23.333 1.00 24.30  ? 177 PHE C CE2 1 
ATOM   5660 C  CZ  . PHE C  1 177 ? 48.810  -5.225  -22.833 1.00 28.55  ? 177 PHE C CZ  1 
ATOM   5661 N  N   . ASN C  1 178 ? 53.438  -7.912  -24.597 1.00 22.86  ? 178 ASN C N   1 
ATOM   5662 C  CA  . ASN C  1 178 ? 53.285  -8.166  -25.958 1.00 23.92  ? 178 ASN C CA  1 
ATOM   5663 C  C   . ASN C  1 178 ? 51.826  -8.002  -26.416 1.00 24.70  ? 178 ASN C C   1 
ATOM   5664 O  O   . ASN C  1 178 ? 50.922  -8.751  -26.071 1.00 24.35  ? 178 ASN C O   1 
ATOM   5665 C  CB  . ASN C  1 178 ? 53.634  -9.609  -26.084 1.00 26.27  ? 178 ASN C CB  1 
ATOM   5666 C  CG  . ASN C  1 178 ? 53.672  -10.049 -27.514 1.00 30.07  ? 178 ASN C CG  1 
ATOM   5667 O  OD1 . ASN C  1 178 ? 53.417  -9.239  -28.484 1.00 24.85  ? 178 ASN C OD1 1 
ATOM   5668 N  ND2 . ASN C  1 178 ? 53.763  -11.345 -27.694 1.00 31.78  ? 178 ASN C ND2 1 
ATOM   5669 N  N   . ILE C  1 179 ? 51.632  -6.875  -27.132 1.00 21.68  ? 179 ILE C N   1 
ATOM   5670 C  CA  . ILE C  1 179 ? 50.304  -6.454  -27.507 1.00 19.78  ? 179 ILE C CA  1 
ATOM   5671 C  C   . ILE C  1 179 ? 49.710  -7.567  -28.409 1.00 18.85  ? 179 ILE C C   1 
ATOM   5672 O  O   . ILE C  1 179 ? 48.458  -7.652  -28.531 1.00 20.04  ? 179 ILE C O   1 
ATOM   5673 C  CB  . ILE C  1 179 ? 50.408  -5.116  -28.228 1.00 19.25  ? 179 ILE C CB  1 
ATOM   5674 C  CG1 . ILE C  1 179 ? 51.065  -4.021  -27.370 1.00 23.24  ? 179 ILE C CG1 1 
ATOM   5675 C  CG2 . ILE C  1 179 ? 49.011  -4.704  -28.730 1.00 21.84  ? 179 ILE C CG2 1 
ATOM   5676 C  CD1 . ILE C  1 179 ? 50.302  -3.792  -26.013 1.00 23.30  ? 179 ILE C CD1 1 
ATOM   5677 N  N   . GLU C  1 180 ? 50.430  -8.388  -29.115 1.00 19.82  ? 180 GLU C N   1 
ATOM   5678 C  CA  . GLU C  1 180 ? 49.988  -9.461  -29.937 1.00 19.88  ? 180 GLU C CA  1 
ATOM   5679 C  C   . GLU C  1 180 ? 49.143  -10.416 -29.134 1.00 22.26  ? 180 GLU C C   1 
ATOM   5680 O  O   . GLU C  1 180 ? 48.291  -11.083 -29.732 1.00 23.29  ? 180 GLU C O   1 
ATOM   5681 C  CB  . GLU C  1 180 ? 51.115  -10.109 -30.717 1.00 26.61  ? 180 GLU C CB  1 
ATOM   5682 C  CG  . GLU C  1 180 ? 50.515  -10.878 -31.858 1.00 29.24  ? 180 GLU C CG  1 
ATOM   5683 C  CD  . GLU C  1 180 ? 51.536  -11.407 -32.850 1.00 31.74  ? 180 GLU C CD  1 
ATOM   5684 O  OE1 . GLU C  1 180 ? 52.702  -11.026 -32.726 1.00 30.76  ? 180 GLU C OE1 1 
ATOM   5685 O  OE2 . GLU C  1 180 ? 51.162  -12.219 -33.736 1.00 34.44  ? 180 GLU C OE2 1 
ATOM   5686 N  N   . GLU C  1 181 ? 49.317  -10.467 -27.806 1.00 21.08  ? 181 GLU C N   1 
ATOM   5687 C  CA  . GLU C  1 181 ? 48.535  -11.426 -27.043 1.00 22.67  ? 181 GLU C CA  1 
ATOM   5688 C  C   . GLU C  1 181 ? 47.055  -10.962 -26.908 1.00 22.45  ? 181 GLU C C   1 
ATOM   5689 O  O   . GLU C  1 181 ? 46.271  -11.749 -26.383 1.00 22.69  ? 181 GLU C O   1 
ATOM   5690 C  CB  . GLU C  1 181 ? 49.100  -11.502 -25.642 1.00 27.96  ? 181 GLU C CB  1 
ATOM   5691 C  CG  . GLU C  1 181 ? 50.524  -12.169 -25.512 1.00 38.86  ? 181 GLU C CG  1 
ATOM   5692 C  CD  . GLU C  1 181 ? 51.111  -12.040 -24.068 1.00 44.10  ? 181 GLU C CD  1 
ATOM   5693 O  OE1 . GLU C  1 181 ? 50.349  -11.722 -23.122 1.00 55.47  ? 181 GLU C OE1 1 
ATOM   5694 O  OE2 . GLU C  1 181 ? 52.378  -12.197 -23.892 1.00 55.98  ? 181 GLU C OE2 1 
ATOM   5695 N  N   . LEU C  1 182 ? 46.746  -9.713  -27.213 1.00 18.31  ? 182 LEU C N   1 
ATOM   5696 C  CA  . LEU C  1 182 ? 45.327  -9.194  -27.259 1.00 18.16  ? 182 LEU C CA  1 
ATOM   5697 C  C   . LEU C  1 182 ? 44.593  -9.703  -28.424 1.00 20.38  ? 182 LEU C C   1 
ATOM   5698 O  O   . LEU C  1 182 ? 43.356  -9.667  -28.492 1.00 20.56  ? 182 LEU C O   1 
ATOM   5699 C  CB  . LEU C  1 182 ? 45.330  -7.643  -27.137 1.00 18.64  ? 182 LEU C CB  1 
ATOM   5700 C  CG  . LEU C  1 182 ? 46.046  -7.064  -25.911 1.00 17.58  ? 182 LEU C CG  1 
ATOM   5701 C  CD1 . LEU C  1 182 ? 46.040  -5.535  -25.905 1.00 21.31  ? 182 LEU C CD1 1 
ATOM   5702 C  CD2 . LEU C  1 182 ? 45.589  -7.681  -24.541 1.00 20.97  ? 182 LEU C CD2 1 
ATOM   5703 N  N   . LEU C  1 183 ? 45.310  -10.254 -29.435 1.00 18.46  ? 183 LEU C N   1 
ATOM   5704 C  CA  . LEU C  1 183 ? 44.669  -10.612 -30.753 1.00 19.10  ? 183 LEU C CA  1 
ATOM   5705 C  C   . LEU C  1 183 ? 44.088  -12.013 -30.633 1.00 18.83  ? 183 LEU C C   1 
ATOM   5706 O  O   . LEU C  1 183 ? 44.597  -12.849 -29.782 1.00 22.51  ? 183 LEU C O   1 
ATOM   5707 C  CB  . LEU C  1 183 ? 45.640  -10.520 -32.005 1.00 19.94  ? 183 LEU C CB  1 
ATOM   5708 C  CG  . LEU C  1 183 ? 46.318  -9.194  -32.125 1.00 21.00  ? 183 LEU C CG  1 
ATOM   5709 C  CD1 . LEU C  1 183 ? 47.303  -9.204  -33.274 1.00 29.19  ? 183 LEU C CD1 1 
ATOM   5710 C  CD2 . LEU C  1 183 ? 45.279  -8.067  -32.180 1.00 23.27  ? 183 LEU C CD2 1 
ATOM   5711 N  N   . PRO C  1 184 ? 43.070  -12.350 -31.377 1.00 19.03  ? 184 PRO C N   1 
ATOM   5712 C  CA  . PRO C  1 184 ? 42.459  -13.646 -31.348 1.00 17.71  ? 184 PRO C CA  1 
ATOM   5713 C  C   . PRO C  1 184 ? 43.244  -14.693 -31.999 1.00 21.88  ? 184 PRO C C   1 
ATOM   5714 O  O   . PRO C  1 184 ? 44.327  -14.458 -32.636 1.00 23.93  ? 184 PRO C O   1 
ATOM   5715 C  CB  . PRO C  1 184 ? 41.076  -13.359 -31.958 1.00 25.06  ? 184 PRO C CB  1 
ATOM   5716 C  CG  . PRO C  1 184 ? 41.523  -12.396 -32.941 1.00 20.28  ? 184 PRO C CG  1 
ATOM   5717 C  CD  . PRO C  1 184 ? 42.362  -11.425 -32.271 1.00 18.40  ? 184 PRO C CD  1 
ATOM   5718 N  N   . GLU C  1 185 ? 42.694  -15.900 -31.988 1.00 24.81  ? 185 GLU C N   1 
ATOM   5719 C  CA  . GLU C  1 185 ? 43.057  -17.036 -32.873 1.00 26.17  ? 185 GLU C CA  1 
ATOM   5720 C  C   . GLU C  1 185 ? 42.760  -16.708 -34.363 1.00 24.58  ? 185 GLU C C   1 
ATOM   5721 O  O   . GLU C  1 185 ? 41.748  -16.016 -34.743 1.00 26.79  ? 185 GLU C O   1 
ATOM   5722 C  CB  . GLU C  1 185 ? 42.354  -18.328 -32.537 1.00 31.37  ? 185 GLU C CB  1 
ATOM   5723 C  CG  . GLU C  1 185 ? 42.617  -18.908 -31.076 1.00 43.92  ? 185 GLU C CG  1 
ATOM   5724 C  CD  . GLU C  1 185 ? 44.045  -19.043 -30.575 1.00 53.58  ? 185 GLU C CD  1 
ATOM   5725 O  OE1 . GLU C  1 185 ? 45.032  -18.693 -31.245 1.00 71.87  ? 185 GLU C OE1 1 
ATOM   5726 O  OE2 . GLU C  1 185 ? 44.191  -19.531 -29.431 1.00 83.70  ? 185 GLU C OE2 1 
ATOM   5727 N  N   . ARG C  1 186 ? 43.701  -17.251 -35.153 1.00 26.04  ? 186 ARG C N   1 
ATOM   5728 C  CA  . ARG C  1 186 ? 43.629  -17.260 -36.616 1.00 30.99  ? 186 ARG C CA  1 
ATOM   5729 C  C   . ARG C  1 186 ? 43.460  -15.857 -37.120 1.00 22.64  ? 186 ARG C C   1 
ATOM   5730 O  O   . ARG C  1 186 ? 42.456  -15.438 -37.810 1.00 24.35  ? 186 ARG C O   1 
ATOM   5731 C  CB  . ARG C  1 186 ? 42.554  -18.171 -37.068 1.00 28.63  ? 186 ARG C CB  1 
ATOM   5732 C  CG  . ARG C  1 186 ? 42.631  -19.534 -36.517 1.00 34.94  ? 186 ARG C CG  1 
ATOM   5733 C  CD  . ARG C  1 186 ? 41.641  -20.544 -37.136 1.00 40.20  ? 186 ARG C CD  1 
ATOM   5734 N  NE  . ARG C  1 186 ? 40.259  -20.531 -36.515 1.00 56.00  ? 186 ARG C NE  1 
ATOM   5735 C  CZ  . ARG C  1 186 ? 39.929  -20.789 -35.222 1.00 64.22  ? 186 ARG C CZ  1 
ATOM   5736 N  NH1 . ARG C  1 186 ? 40.867  -21.018 -34.273 1.00 65.54  ? 186 ARG C NH1 1 
ATOM   5737 N  NH2 . ARG C  1 186 ? 38.622  -20.761 -34.877 1.00 60.38  ? 186 ARG C NH2 1 
ATOM   5738 N  N   . THR C  1 187 ? 44.391  -15.030 -36.748 1.00 21.38  ? 187 THR C N   1 
ATOM   5739 C  CA  . THR C  1 187 ? 44.359  -13.679 -37.265 1.00 19.99  ? 187 THR C CA  1 
ATOM   5740 C  C   . THR C  1 187 ? 44.247  -13.551 -38.785 1.00 23.41  ? 187 THR C C   1 
ATOM   5741 O  O   . THR C  1 187 ? 43.918  -12.512 -39.236 1.00 21.61  ? 187 THR C O   1 
ATOM   5742 C  CB  . THR C  1 187 ? 45.448  -12.752 -36.714 1.00 21.96  ? 187 THR C CB  1 
ATOM   5743 O  OG1 . THR C  1 187 ? 46.692  -13.309 -36.905 1.00 26.46  ? 187 THR C OG1 1 
ATOM   5744 C  CG2 . THR C  1 187 ? 45.181  -12.536 -35.247 1.00 23.52  ? 187 THR C CG2 1 
ATOM   5745 N  N   . ALA C  1 188 ? 44.570  -14.631 -39.517 1.00 21.18  ? 188 ALA C N   1 
ATOM   5746 C  CA  . ALA C  1 188 ? 44.469  -14.570 -40.988 1.00 19.64  ? 188 ALA C CA  1 
ATOM   5747 C  C   . ALA C  1 188 ? 42.985  -14.430 -41.441 1.00 17.71  ? 188 ALA C C   1 
ATOM   5748 O  O   . ALA C  1 188 ? 42.752  -14.073 -42.636 1.00 19.12  ? 188 ALA C O   1 
ATOM   5749 C  CB  . ALA C  1 188 ? 45.126  -15.809 -41.590 1.00 26.22  ? 188 ALA C CB  1 
ATOM   5750 N  N   . GLU C  1 189 ? 42.036  -14.760 -40.576 1.00 19.01  ? 189 GLU C N   1 
ATOM   5751 C  CA  . GLU C  1 189 ? 40.606  -14.609 -40.957 1.00 19.25  ? 189 GLU C CA  1 
ATOM   5752 C  C   . GLU C  1 189 ? 40.072  -13.255 -40.466 1.00 18.06  ? 189 GLU C C   1 
ATOM   5753 O  O   . GLU C  1 189 ? 40.025  -13.014 -39.237 1.00 17.77  ? 189 GLU C O   1 
ATOM   5754 C  CB  . GLU C  1 189 ? 39.757  -15.684 -40.243 1.00 22.39  ? 189 GLU C CB  1 
ATOM   5755 C  CG  . GLU C  1 189 ? 40.203  -17.108 -40.689 1.00 28.77  ? 189 GLU C CG  1 
ATOM   5756 C  CD  . GLU C  1 189 ? 39.642  -18.257 -39.886 1.00 35.44  ? 189 GLU C CD  1 
ATOM   5757 O  OE1 . GLU C  1 189 ? 38.828  -18.123 -38.955 1.00 32.77  ? 189 GLU C OE1 1 
ATOM   5758 O  OE2 . GLU C  1 189 ? 40.060  -19.442 -40.147 1.00 47.27  ? 189 GLU C OE2 1 
ATOM   5759 N  N   . TYR C  1 190 ? 39.644  -12.415 -41.415 1.00 16.51  ? 190 TYR C N   1 
ATOM   5760 C  CA  . TYR C  1 190 ? 39.200  -11.111 -41.058 1.00 15.53  ? 190 TYR C CA  1 
ATOM   5761 C  C   . TYR C  1 190 ? 38.223  -10.568 -42.103 1.00 14.20  ? 190 TYR C C   1 
ATOM   5762 O  O   . TYR C  1 190 ? 38.229  -10.961 -43.256 1.00 15.49  ? 190 TYR C O   1 
ATOM   5763 C  CB  . TYR C  1 190 ? 40.413  -10.163 -40.788 1.00 15.91  ? 190 TYR C CB  1 
ATOM   5764 C  CG  . TYR C  1 190 ? 41.345  -9.979  -41.915 1.00 14.18  ? 190 TYR C CG  1 
ATOM   5765 C  CD1 . TYR C  1 190 ? 41.086  -9.076  -42.910 1.00 15.56  ? 190 TYR C CD1 1 
ATOM   5766 C  CD2 . TYR C  1 190 ? 42.573  -10.699 -41.927 1.00 17.01  ? 190 TYR C CD2 1 
ATOM   5767 C  CE1 . TYR C  1 190 ? 42.029  -8.911  -43.995 1.00 15.84  ? 190 TYR C CE1 1 
ATOM   5768 C  CE2 . TYR C  1 190 ? 43.474  -10.563 -42.960 1.00 17.15  ? 190 TYR C CE2 1 
ATOM   5769 C  CZ  . TYR C  1 190 ? 43.182  -9.664  -43.976 1.00 17.30  ? 190 TYR C CZ  1 
ATOM   5770 O  OH  . TYR C  1 190 ? 44.138  -9.407  -44.995 1.00 17.69  ? 190 TYR C OH  1 
ATOM   5771 N  N   . TYR C  1 191 ? 37.469  -9.575  -41.628 1.00 13.63  ? 191 TYR C N   1 
ATOM   5772 C  CA  . TYR C  1 191 ? 36.667  -8.653  -42.465 1.00 13.03  ? 191 TYR C CA  1 
ATOM   5773 C  C   . TYR C  1 191 ? 37.418  -7.384  -42.738 1.00 11.61  ? 191 TYR C C   1 
ATOM   5774 O  O   . TYR C  1 191 ? 38.132  -6.895  -41.829 1.00 14.08  ? 191 TYR C O   1 
ATOM   5775 C  CB  . TYR C  1 191 ? 35.396  -8.265  -41.687 1.00 13.69  ? 191 TYR C CB  1 
ATOM   5776 C  CG  . TYR C  1 191 ? 34.567  -9.392  -41.139 1.00 13.52  ? 191 TYR C CG  1 
ATOM   5777 C  CD1 . TYR C  1 191 ? 33.516  -9.946  -41.879 1.00 13.71  ? 191 TYR C CD1 1 
ATOM   5778 C  CD2 . TYR C  1 191 ? 34.730  -9.814  -39.812 1.00 13.83  ? 191 TYR C CD2 1 
ATOM   5779 C  CE1 . TYR C  1 191 ? 32.690  -10.967 -41.421 1.00 16.01  ? 191 TYR C CE1 1 
ATOM   5780 C  CE2 . TYR C  1 191 ? 33.882  -10.813 -39.284 1.00 16.19  ? 191 TYR C CE2 1 
ATOM   5781 C  CZ  . TYR C  1 191 ? 32.867  -11.335 -40.076 1.00 16.43  ? 191 TYR C CZ  1 
ATOM   5782 O  OH  . TYR C  1 191 ? 32.005  -12.314 -39.517 1.00 18.70  ? 191 TYR C OH  1 
ATOM   5783 N  N   . ARG C  1 192 ? 37.245  -6.823  -43.947 1.00 13.00  ? 192 ARG C N   1 
ATOM   5784 C  CA  . ARG C  1 192 ? 37.892  -5.591  -44.296 1.00 12.91  ? 192 ARG C CA  1 
ATOM   5785 C  C   . ARG C  1 192 ? 36.986  -4.599  -45.010 1.00 11.37  ? 192 ARG C C   1 
ATOM   5786 O  O   . ARG C  1 192 ? 36.237  -5.051  -45.922 1.00 12.30  ? 192 ARG C O   1 
ATOM   5787 C  CB  . ARG C  1 192 ? 39.060  -5.943  -45.311 1.00 13.49  ? 192 ARG C CB  1 
ATOM   5788 C  CG  . ARG C  1 192 ? 39.679  -4.790  -46.062 1.00 14.44  ? 192 ARG C CG  1 
ATOM   5789 C  CD  . ARG C  1 192 ? 40.456  -3.798  -45.230 1.00 14.85  ? 192 ARG C CD  1 
ATOM   5790 N  NE  . ARG C  1 192 ? 41.430  -4.448  -44.342 1.00 14.95  ? 192 ARG C NE  1 
ATOM   5791 C  CZ  . ARG C  1 192 ? 42.580  -4.997  -44.726 1.00 16.17  ? 192 ARG C CZ  1 
ATOM   5792 N  NH1 . ARG C  1 192 ? 42.939  -4.955  -46.005 1.00 17.43  ? 192 ARG C NH1 1 
ATOM   5793 N  NH2 . ARG C  1 192 ? 43.373  -5.578  -43.827 1.00 17.93  ? 192 ARG C NH2 1 
ATOM   5794 N  N   . TYR C  1 193 ? 36.978  -3.376  -44.589 1.00 10.69  ? 193 TYR C N   1 
ATOM   5795 C  CA  . TYR C  1 193 ? 36.220  -2.374  -45.369 1.00 11.64  ? 193 TYR C CA  1 
ATOM   5796 C  C   . TYR C  1 193 ? 36.804  -1.019  -45.057 1.00 10.75  ? 193 TYR C C   1 
ATOM   5797 O  O   . TYR C  1 193 ? 37.511  -0.828  -44.006 1.00 12.05  ? 193 TYR C O   1 
ATOM   5798 C  CB  . TYR C  1 193 ? 34.702  -2.431  -45.037 1.00 11.88  ? 193 TYR C CB  1 
ATOM   5799 C  CG  . TYR C  1 193 ? 34.282  -1.878  -43.650 1.00 10.38  ? 193 TYR C CG  1 
ATOM   5800 C  CD1 . TYR C  1 193 ? 34.506  -2.645  -42.512 1.00 11.05  ? 193 TYR C CD1 1 
ATOM   5801 C  CD2 . TYR C  1 193 ? 33.790  -0.610  -43.550 1.00 11.22  ? 193 TYR C CD2 1 
ATOM   5802 C  CE1 . TYR C  1 193 ? 34.184  -2.112  -41.254 1.00 11.05  ? 193 TYR C CE1 1 
ATOM   5803 C  CE2 . TYR C  1 193 ? 33.430  -0.107  -42.307 1.00 11.29  ? 193 TYR C CE2 1 
ATOM   5804 C  CZ  . TYR C  1 193 ? 33.634  -0.860  -41.170 1.00 10.50  ? 193 TYR C CZ  1 
ATOM   5805 O  OH  . TYR C  1 193 ? 33.332  -0.279  -39.943 1.00 11.31  ? 193 TYR C OH  1 
ATOM   5806 N  N   . ARG C  1 194 ? 36.477  -0.029  -45.883 1.00 11.65  ? 194 ARG C N   1 
ATOM   5807 C  CA  . ARG C  1 194 ? 36.952  1.349   -45.706 1.00 11.81  ? 194 ARG C CA  1 
ATOM   5808 C  C   . ARG C  1 194 ? 35.834  2.054   -44.861 1.00 11.99  ? 194 ARG C C   1 
ATOM   5809 O  O   . ARG C  1 194 ? 34.637  2.023   -45.249 1.00 12.72  ? 194 ARG C O   1 
ATOM   5810 C  CB  . ARG C  1 194 ? 37.077  2.067   -47.004 1.00 15.11  ? 194 ARG C CB  1 
ATOM   5811 C  CG  . ARG C  1 194 ? 38.233  1.513   -47.819 1.00 18.24  ? 194 ARG C CG  1 
ATOM   5812 C  CD  . ARG C  1 194 ? 38.816  2.370   -48.920 1.00 37.37  ? 194 ARG C CD  1 
ATOM   5813 N  NE  . ARG C  1 194 ? 39.997  1.654   -49.395 1.00 48.91  ? 194 ARG C NE  1 
ATOM   5814 C  CZ  . ARG C  1 194 ? 41.244  1.875   -48.985 1.00 58.04  ? 194 ARG C CZ  1 
ATOM   5815 N  NH1 . ARG C  1 194 ? 41.517  2.845   -48.119 1.00 37.85  ? 194 ARG C NH1 1 
ATOM   5816 N  NH2 . ARG C  1 194 ? 42.227  1.128   -49.465 1.00 49.10  ? 194 ARG C NH2 1 
ATOM   5817 N  N   . GLY C  1 195 ? 36.236  2.700   -43.770 1.00 11.34  ? 195 GLY C N   1 
ATOM   5818 C  CA  . GLY C  1 195 ? 35.223  3.389   -42.928 1.00 11.33  ? 195 GLY C CA  1 
ATOM   5819 C  C   . GLY C  1 195 ? 35.844  4.590   -42.265 1.00 12.04  ? 195 GLY C C   1 
ATOM   5820 O  O   . GLY C  1 195 ? 36.684  5.303   -42.798 1.00 12.22  ? 195 GLY C O   1 
ATOM   5821 N  N   . SER C  1 196 ? 35.397  4.807   -41.000 1.00 11.49  ? 196 SER C N   1 
ATOM   5822 C  CA  . SER C  1 196 ? 35.670  6.104   -40.331 1.00 11.90  ? 196 SER C CA  1 
ATOM   5823 C  C   . SER C  1 196 ? 36.080  5.807   -38.904 1.00 12.04  ? 196 SER C C   1 
ATOM   5824 O  O   . SER C  1 196 ? 35.918  4.701   -38.381 1.00 11.91  ? 196 SER C O   1 
ATOM   5825 C  CB  . SER C  1 196 ? 34.407  6.976   -40.288 1.00 11.64  ? 196 SER C CB  1 
ATOM   5826 O  OG  . SER C  1 196 ? 33.426  6.489   -39.368 1.00 11.30  ? 196 SER C OG  1 
ATOM   5827 N  N   . LEU C  1 197 ? 36.545  6.874   -38.255 1.00 11.59  ? 197 LEU C N   1 
ATOM   5828 C  CA  . LEU C  1 197 ? 36.593  6.799   -36.763 1.00 12.67  ? 197 LEU C CA  1 
ATOM   5829 C  C   . LEU C  1 197 ? 35.144  6.562   -36.313 1.00 11.83  ? 197 LEU C C   1 
ATOM   5830 O  O   . LEU C  1 197 ? 34.215  7.187   -36.849 1.00 12.37  ? 197 LEU C O   1 
ATOM   5831 C  CB  . LEU C  1 197 ? 37.088  8.137   -36.176 1.00 13.67  ? 197 LEU C CB  1 
ATOM   5832 C  CG  . LEU C  1 197 ? 38.564  8.448   -36.210 1.00 16.11  ? 197 LEU C CG  1 
ATOM   5833 C  CD1 . LEU C  1 197 ? 39.053  8.945   -37.594 1.00 18.50  ? 197 LEU C CD1 1 
ATOM   5834 C  CD2 . LEU C  1 197 ? 38.818  9.545   -35.174 1.00 18.13  ? 197 LEU C CD2 1 
ATOM   5835 N  N   . THR C  1 198 ? 34.968  5.845   -35.211 1.00 12.01  ? 198 THR C N   1 
ATOM   5836 C  CA  . THR C  1 198 ? 33.652  5.672   -34.606 1.00 12.06  ? 198 THR C CA  1 
ATOM   5837 C  C   . THR C  1 198 ? 33.342  6.691   -33.549 1.00 12.15  ? 198 THR C C   1 
ATOM   5838 O  O   . THR C  1 198 ? 32.283  6.650   -32.920 1.00 12.57  ? 198 THR C O   1 
ATOM   5839 C  CB  . THR C  1 198 ? 33.484  4.281   -34.020 1.00 12.15  ? 198 THR C CB  1 
ATOM   5840 O  OG1 . THR C  1 198 ? 34.362  4.203   -32.911 1.00 12.38  ? 198 THR C OG1 1 
ATOM   5841 C  CG2 . THR C  1 198 ? 33.796  3.141   -35.001 1.00 12.80  ? 198 THR C CG2 1 
ATOM   5842 N  N   . THR C  1 199 ? 34.323  7.568   -33.299 1.00 12.56  ? 199 THR C N   1 
ATOM   5843 C  CA  . THR C  1 199 ? 34.109  8.730   -32.418 1.00 12.57  ? 199 THR C CA  1 
ATOM   5844 C  C   . THR C  1 199 ? 34.309  10.001  -33.179 1.00 12.41  ? 199 THR C C   1 
ATOM   5845 O  O   . THR C  1 199 ? 35.025  9.941   -34.205 1.00 14.03  ? 199 THR C O   1 
ATOM   5846 C  CB  . THR C  1 199 ? 35.145  8.764   -31.296 1.00 13.77  ? 199 THR C CB  1 
ATOM   5847 O  OG1 . THR C  1 199 ? 36.479  8.918   -31.783 1.00 15.65  ? 199 THR C OG1 1 
ATOM   5848 C  CG2 . THR C  1 199 ? 35.164  7.421   -30.530 1.00 15.20  ? 199 THR C CG2 1 
ATOM   5849 N  N   . PRO C  1 200 ? 33.909  11.151  -32.639 1.00 12.36  ? 200 PRO C N   1 
ATOM   5850 C  CA  . PRO C  1 200 ? 34.314  12.397  -33.256 1.00 14.31  ? 200 PRO C CA  1 
ATOM   5851 C  C   . PRO C  1 200 ? 35.825  12.426  -33.421 1.00 14.69  ? 200 PRO C C   1 
ATOM   5852 O  O   . PRO C  1 200 ? 36.526  11.913  -32.506 1.00 16.16  ? 200 PRO C O   1 
ATOM   5853 C  CB  . PRO C  1 200 ? 33.804  13.461  -32.219 1.00 14.78  ? 200 PRO C CB  1 
ATOM   5854 C  CG  . PRO C  1 200 ? 32.524  12.832  -31.670 1.00 14.78  ? 200 PRO C CG  1 
ATOM   5855 C  CD  . PRO C  1 200 ? 32.940  11.377  -31.534 1.00 14.10  ? 200 PRO C CD  1 
ATOM   5856 N  N   . PRO C  1 201 ? 36.349  13.048  -34.454 1.00 14.26  ? 201 PRO C N   1 
ATOM   5857 C  CA  . PRO C  1 201 ? 35.616  13.770  -35.469 1.00 14.88  ? 201 PRO C CA  1 
ATOM   5858 C  C   . PRO C  1 201 ? 35.025  12.891  -36.625 1.00 12.55  ? 201 PRO C C   1 
ATOM   5859 O  O   . PRO C  1 201 ? 34.546  13.473  -37.591 1.00 14.50  ? 201 PRO C O   1 
ATOM   5860 C  CB  . PRO C  1 201 ? 36.673  14.740  -36.115 1.00 15.40  ? 201 PRO C CB  1 
ATOM   5861 C  CG  . PRO C  1 201 ? 37.736  14.825  -35.118 1.00 18.45  ? 201 PRO C CG  1 
ATOM   5862 C  CD  . PRO C  1 201 ? 37.790  13.417  -34.506 1.00 17.31  ? 201 PRO C CD  1 
ATOM   5863 N  N   . CYS C  1 202 ? 35.075  11.552  -36.471 1.00 12.54  ? 202 CYS C N   1 
ATOM   5864 C  CA  . CYS C  1 202 ? 34.393  10.681  -37.419 1.00 12.17  ? 202 CYS C CA  1 
ATOM   5865 C  C   . CYS C  1 202 ? 34.979  10.739  -38.829 1.00 12.05  ? 202 CYS C C   1 
ATOM   5866 O  O   . CYS C  1 202 ? 34.289  10.429  -39.832 1.00 13.00  ? 202 CYS C O   1 
ATOM   5867 C  CB  . CYS C  1 202 ? 32.853  10.890  -37.528 1.00 13.18  ? 202 CYS C CB  1 
ATOM   5868 S  SG  . CYS C  1 202 ? 31.976  10.846  -35.969 1.00 13.29  ? 202 CYS C SG  1 
ATOM   5869 N  N   . ASN C  1 203 ? 36.268  11.074  -38.959 1.00 12.91  ? 203 ASN C N   1 
ATOM   5870 C  CA  . ASN C  1 203 ? 36.804  11.264  -40.311 1.00 14.17  ? 203 ASN C CA  1 
ATOM   5871 C  C   . ASN C  1 203 ? 36.764  9.919   -41.062 1.00 14.12  ? 203 ASN C C   1 
ATOM   5872 O  O   . ASN C  1 203 ? 37.023  8.851   -40.477 1.00 13.00  ? 203 ASN C O   1 
ATOM   5873 C  CB  . ASN C  1 203 ? 38.290  11.680  -40.245 1.00 15.25  ? 203 ASN C CB  1 
ATOM   5874 C  CG  . ASN C  1 203 ? 38.436  12.882  -39.333 1.00 15.91  ? 203 ASN C CG  1 
ATOM   5875 O  OD1 . ASN C  1 203 ? 38.454  12.739  -38.122 1.00 18.90  ? 203 ASN C OD1 1 
ATOM   5876 N  ND2 . ASN C  1 203 ? 38.373  14.112  -39.884 1.00 19.57  ? 203 ASN C ND2 1 
ATOM   5877 N  N   . PRO C  1 204 ? 36.464  10.008  -42.363 1.00 13.55  ? 204 PRO C N   1 
ATOM   5878 C  CA  . PRO C  1 204 ? 36.274  8.756   -43.184 1.00 14.06  ? 204 PRO C CA  1 
ATOM   5879 C  C   . PRO C  1 204 ? 37.647  8.246   -43.695 1.00 12.75  ? 204 PRO C C   1 
ATOM   5880 O  O   . PRO C  1 204 ? 37.836  8.102   -44.923 1.00 15.59  ? 204 PRO C O   1 
ATOM   5881 C  CB  . PRO C  1 204 ? 35.364  9.242   -44.324 1.00 14.56  ? 204 PRO C CB  1 
ATOM   5882 C  CG  . PRO C  1 204 ? 35.791  10.662  -44.528 1.00 16.62  ? 204 PRO C CG  1 
ATOM   5883 C  CD  . PRO C  1 204 ? 36.016  11.220  -43.104 1.00 15.39  ? 204 PRO C CD  1 
ATOM   5884 N  N   . THR C  1 205 ? 38.591  8.031   -42.769 1.00 13.39  ? 205 THR C N   1 
ATOM   5885 C  CA  . THR C  1 205 ? 39.987  7.837   -43.101 1.00 13.71  ? 205 THR C CA  1 
ATOM   5886 C  C   . THR C  1 205 ? 40.565  6.547   -42.561 1.00 13.82  ? 205 THR C C   1 
ATOM   5887 O  O   . THR C  1 205 ? 41.791  6.310   -42.496 1.00 15.58  ? 205 THR C O   1 
ATOM   5888 C  CB  . THR C  1 205 ? 40.829  9.060   -42.540 1.00 14.91  ? 205 THR C CB  1 
ATOM   5889 O  OG1 . THR C  1 205 ? 40.521  8.994   -41.129 1.00 16.45  ? 205 THR C OG1 1 
ATOM   5890 C  CG2 . THR C  1 205 ? 40.368  10.415  -43.175 1.00 18.75  ? 205 THR C CG2 1 
ATOM   5891 N  N   . VAL C  1 206 ? 39.649  5.626   -42.160 1.00 13.87  ? 206 VAL C N   1 
ATOM   5892 C  CA  . VAL C  1 206 ? 40.085  4.380   -41.505 1.00 12.77  ? 206 VAL C CA  1 
ATOM   5893 C  C   . VAL C  1 206 ? 39.949  3.142   -42.359 1.00 12.08  ? 206 VAL C C   1 
ATOM   5894 O  O   . VAL C  1 206 ? 38.838  2.830   -42.841 1.00 14.24  ? 206 VAL C O   1 
ATOM   5895 C  CB  . VAL C  1 206 ? 39.304  4.131   -40.178 1.00 13.05  ? 206 VAL C CB  1 
ATOM   5896 C  CG1 . VAL C  1 206 ? 39.759  2.774   -39.555 1.00 13.32  ? 206 VAL C CG1 1 
ATOM   5897 C  CG2 . VAL C  1 206 ? 39.486  5.271   -39.183 1.00 13.90  ? 206 VAL C CG2 1 
ATOM   5898 N  N   . LEU C  1 207 ? 41.014  2.392   -42.552 1.00 12.88  ? 207 LEU C N   1 
ATOM   5899 C  CA  . LEU C  1 207 ? 40.952  1.039   -43.148 1.00 13.76  ? 207 LEU C CA  1 
ATOM   5900 C  C   . LEU C  1 207 ? 40.659  0.076   -41.992 1.00 11.68  ? 207 LEU C C   1 
ATOM   5901 O  O   . LEU C  1 207 ? 41.548  -0.090  -41.109 1.00 13.29  ? 207 LEU C O   1 
ATOM   5902 C  CB  . LEU C  1 207 ? 42.297  0.733   -43.841 1.00 15.10  ? 207 LEU C CB  1 
ATOM   5903 C  CG  . LEU C  1 207 ? 42.260  -0.473  -44.704 1.00 18.47  ? 207 LEU C CG  1 
ATOM   5904 C  CD1 . LEU C  1 207 ? 41.246  -0.298  -45.853 1.00 25.32  ? 207 LEU C CD1 1 
ATOM   5905 C  CD2 . LEU C  1 207 ? 43.645  -0.761  -45.311 1.00 32.79  ? 207 LEU C CD2 1 
ATOM   5906 N  N   . TRP C  1 208 ? 39.478  -0.513  -41.938 1.00 12.42  ? 208 TRP C N   1 
ATOM   5907 C  CA  . TRP C  1 208 ? 39.102  -1.421  -40.851 1.00 12.12  ? 208 TRP C CA  1 
ATOM   5908 C  C   . TRP C  1 208 ? 39.442  -2.839  -41.140 1.00 11.50  ? 208 TRP C C   1 
ATOM   5909 O  O   . TRP C  1 208 ? 39.230  -3.356  -42.270 1.00 13.25  ? 208 TRP C O   1 
ATOM   5910 C  CB  . TRP C  1 208 ? 37.587  -1.372  -40.610 1.00 11.90  ? 208 TRP C CB  1 
ATOM   5911 C  CG  . TRP C  1 208 ? 37.188  -0.139  -39.866 1.00 11.08  ? 208 TRP C CG  1 
ATOM   5912 C  CD1 . TRP C  1 208 ? 36.748  1.052   -40.333 1.00 11.66  ? 208 TRP C CD1 1 
ATOM   5913 C  CD2 . TRP C  1 208 ? 37.260  0.006   -38.420 1.00 11.28  ? 208 TRP C CD2 1 
ATOM   5914 N  NE1 . TRP C  1 208 ? 36.593  1.945   -39.306 1.00 11.84  ? 208 TRP C NE1 1 
ATOM   5915 C  CE2 . TRP C  1 208 ? 36.882  1.325   -38.119 1.00 12.39  ? 208 TRP C CE2 1 
ATOM   5916 C  CE3 . TRP C  1 208 ? 37.608  -0.845  -37.372 1.00 12.60  ? 208 TRP C CE3 1 
ATOM   5917 C  CZ2 . TRP C  1 208 ? 36.872  1.854   -36.804 1.00 13.07  ? 208 TRP C CZ2 1 
ATOM   5918 C  CZ3 . TRP C  1 208 ? 37.569  -0.306  -36.035 1.00 12.69  ? 208 TRP C CZ3 1 
ATOM   5919 C  CH2 . TRP C  1 208 ? 37.201  1.019   -35.809 1.00 13.39  ? 208 TRP C CH2 1 
ATOM   5920 N  N   . THR C  1 209 ? 40.013  -3.482  -40.146 1.00 12.65  ? 209 THR C N   1 
ATOM   5921 C  CA  . THR C  1 209 ? 40.231  -4.835  -40.133 1.00 12.27  ? 209 THR C CA  1 
ATOM   5922 C  C   . THR C  1 209 ? 39.615  -5.461  -38.883 1.00 12.58  ? 209 THR C C   1 
ATOM   5923 O  O   . THR C  1 209 ? 40.042  -5.102  -37.805 1.00 14.62  ? 209 THR C O   1 
ATOM   5924 C  CB  . THR C  1 209 ? 41.721  -5.253  -40.169 1.00 13.98  ? 209 THR C CB  1 
ATOM   5925 O  OG1 . THR C  1 209 ? 42.348  -4.748  -41.357 1.00 13.87  ? 209 THR C OG1 1 
ATOM   5926 C  CG2 . THR C  1 209 ? 41.970  -6.719  -40.113 1.00 15.56  ? 209 THR C CG2 1 
ATOM   5927 N  N   . VAL C  1 210 ? 38.555  -6.229  -39.028 1.00 12.89  ? 210 VAL C N   1 
ATOM   5928 C  CA  . VAL C  1 210 ? 37.802  -6.777  -37.885 1.00 12.90  ? 210 VAL C CA  1 
ATOM   5929 C  C   . VAL C  1 210 ? 38.030  -8.256  -37.873 1.00 13.09  ? 210 VAL C C   1 
ATOM   5930 O  O   . VAL C  1 210 ? 37.779  -8.984  -38.858 1.00 13.71  ? 210 VAL C O   1 
ATOM   5931 C  CB  . VAL C  1 210 ? 36.295  -6.550  -37.929 1.00 12.95  ? 210 VAL C CB  1 
ATOM   5932 C  CG1 . VAL C  1 210 ? 35.613  -7.131  -36.675 1.00 13.82  ? 210 VAL C CG1 1 
ATOM   5933 C  CG2 . VAL C  1 210 ? 35.999  -5.079  -38.079 1.00 13.85  ? 210 VAL C CG2 1 
ATOM   5934 N  N   . PHE C  1 211 ? 38.742  -8.800  -36.870 1.00 14.43  ? 211 PHE C N   1 
ATOM   5935 C  CA  . PHE C  1 211 ? 39.019  -10.222 -36.927 1.00 14.47  ? 211 PHE C CA  1 
ATOM   5936 C  C   . PHE C  1 211 ? 37.746  -11.040 -36.810 1.00 15.90  ? 211 PHE C C   1 
ATOM   5937 O  O   . PHE C  1 211 ? 36.814  -10.742 -36.074 1.00 16.16  ? 211 PHE C O   1 
ATOM   5938 C  CB  . PHE C  1 211 ? 40.054  -10.603 -35.796 1.00 15.80  ? 211 PHE C CB  1 
ATOM   5939 C  CG  . PHE C  1 211 ? 41.430  -9.964  -36.027 1.00 14.55  ? 211 PHE C CG  1 
ATOM   5940 C  CD1 . PHE C  1 211 ? 42.228  -10.385 -37.149 1.00 16.07  ? 211 PHE C CD1 1 
ATOM   5941 C  CD2 . PHE C  1 211 ? 41.885  -8.887  -35.285 1.00 18.62  ? 211 PHE C CD2 1 
ATOM   5942 C  CE1 . PHE C  1 211 ? 43.472  -9.757  -37.409 1.00 17.81  ? 211 PHE C CE1 1 
ATOM   5943 C  CE2 . PHE C  1 211 ? 43.121  -8.303  -35.533 1.00 18.49  ? 211 PHE C CE2 1 
ATOM   5944 C  CZ  . PHE C  1 211 ? 43.889  -8.742  -36.576 1.00 19.39  ? 211 PHE C CZ  1 
ATOM   5945 N  N   . ARG C  1 212 ? 37.743  -12.151 -37.502 1.00 15.81  ? 212 ARG C N   1 
ATOM   5946 C  CA  . ARG C  1 212 ? 36.564  -12.991 -37.548 1.00 16.37  ? 212 ARG C CA  1 
ATOM   5947 C  C   . ARG C  1 212 ? 36.234  -13.617 -36.204 1.00 17.12  ? 212 ARG C C   1 
ATOM   5948 O  O   . ARG C  1 212 ? 35.104  -13.774 -35.802 1.00 17.88  ? 212 ARG C O   1 
ATOM   5949 C  CB  . ARG C  1 212 ? 36.662  -14.054 -38.560 1.00 16.02  ? 212 ARG C CB  1 
ATOM   5950 C  CG  . ARG C  1 212 ? 35.526  -15.017 -38.690 1.00 20.81  ? 212 ARG C CG  1 
ATOM   5951 C  CD  . ARG C  1 212 ? 35.818  -16.189 -39.569 1.00 25.16  ? 212 ARG C CD  1 
ATOM   5952 N  NE  . ARG C  1 212 ? 34.625  -16.800 -40.030 1.00 31.30  ? 212 ARG C NE  1 
ATOM   5953 C  CZ  . ARG C  1 212 ? 34.532  -17.675 -41.058 1.00 34.91  ? 212 ARG C CZ  1 
ATOM   5954 N  NH1 . ARG C  1 212 ? 35.630  -18.271 -41.547 1.00 49.30  ? 212 ARG C NH1 1 
ATOM   5955 N  NH2 . ARG C  1 212 ? 33.371  -18.007 -41.565 1.00 33.07  ? 212 ARG C NH2 1 
ATOM   5956 N  N   . ASN C  1 213 ? 37.304  -13.959 -35.466 1.00 17.54  ? 213 ASN C N   1 
ATOM   5957 C  CA  . ASN C  1 213 ? 37.134  -14.789 -34.234 1.00 19.65  ? 213 ASN C CA  1 
ATOM   5958 C  C   . ASN C  1 213 ? 37.362  -13.858 -33.011 1.00 17.37  ? 213 ASN C C   1 
ATOM   5959 O  O   . ASN C  1 213 ? 38.204  -13.056 -32.987 1.00 19.48  ? 213 ASN C O   1 
ATOM   5960 C  CB  . ASN C  1 213 ? 38.194  -15.919 -34.208 1.00 21.45  ? 213 ASN C CB  1 
ATOM   5961 C  CG  . ASN C  1 213 ? 38.048  -16.803 -35.404 1.00 24.62  ? 213 ASN C CG  1 
ATOM   5962 O  OD1 . ASN C  1 213 ? 37.004  -17.444 -35.683 1.00 29.11  ? 213 ASN C OD1 1 
ATOM   5963 N  ND2 . ASN C  1 213 ? 39.141  -17.011 -36.031 1.00 28.98  ? 213 ASN C ND2 1 
ATOM   5964 N  N   . PRO C  1 214 ? 36.446  -13.973 -32.006 1.00 19.05  ? 214 PRO C N   1 
ATOM   5965 C  CA  . PRO C  1 214 ? 36.547  -13.205 -30.821 1.00 18.65  ? 214 PRO C CA  1 
ATOM   5966 C  C   . PRO C  1 214 ? 37.543  -13.755 -29.843 1.00 18.72  ? 214 PRO C C   1 
ATOM   5967 O  O   . PRO C  1 214 ? 37.969  -14.924 -30.093 1.00 23.81  ? 214 PRO C O   1 
ATOM   5968 C  CB  . PRO C  1 214 ? 35.120  -13.317 -30.198 1.00 19.96  ? 214 PRO C CB  1 
ATOM   5969 C  CG  . PRO C  1 214 ? 34.719  -14.669 -30.603 1.00 20.51  ? 214 PRO C CG  1 
ATOM   5970 C  CD  . PRO C  1 214 ? 35.302  -14.859 -32.071 1.00 20.76  ? 214 PRO C CD  1 
ATOM   5971 N  N   . VAL C  1 215 ? 38.015  -12.896 -28.935 1.00 19.54  ? 215 VAL C N   1 
ATOM   5972 C  CA  . VAL C  1 215 ? 38.761  -13.320 -27.738 1.00 21.08  ? 215 VAL C CA  1 
ATOM   5973 C  C   . VAL C  1 215 ? 37.742  -13.419 -26.576 1.00 20.45  ? 215 VAL C C   1 
ATOM   5974 O  O   . VAL C  1 215 ? 36.594  -12.907 -26.648 1.00 20.61  ? 215 VAL C O   1 
ATOM   5975 C  CB  . VAL C  1 215 ? 39.852  -12.317 -27.359 1.00 20.54  ? 215 VAL C CB  1 
ATOM   5976 C  CG1 . VAL C  1 215 ? 40.963  -12.251 -28.434 1.00 21.73  ? 215 VAL C CG1 1 
ATOM   5977 C  CG2 . VAL C  1 215 ? 39.387  -10.949 -26.864 1.00 20.30  ? 215 VAL C CG2 1 
ATOM   5978 N  N   . GLN C  1 216 ? 38.131  -14.101 -25.525 1.00 21.52  ? 216 GLN C N   1 
ATOM   5979 C  CA  . GLN C  1 216 ? 37.397  -14.160 -24.262 1.00 21.39  ? 216 GLN C CA  1 
ATOM   5980 C  C   . GLN C  1 216 ? 38.059  -13.554 -23.032 1.00 24.54  ? 216 GLN C C   1 
ATOM   5981 O  O   . GLN C  1 216 ? 39.313  -13.601 -22.886 1.00 26.24  ? 216 GLN C O   1 
ATOM   5982 C  CB  . GLN C  1 216 ? 37.169  -15.702 -23.978 1.00 24.06  ? 216 GLN C CB  1 
ATOM   5983 C  CG  . GLN C  1 216 ? 36.511  -16.610 -24.967 1.00 26.87  ? 216 GLN C CG  1 
ATOM   5984 C  CD  . GLN C  1 216 ? 35.914  -17.811 -24.399 1.00 50.07  ? 216 GLN C CD  1 
ATOM   5985 O  OE1 . GLN C  1 216 ? 36.500  -18.465 -23.448 1.00 49.50  ? 216 GLN C OE1 1 
ATOM   5986 N  NE2 . GLN C  1 216 ? 34.720  -18.192 -24.996 1.00 45.63  ? 216 GLN C NE2 1 
ATOM   5987 N  N   . ILE C  1 217 ? 37.230  -12.889 -22.275 1.00 22.80  ? 217 ILE C N   1 
ATOM   5988 C  CA  . ILE C  1 217 ? 37.566  -12.394 -20.986 1.00 20.87  ? 217 ILE C CA  1 
ATOM   5989 C  C   . ILE C  1 217 ? 36.541  -12.915 -19.950 1.00 20.98  ? 217 ILE C C   1 
ATOM   5990 O  O   . ILE C  1 217 ? 35.455  -13.430 -20.308 1.00 25.58  ? 217 ILE C O   1 
ATOM   5991 C  CB  . ILE C  1 217 ? 37.732  -10.859 -20.871 1.00 21.27  ? 217 ILE C CB  1 
ATOM   5992 C  CG1 . ILE C  1 217 ? 36.376  -10.095 -21.117 1.00 18.06  ? 217 ILE C CG1 1 
ATOM   5993 C  CG2 . ILE C  1 217 ? 38.790  -10.351 -21.852 1.00 21.73  ? 217 ILE C CG2 1 
ATOM   5994 C  CD1 . ILE C  1 217 ? 36.341  -8.639  -20.797 1.00 19.94  ? 217 ILE C CD1 1 
ATOM   5995 N  N   . SER C  1 218 ? 36.927  -13.090 -18.693 1.00 23.54  ? 218 SER C N   1 
ATOM   5996 C  CA  . SER C  1 218 ? 35.971  -13.759 -17.748 1.00 26.27  ? 218 SER C CA  1 
ATOM   5997 C  C   . SER C  1 218 ? 34.824  -12.805 -17.510 1.00 26.15  ? 218 SER C C   1 
ATOM   5998 O  O   . SER C  1 218 ? 34.989  -11.551 -17.608 1.00 24.97  ? 218 SER C O   1 
ATOM   5999 C  CB  . SER C  1 218 ? 36.713  -14.196 -16.423 1.00 25.09  ? 218 SER C CB  1 
ATOM   6000 O  OG  . SER C  1 218 ? 37.185  -12.968 -15.826 1.00 29.62  ? 218 SER C OG  1 
ATOM   6001 N  N   . GLN C  1 219 ? 33.752  -13.404 -16.914 1.00 32.09  ? 219 GLN C N   1 
ATOM   6002 C  CA  . GLN C  1 219 ? 32.641  -12.612 -16.383 1.00 34.19  ? 219 GLN C CA  1 
ATOM   6003 C  C   . GLN C  1 219 ? 33.215  -11.515 -15.458 1.00 28.96  ? 219 GLN C C   1 
ATOM   6004 O  O   . GLN C  1 219 ? 32.832  -10.347 -15.481 1.00 26.49  ? 219 GLN C O   1 
ATOM   6005 C  CB  . GLN C  1 219 ? 31.545  -13.470 -15.699 1.00 40.95  ? 219 GLN C CB  1 
ATOM   6006 N  N   . GLU C  1 220 ? 34.122  -11.897 -14.559 1.00 31.09  ? 220 GLU C N   1 
ATOM   6007 C  CA  . GLU C  1 220 ? 34.716  -10.913 -13.625 1.00 31.42  ? 220 GLU C CA  1 
ATOM   6008 C  C   . GLU C  1 220 ? 35.421  -9.789  -14.305 1.00 19.76  ? 220 GLU C C   1 
ATOM   6009 O  O   . GLU C  1 220 ? 35.201  -8.617  -14.000 1.00 23.47  ? 220 GLU C O   1 
ATOM   6010 C  CB  . GLU C  1 220 ? 35.469  -11.571 -12.502 1.00 31.62  ? 220 GLU C CB  1 
ATOM   6011 C  CG  . GLU C  1 220 ? 34.784  -12.793 -11.886 1.00 38.72  ? 220 GLU C CG  1 
ATOM   6012 C  CD  . GLU C  1 220 ? 35.093  -14.119 -12.591 1.00 47.70  ? 220 GLU C CD  1 
ATOM   6013 O  OE1 . GLU C  1 220 ? 34.669  -14.306 -13.757 1.00 49.61  ? 220 GLU C OE1 1 
ATOM   6014 O  OE2 . GLU C  1 220 ? 35.734  -15.002 -11.975 1.00 56.03  ? 220 GLU C OE2 1 
ATOM   6015 N  N   . GLN C  1 221 ? 36.291  -10.134 -15.288 1.00 28.60  ? 221 GLN C N   1 
ATOM   6016 C  CA  . GLN C  1 221 ? 37.018  -9.070  -16.013 1.00 25.62  ? 221 GLN C CA  1 
ATOM   6017 C  C   . GLN C  1 221 ? 36.104  -8.122  -16.800 1.00 19.10  ? 221 GLN C C   1 
ATOM   6018 O  O   . GLN C  1 221 ? 36.296  -6.874  -16.726 1.00 22.32  ? 221 GLN C O   1 
ATOM   6019 C  CB  . GLN C  1 221 ? 37.898  -9.692  -17.036 1.00 24.12  ? 221 GLN C CB  1 
ATOM   6020 C  CG  . GLN C  1 221 ? 39.122  -10.332 -16.340 1.00 24.32  ? 221 GLN C CG  1 
ATOM   6021 C  CD  . GLN C  1 221 ? 40.091  -10.905 -17.370 1.00 21.99  ? 221 GLN C CD  1 
ATOM   6022 O  OE1 . GLN C  1 221 ? 39.700  -11.848 -18.089 1.00 23.00  ? 221 GLN C OE1 1 
ATOM   6023 N  NE2 . GLN C  1 221 ? 41.302  -10.355 -17.509 1.00 24.88  ? 221 GLN C NE2 1 
ATOM   6024 N  N   . LEU C  1 222 ? 35.021  -8.645  -17.300 1.00 23.96  ? 222 LEU C N   1 
ATOM   6025 C  CA  . LEU C  1 222 ? 34.044  -7.752  -18.016 1.00 21.38  ? 222 LEU C CA  1 
ATOM   6026 C  C   . LEU C  1 222 ? 33.246  -6.866  -17.161 1.00 20.37  ? 222 LEU C C   1 
ATOM   6027 O  O   . LEU C  1 222 ? 33.148  -5.680  -17.400 1.00 20.54  ? 222 LEU C O   1 
ATOM   6028 C  CB  . LEU C  1 222 ? 33.155  -8.637  -18.819 1.00 23.27  ? 222 LEU C CB  1 
ATOM   6029 C  CG  . LEU C  1 222 ? 32.039  -7.968  -19.664 1.00 23.14  ? 222 LEU C CG  1 
ATOM   6030 C  CD1 . LEU C  1 222 ? 32.654  -7.049  -20.707 1.00 22.53  ? 222 LEU C CD1 1 
ATOM   6031 C  CD2 . LEU C  1 222 ? 31.157  -9.068  -20.242 1.00 24.63  ? 222 LEU C CD2 1 
ATOM   6032 N  N   . LEU C  1 223 ? 32.844  -7.383  -15.915 1.00 20.41  ? 223 LEU C N   1 
ATOM   6033 C  CA  . LEU C  1 223 ? 32.185  -6.580  -14.940 1.00 25.31  ? 223 LEU C CA  1 
ATOM   6034 C  C   . LEU C  1 223 ? 33.060  -5.521  -14.487 1.00 18.97  ? 223 LEU C C   1 
ATOM   6035 O  O   . LEU C  1 223 ? 32.710  -4.393  -14.287 1.00 22.87  ? 223 LEU C O   1 
ATOM   6036 C  CB  . LEU C  1 223 ? 31.761  -7.497  -13.769 1.00 33.40  ? 223 LEU C CB  1 
ATOM   6037 C  CG  . LEU C  1 223 ? 30.640  -6.865  -12.888 1.00 37.09  ? 223 LEU C CG  1 
ATOM   6038 C  CD1 . LEU C  1 223 ? 29.302  -6.631  -13.633 1.00 37.01  ? 223 LEU C CD1 1 
ATOM   6039 C  CD2 . LEU C  1 223 ? 30.456  -7.889  -11.752 1.00 41.33  ? 223 LEU C CD2 1 
ATOM   6040 N  N   . ALA C  1 224 ? 34.304  -5.982  -14.188 1.00 23.82  ? 224 ALA C N   1 
ATOM   6041 C  CA  . ALA C  1 224 ? 35.409  -4.990  -13.849 1.00 29.65  ? 224 ALA C CA  1 
ATOM   6042 C  C   . ALA C  1 224 ? 35.545  -3.787  -14.773 1.00 21.69  ? 224 ALA C C   1 
ATOM   6043 O  O   . ALA C  1 224 ? 35.493  -2.633  -14.386 1.00 27.45  ? 224 ALA C O   1 
ATOM   6044 C  CB  . ALA C  1 224 ? 36.814  -5.670  -13.692 1.00 29.03  ? 224 ALA C CB  1 
ATOM   6045 N  N   . LEU C  1 225 ? 35.572  -4.039  -16.091 1.00 24.59  ? 225 LEU C N   1 
ATOM   6046 C  CA  . LEU C  1 225 ? 35.699  -3.074  -17.138 1.00 24.81  ? 225 LEU C CA  1 
ATOM   6047 C  C   . LEU C  1 225 ? 34.466  -2.182  -17.181 1.00 20.16  ? 225 LEU C C   1 
ATOM   6048 O  O   . LEU C  1 225 ? 34.583  -0.969  -17.187 1.00 23.98  ? 225 LEU C O   1 
ATOM   6049 C  CB  . LEU C  1 225 ? 35.860  -3.831  -18.503 1.00 25.91  ? 225 LEU C CB  1 
ATOM   6050 C  CG  . LEU C  1 225 ? 35.969  -2.815  -19.679 1.00 22.73  ? 225 LEU C CG  1 
ATOM   6051 C  CD1 . LEU C  1 225 ? 37.180  -1.880  -19.521 1.00 23.61  ? 225 LEU C CD1 1 
ATOM   6052 C  CD2 . LEU C  1 225 ? 36.072  -3.597  -21.003 1.00 22.11  ? 225 LEU C CD2 1 
ATOM   6053 N  N   . GLU C  1 226 ? 33.291  -2.849  -17.012 1.00 22.80  ? 226 GLU C N   1 
ATOM   6054 C  CA  . GLU C  1 226 ? 31.980  -2.069  -17.118 1.00 21.06  ? 226 GLU C CA  1 
ATOM   6055 C  C   . GLU C  1 226 ? 31.715  -1.221  -15.851 1.00 22.98  ? 226 GLU C C   1 
ATOM   6056 O  O   . GLU C  1 226 ? 30.994  -0.254  -15.962 1.00 26.15  ? 226 GLU C O   1 
ATOM   6057 C  CB  . GLU C  1 226 ? 30.848  -3.063  -17.201 1.00 23.57  ? 226 GLU C CB  1 
ATOM   6058 C  CG  . GLU C  1 226 ? 30.831  -3.842  -18.537 1.00 19.80  ? 226 GLU C CG  1 
ATOM   6059 C  CD  . GLU C  1 226 ? 29.941  -5.065  -18.499 1.00 19.20  ? 226 GLU C CD  1 
ATOM   6060 O  OE1 . GLU C  1 226 ? 29.648  -5.543  -17.325 1.00 23.28  ? 226 GLU C OE1 1 
ATOM   6061 O  OE2 . GLU C  1 226 ? 29.541  -5.624  -19.550 1.00 22.44  ? 226 GLU C OE2 1 
ATOM   6062 N  N   . THR C  1 227 ? 32.466  -1.472  -14.771 1.00 26.11  ? 227 THR C N   1 
ATOM   6063 C  CA  . THR C  1 227 ? 32.133  -0.758  -13.531 1.00 25.20  ? 227 THR C CA  1 
ATOM   6064 C  C   . THR C  1 227 ? 33.272  0.104   -12.978 1.00 23.14  ? 227 THR C C   1 
ATOM   6065 O  O   . THR C  1 227 ? 33.122  0.699   -11.956 1.00 30.08  ? 227 THR C O   1 
ATOM   6066 C  CB  . THR C  1 227 ? 31.633  -1.754  -12.391 1.00 29.50  ? 227 THR C CB  1 
ATOM   6067 O  OG1 . THR C  1 227 ? 32.627  -2.778  -12.201 1.00 28.98  ? 227 THR C OG1 1 
ATOM   6068 C  CG2 . THR C  1 227 ? 30.252  -2.402  -12.743 1.00 26.64  ? 227 THR C CG2 1 
ATOM   6069 N  N   . ALA C  1 228 ? 34.477  0.103   -13.554 1.00 26.55  ? 228 ALA C N   1 
ATOM   6070 C  CA  . ALA C  1 228 ? 35.596  0.688   -13.016 1.00 24.88  ? 228 ALA C CA  1 
ATOM   6071 C  C   . ALA C  1 228 ? 35.707  2.228   -13.194 1.00 26.87  ? 228 ALA C C   1 
ATOM   6072 O  O   . ALA C  1 228 ? 36.334  2.809   -12.370 1.00 26.23  ? 228 ALA C O   1 
ATOM   6073 C  CB  . ALA C  1 228 ? 36.841  -0.035  -13.473 1.00 32.72  ? 228 ALA C CB  1 
ATOM   6074 N  N   . LEU C  1 229 ? 35.253  2.760   -14.330 1.00 22.22  ? 229 LEU C N   1 
ATOM   6075 C  CA  . LEU C  1 229 ? 35.431  4.186   -14.700 1.00 21.91  ? 229 LEU C CA  1 
ATOM   6076 C  C   . LEU C  1 229 ? 34.309  5.110   -14.619 1.00 21.30  ? 229 LEU C C   1 
ATOM   6077 O  O   . LEU C  1 229 ? 33.137  4.695   -14.783 1.00 21.71  ? 229 LEU C O   1 
ATOM   6078 C  CB  . LEU C  1 229 ? 36.109  4.267   -16.074 1.00 23.26  ? 229 LEU C CB  1 
ATOM   6079 C  CG  . LEU C  1 229 ? 37.222  3.137   -16.355 1.00 20.93  ? 229 LEU C CG  1 
ATOM   6080 C  CD1 . LEU C  1 229 ? 37.795  3.113   -17.778 1.00 32.22  ? 229 LEU C CD1 1 
ATOM   6081 C  CD2 . LEU C  1 229 ? 38.422  3.403   -15.421 1.00 22.90  ? 229 LEU C CD2 1 
ATOM   6082 N  N   . TYR C  1 230 ? 34.591  6.365   -14.488 1.00 24.51  ? 230 TYR C N   1 
ATOM   6083 C  CA  . TYR C  1 230 ? 33.641  7.391   -14.490 1.00 26.69  ? 230 TYR C CA  1 
ATOM   6084 C  C   . TYR C  1 230 ? 34.137  8.177   -15.705 1.00 25.10  ? 230 TYR C C   1 
ATOM   6085 O  O   . TYR C  1 230 ? 35.347  8.088   -16.040 1.00 31.74  ? 230 TYR C O   1 
ATOM   6086 C  CB  . TYR C  1 230 ? 33.777  8.250   -13.196 1.00 26.85  ? 230 TYR C CB  1 
ATOM   6087 C  CG  . TYR C  1 230 ? 33.199  7.415   -12.023 1.00 40.79  ? 230 TYR C CG  1 
ATOM   6088 C  CD1 . TYR C  1 230 ? 33.914  6.326   -11.415 1.00 47.32  ? 230 TYR C CD1 1 
ATOM   6089 C  CD2 . TYR C  1 230 ? 31.903  7.660   -11.590 1.00 33.55  ? 230 TYR C CD2 1 
ATOM   6090 C  CE1 . TYR C  1 230 ? 33.353  5.587   -10.369 1.00 70.70  ? 230 TYR C CE1 1 
ATOM   6091 C  CE2 . TYR C  1 230 ? 31.340  6.930   -10.560 1.00 48.86  ? 230 TYR C CE2 1 
ATOM   6092 C  CZ  . TYR C  1 230 ? 32.063  5.900   -9.965  1.00 58.55  ? 230 TYR C CZ  1 
ATOM   6093 O  OH  . TYR C  1 230 ? 31.514  5.181   -8.932  1.00 85.78  ? 230 TYR C OH  1 
ATOM   6094 N  N   . CYS C  1 231 ? 33.232  8.908   -16.295 1.00 23.16  ? 231 CYS C N   1 
ATOM   6095 C  CA  . CYS C  1 231 ? 33.628  9.696   -17.377 1.00 27.43  ? 231 CYS C CA  1 
ATOM   6096 C  C   . CYS C  1 231 ? 33.700  11.213  -16.914 1.00 31.37  ? 231 CYS C C   1 
ATOM   6097 O  O   . CYS C  1 231 ? 33.939  12.129  -17.637 1.00 28.94  ? 231 CYS C O   1 
ATOM   6098 C  CB  . CYS C  1 231 ? 32.619  9.581   -18.515 1.00 30.82  ? 231 CYS C CB  1 
ATOM   6099 S  SG  . CYS C  1 231 ? 30.866  9.818   -18.115 1.00 38.70  ? 231 CYS C SG  1 
ATOM   6100 N  N   . THR C  1 232 ? 33.462  11.455  -15.621 1.00 24.57  ? 232 THR C N   1 
ATOM   6101 C  CA  . THR C  1 232 ? 33.462  12.785  -14.961 1.00 26.22  ? 232 THR C CA  1 
ATOM   6102 C  C   . THR C  1 232 ? 34.728  12.970  -14.174 1.00 27.42  ? 232 THR C C   1 
ATOM   6103 O  O   . THR C  1 232 ? 35.459  11.978  -13.871 1.00 22.46  ? 232 THR C O   1 
ATOM   6104 C  CB  . THR C  1 232 ? 32.271  12.921  -14.005 1.00 27.06  ? 232 THR C CB  1 
ATOM   6105 O  OG1 . THR C  1 232 ? 32.066  11.652  -13.321 1.00 26.32  ? 232 THR C OG1 1 
ATOM   6106 C  CG2 . THR C  1 232 ? 30.969  13.368  -14.787 1.00 29.32  ? 232 THR C CG2 1 
ATOM   6107 N  N   . HIS C  1 233 ? 35.071  14.273  -13.917 1.00 30.24  ? 233 HIS C N   1 
ATOM   6108 C  CA  . HIS C  1 233 ? 36.342  14.571  -13.163 1.00 27.08  ? 233 HIS C CA  1 
ATOM   6109 C  C   . HIS C  1 233 ? 36.178  14.191  -11.670 1.00 27.12  ? 233 HIS C C   1 
ATOM   6110 O  O   . HIS C  1 233 ? 35.011  14.129  -11.162 1.00 29.77  ? 233 HIS C O   1 
ATOM   6111 C  CB  . HIS C  1 233 ? 36.656  16.041  -13.365 1.00 29.39  ? 233 HIS C CB  1 
ATOM   6112 C  CG  . HIS C  1 233 ? 37.298  16.318  -14.681 1.00 42.77  ? 233 HIS C CG  1 
ATOM   6113 N  ND1 . HIS C  1 233 ? 36.654  17.007  -15.709 1.00 59.43  ? 233 HIS C ND1 1 
ATOM   6114 C  CD2 . HIS C  1 233 ? 38.519  15.974  -15.167 1.00 43.75  ? 233 HIS C CD2 1 
ATOM   6115 C  CE1 . HIS C  1 233 ? 37.454  17.074  -16.762 1.00 45.70  ? 233 HIS C CE1 1 
ATOM   6116 N  NE2 . HIS C  1 233 ? 38.605  16.488  -16.445 1.00 65.08  ? 233 HIS C NE2 1 
ATOM   6117 N  N   . MET C  1 234 ? 37.289  13.853  -10.966 1.00 31.93  ? 234 MET C N   1 
ATOM   6118 C  CA  . MET C  1 234 ? 37.312  13.378  -9.583  1.00 35.91  ? 234 MET C CA  1 
ATOM   6119 C  C   . MET C  1 234 ? 36.536  14.339  -8.690  1.00 40.78  ? 234 MET C C   1 
ATOM   6120 O  O   . MET C  1 234 ? 35.807  13.873  -7.842  1.00 55.39  ? 234 MET C O   1 
ATOM   6121 C  CB  . MET C  1 234 ? 38.794  13.215  -9.143  1.00 39.55  ? 234 MET C CB  1 
ATOM   6122 C  CG  . MET C  1 234 ? 38.981  12.444  -7.816  1.00 56.43  ? 234 MET C CG  1 
ATOM   6123 S  SD  . MET C  1 234 ? 40.649  12.246  -7.164  1.00 59.34  ? 234 MET C SD  1 
ATOM   6124 C  CE  . MET C  1 234 ? 41.077  10.420  -7.260  1.00 39.39  ? 234 MET C CE  1 
ATOM   6125 N  N   . ASP C  1 235 ? 36.587  15.666  -8.998  1.00 43.57  ? 235 ASP C N   1 
ATOM   6126 C  CA  . ASP C  1 235 ? 35.992  16.752  -8.090  1.00 51.46  ? 235 ASP C CA  1 
ATOM   6127 C  C   . ASP C  1 235 ? 34.427  16.949  -8.242  1.00 54.17  ? 235 ASP C C   1 
ATOM   6128 O  O   . ASP C  1 235 ? 33.748  17.529  -7.388  1.00 130.16 ? 235 ASP C O   1 
ATOM   6129 N  N   . ASP C  1 236 ? 33.901  16.436  -9.407  1.00 35.11  ? 236 ASP C N   1 
ATOM   6130 C  CA  . ASP C  1 236 ? 32.449  16.422  -9.725  1.00 35.84  ? 236 ASP C CA  1 
ATOM   6131 C  C   . ASP C  1 236 ? 31.500  15.807  -8.619  1.00 46.21  ? 236 ASP C C   1 
ATOM   6132 O  O   . ASP C  1 236 ? 31.596  14.558  -8.295  1.00 41.84  ? 236 ASP C O   1 
ATOM   6133 C  CB  . ASP C  1 236 ? 32.204  15.666  -11.060 1.00 37.33  ? 236 ASP C CB  1 
ATOM   6134 C  CG  . ASP C  1 236 ? 30.923  16.121  -11.789 1.00 43.62  ? 236 ASP C CG  1 
ATOM   6135 O  OD1 . ASP C  1 236 ? 29.979  16.574  -11.066 1.00 55.23  ? 236 ASP C OD1 1 
ATOM   6136 O  OD2 . ASP C  1 236 ? 30.866  16.102  -13.075 1.00 42.75  ? 236 ASP C OD2 1 
ATOM   6137 N  N   . PRO C  1 237 ? 30.564  16.667  -8.080  1.00 43.44  ? 237 PRO C N   1 
ATOM   6138 C  CA  . PRO C  1 237 ? 29.569  16.243  -7.098  1.00 39.80  ? 237 PRO C CA  1 
ATOM   6139 C  C   . PRO C  1 237 ? 28.466  15.351  -7.758  1.00 38.09  ? 237 PRO C C   1 
ATOM   6140 O  O   . PRO C  1 237 ? 27.699  14.785  -7.027  1.00 36.26  ? 237 PRO C O   1 
ATOM   6141 C  CB  . PRO C  1 237 ? 28.952  17.577  -6.567  1.00 42.42  ? 237 PRO C CB  1 
ATOM   6142 C  CG  . PRO C  1 237 ? 29.130  18.540  -7.674  1.00 38.40  ? 237 PRO C CG  1 
ATOM   6143 C  CD  . PRO C  1 237 ? 30.489  18.141  -8.289  1.00 43.76  ? 237 PRO C CD  1 
ATOM   6144 N  N   . SER C  1 238 ? 28.417  15.226  -9.113  1.00 35.45  ? 238 SER C N   1 
ATOM   6145 C  CA  . SER C  1 238 ? 27.455  14.333  -9.831  1.00 35.81  ? 238 SER C CA  1 
ATOM   6146 C  C   . SER C  1 238 ? 28.237  13.323  -10.732 1.00 39.46  ? 238 SER C C   1 
ATOM   6147 O  O   . SER C  1 238 ? 28.367  13.518  -11.997 1.00 37.72  ? 238 SER C O   1 
ATOM   6148 C  CB  . SER C  1 238 ? 26.583  15.137  -10.784 1.00 43.08  ? 238 SER C CB  1 
ATOM   6149 O  OG  . SER C  1 238 ? 25.819  16.096  -10.147 1.00 56.64  ? 238 SER C OG  1 
ATOM   6150 N  N   . PRO C  1 239 ? 28.886  12.302  -10.113 1.00 30.75  ? 239 PRO C N   1 
ATOM   6151 C  CA  . PRO C  1 239 ? 29.694  11.416  -11.000 1.00 27.86  ? 239 PRO C CA  1 
ATOM   6152 C  C   . PRO C  1 239 ? 28.902  10.514  -11.897 1.00 33.58  ? 239 PRO C C   1 
ATOM   6153 O  O   . PRO C  1 239 ? 27.830  10.004  -11.522 1.00 37.85  ? 239 PRO C O   1 
ATOM   6154 C  CB  . PRO C  1 239 ? 30.335  10.425  -9.991  1.00 33.81  ? 239 PRO C CB  1 
ATOM   6155 C  CG  . PRO C  1 239 ? 29.646  10.642  -8.666  1.00 31.65  ? 239 PRO C CG  1 
ATOM   6156 C  CD  . PRO C  1 239 ? 29.176  12.061  -8.686  1.00 30.57  ? 239 PRO C CD  1 
ATOM   6157 N  N   . ARG C  1 240 ? 29.425  10.226  -13.066 1.00 30.11  ? 240 ARG C N   1 
ATOM   6158 C  CA  . ARG C  1 240 ? 28.671  9.413   -14.006 1.00 28.01  ? 240 ARG C CA  1 
ATOM   6159 C  C   . ARG C  1 240 ? 29.614  8.291   -14.378 1.00 27.65  ? 240 ARG C C   1 
ATOM   6160 O  O   . ARG C  1 240 ? 30.804  8.520   -14.715 1.00 34.02  ? 240 ARG C O   1 
ATOM   6161 C  CB  . ARG C  1 240 ? 28.277  10.220  -15.205 1.00 28.83  ? 240 ARG C CB  1 
ATOM   6162 C  CG  . ARG C  1 240 ? 27.474  9.392   -16.254 1.00 30.75  ? 240 ARG C CG  1 
ATOM   6163 C  CD  . ARG C  1 240 ? 26.955  10.362  -17.303 1.00 47.56  ? 240 ARG C CD  1 
ATOM   6164 N  N   . GLU C  1 241 ? 29.075  7.062   -14.367 1.00 26.56  ? 241 GLU C N   1 
ATOM   6165 C  CA  . GLU C  1 241 ? 29.813  5.846   -14.797 1.00 25.21  ? 241 GLU C CA  1 
ATOM   6166 C  C   . GLU C  1 241 ? 30.035  5.825   -16.315 1.00 24.12  ? 241 GLU C C   1 
ATOM   6167 O  O   . GLU C  1 241 ? 29.149  6.167   -17.091 1.00 27.94  ? 241 GLU C O   1 
ATOM   6168 C  CB  . GLU C  1 241 ? 29.065  4.532   -14.511 1.00 30.84  ? 241 GLU C CB  1 
ATOM   6169 C  CG  . GLU C  1 241 ? 28.781  4.280   -13.075 1.00 35.36  ? 241 GLU C CG  1 
ATOM   6170 C  CD  . GLU C  1 241 ? 27.445  3.563   -12.825 1.00 62.24  ? 241 GLU C CD  1 
ATOM   6171 O  OE1 . GLU C  1 241 ? 26.747  3.064   -13.765 1.00 60.73  ? 241 GLU C OE1 1 
ATOM   6172 O  OE2 . GLU C  1 241 ? 27.084  3.522   -11.633 1.00 75.46  ? 241 GLU C OE2 1 
ATOM   6173 N  N   . MET C  1 242 ? 31.246  5.425   -16.687 1.00 23.69  ? 242 MET C N   1 
ATOM   6174 C  CA  . MET C  1 242 ? 31.605  5.256   -18.088 1.00 20.62  ? 242 MET C CA  1 
ATOM   6175 C  C   . MET C  1 242 ? 31.098  3.884   -18.552 1.00 19.40  ? 242 MET C C   1 
ATOM   6176 O  O   . MET C  1 242 ? 31.735  2.838   -18.309 1.00 20.24  ? 242 MET C O   1 
ATOM   6177 C  CB  . MET C  1 242 ? 33.135  5.309   -18.279 1.00 19.41  ? 242 MET C CB  1 
ATOM   6178 C  CG  . MET C  1 242 ? 33.441  5.357   -19.759 1.00 20.42  ? 242 MET C CG  1 
ATOM   6179 S  SD  . MET C  1 242 ? 35.257  5.346   -20.032 1.00 22.96  ? 242 MET C SD  1 
ATOM   6180 C  CE  . MET C  1 242 ? 35.754  6.960   -19.417 1.00 25.00  ? 242 MET C CE  1 
ATOM   6181 N  N   . ILE C  1 243 ? 29.964  3.890   -19.247 1.00 18.37  ? 243 ILE C N   1 
ATOM   6182 C  CA  . ILE C  1 243 ? 29.307  2.678   -19.725 1.00 18.23  ? 243 ILE C CA  1 
ATOM   6183 C  C   . ILE C  1 243 ? 28.758  3.037   -21.153 1.00 15.40  ? 243 ILE C C   1 
ATOM   6184 O  O   . ILE C  1 243 ? 28.567  4.210   -21.458 1.00 16.80  ? 243 ILE C O   1 
ATOM   6185 C  CB  . ILE C  1 243 ? 28.143  2.255   -18.787 1.00 19.52  ? 243 ILE C CB  1 
ATOM   6186 C  CG1 . ILE C  1 243 ? 27.182  3.413   -18.484 1.00 22.50  ? 243 ILE C CG1 1 
ATOM   6187 C  CG2 . ILE C  1 243 ? 28.772  1.605   -17.520 1.00 23.87  ? 243 ILE C CG2 1 
ATOM   6188 C  CD1 . ILE C  1 243 ? 25.887  2.931   -17.684 1.00 24.55  ? 243 ILE C CD1 1 
ATOM   6189 N  N   . ASN C  1 244 ? 28.464  1.967   -21.866 1.00 15.94  ? 244 ASN C N   1 
ATOM   6190 C  CA  . ASN C  1 244 ? 27.783  2.115   -23.180 1.00 15.99  ? 244 ASN C CA  1 
ATOM   6191 C  C   . ASN C  1 244 ? 28.502  3.095   -24.093 1.00 14.61  ? 244 ASN C C   1 
ATOM   6192 O  O   . ASN C  1 244 ? 27.894  3.892   -24.754 1.00 15.90  ? 244 ASN C O   1 
ATOM   6193 C  CB  . ASN C  1 244 ? 26.333  2.495   -22.943 1.00 16.56  ? 244 ASN C CB  1 
ATOM   6194 C  CG  . ASN C  1 244 ? 25.588  1.584   -22.056 1.00 18.30  ? 244 ASN C CG  1 
ATOM   6195 O  OD1 . ASN C  1 244 ? 25.774  0.372   -22.080 1.00 19.95  ? 244 ASN C OD1 1 
ATOM   6196 N  ND2 . ASN C  1 244 ? 24.779  2.215   -21.120 1.00 25.00  ? 244 ASN C ND2 1 
ATOM   6197 N  N   . ASN C  1 245 ? 29.825  2.939   -24.116 1.00 15.65  ? 245 ASN C N   1 
ATOM   6198 C  CA  . ASN C  1 245 ? 30.687  3.930   -24.875 1.00 14.75  ? 245 ASN C CA  1 
ATOM   6199 C  C   . ASN C  1 245 ? 30.962  3.381   -26.299 1.00 13.97  ? 245 ASN C C   1 
ATOM   6200 O  O   . ASN C  1 245 ? 32.097  3.258   -26.688 1.00 16.23  ? 245 ASN C O   1 
ATOM   6201 C  CB  . ASN C  1 245 ? 31.907  4.309   -24.126 1.00 15.62  ? 245 ASN C CB  1 
ATOM   6202 C  CG  . ASN C  1 245 ? 32.840  3.106   -23.850 1.00 16.38  ? 245 ASN C CG  1 
ATOM   6203 O  OD1 . ASN C  1 245 ? 32.431  1.976   -23.803 1.00 16.54  ? 245 ASN C OD1 1 
ATOM   6204 N  ND2 . ASN C  1 245 ? 34.112  3.342   -23.508 1.00 19.68  ? 245 ASN C ND2 1 
ATOM   6205 N  N   . PHE C  1 246 ? 29.895  3.002   -26.977 1.00 13.41  ? 246 PHE C N   1 
ATOM   6206 C  CA  . PHE C  1 246 ? 29.971  2.459   -28.358 1.00 13.93  ? 246 PHE C CA  1 
ATOM   6207 C  C   . PHE C  1 246 ? 29.009  3.263   -29.193 1.00 13.11  ? 246 PHE C C   1 
ATOM   6208 O  O   . PHE C  1 246 ? 27.963  3.769   -28.694 1.00 12.85  ? 246 PHE C O   1 
ATOM   6209 C  CB  . PHE C  1 246 ? 29.631  0.960   -28.375 1.00 13.28  ? 246 PHE C CB  1 
ATOM   6210 C  CG  . PHE C  1 246 ? 28.251  0.623   -27.919 1.00 13.10  ? 246 PHE C CG  1 
ATOM   6211 C  CD1 . PHE C  1 246 ? 27.993  0.398   -26.549 1.00 14.98  ? 246 PHE C CD1 1 
ATOM   6212 C  CD2 . PHE C  1 246 ? 27.194  0.502   -28.857 1.00 14.42  ? 246 PHE C CD2 1 
ATOM   6213 C  CE1 . PHE C  1 246 ? 26.708  0.145   -26.121 1.00 14.88  ? 246 PHE C CE1 1 
ATOM   6214 C  CE2 . PHE C  1 246 ? 25.907  0.201   -28.383 1.00 14.76  ? 246 PHE C CE2 1 
ATOM   6215 C  CZ  . PHE C  1 246 ? 25.634  0.011   -27.013 1.00 15.75  ? 246 PHE C CZ  1 
ATOM   6216 N  N   . ARG C  1 247 ? 29.314  3.415   -30.472 1.00 11.51  ? 247 ARG C N   1 
ATOM   6217 C  CA  . ARG C  1 247 ? 28.384  4.050   -31.421 1.00 11.34  ? 247 ARG C CA  1 
ATOM   6218 C  C   . ARG C  1 247 ? 27.420  3.020   -31.970 1.00 11.28  ? 247 ARG C C   1 
ATOM   6219 O  O   . ARG C  1 247 ? 27.839  1.887   -32.205 1.00 11.66  ? 247 ARG C O   1 
ATOM   6220 C  CB  . ARG C  1 247 ? 29.217  4.734   -32.549 1.00 11.45  ? 247 ARG C CB  1 
ATOM   6221 C  CG  . ARG C  1 247 ? 28.456  5.697   -33.419 1.00 11.62  ? 247 ARG C CG  1 
ATOM   6222 C  CD  . ARG C  1 247 ? 29.303  6.162   -34.588 1.00 11.03  ? 247 ARG C CD  1 
ATOM   6223 N  NE  . ARG C  1 247 ? 28.677  7.301   -35.235 1.00 11.26  ? 247 ARG C NE  1 
ATOM   6224 C  CZ  . ARG C  1 247 ? 29.154  7.872   -36.368 1.00 10.56  ? 247 ARG C CZ  1 
ATOM   6225 N  NH1 . ARG C  1 247 ? 30.203  7.316   -36.952 1.00 11.90  ? 247 ARG C NH1 1 
ATOM   6226 N  NH2 . ARG C  1 247 ? 28.640  8.996   -36.808 1.00 11.84  ? 247 ARG C NH2 1 
ATOM   6227 N  N   . GLN C  1 248 ? 26.160  3.410   -32.212 1.00 11.15  ? 248 GLN C N   1 
ATOM   6228 C  CA  . GLN C  1 248 ? 25.256  2.513   -32.926 1.00 11.10  ? 248 GLN C CA  1 
ATOM   6229 C  C   . GLN C  1 248 ? 25.779  2.230   -34.350 1.00 10.53  ? 248 GLN C C   1 
ATOM   6230 O  O   . GLN C  1 248 ? 26.499  3.073   -34.944 1.00 10.97  ? 248 GLN C O   1 
ATOM   6231 C  CB  . GLN C  1 248 ? 23.880  3.241   -33.066 1.00 11.01  ? 248 GLN C CB  1 
ATOM   6232 C  CG  . GLN C  1 248 ? 23.187  3.527   -31.738 1.00 11.48  ? 248 GLN C CG  1 
ATOM   6233 C  CD  . GLN C  1 248 ? 22.901  2.305   -30.900 1.00 11.73  ? 248 GLN C CD  1 
ATOM   6234 O  OE1 . GLN C  1 248 ? 23.560  1.949   -29.961 1.00 15.70  ? 248 GLN C OE1 1 
ATOM   6235 N  NE2 . GLN C  1 248 ? 21.750  1.677   -31.225 1.00 14.36  ? 248 GLN C NE2 1 
ATOM   6236 N  N   . VAL C  1 249 ? 25.342  1.100   -34.913 1.00 10.43  ? 249 VAL C N   1 
ATOM   6237 C  CA  . VAL C  1 249 ? 25.759  0.791   -36.273 1.00 10.70  ? 249 VAL C CA  1 
ATOM   6238 C  C   . VAL C  1 249 ? 25.142  1.818   -37.262 1.00 10.62  ? 249 VAL C C   1 
ATOM   6239 O  O   . VAL C  1 249 ? 24.026  2.296   -37.100 1.00 11.14  ? 249 VAL C O   1 
ATOM   6240 C  CB  . VAL C  1 249 ? 25.411  -0.659  -36.676 1.00 12.36  ? 249 VAL C CB  1 
ATOM   6241 C  CG1 . VAL C  1 249 ? 26.247  -1.681  -35.934 1.00 13.24  ? 249 VAL C CG1 1 
ATOM   6242 C  CG2 . VAL C  1 249 ? 23.946  -0.961  -36.638 1.00 14.13  ? 249 VAL C CG2 1 
ATOM   6243 N  N   . GLN C  1 250 ? 25.884  2.026   -38.339 1.00 10.09  ? 250 GLN C N   1 
ATOM   6244 C  CA  . GLN C  1 250 ? 25.559  3.014   -39.358 1.00 10.17  ? 250 GLN C CA  1 
ATOM   6245 C  C   . GLN C  1 250 ? 24.949  2.290   -40.571 1.00 11.02  ? 250 GLN C C   1 
ATOM   6246 O  O   . GLN C  1 250 ? 25.293  1.153   -40.841 1.00 12.63  ? 250 GLN C O   1 
ATOM   6247 C  CB  . GLN C  1 250 ? 26.841  3.684   -39.823 1.00 11.05  ? 250 GLN C CB  1 
ATOM   6248 C  CG  . GLN C  1 250 ? 27.638  4.315   -38.617 1.00 10.87  ? 250 GLN C CG  1 
ATOM   6249 C  CD  . GLN C  1 250 ? 26.917  5.443   -38.005 1.00 10.30  ? 250 GLN C CD  1 
ATOM   6250 O  OE1 . GLN C  1 250 ? 26.666  6.513   -38.640 1.00 11.77  ? 250 GLN C OE1 1 
ATOM   6251 N  NE2 . GLN C  1 250 ? 26.536  5.284   -36.720 1.00 11.39  ? 250 GLN C NE2 1 
ATOM   6252 N  N   . LYS C  1 251 ? 24.136  3.004   -41.328 1.00 11.13  ? 251 LYS C N   1 
ATOM   6253 C  CA  . LYS C  1 251 ? 23.648  2.412   -42.620 1.00 11.04  ? 251 LYS C CA  1 
ATOM   6254 C  C   . LYS C  1 251 ? 24.841  2.142   -43.490 1.00 11.20  ? 251 LYS C C   1 
ATOM   6255 O  O   . LYS C  1 251 ? 25.806  2.923   -43.517 1.00 11.96  ? 251 LYS C O   1 
ATOM   6256 C  CB  . LYS C  1 251 ? 22.716  3.383   -43.301 1.00 13.08  ? 251 LYS C CB  1 
ATOM   6257 C  CG  . LYS C  1 251 ? 21.320  3.298   -42.603 1.00 13.95  ? 251 LYS C CG  1 
ATOM   6258 C  CD  . LYS C  1 251 ? 20.364  4.260   -43.209 1.00 14.43  ? 251 LYS C CD  1 
ATOM   6259 C  CE  . LYS C  1 251 ? 18.875  3.943   -42.855 1.00 12.35  ? 251 LYS C CE  1 
ATOM   6260 N  NZ  . LYS C  1 251 ? 18.673  3.987   -41.379 1.00 10.95  ? 251 LYS C NZ  1 
ATOM   6261 N  N   A PHE C  1 252 ? 24.769  1.106   -44.308 0.50 12.58  ? 252 PHE C N   1 
ATOM   6262 N  N   B PHE C  1 252 ? 24.733  1.065   -44.265 0.50 12.85  ? 252 PHE C N   1 
ATOM   6263 C  CA  A PHE C  1 252 ? 25.906  0.655   -45.171 0.50 13.54  ? 252 PHE C CA  1 
ATOM   6264 C  CA  B PHE C  1 252 ? 25.832  0.558   -45.160 0.50 12.84  ? 252 PHE C CA  1 
ATOM   6265 C  C   A PHE C  1 252 ? 25.217  0.165   -46.430 0.50 12.15  ? 252 PHE C C   1 
ATOM   6266 C  C   B PHE C  1 252 ? 25.129  -0.181  -46.306 0.50 15.60  ? 252 PHE C C   1 
ATOM   6267 O  O   A PHE C  1 252 ? 24.766  -0.975  -46.458 0.50 15.52  ? 252 PHE C O   1 
ATOM   6268 O  O   B PHE C  1 252 ? 24.830  -1.398  -46.237 0.50 16.78  ? 252 PHE C O   1 
ATOM   6269 C  CB  A PHE C  1 252 ? 26.588  -0.485  -44.460 0.50 12.64  ? 252 PHE C CB  1 
ATOM   6270 C  CB  B PHE C  1 252 ? 26.734  -0.322  -44.348 0.50 13.12  ? 252 PHE C CB  1 
ATOM   6271 C  CG  A PHE C  1 252 ? 27.893  -0.970  -45.109 0.50 11.38  ? 252 PHE C CG  1 
ATOM   6272 C  CG  B PHE C  1 252 ? 28.034  -0.758  -45.062 0.50 11.81  ? 252 PHE C CG  1 
ATOM   6273 C  CD1 A PHE C  1 252 ? 29.055  -0.234  -45.058 0.50 13.19  ? 252 PHE C CD1 1 
ATOM   6274 C  CD1 B PHE C  1 252 ? 29.155  0.097   -45.047 0.50 11.74  ? 252 PHE C CD1 1 
ATOM   6275 C  CD2 A PHE C  1 252 ? 27.916  -2.203  -45.733 0.50 12.79  ? 252 PHE C CD2 1 
ATOM   6276 C  CD2 B PHE C  1 252 ? 28.114  -2.004  -45.646 0.50 14.20  ? 252 PHE C CD2 1 
ATOM   6277 C  CE1 A PHE C  1 252 ? 30.228  -0.725  -45.615 0.50 12.14  ? 252 PHE C CE1 1 
ATOM   6278 C  CE1 B PHE C  1 252 ? 30.383  -0.393  -45.600 0.50 12.45  ? 252 PHE C CE1 1 
ATOM   6279 C  CE2 A PHE C  1 252 ? 29.085  -2.695  -46.283 0.50 13.98  ? 252 PHE C CE2 1 
ATOM   6280 C  CE2 B PHE C  1 252 ? 29.332  -2.433  -46.205 0.50 13.80  ? 252 PHE C CE2 1 
ATOM   6281 C  CZ  A PHE C  1 252 ? 30.231  -1.946  -46.207 0.50 11.96  ? 252 PHE C CZ  1 
ATOM   6282 C  CZ  B PHE C  1 252 ? 30.406  -1.646  -46.140 0.50 13.26  ? 252 PHE C CZ  1 
ATOM   6283 N  N   A ASP C  1 253 ? 25.117  1.058   -47.433 0.50 14.14  ? 253 ASP C N   1 
ATOM   6284 N  N   B ASP C  1 253 ? 24.849  0.631   -47.316 0.50 17.79  ? 253 ASP C N   1 
ATOM   6285 C  CA  A ASP C  1 253 ? 24.230  0.797   -48.598 0.50 15.24  ? 253 ASP C CA  1 
ATOM   6286 C  CA  B ASP C  1 253 ? 24.015  0.286   -48.496 0.50 18.24  ? 253 ASP C CA  1 
ATOM   6287 C  C   A ASP C  1 253 ? 24.968  0.488   -49.862 0.50 14.73  ? 253 ASP C C   1 
ATOM   6288 C  C   B ASP C  1 253 ? 24.812  0.410   -49.785 0.50 16.93  ? 253 ASP C C   1 
ATOM   6289 O  O   A ASP C  1 253 ? 25.863  1.268   -50.155 0.50 15.09  ? 253 ASP C O   1 
ATOM   6290 O  O   B ASP C  1 253 ? 25.589  1.299   -49.985 0.50 19.93  ? 253 ASP C O   1 
ATOM   6291 C  CB  A ASP C  1 253 ? 23.235  1.939   -48.800 0.50 19.35  ? 253 ASP C CB  1 
ATOM   6292 C  CB  B ASP C  1 253 ? 22.769  1.169   -48.473 0.50 21.14  ? 253 ASP C CB  1 
ATOM   6293 C  CG  A ASP C  1 253 ? 22.283  2.042   -47.606 0.50 19.55  ? 253 ASP C CG  1 
ATOM   6294 C  CG  B ASP C  1 253 ? 21.499  0.571   -49.288 0.50 31.11  ? 253 ASP C CG  1 
ATOM   6295 O  OD1 A ASP C  1 253 ? 21.686  0.938   -47.290 0.50 26.46  ? 253 ASP C OD1 1 
ATOM   6296 O  OD1 B ASP C  1 253 ? 20.841  -0.519  -48.980 0.50 27.07  ? 253 ASP C OD1 1 
ATOM   6297 O  OD2 A ASP C  1 253 ? 22.215  3.112   -46.924 0.50 28.44  ? 253 ASP C OD2 1 
ATOM   6298 O  OD2 B ASP C  1 253 ? 21.116  1.287   -50.220 0.50 38.03  ? 253 ASP C OD2 1 
ATOM   6299 N  N   . GLU C  1 254 ? 24.592  -0.586  -50.614 1.00 16.39  ? 254 GLU C N   1 
ATOM   6300 C  CA  . GLU C  1 254 ? 25.213  -0.783  -51.895 1.00 17.69  ? 254 GLU C CA  1 
ATOM   6301 C  C   . GLU C  1 254 ? 26.723  -0.869  -51.723 1.00 16.48  ? 254 GLU C C   1 
ATOM   6302 O  O   . GLU C  1 254 ? 27.509  -0.363  -52.575 1.00 18.78  ? 254 GLU C O   1 
ATOM   6303 C  CB  . GLU C  1 254 ? 24.797  0.255   -52.870 1.00 19.92  ? 254 GLU C CB  1 
ATOM   6304 C  CG  . GLU C  1 254 ? 23.323  0.173   -53.163 1.00 24.44  ? 254 GLU C CG  1 
ATOM   6305 C  CD  . GLU C  1 254 ? 23.020  -1.108  -53.881 1.00 30.95  ? 254 GLU C CD  1 
ATOM   6306 O  OE1 . GLU C  1 254 ? 23.608  -1.419  -54.937 1.00 54.09  ? 254 GLU C OE1 1 
ATOM   6307 O  OE2 . GLU C  1 254 ? 22.082  -1.799  -53.365 1.00 40.13  ? 254 GLU C OE2 1 
ATOM   6308 N  N   . ARG C  1 255 ? 27.148  -1.524  -50.629 1.00 15.49  ? 255 ARG C N   1 
ATOM   6309 C  CA  . ARG C  1 255 ? 28.596  -1.699  -50.339 1.00 14.99  ? 255 ARG C CA  1 
ATOM   6310 C  C   . ARG C  1 255 ? 28.827  -3.128  -49.856 1.00 14.21  ? 255 ARG C C   1 
ATOM   6311 O  O   . ARG C  1 255 ? 27.961  -3.787  -49.318 1.00 16.66  ? 255 ARG C O   1 
ATOM   6312 C  CB  . ARG C  1 255 ? 29.181  -0.684  -49.343 1.00 14.63  ? 255 ARG C CB  1 
ATOM   6313 C  CG  . ARG C  1 255 ? 29.073  0.728   -49.839 1.00 16.15  ? 255 ARG C CG  1 
ATOM   6314 C  CD  . ARG C  1 255 ? 29.654  1.683   -48.800 1.00 16.05  ? 255 ARG C CD  1 
ATOM   6315 N  NE  . ARG C  1 255 ? 31.043  1.322   -48.563 1.00 16.89  ? 255 ARG C NE  1 
ATOM   6316 C  CZ  . ARG C  1 255 ? 31.745  1.665   -47.494 1.00 14.55  ? 255 ARG C CZ  1 
ATOM   6317 N  NH1 . ARG C  1 255 ? 31.196  2.402   -46.536 1.00 16.65  ? 255 ARG C NH1 1 
ATOM   6318 N  NH2 . ARG C  1 255 ? 33.005  1.271   -47.384 1.00 14.90  ? 255 ARG C NH2 1 
ATOM   6319 N  N   . LEU C  1 256 ? 30.099  -3.586  -50.042 1.00 15.00  ? 256 LEU C N   1 
ATOM   6320 C  CA  . LEU C  1 256 ? 30.475  -4.919  -49.618 1.00 14.54  ? 256 LEU C CA  1 
ATOM   6321 C  C   . LEU C  1 256 ? 31.470  -4.834  -48.482 1.00 14.61  ? 256 LEU C C   1 
ATOM   6322 O  O   . LEU C  1 256 ? 32.200  -3.848  -48.306 1.00 14.86  ? 256 LEU C O   1 
ATOM   6323 C  CB  . LEU C  1 256 ? 31.190  -5.653  -50.781 1.00 18.03  ? 256 LEU C CB  1 
ATOM   6324 C  CG  . LEU C  1 256 ? 30.269  -5.966  -51.997 1.00 18.32  ? 256 LEU C CG  1 
ATOM   6325 C  CD1 . LEU C  1 256 ? 31.128  -6.415  -53.161 1.00 25.36  ? 256 LEU C CD1 1 
ATOM   6326 C  CD2 . LEU C  1 256 ? 29.172  -6.966  -51.599 1.00 23.52  ? 256 LEU C CD2 1 
ATOM   6327 N  N   . VAL C  1 257 ? 31.501  -5.880  -47.676 1.00 14.19  ? 257 VAL C N   1 
ATOM   6328 C  CA  . VAL C  1 257 ? 32.625  -6.082  -46.699 1.00 13.27  ? 257 VAL C CA  1 
ATOM   6329 C  C   . VAL C  1 257 ? 33.413  -7.262  -47.292 1.00 13.49  ? 257 VAL C C   1 
ATOM   6330 O  O   . VAL C  1 257 ? 32.838  -8.325  -47.657 1.00 15.24  ? 257 VAL C O   1 
ATOM   6331 C  CB  . VAL C  1 257 ? 32.070  -6.420  -45.370 1.00 14.60  ? 257 VAL C CB  1 
ATOM   6332 C  CG1 . VAL C  1 257 ? 33.212  -6.846  -44.418 1.00 17.31  ? 257 VAL C CG1 1 
ATOM   6333 C  CG2 . VAL C  1 257 ? 31.437  -5.198  -44.765 1.00 16.39  ? 257 VAL C CG2 1 
ATOM   6334 N  N   . TYR C  1 258 ? 34.718  -7.053  -47.466 1.00 13.31  ? 258 TYR C N   1 
ATOM   6335 C  CA  . TYR C  1 258 ? 35.520  -8.081  -48.065 1.00 13.06  ? 258 TYR C CA  1 
ATOM   6336 C  C   . TYR C  1 258 ? 36.069  -8.996  -46.982 1.00 14.00  ? 258 TYR C C   1 
ATOM   6337 O  O   . TYR C  1 258 ? 36.395  -8.566  -45.876 1.00 15.58  ? 258 TYR C O   1 
ATOM   6338 C  CB  . TYR C  1 258 ? 36.645  -7.374  -48.854 1.00 13.99  ? 258 TYR C CB  1 
ATOM   6339 C  CG  . TYR C  1 258 ? 36.049  -6.499  -49.910 1.00 15.85  ? 258 TYR C CG  1 
ATOM   6340 C  CD1 . TYR C  1 258 ? 35.566  -7.060  -51.106 1.00 18.26  ? 258 TYR C CD1 1 
ATOM   6341 C  CD2 . TYR C  1 258 ? 35.853  -5.108  -49.676 1.00 17.22  ? 258 TYR C CD2 1 
ATOM   6342 C  CE1 . TYR C  1 258 ? 34.944  -6.277  -52.068 1.00 20.44  ? 258 TYR C CE1 1 
ATOM   6343 C  CE2 . TYR C  1 258 ? 35.205  -4.300  -50.577 1.00 20.93  ? 258 TYR C CE2 1 
ATOM   6344 C  CZ  . TYR C  1 258 ? 34.787  -4.883  -51.791 1.00 19.18  ? 258 TYR C CZ  1 
ATOM   6345 O  OH  . TYR C  1 258 ? 34.108  -4.070  -52.703 1.00 24.39  ? 258 TYR C OH  1 
ATOM   6346 N  N   . THR C  1 259 ? 36.183  -10.295 -47.314 1.00 14.36  ? 259 THR C N   1 
ATOM   6347 C  CA  . THR C  1 259 ? 36.616  -11.241 -46.331 1.00 13.44  ? 259 THR C CA  1 
ATOM   6348 C  C   . THR C  1 259 ? 37.803  -12.029 -46.810 1.00 15.54  ? 259 THR C C   1 
ATOM   6349 O  O   . THR C  1 259 ? 37.987  -12.310 -47.990 1.00 16.55  ? 259 THR C O   1 
ATOM   6350 C  CB  . THR C  1 259 ? 35.510  -12.223 -45.908 1.00 15.86  ? 259 THR C CB  1 
ATOM   6351 O  OG1 . THR C  1 259 ? 35.083  -12.945 -47.127 1.00 18.39  ? 259 THR C OG1 1 
ATOM   6352 C  CG2 . THR C  1 259 ? 34.281  -11.574 -45.306 1.00 16.30  ? 259 THR C CG2 1 
ATOM   6353 N  N   . SER C  1 260 ? 38.718  -12.336 -45.855 1.00 16.10  ? 260 SER C N   1 
ATOM   6354 C  CA  . SER C  1 260 ? 39.945  -13.061 -46.199 1.00 19.17  ? 260 SER C CA  1 
ATOM   6355 C  C   . SER C  1 260 ? 39.647  -14.509 -46.200 1.00 19.81  ? 260 SER C C   1 
ATOM   6356 O  O   . SER C  1 260 ? 40.569  -15.365 -46.544 1.00 28.68  ? 260 SER C O   1 
ATOM   6357 C  CB  . SER C  1 260 ? 41.049  -12.785 -45.189 1.00 20.09  ? 260 SER C CB  1 
ATOM   6358 O  OG  . SER C  1 260 ? 40.627  -13.277 -43.963 1.00 17.82  ? 260 SER C OG  1 
ATOM   6359 N  N   . PHE C  1 261 ? 38.479  -14.961 -45.791 1.00 20.45  ? 261 PHE C N   1 
ATOM   6360 C  CA  . PHE C  1 261 ? 38.114  -16.322 -45.630 1.00 21.46  ? 261 PHE C CA  1 
ATOM   6361 C  C   . PHE C  1 261 ? 36.985  -16.594 -46.483 1.00 22.67  ? 261 PHE C C   1 
ATOM   6362 O  O   . PHE C  1 261 ? 36.275  -15.681 -46.957 1.00 26.68  ? 261 PHE C O   1 
ATOM   6363 C  CB  . PHE C  1 261 ? 37.728  -16.597 -44.156 1.00 21.32  ? 261 PHE C CB  1 
ATOM   6364 C  CG  . PHE C  1 261 ? 36.640  -15.625 -43.629 1.00 18.77  ? 261 PHE C CG  1 
ATOM   6365 C  CD1 . PHE C  1 261 ? 35.330  -15.895 -43.818 1.00 20.45  ? 261 PHE C CD1 1 
ATOM   6366 C  CD2 . PHE C  1 261 ? 36.990  -14.474 -43.043 1.00 18.91  ? 261 PHE C CD2 1 
ATOM   6367 C  CE1 . PHE C  1 261 ? 34.329  -15.016 -43.217 1.00 23.59  ? 261 PHE C CE1 1 
ATOM   6368 C  CE2 . PHE C  1 261 ? 36.086  -13.666 -42.463 1.00 19.62  ? 261 PHE C CE2 1 
ATOM   6369 C  CZ  . PHE C  1 261 ? 34.734  -13.842 -42.573 1.00 21.13  ? 261 PHE C CZ  1 
ATOM   6370 N  N   . SER C  1 262 ? 36.779  -17.842 -46.877 1.00 32.33  ? 262 SER C N   1 
ATOM   6371 C  CA  . SER C  1 262 ? 35.684  -18.087 -47.825 1.00 39.15  ? 262 SER C CA  1 
ATOM   6372 C  C   . SER C  1 262 ? 34.629  -19.065 -47.350 1.00 58.52  ? 262 SER C C   1 
ATOM   6373 O  O   . SER C  1 262 ? 33.522  -19.128 -47.887 1.00 71.21  ? 262 SER C O   1 
ATOM   6374 C  CB  . SER C  1 262 ? 36.244  -18.549 -49.173 1.00 68.74  ? 262 SER C CB  1 
ATOM   6375 O  OG  . SER C  1 262 ? 35.228  -19.119 -49.980 1.00 76.86  ? 262 SER C OG  1 
ATOM   6376 N  N   . GLN C  1 263 ? 34.992  -19.824 -46.334 1.00 47.72  ? 263 GLN C N   1 
ATOM   6377 C  CA  . GLN C  1 263 ? 34.097  -20.860 -45.736 1.00 35.49  ? 263 GLN C CA  1 
ATOM   6378 C  C   . GLN C  1 263 ? 33.762  -20.544 -44.218 1.00 54.81  ? 263 GLN C C   1 
ATOM   6379 O  O   . GLN C  1 263 ? 34.618  -19.935 -43.589 1.00 57.10  ? 263 GLN C O   1 
ATOM   6380 C  CB  . GLN C  1 263 ? 34.656  -22.262 -46.029 1.00 36.56  ? 263 GLN C CB  1 
ATOM   6381 C  CG  . GLN C  1 263 ? 36.106  -22.483 -45.501 1.00 41.53  ? 263 GLN C CG  1 
ATOM   6382 C  CD  . GLN C  1 263 ? 36.724  -23.922 -45.765 1.00 28.71  ? 263 GLN C CD  1 
ATOM   6383 O  OE1 . GLN C  1 263 ? 37.906  -24.197 -45.344 1.00 33.43  ? 263 GLN C OE1 1 
ATOM   6384 N  NE2 . GLN C  1 263 ? 35.984  -24.774 -46.525 1.00 21.50  ? 263 GLN C NE2 1 
ATOM   6385 N  N   . LYS D  1 3   ? 14.028  19.621  -45.512 1.00 42.28  ? 3   LYS D N   1 
ATOM   6386 C  CA  . LYS D  1 3   ? 14.732  18.834  -46.578 1.00 36.76  ? 3   LYS D CA  1 
ATOM   6387 C  C   . LYS D  1 3   ? 15.416  17.650  -45.874 1.00 28.98  ? 3   LYS D C   1 
ATOM   6388 O  O   . LYS D  1 3   ? 16.322  17.036  -46.460 1.00 29.74  ? 3   LYS D O   1 
ATOM   6389 C  CB  . LYS D  1 3   ? 15.820  19.605  -47.299 1.00 44.89  ? 3   LYS D CB  1 
ATOM   6390 C  CG  . LYS D  1 3   ? 16.818  20.294  -46.355 1.00 52.82  ? 3   LYS D CG  1 
ATOM   6391 N  N   . TRP D  1 4   ? 14.977  17.212  -44.633 1.00 17.21  ? 4   TRP D N   1 
ATOM   6392 C  CA  . TRP D  1 4   ? 15.602  16.044  -44.061 1.00 15.72  ? 4   TRP D CA  1 
ATOM   6393 C  C   . TRP D  1 4   ? 15.327  14.800  -44.924 1.00 13.99  ? 4   TRP D C   1 
ATOM   6394 O  O   . TRP D  1 4   ? 14.308  14.742  -45.641 1.00 16.15  ? 4   TRP D O   1 
ATOM   6395 C  CB  . TRP D  1 4   ? 15.050  15.811  -42.632 1.00 14.34  ? 4   TRP D CB  1 
ATOM   6396 C  CG  . TRP D  1 4   ? 13.638  15.532  -42.472 1.00 13.22  ? 4   TRP D CG  1 
ATOM   6397 C  CD1 . TRP D  1 4   ? 12.548  16.393  -42.281 1.00 15.39  ? 4   TRP D CD1 1 
ATOM   6398 C  CD2 . TRP D  1 4   ? 13.032  14.190  -42.467 1.00 13.76  ? 4   TRP D CD2 1 
ATOM   6399 N  NE1 . TRP D  1 4   ? 11.388  15.707  -42.189 1.00 16.16  ? 4   TRP D NE1 1 
ATOM   6400 C  CE2 . TRP D  1 4   ? 11.625  14.371  -42.277 1.00 13.47  ? 4   TRP D CE2 1 
ATOM   6401 C  CE3 . TRP D  1 4   ? 13.556  12.894  -42.575 1.00 13.24  ? 4   TRP D CE3 1 
ATOM   6402 C  CZ2 . TRP D  1 4   ? 10.744  13.279  -42.198 1.00 14.61  ? 4   TRP D CZ2 1 
ATOM   6403 C  CZ3 . TRP D  1 4   ? 12.637  11.809  -42.477 1.00 13.69  ? 4   TRP D CZ3 1 
ATOM   6404 C  CH2 . TRP D  1 4   ? 11.272  12.010  -42.275 1.00 14.18  ? 4   TRP D CH2 1 
ATOM   6405 N  N   . THR D  1 5   ? 16.279  13.870  -44.875 1.00 14.05  ? 5   THR D N   1 
ATOM   6406 C  CA  . THR D  1 5   ? 16.216  12.634  -45.653 1.00 13.67  ? 5   THR D CA  1 
ATOM   6407 C  C   . THR D  1 5   ? 16.653  11.442  -44.818 1.00 13.73  ? 5   THR D C   1 
ATOM   6408 O  O   . THR D  1 5   ? 17.032  11.617  -43.639 1.00 13.37  ? 5   THR D O   1 
ATOM   6409 C  CB  . THR D  1 5   ? 17.139  12.765  -46.927 1.00 15.72  ? 5   THR D CB  1 
ATOM   6410 O  OG1 . THR D  1 5   ? 18.472  12.697  -46.387 1.00 18.34  ? 5   THR D OG1 1 
ATOM   6411 C  CG2 . THR D  1 5   ? 16.897  13.993  -47.736 1.00 17.59  ? 5   THR D CG2 1 
ATOM   6412 N  N   . TYR D  1 6   ? 16.718  10.295  -45.471 1.00 13.37  ? 6   TYR D N   1 
ATOM   6413 C  CA  . TYR D  1 6   ? 17.253  9.110   -44.868 1.00 13.57  ? 6   TYR D CA  1 
ATOM   6414 C  C   . TYR D  1 6   ? 18.613  8.742   -45.445 1.00 13.58  ? 6   TYR D C   1 
ATOM   6415 O  O   . TYR D  1 6   ? 19.162  7.655   -45.091 1.00 14.90  ? 6   TYR D O   1 
ATOM   6416 C  CB  . TYR D  1 6   ? 16.341  7.877   -45.032 1.00 13.45  ? 6   TYR D CB  1 
ATOM   6417 C  CG  . TYR D  1 6   ? 15.108  8.009   -44.162 1.00 11.52  ? 6   TYR D CG  1 
ATOM   6418 C  CD1 . TYR D  1 6   ? 15.125  7.539   -42.863 1.00 11.69  ? 6   TYR D CD1 1 
ATOM   6419 C  CD2 . TYR D  1 6   ? 13.959  8.516   -44.610 1.00 11.70  ? 6   TYR D CD2 1 
ATOM   6420 C  CE1 . TYR D  1 6   ? 13.954  7.574   -42.035 1.00 11.01  ? 6   TYR D CE1 1 
ATOM   6421 C  CE2 . TYR D  1 6   ? 12.777  8.564   -43.874 1.00 11.50  ? 6   TYR D CE2 1 
ATOM   6422 C  CZ  . TYR D  1 6   ? 12.780  8.087   -42.559 1.00 11.20  ? 6   TYR D CZ  1 
ATOM   6423 O  OH  . TYR D  1 6   ? 11.631  8.090   -41.852 1.00 11.97  ? 6   TYR D OH  1 
ATOM   6424 N  N   . PHE D  1 7   ? 19.225  9.548   -46.268 1.00 15.41  ? 7   PHE D N   1 
ATOM   6425 C  CA  . PHE D  1 7   ? 20.491  9.145   -46.875 1.00 18.62  ? 7   PHE D CA  1 
ATOM   6426 C  C   . PHE D  1 7   ? 21.204  10.402  -47.271 1.00 20.34  ? 7   PHE D C   1 
ATOM   6427 O  O   . PHE D  1 7   ? 20.602  11.299  -47.901 1.00 26.80  ? 7   PHE D O   1 
ATOM   6428 C  CB  . PHE D  1 7   ? 20.198  8.327   -48.205 1.00 27.04  ? 7   PHE D CB  1 
ATOM   6429 C  CG  . PHE D  1 7   ? 21.408  7.905   -48.957 1.00 30.23  ? 7   PHE D CG  1 
ATOM   6430 C  CD1 . PHE D  1 7   ? 22.250  6.832   -48.477 1.00 33.41  ? 7   PHE D CD1 1 
ATOM   6431 C  CD2 . PHE D  1 7   ? 21.816  8.582   -50.173 1.00 35.36  ? 7   PHE D CD2 1 
ATOM   6432 C  CE1 . PHE D  1 7   ? 23.390  6.459   -49.170 1.00 35.12  ? 7   PHE D CE1 1 
ATOM   6433 C  CE2 . PHE D  1 7   ? 22.967  8.182   -50.864 1.00 46.63  ? 7   PHE D CE2 1 
ATOM   6434 C  CZ  . PHE D  1 7   ? 23.732  7.135   -50.351 1.00 55.19  ? 7   PHE D CZ  1 
ATOM   6435 N  N   . GLY D  1 8   ? 22.535  10.389  -47.102 1.00 18.70  ? 8   GLY D N   1 
ATOM   6436 C  CA  . GLY D  1 8   ? 23.425  11.478  -47.625 1.00 20.83  ? 8   GLY D CA  1 
ATOM   6437 C  C   . GLY D  1 8   ? 23.473  12.589  -46.577 1.00 20.42  ? 8   GLY D C   1 
ATOM   6438 O  O   . GLY D  1 8   ? 23.190  12.382  -45.315 1.00 20.53  ? 8   GLY D O   1 
ATOM   6439 N  N   . PRO D  1 9   ? 23.849  13.778  -46.994 1.00 21.31  ? 9   PRO D N   1 
ATOM   6440 C  CA  . PRO D  1 9   ? 24.185  14.852  -46.076 1.00 22.51  ? 9   PRO D CA  1 
ATOM   6441 C  C   . PRO D  1 9   ? 23.111  15.262  -45.095 1.00 20.74  ? 9   PRO D C   1 
ATOM   6442 O  O   . PRO D  1 9   ? 23.460  15.793  -44.055 1.00 21.35  ? 9   PRO D O   1 
ATOM   6443 C  CB  . PRO D  1 9   ? 24.637  16.064  -46.961 1.00 26.12  ? 9   PRO D CB  1 
ATOM   6444 C  CG  . PRO D  1 9   ? 24.443  15.595  -48.324 1.00 31.11  ? 9   PRO D CG  1 
ATOM   6445 C  CD  . PRO D  1 9   ? 24.118  14.112  -48.402 1.00 25.56  ? 9   PRO D CD  1 
ATOM   6446 N  N   . ASP D  1 10  ? 21.815  15.150  -45.483 1.00 19.75  ? 10  ASP D N   1 
ATOM   6447 C  CA  . ASP D  1 10  ? 20.687  15.545  -44.639 1.00 18.03  ? 10  ASP D CA  1 
ATOM   6448 C  C   . ASP D  1 10  ? 20.046  14.309  -43.974 1.00 15.11  ? 10  ASP D C   1 
ATOM   6449 O  O   . ASP D  1 10  ? 18.909  14.447  -43.503 1.00 14.89  ? 10  ASP D O   1 
ATOM   6450 C  CB  . ASP D  1 10  ? 19.606  16.336  -45.459 1.00 18.69  ? 10  ASP D CB  1 
ATOM   6451 C  CG  . ASP D  1 10  ? 20.218  17.554  -46.117 1.00 27.52  ? 10  ASP D CG  1 
ATOM   6452 O  OD1 . ASP D  1 10  ? 20.931  18.271  -45.443 1.00 27.92  ? 10  ASP D OD1 1 
ATOM   6453 O  OD2 . ASP D  1 10  ? 20.127  17.748  -47.343 1.00 28.50  ? 10  ASP D OD2 1 
ATOM   6454 N  N   . GLY D  1 11  ? 20.753  13.193  -43.931 1.00 15.76  ? 11  GLY D N   1 
ATOM   6455 C  CA  . GLY D  1 11  ? 20.212  11.963  -43.315 1.00 13.61  ? 11  GLY D CA  1 
ATOM   6456 C  C   . GLY D  1 11  ? 20.311  12.030  -41.794 1.00 12.26  ? 11  GLY D C   1 
ATOM   6457 O  O   . GLY D  1 11  ? 20.495  13.084  -41.160 1.00 12.38  ? 11  GLY D O   1 
ATOM   6458 N  N   . GLU D  1 12  ? 20.016  10.869  -41.190 1.00 11.68  ? 12  GLU D N   1 
ATOM   6459 C  CA  . GLU D  1 12  ? 19.597  10.830  -39.792 1.00 10.98  ? 12  GLU D CA  1 
ATOM   6460 C  C   . GLU D  1 12  ? 20.666  11.306  -38.807 1.00 10.69  ? 12  GLU D C   1 
ATOM   6461 O  O   . GLU D  1 12  ? 20.272  11.797  -37.753 1.00 11.30  ? 12  GLU D O   1 
ATOM   6462 C  CB  . GLU D  1 12  ? 19.127  9.414   -39.414 1.00 11.01  ? 12  GLU D CB  1 
ATOM   6463 C  CG  . GLU D  1 12  ? 20.235  8.406   -39.303 1.00 11.61  ? 12  GLU D CG  1 
ATOM   6464 C  CD  . GLU D  1 12  ? 19.634  6.987   -39.335 1.00 11.82  ? 12  GLU D CD  1 
ATOM   6465 O  OE1 . GLU D  1 12  ? 19.257  6.495   -38.246 1.00 11.35  ? 12  GLU D OE1 1 
ATOM   6466 O  OE2 . GLU D  1 12  ? 19.469  6.446   -40.447 1.00 12.59  ? 12  GLU D OE2 1 
ATOM   6467 N  N   . ASN D  1 13  ? 21.928  11.218  -39.129 1.00 11.26  ? 13  ASN D N   1 
ATOM   6468 C  CA  . ASN D  1 13  ? 22.952  11.738  -38.206 1.00 11.12  ? 13  ASN D CA  1 
ATOM   6469 C  C   . ASN D  1 13  ? 22.956  13.265  -38.213 1.00 11.51  ? 13  ASN D C   1 
ATOM   6470 O  O   . ASN D  1 13  ? 23.606  13.800  -37.291 1.00 12.93  ? 13  ASN D O   1 
ATOM   6471 C  CB  . ASN D  1 13  ? 24.360  11.227  -38.553 1.00 12.11  ? 13  ASN D CB  1 
ATOM   6472 C  CG  . ASN D  1 13  ? 24.528  9.723   -38.264 1.00 11.31  ? 13  ASN D CG  1 
ATOM   6473 O  OD1 . ASN D  1 13  ? 23.593  9.064   -37.765 1.00 11.68  ? 13  ASN D OD1 1 
ATOM   6474 N  ND2 . ASN D  1 13  ? 25.691  9.199   -38.529 1.00 12.14  ? 13  ASN D ND2 1 
ATOM   6475 N  N   . SER D  1 14  ? 22.283  13.899  -39.134 1.00 11.05  ? 14  SER D N   1 
ATOM   6476 C  CA  . SER D  1 14  ? 22.208  15.377  -39.266 1.00 10.79  ? 14  SER D CA  1 
ATOM   6477 C  C   . SER D  1 14  ? 20.874  15.925  -38.820 1.00 10.86  ? 14  SER D C   1 
ATOM   6478 O  O   . SER D  1 14  ? 20.771  17.138  -38.686 1.00 12.08  ? 14  SER D O   1 
ATOM   6479 C  CB  . SER D  1 14  ? 22.531  15.741  -40.690 1.00 12.36  ? 14  SER D CB  1 
ATOM   6480 O  OG  . SER D  1 14  ? 23.899  15.473  -40.946 1.00 15.15  ? 14  SER D OG  1 
ATOM   6481 N  N   . TRP D  1 15  ? 19.871  15.099  -38.533 1.00 10.75  ? 15  TRP D N   1 
ATOM   6482 C  CA  . TRP D  1 15  ? 18.575  15.645  -38.153 1.00 11.56  ? 15  TRP D CA  1 
ATOM   6483 C  C   . TRP D  1 15  ? 18.649  16.599  -36.981 1.00 10.71  ? 15  TRP D C   1 
ATOM   6484 O  O   . TRP D  1 15  ? 17.941  17.606  -36.968 1.00 11.83  ? 15  TRP D O   1 
ATOM   6485 C  CB  . TRP D  1 15  ? 17.599  14.495  -37.780 1.00 11.24  ? 15  TRP D CB  1 
ATOM   6486 C  CG  . TRP D  1 15  ? 17.220  13.612  -38.966 1.00 10.34  ? 15  TRP D CG  1 
ATOM   6487 C  CD1 . TRP D  1 15  ? 17.469  13.790  -40.311 1.00 11.22  ? 15  TRP D CD1 1 
ATOM   6488 C  CD2 . TRP D  1 15  ? 16.447  12.403  -38.851 1.00 10.70  ? 15  TRP D CD2 1 
ATOM   6489 N  NE1 . TRP D  1 15  ? 16.941  12.727  -41.007 1.00 11.00  ? 15  TRP D NE1 1 
ATOM   6490 C  CE2 . TRP D  1 15  ? 16.268  11.893  -40.137 1.00 10.13  ? 15  TRP D CE2 1 
ATOM   6491 C  CE3 . TRP D  1 15  ? 15.880  11.715  -37.762 1.00 10.72  ? 15  TRP D CE3 1 
ATOM   6492 C  CZ2 . TRP D  1 15  ? 15.589  10.695  -40.398 1.00 11.03  ? 15  TRP D CZ2 1 
ATOM   6493 C  CZ3 . TRP D  1 15  ? 15.204  10.549  -38.005 1.00 11.46  ? 15  TRP D CZ3 1 
ATOM   6494 C  CH2 . TRP D  1 15  ? 15.016  10.063  -39.311 1.00 11.19  ? 15  TRP D CH2 1 
ATOM   6495 N  N   . SER D  1 16  ? 19.493  16.267  -36.013 1.00 11.56  ? 16  SER D N   1 
ATOM   6496 C  CA  . SER D  1 16  ? 19.550  17.108  -34.783 1.00 12.24  ? 16  SER D CA  1 
ATOM   6497 C  C   . SER D  1 16  ? 20.077  18.503  -35.056 1.00 12.38  ? 16  SER D C   1 
ATOM   6498 O  O   . SER D  1 16  ? 19.852  19.339  -34.216 1.00 13.55  ? 16  SER D O   1 
ATOM   6499 C  CB  . SER D  1 16  ? 20.478  16.465  -33.818 1.00 13.73  ? 16  SER D CB  1 
ATOM   6500 O  OG  . SER D  1 16  ? 21.830  16.531  -34.325 1.00 18.67  ? 16  SER D OG  1 
ATOM   6501 N  N   . LYS D  1 17  ? 20.637  18.777  -36.224 1.00 11.49  ? 17  LYS D N   1 
ATOM   6502 C  CA  . LYS D  1 17  ? 21.069  20.137  -36.512 1.00 12.67  ? 17  LYS D CA  1 
ATOM   6503 C  C   . LYS D  1 17  ? 19.895  21.067  -36.619 1.00 12.99  ? 17  LYS D C   1 
ATOM   6504 O  O   . LYS D  1 17  ? 20.055  22.293  -36.320 1.00 14.80  ? 17  LYS D O   1 
ATOM   6505 C  CB  . LYS D  1 17  ? 21.871  20.194  -37.816 1.00 13.13  ? 17  LYS D CB  1 
ATOM   6506 C  CG  . LYS D  1 17  ? 23.095  19.353  -37.831 1.00 13.80  ? 17  LYS D CG  1 
ATOM   6507 C  CD  . LYS D  1 17  ? 23.730  19.336  -39.235 1.00 14.83  ? 17  LYS D CD  1 
ATOM   6508 C  CE  . LYS D  1 17  ? 24.867  18.384  -39.418 1.00 14.04  ? 17  LYS D CE  1 
ATOM   6509 N  NZ  . LYS D  1 17  ? 25.576  18.547  -40.740 1.00 15.91  ? 17  LYS D NZ  1 
ATOM   6510 N  N   . LYS D  1 18  ? 18.753  20.635  -37.065 1.00 12.74  ? 18  LYS D N   1 
ATOM   6511 C  CA  . LYS D  1 18  ? 17.538  21.444  -37.256 1.00 13.32  ? 18  LYS D CA  1 
ATOM   6512 C  C   . LYS D  1 18  ? 16.475  21.062  -36.268 1.00 14.10  ? 18  LYS D C   1 
ATOM   6513 O  O   . LYS D  1 18  ? 15.540  21.819  -36.074 1.00 16.98  ? 18  LYS D O   1 
ATOM   6514 C  CB  . LYS D  1 18  ? 17.006  21.272  -38.701 1.00 15.98  ? 18  LYS D CB  1 
ATOM   6515 C  CG  . LYS D  1 18  ? 17.914  21.975  -39.723 1.00 21.42  ? 18  LYS D CG  1 
ATOM   6516 C  CD  . LYS D  1 18  ? 17.281  21.755  -41.143 1.00 23.44  ? 18  LYS D CD  1 
ATOM   6517 C  CE  . LYS D  1 18  ? 18.077  22.537  -42.162 1.00 32.22  ? 18  LYS D CE  1 
ATOM   6518 N  NZ  . LYS D  1 18  ? 17.574  22.206  -43.524 1.00 39.29  ? 18  LYS D NZ  1 
ATOM   6519 N  N   . TYR D  1 19  ? 16.517  19.822  -35.753 1.00 12.34  ? 19  TYR D N   1 
ATOM   6520 C  CA  . TYR D  1 19  ? 15.442  19.250  -34.893 1.00 12.48  ? 19  TYR D CA  1 
ATOM   6521 C  C   . TYR D  1 19  ? 16.033  18.782  -33.628 1.00 13.21  ? 19  TYR D C   1 
ATOM   6522 O  O   . TYR D  1 19  ? 16.497  17.620  -33.547 1.00 12.96  ? 19  TYR D O   1 
ATOM   6523 C  CB  . TYR D  1 19  ? 14.743  18.069  -35.674 1.00 13.54  ? 19  TYR D CB  1 
ATOM   6524 C  CG  . TYR D  1 19  ? 14.146  18.494  -36.970 1.00 12.50  ? 19  TYR D CG  1 
ATOM   6525 C  CD1 . TYR D  1 19  ? 12.942  19.206  -37.023 1.00 14.52  ? 19  TYR D CD1 1 
ATOM   6526 C  CD2 . TYR D  1 19  ? 14.835  18.272  -38.155 1.00 13.37  ? 19  TYR D CD2 1 
ATOM   6527 C  CE1 . TYR D  1 19  ? 12.368  19.581  -38.268 1.00 17.69  ? 19  TYR D CE1 1 
ATOM   6528 C  CE2 . TYR D  1 19  ? 14.285  18.681  -39.377 1.00 15.70  ? 19  TYR D CE2 1 
ATOM   6529 C  CZ  . TYR D  1 19  ? 13.091  19.295  -39.425 1.00 17.50  ? 19  TYR D CZ  1 
ATOM   6530 O  OH  . TYR D  1 19  ? 12.570  19.663  -40.657 1.00 21.17  ? 19  TYR D OH  1 
ATOM   6531 N  N   . PRO D  1 20  ? 16.161  19.639  -32.579 1.00 13.47  ? 20  PRO D N   1 
ATOM   6532 C  CA  . PRO D  1 20  ? 16.964  19.272  -31.457 1.00 14.56  ? 20  PRO D CA  1 
ATOM   6533 C  C   . PRO D  1 20  ? 16.469  18.012  -30.712 1.00 13.18  ? 20  PRO D C   1 
ATOM   6534 O  O   . PRO D  1 20  ? 17.293  17.331  -30.125 1.00 13.73  ? 20  PRO D O   1 
ATOM   6535 C  CB  . PRO D  1 20  ? 16.821  20.537  -30.508 1.00 17.10  ? 20  PRO D CB  1 
ATOM   6536 C  CG  . PRO D  1 20  ? 16.281  21.511  -31.318 1.00 20.56  ? 20  PRO D CG  1 
ATOM   6537 C  CD  . PRO D  1 20  ? 15.698  21.066  -32.579 1.00 14.02  ? 20  PRO D CD  1 
ATOM   6538 N  N   . SER D  1 21  ? 15.163  17.731  -30.775 1.00 13.25  ? 21  SER D N   1 
ATOM   6539 C  CA  . SER D  1 21  ? 14.762  16.507  -30.037 1.00 13.12  ? 21  SER D CA  1 
ATOM   6540 C  C   . SER D  1 21  ? 15.339  15.233  -30.678 1.00 12.64  ? 21  SER D C   1 
ATOM   6541 O  O   . SER D  1 21  ? 15.342  14.244  -29.978 1.00 14.03  ? 21  SER D O   1 
ATOM   6542 C  CB  . SER D  1 21  ? 13.267  16.417  -29.973 1.00 14.07  ? 21  SER D CB  1 
ATOM   6543 O  OG  . SER D  1 21  ? 12.692  17.441  -29.173 1.00 16.33  ? 21  SER D OG  1 
ATOM   6544 N  N   . CYS D  1 22  ? 15.757  15.276  -31.935 1.00 11.79  ? 22  CYS D N   1 
ATOM   6545 C  CA  . CYS D  1 22  ? 16.299  14.095  -32.530 1.00 12.06  ? 22  CYS D CA  1 
ATOM   6546 C  C   . CYS D  1 22  ? 17.650  13.738  -31.899 1.00 14.18  ? 22  CYS D C   1 
ATOM   6547 O  O   . CYS D  1 22  ? 18.129  12.626  -32.070 1.00 14.76  ? 22  CYS D O   1 
ATOM   6548 C  CB  . CYS D  1 22  ? 16.487  14.298  -34.037 1.00 12.84  ? 22  CYS D CB  1 
ATOM   6549 S  SG  . CYS D  1 22  ? 14.987  14.588  -34.955 1.00 12.38  ? 22  CYS D SG  1 
ATOM   6550 N  N   . GLY D  1 23  ? 18.295  14.705  -31.151 1.00 14.15  ? 23  GLY D N   1 
ATOM   6551 C  CA  . GLY D  1 23  ? 19.441  14.465  -30.348 1.00 15.63  ? 23  GLY D CA  1 
ATOM   6552 C  C   . GLY D  1 23  ? 19.176  14.399  -28.848 1.00 16.80  ? 23  GLY D C   1 
ATOM   6553 O  O   . GLY D  1 23  ? 20.146  14.393  -28.000 1.00 18.77  ? 23  GLY D O   1 
ATOM   6554 N  N   . GLY D  1 24  ? 17.935  14.289  -28.448 1.00 15.50  ? 24  GLY D N   1 
ATOM   6555 C  CA  . GLY D  1 24  ? 17.570  14.280  -27.043 1.00 17.84  ? 24  GLY D CA  1 
ATOM   6556 C  C   . GLY D  1 24  ? 17.392  12.883  -26.532 1.00 18.12  ? 24  GLY D C   1 
ATOM   6557 O  O   . GLY D  1 24  ? 17.884  11.872  -27.067 1.00 21.26  ? 24  GLY D O   1 
ATOM   6558 N  N   A LEU D  1 25  ? 16.512  12.866  -25.486 0.50 21.96  ? 25  LEU D N   1 
ATOM   6559 N  N   B LEU D  1 25  ? 16.739  12.737  -25.389 0.50 20.90  ? 25  LEU D N   1 
ATOM   6560 C  CA  A LEU D  1 25  ? 16.059  11.740  -24.671 0.50 24.10  ? 25  LEU D CA  1 
ATOM   6561 C  CA  B LEU D  1 25  ? 16.633  11.412  -24.860 0.50 20.82  ? 25  LEU D CA  1 
ATOM   6562 C  C   A LEU D  1 25  ? 15.032  10.813  -25.283 0.50 20.46  ? 25  LEU D C   1 
ATOM   6563 C  C   B LEU D  1 25  ? 15.355  10.764  -25.406 0.50 17.65  ? 25  LEU D C   1 
ATOM   6564 O  O   A LEU D  1 25  ? 14.066  11.312  -26.024 0.50 20.94  ? 25  LEU D O   1 
ATOM   6565 O  O   B LEU D  1 25  ? 14.546  11.399  -26.187 0.50 15.17  ? 25  LEU D O   1 
ATOM   6566 C  CB  A LEU D  1 25  ? 15.454  12.241  -23.298 0.50 28.49  ? 25  LEU D CB  1 
ATOM   6567 C  CB  B LEU D  1 25  ? 16.615  11.507  -23.286 0.50 24.86  ? 25  LEU D CB  1 
ATOM   6568 C  CG  A LEU D  1 25  ? 16.202  12.988  -22.202 0.50 27.94  ? 25  LEU D CG  1 
ATOM   6569 C  CG  B LEU D  1 25  ? 17.821  12.145  -22.541 0.50 21.02  ? 25  LEU D CG  1 
ATOM   6570 C  CD1 A LEU D  1 25  ? 15.321  13.954  -21.394 0.50 33.10  ? 25  LEU D CD1 1 
ATOM   6571 C  CD1 B LEU D  1 25  ? 17.595  12.400  -21.027 0.50 31.34  ? 25  LEU D CD1 1 
ATOM   6572 C  CD2 A LEU D  1 25  ? 16.760  12.066  -21.118 0.50 35.25  ? 25  LEU D CD2 1 
ATOM   6573 C  CD2 B LEU D  1 25  ? 18.971  11.237  -22.790 0.50 25.41  ? 25  LEU D CD2 1 
ATOM   6574 N  N   . LEU D  1 26  ? 15.154  9.486   -25.032 1.00 19.46  ? 26  LEU D N   1 
ATOM   6575 C  CA  . LEU D  1 26  ? 13.945  8.719   -25.286 1.00 17.26  ? 26  LEU D CA  1 
ATOM   6576 C  C   . LEU D  1 26  ? 13.638  8.530   -26.750 1.00 13.71  ? 26  LEU D C   1 
ATOM   6577 O  O   . LEU D  1 26  ? 12.437  8.543   -27.134 1.00 15.37  ? 26  LEU D O   1 
ATOM   6578 C  CB  . LEU D  1 26  ? 12.690  9.227   -24.534 1.00 22.07  ? 26  LEU D CB  1 
ATOM   6579 C  CG  . LEU D  1 26  ? 12.762  9.425   -22.995 1.00 34.79  ? 26  LEU D CG  1 
ATOM   6580 C  CD1 . LEU D  1 26  ? 11.415  9.988   -22.480 1.00 38.36  ? 26  LEU D CD1 1 
ATOM   6581 C  CD2 . LEU D  1 26  ? 13.029  8.166   -22.237 1.00 39.17  ? 26  LEU D CD2 1 
ATOM   6582 N  N   . GLN D  1 27  ? 14.627  8.301   -27.550 1.00 13.59  ? 27  GLN D N   1 
ATOM   6583 C  CA  . GLN D  1 27  ? 14.416  8.198   -28.969 1.00 10.92  ? 27  GLN D CA  1 
ATOM   6584 C  C   . GLN D  1 27  ? 14.014  6.799   -29.394 1.00 11.13  ? 27  GLN D C   1 
ATOM   6585 O  O   . GLN D  1 27  ? 14.398  5.762   -28.799 1.00 12.33  ? 27  GLN D O   1 
ATOM   6586 C  CB  . GLN D  1 27  ? 15.657  8.616   -29.713 1.00 12.59  ? 27  GLN D CB  1 
ATOM   6587 C  CG  . GLN D  1 27  ? 15.992  10.129  -29.520 1.00 13.66  ? 27  GLN D CG  1 
ATOM   6588 C  CD  . GLN D  1 27  ? 14.916  10.967  -30.160 1.00 12.00  ? 27  GLN D CD  1 
ATOM   6589 O  OE1 . GLN D  1 27  ? 14.913  11.100  -31.403 1.00 12.41  ? 27  GLN D OE1 1 
ATOM   6590 N  NE2 . GLN D  1 27  ? 13.995  11.529  -29.391 1.00 12.78  ? 27  GLN D NE2 1 
ATOM   6591 N  N   . SER D  1 28  ? 13.259  6.733   -30.474 1.00 10.98  ? 28  SER D N   1 
ATOM   6592 C  CA  . SER D  1 28  ? 12.849  5.472   -31.106 1.00 10.93  ? 28  SER D CA  1 
ATOM   6593 C  C   . SER D  1 28  ? 13.398  5.456   -32.537 1.00 10.83  ? 28  SER D C   1 
ATOM   6594 O  O   . SER D  1 28  ? 13.690  6.505   -33.130 1.00 10.95  ? 28  SER D O   1 
ATOM   6595 C  CB  . SER D  1 28  ? 11.346  5.522   -31.194 1.00 10.31  ? 28  SER D CB  1 
ATOM   6596 O  OG  . SER D  1 28  ? 10.772  5.425   -29.863 1.00 11.22  ? 28  SER D OG  1 
ATOM   6597 N  N   . PRO D  1 29  ? 13.511  4.273   -33.183 1.00 9.83   ? 29  PRO D N   1 
ATOM   6598 C  CA  . PRO D  1 29  ? 13.135  2.953   -32.678 1.00 9.90   ? 29  PRO D CA  1 
ATOM   6599 C  C   . PRO D  1 29  ? 14.268  2.389   -31.852 1.00 9.50   ? 29  PRO D C   1 
ATOM   6600 O  O   . PRO D  1 29  ? 15.321  2.955   -31.678 1.00 10.46  ? 29  PRO D O   1 
ATOM   6601 C  CB  . PRO D  1 29  ? 12.924  2.191   -33.999 1.00 10.65  ? 29  PRO D CB  1 
ATOM   6602 C  CG  . PRO D  1 29  ? 14.062  2.761   -34.865 1.00 10.04  ? 29  PRO D CG  1 
ATOM   6603 C  CD  . PRO D  1 29  ? 14.038  4.165   -34.538 1.00 9.69   ? 29  PRO D CD  1 
ATOM   6604 N  N   . ILE D  1 30  ? 14.009  1.140   -31.365 1.00 10.02  ? 30  ILE D N   1 
ATOM   6605 C  CA  . ILE D  1 30  ? 14.995  0.423   -30.533 1.00 10.60  ? 30  ILE D CA  1 
ATOM   6606 C  C   . ILE D  1 30  ? 15.016  -1.043  -30.924 1.00 10.71  ? 30  ILE D C   1 
ATOM   6607 O  O   . ILE D  1 30  ? 14.086  -1.534  -31.595 1.00 11.00  ? 30  ILE D O   1 
ATOM   6608 C  CB  . ILE D  1 30  ? 14.675  0.606   -29.012 1.00 11.44  ? 30  ILE D CB  1 
ATOM   6609 C  CG1 . ILE D  1 30  ? 13.245  0.060   -28.688 1.00 13.28  ? 30  ILE D CG1 1 
ATOM   6610 C  CG2 . ILE D  1 30  ? 14.931  2.047   -28.605 1.00 14.58  ? 30  ILE D CG2 1 
ATOM   6611 C  CD1 . ILE D  1 30  ? 12.992  -0.046  -27.201 1.00 15.92  ? 30  ILE D CD1 1 
ATOM   6612 N  N   . ASP D  1 31  ? 16.077  -1.717  -30.483 1.00 10.92  ? 31  ASP D N   1 
ATOM   6613 C  CA  . ASP D  1 31  ? 16.169  -3.164  -30.590 1.00 11.16  ? 31  ASP D CA  1 
ATOM   6614 C  C   . ASP D  1 31  ? 15.510  -3.851  -29.426 1.00 11.32  ? 31  ASP D C   1 
ATOM   6615 O  O   . ASP D  1 31  ? 15.893  -3.613  -28.281 1.00 15.88  ? 31  ASP D O   1 
ATOM   6616 C  CB  . ASP D  1 31  ? 17.641  -3.578  -30.724 1.00 12.07  ? 31  ASP D CB  1 
ATOM   6617 C  CG  . ASP D  1 31  ? 17.748  -5.114  -30.855 1.00 13.51  ? 31  ASP D CG  1 
ATOM   6618 O  OD1 . ASP D  1 31  ? 17.177  -5.725  -31.771 1.00 13.78  ? 31  ASP D OD1 1 
ATOM   6619 O  OD2 . ASP D  1 31  ? 18.364  -5.738  -29.936 1.00 18.05  ? 31  ASP D OD2 1 
ATOM   6620 N  N   . LEU D  1 32  ? 14.598  -4.756  -29.658 1.00 11.75  ? 32  LEU D N   1 
ATOM   6621 C  CA  . LEU D  1 32  ? 13.876  -5.428  -28.591 1.00 13.11  ? 32  LEU D CA  1 
ATOM   6622 C  C   . LEU D  1 32  ? 14.634  -6.723  -28.360 1.00 13.48  ? 32  LEU D C   1 
ATOM   6623 O  O   . LEU D  1 32  ? 14.641  -7.641  -29.193 1.00 14.94  ? 32  LEU D O   1 
ATOM   6624 C  CB  . LEU D  1 32  ? 12.470  -5.698  -29.120 1.00 14.98  ? 32  LEU D CB  1 
ATOM   6625 C  CG  . LEU D  1 32  ? 11.728  -4.432  -29.520 1.00 13.97  ? 32  LEU D CG  1 
ATOM   6626 C  CD1 . LEU D  1 32  ? 10.486  -4.746  -30.233 1.00 14.39  ? 32  LEU D CD1 1 
ATOM   6627 C  CD2 . LEU D  1 32  ? 11.451  -3.546  -28.259 1.00 17.77  ? 32  LEU D CD2 1 
ATOM   6628 N  N   . HIS D  1 33  ? 15.330  -6.852  -27.233 1.00 14.09  ? 33  HIS D N   1 
ATOM   6629 C  CA  . HIS D  1 33  ? 16.196  -8.077  -26.973 1.00 13.55  ? 33  HIS D CA  1 
ATOM   6630 C  C   . HIS D  1 33  ? 16.115  -8.329  -25.497 1.00 13.48  ? 33  HIS D C   1 
ATOM   6631 O  O   . HIS D  1 33  ? 15.761  -7.497  -24.668 1.00 14.59  ? 33  HIS D O   1 
ATOM   6632 C  CB  . HIS D  1 33  ? 17.642  -7.831  -27.420 1.00 15.86  ? 33  HIS D CB  1 
ATOM   6633 C  CG  . HIS D  1 33  ? 18.369  -6.749  -26.694 1.00 16.26  ? 33  HIS D CG  1 
ATOM   6634 N  ND1 . HIS D  1 33  ? 18.283  -5.425  -27.008 1.00 20.08  ? 33  HIS D ND1 1 
ATOM   6635 C  CD2 . HIS D  1 33  ? 19.179  -6.778  -25.628 1.00 19.11  ? 33  HIS D CD2 1 
ATOM   6636 C  CE1 . HIS D  1 33  ? 19.037  -4.686  -26.177 1.00 21.58  ? 33  HIS D CE1 1 
ATOM   6637 N  NE2 . HIS D  1 33  ? 19.613  -5.508  -25.374 1.00 19.94  ? 33  HIS D NE2 1 
ATOM   6638 N  N   . SER D  1 34  ? 16.370  -9.599  -25.155 1.00 16.33  ? 34  SER D N   1 
ATOM   6639 C  CA  . SER D  1 34  ? 16.006  -10.177 -23.857 1.00 15.83  ? 34  SER D CA  1 
ATOM   6640 C  C   . SER D  1 34  ? 16.523  -9.356  -22.663 1.00 16.41  ? 34  SER D C   1 
ATOM   6641 O  O   . SER D  1 34  ? 15.761  -9.210  -21.654 1.00 17.19  ? 34  SER D O   1 
ATOM   6642 C  CB  . SER D  1 34  ? 16.563  -11.570 -23.818 1.00 20.96  ? 34  SER D CB  1 
ATOM   6643 O  OG  . SER D  1 34  ? 17.997  -11.550 -23.745 1.00 24.85  ? 34  SER D OG  1 
ATOM   6644 N  N   . ASP D  1 35  ? 17.723  -8.780  -22.720 1.00 15.21  ? 35  ASP D N   1 
ATOM   6645 C  CA  . ASP D  1 35  ? 18.279  -8.177  -21.491 1.00 16.89  ? 35  ASP D CA  1 
ATOM   6646 C  C   . ASP D  1 35  ? 17.490  -6.985  -21.043 1.00 15.82  ? 35  ASP D C   1 
ATOM   6647 O  O   . ASP D  1 35  ? 17.575  -6.571  -19.887 1.00 19.23  ? 35  ASP D O   1 
ATOM   6648 C  CB  . ASP D  1 35  ? 19.732  -7.707  -21.686 1.00 22.21  ? 35  ASP D CB  1 
ATOM   6649 C  CG  . ASP D  1 35  ? 20.613  -8.692  -22.388 1.00 24.30  ? 35  ASP D CG  1 
ATOM   6650 O  OD1 . ASP D  1 35  ? 20.329  -9.086  -23.638 1.00 25.35  ? 35  ASP D OD1 1 
ATOM   6651 O  OD2 . ASP D  1 35  ? 21.628  -9.082  -21.770 1.00 23.68  ? 35  ASP D OD2 1 
ATOM   6652 N  N   . ILE D  1 36  ? 16.720  -6.305  -21.957 1.00 15.94  ? 36  ILE D N   1 
ATOM   6653 C  CA  . ILE D  1 36  ? 15.981  -5.132  -21.573 1.00 15.66  ? 36  ILE D CA  1 
ATOM   6654 C  C   . ILE D  1 36  ? 14.505  -5.377  -21.551 1.00 14.35  ? 36  ILE D C   1 
ATOM   6655 O  O   . ILE D  1 36  ? 13.741  -4.423  -21.374 1.00 17.79  ? 36  ILE D O   1 
ATOM   6656 C  CB  . ILE D  1 36  ? 16.398  -3.892  -22.487 1.00 18.60  ? 36  ILE D CB  1 
ATOM   6657 C  CG1 . ILE D  1 36  ? 16.275  -4.159  -23.904 1.00 21.19  ? 36  ILE D CG1 1 
ATOM   6658 C  CG2 . ILE D  1 36  ? 17.877  -3.582  -22.229 1.00 24.61  ? 36  ILE D CG2 1 
ATOM   6659 C  CD1 . ILE D  1 36  ? 14.927  -4.294  -24.465 1.00 19.89  ? 36  ILE D CD1 1 
ATOM   6660 N  N   . LEU D  1 37  ? 14.014  -6.637  -21.616 1.00 14.66  ? 37  LEU D N   1 
ATOM   6661 C  CA  . LEU D  1 37  ? 12.618  -6.906  -21.562 1.00 14.48  ? 37  LEU D CA  1 
ATOM   6662 C  C   . LEU D  1 37  ? 12.176  -7.277  -20.139 1.00 16.74  ? 37  LEU D C   1 
ATOM   6663 O  O   . LEU D  1 37  ? 12.930  -7.978  -19.432 1.00 19.13  ? 37  LEU D O   1 
ATOM   6664 C  CB  . LEU D  1 37  ? 12.198  -8.110  -22.438 1.00 15.29  ? 37  LEU D CB  1 
ATOM   6665 C  CG  . LEU D  1 37  ? 12.525  -7.895  -23.907 1.00 16.59  ? 37  LEU D CG  1 
ATOM   6666 C  CD1 . LEU D  1 37  ? 12.138  -9.161  -24.677 1.00 22.42  ? 37  LEU D CD1 1 
ATOM   6667 C  CD2 . LEU D  1 37  ? 11.834  -6.690  -24.506 1.00 16.80  ? 37  LEU D CD2 1 
ATOM   6668 N  N   . GLN D  1 38  ? 11.022  -6.860  -19.742 1.00 14.96  ? 38  GLN D N   1 
ATOM   6669 C  CA  . GLN D  1 38  ? 10.506  -7.248  -18.425 1.00 16.03  ? 38  GLN D CA  1 
ATOM   6670 C  C   . GLN D  1 38  ? 9.039   -7.416  -18.475 1.00 14.23  ? 38  GLN D C   1 
ATOM   6671 O  O   . GLN D  1 38  ? 8.300   -6.504  -18.911 1.00 15.03  ? 38  GLN D O   1 
ATOM   6672 C  CB  . GLN D  1 38  ? 10.875  -6.222  -17.384 1.00 19.97  ? 38  GLN D CB  1 
ATOM   6673 C  CG  . GLN D  1 38  ? 10.434  -6.650  -16.004 1.00 25.05  ? 38  GLN D CG  1 
ATOM   6674 C  CD  . GLN D  1 38  ? 11.106  -5.853  -15.019 1.00 34.38  ? 38  GLN D CD  1 
ATOM   6675 O  OE1 . GLN D  1 38  ? 12.309  -6.051  -14.758 1.00 40.58  ? 38  GLN D OE1 1 
ATOM   6676 N  NE2 . GLN D  1 38  ? 10.372  -4.798  -14.580 1.00 32.08  ? 38  GLN D NE2 1 
ATOM   6677 N  N   . TYR D  1 39  ? 8.481   -8.567  -18.034 1.00 15.31  ? 39  TYR D N   1 
ATOM   6678 C  CA  . TYR D  1 39  ? 7.112   -8.764  -18.036 1.00 13.08  ? 39  TYR D CA  1 
ATOM   6679 C  C   . TYR D  1 39  ? 6.441   -7.763  -17.035 1.00 13.78  ? 39  TYR D C   1 
ATOM   6680 O  O   . TYR D  1 39  ? 6.956   -7.523  -15.932 1.00 16.14  ? 39  TYR D O   1 
ATOM   6681 C  CB  . TYR D  1 39  ? 6.837   -10.216 -17.568 1.00 16.76  ? 39  TYR D CB  1 
ATOM   6682 C  CG  . TYR D  1 39  ? 5.377   -10.495 -17.299 1.00 15.54  ? 39  TYR D CG  1 
ATOM   6683 C  CD1 . TYR D  1 39  ? 4.456   -10.495 -18.332 1.00 16.96  ? 39  TYR D CD1 1 
ATOM   6684 C  CD2 . TYR D  1 39  ? 4.917   -10.730 -16.011 1.00 16.95  ? 39  TYR D CD2 1 
ATOM   6685 C  CE1 . TYR D  1 39  ? 3.116   -10.731 -18.096 1.00 17.27  ? 39  TYR D CE1 1 
ATOM   6686 C  CE2 . TYR D  1 39  ? 3.577   -10.950 -15.767 1.00 18.11  ? 39  TYR D CE2 1 
ATOM   6687 C  CZ  . TYR D  1 39  ? 2.685   -10.957 -16.817 1.00 18.44  ? 39  TYR D CZ  1 
ATOM   6688 O  OH  . TYR D  1 39  ? 1.352   -11.179 -16.574 1.00 21.78  ? 39  TYR D OH  1 
ATOM   6689 N  N   . ASP D  1 40  ? 5.254   -7.271  -17.444 1.00 13.71  ? 40  ASP D N   1 
ATOM   6690 C  CA  . ASP D  1 40  ? 4.527   -6.362  -16.573 1.00 14.20  ? 40  ASP D CA  1 
ATOM   6691 C  C   . ASP D  1 40  ? 3.109   -6.731  -16.639 1.00 14.55  ? 40  ASP D C   1 
ATOM   6692 O  O   . ASP D  1 40  ? 2.402   -6.648  -17.674 1.00 15.56  ? 40  ASP D O   1 
ATOM   6693 C  CB  . ASP D  1 40  ? 4.740   -4.956  -17.068 1.00 15.47  ? 40  ASP D CB  1 
ATOM   6694 C  CG  . ASP D  1 40  ? 4.001   -3.874  -16.222 1.00 18.72  ? 40  ASP D CG  1 
ATOM   6695 O  OD1 . ASP D  1 40  ? 3.301   -4.209  -15.329 1.00 18.02  ? 40  ASP D OD1 1 
ATOM   6696 O  OD2 . ASP D  1 40  ? 4.074   -2.700  -16.623 1.00 24.54  ? 40  ASP D OD2 1 
ATOM   6697 N  N   . ALA D  1 41  ? 2.536   -7.251  -15.497 1.00 13.92  ? 41  ALA D N   1 
ATOM   6698 C  CA  . ALA D  1 41  ? 1.133   -7.702  -15.512 1.00 15.22  ? 41  ALA D CA  1 
ATOM   6699 C  C   . ALA D  1 41  ? 0.157   -6.555  -15.628 1.00 15.16  ? 41  ALA D C   1 
ATOM   6700 O  O   . ALA D  1 41  ? -1.013  -6.785  -15.877 1.00 16.43  ? 41  ALA D O   1 
ATOM   6701 C  CB  . ALA D  1 41  ? 0.846   -8.439  -14.184 1.00 17.35  ? 41  ALA D CB  1 
ATOM   6702 N  N   . SER D  1 42  ? 0.594   -5.301  -15.549 1.00 14.94  ? 42  SER D N   1 
ATOM   6703 C  CA  . SER D  1 42  ? -0.312  -4.172  -15.752 1.00 16.91  ? 42  SER D CA  1 
ATOM   6704 C  C   . SER D  1 42  ? -0.677  -4.023  -17.231 1.00 17.04  ? 42  SER D C   1 
ATOM   6705 O  O   . SER D  1 42  ? -1.582  -3.222  -17.528 1.00 20.54  ? 42  SER D O   1 
ATOM   6706 C  CB  . SER D  1 42  ? 0.263   -2.860  -15.141 1.00 21.55  ? 42  SER D CB  1 
ATOM   6707 O  OG  . SER D  1 42  ? 1.172   -2.331  -16.066 1.00 23.28  ? 42  SER D OG  1 
ATOM   6708 N  N   . LEU D  1 43  ? 0.075   -4.685  -18.136 1.00 16.28  ? 43  LEU D N   1 
ATOM   6709 C  CA  . LEU D  1 43  ? -0.171  -4.485  -19.607 1.00 17.58  ? 43  LEU D CA  1 
ATOM   6710 C  C   . LEU D  1 43  ? -1.259  -5.325  -20.082 1.00 17.82  ? 43  LEU D C   1 
ATOM   6711 O  O   . LEU D  1 43  ? -1.146  -6.455  -20.601 1.00 18.85  ? 43  LEU D O   1 
ATOM   6712 C  CB  . LEU D  1 43  ? 1.170   -4.712  -20.314 1.00 15.06  ? 43  LEU D CB  1 
ATOM   6713 C  CG  . LEU D  1 43  ? 2.241   -3.752  -19.985 1.00 18.25  ? 43  LEU D CG  1 
ATOM   6714 C  CD1 . LEU D  1 43  ? 3.452   -4.206  -20.816 1.00 17.81  ? 43  LEU D CD1 1 
ATOM   6715 C  CD2 . LEU D  1 43  ? 1.862   -2.320  -20.297 1.00 19.02  ? 43  LEU D CD2 1 
ATOM   6716 N  N   . THR D  1 44  ? -2.503  -4.815  -19.982 1.00 18.14  ? 44  THR D N   1 
ATOM   6717 C  CA  . THR D  1 44  ? -3.684  -5.554  -20.271 1.00 17.53  ? 44  THR D CA  1 
ATOM   6718 C  C   . THR D  1 44  ? -4.094  -5.316  -21.719 1.00 18.03  ? 44  THR D C   1 
ATOM   6719 O  O   . THR D  1 44  ? -3.474  -4.512  -22.437 1.00 17.01  ? 44  THR D O   1 
ATOM   6720 C  CB  . THR D  1 44  ? -4.897  -5.045  -19.331 1.00 20.29  ? 44  THR D CB  1 
ATOM   6721 O  OG1 . THR D  1 44  ? -4.926  -3.683  -19.429 1.00 25.41  ? 44  THR D OG1 1 
ATOM   6722 C  CG2 . THR D  1 44  ? -4.564  -5.380  -17.867 1.00 25.62  ? 44  THR D CG2 1 
ATOM   6723 N  N   . PRO D  1 45  ? -5.027  -6.106  -22.310 1.00 16.86  ? 45  PRO D N   1 
ATOM   6724 C  CA  . PRO D  1 45  ? -5.263  -6.052  -23.735 1.00 20.05  ? 45  PRO D CA  1 
ATOM   6725 C  C   . PRO D  1 45  ? -5.834  -4.735  -24.208 1.00 18.36  ? 45  PRO D C   1 
ATOM   6726 O  O   . PRO D  1 45  ? -6.764  -4.194  -23.580 1.00 22.27  ? 45  PRO D O   1 
ATOM   6727 C  CB  . PRO D  1 45  ? -6.209  -7.226  -24.052 1.00 23.82  ? 45  PRO D CB  1 
ATOM   6728 C  CG  . PRO D  1 45  ? -6.018  -8.100  -22.846 1.00 21.94  ? 45  PRO D CG  1 
ATOM   6729 C  CD  . PRO D  1 45  ? -5.748  -7.186  -21.659 1.00 20.83  ? 45  PRO D CD  1 
ATOM   6730 N  N   . LEU D  1 46  ? -5.420  -4.274  -25.342 1.00 19.36  ? 46  LEU D N   1 
ATOM   6731 C  CA  . LEU D  1 46  ? -6.027  -3.095  -25.972 1.00 18.10  ? 46  LEU D CA  1 
ATOM   6732 C  C   . LEU D  1 46  ? -7.252  -3.538  -26.721 1.00 20.04  ? 46  LEU D C   1 
ATOM   6733 O  O   . LEU D  1 46  ? -7.402  -4.672  -27.307 1.00 19.74  ? 46  LEU D O   1 
ATOM   6734 C  CB  . LEU D  1 46  ? -5.101  -2.479  -27.016 1.00 19.80  ? 46  LEU D CB  1 
ATOM   6735 C  CG  . LEU D  1 46  ? -3.859  -1.907  -26.307 1.00 20.47  ? 46  LEU D CG  1 
ATOM   6736 C  CD1 . LEU D  1 46  ? -2.922  -1.338  -27.386 1.00 24.00  ? 46  LEU D CD1 1 
ATOM   6737 C  CD2 . LEU D  1 46  ? -4.175  -0.884  -25.207 1.00 29.24  ? 46  LEU D CD2 1 
ATOM   6738 N  N   . GLU D  1 47  ? -8.205  -2.585  -26.900 1.00 23.41  ? 47  GLU D N   1 
ATOM   6739 C  CA  . GLU D  1 47  ? -9.339  -2.819  -27.753 1.00 24.69  ? 47  GLU D CA  1 
ATOM   6740 C  C   . GLU D  1 47  ? -9.429  -1.721  -28.877 1.00 21.89  ? 47  GLU D C   1 
ATOM   6741 O  O   . GLU D  1 47  ? -9.018  -0.522  -28.634 1.00 23.34  ? 47  GLU D O   1 
ATOM   6742 C  CB  . GLU D  1 47  ? -10.734 -2.832  -27.035 1.00 26.36  ? 47  GLU D CB  1 
ATOM   6743 C  CG  . GLU D  1 47  ? -10.840 -4.031  -26.111 1.00 31.85  ? 47  GLU D CG  1 
ATOM   6744 C  CD  . GLU D  1 47  ? -11.913 -3.899  -24.999 1.00 44.16  ? 47  GLU D CD  1 
ATOM   6745 O  OE1 . GLU D  1 47  ? -12.962 -3.290  -25.222 1.00 51.71  ? 47  GLU D OE1 1 
ATOM   6746 O  OE2 . GLU D  1 47  ? -11.735 -4.421  -23.883 1.00 61.36  ? 47  GLU D OE2 1 
ATOM   6747 N  N   . PHE D  1 48  ? -9.692  -2.210  -30.068 1.00 20.73  ? 48  PHE D N   1 
ATOM   6748 C  CA  . PHE D  1 48  ? -9.603  -1.381  -31.264 1.00 18.10  ? 48  PHE D CA  1 
ATOM   6749 C  C   . PHE D  1 48  ? -11.020 -1.041  -31.709 1.00 24.46  ? 48  PHE D C   1 
ATOM   6750 O  O   . PHE D  1 48  ? -11.724 -1.938  -32.256 1.00 27.51  ? 48  PHE D O   1 
ATOM   6751 C  CB  . PHE D  1 48  ? -8.852  -2.127  -32.365 1.00 19.32  ? 48  PHE D CB  1 
ATOM   6752 C  CG  . PHE D  1 48  ? -7.532  -2.695  -31.879 1.00 17.67  ? 48  PHE D CG  1 
ATOM   6753 C  CD1 . PHE D  1 48  ? -6.509  -1.839  -31.498 1.00 17.54  ? 48  PHE D CD1 1 
ATOM   6754 C  CD2 . PHE D  1 48  ? -7.442  -4.076  -31.569 1.00 19.63  ? 48  PHE D CD2 1 
ATOM   6755 C  CE1 . PHE D  1 48  ? -5.316  -2.350  -30.942 1.00 18.81  ? 48  PHE D CE1 1 
ATOM   6756 C  CE2 . PHE D  1 48  ? -6.221  -4.576  -31.017 1.00 21.08  ? 48  PHE D CE2 1 
ATOM   6757 C  CZ  . PHE D  1 48  ? -5.184  -3.687  -30.682 1.00 19.83  ? 48  PHE D CZ  1 
ATOM   6758 N  N   . GLN D  1 49  ? -11.383 0.225   -31.523 1.00 18.99  ? 49  GLN D N   1 
ATOM   6759 C  CA  . GLN D  1 49  ? -12.769 0.676   -31.725 1.00 21.88  ? 49  GLN D CA  1 
ATOM   6760 C  C   . GLN D  1 49  ? -12.896 1.505   -32.976 1.00 18.44  ? 49  GLN D C   1 
ATOM   6761 O  O   . GLN D  1 49  ? -12.089 2.456   -33.197 1.00 18.37  ? 49  GLN D O   1 
ATOM   6762 C  CB  . GLN D  1 49  ? -13.206 1.412   -30.525 1.00 23.53  ? 49  GLN D CB  1 
ATOM   6763 C  CG  . GLN D  1 49  ? -13.276 0.674   -29.251 1.00 22.90  ? 49  GLN D CG  1 
ATOM   6764 C  CD  . GLN D  1 49  ? -14.131 -0.644  -29.290 1.00 25.75  ? 49  GLN D CD  1 
ATOM   6765 O  OE1 . GLN D  1 49  ? -15.382 -0.665  -29.435 1.00 42.33  ? 49  GLN D OE1 1 
ATOM   6766 N  NE2 . GLN D  1 49  ? -13.438 -1.767  -29.167 1.00 32.37  ? 49  GLN D NE2 1 
ATOM   6767 N  N   . GLY D  1 50  ? -13.968 1.265   -33.783 1.00 18.85  ? 50  GLY D N   1 
ATOM   6768 C  CA  . GLY D  1 50  ? -14.152 2.092   -34.995 1.00 21.08  ? 50  GLY D CA  1 
ATOM   6769 C  C   . GLY D  1 50  ? -13.039 1.824   -36.062 1.00 17.47  ? 50  GLY D C   1 
ATOM   6770 O  O   . GLY D  1 50  ? -12.884 2.643   -36.907 1.00 18.12  ? 50  GLY D O   1 
ATOM   6771 N  N   . TYR D  1 51  ? -12.388 0.670   -35.991 1.00 17.85  ? 51  TYR D N   1 
ATOM   6772 C  CA  . TYR D  1 51  ? -11.356 0.383   -36.992 1.00 15.33  ? 51  TYR D CA  1 
ATOM   6773 C  C   . TYR D  1 51  ? -11.984 -0.218  -38.229 1.00 16.17  ? 51  TYR D C   1 
ATOM   6774 O  O   . TYR D  1 51  ? -11.325 -0.271  -39.304 1.00 15.98  ? 51  TYR D O   1 
ATOM   6775 C  CB  . TYR D  1 51  ? -10.379 -0.730  -36.468 1.00 16.34  ? 51  TYR D CB  1 
ATOM   6776 C  CG  . TYR D  1 51  ? -9.220  -0.172  -35.674 1.00 14.29  ? 51  TYR D CG  1 
ATOM   6777 C  CD1 . TYR D  1 51  ? -9.359  0.803   -34.699 1.00 15.98  ? 51  TYR D CD1 1 
ATOM   6778 C  CD2 . TYR D  1 51  ? -7.921  -0.657  -35.934 1.00 13.69  ? 51  TYR D CD2 1 
ATOM   6779 C  CE1 . TYR D  1 51  ? -8.302  1.322   -33.980 1.00 15.00  ? 51  TYR D CE1 1 
ATOM   6780 C  CE2 . TYR D  1 51  ? -6.827  -0.140  -35.227 1.00 13.47  ? 51  TYR D CE2 1 
ATOM   6781 C  CZ  . TYR D  1 51  ? -6.977  0.845   -34.291 1.00 14.62  ? 51  TYR D CZ  1 
ATOM   6782 O  OH  . TYR D  1 51  ? -5.859  1.328   -33.669 1.00 16.90  ? 51  TYR D OH  1 
ATOM   6783 N  N   . ASN D  1 52  ? -13.300 -0.590  -38.188 1.00 18.11  ? 52  ASN D N   1 
ATOM   6784 C  CA  . ASN D  1 52  ? -13.868 -1.147  -39.327 1.00 18.48  ? 52  ASN D CA  1 
ATOM   6785 C  C   . ASN D  1 52  ? -14.459 -0.022  -40.201 1.00 18.64  ? 52  ASN D C   1 
ATOM   6786 O  O   . ASN D  1 52  ? -15.643 0.318   -40.031 1.00 21.66  ? 52  ASN D O   1 
ATOM   6787 C  CB  . ASN D  1 52  ? -14.917 -2.198  -38.933 1.00 20.19  ? 52  ASN D CB  1 
ATOM   6788 C  CG  . ASN D  1 52  ? -15.469 -2.962  -40.108 1.00 21.51  ? 52  ASN D CG  1 
ATOM   6789 O  OD1 . ASN D  1 52  ? -15.318 -2.593  -41.233 1.00 31.89  ? 52  ASN D OD1 1 
ATOM   6790 N  ND2 . ASN D  1 52  ? -16.279 -3.917  -39.835 1.00 33.51  ? 52  ASN D ND2 1 
ATOM   6791 N  N   . LEU D  1 53  ? -13.703 0.520   -41.146 1.00 17.88  ? 53  LEU D N   1 
ATOM   6792 C  CA  . LEU D  1 53  ? -14.126 1.697   -41.882 1.00 16.11  ? 53  LEU D CA  1 
ATOM   6793 C  C   . LEU D  1 53  ? -15.065 1.272   -43.036 1.00 16.20  ? 53  LEU D C   1 
ATOM   6794 O  O   . LEU D  1 53  ? -14.840 0.243   -43.659 1.00 19.84  ? 53  LEU D O   1 
ATOM   6795 C  CB  . LEU D  1 53  ? -12.896 2.403   -42.393 1.00 16.25  ? 53  LEU D CB  1 
ATOM   6796 C  CG  . LEU D  1 53  ? -11.835 2.813   -41.380 1.00 16.96  ? 53  LEU D CG  1 
ATOM   6797 C  CD1 . LEU D  1 53  ? -10.707 3.577   -42.073 1.00 19.58  ? 53  LEU D CD1 1 
ATOM   6798 C  CD2 . LEU D  1 53  ? -12.418 3.599   -40.227 1.00 20.80  ? 53  LEU D CD2 1 
ATOM   6799 N  N   . SER D  1 54  ? -16.098 2.044   -43.221 1.00 18.04  ? 54  SER D N   1 
ATOM   6800 C  CA  . SER D  1 54  ? -17.070 1.728   -44.274 1.00 19.10  ? 54  SER D CA  1 
ATOM   6801 C  C   . SER D  1 54  ? -16.470 1.772   -45.663 1.00 17.95  ? 54  SER D C   1 
ATOM   6802 O  O   . SER D  1 54  ? -15.826 2.718   -46.037 1.00 18.08  ? 54  SER D O   1 
ATOM   6803 C  CB  . SER D  1 54  ? -18.178 2.773   -44.153 1.00 19.53  ? 54  SER D CB  1 
ATOM   6804 O  OG  . SER D  1 54  ? -19.094 2.407   -45.213 1.00 22.48  ? 54  SER D OG  1 
ATOM   6805 N  N   . ALA D  1 55  ? -16.865 0.785   -46.484 1.00 21.71  ? 55  ALA D N   1 
ATOM   6806 C  CA  . ALA D  1 55  ? -16.478 0.751   -47.910 1.00 20.77  ? 55  ALA D CA  1 
ATOM   6807 C  C   . ALA D  1 55  ? -17.112 1.901   -48.698 1.00 21.19  ? 55  ALA D C   1 
ATOM   6808 O  O   . ALA D  1 55  ? -16.623 2.225   -49.804 1.00 21.71  ? 55  ALA D O   1 
ATOM   6809 C  CB  . ALA D  1 55  ? -16.930 -0.590  -48.465 1.00 29.41  ? 55  ALA D CB  1 
ATOM   6810 N  N   . ASN D  1 56  ? -18.166 2.536   -48.196 1.00 22.71  ? 56  ASN D N   1 
ATOM   6811 C  CA  . ASN D  1 56  ? -18.825 3.675   -48.837 1.00 23.55  ? 56  ASN D CA  1 
ATOM   6812 C  C   . ASN D  1 56  ? -18.166 4.996   -48.534 1.00 22.65  ? 56  ASN D C   1 
ATOM   6813 O  O   . ASN D  1 56  ? -18.643 6.043   -49.011 1.00 30.09  ? 56  ASN D O   1 
ATOM   6814 C  CB  . ASN D  1 56  ? -20.262 3.774   -48.648 1.00 23.58  ? 56  ASN D CB  1 
ATOM   6815 C  CG  . ASN D  1 56  ? -21.098 2.635   -49.276 1.00 42.01  ? 56  ASN D CG  1 
ATOM   6816 O  OD1 . ASN D  1 56  ? -20.625 1.894   -50.129 1.00 43.05  ? 56  ASN D OD1 1 
ATOM   6817 N  ND2 . ASN D  1 56  ? -22.395 2.545   -48.852 1.00 56.14  ? 56  ASN D ND2 1 
ATOM   6818 N  N   A LYS D  1 57  ? -17.164 4.959   -47.681 0.50 20.97  ? 57  LYS D N   1 
ATOM   6819 N  N   B LYS D  1 57  ? -17.232 4.973   -47.578 0.50 18.76  ? 57  LYS D N   1 
ATOM   6820 C  CA  A LYS D  1 57  ? -16.457 6.129   -47.236 0.50 20.74  ? 57  LYS D CA  1 
ATOM   6821 C  CA  B LYS D  1 57  ? -16.446 6.147   -47.220 0.50 18.89  ? 57  LYS D CA  1 
ATOM   6822 C  C   A LYS D  1 57  ? -15.051 6.075   -47.820 0.50 19.26  ? 57  LYS D C   1 
ATOM   6823 C  C   B LYS D  1 57  ? -15.108 6.064   -47.957 0.50 17.29  ? 57  LYS D C   1 
ATOM   6824 O  O   A LYS D  1 57  ? -14.564 4.997   -48.051 0.50 19.12  ? 57  LYS D O   1 
ATOM   6825 O  O   B LYS D  1 57  ? -14.750 4.934   -48.448 0.50 16.45  ? 57  LYS D O   1 
ATOM   6826 C  CB  A LYS D  1 57  ? -16.454 6.187   -45.708 0.50 20.81  ? 57  LYS D CB  1 
ATOM   6827 C  CB  B LYS D  1 57  ? -16.339 6.347   -45.686 0.50 18.10  ? 57  LYS D CB  1 
ATOM   6828 C  CG  A LYS D  1 57  ? -17.859 6.366   -45.108 0.50 23.17  ? 57  LYS D CG  1 
ATOM   6829 C  CG  B LYS D  1 57  ? -17.628 6.860   -45.064 0.50 21.29  ? 57  LYS D CG  1 
ATOM   6830 C  CD  A LYS D  1 57  ? -17.713 6.861   -43.673 0.50 27.38  ? 57  LYS D CD  1 
ATOM   6831 C  CD  B LYS D  1 57  ? -17.404 7.516   -43.697 0.50 24.55  ? 57  LYS D CD  1 
ATOM   6832 C  CE  A LYS D  1 57  ? -18.925 7.609   -43.155 0.50 37.18  ? 57  LYS D CE  1 
ATOM   6833 C  CE  B LYS D  1 57  ? -18.693 7.435   -42.907 0.50 24.84  ? 57  LYS D CE  1 
ATOM   6834 N  NZ  A LYS D  1 57  ? -19.227 8.858   -43.923 0.50 26.88  ? 57  LYS D NZ  1 
ATOM   6835 N  NZ  B LYS D  1 57  ? -18.630 7.750   -41.474 0.50 32.61  ? 57  LYS D NZ  1 
ATOM   6836 N  N   . GLN D  1 58  ? -14.422 7.210   -48.029 1.00 18.97  ? 58  GLN D N   1 
ATOM   6837 C  CA  . GLN D  1 58  ? -13.078 7.230   -48.658 1.00 18.78  ? 58  GLN D CA  1 
ATOM   6838 C  C   . GLN D  1 58  ? -12.172 8.013   -47.769 1.00 17.04  ? 58  GLN D C   1 
ATOM   6839 O  O   . GLN D  1 58  ? -12.555 8.881   -47.061 1.00 17.90  ? 58  GLN D O   1 
ATOM   6840 C  CB  . GLN D  1 58  ? -13.093 7.893   -50.000 1.00 27.36  ? 58  GLN D CB  1 
ATOM   6841 C  CG  . GLN D  1 58  ? -14.259 8.276   -50.668 1.00 35.27  ? 58  GLN D CG  1 
ATOM   6842 C  CD  . GLN D  1 58  ? -13.793 8.857   -52.010 1.00 32.67  ? 58  GLN D CD  1 
ATOM   6843 O  OE1 . GLN D  1 58  ? -13.341 8.065   -52.828 1.00 29.61  ? 58  GLN D OE1 1 
ATOM   6844 N  NE2 . GLN D  1 58  ? -13.875 10.206  -52.256 1.00 39.56  ? 58  GLN D NE2 1 
ATOM   6845 N  N   . PHE D  1 59  ? -10.905 7.585   -47.812 1.00 15.43  ? 59  PHE D N   1 
ATOM   6846 C  CA  . PHE D  1 59  ? -9.852  8.106   -46.896 1.00 14.82  ? 59  PHE D CA  1 
ATOM   6847 C  C   . PHE D  1 59  ? -8.677  8.496   -47.737 1.00 13.76  ? 59  PHE D C   1 
ATOM   6848 O  O   . PHE D  1 59  ? -8.325  7.834   -48.716 1.00 14.92  ? 59  PHE D O   1 
ATOM   6849 C  CB  . PHE D  1 59  ? -9.515  7.015   -45.888 1.00 14.78  ? 59  PHE D CB  1 
ATOM   6850 C  CG  . PHE D  1 59  ? -10.721 6.641   -45.050 1.00 14.14  ? 59  PHE D CG  1 
ATOM   6851 C  CD1 . PHE D  1 59  ? -11.665 5.697   -45.539 1.00 14.99  ? 59  PHE D CD1 1 
ATOM   6852 C  CD2 . PHE D  1 59  ? -11.023 7.404   -43.946 1.00 16.00  ? 59  PHE D CD2 1 
ATOM   6853 C  CE1 . PHE D  1 59  ? -12.869 5.495   -44.784 1.00 15.11  ? 59  PHE D CE1 1 
ATOM   6854 C  CE2 . PHE D  1 59  ? -12.183 7.208   -43.203 1.00 16.64  ? 59  PHE D CE2 1 
ATOM   6855 C  CZ  . PHE D  1 59  ? -13.119 6.280   -43.657 1.00 16.95  ? 59  PHE D CZ  1 
ATOM   6856 N  N   . LEU D  1 60  ? -8.070  9.607   -47.394 1.00 14.02  ? 60  LEU D N   1 
ATOM   6857 C  CA  . LEU D  1 60  ? -7.028  10.183  -48.292 1.00 14.89  ? 60  LEU D CA  1 
ATOM   6858 C  C   . LEU D  1 60  ? -5.676  9.530   -48.075 1.00 13.46  ? 60  LEU D C   1 
ATOM   6859 O  O   . LEU D  1 60  ? -5.168  9.528   -46.941 1.00 14.34  ? 60  LEU D O   1 
ATOM   6860 C  CB  . LEU D  1 60  ? -6.952  11.670  -47.885 1.00 17.48  ? 60  LEU D CB  1 
ATOM   6861 C  CG  . LEU D  1 60  ? -6.203  12.478  -48.948 1.00 22.61  ? 60  LEU D CG  1 
ATOM   6862 C  CD1 . LEU D  1 60  ? -6.867  12.475  -50.316 1.00 23.95  ? 60  LEU D CD1 1 
ATOM   6863 C  CD2 . LEU D  1 60  ? -6.084  13.912  -48.398 1.00 30.11  ? 60  LEU D CD2 1 
ATOM   6864 N  N   . LEU D  1 61  ? -5.105  9.020   -49.136 1.00 13.84  ? 61  LEU D N   1 
ATOM   6865 C  CA  . LEU D  1 61  ? -3.729  8.507   -49.185 1.00 12.83  ? 61  LEU D CA  1 
ATOM   6866 C  C   . LEU D  1 61  ? -2.846  9.603   -49.777 1.00 12.77  ? 61  LEU D C   1 
ATOM   6867 O  O   . LEU D  1 61  ? -3.216  10.209  -50.795 1.00 16.36  ? 61  LEU D O   1 
ATOM   6868 C  CB  . LEU D  1 61  ? -3.727  7.264   -50.058 1.00 14.67  ? 61  LEU D CB  1 
ATOM   6869 C  CG  . LEU D  1 61  ? -2.456  6.444   -50.083 1.00 14.66  ? 61  LEU D CG  1 
ATOM   6870 C  CD1 . LEU D  1 61  ? -2.333  5.656   -48.791 1.00 16.10  ? 61  LEU D CD1 1 
ATOM   6871 C  CD2 . LEU D  1 61  ? -2.478  5.482   -51.248 1.00 18.39  ? 61  LEU D CD2 1 
ATOM   6872 N  N   . THR D  1 62  ? -1.705  9.849   -49.182 1.00 13.51  ? 62  THR D N   1 
ATOM   6873 C  CA  . THR D  1 62  ? -0.833  10.924  -49.645 1.00 14.21  ? 62  THR D CA  1 
ATOM   6874 C  C   . THR D  1 62  ? 0.644   10.430  -49.590 1.00 14.68  ? 62  THR D C   1 
ATOM   6875 O  O   . THR D  1 62  ? 1.069   9.713   -48.670 1.00 15.47  ? 62  THR D O   1 
ATOM   6876 C  CB  . THR D  1 62  ? -0.870  12.101  -48.646 1.00 19.58  ? 62  THR D CB  1 
ATOM   6877 O  OG1 . THR D  1 62  ? -2.199  12.612  -48.475 1.00 23.29  ? 62  THR D OG1 1 
ATOM   6878 C  CG2 . THR D  1 62  ? -0.058  13.335  -49.169 1.00 26.19  ? 62  THR D CG2 1 
ATOM   6879 N  N   . ASN D  1 63  ? 1.402   10.859  -50.575 1.00 14.56  ? 63  ASN D N   1 
ATOM   6880 C  CA  . ASN D  1 63  ? 2.877   10.738  -50.506 1.00 14.51  ? 63  ASN D CA  1 
ATOM   6881 C  C   . ASN D  1 63  ? 3.414   12.017  -49.918 1.00 14.79  ? 63  ASN D C   1 
ATOM   6882 O  O   . ASN D  1 63  ? 3.217   13.137  -50.449 1.00 16.14  ? 63  ASN D O   1 
ATOM   6883 C  CB  . ASN D  1 63  ? 3.362   10.510  -51.942 1.00 15.94  ? 63  ASN D CB  1 
ATOM   6884 C  CG  . ASN D  1 63  ? 4.904   10.554  -52.078 1.00 14.49  ? 63  ASN D CG  1 
ATOM   6885 O  OD1 . ASN D  1 63  ? 5.593   11.127  -51.171 1.00 15.24  ? 63  ASN D OD1 1 
ATOM   6886 N  ND2 . ASN D  1 63  ? 5.415   9.913   -53.088 1.00 16.05  ? 63  ASN D ND2 1 
ATOM   6887 N  N   . ASN D  1 64  ? 3.874   11.964  -48.675 1.00 14.89  ? 64  ASN D N   1 
ATOM   6888 C  CA  . ASN D  1 64  ? 4.320   13.218  -48.014 1.00 17.32  ? 64  ASN D CA  1 
ATOM   6889 C  C   . ASN D  1 64  ? 5.861   13.459  -48.167 1.00 17.00  ? 64  ASN D C   1 
ATOM   6890 O  O   . ASN D  1 64  ? 6.443   14.314  -47.479 1.00 17.81  ? 64  ASN D O   1 
ATOM   6891 C  CB  . ASN D  1 64  ? 3.910   13.177  -46.527 1.00 16.94  ? 64  ASN D CB  1 
ATOM   6892 C  CG  . ASN D  1 64  ? 4.563   12.062  -45.803 1.00 15.15  ? 64  ASN D CG  1 
ATOM   6893 O  OD1 . ASN D  1 64  ? 5.551   11.411  -46.283 1.00 15.96  ? 64  ASN D OD1 1 
ATOM   6894 N  ND2 . ASN D  1 64  ? 4.134   11.816  -44.548 1.00 19.77  ? 64  ASN D ND2 1 
ATOM   6895 N  N   . GLY D  1 65  ? 6.460   12.735  -49.132 1.00 14.89  ? 65  GLY D N   1 
ATOM   6896 C  CA  . GLY D  1 65  ? 7.900   12.958  -49.320 1.00 16.80  ? 65  GLY D CA  1 
ATOM   6897 C  C   . GLY D  1 65  ? 8.755   12.075  -48.386 1.00 16.22  ? 65  GLY D C   1 
ATOM   6898 O  O   . GLY D  1 65  ? 9.985   12.000  -48.583 1.00 20.84  ? 65  GLY D O   1 
ATOM   6899 N  N   . HIS D  1 66  ? 8.128   11.354  -47.453 1.00 13.70  ? 66  HIS D N   1 
ATOM   6900 C  CA  . HIS D  1 66  ? 8.881   10.541  -46.471 1.00 14.25  ? 66  HIS D CA  1 
ATOM   6901 C  C   . HIS D  1 66  ? 8.348   9.149   -46.324 1.00 13.81  ? 66  HIS D C   1 
ATOM   6902 O  O   . HIS D  1 66  ? 9.082   8.237   -45.874 1.00 14.65  ? 66  HIS D O   1 
ATOM   6903 C  CB  . HIS D  1 66  ? 8.922   11.238  -45.091 1.00 18.42  ? 66  HIS D CB  1 
ATOM   6904 C  CG  . HIS D  1 66  ? 9.553   12.649  -45.194 1.00 19.10  ? 66  HIS D CG  1 
ATOM   6905 N  ND1 . HIS D  1 66  ? 10.905  12.929  -45.474 1.00 19.78  ? 66  HIS D ND1 1 
ATOM   6906 C  CD2 . HIS D  1 66  ? 8.958   13.851  -45.079 1.00 20.42  ? 66  HIS D CD2 1 
ATOM   6907 C  CE1 . HIS D  1 66  ? 11.059  14.263  -45.485 1.00 18.46  ? 66  HIS D CE1 1 
ATOM   6908 N  NE2 . HIS D  1 66  ? 9.883   14.824  -45.232 1.00 20.41  ? 66  HIS D NE2 1 
ATOM   6909 N  N   . SER D  1 67  ? 7.071   8.984   -46.590 1.00 13.63  ? 67  SER D N   1 
ATOM   6910 C  CA  . SER D  1 67  ? 6.419   7.673   -46.582 1.00 12.14  ? 67  SER D CA  1 
ATOM   6911 C  C   . SER D  1 67  ? 5.124   7.812   -47.416 1.00 12.10  ? 67  SER D C   1 
ATOM   6912 O  O   . SER D  1 67  ? 4.896   8.865   -48.060 1.00 13.77  ? 67  SER D O   1 
ATOM   6913 C  CB  . SER D  1 67  ? 6.035   7.362   -45.114 1.00 13.58  ? 67  SER D CB  1 
ATOM   6914 O  OG  . SER D  1 67  ? 5.435   6.086   -44.990 1.00 13.96  ? 67  SER D OG  1 
ATOM   6915 N  N   . VAL D  1 68  ? 4.301   6.771   -47.431 1.00 13.03  ? 68  VAL D N   1 
ATOM   6916 C  CA  . VAL D  1 68  ? 2.924   6.858   -47.908 1.00 14.52  ? 68  VAL D CA  1 
ATOM   6917 C  C   . VAL D  1 68  ? 2.055   6.819   -46.634 1.00 12.85  ? 68  VAL D C   1 
ATOM   6918 O  O   . VAL D  1 68  ? 2.236   5.920   -45.828 1.00 13.15  ? 68  VAL D O   1 
ATOM   6919 C  CB  . VAL D  1 68  ? 2.624   5.788   -48.927 1.00 15.61  ? 68  VAL D CB  1 
ATOM   6920 C  CG1 . VAL D  1 68  ? 2.910   4.373   -48.439 1.00 16.07  ? 68  VAL D CG1 1 
ATOM   6921 C  CG2 . VAL D  1 68  ? 1.230   5.963   -49.452 1.00 20.77  ? 68  VAL D CG2 1 
ATOM   6922 N  N   . LYS D  1 69  ? 1.148   7.776   -46.550 1.00 13.33  ? 69  LYS D N   1 
ATOM   6923 C  CA  . LYS D  1 69  ? 0.292   7.874   -45.361 1.00 12.12  ? 69  LYS D CA  1 
ATOM   6924 C  C   . LYS D  1 69  ? -1.191  7.890   -45.734 1.00 11.10  ? 69  LYS D C   1 
ATOM   6925 O  O   . LYS D  1 69  ? -1.611  8.496   -46.709 1.00 14.30  ? 69  LYS D O   1 
ATOM   6926 C  CB  . LYS D  1 69  ? 0.619   9.149   -44.589 1.00 18.50  ? 69  LYS D CB  1 
ATOM   6927 C  CG  . LYS D  1 69  ? -0.091  10.381  -44.744 1.00 27.49  ? 69  LYS D CG  1 
ATOM   6928 C  CD  . LYS D  1 69  ? 0.081   11.431  -43.616 1.00 25.23  ? 69  LYS D CD  1 
ATOM   6929 C  CE  . LYS D  1 69  ? -0.378  12.669  -44.264 1.00 27.77  ? 69  LYS D CE  1 
ATOM   6930 N  NZ  . LYS D  1 69  ? 0.006   13.684  -43.333 1.00 27.11  ? 69  LYS D NZ  1 
ATOM   6931 N  N   . LEU D  1 70  ? -1.962  7.203   -44.927 1.00 10.98  ? 70  LEU D N   1 
ATOM   6932 C  CA  . LEU D  1 70  ? -3.444  7.109   -45.052 1.00 10.97  ? 70  LEU D CA  1 
ATOM   6933 C  C   . LEU D  1 70  ? -4.033  7.879   -43.889 1.00 10.97  ? 70  LEU D C   1 
ATOM   6934 O  O   . LEU D  1 70  ? -3.737  7.563   -42.743 1.00 11.77  ? 70  LEU D O   1 
ATOM   6935 C  CB  . LEU D  1 70  ? -3.893  5.699   -45.031 1.00 11.92  ? 70  LEU D CB  1 
ATOM   6936 C  CG  . LEU D  1 70  ? -5.418  5.485   -45.199 1.00 12.35  ? 70  LEU D CG  1 
ATOM   6937 C  CD1 . LEU D  1 70  ? -5.875  5.975   -46.571 1.00 14.20  ? 70  LEU D CD1 1 
ATOM   6938 C  CD2 . LEU D  1 70  ? -5.767  4.004   -44.963 1.00 14.64  ? 70  LEU D CD2 1 
ATOM   6939 N  N   . ASN D  1 71  ? -4.839  8.886   -44.171 1.00 11.66  ? 71  ASN D N   1 
ATOM   6940 C  CA  . ASN D  1 71  ? -5.579  9.565   -43.078 1.00 12.84  ? 71  ASN D CA  1 
ATOM   6941 C  C   . ASN D  1 71  ? -6.633  8.748   -42.520 1.00 13.47  ? 71  ASN D C   1 
ATOM   6942 O  O   . ASN D  1 71  ? -7.306  7.943   -43.247 1.00 15.82  ? 71  ASN D O   1 
ATOM   6943 C  CB  . ASN D  1 71  ? -6.211  10.857  -43.664 1.00 17.47  ? 71  ASN D CB  1 
ATOM   6944 C  CG  . ASN D  1 71  ? -5.247  11.915  -43.895 1.00 20.02  ? 71  ASN D CG  1 
ATOM   6945 O  OD1 . ASN D  1 71  ? -4.060  11.803  -43.577 1.00 22.77  ? 71  ASN D OD1 1 
ATOM   6946 N  ND2 . ASN D  1 71  ? -5.760  13.063  -44.390 1.00 26.05  ? 71  ASN D ND2 1 
ATOM   6947 N  N   . LEU D  1 72  ? -6.832  8.845   -41.218 1.00 12.78  ? 72  LEU D N   1 
ATOM   6948 C  CA  . LEU D  1 72  ? -7.775  8.022   -40.503 1.00 13.56  ? 72  LEU D CA  1 
ATOM   6949 C  C   . LEU D  1 72  ? -8.749  8.953   -39.701 1.00 13.27  ? 72  LEU D C   1 
ATOM   6950 O  O   . LEU D  1 72  ? -8.348  10.054  -39.278 1.00 15.44  ? 72  LEU D O   1 
ATOM   6951 C  CB  . LEU D  1 72  ? -7.039  7.132   -39.455 1.00 13.15  ? 72  LEU D CB  1 
ATOM   6952 C  CG  . LEU D  1 72  ? -6.142  6.078   -40.163 1.00 13.68  ? 72  LEU D CG  1 
ATOM   6953 C  CD1 . LEU D  1 72  ? -5.309  5.368   -39.171 1.00 12.52  ? 72  LEU D CD1 1 
ATOM   6954 C  CD2 . LEU D  1 72  ? -6.950  5.085   -41.022 1.00 13.91  ? 72  LEU D CD2 1 
ATOM   6955 N  N   . PRO D  1 73  ? -9.970  8.477   -39.465 1.00 14.14  ? 73  PRO D N   1 
ATOM   6956 C  CA  . PRO D  1 73  ? -10.996 9.328   -38.795 1.00 15.34  ? 73  PRO D CA  1 
ATOM   6957 C  C   . PRO D  1 73  ? -10.824 9.287   -37.275 1.00 17.03  ? 73  PRO D C   1 
ATOM   6958 O  O   . PRO D  1 73  ? -10.391 8.249   -36.693 1.00 18.70  ? 73  PRO D O   1 
ATOM   6959 C  CB  . PRO D  1 73  ? -12.289 8.674   -39.291 1.00 18.28  ? 73  PRO D CB  1 
ATOM   6960 C  CG  . PRO D  1 73  ? -11.965 7.156   -39.378 1.00 17.19  ? 73  PRO D CG  1 
ATOM   6961 C  CD  . PRO D  1 73  ? -10.507 7.152   -39.921 1.00 15.47  ? 73  PRO D CD  1 
ATOM   6962 N  N   . SER D  1 74  ? -11.150 10.370  -36.610 1.00 18.99  ? 74  SER D N   1 
ATOM   6963 C  CA  . SER D  1 74  ? -10.926 10.391  -35.163 1.00 19.30  ? 74  SER D CA  1 
ATOM   6964 C  C   . SER D  1 74  ? -11.905 9.544   -34.383 1.00 19.75  ? 74  SER D C   1 
ATOM   6965 O  O   . SER D  1 74  ? -11.660 9.350   -33.185 1.00 21.88  ? 74  SER D O   1 
ATOM   6966 C  CB  . SER D  1 74  ? -10.840 11.823  -34.627 1.00 25.17  ? 74  SER D CB  1 
ATOM   6967 O  OG  . SER D  1 74  ? -12.062 12.514  -34.937 1.00 26.27  ? 74  SER D OG  1 
ATOM   6968 N  N   . ASP D  1 75  ? -12.983 9.052   -34.983 1.00 20.06  ? 75  ASP D N   1 
ATOM   6969 C  CA  . ASP D  1 75  ? -13.906 8.096   -34.322 1.00 19.96  ? 75  ASP D CA  1 
ATOM   6970 C  C   . ASP D  1 75  ? -13.230 6.768   -34.134 1.00 21.22  ? 75  ASP D C   1 
ATOM   6971 O  O   . ASP D  1 75  ? -13.621 6.033   -33.252 1.00 22.43  ? 75  ASP D O   1 
ATOM   6972 C  CB  . ASP D  1 75  ? -15.288 7.991   -34.993 1.00 26.43  ? 75  ASP D CB  1 
ATOM   6973 C  CG  . ASP D  1 75  ? -15.332 7.212   -36.300 1.00 37.94  ? 75  ASP D CG  1 
ATOM   6974 O  OD1 . ASP D  1 75  ? -14.785 7.623   -37.349 1.00 46.36  ? 75  ASP D OD1 1 
ATOM   6975 O  OD2 . ASP D  1 75  ? -16.087 6.213   -36.338 1.00 63.29  ? 75  ASP D OD2 1 
ATOM   6976 N  N   . MET D  1 76  ? -12.162 6.496   -34.859 1.00 19.18  ? 76  MET D N   1 
ATOM   6977 C  CA  . MET D  1 76  ? -11.367 5.276   -34.660 1.00 18.24  ? 76  MET D CA  1 
ATOM   6978 C  C   . MET D  1 76  ? -10.426 5.539   -33.440 1.00 17.48  ? 76  MET D C   1 
ATOM   6979 O  O   . MET D  1 76  ? -9.770  6.613   -33.355 1.00 17.69  ? 76  MET D O   1 
ATOM   6980 C  CB  . MET D  1 76  ? -10.626 5.044   -36.021 1.00 18.24  ? 76  MET D CB  1 
ATOM   6981 C  CG  . MET D  1 76  ? -9.694  3.946   -35.924 1.00 19.97  ? 76  MET D CG  1 
ATOM   6982 S  SD  . MET D  1 76  ? -8.950  3.824   -37.637 1.00 18.32  ? 76  MET D SD  1 
ATOM   6983 C  CE  . MET D  1 76  ? -7.534  2.886   -37.168 1.00 17.38  ? 76  MET D CE  1 
ATOM   6984 N  N   . HIS D  1 77  ? -10.413 4.604   -32.448 1.00 17.92  ? 77  HIS D N   1 
ATOM   6985 C  CA  . HIS D  1 77  ? -9.628  4.903   -31.256 1.00 18.20  ? 77  HIS D CA  1 
ATOM   6986 C  C   . HIS D  1 77  ? -9.233  3.622   -30.609 1.00 17.40  ? 77  HIS D C   1 
ATOM   6987 O  O   . HIS D  1 77  ? -9.792  2.528   -30.903 1.00 18.17  ? 77  HIS D O   1 
ATOM   6988 C  CB  . HIS D  1 77  ? -10.422 5.804   -30.310 1.00 19.09  ? 77  HIS D CB  1 
ATOM   6989 C  CG  . HIS D  1 77  ? -11.724 5.175   -29.829 1.00 20.92  ? 77  HIS D CG  1 
ATOM   6990 N  ND1 . HIS D  1 77  ? -12.932 5.178   -30.563 1.00 24.26  ? 77  HIS D ND1 1 
ATOM   6991 C  CD2 . HIS D  1 77  ? -12.045 4.562   -28.658 1.00 25.52  ? 77  HIS D CD2 1 
ATOM   6992 C  CE1 . HIS D  1 77  ? -13.911 4.620   -29.831 1.00 27.52  ? 77  HIS D CE1 1 
ATOM   6993 N  NE2 . HIS D  1 77  ? -13.416 4.312   -28.647 1.00 27.77  ? 77  HIS D NE2 1 
ATOM   6994 N  N   . ILE D  1 78  ? -8.248  3.752   -29.731 1.00 17.27  ? 78  ILE D N   1 
ATOM   6995 C  CA  . ILE D  1 78  ? -7.848  2.668   -28.838 1.00 18.20  ? 78  ILE D CA  1 
ATOM   6996 C  C   . ILE D  1 78  ? -8.435  2.850   -27.485 1.00 23.21  ? 78  ILE D C   1 
ATOM   6997 O  O   . ILE D  1 78  ? -8.396  3.995   -26.946 1.00 26.29  ? 78  ILE D O   1 
ATOM   6998 C  CB  . ILE D  1 78  ? -6.352  2.635   -28.709 1.00 15.89  ? 78  ILE D CB  1 
ATOM   6999 C  CG1 . ILE D  1 78  ? -5.677  2.310   -30.016 1.00 20.69  ? 78  ILE D CG1 1 
ATOM   7000 C  CG2 . ILE D  1 78  ? -5.909  1.661   -27.672 1.00 20.68  ? 78  ILE D CG2 1 
ATOM   7001 C  CD1 . ILE D  1 78  ? -4.205  2.847   -29.893 1.00 20.33  ? 78  ILE D CD1 1 
ATOM   7002 N  N   . GLN D  1 79  ? -8.993  1.732   -27.022 1.00 26.29  ? 79  GLN D N   1 
ATOM   7003 C  CA  . GLN D  1 79  ? -9.547  1.553   -25.658 1.00 31.15  ? 79  GLN D CA  1 
ATOM   7004 C  C   . GLN D  1 79  ? -8.533  0.774   -24.855 1.00 32.64  ? 79  GLN D C   1 
ATOM   7005 O  O   . GLN D  1 79  ? -8.061  -0.283  -25.340 1.00 31.94  ? 79  GLN D O   1 
ATOM   7006 C  CB  . GLN D  1 79  ? -10.841 0.698   -25.612 1.00 43.78  ? 79  GLN D CB  1 
ATOM   7007 C  CG  . GLN D  1 79  ? -12.151 1.271   -26.134 1.00 50.69  ? 79  GLN D CG  1 
ATOM   7008 C  CD  . GLN D  1 79  ? -12.882 2.267   -25.241 1.00 59.36  ? 79  GLN D CD  1 
ATOM   7009 O  OE1 . GLN D  1 79  ? -12.671 2.269   -23.996 1.00 39.75  ? 79  GLN D OE1 1 
ATOM   7010 N  NE2 . GLN D  1 79  ? -13.799 3.156   -25.885 1.00 48.72  ? 79  GLN D NE2 1 
ATOM   7011 N  N   . GLY D  1 80  ? -8.098  1.304   -23.704 1.00 37.13  ? 80  GLY D N   1 
ATOM   7012 C  CA  . GLY D  1 80  ? -7.129  0.606   -22.860 1.00 26.60  ? 80  GLY D CA  1 
ATOM   7013 C  C   . GLY D  1 80  ? -5.933  1.288   -22.179 1.00 27.51  ? 80  GLY D C   1 
ATOM   7014 O  O   . GLY D  1 80  ? -5.392  0.739   -21.220 1.00 34.16  ? 80  GLY D O   1 
ATOM   7015 N  N   . LEU D  1 81  ? -5.514  2.462   -22.652 1.00 20.75  ? 81  LEU D N   1 
ATOM   7016 C  CA  . LEU D  1 81  ? -4.312  3.215   -22.080 1.00 23.07  ? 81  LEU D CA  1 
ATOM   7017 C  C   . LEU D  1 81  ? -4.671  4.278   -20.895 1.00 19.53  ? 81  LEU D C   1 
ATOM   7018 O  O   . LEU D  1 81  ? -5.760  4.297   -20.473 1.00 34.95  ? 81  LEU D O   1 
ATOM   7019 C  CB  . LEU D  1 81  ? -3.649  3.924   -23.303 1.00 27.52  ? 81  LEU D CB  1 
ATOM   7020 C  CG  . LEU D  1 81  ? -3.245  2.971   -24.426 1.00 21.40  ? 81  LEU D CG  1 
ATOM   7021 C  CD1 . LEU D  1 81  ? -2.904  3.799   -25.692 1.00 23.82  ? 81  LEU D CD1 1 
ATOM   7022 C  CD2 . LEU D  1 81  ? -2.050  2.142   -23.906 1.00 21.56  ? 81  LEU D CD2 1 
ATOM   7023 N  N   . GLN D  1 82  ? -3.713  5.168   -20.561 1.00 21.46  ? 82  GLN D N   1 
ATOM   7024 C  CA  . GLN D  1 82  ? -3.995  6.109   -19.391 1.00 19.57  ? 82  GLN D CA  1 
ATOM   7025 C  C   . GLN D  1 82  ? -5.076  7.101   -19.916 1.00 23.64  ? 82  GLN D C   1 
ATOM   7026 O  O   . GLN D  1 82  ? -5.578  7.774   -19.056 1.00 22.54  ? 82  GLN D O   1 
ATOM   7027 C  CB  . GLN D  1 82  ? -2.656  6.715   -18.848 1.00 25.67  ? 82  GLN D CB  1 
ATOM   7028 C  CG  . GLN D  1 82  ? -2.245  8.144   -19.379 1.00 31.44  ? 82  GLN D CG  1 
ATOM   7029 C  CD  . GLN D  1 82  ? -1.788  8.015   -20.824 1.00 30.70  ? 82  GLN D CD  1 
ATOM   7030 O  OE1 . GLN D  1 82  ? -1.485  6.909   -21.398 1.00 30.16  ? 82  GLN D OE1 1 
ATOM   7031 N  NE2 . GLN D  1 82  ? -1.713  9.127   -21.475 1.00 25.38  ? 82  GLN D NE2 1 
ATOM   7032 N  N   . SER D  1 83  ? -5.413  7.211   -21.252 1.00 25.23  ? 83  SER D N   1 
ATOM   7033 C  CA  . SER D  1 83  ? -6.423  8.174   -21.875 1.00 23.78  ? 83  SER D CA  1 
ATOM   7034 C  C   . SER D  1 83  ? -6.905  7.668   -23.192 1.00 21.22  ? 83  SER D C   1 
ATOM   7035 O  O   . SER D  1 83  ? -6.324  6.651   -23.715 1.00 23.74  ? 83  SER D O   1 
ATOM   7036 C  CB  . SER D  1 83  ? -5.683  9.520   -22.125 1.00 23.79  ? 83  SER D CB  1 
ATOM   7037 O  OG  . SER D  1 83  ? -5.063  10.069  -20.966 1.00 30.75  ? 83  SER D OG  1 
ATOM   7038 N  N   . ARG D  1 84  ? -7.969  8.214   -23.741 1.00 21.52  ? 84  ARG D N   1 
ATOM   7039 C  CA  . ARG D  1 84  ? -8.392  7.846   -25.064 1.00 19.64  ? 84  ARG D CA  1 
ATOM   7040 C  C   . ARG D  1 84  ? -7.455  8.408   -26.127 1.00 18.87  ? 84  ARG D C   1 
ATOM   7041 O  O   . ARG D  1 84  ? -7.083  9.597   -26.098 1.00 19.75  ? 84  ARG D O   1 
ATOM   7042 C  CB  . ARG D  1 84  ? -9.806  8.449   -25.473 1.00 21.77  ? 84  ARG D CB  1 
ATOM   7043 C  CG  . ARG D  1 84  ? -10.201 8.136   -26.950 1.00 23.84  ? 84  ARG D CG  1 
ATOM   7044 C  CD  . ARG D  1 84  ? -11.666 8.427   -27.269 1.00 24.28  ? 84  ARG D CD  1 
ATOM   7045 N  NE  . ARG D  1 84  ? -11.856 8.518   -28.731 1.00 29.91  ? 84  ARG D NE  1 
ATOM   7046 C  CZ  . ARG D  1 84  ? -13.016 8.385   -29.403 1.00 32.43  ? 84  ARG D CZ  1 
ATOM   7047 N  NH1 . ARG D  1 84  ? -14.163 8.197   -28.682 1.00 42.76  ? 84  ARG D NH1 1 
ATOM   7048 N  NH2 . ARG D  1 84  ? -13.009 8.432   -30.744 1.00 30.38  ? 84  ARG D NH2 1 
ATOM   7049 N  N   . TYR D  1 85  ? -6.945  7.538   -27.017 1.00 16.95  ? 85  TYR D N   1 
ATOM   7050 C  CA  . TYR D  1 85  ? -6.122  7.920   -28.113 1.00 14.21  ? 85  TYR D CA  1 
ATOM   7051 C  C   . TYR D  1 85  ? -6.869  7.664   -29.401 1.00 16.43  ? 85  TYR D C   1 
ATOM   7052 O  O   . TYR D  1 85  ? -7.321  6.524   -29.703 1.00 16.65  ? 85  TYR D O   1 
ATOM   7053 C  CB  . TYR D  1 85  ? -4.795  7.116   -28.081 1.00 16.06  ? 85  TYR D CB  1 
ATOM   7054 C  CG  . TYR D  1 85  ? -3.784  7.649   -27.084 1.00 14.29  ? 85  TYR D CG  1 
ATOM   7055 C  CD1 . TYR D  1 85  ? -3.842  7.177   -25.714 1.00 16.39  ? 85  TYR D CD1 1 
ATOM   7056 C  CD2 . TYR D  1 85  ? -2.860  8.606   -27.427 1.00 14.35  ? 85  TYR D CD2 1 
ATOM   7057 C  CE1 . TYR D  1 85  ? -2.895  7.700   -24.806 1.00 17.49  ? 85  TYR D CE1 1 
ATOM   7058 C  CE2 . TYR D  1 85  ? -1.932  9.082   -26.534 1.00 14.71  ? 85  TYR D CE2 1 
ATOM   7059 C  CZ  . TYR D  1 85  ? -1.976  8.637   -25.208 1.00 16.72  ? 85  TYR D CZ  1 
ATOM   7060 O  OH  . TYR D  1 85  ? -1.045  9.087   -24.241 1.00 18.61  ? 85  TYR D OH  1 
ATOM   7061 N  N   . SER D  1 86  ? -7.054  8.721   -30.170 1.00 15.13  ? 86  SER D N   1 
ATOM   7062 C  CA  . SER D  1 86  ? -7.872  8.631   -31.395 1.00 15.77  ? 86  SER D CA  1 
ATOM   7063 C  C   . SER D  1 86  ? -6.919  8.640   -32.632 1.00 12.57  ? 86  SER D C   1 
ATOM   7064 O  O   . SER D  1 86  ? -5.874  9.266   -32.635 1.00 13.85  ? 86  SER D O   1 
ATOM   7065 C  CB  . SER D  1 86  ? -8.722  9.969   -31.513 1.00 16.83  ? 86  SER D CB  1 
ATOM   7066 O  OG  . SER D  1 86  ? -9.670  9.969   -30.425 1.00 17.83  ? 86  SER D OG  1 
ATOM   7067 N  N   . ALA D  1 87  ? -7.337  7.827   -33.618 1.00 13.02  ? 87  ALA D N   1 
ATOM   7068 C  CA  . ALA D  1 87  ? -6.415  7.705   -34.793 1.00 13.53  ? 87  ALA D CA  1 
ATOM   7069 C  C   . ALA D  1 87  ? -6.300  8.970   -35.582 1.00 13.21  ? 87  ALA D C   1 
ATOM   7070 O  O   . ALA D  1 87  ? -7.243  9.793   -35.635 1.00 14.53  ? 87  ALA D O   1 
ATOM   7071 C  CB  . ALA D  1 87  ? -7.043  6.655   -35.691 1.00 15.38  ? 87  ALA D CB  1 
ATOM   7072 N  N   . THR D  1 88  ? -5.152  9.147   -36.196 1.00 12.64  ? 88  THR D N   1 
ATOM   7073 C  CA  . THR D  1 88  ? -4.911  10.250  -37.087 1.00 13.19  ? 88  THR D CA  1 
ATOM   7074 C  C   . THR D  1 88  ? -4.385  9.806   -38.454 1.00 11.63  ? 88  THR D C   1 
ATOM   7075 O  O   . THR D  1 88  ? -4.837  10.326  -39.488 1.00 12.11  ? 88  THR D O   1 
ATOM   7076 C  CB  . THR D  1 88  ? -4.046  11.350  -36.419 1.00 14.31  ? 88  THR D CB  1 
ATOM   7077 O  OG1 . THR D  1 88  ? -3.861  12.449  -37.345 1.00 17.24  ? 88  THR D OG1 1 
ATOM   7078 C  CG2 . THR D  1 88  ? -2.712  10.897  -36.017 1.00 15.38  ? 88  THR D CG2 1 
ATOM   7079 N  N   . GLN D  1 89  ? -3.445  8.862   -38.506 1.00 11.06  ? 89  GLN D N   1 
ATOM   7080 C  CA  . GLN D  1 89  ? -2.923  8.379   -39.811 1.00 10.83  ? 89  GLN D CA  1 
ATOM   7081 C  C   . GLN D  1 89  ? -2.226  7.064   -39.600 1.00 9.84   ? 89  GLN D C   1 
ATOM   7082 O  O   . GLN D  1 89  ? -1.794  6.767   -38.469 1.00 11.16  ? 89  GLN D O   1 
ATOM   7083 C  CB  . GLN D  1 89  ? -1.978  9.439   -40.467 1.00 10.97  ? 89  GLN D CB  1 
ATOM   7084 C  CG  . GLN D  1 89  ? -0.869  9.911   -39.552 1.00 14.15  ? 89  GLN D CG  1 
ATOM   7085 C  CD  . GLN D  1 89  ? 0.463   9.536   -39.995 1.00 13.12  ? 89  GLN D CD  1 
ATOM   7086 O  OE1 . GLN D  1 89  ? 0.664   8.334   -40.232 1.00 14.06  ? 89  GLN D OE1 1 
ATOM   7087 N  NE2 . GLN D  1 89  ? 1.433   10.352  -39.988 1.00 19.38  ? 89  GLN D NE2 1 
ATOM   7088 N  N   . LEU D  1 90  ? -2.022  6.339   -40.693 1.00 10.00  ? 90  LEU D N   1 
ATOM   7089 C  CA  . LEU D  1 90  ? -1.073  5.246   -40.678 1.00 9.96   ? 90  LEU D CA  1 
ATOM   7090 C  C   . LEU D  1 90  ? -0.083  5.423   -41.856 1.00 9.09   ? 90  LEU D C   1 
ATOM   7091 O  O   . LEU D  1 90  ? -0.381  6.110   -42.826 1.00 10.34  ? 90  LEU D O   1 
ATOM   7092 C  CB  . LEU D  1 90  ? -1.779  3.850   -40.687 1.00 10.48  ? 90  LEU D CB  1 
ATOM   7093 C  CG  . LEU D  1 90  ? -2.726  3.488   -41.827 1.00 10.76  ? 90  LEU D CG  1 
ATOM   7094 C  CD1 . LEU D  1 90  ? -1.943  3.147   -43.148 1.00 11.53  ? 90  LEU D CD1 1 
ATOM   7095 C  CD2 . LEU D  1 90  ? -3.553  2.339   -41.434 1.00 13.09  ? 90  LEU D CD2 1 
ATOM   7096 N  N   . HIS D  1 91  ? 1.064   4.783   -41.719 1.00 9.28   ? 91  HIS D N   1 
ATOM   7097 C  CA  . HIS D  1 91  ? 2.088   4.876   -42.758 1.00 9.12   ? 91  HIS D CA  1 
ATOM   7098 C  C   . HIS D  1 91  ? 3.037   3.704   -42.566 1.00 8.95   ? 91  HIS D C   1 
ATOM   7099 O  O   . HIS D  1 91  ? 2.939   2.940   -41.597 1.00 9.54   ? 91  HIS D O   1 
ATOM   7100 C  CB  . HIS D  1 91  ? 2.807   6.241   -42.691 1.00 9.31   ? 91  HIS D CB  1 
ATOM   7101 C  CG  . HIS D  1 91  ? 3.575   6.396   -41.419 1.00 8.67   ? 91  HIS D CG  1 
ATOM   7102 N  ND1 . HIS D  1 91  ? 3.064   7.055   -40.302 1.00 9.95   ? 91  HIS D ND1 1 
ATOM   7103 C  CD2 . HIS D  1 91  ? 4.753   5.882   -41.011 1.00 9.42   ? 91  HIS D CD2 1 
ATOM   7104 C  CE1 . HIS D  1 91  ? 3.938   6.912   -39.300 1.00 9.52   ? 91  HIS D CE1 1 
ATOM   7105 N  NE2 . HIS D  1 91  ? 4.974   6.192   -39.686 1.00 9.15   ? 91  HIS D NE2 1 
ATOM   7106 N  N   . LEU D  1 92  ? 4.007   3.592   -43.505 1.00 9.35   ? 92  LEU D N   1 
ATOM   7107 C  CA  . LEU D  1 92  ? 4.919   2.450   -43.498 1.00 9.66   ? 92  LEU D CA  1 
ATOM   7108 C  C   . LEU D  1 92  ? 6.395   2.868   -43.588 1.00 8.62   ? 92  LEU D C   1 
ATOM   7109 O  O   . LEU D  1 92  ? 6.722   3.997   -43.967 1.00 10.25  ? 92  LEU D O   1 
ATOM   7110 C  CB  . LEU D  1 92  ? 4.617   1.501   -44.649 1.00 12.48  ? 92  LEU D CB  1 
ATOM   7111 C  CG  . LEU D  1 92  ? 3.229   0.816   -44.530 1.00 12.95  ? 92  LEU D CG  1 
ATOM   7112 C  CD1 . LEU D  1 92  ? 2.244   1.468   -45.324 1.00 18.00  ? 92  LEU D CD1 1 
ATOM   7113 C  CD2 . LEU D  1 92  ? 3.328   -0.607  -44.633 1.00 16.98  ? 92  LEU D CD2 1 
ATOM   7114 N  N   . HIS D  1 93  ? 7.260   1.945   -43.243 1.00 9.31   ? 93  HIS D N   1 
ATOM   7115 C  CA  . HIS D  1 93  ? 8.723   2.087   -43.429 1.00 9.17   ? 93  HIS D CA  1 
ATOM   7116 C  C   . HIS D  1 93  ? 9.224   0.816   -44.076 1.00 9.05   ? 93  HIS D C   1 
ATOM   7117 O  O   . HIS D  1 93  ? 8.733   -0.275  -43.751 1.00 10.14  ? 93  HIS D O   1 
ATOM   7118 C  CB  . HIS D  1 93  ? 9.404   2.276   -42.062 1.00 9.36   ? 93  HIS D CB  1 
ATOM   7119 C  CG  . HIS D  1 93  ? 8.934   3.465   -41.316 1.00 9.08   ? 93  HIS D CG  1 
ATOM   7120 N  ND1 . HIS D  1 93  ? 9.520   4.697   -41.380 1.00 9.64   ? 93  HIS D ND1 1 
ATOM   7121 C  CD2 . HIS D  1 93  ? 7.857   3.623   -40.460 1.00 9.15   ? 93  HIS D CD2 1 
ATOM   7122 C  CE1 . HIS D  1 93  ? 8.839   5.570   -40.596 1.00 9.96   ? 93  HIS D CE1 1 
ATOM   7123 N  NE2 . HIS D  1 93  ? 7.849   4.948   -40.017 1.00 8.77   ? 93  HIS D NE2 1 
ATOM   7124 N  N   . TRP D  1 94  ? 10.151  0.966   -45.019 1.00 9.16   ? 94  TRP D N   1 
ATOM   7125 C  CA  . TRP D  1 94  ? 10.628  -0.186  -45.772 1.00 9.53   ? 94  TRP D CA  1 
ATOM   7126 C  C   . TRP D  1 94  ? 12.064  0.050   -46.239 1.00 9.86   ? 94  TRP D C   1 
ATOM   7127 O  O   . TRP D  1 94  ? 12.678  1.099   -46.048 1.00 10.02  ? 94  TRP D O   1 
ATOM   7128 C  CB  . TRP D  1 94  ? 9.706   -0.478  -46.968 1.00 10.44  ? 94  TRP D CB  1 
ATOM   7129 C  CG  . TRP D  1 94  ? 9.567   0.737   -47.918 1.00 10.17  ? 94  TRP D CG  1 
ATOM   7130 C  CD1 . TRP D  1 94  ? 10.406  1.028   -48.954 1.00 10.72  ? 94  TRP D CD1 1 
ATOM   7131 C  CD2 . TRP D  1 94  ? 8.620   1.791   -47.893 1.00 10.51  ? 94  TRP D CD2 1 
ATOM   7132 N  NE1 . TRP D  1 94  ? 10.005  2.171   -49.578 1.00 10.86  ? 94  TRP D NE1 1 
ATOM   7133 C  CE2 . TRP D  1 94  ? 8.879   2.636   -48.965 1.00 10.60  ? 94  TRP D CE2 1 
ATOM   7134 C  CE3 . TRP D  1 94  ? 7.513   2.074   -47.034 1.00 10.45  ? 94  TRP D CE3 1 
ATOM   7135 C  CZ2 . TRP D  1 94  ? 8.078   3.731   -49.270 1.00 11.81  ? 94  TRP D CZ2 1 
ATOM   7136 C  CZ3 . TRP D  1 94  ? 6.759   3.202   -47.325 1.00 11.15  ? 94  TRP D CZ3 1 
ATOM   7137 C  CH2 . TRP D  1 94  ? 7.060   4.039   -48.431 1.00 11.73  ? 94  TRP D CH2 1 
ATOM   7138 N  N   . GLY D  1 95  ? 12.603  -1.014  -46.859 1.00 10.43  ? 95  GLY D N   1 
ATOM   7139 C  CA  . GLY D  1 95  ? 14.018  -1.083  -47.280 1.00 11.49  ? 95  GLY D CA  1 
ATOM   7140 C  C   . GLY D  1 95  ? 14.042  -0.819  -48.810 1.00 11.75  ? 95  GLY D C   1 
ATOM   7141 O  O   . GLY D  1 95  ? 13.604  0.211   -49.329 1.00 11.60  ? 95  GLY D O   1 
ATOM   7142 N  N   . ASN D  1 96  ? 14.677  -1.775  -49.527 1.00 12.46  ? 96  ASN D N   1 
ATOM   7143 C  CA  . ASN D  1 96  ? 14.748  -1.593  -51.026 1.00 13.63  ? 96  ASN D CA  1 
ATOM   7144 C  C   . ASN D  1 96  ? 14.918  -2.974  -51.576 1.00 13.92  ? 96  ASN D C   1 
ATOM   7145 O  O   . ASN D  1 96  ? 15.125  -3.962  -50.847 1.00 15.35  ? 96  ASN D O   1 
ATOM   7146 C  CB  . ASN D  1 96  ? 15.933  -0.666  -51.382 1.00 16.07  ? 96  ASN D CB  1 
ATOM   7147 C  CG  . ASN D  1 96  ? 17.269  -1.318  -51.187 1.00 16.72  ? 96  ASN D CG  1 
ATOM   7148 O  OD1 . ASN D  1 96  ? 17.724  -2.021  -52.116 1.00 20.28  ? 96  ASN D OD1 1 
ATOM   7149 N  ND2 . ASN D  1 96  ? 17.887  -1.124  -50.057 1.00 17.56  ? 96  ASN D ND2 1 
ATOM   7150 N  N   . PRO D  1 97  ? 14.827  -3.167  -52.951 1.00 15.62  ? 97  PRO D N   1 
ATOM   7151 C  CA  . PRO D  1 97  ? 14.784  -4.539  -53.502 1.00 20.59  ? 97  PRO D CA  1 
ATOM   7152 C  C   . PRO D  1 97  ? 16.084  -5.269  -53.182 1.00 18.87  ? 97  PRO D C   1 
ATOM   7153 O  O   . PRO D  1 97  ? 16.044  -6.525  -53.024 1.00 25.89  ? 97  PRO D O   1 
ATOM   7154 C  CB  . PRO D  1 97  ? 14.595  -4.280  -55.001 1.00 24.14  ? 97  PRO D CB  1 
ATOM   7155 C  CG  . PRO D  1 97  ? 13.917  -2.900  -55.064 1.00 22.61  ? 97  PRO D CG  1 
ATOM   7156 C  CD  . PRO D  1 97  ? 14.509  -2.119  -53.906 1.00 17.33  ? 97  PRO D CD  1 
ATOM   7157 N  N   . ASN D  1 98  ? 17.223  -4.540  -53.041 1.00 16.24  ? 98  ASN D N   1 
ATOM   7158 C  CA  . ASN D  1 98  ? 18.512  -5.275  -52.768 1.00 20.22  ? 98  ASN D CA  1 
ATOM   7159 C  C   . ASN D  1 98  ? 18.691  -5.556  -51.276 1.00 22.66  ? 98  ASN D C   1 
ATOM   7160 O  O   . ASN D  1 98  ? 19.545  -6.376  -50.974 1.00 27.35  ? 98  ASN D O   1 
ATOM   7161 C  CB  . ASN D  1 98  ? 19.683  -4.389  -53.213 1.00 19.64  ? 98  ASN D CB  1 
ATOM   7162 C  CG  . ASN D  1 98  ? 19.635  -4.063  -54.732 1.00 26.25  ? 98  ASN D CG  1 
ATOM   7163 O  OD1 . ASN D  1 98  ? 19.011  -4.773  -55.498 1.00 34.30  ? 98  ASN D OD1 1 
ATOM   7164 N  ND2 . ASN D  1 98  ? 20.391  -3.054  -55.162 1.00 31.53  ? 98  ASN D ND2 1 
ATOM   7165 N  N   . ASP D  1 99  ? 17.883  -4.940  -50.413 1.00 17.86  ? 99  ASP D N   1 
ATOM   7166 C  CA  . ASP D  1 99  ? 17.989  -5.172  -48.970 1.00 17.20  ? 99  ASP D CA  1 
ATOM   7167 C  C   . ASP D  1 99  ? 16.545  -4.994  -48.398 1.00 14.41  ? 99  ASP D C   1 
ATOM   7168 O  O   . ASP D  1 99  ? 16.212  -3.887  -47.895 1.00 14.79  ? 99  ASP D O   1 
ATOM   7169 C  CB  . ASP D  1 99  ? 19.010  -4.187  -48.317 1.00 20.28  ? 99  ASP D CB  1 
ATOM   7170 C  CG  . ASP D  1 99  ? 19.118  -4.321  -46.786 1.00 22.74  ? 99  ASP D CG  1 
ATOM   7171 O  OD1 . ASP D  1 99  ? 18.784  -5.430  -46.307 1.00 26.03  ? 99  ASP D OD1 1 
ATOM   7172 O  OD2 . ASP D  1 99  ? 19.505  -3.325  -46.068 1.00 33.35  ? 99  ASP D OD2 1 
ATOM   7173 N  N   . PRO D  1 100 ? 15.742  -6.012  -48.492 1.00 14.86  ? 100 PRO D N   1 
ATOM   7174 C  CA  . PRO D  1 100 ? 14.299  -5.871  -48.052 1.00 14.97  ? 100 PRO D CA  1 
ATOM   7175 C  C   . PRO D  1 100 ? 14.210  -6.079  -46.563 1.00 13.56  ? 100 PRO D C   1 
ATOM   7176 O  O   . PRO D  1 100 ? 13.544  -7.009  -46.076 1.00 15.74  ? 100 PRO D O   1 
ATOM   7177 C  CB  . PRO D  1 100 ? 13.599  -6.918  -48.858 1.00 18.89  ? 100 PRO D CB  1 
ATOM   7178 C  CG  . PRO D  1 100 ? 14.706  -8.052  -49.033 1.00 20.13  ? 100 PRO D CG  1 
ATOM   7179 C  CD  . PRO D  1 100 ? 16.033  -7.308  -49.147 1.00 18.02  ? 100 PRO D CD  1 
ATOM   7180 N  N   . HIS D  1 101 ? 14.854  -5.201  -45.770 1.00 13.65  ? 101 HIS D N   1 
ATOM   7181 C  CA  . HIS D  1 101 ? 14.973  -5.350  -44.309 1.00 13.61  ? 101 HIS D CA  1 
ATOM   7182 C  C   . HIS D  1 101 ? 14.880  -3.973  -43.664 1.00 12.91  ? 101 HIS D C   1 
ATOM   7183 O  O   . HIS D  1 101 ? 15.800  -3.485  -42.990 1.00 16.19  ? 101 HIS D O   1 
ATOM   7184 C  CB  . HIS D  1 101 ? 16.318  -6.073  -43.970 1.00 17.19  ? 101 HIS D CB  1 
ATOM   7185 C  CG  . HIS D  1 101 ? 16.419  -7.440  -44.593 1.00 20.59  ? 101 HIS D CG  1 
ATOM   7186 N  ND1 . HIS D  1 101 ? 15.719  -8.539  -44.180 1.00 26.36  ? 101 HIS D ND1 1 
ATOM   7187 C  CD2 . HIS D  1 101 ? 17.085  -7.827  -45.709 1.00 21.36  ? 101 HIS D CD2 1 
ATOM   7188 C  CE1 . HIS D  1 101 ? 16.052  -9.595  -44.913 1.00 28.60  ? 101 HIS D CE1 1 
ATOM   7189 N  NE2 . HIS D  1 101 ? 16.876  -9.175  -45.858 1.00 25.88  ? 101 HIS D NE2 1 
ATOM   7190 N  N   . GLY D  1 102 ? 13.717  -3.337  -43.862 1.00 11.52  ? 102 GLY D N   1 
ATOM   7191 C  CA  . GLY D  1 102 ? 13.530  -1.969  -43.528 1.00 11.96  ? 102 GLY D CA  1 
ATOM   7192 C  C   . GLY D  1 102 ? 12.543  -1.706  -42.402 1.00 10.22  ? 102 GLY D C   1 
ATOM   7193 O  O   . GLY D  1 102 ? 12.054  -0.579  -42.284 1.00 11.69  ? 102 GLY D O   1 
ATOM   7194 N  N   . SER D  1 103 ? 12.293  -2.690  -41.514 1.00 10.33  ? 103 SER D N   1 
ATOM   7195 C  CA  . SER D  1 103 ? 11.589  -2.305  -40.288 1.00 10.05  ? 103 SER D CA  1 
ATOM   7196 C  C   . SER D  1 103 ? 12.407  -1.288  -39.473 1.00 9.32   ? 103 SER D C   1 
ATOM   7197 O  O   . SER D  1 103 ? 13.636  -1.252  -39.600 1.00 11.56  ? 103 SER D O   1 
ATOM   7198 C  CB  . SER D  1 103 ? 11.273  -3.507  -39.438 1.00 10.37  ? 103 SER D CB  1 
ATOM   7199 O  OG  . SER D  1 103 ? 12.423  -4.116  -38.888 1.00 10.23  ? 103 SER D OG  1 
ATOM   7200 N  N   . GLU D  1 104 ? 11.728  -0.542  -38.634 1.00 9.81   ? 104 GLU D N   1 
ATOM   7201 C  CA  . GLU D  1 104 ? 12.421  0.371   -37.722 1.00 9.90   ? 104 GLU D CA  1 
ATOM   7202 C  C   . GLU D  1 104 ? 12.831  -0.339  -36.459 1.00 9.12   ? 104 GLU D C   1 
ATOM   7203 O  O   . GLU D  1 104 ? 14.005  -0.368  -36.092 1.00 9.90   ? 104 GLU D O   1 
ATOM   7204 C  CB  . GLU D  1 104 ? 11.494  1.566   -37.432 1.00 10.85  ? 104 GLU D CB  1 
ATOM   7205 C  CG  . GLU D  1 104 ? 11.099  2.309   -38.717 1.00 10.36  ? 104 GLU D CG  1 
ATOM   7206 C  CD  . GLU D  1 104 ? 11.021  3.782   -38.481 1.00 9.61   ? 104 GLU D CD  1 
ATOM   7207 O  OE1 . GLU D  1 104 ? 10.063  4.210   -37.872 1.00 10.72  ? 104 GLU D OE1 1 
ATOM   7208 O  OE2 . GLU D  1 104 ? 12.021  4.485   -38.855 1.00 11.06  ? 104 GLU D OE2 1 
ATOM   7209 N  N   . HIS D  1 105 ? 11.840  -0.916  -35.733 1.00 9.94   ? 105 HIS D N   1 
ATOM   7210 C  CA  . HIS D  1 105 ? 12.214  -1.795  -34.620 1.00 9.51   ? 105 HIS D CA  1 
ATOM   7211 C  C   . HIS D  1 105 ? 12.869  -3.062  -35.127 1.00 9.73   ? 105 HIS D C   1 
ATOM   7212 O  O   . HIS D  1 105 ? 12.515  -3.574  -36.204 1.00 11.07  ? 105 HIS D O   1 
ATOM   7213 C  CB  . HIS D  1 105 ? 10.969  -2.070  -33.772 1.00 10.16  ? 105 HIS D CB  1 
ATOM   7214 C  CG  . HIS D  1 105 ? 10.447  -0.875  -33.106 1.00 10.01  ? 105 HIS D CG  1 
ATOM   7215 N  ND1 . HIS D  1 105 ? 9.527   -0.025  -33.658 1.00 10.71  ? 105 HIS D ND1 1 
ATOM   7216 C  CD2 . HIS D  1 105 ? 10.776  -0.306  -31.879 1.00 10.90  ? 105 HIS D CD2 1 
ATOM   7217 C  CE1 . HIS D  1 105 ? 9.334   1.019   -32.838 1.00 11.45  ? 105 HIS D CE1 1 
ATOM   7218 N  NE2 . HIS D  1 105 ? 10.072  0.873   -31.732 1.00 11.03  ? 105 HIS D NE2 1 
ATOM   7219 N  N   . THR D  1 106 ? 13.768  -3.564  -34.351 1.00 10.73  ? 106 THR D N   1 
ATOM   7220 C  CA  . THR D  1 106 ? 14.399  -4.859  -34.615 1.00 10.82  ? 106 THR D CA  1 
ATOM   7221 C  C   . THR D  1 106 ? 14.083  -5.770  -33.378 1.00 10.93  ? 106 THR D C   1 
ATOM   7222 O  O   . THR D  1 106 ? 13.813  -5.298  -32.307 1.00 11.84  ? 106 THR D O   1 
ATOM   7223 C  CB  . THR D  1 106 ? 15.890  -4.713  -34.895 1.00 11.45  ? 106 THR D CB  1 
ATOM   7224 O  OG1 . THR D  1 106 ? 16.555  -4.114  -33.793 1.00 12.68  ? 106 THR D OG1 1 
ATOM   7225 C  CG2 . THR D  1 106 ? 16.081  -3.828  -36.124 1.00 13.26  ? 106 THR D CG2 1 
ATOM   7226 N  N   . VAL D  1 107 ? 14.168  -7.071  -33.642 1.00 11.80  ? 107 VAL D N   1 
ATOM   7227 C  CA  . VAL D  1 107 ? 13.952  -8.088  -32.555 1.00 12.63  ? 107 VAL D CA  1 
ATOM   7228 C  C   . VAL D  1 107 ? 15.192  -8.942  -32.485 1.00 13.59  ? 107 VAL D C   1 
ATOM   7229 O  O   . VAL D  1 107 ? 15.562  -9.556  -33.506 1.00 14.49  ? 107 VAL D O   1 
ATOM   7230 C  CB  . VAL D  1 107 ? 12.684  -8.922  -32.751 1.00 13.90  ? 107 VAL D CB  1 
ATOM   7231 C  CG1 . VAL D  1 107 ? 12.633  -10.006 -31.625 1.00 18.00  ? 107 VAL D CG1 1 
ATOM   7232 C  CG2 . VAL D  1 107 ? 11.451  -8.018  -32.787 1.00 15.42  ? 107 VAL D CG2 1 
ATOM   7233 N  N   . SER D  1 108 ? 15.877  -8.904  -31.332 1.00 13.71  ? 108 SER D N   1 
ATOM   7234 C  CA  . SER D  1 108 ? 17.122  -9.720  -31.160 1.00 15.45  ? 108 SER D CA  1 
ATOM   7235 C  C   . SER D  1 108 ? 18.072  -9.400  -32.354 1.00 13.60  ? 108 SER D C   1 
ATOM   7236 O  O   . SER D  1 108 ? 18.717  -10.333 -32.922 1.00 16.63  ? 108 SER D O   1 
ATOM   7237 C  CB  . SER D  1 108 ? 16.783  -11.194 -31.066 1.00 18.32  ? 108 SER D CB  1 
ATOM   7238 O  OG  . SER D  1 108 ? 16.032  -11.395 -29.889 1.00 20.03  ? 108 SER D OG  1 
ATOM   7239 N  N   . GLY D  1 109 ? 18.201  -8.125  -32.669 1.00 13.81  ? 109 GLY D N   1 
ATOM   7240 C  CA  . GLY D  1 109 ? 19.130  -7.637  -33.694 1.00 14.20  ? 109 GLY D CA  1 
ATOM   7241 C  C   . GLY D  1 109 ? 18.688  -7.855  -35.129 1.00 15.63  ? 109 GLY D C   1 
ATOM   7242 O  O   . GLY D  1 109 ? 19.525  -7.475  -36.027 1.00 20.90  ? 109 GLY D O   1 
ATOM   7243 N  N   . GLN D  1 110 ? 17.526  -8.337  -35.414 1.00 14.75  ? 110 GLN D N   1 
ATOM   7244 C  CA  . GLN D  1 110 ? 17.115  -8.640  -36.766 1.00 14.64  ? 110 GLN D CA  1 
ATOM   7245 C  C   . GLN D  1 110 ? 15.998  -7.672  -37.197 1.00 12.70  ? 110 GLN D C   1 
ATOM   7246 O  O   . GLN D  1 110 ? 15.026  -7.456  -36.488 1.00 12.33  ? 110 GLN D O   1 
ATOM   7247 C  CB  . GLN D  1 110 ? 16.526  -10.088 -36.831 1.00 18.14  ? 110 GLN D CB  1 
ATOM   7248 C  CG  . GLN D  1 110 ? 17.411  -11.214 -36.246 1.00 22.87  ? 110 GLN D CG  1 
ATOM   7249 C  CD  . GLN D  1 110 ? 18.798  -11.050 -36.794 1.00 26.31  ? 110 GLN D CD  1 
ATOM   7250 O  OE1 . GLN D  1 110 ? 19.042  -11.172 -37.989 1.00 30.56  ? 110 GLN D OE1 1 
ATOM   7251 N  NE2 . GLN D  1 110 ? 19.785  -10.901 -35.857 1.00 28.30  ? 110 GLN D NE2 1 
ATOM   7252 N  N   . HIS D  1 111 ? 16.184  -7.115  -38.403 1.00 13.30  ? 111 HIS D N   1 
ATOM   7253 C  CA  . HIS D  1 111 ? 15.112  -6.380  -39.035 1.00 12.43  ? 111 HIS D CA  1 
ATOM   7254 C  C   . HIS D  1 111 ? 14.049  -7.321  -39.636 1.00 13.30  ? 111 HIS D C   1 
ATOM   7255 O  O   . HIS D  1 111 ? 14.369  -8.475  -39.992 1.00 17.52  ? 111 HIS D O   1 
ATOM   7256 C  CB  . HIS D  1 111 ? 15.596  -5.548  -40.240 1.00 13.95  ? 111 HIS D CB  1 
ATOM   7257 C  CG  . HIS D  1 111 ? 16.346  -4.315  -39.861 1.00 12.65  ? 111 HIS D CG  1 
ATOM   7258 N  ND1 . HIS D  1 111 ? 15.728  -3.076  -39.667 1.00 13.61  ? 111 HIS D ND1 1 
ATOM   7259 C  CD2 . HIS D  1 111 ? 17.649  -4.135  -39.594 1.00 14.86  ? 111 HIS D CD2 1 
ATOM   7260 C  CE1 . HIS D  1 111 ? 16.682  -2.203  -39.312 1.00 14.91  ? 111 HIS D CE1 1 
ATOM   7261 N  NE2 . HIS D  1 111 ? 17.837  -2.799  -39.327 1.00 17.02  ? 111 HIS D NE2 1 
ATOM   7262 N  N   . PHE D  1 112 ? 12.858  -6.828  -39.693 1.00 11.04  ? 112 PHE D N   1 
ATOM   7263 C  CA  . PHE D  1 112 ? 11.813  -7.395  -40.492 1.00 11.35  ? 112 PHE D CA  1 
ATOM   7264 C  C   . PHE D  1 112 ? 11.843  -6.641  -41.850 1.00 9.91   ? 112 PHE D C   1 
ATOM   7265 O  O   . PHE D  1 112 ? 12.552  -5.635  -41.988 1.00 10.91  ? 112 PHE D O   1 
ATOM   7266 C  CB  . PHE D  1 112 ? 10.502  -7.342  -39.789 1.00 13.21  ? 112 PHE D CB  1 
ATOM   7267 C  CG  . PHE D  1 112 ? 10.381  -8.367  -38.681 1.00 13.69  ? 112 PHE D CG  1 
ATOM   7268 C  CD1 . PHE D  1 112 ? 10.967  -8.195  -37.475 1.00 18.54  ? 112 PHE D CD1 1 
ATOM   7269 C  CD2 . PHE D  1 112 ? 9.678   -9.542  -38.956 1.00 18.56  ? 112 PHE D CD2 1 
ATOM   7270 C  CE1 . PHE D  1 112 ? 10.831  -9.287  -36.519 1.00 19.68  ? 112 PHE D CE1 1 
ATOM   7271 C  CE2 . PHE D  1 112 ? 9.543   -10.580 -38.085 1.00 24.45  ? 112 PHE D CE2 1 
ATOM   7272 C  CZ  . PHE D  1 112 ? 10.131  -10.425 -36.896 1.00 21.05  ? 112 PHE D CZ  1 
ATOM   7273 N  N   . ALA D  1 113 ? 11.032  -7.108  -42.788 1.00 10.31  ? 113 ALA D N   1 
ATOM   7274 C  CA  . ALA D  1 113 ? 11.053  -6.496  -44.118 1.00 10.56  ? 113 ALA D CA  1 
ATOM   7275 C  C   . ALA D  1 113 ? 10.567  -5.022  -44.072 1.00 10.20  ? 113 ALA D C   1 
ATOM   7276 O  O   . ALA D  1 113 ? 11.060  -4.192  -44.830 1.00 10.50  ? 113 ALA D O   1 
ATOM   7277 C  CB  . ALA D  1 113 ? 10.183  -7.321  -45.066 1.00 12.60  ? 113 ALA D CB  1 
ATOM   7278 N  N   . ALA D  1 114 ? 9.502   -4.764  -43.294 1.00 9.89   ? 114 ALA D N   1 
ATOM   7279 C  CA  . ALA D  1 114 ? 8.875   -3.451  -43.299 1.00 9.27   ? 114 ALA D CA  1 
ATOM   7280 C  C   . ALA D  1 114 ? 8.155   -3.299  -41.948 1.00 9.19   ? 114 ALA D C   1 
ATOM   7281 O  O   . ALA D  1 114 ? 8.172   -4.232  -41.088 1.00 9.49   ? 114 ALA D O   1 
ATOM   7282 C  CB  . ALA D  1 114 ? 7.943   -3.300  -44.473 1.00 10.44  ? 114 ALA D CB  1 
ATOM   7283 N  N   . GLU D  1 115 ? 7.541   -2.133  -41.752 1.00 9.10   ? 115 GLU D N   1 
ATOM   7284 C  CA  . GLU D  1 115 ? 6.799   -1.894  -40.495 1.00 10.04  ? 115 GLU D CA  1 
ATOM   7285 C  C   . GLU D  1 115 ? 5.695   -0.929  -40.780 1.00 8.97   ? 115 GLU D C   1 
ATOM   7286 O  O   . GLU D  1 115 ? 5.853   0.066   -41.498 1.00 10.84  ? 115 GLU D O   1 
ATOM   7287 C  CB  . GLU D  1 115 ? 7.790   -1.300  -39.434 1.00 10.25  ? 115 GLU D CB  1 
ATOM   7288 C  CG  . GLU D  1 115 ? 7.255   -1.201  -38.060 1.00 11.06  ? 115 GLU D CG  1 
ATOM   7289 C  CD  . GLU D  1 115 ? 8.322   -0.939  -37.006 1.00 9.93   ? 115 GLU D CD  1 
ATOM   7290 O  OE1 . GLU D  1 115 ? 9.475   -1.398  -37.193 1.00 10.62  ? 115 GLU D OE1 1 
ATOM   7291 O  OE2 . GLU D  1 115 ? 8.025   -0.294  -35.956 1.00 10.47  ? 115 GLU D OE2 1 
ATOM   7292 N  N   . LEU D  1 116 ? 4.502   -1.199  -40.187 1.00 9.08   ? 116 LEU D N   1 
ATOM   7293 C  CA  . LEU D  1 116 ? 3.356   -0.307  -40.213 1.00 8.96   ? 116 LEU D CA  1 
ATOM   7294 C  C   . LEU D  1 116 ? 3.217   0.420   -38.915 1.00 9.12   ? 116 LEU D C   1 
ATOM   7295 O  O   . LEU D  1 116 ? 3.333   -0.215  -37.838 1.00 9.85   ? 116 LEU D O   1 
ATOM   7296 C  CB  . LEU D  1 116 ? 2.085   -1.189  -40.416 1.00 10.99  ? 116 LEU D CB  1 
ATOM   7297 C  CG  . LEU D  1 116 ? 0.739   -0.414  -40.304 1.00 10.61  ? 116 LEU D CG  1 
ATOM   7298 C  CD1 . LEU D  1 116 ? 0.509   0.419   -41.521 1.00 11.58  ? 116 LEU D CD1 1 
ATOM   7299 C  CD2 . LEU D  1 116 ? -0.373  -1.441  -40.085 1.00 12.91  ? 116 LEU D CD2 1 
ATOM   7300 N  N   . HIS D  1 117 ? 2.978   1.726   -38.971 1.00 8.93   ? 117 HIS D N   1 
ATOM   7301 C  CA  . HIS D  1 117 ? 2.696   2.535   -37.782 1.00 8.97   ? 117 HIS D CA  1 
ATOM   7302 C  C   . HIS D  1 117 ? 1.313   3.096   -37.915 1.00 8.55   ? 117 HIS D C   1 
ATOM   7303 O  O   . HIS D  1 117 ? 1.011   3.806   -38.895 1.00 9.95   ? 117 HIS D O   1 
ATOM   7304 C  CB  . HIS D  1 117 ? 3.714   3.668   -37.695 1.00 9.26   ? 117 HIS D CB  1 
ATOM   7305 C  CG  . HIS D  1 117 ? 5.062   3.189   -37.351 1.00 9.38   ? 117 HIS D CG  1 
ATOM   7306 N  ND1 . HIS D  1 117 ? 6.233   3.881   -37.623 1.00 8.61   ? 117 HIS D ND1 1 
ATOM   7307 C  CD2 . HIS D  1 117 ? 5.432   2.021   -36.745 1.00 10.29  ? 117 HIS D CD2 1 
ATOM   7308 C  CE1 . HIS D  1 117 ? 7.248   3.119   -37.188 1.00 9.14   ? 117 HIS D CE1 1 
ATOM   7309 N  NE2 . HIS D  1 117 ? 6.784   1.970   -36.655 1.00 9.42   ? 117 HIS D NE2 1 
ATOM   7310 N  N   . ILE D  1 118 ? 0.488   2.856   -36.896 1.00 9.10   ? 118 ILE D N   1 
ATOM   7311 C  CA  . ILE D  1 118 ? -0.881  3.468   -36.834 1.00 9.84   ? 118 ILE D CA  1 
ATOM   7312 C  C   . ILE D  1 118 ? -0.828  4.485   -35.741 1.00 10.09  ? 118 ILE D C   1 
ATOM   7313 O  O   . ILE D  1 118 ? -0.711  4.141   -34.538 1.00 11.11  ? 118 ILE D O   1 
ATOM   7314 C  CB  . ILE D  1 118 ? -2.014  2.442   -36.585 1.00 10.77  ? 118 ILE D CB  1 
ATOM   7315 C  CG1 . ILE D  1 118 ? -1.876  1.242   -37.551 1.00 11.39  ? 118 ILE D CG1 1 
ATOM   7316 C  CG2 . ILE D  1 118 ? -3.363  3.135   -36.764 1.00 12.33  ? 118 ILE D CG2 1 
ATOM   7317 C  CD1 . ILE D  1 118 ? -2.992  0.190   -37.292 1.00 13.77  ? 118 ILE D CD1 1 
ATOM   7318 N  N   . VAL D  1 119 ? -0.789  5.760   -36.101 1.00 10.22  ? 119 VAL D N   1 
ATOM   7319 C  CA  . VAL D  1 119 ? -0.571  6.864   -35.177 1.00 10.33  ? 119 VAL D CA  1 
ATOM   7320 C  C   . VAL D  1 119 ? -1.910  7.387   -34.647 1.00 10.69  ? 119 VAL D C   1 
ATOM   7321 O  O   . VAL D  1 119 ? -2.838  7.652   -35.386 1.00 11.49  ? 119 VAL D O   1 
ATOM   7322 C  CB  . VAL D  1 119 ? 0.150   8.030   -35.907 1.00 11.17  ? 119 VAL D CB  1 
ATOM   7323 C  CG1 . VAL D  1 119 ? 0.525   9.152   -34.930 1.00 12.09  ? 119 VAL D CG1 1 
ATOM   7324 C  CG2 . VAL D  1 119 ? 1.449   7.505   -36.634 1.00 11.35  ? 119 VAL D CG2 1 
ATOM   7325 N  N   . HIS D  1 120 ? -1.904  7.538   -33.294 1.00 11.37  ? 120 HIS D N   1 
ATOM   7326 C  CA  . HIS D  1 120 ? -3.071  8.081   -32.584 1.00 11.68  ? 120 HIS D CA  1 
ATOM   7327 C  C   . HIS D  1 120 ? -2.610  9.228   -31.687 1.00 12.84  ? 120 HIS D C   1 
ATOM   7328 O  O   . HIS D  1 120 ? -1.439  9.301   -31.322 1.00 12.93  ? 120 HIS D O   1 
ATOM   7329 C  CB  . HIS D  1 120 ? -3.627  6.952   -31.615 1.00 12.69  ? 120 HIS D CB  1 
ATOM   7330 C  CG  . HIS D  1 120 ? -4.085  5.712   -32.331 1.00 12.43  ? 120 HIS D CG  1 
ATOM   7331 N  ND1 . HIS D  1 120 ? -3.174  4.799   -32.878 1.00 13.01  ? 120 HIS D ND1 1 
ATOM   7332 C  CD2 . HIS D  1 120 ? -5.307  5.184   -32.504 1.00 12.89  ? 120 HIS D CD2 1 
ATOM   7333 C  CE1 . HIS D  1 120 ? -3.881  3.773   -33.349 1.00 13.69  ? 120 HIS D CE1 1 
ATOM   7334 N  NE2 . HIS D  1 120 ? -5.204  3.943   -33.118 1.00 13.21  ? 120 HIS D NE2 1 
ATOM   7335 N  N   . TYR D  1 121 ? -3.545  10.142  -31.351 1.00 13.36  ? 121 TYR D N   1 
ATOM   7336 C  CA  . TYR D  1 121 ? -3.165  11.259  -30.491 1.00 13.64  ? 121 TYR D CA  1 
ATOM   7337 C  C   . TYR D  1 121 ? -4.119  11.229  -29.298 1.00 13.84  ? 121 TYR D C   1 
ATOM   7338 O  O   . TYR D  1 121 ? -5.230  10.711  -29.315 1.00 14.32  ? 121 TYR D O   1 
ATOM   7339 C  CB  . TYR D  1 121 ? -3.307  12.593  -31.234 1.00 13.42  ? 121 TYR D CB  1 
ATOM   7340 C  CG  . TYR D  1 121 ? -4.669  13.049  -31.567 1.00 13.49  ? 121 TYR D CG  1 
ATOM   7341 C  CD1 . TYR D  1 121 ? -5.373  12.558  -32.668 1.00 15.18  ? 121 TYR D CD1 1 
ATOM   7342 C  CD2 . TYR D  1 121 ? -5.263  14.077  -30.775 1.00 14.48  ? 121 TYR D CD2 1 
ATOM   7343 C  CE1 . TYR D  1 121 ? -6.648  12.990  -32.935 1.00 17.60  ? 121 TYR D CE1 1 
ATOM   7344 C  CE2 . TYR D  1 121 ? -6.545  14.524  -31.089 1.00 18.29  ? 121 TYR D CE2 1 
ATOM   7345 C  CZ  . TYR D  1 121 ? -7.264  13.965  -32.146 1.00 21.28  ? 121 TYR D CZ  1 
ATOM   7346 O  OH  . TYR D  1 121 ? -8.532  14.385  -32.371 1.00 26.82  ? 121 TYR D OH  1 
ATOM   7347 N  N   . ASN D  1 122 ? -3.631  11.904  -28.234 1.00 13.89  ? 122 ASN D N   1 
ATOM   7348 C  CA  . ASN D  1 122 ? -4.381  11.967  -26.935 1.00 16.39  ? 122 ASN D CA  1 
ATOM   7349 C  C   . ASN D  1 122 ? -5.500  12.999  -27.074 1.00 15.12  ? 122 ASN D C   1 
ATOM   7350 O  O   . ASN D  1 122 ? -5.246  14.216  -26.848 1.00 16.03  ? 122 ASN D O   1 
ATOM   7351 C  CB  . ASN D  1 122 ? -3.424  12.312  -25.839 1.00 17.68  ? 122 ASN D CB  1 
ATOM   7352 C  CG  . ASN D  1 122 ? -4.068  12.191  -24.461 1.00 17.36  ? 122 ASN D CG  1 
ATOM   7353 O  OD1 . ASN D  1 122 ? -5.291  12.343  -24.298 1.00 18.75  ? 122 ASN D OD1 1 
ATOM   7354 N  ND2 . ASN D  1 122 ? -3.163  11.875  -23.516 1.00 19.52  ? 122 ASN D ND2 1 
ATOM   7355 N  N   . SER D  1 123 ? -6.689  12.534  -27.424 1.00 15.87  ? 123 SER D N   1 
ATOM   7356 C  CA  . SER D  1 123 ? -7.804  13.421  -27.631 1.00 18.81  ? 123 SER D CA  1 
ATOM   7357 C  C   . SER D  1 123 ? -8.484  13.824  -26.347 1.00 18.23  ? 123 SER D C   1 
ATOM   7358 O  O   . SER D  1 123 ? -9.378  14.697  -26.345 1.00 21.27  ? 123 SER D O   1 
ATOM   7359 C  CB  . SER D  1 123 ? -8.790  12.795  -28.652 1.00 17.67  ? 123 SER D CB  1 
ATOM   7360 O  OG  . SER D  1 123 ? -9.160  11.494  -28.319 1.00 18.80  ? 123 SER D OG  1 
ATOM   7361 N  N   . ASP D  1 124 ? -8.098  13.185  -25.225 1.00 20.18  ? 124 ASP D N   1 
ATOM   7362 C  CA  . ASP D  1 124 ? -8.635  13.720  -23.925 1.00 21.52  ? 124 ASP D CA  1 
ATOM   7363 C  C   . ASP D  1 124 ? -7.863  14.993  -23.578 1.00 21.77  ? 124 ASP D C   1 
ATOM   7364 O  O   . ASP D  1 124 ? -8.478  15.862  -22.886 1.00 28.40  ? 124 ASP D O   1 
ATOM   7365 C  CB  . ASP D  1 124 ? -8.195  12.735  -22.781 1.00 22.88  ? 124 ASP D CB  1 
ATOM   7366 C  CG  . ASP D  1 124 ? -9.041  11.502  -22.752 1.00 24.91  ? 124 ASP D CG  1 
ATOM   7367 O  OD1 . ASP D  1 124 ? -10.084 11.433  -23.439 1.00 23.28  ? 124 ASP D OD1 1 
ATOM   7368 O  OD2 . ASP D  1 124 ? -8.707  10.591  -22.004 1.00 25.84  ? 124 ASP D OD2 1 
ATOM   7369 N  N   . LEU D  1 125 ? -6.649  15.139  -23.913 1.00 18.83  ? 125 LEU D N   1 
ATOM   7370 C  CA  . LEU D  1 125 ? -5.838  16.296  -23.562 1.00 19.71  ? 125 LEU D CA  1 
ATOM   7371 C  C   . LEU D  1 125 ? -5.770  17.401  -24.599 1.00 18.15  ? 125 LEU D C   1 
ATOM   7372 O  O   . LEU D  1 125 ? -5.598  18.554  -24.268 1.00 20.58  ? 125 LEU D O   1 
ATOM   7373 C  CB  . LEU D  1 125 ? -4.399  15.980  -23.198 1.00 21.46  ? 125 LEU D CB  1 
ATOM   7374 C  CG  . LEU D  1 125 ? -4.114  15.483  -21.756 1.00 25.35  ? 125 LEU D CG  1 
ATOM   7375 C  CD1 . LEU D  1 125 ? -5.064  14.371  -21.317 1.00 27.19  ? 125 LEU D CD1 1 
ATOM   7376 C  CD2 . LEU D  1 125 ? -2.703  15.074  -21.533 1.00 27.93  ? 125 LEU D CD2 1 
ATOM   7377 N  N   . TYR D  1 126 ? -5.785  16.978  -25.869 1.00 16.20  ? 126 TYR D N   1 
ATOM   7378 C  CA  . TYR D  1 126 ? -5.486  17.848  -26.952 1.00 16.16  ? 126 TYR D CA  1 
ATOM   7379 C  C   . TYR D  1 126 ? -6.532  17.861  -28.038 1.00 17.06  ? 126 TYR D C   1 
ATOM   7380 O  O   . TYR D  1 126 ? -7.238  16.866  -28.309 1.00 17.81  ? 126 TYR D O   1 
ATOM   7381 C  CB  . TYR D  1 126 ? -4.097  17.372  -27.558 1.00 15.81  ? 126 TYR D CB  1 
ATOM   7382 C  CG  . TYR D  1 126 ? -3.000  17.386  -26.527 1.00 16.23  ? 126 TYR D CG  1 
ATOM   7383 C  CD1 . TYR D  1 126 ? -2.613  18.535  -25.853 1.00 18.65  ? 126 TYR D CD1 1 
ATOM   7384 C  CD2 . TYR D  1 126 ? -2.373  16.168  -26.146 1.00 15.64  ? 126 TYR D CD2 1 
ATOM   7385 C  CE1 . TYR D  1 126 ? -1.658  18.485  -24.819 1.00 17.40  ? 126 TYR D CE1 1 
ATOM   7386 C  CE2 . TYR D  1 126 ? -1.446  16.124  -25.141 1.00 16.99  ? 126 TYR D CE2 1 
ATOM   7387 C  CZ  . TYR D  1 126 ? -1.122  17.258  -24.476 1.00 17.19  ? 126 TYR D CZ  1 
ATOM   7388 O  OH  . TYR D  1 126 ? -0.181  17.198  -23.453 1.00 18.19  ? 126 TYR D OH  1 
ATOM   7389 N  N   . PRO D  1 127 ? -6.598  19.044  -28.727 1.00 16.67  ? 127 PRO D N   1 
ATOM   7390 C  CA  . PRO D  1 127 ? -7.703  19.205  -29.651 1.00 18.08  ? 127 PRO D CA  1 
ATOM   7391 C  C   . PRO D  1 127 ? -7.485  18.630  -31.026 1.00 17.76  ? 127 PRO D C   1 
ATOM   7392 O  O   . PRO D  1 127 ? -8.411  18.509  -31.796 1.00 19.37  ? 127 PRO D O   1 
ATOM   7393 C  CB  . PRO D  1 127 ? -7.832  20.741  -29.806 1.00 18.96  ? 127 PRO D CB  1 
ATOM   7394 C  CG  . PRO D  1 127 ? -6.407  21.233  -29.481 1.00 19.66  ? 127 PRO D CG  1 
ATOM   7395 C  CD  . PRO D  1 127 ? -5.887  20.318  -28.420 1.00 18.20  ? 127 PRO D CD  1 
ATOM   7396 N  N   . ASP D  1 128 ? -6.235  18.273  -31.344 1.00 15.59  ? 128 ASP D N   1 
ATOM   7397 C  CA  . ASP D  1 128 ? -5.902  17.735  -32.650 1.00 15.01  ? 128 ASP D CA  1 
ATOM   7398 C  C   . ASP D  1 128 ? -4.528  17.144  -32.572 1.00 15.24  ? 128 ASP D C   1 
ATOM   7399 O  O   . ASP D  1 128 ? -3.744  17.416  -31.648 1.00 15.42  ? 128 ASP D O   1 
ATOM   7400 C  CB  . ASP D  1 128 ? -5.952  18.863  -33.718 1.00 16.84  ? 128 ASP D CB  1 
ATOM   7401 C  CG  . ASP D  1 128 ? -4.928  19.923  -33.449 1.00 16.79  ? 128 ASP D CG  1 
ATOM   7402 O  OD1 . ASP D  1 128 ? -5.211  20.920  -32.695 1.00 18.63  ? 128 ASP D OD1 1 
ATOM   7403 O  OD2 . ASP D  1 128 ? -3.784  19.838  -33.978 1.00 19.44  ? 128 ASP D OD2 1 
ATOM   7404 N  N   . ALA D  1 129 ? -4.196  16.326  -33.600 1.00 15.09  ? 129 ALA D N   1 
ATOM   7405 C  CA  . ALA D  1 129 ? -2.977  15.602  -33.518 1.00 13.80  ? 129 ALA D CA  1 
ATOM   7406 C  C   . ALA D  1 129 ? -1.710  16.434  -33.584 1.00 14.36  ? 129 ALA D C   1 
ATOM   7407 O  O   . ALA D  1 129 ? -0.669  16.158  -32.944 1.00 15.70  ? 129 ALA D O   1 
ATOM   7408 C  CB  . ALA D  1 129 ? -2.962  14.557  -34.635 1.00 18.42  ? 129 ALA D CB  1 
ATOM   7409 N  N   A SER D  1 130 ? -1.773  17.498  -34.415 0.50 15.65  ? 130 SER D N   1 
ATOM   7410 N  N   B SER D  1 130 ? -1.672  17.508  -34.413 0.50 14.47  ? 130 SER D N   1 
ATOM   7411 C  CA  A SER D  1 130 ? -0.641  18.414  -34.565 0.50 16.05  ? 130 SER D CA  1 
ATOM   7412 C  CA  B SER D  1 130 ? -0.445  18.351  -34.480 0.50 15.44  ? 130 SER D CA  1 
ATOM   7413 C  C   A SER D  1 130 ? -0.237  19.012  -33.224 0.50 15.31  ? 130 SER D C   1 
ATOM   7414 C  C   B SER D  1 130 ? -0.163  19.019  -33.148 0.50 14.84  ? 130 SER D C   1 
ATOM   7415 O  O   A SER D  1 130 ? 0.916   18.979  -32.805 0.50 15.73  ? 130 SER D O   1 
ATOM   7416 O  O   B SER D  1 130 ? 0.998   19.075  -32.673 0.50 16.89  ? 130 SER D O   1 
ATOM   7417 C  CB  A SER D  1 130 ? -1.008  19.465  -35.626 0.50 18.21  ? 130 SER D CB  1 
ATOM   7418 C  CB  B SER D  1 130 ? -0.607  19.401  -35.585 0.50 14.20  ? 130 SER D CB  1 
ATOM   7419 O  OG  A SER D  1 130 ? -0.873  18.832  -36.902 0.50 20.78  ? 130 SER D OG  1 
ATOM   7420 O  OG  B SER D  1 130 ? 0.498   20.228  -35.713 0.50 16.90  ? 130 SER D OG  1 
ATOM   7421 N  N   . THR D  1 131 ? -1.233  19.545  -32.558 1.00 16.22  ? 131 THR D N   1 
ATOM   7422 C  CA  . THR D  1 131 ? -1.052  20.159  -31.189 1.00 14.83  ? 131 THR D CA  1 
ATOM   7423 C  C   . THR D  1 131 ? -0.516  19.139  -30.230 1.00 16.61  ? 131 THR D C   1 
ATOM   7424 O  O   . THR D  1 131 ? 0.374   19.458  -29.405 1.00 16.36  ? 131 THR D O   1 
ATOM   7425 C  CB  . THR D  1 131 ? -2.444  20.705  -30.718 1.00 16.92  ? 131 THR D CB  1 
ATOM   7426 O  OG1 . THR D  1 131 ? -2.784  21.748  -31.623 1.00 18.08  ? 131 THR D OG1 1 
ATOM   7427 C  CG2 . THR D  1 131 ? -2.260  21.353  -29.300 1.00 20.97  ? 131 THR D CG2 1 
ATOM   7428 N  N   . ALA D  1 132 ? -1.041  17.914  -30.274 1.00 14.89  ? 132 ALA D N   1 
ATOM   7429 C  CA  . ALA D  1 132 ? -0.611  16.871  -29.360 1.00 15.19  ? 132 ALA D CA  1 
ATOM   7430 C  C   . ALA D  1 132 ? 0.818   16.440  -29.572 1.00 14.50  ? 132 ALA D C   1 
ATOM   7431 O  O   . ALA D  1 132 ? 1.467   15.971  -28.606 1.00 15.80  ? 132 ALA D O   1 
ATOM   7432 C  CB  . ALA D  1 132 ? -1.471  15.629  -29.587 1.00 14.97  ? 132 ALA D CB  1 
ATOM   7433 N  N   . SER D  1 133 ? 1.323   16.556  -30.816 1.00 14.58  ? 133 SER D N   1 
ATOM   7434 C  CA  . SER D  1 133 ? 2.542   15.819  -31.155 1.00 14.42  ? 133 SER D CA  1 
ATOM   7435 C  C   . SER D  1 133 ? 3.761   16.293  -30.414 1.00 15.72  ? 133 SER D C   1 
ATOM   7436 O  O   . SER D  1 133 ? 4.734   15.500  -30.304 1.00 15.37  ? 133 SER D O   1 
ATOM   7437 C  CB  . SER D  1 133 ? 2.791   15.918  -32.655 1.00 16.72  ? 133 SER D CB  1 
ATOM   7438 O  OG  . SER D  1 133 ? 3.116   17.214  -33.031 1.00 18.49  ? 133 SER D OG  1 
ATOM   7439 N  N   . ASN D  1 134 ? 3.801   17.525  -29.938 1.00 15.95  ? 134 ASN D N   1 
ATOM   7440 C  CA  . ASN D  1 134 ? 5.006   17.995  -29.204 1.00 16.73  ? 134 ASN D CA  1 
ATOM   7441 C  C   . ASN D  1 134 ? 4.789   18.141  -27.722 1.00 16.06  ? 134 ASN D C   1 
ATOM   7442 O  O   . ASN D  1 134 ? 5.541   18.811  -27.021 1.00 18.50  ? 134 ASN D O   1 
ATOM   7443 C  CB  . ASN D  1 134 ? 5.747   19.253  -29.765 1.00 21.80  ? 134 ASN D CB  1 
ATOM   7444 C  CG  . ASN D  1 134 ? 4.888   20.487  -29.604 1.00 23.66  ? 134 ASN D CG  1 
ATOM   7445 O  OD1 . ASN D  1 134 ? 3.674   20.350  -29.491 1.00 20.43  ? 134 ASN D OD1 1 
ATOM   7446 N  ND2 . ASN D  1 134 ? 5.518   21.718  -29.554 1.00 24.66  ? 134 ASN D ND2 1 
ATOM   7447 N  N   . LYS D  1 135 ? 3.727   17.529  -27.230 1.00 15.62  ? 135 LYS D N   1 
ATOM   7448 C  CA  . LYS D  1 135 ? 3.325   17.730  -25.798 1.00 17.60  ? 135 LYS D CA  1 
ATOM   7449 C  C   . LYS D  1 135 ? 3.232   16.421  -25.055 1.00 16.05  ? 135 LYS D C   1 
ATOM   7450 O  O   . LYS D  1 135 ? 3.117   15.316  -25.637 1.00 16.63  ? 135 LYS D O   1 
ATOM   7451 C  CB  . LYS D  1 135 ? 1.977   18.487  -25.768 1.00 17.49  ? 135 LYS D CB  1 
ATOM   7452 C  CG  . LYS D  1 135 ? 2.189   19.935  -26.306 1.00 21.05  ? 135 LYS D CG  1 
ATOM   7453 C  CD  . LYS D  1 135 ? 0.889   20.744  -26.310 1.00 20.70  ? 135 LYS D CD  1 
ATOM   7454 C  CE  . LYS D  1 135 ? 1.027   22.036  -27.084 1.00 22.88  ? 135 LYS D CE  1 
ATOM   7455 N  NZ  . LYS D  1 135 ? 1.525   21.897  -28.511 1.00 21.21  ? 135 LYS D NZ  1 
ATOM   7456 N  N   A SER D  1 136 ? 3.279   16.505  -23.713 0.50 17.24  ? 136 SER D N   1 
ATOM   7457 N  N   B SER D  1 136 ? 3.382   16.506  -23.708 0.50 17.42  ? 136 SER D N   1 
ATOM   7458 C  CA  A SER D  1 136 ? 3.366   15.355  -22.882 0.50 17.91  ? 136 SER D CA  1 
ATOM   7459 C  CA  B SER D  1 136 ? 3.352   15.367  -22.814 0.50 16.91  ? 136 SER D CA  1 
ATOM   7460 C  C   A SER D  1 136 ? 2.202   14.369  -23.106 0.50 15.65  ? 136 SER D C   1 
ATOM   7461 C  C   B SER D  1 136 ? 2.239   14.386  -23.133 0.50 15.57  ? 136 SER D C   1 
ATOM   7462 O  O   A SER D  1 136 ? 0.992   14.786  -23.208 0.50 15.02  ? 136 SER D O   1 
ATOM   7463 O  O   B SER D  1 136 ? 1.073   14.842  -23.275 0.50 16.26  ? 136 SER D O   1 
ATOM   7464 C  CB  A SER D  1 136 ? 3.321   15.880  -21.444 0.50 22.16  ? 136 SER D CB  1 
ATOM   7465 C  CB  B SER D  1 136 ? 2.993   15.894  -21.412 0.50 20.31  ? 136 SER D CB  1 
ATOM   7466 O  OG  A SER D  1 136 ? 3.526   14.858  -20.516 0.50 22.75  ? 136 SER D OG  1 
ATOM   7467 O  OG  B SER D  1 136 ? 3.979   16.744  -20.934 0.50 23.12  ? 136 SER D OG  1 
ATOM   7468 N  N   . GLU D  1 137 ? 2.532   13.089  -23.168 1.00 17.65  ? 137 GLU D N   1 
ATOM   7469 C  CA  . GLU D  1 137 ? 1.539   12.099  -23.379 1.00 16.97  ? 137 GLU D CA  1 
ATOM   7470 C  C   . GLU D  1 137 ? 0.791   12.273  -24.727 1.00 15.40  ? 137 GLU D C   1 
ATOM   7471 O  O   . GLU D  1 137 ? -0.315  11.793  -24.836 1.00 16.64  ? 137 GLU D O   1 
ATOM   7472 C  CB  . GLU D  1 137 ? 0.457   12.038  -22.188 1.00 19.14  ? 137 GLU D CB  1 
ATOM   7473 C  CG  . GLU D  1 137 ? 1.068   11.900  -20.836 1.00 23.41  ? 137 GLU D CG  1 
ATOM   7474 C  CD  . GLU D  1 137 ? 1.684   10.462  -20.622 1.00 26.89  ? 137 GLU D CD  1 
ATOM   7475 O  OE1 . GLU D  1 137 ? 1.331   9.507   -21.273 1.00 42.78  ? 137 GLU D OE1 1 
ATOM   7476 O  OE2 . GLU D  1 137 ? 2.464   10.268  -19.701 1.00 39.53  ? 137 GLU D OE2 1 
ATOM   7477 N  N   . GLY D  1 138 ? 1.362   12.961  -25.684 1.00 16.10  ? 138 GLY D N   1 
ATOM   7478 C  CA  . GLY D  1 138 ? 0.517   13.365  -26.823 1.00 14.96  ? 138 GLY D CA  1 
ATOM   7479 C  C   . GLY D  1 138 ? 0.152   12.243  -27.794 1.00 13.28  ? 138 GLY D C   1 
ATOM   7480 O  O   . GLY D  1 138 ? -0.858  12.351  -28.417 1.00 14.13  ? 138 GLY D O   1 
ATOM   7481 N  N   . LEU D  1 139 ? 1.010   11.227  -28.003 1.00 13.42  ? 139 LEU D N   1 
ATOM   7482 C  CA  . LEU D  1 139 ? 0.797   10.303  -29.122 1.00 12.44  ? 139 LEU D CA  1 
ATOM   7483 C  C   . LEU D  1 139 ? 0.914   8.862   -28.611 1.00 12.25  ? 139 LEU D C   1 
ATOM   7484 O  O   . LEU D  1 139 ? 1.651   8.530   -27.635 1.00 13.85  ? 139 LEU D O   1 
ATOM   7485 C  CB  . LEU D  1 139 ? 1.865   10.509  -30.221 1.00 13.14  ? 139 LEU D CB  1 
ATOM   7486 C  CG  . LEU D  1 139 ? 1.860   11.895  -30.899 1.00 13.26  ? 139 LEU D CG  1 
ATOM   7487 C  CD1 . LEU D  1 139 ? 3.055   11.994  -31.792 1.00 14.36  ? 139 LEU D CD1 1 
ATOM   7488 C  CD2 . LEU D  1 139 ? 0.494   12.156  -31.631 1.00 15.47  ? 139 LEU D CD2 1 
ATOM   7489 N  N   . ALA D  1 140 ? 0.245   7.946   -29.335 1.00 12.69  ? 140 ALA D N   1 
ATOM   7490 C  CA  . ALA D  1 140 ? 0.419   6.517   -29.088 1.00 11.98  ? 140 ALA D CA  1 
ATOM   7491 C  C   . ALA D  1 140 ? 0.468   5.885   -30.488 1.00 10.91  ? 140 ALA D C   1 
ATOM   7492 O  O   . ALA D  1 140 ? -0.408  6.153   -31.339 1.00 12.70  ? 140 ALA D O   1 
ATOM   7493 C  CB  . ALA D  1 140 ? -0.749  5.918   -28.303 1.00 14.45  ? 140 ALA D CB  1 
ATOM   7494 N  N   . VAL D  1 141 ? 1.454   5.036   -30.712 1.00 11.08  ? 141 VAL D N   1 
ATOM   7495 C  CA  . VAL D  1 141 ? 1.551   4.371   -32.004 1.00 11.04  ? 141 VAL D CA  1 
ATOM   7496 C  C   . VAL D  1 141 ? 1.419   2.852   -31.819 1.00 10.74  ? 141 VAL D C   1 
ATOM   7497 O  O   . VAL D  1 141 ? 2.028   2.275   -30.882 1.00 12.10  ? 141 VAL D O   1 
ATOM   7498 C  CB  . VAL D  1 141 ? 2.913   4.709   -32.689 1.00 10.46  ? 141 VAL D CB  1 
ATOM   7499 C  CG1 . VAL D  1 141 ? 3.014   3.976   -34.068 1.00 12.16  ? 141 VAL D CG1 1 
ATOM   7500 C  CG2 . VAL D  1 141 ? 2.998   6.190   -32.938 1.00 12.82  ? 141 VAL D CG2 1 
ATOM   7501 N  N   . LEU D  1 142 ? 0.699   2.206   -32.717 1.00 10.17  ? 142 LEU D N   1 
ATOM   7502 C  CA  . LEU D  1 142 ? 0.688   0.761   -32.833 1.00 10.82  ? 142 LEU D CA  1 
ATOM   7503 C  C   . LEU D  1 142 ? 1.620   0.390   -33.957 1.00 10.53  ? 142 LEU D C   1 
ATOM   7504 O  O   . LEU D  1 142 ? 1.471   0.888   -35.080 1.00 11.65  ? 142 LEU D O   1 
ATOM   7505 C  CB  . LEU D  1 142 ? -0.683  0.243   -33.180 1.00 13.01  ? 142 LEU D CB  1 
ATOM   7506 C  CG  . LEU D  1 142 ? -1.812  0.565   -32.192 1.00 12.80  ? 142 LEU D CG  1 
ATOM   7507 C  CD1 . LEU D  1 142 ? -3.128  -0.037  -32.690 1.00 15.04  ? 142 LEU D CD1 1 
ATOM   7508 C  CD2 . LEU D  1 142 ? -1.463  0.181   -30.751 1.00 14.52  ? 142 LEU D CD2 1 
ATOM   7509 N  N   . ALA D  1 143 ? 2.582   -0.475  -33.673 1.00 10.72  ? 143 ALA D N   1 
ATOM   7510 C  CA  . ALA D  1 143 ? 3.569   -0.914  -34.706 1.00 10.15  ? 143 ALA D CA  1 
ATOM   7511 C  C   . ALA D  1 143 ? 3.375   -2.354  -34.983 1.00 9.46   ? 143 ALA D C   1 
ATOM   7512 O  O   . ALA D  1 143 ? 3.337   -3.237  -34.078 1.00 10.77  ? 143 ALA D O   1 
ATOM   7513 C  CB  . ALA D  1 143 ? 4.977   -0.670  -34.135 1.00 11.26  ? 143 ALA D CB  1 
ATOM   7514 N  N   . VAL D  1 144 ? 3.281   -2.656  -36.294 1.00 9.83   ? 144 VAL D N   1 
ATOM   7515 C  CA  . VAL D  1 144 ? 3.153   -4.038  -36.784 1.00 10.11  ? 144 VAL D CA  1 
ATOM   7516 C  C   . VAL D  1 144 ? 4.419   -4.335  -37.583 1.00 9.75   ? 144 VAL D C   1 
ATOM   7517 O  O   . VAL D  1 144 ? 4.711   -3.648  -38.589 1.00 10.90  ? 144 VAL D O   1 
ATOM   7518 C  CB  . VAL D  1 144 ? 1.933   -4.227  -37.641 1.00 11.50  ? 144 VAL D CB  1 
ATOM   7519 C  CG1 . VAL D  1 144 ? 1.827   -5.685  -38.076 1.00 12.60  ? 144 VAL D CG1 1 
ATOM   7520 C  CG2 . VAL D  1 144 ? 0.669   -3.816  -36.889 1.00 12.42  ? 144 VAL D CG2 1 
ATOM   7521 N  N   . LEU D  1 145 ? 5.132   -5.362  -37.201 1.00 10.23  ? 145 LEU D N   1 
ATOM   7522 C  CA  . LEU D  1 145 ? 6.279   -5.860  -37.947 1.00 10.52  ? 145 LEU D CA  1 
ATOM   7523 C  C   . LEU D  1 145 ? 5.828   -6.657  -39.114 1.00 9.96   ? 145 LEU D C   1 
ATOM   7524 O  O   . LEU D  1 145 ? 4.879   -7.447  -38.981 1.00 11.43  ? 145 LEU D O   1 
ATOM   7525 C  CB  . LEU D  1 145 ? 7.155   -6.724  -37.012 1.00 11.51  ? 145 LEU D CB  1 
ATOM   7526 C  CG  . LEU D  1 145 ? 7.673   -5.930  -35.780 1.00 13.89  ? 145 LEU D CG  1 
ATOM   7527 C  CD1 . LEU D  1 145 ? 8.202   -6.956  -34.741 1.00 16.18  ? 145 LEU D CD1 1 
ATOM   7528 C  CD2 . LEU D  1 145 ? 8.809   -4.941  -36.166 1.00 16.50  ? 145 LEU D CD2 1 
ATOM   7529 N  N   . ILE D  1 146 ? 6.461   -6.445  -40.294 1.00 10.36  ? 146 ILE D N   1 
ATOM   7530 C  CA  . ILE D  1 146 ? 6.014   -7.089  -41.519 1.00 10.40  ? 146 ILE D CA  1 
ATOM   7531 C  C   . ILE D  1 146 ? 7.101   -7.944  -42.066 1.00 10.17  ? 146 ILE D C   1 
ATOM   7532 O  O   . ILE D  1 146 ? 8.215   -7.467  -42.334 1.00 11.37  ? 146 ILE D O   1 
ATOM   7533 C  CB  . ILE D  1 146 ? 5.597   -6.015  -42.560 1.00 10.81  ? 146 ILE D CB  1 
ATOM   7534 C  CG1 . ILE D  1 146 ? 4.473   -5.092  -42.027 1.00 11.98  ? 146 ILE D CG1 1 
ATOM   7535 C  CG2 . ILE D  1 146 ? 5.257   -6.663  -43.891 1.00 12.09  ? 146 ILE D CG2 1 
ATOM   7536 C  CD1 . ILE D  1 146 ? 4.167   -3.888  -42.930 1.00 11.90  ? 146 ILE D CD1 1 
ATOM   7537 N  N   A GLU D  1 147 ? 6.924   -9.260  -42.152 0.50 9.52   ? 147 GLU D N   1 
ATOM   7538 N  N   B GLU D  1 147 ? 6.722   -9.182  -42.395 0.50 10.56  ? 147 GLU D N   1 
ATOM   7539 C  CA  A GLU D  1 147 ? 7.940   -10.146 -42.717 0.50 11.70  ? 147 GLU D CA  1 
ATOM   7540 C  CA  B GLU D  1 147 ? 7.601   -10.197 -42.889 0.50 10.53  ? 147 GLU D CA  1 
ATOM   7541 C  C   A GLU D  1 147 ? 7.446   -10.605 -44.148 0.50 10.57  ? 147 GLU D C   1 
ATOM   7542 C  C   B GLU D  1 147 ? 7.321   -10.546 -44.305 0.50 9.98   ? 147 GLU D C   1 
ATOM   7543 O  O   A GLU D  1 147 ? 6.274   -10.686 -44.459 0.50 9.78   ? 147 GLU D O   1 
ATOM   7544 O  O   B GLU D  1 147 ? 6.181   -10.407 -44.803 0.50 11.81  ? 147 GLU D O   1 
ATOM   7545 C  CB  A GLU D  1 147 ? 8.125   -11.391 -41.835 0.50 15.83  ? 147 GLU D CB  1 
ATOM   7546 C  CB  B GLU D  1 147 ? 7.432   -11.477 -41.963 0.50 10.93  ? 147 GLU D CB  1 
ATOM   7547 C  CG  A GLU D  1 147 ? 7.138   -12.547 -42.051 0.50 21.07  ? 147 GLU D CG  1 
ATOM   7548 C  CG  B GLU D  1 147 ? 8.465   -12.552 -42.226 0.50 11.95  ? 147 GLU D CG  1 
ATOM   7549 C  CD  A GLU D  1 147 ? 7.300   -13.680 -41.022 0.50 21.32  ? 147 GLU D CD  1 
ATOM   7550 C  CD  B GLU D  1 147 ? 8.706   -13.530 -41.101 0.50 18.53  ? 147 GLU D CD  1 
ATOM   7551 O  OE1 A GLU D  1 147 ? 8.172   -13.595 -40.126 0.50 22.64  ? 147 GLU D OE1 1 
ATOM   7552 O  OE1 B GLU D  1 147 ? 8.435   -13.262 -39.915 0.50 26.19  ? 147 GLU D OE1 1 
ATOM   7553 O  OE2 A GLU D  1 147 ? 6.551   -14.677 -41.100 0.50 27.42  ? 147 GLU D OE2 1 
ATOM   7554 O  OE2 B GLU D  1 147 ? 9.255   -14.590 -41.431 0.50 27.60  ? 147 GLU D OE2 1 
ATOM   7555 N  N   . MET D  1 148 ? 8.417   -10.849 -45.013 1.00 11.44  ? 148 MET D N   1 
ATOM   7556 C  CA  . MET D  1 148 ? 8.193   -11.342 -46.371 1.00 11.11  ? 148 MET D CA  1 
ATOM   7557 C  C   . MET D  1 148 ? 7.585   -12.743 -46.256 1.00 11.31  ? 148 MET D C   1 
ATOM   7558 O  O   . MET D  1 148 ? 8.200   -13.643 -45.666 1.00 13.10  ? 148 MET D O   1 
ATOM   7559 C  CB  . MET D  1 148 ? 9.499   -11.364 -47.125 1.00 13.20  ? 148 MET D CB  1 
ATOM   7560 C  CG  . MET D  1 148 ? 9.350   -11.777 -48.536 1.00 14.65  ? 148 MET D CG  1 
ATOM   7561 S  SD  . MET D  1 148 ? 10.893  -11.858 -49.486 1.00 16.35  ? 148 MET D SD  1 
ATOM   7562 C  CE  . MET D  1 148 ? 11.361  -10.188 -49.473 1.00 18.17  ? 148 MET D CE  1 
ATOM   7563 N  N   . GLY D  1 149 ? 6.441   -12.945 -46.867 1.00 11.88  ? 149 GLY D N   1 
ATOM   7564 C  CA  . GLY D  1 149 ? 5.694   -14.191 -46.728 1.00 11.93  ? 149 GLY D CA  1 
ATOM   7565 C  C   . GLY D  1 149 ? 4.597   -14.311 -47.756 1.00 11.41  ? 149 GLY D C   1 
ATOM   7566 O  O   . GLY D  1 149 ? 4.816   -14.067 -49.008 1.00 12.25  ? 149 GLY D O   1 
ATOM   7567 N  N   . SER D  1 150 ? 3.390   -14.647 -47.316 1.00 11.88  ? 150 SER D N   1 
ATOM   7568 C  CA  . SER D  1 150 ? 2.245   -14.780 -48.199 1.00 11.62  ? 150 SER D CA  1 
ATOM   7569 C  C   . SER D  1 150 ? 1.678   -13.421 -48.566 1.00 11.68  ? 150 SER D C   1 
ATOM   7570 O  O   . SER D  1 150 ? 1.731   -12.476 -47.835 1.00 13.30  ? 150 SER D O   1 
ATOM   7571 C  CB  . SER D  1 150 ? 1.156   -15.622 -47.541 1.00 13.55  ? 150 SER D CB  1 
ATOM   7572 O  OG  . SER D  1 150 ? 1.598   -16.961 -47.327 1.00 13.49  ? 150 SER D OG  1 
ATOM   7573 N  N   . PHE D  1 151 ? 1.070   -13.411 -49.754 1.00 13.08  ? 151 PHE D N   1 
ATOM   7574 C  CA  . PHE D  1 151 ? 0.253   -12.248 -50.205 1.00 12.60  ? 151 PHE D CA  1 
ATOM   7575 C  C   . PHE D  1 151 ? -0.798  -11.926 -49.182 1.00 11.98  ? 151 PHE D C   1 
ATOM   7576 O  O   . PHE D  1 151 ? -1.475  -12.794 -48.637 1.00 14.24  ? 151 PHE D O   1 
ATOM   7577 C  CB  . PHE D  1 151 ? -0.409  -12.637 -51.506 1.00 13.25  ? 151 PHE D CB  1 
ATOM   7578 C  CG  . PHE D  1 151 ? -1.246  -11.525 -52.074 1.00 13.26  ? 151 PHE D CG  1 
ATOM   7579 C  CD1 . PHE D  1 151 ? -0.665  -10.459 -52.699 1.00 14.54  ? 151 PHE D CD1 1 
ATOM   7580 C  CD2 . PHE D  1 151 ? -2.644  -11.503 -51.901 1.00 15.54  ? 151 PHE D CD2 1 
ATOM   7581 C  CE1 . PHE D  1 151 ? -1.427  -9.353  -53.201 1.00 16.74  ? 151 PHE D CE1 1 
ATOM   7582 C  CE2 . PHE D  1 151 ? -3.415  -10.431 -52.404 1.00 16.51  ? 151 PHE D CE2 1 
ATOM   7583 C  CZ  . PHE D  1 151 ? -2.759  -9.396  -53.065 1.00 16.40  ? 151 PHE D CZ  1 
ATOM   7584 N  N   . ASN D  1 152 ? -0.947  -10.595 -48.930 1.00 12.33  ? 152 ASN D N   1 
ATOM   7585 C  CA  . ASN D  1 152 ? -1.834  -10.138 -47.908 1.00 12.45  ? 152 ASN D CA  1 
ATOM   7586 C  C   . ASN D  1 152 ? -2.892  -9.235  -48.583 1.00 12.41  ? 152 ASN D C   1 
ATOM   7587 O  O   . ASN D  1 152 ? -2.636  -8.096  -48.975 1.00 12.50  ? 152 ASN D O   1 
ATOM   7588 C  CB  . ASN D  1 152 ? -1.042  -9.359  -46.862 1.00 12.26  ? 152 ASN D CB  1 
ATOM   7589 C  CG  . ASN D  1 152 ? -1.837  -9.097  -45.624 1.00 13.03  ? 152 ASN D CG  1 
ATOM   7590 O  OD1 . ASN D  1 152 ? -3.008  -8.584  -45.763 1.00 13.71  ? 152 ASN D OD1 1 
ATOM   7591 N  ND2 . ASN D  1 152 ? -1.311  -9.389  -44.447 1.00 13.09  ? 152 ASN D ND2 1 
ATOM   7592 N  N   . PRO D  1 153 ? -4.144  -9.743  -48.731 1.00 13.47  ? 153 PRO D N   1 
ATOM   7593 C  CA  . PRO D  1 153 ? -5.172  -8.993  -49.430 1.00 15.31  ? 153 PRO D CA  1 
ATOM   7594 C  C   . PRO D  1 153 ? -5.543  -7.696  -48.669 1.00 13.86  ? 153 PRO D C   1 
ATOM   7595 O  O   . PRO D  1 153 ? -5.905  -6.709  -49.371 1.00 16.97  ? 153 PRO D O   1 
ATOM   7596 C  CB  . PRO D  1 153 ? -6.375  -9.917  -49.525 1.00 16.37  ? 153 PRO D CB  1 
ATOM   7597 C  CG  . PRO D  1 153 ? -5.855  -11.257 -49.312 1.00 22.88  ? 153 PRO D CG  1 
ATOM   7598 C  CD  . PRO D  1 153 ? -4.589  -11.116 -48.444 1.00 17.13  ? 153 PRO D CD  1 
ATOM   7599 N  N   . SER D  1 154 ? -5.395  -7.638  -47.374 1.00 14.14  ? 154 SER D N   1 
ATOM   7600 C  CA  . SER D  1 154 ? -5.790  -6.471  -46.637 1.00 15.48  ? 154 SER D CA  1 
ATOM   7601 C  C   . SER D  1 154 ? -4.755  -5.374  -46.836 1.00 14.36  ? 154 SER D C   1 
ATOM   7602 O  O   . SER D  1 154 ? -5.106  -4.206  -47.119 1.00 15.16  ? 154 SER D O   1 
ATOM   7603 C  CB  . SER D  1 154 ? -5.891  -6.865  -45.167 1.00 17.03  ? 154 SER D CB  1 
ATOM   7604 O  OG  . SER D  1 154 ? -6.923  -7.801  -44.994 1.00 20.30  ? 154 SER D OG  1 
ATOM   7605 N  N   . TYR D  1 155 ? -3.427  -5.679  -46.765 1.00 13.40  ? 155 TYR D N   1 
ATOM   7606 C  CA  . TYR D  1 155 ? -2.429  -4.652  -47.131 1.00 13.51  ? 155 TYR D CA  1 
ATOM   7607 C  C   . TYR D  1 155 ? -2.561  -4.192  -48.553 1.00 12.95  ? 155 TYR D C   1 
ATOM   7608 O  O   . TYR D  1 155 ? -2.251  -3.033  -48.889 1.00 13.71  ? 155 TYR D O   1 
ATOM   7609 C  CB  . TYR D  1 155 ? -0.985  -5.073  -46.763 1.00 13.49  ? 155 TYR D CB  1 
ATOM   7610 C  CG  . TYR D  1 155 ? -0.643  -4.972  -45.258 1.00 12.23  ? 155 TYR D CG  1 
ATOM   7611 C  CD1 . TYR D  1 155 ? -1.090  -5.926  -44.338 1.00 12.49  ? 155 TYR D CD1 1 
ATOM   7612 C  CD2 . TYR D  1 155 ? 0.122   -3.880  -44.820 1.00 12.94  ? 155 TYR D CD2 1 
ATOM   7613 C  CE1 . TYR D  1 155 ? -0.797  -5.826  -43.032 1.00 13.07  ? 155 TYR D CE1 1 
ATOM   7614 C  CE2 . TYR D  1 155 ? 0.377   -3.750  -43.505 1.00 13.61  ? 155 TYR D CE2 1 
ATOM   7615 C  CZ  . TYR D  1 155 ? -0.091  -4.701  -42.572 1.00 11.90  ? 155 TYR D CZ  1 
ATOM   7616 O  OH  . TYR D  1 155 ? 0.217   -4.522  -41.244 1.00 13.21  ? 155 TYR D OH  1 
ATOM   7617 N  N   . ASP D  1 156 ? -3.000  -5.075  -49.443 1.00 13.32  ? 156 ASP D N   1 
ATOM   7618 C  CA  . ASP D  1 156 ? -3.190  -4.746  -50.823 1.00 14.79  ? 156 ASP D CA  1 
ATOM   7619 C  C   . ASP D  1 156 ? -4.278  -3.664  -51.025 1.00 14.74  ? 156 ASP D C   1 
ATOM   7620 O  O   . ASP D  1 156 ? -4.241  -2.982  -52.032 1.00 15.38  ? 156 ASP D O   1 
ATOM   7621 C  CB  . ASP D  1 156 ? -3.457  -5.933  -51.738 1.00 15.93  ? 156 ASP D CB  1 
ATOM   7622 C  CG  . ASP D  1 156 ? -2.594  -5.816  -52.989 1.00 18.13  ? 156 ASP D CG  1 
ATOM   7623 O  OD1 . ASP D  1 156 ? -1.282  -5.687  -52.829 1.00 16.60  ? 156 ASP D OD1 1 
ATOM   7624 O  OD2 . ASP D  1 156 ? -3.147  -5.877  -54.065 1.00 19.92  ? 156 ASP D OD2 1 
ATOM   7625 N  N   . LYS D  1 157 ? -5.186  -3.485  -50.035 1.00 14.59  ? 157 LYS D N   1 
ATOM   7626 C  CA  . LYS D  1 157 ? -6.195  -2.453  -50.204 1.00 16.07  ? 157 LYS D CA  1 
ATOM   7627 C  C   . LYS D  1 157 ? -5.466  -1.083  -50.134 1.00 17.86  ? 157 LYS D C   1 
ATOM   7628 O  O   . LYS D  1 157 ? -6.041  -0.088  -50.654 1.00 20.36  ? 157 LYS D O   1 
ATOM   7629 C  CB  . LYS D  1 157 ? -7.207  -2.582  -49.104 1.00 18.25  ? 157 LYS D CB  1 
ATOM   7630 C  CG  . LYS D  1 157 ? -8.060  -3.852  -49.295 1.00 19.66  ? 157 LYS D CG  1 
ATOM   7631 C  CD  . LYS D  1 157 ? -9.007  -4.200  -48.164 1.00 23.63  ? 157 LYS D CD  1 
ATOM   7632 C  CE  . LYS D  1 157 ? -9.797  -5.498  -48.430 1.00 26.02  ? 157 LYS D CE  1 
ATOM   7633 N  NZ  . LYS D  1 157 ? -10.494 -6.067  -47.168 1.00 32.61  ? 157 LYS D NZ  1 
ATOM   7634 N  N   . ILE D  1 158 ? -4.283  -0.976  -49.521 1.00 15.24  ? 158 ILE D N   1 
ATOM   7635 C  CA  . ILE D  1 158 ? -3.443  0.231   -49.572 1.00 15.78  ? 158 ILE D CA  1 
ATOM   7636 C  C   . ILE D  1 158 ? -2.613  0.147   -50.839 1.00 14.14  ? 158 ILE D C   1 
ATOM   7637 O  O   . ILE D  1 158 ? -2.523  1.114   -51.616 1.00 15.13  ? 158 ILE D O   1 
ATOM   7638 C  CB  . ILE D  1 158 ? -2.551  0.338   -48.330 1.00 15.98  ? 158 ILE D CB  1 
ATOM   7639 C  CG1 . ILE D  1 158 ? -3.463  0.561   -47.056 1.00 20.76  ? 158 ILE D CG1 1 
ATOM   7640 C  CG2 . ILE D  1 158 ? -1.537  1.463   -48.438 1.00 16.22  ? 158 ILE D CG2 1 
ATOM   7641 C  CD1 . ILE D  1 158 ? -2.776  0.370   -45.741 1.00 24.53  ? 158 ILE D CD1 1 
ATOM   7642 N  N   . PHE D  1 159 ? -1.816  -0.961  -50.969 1.00 14.41  ? 159 PHE D N   1 
ATOM   7643 C  CA  . PHE D  1 159 ? -0.877  -0.984  -52.025 1.00 14.07  ? 159 PHE D CA  1 
ATOM   7644 C  C   . PHE D  1 159 ? -1.350  -0.838  -53.428 1.00 14.13  ? 159 PHE D C   1 
ATOM   7645 O  O   . PHE D  1 159 ? -0.597  -0.386  -54.313 1.00 15.82  ? 159 PHE D O   1 
ATOM   7646 C  CB  . PHE D  1 159 ? 0.025   -2.250  -51.942 1.00 14.19  ? 159 PHE D CB  1 
ATOM   7647 C  CG  . PHE D  1 159 ? 0.740   -2.469  -50.602 1.00 13.50  ? 159 PHE D CG  1 
ATOM   7648 C  CD1 . PHE D  1 159 ? 1.145   -1.412  -49.756 1.00 16.61  ? 159 PHE D CD1 1 
ATOM   7649 C  CD2 . PHE D  1 159 ? 1.024   -3.767  -50.202 1.00 14.54  ? 159 PHE D CD2 1 
ATOM   7650 C  CE1 . PHE D  1 159 ? 1.806   -1.680  -48.555 1.00 16.65  ? 159 PHE D CE1 1 
ATOM   7651 C  CE2 . PHE D  1 159 ? 1.684   -4.035  -49.016 1.00 15.44  ? 159 PHE D CE2 1 
ATOM   7652 C  CZ  . PHE D  1 159 ? 2.089   -2.994  -48.199 1.00 17.69  ? 159 PHE D CZ  1 
ATOM   7653 N  N   . SER D  1 160 ? -2.586  -1.223  -53.686 1.00 15.58  ? 160 SER D N   1 
ATOM   7654 C  CA  . SER D  1 160 ? -3.108  -1.107  -55.053 1.00 14.89  ? 160 SER D CA  1 
ATOM   7655 C  C   . SER D  1 160 ? -3.192  0.337   -55.486 1.00 16.82  ? 160 SER D C   1 
ATOM   7656 O  O   . SER D  1 160 ? -3.315  0.604   -56.710 1.00 18.89  ? 160 SER D O   1 
ATOM   7657 C  CB  . SER D  1 160 ? -4.477  -1.792  -55.170 1.00 18.91  ? 160 SER D CB  1 
ATOM   7658 O  OG  . SER D  1 160 ? -5.412  -1.127  -54.403 1.00 19.72  ? 160 SER D OG  1 
ATOM   7659 N  N   . HIS D  1 161 ? -3.142  1.294   -54.578 1.00 15.40  ? 161 HIS D N   1 
ATOM   7660 C  CA  . HIS D  1 161 ? -3.289  2.720   -54.938 1.00 15.61  ? 161 HIS D CA  1 
ATOM   7661 C  C   . HIS D  1 161 ? -1.939  3.438   -55.123 1.00 15.13  ? 161 HIS D C   1 
ATOM   7662 O  O   . HIS D  1 161 ? -1.884  4.633   -55.416 1.00 16.70  ? 161 HIS D O   1 
ATOM   7663 C  CB  . HIS D  1 161 ? -4.108  3.470   -53.880 1.00 15.72  ? 161 HIS D CB  1 
ATOM   7664 C  CG  . HIS D  1 161 ? -5.489  2.983   -53.779 1.00 17.84  ? 161 HIS D CG  1 
ATOM   7665 N  ND1 . HIS D  1 161 ? -6.544  3.580   -54.473 1.00 19.36  ? 161 HIS D ND1 1 
ATOM   7666 C  CD2 . HIS D  1 161 ? -6.039  1.971   -53.047 1.00 18.89  ? 161 HIS D CD2 1 
ATOM   7667 C  CE1 . HIS D  1 161 ? -7.654  2.893   -54.246 1.00 22.24  ? 161 HIS D CE1 1 
ATOM   7668 N  NE2 . HIS D  1 161 ? -7.383  1.969   -53.340 1.00 20.22  ? 161 HIS D NE2 1 
ATOM   7669 N  N   . LEU D  1 162 ? -0.825  2.714   -54.920 1.00 16.74  ? 162 LEU D N   1 
ATOM   7670 C  CA  . LEU D  1 162 ? 0.519   3.383   -54.898 1.00 17.65  ? 162 LEU D CA  1 
ATOM   7671 C  C   . LEU D  1 162 ? 0.835   4.111   -56.171 1.00 16.95  ? 162 LEU D C   1 
ATOM   7672 O  O   . LEU D  1 162 ? 1.433   5.177   -56.129 1.00 19.66  ? 162 LEU D O   1 
ATOM   7673 C  CB  . LEU D  1 162 ? 1.642   2.378   -54.532 1.00 19.96  ? 162 LEU D CB  1 
ATOM   7674 C  CG  . LEU D  1 162 ? 1.607   1.761   -53.177 1.00 19.22  ? 162 LEU D CG  1 
ATOM   7675 C  CD1 . LEU D  1 162 ? 2.593   0.551   -53.013 1.00 25.33  ? 162 LEU D CD1 1 
ATOM   7676 C  CD2 . LEU D  1 162 ? 1.833   2.826   -52.162 1.00 25.14  ? 162 LEU D CD2 1 
ATOM   7677 N  N   . GLN D  1 163 ? 0.395   3.606   -57.306 1.00 20.96  ? 163 GLN D N   1 
ATOM   7678 C  CA  . GLN D  1 163 ? 0.693   4.242   -58.583 1.00 24.77  ? 163 GLN D CA  1 
ATOM   7679 C  C   . GLN D  1 163 ? 0.080   5.603   -58.712 1.00 24.25  ? 163 GLN D C   1 
ATOM   7680 O  O   . GLN D  1 163 ? 0.548   6.437   -59.526 1.00 34.88  ? 163 GLN D O   1 
ATOM   7681 C  CB  . GLN D  1 163 ? 0.432   3.343   -59.767 1.00 34.27  ? 163 GLN D CB  1 
ATOM   7682 C  CG  . GLN D  1 163 ? 1.359   2.121   -59.622 1.00 46.27  ? 163 GLN D CG  1 
ATOM   7683 C  CD  . GLN D  1 163 ? 2.897   2.316   -59.380 1.00 51.40  ? 163 GLN D CD  1 
ATOM   7684 O  OE1 . GLN D  1 163 ? 3.494   3.289   -59.844 1.00 96.28  ? 163 GLN D OE1 1 
ATOM   7685 N  NE2 . GLN D  1 163 ? 3.484   1.403   -58.655 1.00 40.75  ? 163 GLN D NE2 1 
ATOM   7686 N  N   . HIS D  1 164 ? -0.909  5.902   -57.923 1.00 19.78  ? 164 HIS D N   1 
ATOM   7687 C  CA  . HIS D  1 164 ? -1.575  7.211   -57.913 1.00 22.53  ? 164 HIS D CA  1 
ATOM   7688 C  C   . HIS D  1 164 ? -1.009  8.262   -56.962 1.00 20.62  ? 164 HIS D C   1 
ATOM   7689 O  O   . HIS D  1 164 ? -1.404  9.459   -56.951 1.00 24.84  ? 164 HIS D O   1 
ATOM   7690 C  CB  . HIS D  1 164 ? -3.060  7.057   -57.686 1.00 22.97  ? 164 HIS D CB  1 
ATOM   7691 C  CG  . HIS D  1 164 ? -3.697  6.087   -58.664 1.00 27.89  ? 164 HIS D CG  1 
ATOM   7692 N  ND1 . HIS D  1 164 ? -3.760  6.311   -60.012 1.00 39.87  ? 164 HIS D ND1 1 
ATOM   7693 C  CD2 . HIS D  1 164 ? -4.098  4.812   -58.480 1.00 36.25  ? 164 HIS D CD2 1 
ATOM   7694 C  CE1 . HIS D  1 164 ? -4.329  5.275   -60.613 1.00 48.69  ? 164 HIS D CE1 1 
ATOM   7695 N  NE2 . HIS D  1 164 ? -4.585  4.360   -59.703 1.00 48.03  ? 164 HIS D NE2 1 
ATOM   7696 N  N   . VAL D  1 165 ? 0.003   7.844   -56.143 1.00 18.07  ? 165 VAL D N   1 
ATOM   7697 C  CA  . VAL D  1 165 ? 0.686   8.763   -55.215 1.00 17.98  ? 165 VAL D CA  1 
ATOM   7698 C  C   . VAL D  1 165 ? 2.202   8.637   -55.376 1.00 16.75  ? 165 VAL D C   1 
ATOM   7699 O  O   . VAL D  1 165 ? 2.957   8.779   -54.436 1.00 16.68  ? 165 VAL D O   1 
ATOM   7700 C  CB  . VAL D  1 165 ? 0.255   8.530   -53.787 1.00 18.22  ? 165 VAL D CB  1 
ATOM   7701 C  CG1 . VAL D  1 165 ? -1.224  8.893   -53.608 1.00 19.62  ? 165 VAL D CG1 1 
ATOM   7702 C  CG2 . VAL D  1 165 ? 0.544   7.099   -53.277 1.00 16.83  ? 165 VAL D CG2 1 
ATOM   7703 N  N   . LYS D  1 166 ? 2.650   8.486   -56.630 1.00 16.09  ? 166 LYS D N   1 
ATOM   7704 C  CA  . LYS D  1 166 ? 4.020   8.288   -56.899 1.00 16.64  ? 166 LYS D CA  1 
ATOM   7705 C  C   . LYS D  1 166 ? 4.988   9.440   -56.455 1.00 16.71  ? 166 LYS D C   1 
ATOM   7706 O  O   . LYS D  1 166 ? 6.110   9.134   -56.082 1.00 17.16  ? 166 LYS D O   1 
ATOM   7707 C  CB  . LYS D  1 166 ? 4.205   8.031   -58.380 1.00 20.92  ? 166 LYS D CB  1 
ATOM   7708 C  CG  . LYS D  1 166 ? 5.552   7.787   -58.847 1.00 25.09  ? 166 LYS D CG  1 
ATOM   7709 C  CD  . LYS D  1 166 ? 5.442   7.214   -60.293 1.00 38.57  ? 166 LYS D CD  1 
ATOM   7710 N  N   . TYR D  1 167 ? 4.532   10.702  -56.504 1.00 16.79  ? 167 TYR D N   1 
ATOM   7711 C  CA  . TYR D  1 167 ? 5.384   11.835  -56.193 1.00 15.46  ? 167 TYR D CA  1 
ATOM   7712 C  C   . TYR D  1 167 ? 4.892   12.628  -54.987 1.00 15.14  ? 167 TYR D C   1 
ATOM   7713 O  O   . TYR D  1 167 ? 3.717   12.598  -54.632 1.00 15.66  ? 167 TYR D O   1 
ATOM   7714 C  CB  . TYR D  1 167 ? 5.496   12.800  -57.380 1.00 16.37  ? 167 TYR D CB  1 
ATOM   7715 C  CG  . TYR D  1 167 ? 6.193   12.113  -58.504 1.00 19.69  ? 167 TYR D CG  1 
ATOM   7716 C  CD1 . TYR D  1 167 ? 7.591   12.008  -58.467 1.00 19.78  ? 167 TYR D CD1 1 
ATOM   7717 C  CD2 . TYR D  1 167 ? 5.465   11.593  -59.558 1.00 20.23  ? 167 TYR D CD2 1 
ATOM   7718 C  CE1 . TYR D  1 167 ? 8.284   11.380  -59.478 1.00 22.18  ? 167 TYR D CE1 1 
ATOM   7719 C  CE2 . TYR D  1 167 ? 6.125   10.992  -60.649 1.00 25.30  ? 167 TYR D CE2 1 
ATOM   7720 C  CZ  . TYR D  1 167 ? 7.511   10.865  -60.552 1.00 20.13  ? 167 TYR D CZ  1 
ATOM   7721 O  OH  . TYR D  1 167 ? 8.172   10.224  -61.589 1.00 28.38  ? 167 TYR D OH  1 
ATOM   7722 N  N   . LYS D  1 168 ? 5.852   13.313  -54.353 1.00 14.91  ? 168 LYS D N   1 
ATOM   7723 C  CA  . LYS D  1 168 ? 5.619   14.071  -53.213 1.00 16.76  ? 168 LYS D CA  1 
ATOM   7724 C  C   . LYS D  1 168 ? 4.464   15.026  -53.471 1.00 16.39  ? 168 LYS D C   1 
ATOM   7725 O  O   . LYS D  1 168 ? 4.373   15.749  -54.489 1.00 18.68  ? 168 LYS D O   1 
ATOM   7726 C  CB  . LYS D  1 168 ? 6.854   14.899  -52.799 1.00 17.92  ? 168 LYS D CB  1 
ATOM   7727 C  CG  . LYS D  1 168 ? 6.586   15.700  -51.510 1.00 19.27  ? 168 LYS D CG  1 
ATOM   7728 C  CD  . LYS D  1 168 ? 7.845   16.296  -50.987 1.00 20.53  ? 168 LYS D CD  1 
ATOM   7729 C  CE  . LYS D  1 168 ? 7.695   17.006  -49.613 1.00 29.40  ? 168 LYS D CE  1 
ATOM   7730 N  NZ  . LYS D  1 168 ? 8.968   17.545  -49.022 1.00 32.99  ? 168 LYS D NZ  1 
ATOM   7731 N  N   . GLY D  1 169 ? 3.465   15.039  -52.530 1.00 17.75  ? 169 GLY D N   1 
ATOM   7732 C  CA  . GLY D  1 169 ? 2.321   15.871  -52.634 1.00 20.78  ? 169 GLY D CA  1 
ATOM   7733 C  C   . GLY D  1 169 ? 1.083   15.295  -53.335 1.00 21.00  ? 169 GLY D C   1 
ATOM   7734 O  O   . GLY D  1 169 ? -0.021  15.797  -53.235 1.00 24.53  ? 169 GLY D O   1 
ATOM   7735 N  N   . GLN D  1 170 ? 1.256   14.224  -54.074 1.00 18.42  ? 170 GLN D N   1 
ATOM   7736 C  CA  . GLN D  1 170 ? 0.143   13.542  -54.707 1.00 17.96  ? 170 GLN D CA  1 
ATOM   7737 C  C   . GLN D  1 170 ? -0.757  12.819  -53.696 1.00 16.26  ? 170 GLN D C   1 
ATOM   7738 O  O   . GLN D  1 170 ? -0.290  12.338  -52.653 1.00 16.88  ? 170 GLN D O   1 
ATOM   7739 C  CB  . GLN D  1 170 ? 0.630   12.624  -55.787 1.00 18.76  ? 170 GLN D CB  1 
ATOM   7740 C  CG  . GLN D  1 170 ? 1.332   13.428  -56.920 1.00 19.48  ? 170 GLN D CG  1 
ATOM   7741 C  CD  . GLN D  1 170 ? 1.688   12.573  -58.108 1.00 20.36  ? 170 GLN D CD  1 
ATOM   7742 O  OE1 . GLN D  1 170 ? 2.074   11.422  -57.981 1.00 20.14  ? 170 GLN D OE1 1 
ATOM   7743 N  NE2 . GLN D  1 170 ? 1.734   13.236  -59.294 1.00 27.09  ? 170 GLN D NE2 1 
ATOM   7744 N  N   . GLU D  1 171 ? -2.021  12.703  -54.085 1.00 18.16  ? 171 GLU D N   1 
ATOM   7745 C  CA  . GLU D  1 171 ? -3.087  12.187  -53.229 1.00 19.81  ? 171 GLU D CA  1 
ATOM   7746 C  C   . GLU D  1 171 ? -3.997  11.274  -53.994 1.00 20.08  ? 171 GLU D C   1 
ATOM   7747 O  O   . GLU D  1 171 ? -4.268  11.572  -55.205 1.00 24.36  ? 171 GLU D O   1 
ATOM   7748 C  CB  . GLU D  1 171 ? -3.883  13.388  -52.690 1.00 27.25  ? 171 GLU D CB  1 
ATOM   7749 C  CG  . GLU D  1 171 ? -3.166  14.250  -51.658 1.00 28.18  ? 171 GLU D CG  1 
ATOM   7750 C  CD  . GLU D  1 171 ? -4.039  15.444  -51.388 1.00 43.18  ? 171 GLU D CD  1 
ATOM   7751 O  OE1 . GLU D  1 171 ? -5.008  15.579  -52.169 1.00 46.45  ? 171 GLU D OE1 1 
ATOM   7752 O  OE2 . GLU D  1 171 ? -3.788  16.149  -50.391 1.00 39.77  ? 171 GLU D OE2 1 
ATOM   7753 N  N   . ALA D  1 172 ? -4.622  10.350  -53.306 1.00 18.86  ? 172 ALA D N   1 
ATOM   7754 C  CA  . ALA D  1 172 ? -5.610  9.478   -53.951 1.00 19.50  ? 172 ALA D CA  1 
ATOM   7755 C  C   . ALA D  1 172 ? -6.585  9.037   -52.826 1.00 17.50  ? 172 ALA D C   1 
ATOM   7756 O  O   . ALA D  1 172 ? -6.225  8.945   -51.692 1.00 18.72  ? 172 ALA D O   1 
ATOM   7757 C  CB  . ALA D  1 172 ? -4.964  8.213   -54.539 1.00 23.52  ? 172 ALA D CB  1 
ATOM   7758 N  N   . PHE D  1 173 ? -7.795  8.692   -53.197 1.00 19.82  ? 173 PHE D N   1 
ATOM   7759 C  CA  . PHE D  1 173 ? -8.777  8.234   -52.193 1.00 17.27  ? 173 PHE D CA  1 
ATOM   7760 C  C   . PHE D  1 173 ? -8.780  6.741   -52.149 1.00 18.92  ? 173 PHE D C   1 
ATOM   7761 O  O   . PHE D  1 173 ? -8.785  6.108   -53.235 1.00 22.96  ? 173 PHE D O   1 
ATOM   7762 C  CB  . PHE D  1 173 ? -10.146 8.830   -52.502 1.00 21.80  ? 173 PHE D CB  1 
ATOM   7763 C  CG  . PHE D  1 173 ? -10.302 10.226  -51.928 1.00 22.94  ? 173 PHE D CG  1 
ATOM   7764 C  CD1 . PHE D  1 173 ? -10.356 10.430  -50.496 1.00 29.61  ? 173 PHE D CD1 1 
ATOM   7765 C  CD2 . PHE D  1 173 ? -10.446 11.351  -52.759 1.00 36.07  ? 173 PHE D CD2 1 
ATOM   7766 C  CE1 . PHE D  1 173 ? -10.567 11.724  -49.932 1.00 33.53  ? 173 PHE D CE1 1 
ATOM   7767 C  CE2 . PHE D  1 173 ? -10.568 12.647  -52.201 1.00 40.22  ? 173 PHE D CE2 1 
ATOM   7768 C  CZ  . PHE D  1 173 ? -10.661 12.840  -50.812 1.00 45.33  ? 173 PHE D CZ  1 
ATOM   7769 N  N   . VAL D  1 174 ? -8.853  6.180   -50.960 1.00 16.00  ? 174 VAL D N   1 
ATOM   7770 C  CA  . VAL D  1 174 ? -8.892  4.765   -50.680 1.00 17.66  ? 174 VAL D CA  1 
ATOM   7771 C  C   . VAL D  1 174 ? -10.301 4.497   -50.068 1.00 15.79  ? 174 VAL D C   1 
ATOM   7772 O  O   . VAL D  1 174 ? -10.600 5.076   -49.043 1.00 16.34  ? 174 VAL D O   1 
ATOM   7773 C  CB  . VAL D  1 174 ? -7.731  4.298   -49.700 1.00 17.05  ? 174 VAL D CB  1 
ATOM   7774 C  CG1 . VAL D  1 174 ? -7.835  2.792   -49.422 1.00 19.17  ? 174 VAL D CG1 1 
ATOM   7775 C  CG2 . VAL D  1 174 ? -6.388  4.610   -50.427 1.00 20.10  ? 174 VAL D CG2 1 
ATOM   7776 N  N   . PRO D  1 175 ? -11.076 3.537   -50.616 1.00 15.94  ? 175 PRO D N   1 
ATOM   7777 C  CA  . PRO D  1 175 ? -12.303 3.167   -49.873 1.00 15.81  ? 175 PRO D CA  1 
ATOM   7778 C  C   . PRO D  1 175 ? -11.954 2.536   -48.503 1.00 15.72  ? 175 PRO D C   1 
ATOM   7779 O  O   . PRO D  1 175 ? -10.986 1.852   -48.320 1.00 16.74  ? 175 PRO D O   1 
ATOM   7780 C  CB  . PRO D  1 175 ? -12.928 2.077   -50.820 1.00 18.58  ? 175 PRO D CB  1 
ATOM   7781 C  CG  . PRO D  1 175 ? -12.342 2.289   -52.190 1.00 23.52  ? 175 PRO D CG  1 
ATOM   7782 C  CD  . PRO D  1 175 ? -10.906 2.729   -51.848 1.00 16.51  ? 175 PRO D CD  1 
ATOM   7783 N  N   . GLY D  1 176 ? -12.850 2.791   -47.530 1.00 16.04  ? 176 GLY D N   1 
ATOM   7784 C  CA  . GLY D  1 176 ? -12.675 2.176   -46.246 1.00 15.47  ? 176 GLY D CA  1 
ATOM   7785 C  C   . GLY D  1 176 ? -12.590 0.685   -46.275 1.00 15.82  ? 176 GLY D C   1 
ATOM   7786 O  O   . GLY D  1 176 ? -13.286 0.017   -47.077 1.00 18.85  ? 176 GLY D O   1 
ATOM   7787 N  N   . PHE D  1 177 ? -11.842 0.184   -45.314 1.00 16.57  ? 177 PHE D N   1 
ATOM   7788 C  CA  . PHE D  1 177 ? -11.808 -1.239  -45.068 1.00 16.82  ? 177 PHE D CA  1 
ATOM   7789 C  C   . PHE D  1 177 ? -11.480 -1.380  -43.575 1.00 15.55  ? 177 PHE D C   1 
ATOM   7790 O  O   . PHE D  1 177 ? -11.250 -0.440  -42.796 1.00 16.93  ? 177 PHE D O   1 
ATOM   7791 C  CB  . PHE D  1 177 ? -10.805 -1.950  -45.971 1.00 17.28  ? 177 PHE D CB  1 
ATOM   7792 C  CG  . PHE D  1 177 ? -9.338  -1.557  -45.730 1.00 17.32  ? 177 PHE D CG  1 
ATOM   7793 C  CD1 . PHE D  1 177 ? -8.799  -0.358  -46.280 1.00 17.33  ? 177 PHE D CD1 1 
ATOM   7794 C  CD2 . PHE D  1 177 ? -8.510  -2.381  -44.935 1.00 19.66  ? 177 PHE D CD2 1 
ATOM   7795 C  CE1 . PHE D  1 177 ? -7.476  -0.060  -46.049 1.00 17.69  ? 177 PHE D CE1 1 
ATOM   7796 C  CE2 . PHE D  1 177 ? -7.142  -2.016  -44.654 1.00 21.89  ? 177 PHE D CE2 1 
ATOM   7797 C  CZ  . PHE D  1 177 ? -6.657  -0.905  -45.303 1.00 19.21  ? 177 PHE D CZ  1 
ATOM   7798 N  N   . ASN D  1 178 ? -11.503 -2.638  -43.135 1.00 18.25  ? 178 ASN D N   1 
ATOM   7799 C  CA  . ASN D  1 178 ? -11.296 -2.934  -41.682 1.00 18.34  ? 178 ASN D CA  1 
ATOM   7800 C  C   . ASN D  1 178 ? -9.786  -2.891  -41.378 1.00 16.39  ? 178 ASN D C   1 
ATOM   7801 O  O   . ASN D  1 178 ? -9.059  -3.807  -41.673 1.00 17.03  ? 178 ASN D O   1 
ATOM   7802 C  CB  . ASN D  1 178 ? -11.949 -4.291  -41.347 1.00 20.66  ? 178 ASN D CB  1 
ATOM   7803 C  CG  . ASN D  1 178 ? -11.864 -4.571  -39.936 1.00 20.01  ? 178 ASN D CG  1 
ATOM   7804 O  OD1 . ASN D  1 178 ? -11.395 -3.702  -39.052 1.00 19.62  ? 178 ASN D OD1 1 
ATOM   7805 N  ND2 . ASN D  1 178 ? -12.258 -5.813  -39.615 1.00 26.33  ? 178 ASN D ND2 1 
ATOM   7806 N  N   . ILE D  1 179 ? -9.367  -1.832  -40.717 1.00 15.29  ? 179 ILE D N   1 
ATOM   7807 C  CA  . ILE D  1 179 ? -7.964  -1.625  -40.406 1.00 14.94  ? 179 ILE D CA  1 
ATOM   7808 C  C   . ILE D  1 179 ? -7.482  -2.693  -39.434 1.00 15.26  ? 179 ILE D C   1 
ATOM   7809 O  O   . ILE D  1 179 ? -6.271  -2.994  -39.360 1.00 15.22  ? 179 ILE D O   1 
ATOM   7810 C  CB  . ILE D  1 179 ? -7.759  -0.152  -39.829 1.00 14.74  ? 179 ILE D CB  1 
ATOM   7811 C  CG1 . ILE D  1 179 ? -8.288  0.879   -40.750 1.00 16.38  ? 179 ILE D CG1 1 
ATOM   7812 C  CG2 . ILE D  1 179 ? -6.311  0.028   -39.430 1.00 15.93  ? 179 ILE D CG2 1 
ATOM   7813 C  CD1 . ILE D  1 179 ? -7.648  0.852   -42.191 1.00 16.77  ? 179 ILE D CD1 1 
ATOM   7814 N  N   . GLU D  1 180 ? -8.391  -3.322  -38.659 1.00 15.41  ? 180 GLU D N   1 
ATOM   7815 C  CA  . GLU D  1 180 ? -7.943  -4.396  -37.814 1.00 16.36  ? 180 GLU D CA  1 
ATOM   7816 C  C   . GLU D  1 180 ? -7.341  -5.572  -38.597 1.00 14.93  ? 180 GLU D C   1 
ATOM   7817 O  O   . GLU D  1 180 ? -6.535  -6.375  -38.016 1.00 16.24  ? 180 GLU D O   1 
ATOM   7818 C  CB  . GLU D  1 180 ? -9.055  -4.917  -36.916 1.00 19.95  ? 180 GLU D CB  1 
ATOM   7819 C  CG  . GLU D  1 180 ? -8.583  -5.626  -35.701 1.00 24.27  ? 180 GLU D CG  1 
ATOM   7820 C  CD  . GLU D  1 180 ? -9.676  -5.779  -34.653 1.00 29.23  ? 180 GLU D CD  1 
ATOM   7821 O  OE1 . GLU D  1 180 ? -10.821 -5.286  -34.773 1.00 33.47  ? 180 GLU D OE1 1 
ATOM   7822 O  OE2 . GLU D  1 180 ? -9.365  -6.380  -33.639 1.00 32.36  ? 180 GLU D OE2 1 
ATOM   7823 N  N   . GLU D  1 181 ? -7.703  -5.680  -39.865 1.00 15.31  ? 181 GLU D N   1 
ATOM   7824 C  CA  . GLU D  1 181 ? -7.130  -6.722  -40.712 1.00 15.24  ? 181 GLU D CA  1 
ATOM   7825 C  C   . GLU D  1 181 ? -5.603  -6.526  -40.967 1.00 14.60  ? 181 GLU D C   1 
ATOM   7826 O  O   . GLU D  1 181 ? -4.974  -7.471  -41.406 1.00 16.24  ? 181 GLU D O   1 
ATOM   7827 C  CB  . GLU D  1 181 ? -7.822  -6.741  -42.066 1.00 17.68  ? 181 GLU D CB  1 
ATOM   7828 C  CG  . GLU D  1 181 ? -9.243  -7.226  -42.029 1.00 20.94  ? 181 GLU D CG  1 
ATOM   7829 C  CD  . GLU D  1 181 ? -9.939  -6.932  -43.401 1.00 25.57  ? 181 GLU D CD  1 
ATOM   7830 O  OE1 . GLU D  1 181 ? -9.241  -6.612  -44.420 1.00 27.19  ? 181 GLU D OE1 1 
ATOM   7831 O  OE2 . GLU D  1 181 ? -11.208 -6.988  -43.522 1.00 26.44  ? 181 GLU D OE2 1 
ATOM   7832 N  N   . LEU D  1 182 ? -5.123  -5.326  -40.670 1.00 13.04  ? 182 LEU D N   1 
ATOM   7833 C  CA  . LEU D  1 182 ? -3.654  -5.085  -40.792 1.00 13.14  ? 182 LEU D CA  1 
ATOM   7834 C  C   . LEU D  1 182 ? -2.907  -5.597  -39.577 1.00 11.94  ? 182 LEU D C   1 
ATOM   7835 O  O   . LEU D  1 182 ? -1.664  -5.588  -39.599 1.00 13.68  ? 182 LEU D O   1 
ATOM   7836 C  CB  . LEU D  1 182 ? -3.402  -3.579  -41.011 1.00 13.51  ? 182 LEU D CB  1 
ATOM   7837 C  CG  . LEU D  1 182 ? -4.107  -2.969  -42.187 1.00 13.14  ? 182 LEU D CG  1 
ATOM   7838 C  CD1 . LEU D  1 182 ? -3.773  -1.483  -42.284 1.00 14.09  ? 182 LEU D CD1 1 
ATOM   7839 C  CD2 . LEU D  1 182 ? -3.815  -3.644  -43.539 1.00 14.18  ? 182 LEU D CD2 1 
ATOM   7840 N  N   . LEU D  1 183 ? -3.582  -5.901  -38.450 1.00 14.46  ? 183 LEU D N   1 
ATOM   7841 C  CA  . LEU D  1 183 ? -2.929  -6.292  -37.218 1.00 14.90  ? 183 LEU D CA  1 
ATOM   7842 C  C   . LEU D  1 183 ? -2.649  -7.764  -37.205 1.00 13.68  ? 183 LEU D C   1 
ATOM   7843 O  O   . LEU D  1 183 ? -3.356  -8.529  -37.882 1.00 15.45  ? 183 LEU D O   1 
ATOM   7844 C  CB  . LEU D  1 183 ? -3.848  -5.928  -36.016 1.00 15.88  ? 183 LEU D CB  1 
ATOM   7845 C  CG  . LEU D  1 183 ? -4.278  -4.409  -35.909 1.00 16.12  ? 183 LEU D CG  1 
ATOM   7846 C  CD1 . LEU D  1 183 ? -5.040  -4.212  -34.589 1.00 21.98  ? 183 LEU D CD1 1 
ATOM   7847 C  CD2 . LEU D  1 183 ? -3.020  -3.508  -35.838 1.00 19.33  ? 183 LEU D CD2 1 
ATOM   7848 N  N   . PRO D  1 184 ? -1.673  -8.192  -36.428 1.00 13.01  ? 184 PRO D N   1 
ATOM   7849 C  CA  . PRO D  1 184 ? -1.311  -9.604  -36.322 1.00 16.49  ? 184 PRO D CA  1 
ATOM   7850 C  C   . PRO D  1 184 ? -2.133  -10.369 -35.386 1.00 16.94  ? 184 PRO D C   1 
ATOM   7851 O  O   . PRO D  1 184 ? -3.066  -9.831  -34.742 1.00 20.26  ? 184 PRO D O   1 
ATOM   7852 C  CB  . PRO D  1 184 ? 0.222   -9.463  -35.828 1.00 15.46  ? 184 PRO D CB  1 
ATOM   7853 C  CG  . PRO D  1 184 ? 0.080   -8.296  -34.925 1.00 14.53  ? 184 PRO D CG  1 
ATOM   7854 C  CD  . PRO D  1 184 ? -0.790  -7.352  -35.633 1.00 14.49  ? 184 PRO D CD  1 
ATOM   7855 N  N   . GLU D  1 185 ? -1.757  -11.697 -35.318 1.00 17.54  ? 185 GLU D N   1 
ATOM   7856 C  CA  . GLU D  1 185 ? -2.405  -12.552 -34.350 1.00 18.57  ? 185 GLU D CA  1 
ATOM   7857 C  C   . GLU D  1 185 ? -1.963  -12.172 -32.947 1.00 19.94  ? 185 GLU D C   1 
ATOM   7858 O  O   . GLU D  1 185 ? -0.885  -11.686 -32.715 1.00 19.39  ? 185 GLU D O   1 
ATOM   7859 C  CB  . GLU D  1 185 ? -1.952  -14.016 -34.609 1.00 21.47  ? 185 GLU D CB  1 
ATOM   7860 C  CG  . GLU D  1 185 ? -2.360  -14.510 -35.974 1.00 26.75  ? 185 GLU D CG  1 
ATOM   7861 N  N   . ARG D  1 186 ? -2.932  -12.456 -31.999 1.00 17.63  ? 186 ARG D N   1 
ATOM   7862 C  CA  . ARG D  1 186 ? -2.578  -12.348 -30.559 1.00 18.71  ? 186 ARG D CA  1 
ATOM   7863 C  C   . ARG D  1 186 ? -2.133  -10.956 -30.239 1.00 17.27  ? 186 ARG D C   1 
ATOM   7864 O  O   . ARG D  1 186 ? -1.037  -10.731 -29.624 1.00 17.54  ? 186 ARG D O   1 
ATOM   7865 C  CB  . ARG D  1 186 ? -1.637  -13.509 -30.131 1.00 21.91  ? 186 ARG D CB  1 
ATOM   7866 C  CG  . ARG D  1 186 ? -2.273  -14.874 -30.325 1.00 26.52  ? 186 ARG D CG  1 
ATOM   7867 C  CD  . ARG D  1 186 ? -1.362  -15.999 -29.878 1.00 35.97  ? 186 ARG D CD  1 
ATOM   7868 N  NE  . ARG D  1 186 ? -0.183  -16.101 -30.844 1.00 36.70  ? 186 ARG D NE  1 
ATOM   7869 C  CZ  . ARG D  1 186 ? -0.218  -16.771 -32.027 1.00 47.45  ? 186 ARG D CZ  1 
ATOM   7870 N  NH1 . ARG D  1 186 ? -1.357  -17.335 -32.458 1.00 46.91  ? 186 ARG D NH1 1 
ATOM   7871 N  NH2 . ARG D  1 186 ? 0.857   -16.807 -32.835 1.00 60.25  ? 186 ARG D NH2 1 
ATOM   7872 N  N   . THR D  1 187 ? -3.012  -9.992  -30.594 1.00 16.65  ? 187 THR D N   1 
ATOM   7873 C  CA  . THR D  1 187 ? -2.674  -8.660  -30.224 1.00 16.74  ? 187 THR D CA  1 
ATOM   7874 C  C   . THR D  1 187 ? -2.453  -8.351  -28.734 1.00 15.91  ? 187 THR D C   1 
ATOM   7875 O  O   . THR D  1 187 ? -1.907  -7.327  -28.379 1.00 17.00  ? 187 THR D O   1 
ATOM   7876 C  CB  . THR D  1 187 ? -3.663  -7.678  -30.858 1.00 15.51  ? 187 THR D CB  1 
ATOM   7877 O  OG1 . THR D  1 187 ? -5.003  -7.953  -30.431 1.00 19.09  ? 187 THR D OG1 1 
ATOM   7878 C  CG2 . THR D  1 187 ? -3.646  -7.699  -32.348 1.00 18.74  ? 187 THR D CG2 1 
ATOM   7879 N  N   . ALA D  1 188 ? -3.006  -9.252  -27.820 1.00 15.68  ? 188 ALA D N   1 
ATOM   7880 C  CA  . ALA D  1 188 ? -2.752  -9.098  -26.396 1.00 17.04  ? 188 ALA D CA  1 
ATOM   7881 C  C   . ALA D  1 188 ? -1.280  -9.253  -26.060 1.00 14.69  ? 188 ALA D C   1 
ATOM   7882 O  O   . ALA D  1 188 ? -0.890  -8.792  -24.993 1.00 16.30  ? 188 ALA D O   1 
ATOM   7883 C  CB  . ALA D  1 188 ? -3.530  -10.156 -25.611 1.00 18.83  ? 188 ALA D CB  1 
ATOM   7884 N  N   . GLU D  1 189 ? -0.465  -9.818  -27.004 1.00 15.95  ? 189 GLU D N   1 
ATOM   7885 C  CA  . GLU D  1 189 ? 0.967   -9.958  -26.730 1.00 15.02  ? 189 GLU D CA  1 
ATOM   7886 C  C   . GLU D  1 189 ? 1.765   -8.813  -27.429 1.00 11.90  ? 189 GLU D C   1 
ATOM   7887 O  O   . GLU D  1 189 ? 1.726   -8.787  -28.714 1.00 13.09  ? 189 GLU D O   1 
ATOM   7888 C  CB  . GLU D  1 189 ? 1.416   -11.281 -27.287 1.00 16.87  ? 189 GLU D CB  1 
ATOM   7889 C  CG  . GLU D  1 189 ? 0.751   -12.455 -26.417 1.00 20.14  ? 189 GLU D CG  1 
ATOM   7890 C  CD  . GLU D  1 189 ? 1.071   -13.823 -26.910 1.00 26.09  ? 189 GLU D CD  1 
ATOM   7891 O  OE1 . GLU D  1 189 ? 2.211   -14.036 -27.329 1.00 25.33  ? 189 GLU D OE1 1 
ATOM   7892 O  OE2 . GLU D  1 189 ? 0.267   -14.764 -26.699 1.00 42.99  ? 189 GLU D OE2 1 
ATOM   7893 N  N   . TYR D  1 190 ? 2.380   -7.978  -26.653 1.00 13.11  ? 190 TYR D N   1 
ATOM   7894 C  CA  . TYR D  1 190 ? 3.055   -6.789  -27.190 1.00 11.56  ? 190 TYR D CA  1 
ATOM   7895 C  C   . TYR D  1 190 ? 4.129   -6.373  -26.307 1.00 12.35  ? 190 TYR D C   1 
ATOM   7896 O  O   . TYR D  1 190 ? 4.185   -6.768  -25.111 1.00 12.98  ? 190 TYR D O   1 
ATOM   7897 C  CB  . TYR D  1 190 ? 2.009   -5.695  -27.476 1.00 13.76  ? 190 TYR D CB  1 
ATOM   7898 C  CG  . TYR D  1 190 ? 1.226   -5.226  -26.208 1.00 12.36  ? 190 TYR D CG  1 
ATOM   7899 C  CD1 . TYR D  1 190 ? 1.798   -4.343  -25.294 1.00 12.67  ? 190 TYR D CD1 1 
ATOM   7900 C  CD2 . TYR D  1 190 ? -0.063  -5.709  -25.992 1.00 14.65  ? 190 TYR D CD2 1 
ATOM   7901 C  CE1 . TYR D  1 190 ? 1.057   -3.881  -24.138 1.00 14.13  ? 190 TYR D CE1 1 
ATOM   7902 C  CE2 . TYR D  1 190 ? -0.777  -5.250  -24.852 1.00 13.59  ? 190 TYR D CE2 1 
ATOM   7903 C  CZ  . TYR D  1 190 ? -0.166  -4.368  -23.984 1.00 14.62  ? 190 TYR D CZ  1 
ATOM   7904 O  OH  . TYR D  1 190 ? -0.942  -3.917  -22.856 1.00 14.85  ? 190 TYR D OH  1 
ATOM   7905 N  N   . TYR D  1 191 ? 5.013   -5.539  -26.896 1.00 11.29  ? 191 TYR D N   1 
ATOM   7906 C  CA  . TYR D  1 191 ? 6.040   -4.765  -26.230 1.00 12.07  ? 191 TYR D CA  1 
ATOM   7907 C  C   . TYR D  1 191 ? 5.514   -3.372  -26.019 1.00 11.65  ? 191 TYR D C   1 
ATOM   7908 O  O   . TYR D  1 191 ? 4.887   -2.819  -26.908 1.00 13.04  ? 191 TYR D O   1 
ATOM   7909 C  CB  . TYR D  1 191 ? 7.288   -4.692  -27.133 1.00 12.08  ? 191 TYR D CB  1 
ATOM   7910 C  CG  . TYR D  1 191 ? 7.825   -6.013  -27.624 1.00 11.88  ? 191 TYR D CG  1 
ATOM   7911 C  CD1 . TYR D  1 191 ? 8.810   -6.717  -26.910 1.00 12.67  ? 191 TYR D CD1 1 
ATOM   7912 C  CD2 . TYR D  1 191 ? 7.448   -6.516  -28.814 1.00 12.60  ? 191 TYR D CD2 1 
ATOM   7913 C  CE1 . TYR D  1 191 ? 9.411   -7.851  -27.420 1.00 13.70  ? 191 TYR D CE1 1 
ATOM   7914 C  CE2 . TYR D  1 191 ? 8.066   -7.707  -29.355 1.00 13.97  ? 191 TYR D CE2 1 
ATOM   7915 C  CZ  . TYR D  1 191 ? 9.028   -8.377  -28.616 1.00 13.30  ? 191 TYR D CZ  1 
ATOM   7916 O  OH  . TYR D  1 191 ? 9.616   -9.492  -29.148 1.00 16.89  ? 191 TYR D OH  1 
ATOM   7917 N  N   . ARG D  1 192 ? 5.859   -2.754  -24.874 1.00 12.41  ? 192 ARG D N   1 
ATOM   7918 C  CA  . ARG D  1 192 ? 5.435   -1.374  -24.550 1.00 12.30  ? 192 ARG D CA  1 
ATOM   7919 C  C   . ARG D  1 192 ? 6.578   -0.597  -24.021 1.00 11.99  ? 192 ARG D C   1 
ATOM   7920 O  O   . ARG D  1 192 ? 7.309   -1.057  -23.115 1.00 13.06  ? 192 ARG D O   1 
ATOM   7921 C  CB  . ARG D  1 192 ? 4.310   -1.489  -23.476 1.00 14.03  ? 192 ARG D CB  1 
ATOM   7922 C  CG  . ARG D  1 192 ? 4.027   -0.167  -22.746 1.00 17.52  ? 192 ARG D CG  1 
ATOM   7923 C  CD  . ARG D  1 192 ? 3.380   0.789   -23.688 1.00 16.77  ? 192 ARG D CD  1 
ATOM   7924 N  NE  . ARG D  1 192 ? 2.202   0.270   -24.438 1.00 16.25  ? 192 ARG D NE  1 
ATOM   7925 C  CZ  . ARG D  1 192 ? 1.027   -0.077  -23.963 1.00 15.52  ? 192 ARG D CZ  1 
ATOM   7926 N  NH1 . ARG D  1 192 ? 0.713   0.096   -22.625 1.00 20.78  ? 192 ARG D NH1 1 
ATOM   7927 N  NH2 . ARG D  1 192 ? 0.084   -0.616  -24.724 1.00 16.83  ? 192 ARG D NH2 1 
ATOM   7928 N  N   . TYR D  1 193 ? 6.838   0.616   -24.567 1.00 12.22  ? 193 TYR D N   1 
ATOM   7929 C  CA  . TYR D  1 193 ? 7.877   1.493   -23.977 1.00 12.42  ? 193 TYR D CA  1 
ATOM   7930 C  C   . TYR D  1 193 ? 7.578   2.918   -24.359 1.00 12.09  ? 193 TYR D C   1 
ATOM   7931 O  O   . TYR D  1 193 ? 6.736   3.210   -25.233 1.00 13.08  ? 193 TYR D O   1 
ATOM   7932 C  CB  . TYR D  1 193 ? 9.279   1.077   -24.455 1.00 12.05  ? 193 TYR D CB  1 
ATOM   7933 C  CG  . TYR D  1 193 ? 9.627   1.437   -25.874 1.00 12.00  ? 193 TYR D CG  1 
ATOM   7934 C  CD1 . TYR D  1 193 ? 9.190   0.635   -26.969 1.00 12.42  ? 193 TYR D CD1 1 
ATOM   7935 C  CD2 . TYR D  1 193 ? 10.393  2.566   -26.106 1.00 13.03  ? 193 TYR D CD2 1 
ATOM   7936 C  CE1 . TYR D  1 193 ? 9.443   1.013   -28.307 1.00 11.32  ? 193 TYR D CE1 1 
ATOM   7937 C  CE2 . TYR D  1 193 ? 10.670  2.954   -27.442 1.00 13.28  ? 193 TYR D CE2 1 
ATOM   7938 C  CZ  . TYR D  1 193 ? 10.202  2.182   -28.487 1.00 11.68  ? 193 TYR D CZ  1 
ATOM   7939 O  OH  . TYR D  1 193 ? 10.530  2.592   -29.767 1.00 11.60  ? 193 TYR D OH  1 
ATOM   7940 N  N   . ARG D  1 194 ? 8.271   3.793   -23.685 1.00 14.03  ? 194 ARG D N   1 
ATOM   7941 C  CA  . ARG D  1 194 ? 8.133   5.269   -23.899 1.00 15.89  ? 194 ARG D CA  1 
ATOM   7942 C  C   . ARG D  1 194 ? 9.236   5.681   -24.852 1.00 13.70  ? 194 ARG D C   1 
ATOM   7943 O  O   . ARG D  1 194 ? 10.425  5.438   -24.648 1.00 14.90  ? 194 ARG D O   1 
ATOM   7944 C  CB  . ARG D  1 194 ? 8.441   6.030   -22.591 1.00 19.64  ? 194 ARG D CB  1 
ATOM   7945 C  CG  . ARG D  1 194 ? 7.380   5.662   -21.551 1.00 28.26  ? 194 ARG D CG  1 
ATOM   7946 C  CD  . ARG D  1 194 ? 6.039   6.255   -21.966 1.00 34.85  ? 194 ARG D CD  1 
ATOM   7947 N  NE  . ARG D  1 194 ? 4.973   6.013   -21.000 1.00 56.57  ? 194 ARG D NE  1 
ATOM   7948 C  CZ  . ARG D  1 194 ? 3.992   6.874   -20.750 1.00 72.65  ? 194 ARG D CZ  1 
ATOM   7949 N  NH1 . ARG D  1 194 ? 3.950   8.035   -21.391 1.00 93.48  ? 194 ARG D NH1 1 
ATOM   7950 N  NH2 . ARG D  1 194 ? 3.052   6.578   -19.863 1.00 58.65  ? 194 ARG D NH2 1 
ATOM   7951 N  N   . GLY D  1 195 ? 8.818   6.358   -25.973 1.00 12.97  ? 195 GLY D N   1 
ATOM   7952 C  CA  . GLY D  1 195 ? 9.791   6.791   -26.938 1.00 13.23  ? 195 GLY D CA  1 
ATOM   7953 C  C   . GLY D  1 195 ? 9.339   8.024   -27.660 1.00 12.62  ? 195 GLY D C   1 
ATOM   7954 O  O   . GLY D  1 195 ? 8.706   8.934   -27.101 1.00 12.78  ? 195 GLY D O   1 
ATOM   7955 N  N   . SER D  1 196 ? 9.687   8.068   -28.974 1.00 11.14  ? 196 SER D N   1 
ATOM   7956 C  CA  . SER D  1 196 ? 9.603   9.306   -29.721 1.00 11.02  ? 196 SER D CA  1 
ATOM   7957 C  C   . SER D  1 196 ? 8.998   9.044   -31.059 1.00 10.98  ? 196 SER D C   1 
ATOM   7958 O  O   . SER D  1 196 ? 8.916   7.883   -31.530 1.00 10.90  ? 196 SER D O   1 
ATOM   7959 C  CB  . SER D  1 196 ? 11.002  9.938   -29.888 1.00 12.44  ? 196 SER D CB  1 
ATOM   7960 O  OG  . SER D  1 196 ? 11.793  9.205   -30.829 1.00 11.68  ? 196 SER D OG  1 
ATOM   7961 N  N   . LEU D  1 197 ? 8.711   10.116  -31.777 1.00 10.94  ? 197 LEU D N   1 
ATOM   7962 C  CA  . LEU D  1 197 ? 8.569   9.986   -33.240 1.00 10.45  ? 197 LEU D CA  1 
ATOM   7963 C  C   . LEU D  1 197 ? 9.900   9.493   -33.793 1.00 10.16  ? 197 LEU D C   1 
ATOM   7964 O  O   . LEU D  1 197 ? 10.986  9.876   -33.373 1.00 10.85  ? 197 LEU D O   1 
ATOM   7965 C  CB  . LEU D  1 197 ? 8.354   11.356  -33.918 1.00 10.81  ? 197 LEU D CB  1 
ATOM   7966 C  CG  . LEU D  1 197 ? 6.947   11.924  -33.843 1.00 12.52  ? 197 LEU D CG  1 
ATOM   7967 C  CD1 . LEU D  1 197 ? 6.661   12.491  -32.437 1.00 16.41  ? 197 LEU D CD1 1 
ATOM   7968 C  CD2 . LEU D  1 197 ? 6.838   13.067  -34.911 1.00 13.81  ? 197 LEU D CD2 1 
ATOM   7969 N  N   . THR D  1 198 ? 9.846   8.591   -34.830 1.00 9.81   ? 198 THR D N   1 
ATOM   7970 C  CA  . THR D  1 198 ? 11.071  8.095   -35.444 1.00 10.10  ? 198 THR D CA  1 
ATOM   7971 C  C   . THR D  1 198 ? 11.524  8.957   -36.600 1.00 9.31   ? 198 THR D C   1 
ATOM   7972 O  O   . THR D  1 198 ? 12.495  8.651   -37.240 1.00 10.09  ? 198 THR D O   1 
ATOM   7973 C  CB  . THR D  1 198 ? 10.924  6.679   -35.962 1.00 9.44   ? 198 THR D CB  1 
ATOM   7974 O  OG1 . THR D  1 198 ? 9.990   6.696   -37.009 1.00 9.67   ? 198 THR D OG1 1 
ATOM   7975 C  CG2 . THR D  1 198 ? 10.457  5.661   -34.853 1.00 10.76  ? 198 THR D CG2 1 
ATOM   7976 N  N   . THR D  1 199 ? 10.766  10.035  -36.863 1.00 10.15  ? 199 THR D N   1 
ATOM   7977 C  CA  . THR D  1 199 ? 11.137  11.025  -37.884 1.00 10.04  ? 199 THR D CA  1 
ATOM   7978 C  C   . THR D  1 199 ? 11.250  12.365  -37.211 1.00 10.95  ? 199 THR D C   1 
ATOM   7979 O  O   . THR D  1 199 ? 10.602  12.574  -36.153 1.00 11.70  ? 199 THR D O   1 
ATOM   7980 C  CB  . THR D  1 199 ? 10.033  11.130  -38.953 1.00 10.85  ? 199 THR D CB  1 
ATOM   7981 O  OG1 . THR D  1 199 ? 8.832   11.644  -38.340 1.00 12.33  ? 199 THR D OG1 1 
ATOM   7982 C  CG2 . THR D  1 199 ? 9.708   9.818   -39.571 1.00 12.05  ? 199 THR D CG2 1 
ATOM   7983 N  N   . PRO D  1 200 ? 11.925  13.365  -37.820 1.00 10.35  ? 200 PRO D N   1 
ATOM   7984 C  CA  . PRO D  1 200 ? 11.827  14.736  -37.327 1.00 11.07  ? 200 PRO D CA  1 
ATOM   7985 C  C   . PRO D  1 200 ? 10.360  15.096  -37.154 1.00 12.01  ? 200 PRO D C   1 
ATOM   7986 O  O   . PRO D  1 200 ? 9.511   14.714  -37.965 1.00 12.75  ? 200 PRO D O   1 
ATOM   7987 C  CB  . PRO D  1 200 ? 12.488  15.535  -38.452 1.00 12.04  ? 200 PRO D CB  1 
ATOM   7988 C  CG  . PRO D  1 200 ? 13.546  14.562  -38.945 1.00 12.07  ? 200 PRO D CG  1 
ATOM   7989 C  CD  . PRO D  1 200 ? 12.808  13.249  -38.984 1.00 11.04  ? 200 PRO D CD  1 
ATOM   7990 N  N   . PRO D  1 201 ? 10.013  15.886  -36.091 1.00 11.99  ? 201 PRO D N   1 
ATOM   7991 C  CA  . PRO D  1 201 ? 10.995  16.516  -35.138 1.00 12.13  ? 201 PRO D CA  1 
ATOM   7992 C  C   . PRO D  1 201 ? 11.394  15.615  -34.018 1.00 11.66  ? 201 PRO D C   1 
ATOM   7993 O  O   . PRO D  1 201 ? 12.032  16.096  -33.068 1.00 13.01  ? 201 PRO D O   1 
ATOM   7994 C  CB  . PRO D  1 201 ? 10.234  17.775  -34.591 1.00 14.69  ? 201 PRO D CB  1 
ATOM   7995 C  CG  . PRO D  1 201 ? 9.007   17.809  -35.310 1.00 21.86  ? 201 PRO D CG  1 
ATOM   7996 C  CD  . PRO D  1 201 ? 8.703   16.472  -35.984 1.00 14.30  ? 201 PRO D CD  1 
ATOM   7997 N  N   . CYS D  1 202 ? 11.075  14.307  -34.005 1.00 11.86  ? 202 CYS D N   1 
ATOM   7998 C  CA  . CYS D  1 202 ? 11.630  13.332  -33.040 1.00 11.70  ? 202 CYS D CA  1 
ATOM   7999 C  C   . CYS D  1 202 ? 11.114  13.620  -31.602 1.00 12.14  ? 202 CYS D C   1 
ATOM   8000 O  O   . CYS D  1 202 ? 11.808  13.230  -30.643 1.00 13.55  ? 202 CYS D O   1 
ATOM   8001 C  CB  . CYS D  1 202 ? 13.142  13.229  -33.026 1.00 13.35  ? 202 CYS D CB  1 
ATOM   8002 S  SG  . CYS D  1 202 ? 13.887  12.899  -34.613 1.00 12.11  ? 202 CYS D SG  1 
ATOM   8003 N  N   . ASN D  1 203 ? 9.941   14.257  -31.463 1.00 12.46  ? 203 ASN D N   1 
ATOM   8004 C  CA  . ASN D  1 203 ? 9.482   14.591  -30.088 1.00 13.90  ? 203 ASN D CA  1 
ATOM   8005 C  C   . ASN D  1 203 ? 9.372   13.336  -29.252 1.00 12.45  ? 203 ASN D C   1 
ATOM   8006 O  O   . ASN D  1 203 ? 8.829   12.323  -29.718 1.00 12.46  ? 203 ASN D O   1 
ATOM   8007 C  CB  . ASN D  1 203 ? 8.135   15.302  -30.168 1.00 15.63  ? 203 ASN D CB  1 
ATOM   8008 C  CG  . ASN D  1 203 ? 8.170   16.457  -31.172 1.00 17.49  ? 203 ASN D CG  1 
ATOM   8009 O  OD1 . ASN D  1 203 ? 8.071   16.204  -32.353 1.00 22.72  ? 203 ASN D OD1 1 
ATOM   8010 N  ND2 . ASN D  1 203 ? 8.451   17.570  -30.745 1.00 21.81  ? 203 ASN D ND2 1 
ATOM   8011 N  N   . PRO D  1 204 ? 9.810   13.379  -27.972 1.00 13.07  ? 204 PRO D N   1 
ATOM   8012 C  CA  . PRO D  1 204 ? 9.737   12.172  -27.112 1.00 12.46  ? 204 PRO D CA  1 
ATOM   8013 C  C   . PRO D  1 204 ? 8.353   12.084  -26.466 1.00 12.89  ? 204 PRO D C   1 
ATOM   8014 O  O   . PRO D  1 204 ? 8.233   12.080  -25.213 1.00 15.80  ? 204 PRO D O   1 
ATOM   8015 C  CB  . PRO D  1 204 ? 10.861  12.443  -26.096 1.00 14.92  ? 204 PRO D CB  1 
ATOM   8016 C  CG  . PRO D  1 204 ? 10.861  13.937  -25.944 1.00 16.02  ? 204 PRO D CG  1 
ATOM   8017 C  CD  . PRO D  1 204 ? 10.672  14.454  -27.392 1.00 16.15  ? 204 PRO D CD  1 
ATOM   8018 N  N   . THR D  1 205 ? 7.310   11.944  -27.258 1.00 12.12  ? 205 THR D N   1 
ATOM   8019 C  CA  . THR D  1 205 ? 5.956   12.110  -26.856 1.00 13.25  ? 205 THR D CA  1 
ATOM   8020 C  C   . THR D  1 205 ? 5.093   10.877  -27.215 1.00 12.60  ? 205 THR D C   1 
ATOM   8021 O  O   . THR D  1 205 ? 3.868   10.926  -27.167 1.00 13.51  ? 205 THR D O   1 
ATOM   8022 C  CB  . THR D  1 205 ? 5.332   13.367  -27.448 1.00 14.25  ? 205 THR D CB  1 
ATOM   8023 O  OG1 . THR D  1 205 ? 5.524   13.145  -28.871 1.00 14.45  ? 205 THR D OG1 1 
ATOM   8024 C  CG2 . THR D  1 205 ? 6.113   14.644  -26.915 1.00 15.46  ? 205 THR D CG2 1 
ATOM   8025 N  N   . VAL D  1 206 ? 5.750   9.763   -27.553 1.00 12.53  ? 206 VAL D N   1 
ATOM   8026 C  CA  . VAL D  1 206 ? 5.029   8.613   -28.069 1.00 12.30  ? 206 VAL D CA  1 
ATOM   8027 C  C   . VAL D  1 206 ? 5.067   7.396   -27.067 1.00 12.50  ? 206 VAL D C   1 
ATOM   8028 O  O   . VAL D  1 206 ? 6.126   6.966   -26.658 1.00 13.85  ? 206 VAL D O   1 
ATOM   8029 C  CB  . VAL D  1 206 ? 5.641   8.114   -29.410 1.00 12.35  ? 206 VAL D CB  1 
ATOM   8030 C  CG1 . VAL D  1 206 ? 4.909   6.854   -29.904 1.00 12.70  ? 206 VAL D CG1 1 
ATOM   8031 C  CG2 . VAL D  1 206 ? 5.603   9.209   -30.474 1.00 12.30  ? 206 VAL D CG2 1 
ATOM   8032 N  N   . LEU D  1 207 ? 3.886   6.900   -26.786 1.00 11.66  ? 207 LEU D N   1 
ATOM   8033 C  CA  . LEU D  1 207 ? 3.742   5.635   -26.120 1.00 12.82  ? 207 LEU D CA  1 
ATOM   8034 C  C   . LEU D  1 207 ? 3.713   4.545   -27.200 1.00 12.15  ? 207 LEU D C   1 
ATOM   8035 O  O   . LEU D  1 207 ? 2.726   4.468   -28.000 1.00 12.63  ? 207 LEU D O   1 
ATOM   8036 C  CB  . LEU D  1 207 ? 2.392   5.643   -25.374 1.00 16.94  ? 207 LEU D CB  1 
ATOM   8037 C  CG  . LEU D  1 207 ? 2.332   4.434   -24.388 1.00 20.49  ? 207 LEU D CG  1 
ATOM   8038 C  CD1 . LEU D  1 207 ? 3.566   4.300   -23.343 1.00 23.93  ? 207 LEU D CD1 1 
ATOM   8039 C  CD2 . LEU D  1 207 ? 0.993   4.585   -23.715 1.00 34.92  ? 207 LEU D CD2 1 
ATOM   8040 N  N   . TRP D  1 208 ? 4.749   3.725   -27.247 1.00 12.06  ? 208 TRP D N   1 
ATOM   8041 C  CA  . TRP D  1 208 ? 4.844   2.660   -28.322 1.00 12.04  ? 208 TRP D CA  1 
ATOM   8042 C  C   . TRP D  1 208 ? 4.286   1.351   -27.852 1.00 11.38  ? 208 TRP D C   1 
ATOM   8043 O  O   . TRP D  1 208 ? 4.547   0.905   -26.737 1.00 13.26  ? 208 TRP D O   1 
ATOM   8044 C  CB  . TRP D  1 208 ? 6.369   2.470   -28.663 1.00 11.86  ? 208 TRP D CB  1 
ATOM   8045 C  CG  . TRP D  1 208 ? 6.874   3.510   -29.565 1.00 11.14  ? 208 TRP D CG  1 
ATOM   8046 C  CD1 . TRP D  1 208 ? 7.522   4.691   -29.218 1.00 11.43  ? 208 TRP D CD1 1 
ATOM   8047 C  CD2 . TRP D  1 208 ? 6.699   3.539   -30.984 1.00 10.90  ? 208 TRP D CD2 1 
ATOM   8048 N  NE1 . TRP D  1 208 ? 7.784   5.436   -30.347 1.00 11.21  ? 208 TRP D NE1 1 
ATOM   8049 C  CE2 . TRP D  1 208 ? 7.284   4.753   -31.446 1.00 10.57  ? 208 TRP D CE2 1 
ATOM   8050 C  CE3 . TRP D  1 208 ? 6.117   2.659   -31.919 1.00 10.52  ? 208 TRP D CE3 1 
ATOM   8051 C  CZ2 . TRP D  1 208 ? 7.260   5.125   -32.802 1.00 11.17  ? 208 TRP D CZ2 1 
ATOM   8052 C  CZ3 . TRP D  1 208 ? 6.167   3.031   -33.277 1.00 10.29  ? 208 TRP D CZ3 1 
ATOM   8053 C  CH2 . TRP D  1 208 ? 6.675   4.219   -33.691 1.00 10.50  ? 208 TRP D CH2 1 
ATOM   8054 N  N   . THR D  1 209 ? 3.512   0.732   -28.748 1.00 10.70  ? 209 THR D N   1 
ATOM   8055 C  CA  . THR D  1 209 ? 3.075   -0.635  -28.619 1.00 10.85  ? 209 THR D CA  1 
ATOM   8056 C  C   . THR D  1 209 ? 3.540   -1.389  -29.882 1.00 10.47  ? 209 THR D C   1 
ATOM   8057 O  O   . THR D  1 209 ? 3.066   -1.033  -30.954 1.00 12.12  ? 209 THR D O   1 
ATOM   8058 C  CB  . THR D  1 209 ? 1.532   -0.685  -28.448 1.00 11.55  ? 209 THR D CB  1 
ATOM   8059 O  OG1 . THR D  1 209 ? 1.166   0.033   -27.285 1.00 12.97  ? 209 THR D OG1 1 
ATOM   8060 C  CG2 . THR D  1 209 ? 1.056   -2.133  -28.332 1.00 13.83  ? 209 THR D CG2 1 
ATOM   8061 N  N   . VAL D  1 210 ? 4.397   -2.359  -29.734 1.00 10.73  ? 210 VAL D N   1 
ATOM   8062 C  CA  . VAL D  1 210 ? 4.890   -3.125  -30.868 1.00 10.73  ? 210 VAL D CA  1 
ATOM   8063 C  C   . VAL D  1 210 ? 4.353   -4.542  -30.688 1.00 10.64  ? 210 VAL D C   1 
ATOM   8064 O  O   . VAL D  1 210 ? 4.618   -5.173  -29.676 1.00 11.54  ? 210 VAL D O   1 
ATOM   8065 C  CB  . VAL D  1 210 ? 6.441   -3.152  -30.952 1.00 10.97  ? 210 VAL D CB  1 
ATOM   8066 C  CG1 . VAL D  1 210 ? 6.861   -3.969  -32.178 1.00 12.21  ? 210 VAL D CG1 1 
ATOM   8067 C  CG2 . VAL D  1 210 ? 7.062   -1.744  -30.922 1.00 11.77  ? 210 VAL D CG2 1 
ATOM   8068 N  N   . PHE D  1 211 ? 3.526   -4.991  -31.582 1.00 10.35  ? 211 PHE D N   1 
ATOM   8069 C  CA  . PHE D  1 211 ? 2.957   -6.296  -31.367 1.00 11.17  ? 211 PHE D CA  1 
ATOM   8070 C  C   . PHE D  1 211 ? 4.054   -7.384  -31.482 1.00 11.83  ? 211 PHE D C   1 
ATOM   8071 O  O   . PHE D  1 211 ? 4.979   -7.291  -32.286 1.00 12.55  ? 211 PHE D O   1 
ATOM   8072 C  CB  . PHE D  1 211 ? 1.830   -6.581  -32.367 1.00 12.10  ? 211 PHE D CB  1 
ATOM   8073 C  CG  . PHE D  1 211 ? 0.634   -5.694  -32.137 1.00 12.05  ? 211 PHE D CG  1 
ATOM   8074 C  CD1 . PHE D  1 211 ? -0.157  -5.848  -30.967 1.00 13.58  ? 211 PHE D CD1 1 
ATOM   8075 C  CD2 . PHE D  1 211 ? 0.323   -4.632  -32.968 1.00 13.46  ? 211 PHE D CD2 1 
ATOM   8076 C  CE1 . PHE D  1 211 ? -1.216  -5.012  -30.749 1.00 15.08  ? 211 PHE D CE1 1 
ATOM   8077 C  CE2 . PHE D  1 211 ? -0.723  -3.790  -32.740 1.00 14.90  ? 211 PHE D CE2 1 
ATOM   8078 C  CZ  . PHE D  1 211 ? -1.498  -3.940  -31.623 1.00 16.67  ? 211 PHE D CZ  1 
ATOM   8079 N  N   . ARG D  1 212 ? 3.900   -8.463  -30.671 1.00 11.87  ? 212 ARG D N   1 
ATOM   8080 C  CA  . ARG D  1 212 ? 4.891   -9.468  -30.708 1.00 12.89  ? 212 ARG D CA  1 
ATOM   8081 C  C   . ARG D  1 212 ? 4.963   -10.268 -32.009 1.00 12.47  ? 212 ARG D C   1 
ATOM   8082 O  O   . ARG D  1 212 ? 6.066   -10.614 -32.473 1.00 14.05  ? 212 ARG D O   1 
ATOM   8083 C  CB  . ARG D  1 212 ? 4.533   -10.500 -29.554 1.00 14.26  ? 212 ARG D CB  1 
ATOM   8084 C  CG  . ARG D  1 212 ? 5.643   -11.580 -29.428 1.00 15.31  ? 212 ARG D CG  1 
ATOM   8085 C  CD  . ARG D  1 212 ? 5.171   -12.596 -28.433 1.00 16.10  ? 212 ARG D CD  1 
ATOM   8086 N  NE  . ARG D  1 212 ? 6.238   -13.533 -28.153 1.00 18.54  ? 212 ARG D NE  1 
ATOM   8087 C  CZ  . ARG D  1 212 ? 6.158   -14.526 -27.284 1.00 22.27  ? 212 ARG D CZ  1 
ATOM   8088 N  NH1 . ARG D  1 212 ? 5.021   -14.773 -26.643 1.00 23.44  ? 212 ARG D NH1 1 
ATOM   8089 N  NH2 . ARG D  1 212 ? 7.244   -15.258 -27.055 1.00 25.88  ? 212 ARG D NH2 1 
ATOM   8090 N  N   . ASN D  1 213 ? 3.825   -10.493 -32.634 1.00 12.20  ? 213 ASN D N   1 
ATOM   8091 C  CA  . ASN D  1 213 ? 3.784   -11.311 -33.807 1.00 12.63  ? 213 ASN D CA  1 
ATOM   8092 C  C   . ASN D  1 213 ? 3.794   -10.430 -35.095 1.00 12.75  ? 213 ASN D C   1 
ATOM   8093 O  O   . ASN D  1 213 ? 3.046   -9.445  -35.146 1.00 13.00  ? 213 ASN D O   1 
ATOM   8094 C  CB  . ASN D  1 213 ? 2.556   -12.194 -33.774 1.00 14.65  ? 213 ASN D CB  1 
ATOM   8095 C  CG  . ASN D  1 213 ? 2.623   -13.169 -32.686 1.00 18.49  ? 213 ASN D CG  1 
ATOM   8096 O  OD1 . ASN D  1 213 ? 3.618   -13.832 -32.491 1.00 24.83  ? 213 ASN D OD1 1 
ATOM   8097 N  ND2 . ASN D  1 213 ? 1.597   -13.179 -31.902 1.00 23.76  ? 213 ASN D ND2 1 
ATOM   8098 N  N   . PRO D  1 214 ? 4.550   -10.809 -36.115 1.00 13.20  ? 214 PRO D N   1 
ATOM   8099 C  CA  . PRO D  1 214 ? 4.506   -10.100 -37.370 1.00 12.45  ? 214 PRO D CA  1 
ATOM   8100 C  C   . PRO D  1 214 ? 3.304   -10.495 -38.200 1.00 11.99  ? 214 PRO D C   1 
ATOM   8101 O  O   . PRO D  1 214 ? 2.676   -11.553 -37.974 1.00 14.14  ? 214 PRO D O   1 
ATOM   8102 C  CB  . PRO D  1 214 ? 5.828   -10.496 -38.060 1.00 13.47  ? 214 PRO D CB  1 
ATOM   8103 C  CG  . PRO D  1 214 ? 6.019   -11.913 -37.558 1.00 16.61  ? 214 PRO D CG  1 
ATOM   8104 C  CD  . PRO D  1 214 ? 5.545   -11.917 -36.094 1.00 15.64  ? 214 PRO D CD  1 
ATOM   8105 N  N   . VAL D  1 215 ? 3.038   -9.697  -39.241 1.00 11.83  ? 215 VAL D N   1 
ATOM   8106 C  CA  . VAL D  1 215 ? 2.208   -10.113 -40.352 1.00 11.60  ? 215 VAL D CA  1 
ATOM   8107 C  C   . VAL D  1 215 ? 3.060   -10.420 -41.522 1.00 11.36  ? 215 VAL D C   1 
ATOM   8108 O  O   . VAL D  1 215 ? 4.262   -10.153 -41.496 1.00 12.96  ? 215 VAL D O   1 
ATOM   8109 C  CB  . VAL D  1 215 ? 1.136   -9.031  -40.733 1.00 11.51  ? 215 VAL D CB  1 
ATOM   8110 C  CG1 . VAL D  1 215 ? 0.206   -8.730  -39.584 1.00 14.68  ? 215 VAL D CG1 1 
ATOM   8111 C  CG2 . VAL D  1 215 ? 1.811   -7.801  -41.251 1.00 12.59  ? 215 VAL D CG2 1 
ATOM   8112 N  N   . GLN D  1 216 ? 2.495   -10.995 -42.578 1.00 11.33  ? 216 GLN D N   1 
ATOM   8113 C  CA  . GLN D  1 216 ? 3.236   -11.276 -43.808 1.00 10.94  ? 216 GLN D CA  1 
ATOM   8114 C  C   . GLN D  1 216 ? 2.639   -10.472 -44.946 1.00 11.39  ? 216 GLN D C   1 
ATOM   8115 O  O   . GLN D  1 216 ? 1.406   -10.358 -45.051 1.00 12.53  ? 216 GLN D O   1 
ATOM   8116 C  CB  . GLN D  1 216 ? 3.159   -12.737 -44.202 1.00 12.63  ? 216 GLN D CB  1 
ATOM   8117 C  CG  . GLN D  1 216 ? 3.929   -13.631 -43.195 1.00 13.76  ? 216 GLN D CG  1 
ATOM   8118 C  CD  . GLN D  1 216 ? 3.990   -15.081 -43.634 1.00 15.46  ? 216 GLN D CD  1 
ATOM   8119 O  OE1 . GLN D  1 216 ? 3.409   -15.534 -44.661 1.00 14.39  ? 216 GLN D OE1 1 
ATOM   8120 N  NE2 . GLN D  1 216 ? 4.592   -15.857 -42.794 1.00 20.39  ? 216 GLN D NE2 1 
ATOM   8121 N  N   . ILE D  1 217 ? 3.484   -10.021 -45.860 1.00 10.65  ? 217 ILE D N   1 
ATOM   8122 C  CA  . ILE D  1 217 ? 3.092   -9.575  -47.204 1.00 11.16  ? 217 ILE D CA  1 
ATOM   8123 C  C   . ILE D  1 217 ? 4.053   -10.246 -48.189 1.00 10.44  ? 217 ILE D C   1 
ATOM   8124 O  O   . ILE D  1 217 ? 5.131   -10.693 -47.805 1.00 11.49  ? 217 ILE D O   1 
ATOM   8125 C  CB  . ILE D  1 217 ? 3.085   -8.004  -47.353 1.00 11.42  ? 217 ILE D CB  1 
ATOM   8126 C  CG1 . ILE D  1 217 ? 4.509   -7.434  -47.408 1.00 12.15  ? 217 ILE D CG1 1 
ATOM   8127 C  CG2 . ILE D  1 217 ? 2.184   -7.381  -46.318 1.00 13.20  ? 217 ILE D CG2 1 
ATOM   8128 C  CD1 . ILE D  1 217 ? 4.546   -5.944  -47.563 1.00 14.35  ? 217 ILE D CD1 1 
ATOM   8129 N  N   . SER D  1 218 ? 3.684   -10.333 -49.451 1.00 10.87  ? 218 SER D N   1 
ATOM   8130 C  CA  . SER D  1 218 ? 4.518   -11.086 -50.371 1.00 10.98  ? 218 SER D CA  1 
ATOM   8131 C  C   . SER D  1 218 ? 5.708   -10.297 -50.846 1.00 11.35  ? 218 SER D C   1 
ATOM   8132 O  O   . SER D  1 218 ? 5.747   -9.076  -50.805 1.00 11.69  ? 218 SER D O   1 
ATOM   8133 C  CB  . SER D  1 218 ? 3.726   -11.592 -51.536 1.00 12.21  ? 218 SER D CB  1 
ATOM   8134 O  OG  . SER D  1 218 ? 3.325   -10.520 -52.373 1.00 12.65  ? 218 SER D OG  1 
ATOM   8135 N  N   . GLN D  1 219 ? 6.674   -11.020 -51.451 1.00 12.49  ? 219 GLN D N   1 
ATOM   8136 C  CA  . GLN D  1 219 ? 7.760   -10.400 -52.118 1.00 13.69  ? 219 GLN D CA  1 
ATOM   8137 C  C   . GLN D  1 219 ? 7.268   -9.411  -53.174 1.00 11.96  ? 219 GLN D C   1 
ATOM   8138 O  O   . GLN D  1 219 ? 7.833   -8.329  -53.344 1.00 13.37  ? 219 GLN D O   1 
ATOM   8139 C  CB  . GLN D  1 219 ? 8.661   -11.476 -52.730 1.00 17.45  ? 219 GLN D CB  1 
ATOM   8140 C  CG  . GLN D  1 219 ? 9.999   -10.836 -53.237 1.00 19.97  ? 219 GLN D CG  1 
ATOM   8141 C  CD  . GLN D  1 219 ? 9.945   -10.182 -54.499 1.00 23.36  ? 219 GLN D CD  1 
ATOM   8142 O  OE1 . GLN D  1 219 ? 10.719  -9.121  -54.668 1.00 30.41  ? 219 GLN D OE1 1 
ATOM   8143 N  NE2 . GLN D  1 219 ? 9.125   -10.676 -55.421 1.00 27.94  ? 219 GLN D NE2 1 
ATOM   8144 N  N   . GLU D  1 220 ? 6.261   -9.816  -53.944 1.00 13.08  ? 220 GLU D N   1 
ATOM   8145 C  CA  . GLU D  1 220 ? 5.722   -8.932  -55.034 1.00 12.77  ? 220 GLU D CA  1 
ATOM   8146 C  C   . GLU D  1 220 ? 5.173   -7.677  -54.385 1.00 12.07  ? 220 GLU D C   1 
ATOM   8147 O  O   . GLU D  1 220 ? 5.334   -6.574  -54.944 1.00 12.81  ? 220 GLU D O   1 
ATOM   8148 C  CB  . GLU D  1 220 ? 4.688   -9.654  -55.859 1.00 15.56  ? 220 GLU D CB  1 
ATOM   8149 C  CG  . GLU D  1 220 ? 5.335   -10.768 -56.704 1.00 16.50  ? 220 GLU D CG  1 
ATOM   8150 C  CD  . GLU D  1 220 ? 5.550   -12.105 -55.972 1.00 22.48  ? 220 GLU D CD  1 
ATOM   8151 O  OE1 . GLU D  1 220 ? 5.130   -12.248 -54.808 1.00 21.63  ? 220 GLU D OE1 1 
ATOM   8152 O  OE2 . GLU D  1 220 ? 6.134   -13.045 -56.560 1.00 33.69  ? 220 GLU D OE2 1 
ATOM   8153 N  N   . GLN D  1 221 ? 4.440   -7.775  -53.267 1.00 11.99  ? 221 GLN D N   1 
ATOM   8154 C  CA  . GLN D  1 221 ? 3.925   -6.566  -52.601 1.00 12.06  ? 221 GLN D CA  1 
ATOM   8155 C  C   . GLN D  1 221 ? 5.044   -5.667  -52.121 1.00 11.09  ? 221 GLN D C   1 
ATOM   8156 O  O   . GLN D  1 221 ? 5.000   -4.459  -52.231 1.00 12.26  ? 221 GLN D O   1 
ATOM   8157 C  CB  . GLN D  1 221 ? 3.007   -6.992  -51.444 1.00 12.10  ? 221 GLN D CB  1 
ATOM   8158 C  CG  . GLN D  1 221 ? 1.706   -7.616  -51.916 1.00 11.92  ? 221 GLN D CG  1 
ATOM   8159 C  CD  . GLN D  1 221 ? 0.795   -7.974  -50.795 1.00 11.76  ? 221 GLN D CD  1 
ATOM   8160 O  OE1 . GLN D  1 221 ? 1.095   -8.913  -50.005 1.00 11.77  ? 221 GLN D OE1 1 
ATOM   8161 N  NE2 . GLN D  1 221 ? -0.340  -7.306  -50.645 1.00 11.61  ? 221 GLN D NE2 1 
ATOM   8162 N  N   . LEU D  1 222 ? 6.085   -6.298  -51.503 1.00 11.69  ? 222 LEU D N   1 
ATOM   8163 C  CA  . LEU D  1 222 ? 7.216   -5.539  -50.997 1.00 11.36  ? 222 LEU D CA  1 
ATOM   8164 C  C   . LEU D  1 222 ? 7.935   -4.851  -52.177 1.00 11.46  ? 222 LEU D C   1 
ATOM   8165 O  O   . LEU D  1 222 ? 8.304   -3.678  -52.033 1.00 12.40  ? 222 LEU D O   1 
ATOM   8166 C  CB  . LEU D  1 222 ? 8.172   -6.452  -50.279 1.00 12.92  ? 222 LEU D CB  1 
ATOM   8167 C  CG  . LEU D  1 222 ? 7.824   -6.716  -48.862 1.00 14.68  ? 222 LEU D CG  1 
ATOM   8168 C  CD1 . LEU D  1 222 ? 8.557   -7.973  -48.368 1.00 16.19  ? 222 LEU D CD1 1 
ATOM   8169 C  CD2 . LEU D  1 222 ? 8.266   -5.440  -47.947 1.00 16.26  ? 222 LEU D CD2 1 
ATOM   8170 N  N   . LEU D  1 223 ? 8.120   -5.550  -53.269 1.00 11.50  ? 223 LEU D N   1 
ATOM   8171 C  CA  . LEU D  1 223 ? 8.811   -4.952  -54.407 1.00 12.65  ? 223 LEU D CA  1 
ATOM   8172 C  C   . LEU D  1 223 ? 7.980   -3.772  -54.939 1.00 12.35  ? 223 LEU D C   1 
ATOM   8173 O  O   . LEU D  1 223 ? 8.525   -2.714  -55.325 1.00 13.53  ? 223 LEU D O   1 
ATOM   8174 C  CB  . LEU D  1 223 ? 9.042   -5.992  -55.524 1.00 13.84  ? 223 LEU D CB  1 
ATOM   8175 C  CG  . LEU D  1 223 ? 9.780   -5.483  -56.741 1.00 16.01  ? 223 LEU D CG  1 
ATOM   8176 C  CD1 . LEU D  1 223 ? 11.226  -5.070  -56.342 1.00 18.50  ? 223 LEU D CD1 1 
ATOM   8177 C  CD2 . LEU D  1 223 ? 9.877   -6.595  -57.770 1.00 17.52  ? 223 LEU D CD2 1 
ATOM   8178 N  N   . ALA D  1 224 ? 6.682   -3.932  -55.004 1.00 13.01  ? 224 ALA D N   1 
ATOM   8179 C  CA  . ALA D  1 224 ? 5.799   -2.827  -55.455 1.00 14.00  ? 224 ALA D CA  1 
ATOM   8180 C  C   . ALA D  1 224 ? 5.968   -1.611  -54.530 1.00 13.46  ? 224 ALA D C   1 
ATOM   8181 O  O   . ALA D  1 224 ? 6.162   -0.486  -55.013 1.00 16.28  ? 224 ALA D O   1 
ATOM   8182 C  CB  . ALA D  1 224 ? 4.313   -3.271  -55.594 1.00 17.37  ? 224 ALA D CB  1 
ATOM   8183 N  N   . LEU D  1 225 ? 5.933   -1.841  -53.215 1.00 13.79  ? 225 LEU D N   1 
ATOM   8184 C  CA  . LEU D  1 225 ? 6.110   -0.745  -52.294 1.00 13.95  ? 225 LEU D CA  1 
ATOM   8185 C  C   . LEU D  1 225 ? 7.455   -0.071  -52.391 1.00 13.29  ? 225 LEU D C   1 
ATOM   8186 O  O   . LEU D  1 225 ? 7.532   1.139   -52.381 1.00 15.52  ? 225 LEU D O   1 
ATOM   8187 C  CB  . LEU D  1 225 ? 5.858   -1.327  -50.884 1.00 13.57  ? 225 LEU D CB  1 
ATOM   8188 C  CG  . LEU D  1 225 ? 6.051   -0.359  -49.729 1.00 14.32  ? 225 LEU D CG  1 
ATOM   8189 C  CD1 . LEU D  1 225 ? 5.039   0.798   -49.754 1.00 15.33  ? 225 LEU D CD1 1 
ATOM   8190 C  CD2 . LEU D  1 225 ? 5.950   -1.109  -48.369 1.00 15.17  ? 225 LEU D CD2 1 
ATOM   8191 N  N   . GLU D  1 226 ? 8.501   -0.900  -52.597 1.00 12.95  ? 226 GLU D N   1 
ATOM   8192 C  CA  . GLU D  1 226 ? 9.854   -0.422  -52.670 1.00 13.27  ? 226 GLU D CA  1 
ATOM   8193 C  C   . GLU D  1 226 ? 10.175  0.295   -53.944 1.00 14.38  ? 226 GLU D C   1 
ATOM   8194 O  O   . GLU D  1 226 ? 11.242  0.995   -53.987 1.00 18.18  ? 226 GLU D O   1 
ATOM   8195 C  CB  . GLU D  1 226 ? 10.836  -1.601  -52.500 1.00 12.83  ? 226 GLU D CB  1 
ATOM   8196 C  CG  . GLU D  1 226 ? 10.856  -2.244  -51.125 1.00 12.93  ? 226 GLU D CG  1 
ATOM   8197 C  CD  . GLU D  1 226 ? 11.285  -3.707  -51.092 1.00 13.58  ? 226 GLU D CD  1 
ATOM   8198 O  OE1 . GLU D  1 226 ? 11.542  -4.293  -52.180 1.00 14.29  ? 226 GLU D OE1 1 
ATOM   8199 O  OE2 . GLU D  1 226 ? 11.277  -4.324  -50.037 1.00 18.27  ? 226 GLU D OE2 1 
ATOM   8200 N  N   . THR D  1 227 ? 9.407   0.130   -54.962 1.00 13.24  ? 227 THR D N   1 
ATOM   8201 C  CA  . THR D  1 227 ? 9.733   0.762   -56.290 1.00 15.38  ? 227 THR D CA  1 
ATOM   8202 C  C   . THR D  1 227 ? 8.666   1.737   -56.697 1.00 16.14  ? 227 THR D C   1 
ATOM   8203 O  O   . THR D  1 227 ? 8.823   2.341   -57.787 1.00 19.35  ? 227 THR D O   1 
ATOM   8204 C  CB  . THR D  1 227 ? 9.917   -0.298  -57.374 1.00 16.59  ? 227 THR D CB  1 
ATOM   8205 O  OG1 . THR D  1 227 ? 8.711   -1.069  -57.524 1.00 17.23  ? 227 THR D OG1 1 
ATOM   8206 C  CG2 . THR D  1 227 ? 11.083  -1.206  -57.043 1.00 17.84  ? 227 THR D CG2 1 
ATOM   8207 N  N   . ALA D  1 228 ? 7.589   1.949   -55.952 1.00 14.66  ? 228 ALA D N   1 
ATOM   8208 C  CA  . ALA D  1 228 ? 6.445   2.738   -56.510 1.00 17.44  ? 228 ALA D CA  1 
ATOM   8209 C  C   . ALA D  1 228 ? 6.708   4.262   -56.297 1.00 17.50  ? 228 ALA D C   1 
ATOM   8210 O  O   . ALA D  1 228 ? 6.194   4.968   -57.139 1.00 23.74  ? 228 ALA D O   1 
ATOM   8211 C  CB  . ALA D  1 228 ? 5.151   2.360   -55.795 1.00 21.06  ? 228 ALA D CB  1 
ATOM   8212 N  N   . LEU D  1 229 ? 7.434   4.662   -55.283 1.00 14.41  ? 229 LEU D N   1 
ATOM   8213 C  CA  . LEU D  1 229 ? 7.329   6.046   -54.864 1.00 15.60  ? 229 LEU D CA  1 
ATOM   8214 C  C   . LEU D  1 229 ? 8.642   6.828   -54.956 1.00 15.93  ? 229 LEU D C   1 
ATOM   8215 O  O   . LEU D  1 229 ? 9.729   6.229   -54.828 1.00 14.95  ? 229 LEU D O   1 
ATOM   8216 C  CB  . LEU D  1 229 ? 6.868   6.127   -53.406 1.00 16.05  ? 229 LEU D CB  1 
ATOM   8217 C  CG  . LEU D  1 229 ? 5.579   5.338   -53.082 1.00 15.85  ? 229 LEU D CG  1 
ATOM   8218 C  CD1 . LEU D  1 229 ? 5.312   5.242   -51.621 1.00 20.54  ? 229 LEU D CD1 1 
ATOM   8219 C  CD2 . LEU D  1 229 ? 4.408   5.713   -53.914 1.00 18.35  ? 229 LEU D CD2 1 
ATOM   8220 N  N   . TYR D  1 230 ? 8.510   8.130   -55.005 1.00 17.99  ? 230 TYR D N   1 
ATOM   8221 C  CA  . TYR D  1 230 ? 9.601   9.091   -54.998 1.00 17.51  ? 230 TYR D CA  1 
ATOM   8222 C  C   . TYR D  1 230 ? 9.451   10.063  -53.859 1.00 17.05  ? 230 TYR D C   1 
ATOM   8223 O  O   . TYR D  1 230 ? 8.323   10.444  -53.519 1.00 18.49  ? 230 TYR D O   1 
ATOM   8224 C  CB  . TYR D  1 230 ? 9.630   9.909   -56.333 1.00 19.00  ? 230 TYR D CB  1 
ATOM   8225 C  CG  . TYR D  1 230 ? 10.110  9.014   -57.395 1.00 20.23  ? 230 TYR D CG  1 
ATOM   8226 C  CD1 . TYR D  1 230 ? 9.221   8.194   -58.020 1.00 23.31  ? 230 TYR D CD1 1 
ATOM   8227 C  CD2 . TYR D  1 230 ? 11.448  9.008   -57.827 1.00 21.48  ? 230 TYR D CD2 1 
ATOM   8228 C  CE1 . TYR D  1 230 ? 9.593   7.250   -59.005 1.00 27.79  ? 230 TYR D CE1 1 
ATOM   8229 C  CE2 . TYR D  1 230 ? 11.879  8.074   -58.816 1.00 25.06  ? 230 TYR D CE2 1 
ATOM   8230 C  CZ  . TYR D  1 230 ? 10.945  7.229   -59.411 1.00 29.44  ? 230 TYR D CZ  1 
ATOM   8231 O  OH  . TYR D  1 230 ? 11.286  6.340   -60.382 1.00 37.46  ? 230 TYR D OH  1 
ATOM   8232 N  N   . CYS D  1 231 ? 10.522  10.481  -53.257 1.00 18.08  ? 231 CYS D N   1 
ATOM   8233 C  CA  . CYS D  1 231 ? 10.497  11.431  -52.181 1.00 19.13  ? 231 CYS D CA  1 
ATOM   8234 C  C   . CYS D  1 231 ? 10.380  12.909  -52.702 1.00 17.42  ? 231 CYS D C   1 
ATOM   8235 O  O   . CYS D  1 231 ? 10.037  13.813  -51.963 1.00 21.64  ? 231 CYS D O   1 
ATOM   8236 C  CB  . CYS D  1 231 ? 11.942  11.452  -51.570 1.00 30.49  ? 231 CYS D CB  1 
ATOM   8237 S  SG  . CYS D  1 231 ? 12.403  10.095  -50.461 1.00 30.31  ? 231 CYS D SG  1 
ATOM   8238 N  N   . THR D  1 232 ? 10.608  13.025  -54.013 1.00 18.18  ? 232 THR D N   1 
ATOM   8239 C  CA  . THR D  1 232 ? 10.648  14.377  -54.629 1.00 18.06  ? 232 THR D CA  1 
ATOM   8240 C  C   . THR D  1 232 ? 9.332   14.644  -55.392 1.00 16.63  ? 232 THR D C   1 
ATOM   8241 O  O   . THR D  1 232 ? 8.506   13.780  -55.740 1.00 17.50  ? 232 THR D O   1 
ATOM   8242 C  CB  . THR D  1 232 ? 11.846  14.417  -55.598 1.00 17.92  ? 232 THR D CB  1 
ATOM   8243 O  OG1 . THR D  1 232 ? 11.837  13.146  -56.278 1.00 19.34  ? 232 THR D OG1 1 
ATOM   8244 C  CG2 . THR D  1 232 ? 13.161  14.465  -54.875 1.00 23.42  ? 232 THR D CG2 1 
ATOM   8245 N  N   . HIS D  1 233 ? 9.127   15.942  -55.605 1.00 15.86  ? 233 HIS D N   1 
ATOM   8246 C  CA  . HIS D  1 233 ? 7.961   16.383  -56.437 1.00 16.58  ? 233 HIS D CA  1 
ATOM   8247 C  C   . HIS D  1 233 ? 8.152   15.913  -57.837 1.00 16.32  ? 233 HIS D C   1 
ATOM   8248 O  O   . HIS D  1 233 ? 9.296   15.746  -58.355 1.00 17.22  ? 233 HIS D O   1 
ATOM   8249 C  CB  . HIS D  1 233 ? 7.877   17.926  -56.420 1.00 19.71  ? 233 HIS D CB  1 
ATOM   8250 C  CG  . HIS D  1 233 ? 7.388   18.432  -55.070 1.00 21.95  ? 233 HIS D CG  1 
ATOM   8251 N  ND1 . HIS D  1 233 ? 8.156   19.184  -54.177 1.00 33.58  ? 233 HIS D ND1 1 
ATOM   8252 C  CD2 . HIS D  1 233 ? 6.192   18.277  -54.451 1.00 26.77  ? 233 HIS D CD2 1 
ATOM   8253 C  CE1 . HIS D  1 233 ? 7.468   19.465  -53.092 1.00 35.11  ? 233 HIS D CE1 1 
ATOM   8254 N  NE2 . HIS D  1 233 ? 6.264   18.957  -53.251 1.00 30.25  ? 233 HIS D NE2 1 
ATOM   8255 N  N   . MET D  1 234 ? 7.047   15.811  -58.547 1.00 17.21  ? 234 MET D N   1 
ATOM   8256 C  CA  . MET D  1 234 ? 7.081   15.294  -59.910 1.00 18.10  ? 234 MET D CA  1 
ATOM   8257 C  C   . MET D  1 234 ? 8.040   16.104  -60.830 1.00 19.55  ? 234 MET D C   1 
ATOM   8258 O  O   . MET D  1 234 ? 8.707   15.543  -61.718 1.00 22.32  ? 234 MET D O   1 
ATOM   8259 C  CB  . MET D  1 234 ? 5.675   15.258  -60.417 1.00 20.61  ? 234 MET D CB  1 
ATOM   8260 C  CG  . MET D  1 234 ? 5.552   14.591  -61.732 1.00 25.21  ? 234 MET D CG  1 
ATOM   8261 S  SD  . MET D  1 234 ? 3.771   14.649  -62.279 1.00 33.50  ? 234 MET D SD  1 
ATOM   8262 C  CE  . MET D  1 234 ? 3.993   14.010  -63.870 1.00 37.53  ? 234 MET D CE  1 
ATOM   8263 N  N   . ASP D  1 235 ? 8.083   17.416  -60.614 1.00 20.32  ? 235 ASP D N   1 
ATOM   8264 C  CA  . ASP D  1 235 ? 8.921   18.213  -61.534 1.00 24.16  ? 235 ASP D CA  1 
ATOM   8265 C  C   . ASP D  1 235 ? 10.350  18.450  -61.055 1.00 23.41  ? 235 ASP D C   1 
ATOM   8266 O  O   . ASP D  1 235 ? 11.114  19.213  -61.664 1.00 25.71  ? 235 ASP D O   1 
ATOM   8267 C  CB  . ASP D  1 235 ? 8.181   19.557  -61.835 1.00 32.51  ? 235 ASP D CB  1 
ATOM   8268 C  CG  . ASP D  1 235 ? 7.920   20.428  -60.570 1.00 39.93  ? 235 ASP D CG  1 
ATOM   8269 O  OD1 . ASP D  1 235 ? 8.401   20.089  -59.429 1.00 35.59  ? 235 ASP D OD1 1 
ATOM   8270 O  OD2 . ASP D  1 235 ? 7.195   21.410  -60.682 1.00 42.71  ? 235 ASP D OD2 1 
ATOM   8271 N  N   . ASP D  1 236 ? 10.774  17.747  -60.003 1.00 20.43  ? 236 ASP D N   1 
ATOM   8272 C  CA  . ASP D  1 236 ? 12.104  17.949  -59.553 1.00 21.25  ? 236 ASP D CA  1 
ATOM   8273 C  C   . ASP D  1 236 ? 13.112  17.415  -60.572 1.00 25.16  ? 236 ASP D C   1 
ATOM   8274 O  O   . ASP D  1 236 ? 12.999  16.231  -60.968 1.00 24.92  ? 236 ASP D O   1 
ATOM   8275 C  CB  . ASP D  1 236 ? 12.344  17.099  -58.254 1.00 20.58  ? 236 ASP D CB  1 
ATOM   8276 C  CG  . ASP D  1 236 ? 13.492  17.547  -57.500 1.00 22.08  ? 236 ASP D CG  1 
ATOM   8277 O  OD1 . ASP D  1 236 ? 14.614  17.675  -58.077 1.00 25.02  ? 236 ASP D OD1 1 
ATOM   8278 O  OD2 . ASP D  1 236 ? 13.355  17.744  -56.278 1.00 24.29  ? 236 ASP D OD2 1 
ATOM   8279 N  N   . PRO D  1 237 ? 14.092  18.214  -61.023 1.00 24.97  ? 237 PRO D N   1 
ATOM   8280 C  CA  . PRO D  1 237 ? 15.126  17.668  -61.918 1.00 27.66  ? 237 PRO D CA  1 
ATOM   8281 C  C   . PRO D  1 237 ? 16.094  16.621  -61.355 1.00 31.31  ? 237 PRO D C   1 
ATOM   8282 O  O   . PRO D  1 237 ? 16.791  15.956  -62.202 1.00 36.54  ? 237 PRO D O   1 
ATOM   8283 C  CB  . PRO D  1 237 ? 15.954  18.937  -62.320 1.00 31.95  ? 237 PRO D CB  1 
ATOM   8284 C  CG  . PRO D  1 237 ? 15.686  19.910  -61.197 1.00 31.67  ? 237 PRO D CG  1 
ATOM   8285 C  CD  . PRO D  1 237 ? 14.329  19.616  -60.598 1.00 28.48  ? 237 PRO D CD  1 
ATOM   8286 N  N   . SER D  1 238 ? 16.101  16.380  -60.019 1.00 27.71  ? 238 SER D N   1 
ATOM   8287 C  CA  . SER D  1 238 ? 16.940  15.395  -59.383 1.00 29.64  ? 238 SER D CA  1 
ATOM   8288 C  C   . SER D  1 238 ? 16.023  14.476  -58.588 1.00 27.23  ? 238 SER D C   1 
ATOM   8289 O  O   . SER D  1 238 ? 15.908  14.610  -57.378 1.00 26.94  ? 238 SER D O   1 
ATOM   8290 C  CB  . SER D  1 238 ? 17.879  16.122  -58.420 1.00 32.17  ? 238 SER D CB  1 
ATOM   8291 O  OG  . SER D  1 238 ? 18.968  15.284  -58.004 1.00 49.56  ? 238 SER D OG  1 
ATOM   8292 N  N   . PRO D  1 239 ? 15.334  13.556  -59.267 1.00 26.53  ? 239 PRO D N   1 
ATOM   8293 C  CA  . PRO D  1 239 ? 14.374  12.618  -58.544 1.00 26.25  ? 239 PRO D CA  1 
ATOM   8294 C  C   . PRO D  1 239 ? 15.075  11.650  -57.640 1.00 30.21  ? 239 PRO D C   1 
ATOM   8295 O  O   . PRO D  1 239 ? 16.172  11.196  -58.026 1.00 37.71  ? 239 PRO D O   1 
ATOM   8296 C  CB  . PRO D  1 239 ? 13.664  11.881  -59.685 1.00 26.89  ? 239 PRO D CB  1 
ATOM   8297 C  CG  . PRO D  1 239 ? 14.465  12.130  -60.929 1.00 36.50  ? 239 PRO D CG  1 
ATOM   8298 C  CD  . PRO D  1 239 ? 15.256  13.408  -60.722 1.00 31.02  ? 239 PRO D CD  1 
ATOM   8299 N  N   . ARG D  1 240 ? 14.433  11.364  -56.467 1.00 26.69  ? 240 ARG D N   1 
ATOM   8300 C  CA  . ARG D  1 240 ? 15.090  10.518  -55.401 1.00 22.64  ? 240 ARG D CA  1 
ATOM   8301 C  C   . ARG D  1 240 ? 14.003  9.421   -55.115 1.00 24.13  ? 240 ARG D C   1 
ATOM   8302 O  O   . ARG D  1 240 ? 12.819  9.803   -54.822 1.00 21.47  ? 240 ARG D O   1 
ATOM   8303 C  CB  . ARG D  1 240 ? 15.409  11.204  -54.032 1.00 29.70  ? 240 ARG D CB  1 
ATOM   8304 N  N   . GLU D  1 241 ? 14.325  8.130   -55.348 1.00 20.01  ? 241 GLU D N   1 
ATOM   8305 C  CA  . GLU D  1 241 ? 13.385  7.121   -54.950 1.00 18.07  ? 241 GLU D CA  1 
ATOM   8306 C  C   . GLU D  1 241 ? 13.174  7.058   -53.482 1.00 18.93  ? 241 GLU D C   1 
ATOM   8307 O  O   . GLU D  1 241 ? 14.123  7.122   -52.673 1.00 20.46  ? 241 GLU D O   1 
ATOM   8308 C  CB  . GLU D  1 241 ? 14.008  5.782   -55.443 1.00 22.21  ? 241 GLU D CB  1 
ATOM   8309 C  CG  . GLU D  1 241 ? 14.029  5.639   -57.026 1.00 26.90  ? 241 GLU D CG  1 
ATOM   8310 C  CD  . GLU D  1 241 ? 14.884  4.442   -57.364 1.00 32.41  ? 241 GLU D CD  1 
ATOM   8311 O  OE1 . GLU D  1 241 ? 16.147  4.518   -57.077 1.00 44.49  ? 241 GLU D OE1 1 
ATOM   8312 O  OE2 . GLU D  1 241 ? 14.348  3.408   -57.819 1.00 39.06  ? 241 GLU D OE2 1 
ATOM   8313 N  N   . MET D  1 242 ? 11.943  6.677   -53.098 1.00 16.33  ? 242 MET D N   1 
ATOM   8314 C  CA  . MET D  1 242 ? 11.620  6.583   -51.691 1.00 15.89  ? 242 MET D CA  1 
ATOM   8315 C  C   . MET D  1 242 ? 11.911  5.123   -51.252 1.00 12.97  ? 242 MET D C   1 
ATOM   8316 O  O   . MET D  1 242 ? 11.070  4.211   -51.397 1.00 14.31  ? 242 MET D O   1 
ATOM   8317 C  CB  . MET D  1 242 ? 10.160  6.951   -51.461 1.00 14.49  ? 242 MET D CB  1 
ATOM   8318 C  CG  . MET D  1 242 ? 9.902   7.000   -49.909 1.00 15.29  ? 242 MET D CG  1 
ATOM   8319 S  SD  . MET D  1 242 ? 8.114   7.327   -49.573 1.00 14.79  ? 242 MET D SD  1 
ATOM   8320 C  CE  . MET D  1 242 ? 7.983   8.986   -50.195 1.00 16.18  ? 242 MET D CE  1 
ATOM   8321 N  N   . ILE D  1 243 ? 13.111  4.910   -50.715 1.00 12.27  ? 243 ILE D N   1 
ATOM   8322 C  CA  . ILE D  1 243 ? 13.595  3.618   -50.264 1.00 12.79  ? 243 ILE D CA  1 
ATOM   8323 C  C   . ILE D  1 243 ? 14.351  3.829   -48.943 1.00 10.51  ? 243 ILE D C   1 
ATOM   8324 O  O   . ILE D  1 243 ? 14.786  4.965   -48.621 1.00 11.71  ? 243 ILE D O   1 
ATOM   8325 C  CB  . ILE D  1 243 ? 14.548  2.963   -51.285 1.00 13.82  ? 243 ILE D CB  1 
ATOM   8326 C  CG1 . ILE D  1 243 ? 15.725  3.882   -51.645 1.00 16.69  ? 243 ILE D CG1 1 
ATOM   8327 C  CG2 . ILE D  1 243 ? 13.793  2.479   -52.496 1.00 17.19  ? 243 ILE D CG2 1 
ATOM   8328 C  CD1 . ILE D  1 243 ? 16.843  3.351   -52.587 1.00 20.85  ? 243 ILE D CD1 1 
ATOM   8329 N  N   . ASN D  1 244 ? 14.467  2.731   -48.173 1.00 10.58  ? 244 ASN D N   1 
ATOM   8330 C  CA  . ASN D  1 244 ? 15.254  2.770   -46.947 1.00 10.26  ? 244 ASN D CA  1 
ATOM   8331 C  C   . ASN D  1 244 ? 14.817  3.907   -46.021 1.00 10.24  ? 244 ASN D C   1 
ATOM   8332 O  O   . ASN D  1 244 ? 15.678  4.574   -45.415 1.00 10.84  ? 244 ASN D O   1 
ATOM   8333 C  CB  . ASN D  1 244 ? 16.747  2.855   -47.247 1.00 11.48  ? 244 ASN D CB  1 
ATOM   8334 C  CG  . ASN D  1 244 ? 17.176  1.703   -48.104 1.00 14.46  ? 244 ASN D CG  1 
ATOM   8335 O  OD1 . ASN D  1 244 ? 16.719  0.586   -48.110 1.00 14.91  ? 244 ASN D OD1 1 
ATOM   8336 N  ND2 . ASN D  1 244 ? 18.106  2.078   -49.050 1.00 22.39  ? 244 ASN D ND2 1 
ATOM   8337 N  N   . ASN D  1 245 ? 13.487  4.075   -45.850 1.00 9.74   ? 245 ASN D N   1 
ATOM   8338 C  CA  . ASN D  1 245 ? 12.959  5.170   -45.089 1.00 9.55   ? 245 ASN D CA  1 
ATOM   8339 C  C   . ASN D  1 245 ? 12.721  4.705   -43.634 1.00 9.44   ? 245 ASN D C   1 
ATOM   8340 O  O   . ASN D  1 245 ? 11.634  4.844   -43.107 1.00 11.27  ? 245 ASN D O   1 
ATOM   8341 C  CB  . ASN D  1 245 ? 11.709  5.772   -45.738 1.00 10.22  ? 245 ASN D CB  1 
ATOM   8342 C  CG  . ASN D  1 245 ? 10.591  4.774   -45.885 1.00 9.89   ? 245 ASN D CG  1 
ATOM   8343 O  OD1 . ASN D  1 245 ? 10.793  3.554   -45.868 1.00 10.80  ? 245 ASN D OD1 1 
ATOM   8344 N  ND2 . ASN D  1 245 ? 9.351   5.269   -46.080 1.00 12.21  ? 245 ASN D ND2 1 
ATOM   8345 N  N   . PHE D  1 246 ? 13.770  4.197   -43.022 1.00 9.89   ? 246 PHE D N   1 
ATOM   8346 C  CA  . PHE D  1 246 ? 13.734  3.756   -41.611 1.00 9.50   ? 246 PHE D CA  1 
ATOM   8347 C  C   . PHE D  1 246 ? 14.901  4.387   -40.934 1.00 9.10   ? 246 PHE D C   1 
ATOM   8348 O  O   . PHE D  1 246 ? 15.993  4.529   -41.493 1.00 10.12  ? 246 PHE D O   1 
ATOM   8349 C  CB  . PHE D  1 246 ? 13.760  2.196   -41.507 1.00 10.31  ? 246 PHE D CB  1 
ATOM   8350 C  CG  . PHE D  1 246 ? 15.000  1.574   -42.094 1.00 10.47  ? 246 PHE D CG  1 
ATOM   8351 C  CD1 . PHE D  1 246 ? 15.075  1.262   -43.450 1.00 10.72  ? 246 PHE D CD1 1 
ATOM   8352 C  CD2 . PHE D  1 246 ? 16.085  1.250   -41.258 1.00 12.05  ? 246 PHE D CD2 1 
ATOM   8353 C  CE1 . PHE D  1 246 ? 16.238  0.644   -43.979 1.00 11.64  ? 246 PHE D CE1 1 
ATOM   8354 C  CE2 . PHE D  1 246 ? 17.235  0.667   -41.798 1.00 12.93  ? 246 PHE D CE2 1 
ATOM   8355 C  CZ  . PHE D  1 246 ? 17.298  0.341   -43.155 1.00 12.90  ? 246 PHE D CZ  1 
ATOM   8356 N  N   . ARG D  1 247 ? 14.736  4.683   -39.629 1.00 9.09   ? 247 ARG D N   1 
ATOM   8357 C  CA  . ARG D  1 247 ? 15.800  5.163   -38.789 1.00 9.01   ? 247 ARG D CA  1 
ATOM   8358 C  C   . ARG D  1 247 ? 16.545  3.988   -38.161 1.00 9.20   ? 247 ARG D C   1 
ATOM   8359 O  O   . ARG D  1 247 ? 15.899  2.991   -37.809 1.00 9.84   ? 247 ARG D O   1 
ATOM   8360 C  CB  . ARG D  1 247 ? 15.206  6.049   -37.686 1.00 9.88   ? 247 ARG D CB  1 
ATOM   8361 C  CG  . ARG D  1 247 ? 16.166  6.941   -36.936 1.00 9.89   ? 247 ARG D CG  1 
ATOM   8362 C  CD  . ARG D  1 247 ? 15.516  7.627   -35.788 1.00 10.11  ? 247 ARG D CD  1 
ATOM   8363 N  NE  . ARG D  1 247 ? 16.366  8.712   -35.230 1.00 10.07  ? 247 ARG D NE  1 
ATOM   8364 C  CZ  . ARG D  1 247 ? 16.043  9.461   -34.167 1.00 10.08  ? 247 ARG D CZ  1 
ATOM   8365 N  NH1 . ARG D  1 247 ? 14.946  9.164   -33.457 1.00 11.32  ? 247 ARG D NH1 1 
ATOM   8366 N  NH2 . ARG D  1 247 ? 16.817  10.458  -33.815 1.00 10.90  ? 247 ARG D NH2 1 
ATOM   8367 N  N   . GLN D  1 248 ? 17.861  4.121   -37.944 1.00 9.48   ? 248 GLN D N   1 
ATOM   8368 C  CA  . GLN D  1 248 ? 18.586  3.118   -37.160 1.00 9.02   ? 248 GLN D CA  1 
ATOM   8369 C  C   . GLN D  1 248 ? 18.059  3.088   -35.746 1.00 9.34   ? 248 GLN D C   1 
ATOM   8370 O  O   . GLN D  1 248 ? 17.536  4.074   -35.203 1.00 9.75   ? 248 GLN D O   1 
ATOM   8371 C  CB  . GLN D  1 248 ? 20.092  3.486   -37.117 1.00 10.33  ? 248 GLN D CB  1 
ATOM   8372 C  CG  . GLN D  1 248 ? 20.774  3.531   -38.461 1.00 10.49  ? 248 GLN D CG  1 
ATOM   8373 C  CD  . GLN D  1 248 ? 20.796  2.148   -39.133 1.00 10.20  ? 248 GLN D CD  1 
ATOM   8374 O  OE1 . GLN D  1 248 ? 19.891  1.806   -39.904 1.00 11.50  ? 248 GLN D OE1 1 
ATOM   8375 N  NE2 . GLN D  1 248 ? 21.813  1.374   -38.832 1.00 12.45  ? 248 GLN D NE2 1 
ATOM   8376 N  N   . VAL D  1 249 ? 18.288  1.947   -35.069 1.00 10.22  ? 249 VAL D N   1 
ATOM   8377 C  CA  . VAL D  1 249 ? 17.899  1.833   -33.645 1.00 10.15  ? 249 VAL D CA  1 
ATOM   8378 C  C   . VAL D  1 249 ? 18.752  2.787   -32.786 1.00 10.72  ? 249 VAL D C   1 
ATOM   8379 O  O   . VAL D  1 249 ? 19.921  3.081   -33.108 1.00 10.85  ? 249 VAL D O   1 
ATOM   8380 C  CB  . VAL D  1 249 ? 17.960  0.381   -33.134 1.00 10.82  ? 249 VAL D CB  1 
ATOM   8381 C  CG1 . VAL D  1 249 ? 16.865  -0.432  -33.868 1.00 12.16  ? 249 VAL D CG1 1 
ATOM   8382 C  CG2 . VAL D  1 249 ? 19.333  -0.231  -33.234 1.00 13.93  ? 249 VAL D CG2 1 
ATOM   8383 N  N   . GLN D  1 250 ? 18.167  3.161   -31.649 1.00 10.89  ? 250 GLN D N   1 
ATOM   8384 C  CA  . GLN D  1 250 ? 18.722  4.201   -30.761 1.00 11.09  ? 250 GLN D CA  1 
ATOM   8385 C  C   . GLN D  1 250 ? 19.193  3.592   -29.459 1.00 11.40  ? 250 GLN D C   1 
ATOM   8386 O  O   . GLN D  1 250 ? 18.744  2.529   -29.022 1.00 12.74  ? 250 GLN D O   1 
ATOM   8387 C  CB  . GLN D  1 250 ? 17.580  5.140   -30.413 1.00 11.01  ? 250 GLN D CB  1 
ATOM   8388 C  CG  . GLN D  1 250 ? 16.912  5.785   -31.679 1.00 11.61  ? 250 GLN D CG  1 
ATOM   8389 C  CD  . GLN D  1 250 ? 17.855  6.716   -32.430 1.00 9.99   ? 250 GLN D CD  1 
ATOM   8390 O  OE1 . GLN D  1 250 ? 18.299  7.763   -31.845 1.00 11.46  ? 250 GLN D OE1 1 
ATOM   8391 N  NE2 . GLN D  1 250 ? 18.148  6.407   -33.651 1.00 10.98  ? 250 GLN D NE2 1 
ATOM   8392 N  N   . LYS D  1 251 ? 20.074  4.303   -28.801 1.00 11.97  ? 251 LYS D N   1 
ATOM   8393 C  CA  . LYS D  1 251 ? 20.496  3.885   -27.404 1.00 13.69  ? 251 LYS D CA  1 
ATOM   8394 C  C   . LYS D  1 251 ? 19.257  3.819   -26.520 1.00 13.53  ? 251 LYS D C   1 
ATOM   8395 O  O   . LYS D  1 251 ? 18.327  4.635   -26.575 1.00 13.43  ? 251 LYS D O   1 
ATOM   8396 C  CB  . LYS D  1 251 ? 21.457  4.959   -26.810 1.00 16.09  ? 251 LYS D CB  1 
ATOM   8397 C  CG  . LYS D  1 251 ? 22.843  5.037   -27.393 1.00 16.74  ? 251 LYS D CG  1 
ATOM   8398 C  CD  . LYS D  1 251 ? 23.715  3.917   -26.914 1.00 17.16  ? 251 LYS D CD  1 
ATOM   8399 C  CE  . LYS D  1 251 ? 25.203  3.926   -27.326 1.00 16.67  ? 251 LYS D CE  1 
ATOM   8400 N  NZ  . LYS D  1 251 ? 25.323  3.891   -28.786 1.00 14.62  ? 251 LYS D NZ  1 
ATOM   8401 N  N   . PHE D  1 252 ? 19.270  2.884   -25.588 1.00 15.44  ? 252 PHE D N   1 
ATOM   8402 C  CA  . PHE D  1 252 ? 18.159  2.752   -24.685 1.00 14.78  ? 252 PHE D CA  1 
ATOM   8403 C  C   . PHE D  1 252 ? 18.097  3.903   -23.612 1.00 19.83  ? 252 PHE D C   1 
ATOM   8404 O  O   . PHE D  1 252 ? 16.995  4.156   -23.083 1.00 20.58  ? 252 PHE D O   1 
ATOM   8405 C  CB  . PHE D  1 252 ? 18.383  1.480   -23.855 1.00 19.79  ? 252 PHE D CB  1 
ATOM   8406 C  CG  . PHE D  1 252 ? 17.762  0.321   -24.639 1.00 24.02  ? 252 PHE D CG  1 
ATOM   8407 C  CD1 . PHE D  1 252 ? 18.399  -0.236  -25.763 1.00 32.31  ? 252 PHE D CD1 1 
ATOM   8408 C  CD2 . PHE D  1 252 ? 16.427  0.011   -24.453 1.00 30.57  ? 252 PHE D CD2 1 
ATOM   8409 C  CE1 . PHE D  1 252 ? 17.760  -1.200  -26.549 1.00 29.82  ? 252 PHE D CE1 1 
ATOM   8410 C  CE2 . PHE D  1 252 ? 15.789  -0.945  -25.230 1.00 33.87  ? 252 PHE D CE2 1 
ATOM   8411 C  CZ  . PHE D  1 252 ? 16.451  -1.554  -26.278 1.00 27.34  ? 252 PHE D CZ  1 
ATOM   8412 N  N   . ASP D  1 253 ? 19.164  4.640   -23.234 1.00 20.84  ? 253 ASP D N   1 
ATOM   8413 C  CA  . ASP D  1 253 ? 18.982  5.697   -22.212 1.00 21.94  ? 253 ASP D CA  1 
ATOM   8414 C  C   . ASP D  1 253 ? 18.337  5.153   -20.902 1.00 22.63  ? 253 ASP D C   1 
ATOM   8415 O  O   . ASP D  1 253 ? 17.492  5.933   -20.361 1.00 28.15  ? 253 ASP D O   1 
ATOM   8416 C  CB  . ASP D  1 253 ? 18.143  6.892   -22.716 1.00 27.82  ? 253 ASP D CB  1 
ATOM   8417 C  CG  . ASP D  1 253 ? 18.843  7.651   -23.939 1.00 25.99  ? 253 ASP D CG  1 
ATOM   8418 O  OD1 . ASP D  1 253 ? 20.103  7.574   -24.044 1.00 30.88  ? 253 ASP D OD1 1 
ATOM   8419 O  OD2 . ASP D  1 253 ? 18.109  8.273   -24.727 1.00 27.28  ? 253 ASP D OD2 1 
ATOM   8420 N  N   . GLU D  1 254 ? 18.723  3.922   -20.462 1.00 25.31  ? 254 GLU D N   1 
ATOM   8421 C  CA  . GLU D  1 254 ? 18.295  3.378   -19.188 1.00 27.66  ? 254 GLU D CA  1 
ATOM   8422 C  C   . GLU D  1 254 ? 16.826  2.866   -19.220 1.00 24.93  ? 254 GLU D C   1 
ATOM   8423 O  O   . GLU D  1 254 ? 16.323  2.274   -18.226 1.00 30.73  ? 254 GLU D O   1 
ATOM   8424 C  CB  . GLU D  1 254 ? 18.503  4.330   -17.948 1.00 27.91  ? 254 GLU D CB  1 
ATOM   8425 C  CG  . GLU D  1 254 ? 19.963  4.826   -17.773 1.00 43.87  ? 254 GLU D CG  1 
ATOM   8426 C  CD  . GLU D  1 254 ? 20.898  3.776   -17.180 1.00 65.44  ? 254 GLU D CD  1 
ATOM   8427 O  OE1 . GLU D  1 254 ? 22.124  4.049   -17.054 1.00 89.75  ? 254 GLU D OE1 1 
ATOM   8428 O  OE2 . GLU D  1 254 ? 20.409  2.654   -16.897 1.00 68.26  ? 254 GLU D OE2 1 
ATOM   8429 N  N   . ARG D  1 255 ? 16.165  2.978   -20.346 1.00 22.40  ? 255 ARG D N   1 
ATOM   8430 C  CA  . ARG D  1 255 ? 14.830  2.429   -20.361 1.00 17.78  ? 255 ARG D CA  1 
ATOM   8431 C  C   . ARG D  1 255 ? 14.711  0.846   -20.498 1.00 19.96  ? 255 ARG D C   1 
ATOM   8432 O  O   . ARG D  1 255 ? 15.689  0.143   -20.952 1.00 25.33  ? 255 ARG D O   1 
ATOM   8433 C  CB  . ARG D  1 255 ? 14.175  2.897   -21.746 1.00 20.09  ? 255 ARG D CB  1 
ATOM   8434 C  CG  . ARG D  1 255 ? 13.816  4.389   -21.893 1.00 22.34  ? 255 ARG D CG  1 
ATOM   8435 C  CD  . ARG D  1 255 ? 13.340  4.750   -23.304 1.00 21.42  ? 255 ARG D CD  1 
ATOM   8436 N  NE  . ARG D  1 255 ? 14.448  4.758   -24.278 1.00 19.83  ? 255 ARG D NE  1 
ATOM   8437 C  CZ  . ARG D  1 255 ? 14.331  5.039   -25.564 1.00 17.82  ? 255 ARG D CZ  1 
ATOM   8438 N  NH1 . ARG D  1 255 ? 13.117  5.275   -26.063 1.00 16.04  ? 255 ARG D NH1 1 
ATOM   8439 N  NH2 . ARG D  1 255 ? 15.431  5.081   -26.342 1.00 16.96  ? 255 ARG D NH2 1 
ATOM   8440 N  N   . LEU D  1 256 ? 13.623  0.305   -19.924 1.00 20.17  ? 256 LEU D N   1 
ATOM   8441 C  CA  . LEU D  1 256 ? 13.235  -1.066  -20.143 1.00 18.74  ? 256 LEU D CA  1 
ATOM   8442 C  C   . LEU D  1 256 ? 12.033  -1.083  -21.067 1.00 18.26  ? 256 LEU D C   1 
ATOM   8443 O  O   . LEU D  1 256 ? 11.348  -0.064  -21.333 1.00 21.12  ? 256 LEU D O   1 
ATOM   8444 C  CB  . LEU D  1 256 ? 12.885  -1.779  -18.877 1.00 20.91  ? 256 LEU D CB  1 
ATOM   8445 C  CG  . LEU D  1 256 ? 13.957  -1.913  -17.850 1.00 23.81  ? 256 LEU D CG  1 
ATOM   8446 C  CD1 . LEU D  1 256 ? 13.374  -2.579  -16.557 1.00 36.19  ? 256 LEU D CD1 1 
ATOM   8447 C  CD2 . LEU D  1 256 ? 15.174  -2.764  -18.396 1.00 30.26  ? 256 LEU D CD2 1 
ATOM   8448 N  N   . VAL D  1 257 ? 11.887  -2.218  -21.653 1.00 16.57  ? 257 VAL D N   1 
ATOM   8449 C  CA  . VAL D  1 257 ? 10.700  -2.416  -22.503 1.00 15.19  ? 257 VAL D CA  1 
ATOM   8450 C  C   . VAL D  1 257 ? 9.887   -3.486  -21.757 1.00 14.48  ? 257 VAL D C   1 
ATOM   8451 O  O   . VAL D  1 257 ? 10.347  -4.559  -21.370 1.00 16.71  ? 257 VAL D O   1 
ATOM   8452 C  CB  . VAL D  1 257 ? 11.081  -3.002  -23.917 1.00 16.38  ? 257 VAL D CB  1 
ATOM   8453 C  CG1 . VAL D  1 257 ? 9.852   -3.477  -24.690 1.00 16.00  ? 257 VAL D CG1 1 
ATOM   8454 C  CG2 . VAL D  1 257 ? 11.872  -1.994  -24.687 1.00 16.25  ? 257 VAL D CG2 1 
ATOM   8455 N  N   . TYR D  1 258 ? 8.662   -3.151  -21.551 1.00 13.92  ? 258 TYR D N   1 
ATOM   8456 C  CA  . TYR D  1 258 ? 7.762   -3.960  -20.742 1.00 14.10  ? 258 TYR D CA  1 
ATOM   8457 C  C   . TYR D  1 258 ? 6.938   -4.851  -21.676 1.00 12.57  ? 258 TYR D C   1 
ATOM   8458 O  O   . TYR D  1 258 ? 6.560   -4.436  -22.774 1.00 16.57  ? 258 TYR D O   1 
ATOM   8459 C  CB  . TYR D  1 258 ? 6.866   -3.073  -19.849 1.00 15.91  ? 258 TYR D CB  1 
ATOM   8460 C  CG  . TYR D  1 258 ? 7.683   -2.256  -18.986 1.00 17.12  ? 258 TYR D CG  1 
ATOM   8461 C  CD1 . TYR D  1 258 ? 8.173   -2.811  -17.784 1.00 18.78  ? 258 TYR D CD1 1 
ATOM   8462 C  CD2 . TYR D  1 258 ? 8.080   -0.951  -19.309 1.00 20.70  ? 258 TYR D CD2 1 
ATOM   8463 C  CE1 . TYR D  1 258 ? 9.107   -2.052  -16.953 1.00 22.03  ? 258 TYR D CE1 1 
ATOM   8464 C  CE2 . TYR D  1 258 ? 8.890   -0.210  -18.496 1.00 22.69  ? 258 TYR D CE2 1 
ATOM   8465 C  CZ  . TYR D  1 258 ? 9.448   -0.731  -17.346 1.00 20.59  ? 258 TYR D CZ  1 
ATOM   8466 O  OH  . TYR D  1 258 ? 10.261  0.073   -16.543 1.00 27.70  ? 258 TYR D OH  1 
ATOM   8467 N  N   . THR D  1 259 ? 6.733   -6.107  -21.283 1.00 13.36  ? 259 THR D N   1 
ATOM   8468 C  CA  . THR D  1 259 ? 6.038   -7.052  -22.142 1.00 13.28  ? 259 THR D CA  1 
ATOM   8469 C  C   . THR D  1 259 ? 4.798   -7.507  -21.511 1.00 12.63  ? 259 THR D C   1 
ATOM   8470 O  O   . THR D  1 259 ? 4.733   -7.688  -20.250 1.00 15.10  ? 259 THR D O   1 
ATOM   8471 C  CB  . THR D  1 259 ? 6.900   -8.276  -22.608 1.00 14.71  ? 259 THR D CB  1 
ATOM   8472 O  OG1 . THR D  1 259 ? 7.289   -8.928  -21.406 1.00 15.28  ? 259 THR D OG1 1 
ATOM   8473 C  CG2 . THR D  1 259 ? 8.109   -7.804  -23.355 1.00 15.33  ? 259 THR D CG2 1 
ATOM   8474 N  N   . SER D  1 260 ? 3.781   -7.822  -22.299 1.00 13.11  ? 260 SER D N   1 
ATOM   8475 C  CA  . SER D  1 260 ? 2.505   -8.368  -21.787 1.00 15.01  ? 260 SER D CA  1 
ATOM   8476 C  C   . SER D  1 260 ? 2.521   -9.908  -21.814 1.00 17.29  ? 260 SER D C   1 
ATOM   8477 O  O   . SER D  1 260 ? 1.535   -10.554 -21.430 1.00 24.34  ? 260 SER D O   1 
ATOM   8478 C  CB  . SER D  1 260 ? 1.342   -7.851  -22.590 1.00 17.93  ? 260 SER D CB  1 
ATOM   8479 O  OG  . SER D  1 260 ? 1.468   -8.386  -23.928 1.00 16.00  ? 260 SER D OG  1 
ATOM   8480 N  N   . PHE D  1 261 ? 3.643   -10.502 -22.135 1.00 16.49  ? 261 PHE D N   1 
ATOM   8481 C  CA  . PHE D  1 261 ? 3.836   -11.936 -22.236 1.00 18.55  ? 261 PHE D CA  1 
ATOM   8482 C  C   . PHE D  1 261 ? 5.080   -12.240 -21.494 1.00 21.14  ? 261 PHE D C   1 
ATOM   8483 O  O   . PHE D  1 261 ? 5.999   -11.452 -21.384 1.00 17.59  ? 261 PHE D O   1 
ATOM   8484 C  CB  . PHE D  1 261 ? 3.918   -12.461 -23.713 1.00 19.73  ? 261 PHE D CB  1 
ATOM   8485 C  CG  . PHE D  1 261 ? 4.954   -11.711 -24.508 1.00 17.76  ? 261 PHE D CG  1 
ATOM   8486 C  CD1 . PHE D  1 261 ? 4.691   -10.453 -25.106 1.00 16.70  ? 261 PHE D CD1 1 
ATOM   8487 C  CD2 . PHE D  1 261 ? 6.265   -12.233 -24.668 1.00 19.24  ? 261 PHE D CD2 1 
ATOM   8488 C  CE1 . PHE D  1 261 ? 5.701   -9.859  -25.844 1.00 16.09  ? 261 PHE D CE1 1 
ATOM   8489 C  CE2 . PHE D  1 261 ? 7.270   -11.631 -25.435 1.00 20.18  ? 261 PHE D CE2 1 
ATOM   8490 C  CZ  . PHE D  1 261 ? 6.943   -10.385 -26.029 1.00 16.86  ? 261 PHE D CZ  1 
ATOM   8491 N  N   . SER D  1 262 ? 4.941   -13.353 -20.789 1.00 32.72  ? 262 SER D N   1 
ATOM   8492 C  CA  . SER D  1 262 ? 6.130   -13.745 -19.998 1.00 40.00  ? 262 SER D CA  1 
ATOM   8493 C  C   . SER D  1 262 ? 6.892   -14.759 -20.775 1.00 57.33  ? 262 SER D C   1 
ATOM   8494 O  O   . SER D  1 262 ? 8.104   -14.961 -20.546 1.00 63.50  ? 262 SER D O   1 
ATOM   8495 C  CB  . SER D  1 262 ? 5.823   -14.213 -18.559 1.00 51.01  ? 262 SER D CB  1 
ATOM   8496 O  OG  . SER D  1 262 ? 4.662   -15.064 -18.476 1.00 50.07  ? 262 SER D OG  1 
ATOM   8497 N  N   . GLN D  1 263 ? 6.242   -15.429 -21.691 1.00 45.61  ? 263 GLN D N   1 
ATOM   8498 C  CA  . GLN D  1 263 ? 6.919   -16.534 -22.344 1.00 66.24  ? 263 GLN D CA  1 
ATOM   8499 C  C   . GLN D  1 263 ? 6.452   -16.681 -23.794 1.00 74.45  ? 263 GLN D C   1 
ATOM   8500 O  O   . GLN D  1 263 ? 7.125   -17.139 -24.658 1.00 69.72  ? 263 GLN D O   1 
ATOM   8501 O  OXT . GLN D  1 263 ? 5.332   -16.160 -24.127 1.00 73.16  ? 263 GLN D OXT 1 
HETATM 8502 ZN ZN  . ZN  E  2 .   ? 22.954  0.640   12.309  1.00 9.17   ? 301 ZN  A ZN  1 
HETATM 8503 C  C6  A EM5 F  3 .   ? 25.725  4.079   9.292   0.50 10.24  ? 302 EM5 A C6  1 
HETATM 8504 C  C6  B EM5 F  3 .   ? 25.719  4.085   9.294   0.50 11.80  ? 302 EM5 A C6  1 
HETATM 8505 C  C7  A EM5 F  3 .   ? 26.558  5.177   9.570   0.50 10.48  ? 302 EM5 A C7  1 
HETATM 8506 C  C7  B EM5 F  3 .   ? 26.558  5.181   9.577   0.50 11.12  ? 302 EM5 A C7  1 
HETATM 8507 C  C8  A EM5 F  3 .   ? 26.449  5.811   10.804  0.50 11.85  ? 302 EM5 A C8  1 
HETATM 8508 C  C8  B EM5 F  3 .   ? 26.451  5.825   10.811  0.50 12.79  ? 302 EM5 A C8  1 
HETATM 8509 C  C9  A EM5 F  3 .   ? 25.438  5.431   11.718  0.50 11.73  ? 302 EM5 A C9  1 
HETATM 8510 C  C9  B EM5 F  3 .   ? 25.430  5.456   11.719  0.50 12.46  ? 302 EM5 A C9  1 
HETATM 8511 C  C10 A EM5 F  3 .   ? 24.604  4.370   11.361  0.50 9.89   ? 302 EM5 A C10 1 
HETATM 8512 C  C10 B EM5 F  3 .   ? 24.585  4.384   11.365  0.50 11.56  ? 302 EM5 A C10 1 
HETATM 8513 C  C12 A EM5 F  3 .   ? 25.330  6.090   13.017  0.50 12.81  ? 302 EM5 A C12 1 
HETATM 8514 C  C12 B EM5 F  3 .   ? 25.304  6.091   13.036  0.50 15.00  ? 302 EM5 A C12 1 
HETATM 8515 C  C2  A EM5 F  3 .   ? 24.700  3.688   10.194  0.50 9.81   ? 302 EM5 A C2  1 
HETATM 8516 C  C2  B EM5 F  3 .   ? 24.697  3.691   10.198  0.50 10.07  ? 302 EM5 A C2  1 
HETATM 8517 N  N5  A EM5 F  3 .   ? 22.660  2.147   11.094  0.50 9.07   ? 302 EM5 A N5  1 
HETATM 8518 N  N5  B EM5 F  3 .   ? 22.670  2.167   11.117  0.50 11.51  ? 302 EM5 A N5  1 
HETATM 8519 C  C15 A EM5 F  3 .   ? 24.123  7.345   14.625  0.50 18.22  ? 302 EM5 A C15 1 
HETATM 8520 C  C15 B EM5 F  3 .   ? 23.880  7.195   14.742  0.50 16.87  ? 302 EM5 A C15 1 
HETATM 8521 C  C16 A EM5 F  3 .   ? 23.132  6.816   15.523  0.50 20.40  ? 302 EM5 A C16 1 
HETATM 8522 C  C16 B EM5 F  3 .   ? 23.829  8.746   14.632  0.50 26.97  ? 302 EM5 A C16 1 
HETATM 8523 O  O13 A EM5 F  3 .   ? 26.338  6.147   13.814  0.50 15.88  ? 302 EM5 A O13 1 
HETATM 8524 O  O13 B EM5 F  3 .   ? 26.317  6.186   13.811  0.50 20.22  ? 302 EM5 A O13 1 
HETATM 8525 N  N14 A EM5 F  3 .   ? 24.234  6.602   13.393  0.50 12.94  ? 302 EM5 A N14 1 
HETATM 8526 N  N14 B EM5 F  3 .   ? 24.178  6.535   13.446  0.50 15.06  ? 302 EM5 A N14 1 
HETATM 8527 O  O17 A EM5 F  3 .   ? 23.707  5.701   16.116  0.50 29.07  ? 302 EM5 A O17 1 
HETATM 8528 O  O17 B EM5 F  3 .   ? 24.967  9.165   13.959  0.50 30.94  ? 302 EM5 A O17 1 
HETATM 8529 S  S1  A EM5 F  3 .   ? 23.686  2.281   9.889   0.50 9.68   ? 302 EM5 A S1  1 
HETATM 8530 S  S1  B EM5 F  3 .   ? 23.687  2.281   9.890   0.50 10.00  ? 302 EM5 A S1  1 
HETATM 8531 O  O4  A EM5 F  3 .   ? 22.966  2.527   8.649   0.50 9.43   ? 302 EM5 A O4  1 
HETATM 8532 O  O4  B EM5 F  3 .   ? 22.967  2.528   8.652   0.50 9.81   ? 302 EM5 A O4  1 
HETATM 8533 O  O3  A EM5 F  3 .   ? 24.603  1.169   9.908   0.50 9.91   ? 302 EM5 A O3  1 
HETATM 8534 O  O3  B EM5 F  3 .   ? 24.602  1.169   9.906   0.50 10.34  ? 302 EM5 A O3  1 
HETATM 8535 CL CL1 A EM5 F  3 .   ? 25.920  3.298   7.784   0.50 11.07  ? 302 EM5 A CL1 1 
HETATM 8536 CL CL1 B EM5 F  3 .   ? 25.921  3.300   7.786   0.50 11.69  ? 302 EM5 A CL1 1 
HETATM 8537 N  N18 A EM5 F  3 .   ? 27.238  6.918   11.096  0.50 15.12  ? 302 EM5 A N18 1 
HETATM 8538 N  N18 B EM5 F  3 .   ? 27.243  6.940   11.101  0.50 15.48  ? 302 EM5 A N18 1 
HETATM 8539 C  C19 A EM5 F  3 .   ? 28.207  7.471   10.138  0.50 16.34  ? 302 EM5 A C19 1 
HETATM 8540 C  C19 B EM5 F  3 .   ? 28.206  7.473   10.115  0.50 17.15  ? 302 EM5 A C19 1 
HETATM 8541 C  C23 A EM5 F  3 .   ? 28.514  8.896   10.543  0.50 18.03  ? 302 EM5 A C23 1 
HETATM 8542 C  C23 B EM5 F  3 .   ? 28.462  8.932   10.454  0.50 21.07  ? 302 EM5 A C23 1 
HETATM 8543 C  C24 A EM5 F  3 .   ? 29.513  9.556   9.675   0.50 21.03  ? 302 EM5 A C24 1 
HETATM 8544 C  C24 B EM5 F  3 .   ? 29.631  9.551   9.778   0.50 20.78  ? 302 EM5 A C24 1 
HETATM 8545 C  C22 A EM5 F  3 .   ? 30.776  8.741   9.614   0.50 19.44  ? 302 EM5 A C22 1 
HETATM 8546 C  C22 B EM5 F  3 .   ? 30.851  8.708   9.771   0.50 22.24  ? 302 EM5 A C22 1 
HETATM 8547 C  C21 A EM5 F  3 .   ? 30.486  7.288   9.222   0.50 18.85  ? 302 EM5 A C21 1 
HETATM 8548 C  C21 B EM5 F  3 .   ? 30.533  7.295   9.302   0.50 24.22  ? 302 EM5 A C21 1 
HETATM 8549 C  C20 A EM5 F  3 .   ? 29.492  6.647   10.153  0.50 17.88  ? 302 EM5 A C20 1 
HETATM 8550 C  C20 B EM5 F  3 .   ? 29.500  6.665   10.187  0.50 20.72  ? 302 EM5 A C20 1 
HETATM 8551 C  C1  . EDO G  4 .   ? 24.460  9.497   -4.186  1.00 62.92  ? 303 EDO A C1  1 
HETATM 8552 O  O1  . EDO G  4 .   ? 24.693  8.155   -3.728  1.00 57.53  ? 303 EDO A O1  1 
HETATM 8553 C  C2  . EDO G  4 .   ? 25.516  10.456  -3.660  1.00 45.92  ? 303 EDO A C2  1 
HETATM 8554 O  O2  . EDO G  4 .   ? 24.867  11.211  -2.669  1.00 49.05  ? 303 EDO A O2  1 
HETATM 8555 C  C1  . PEG H  5 .   ? 27.160  12.099  7.646   1.00 41.44  ? 304 PEG A C1  1 
HETATM 8556 O  O1  . PEG H  5 .   ? 26.190  11.953  6.519   1.00 27.91  ? 304 PEG A O1  1 
HETATM 8557 C  C2  . PEG H  5 .   ? 26.979  12.614  9.131   1.00 29.86  ? 304 PEG A C2  1 
HETATM 8558 O  O2  . PEG H  5 .   ? 26.418  11.888  10.300  1.00 51.76  ? 304 PEG A O2  1 
HETATM 8559 C  C3  . PEG H  5 .   ? 26.875  12.593  11.474  1.00 76.67  ? 304 PEG A C3  1 
HETATM 8560 C  C4  . PEG H  5 .   ? 26.542  11.907  12.800  1.00 75.35  ? 304 PEG A C4  1 
HETATM 8561 O  O4  . PEG H  5 .   ? 27.754  11.655  13.567  1.00 63.60  ? 304 PEG A O4  1 
HETATM 8562 C  C1  . EDO I  4 .   ? 45.470  -5.900  13.507  1.00 25.31  ? 305 EDO A C1  1 
HETATM 8563 O  O1  . EDO I  4 .   ? 45.406  -7.278  13.034  1.00 42.44  ? 305 EDO A O1  1 
HETATM 8564 C  C2  . EDO I  4 .   ? 44.249  -5.448  12.827  1.00 29.96  ? 305 EDO A C2  1 
HETATM 8565 O  O2  . EDO I  4 .   ? 43.601  -4.196  12.868  1.00 22.07  ? 305 EDO A O2  1 
HETATM 8566 ZN ZN  . ZN  J  2 .   ? -8.070  3.605   4.901   1.00 7.83   ? 301 ZN  B ZN  1 
HETATM 8567 C  C6  A EM5 K  3 .   ? -10.036 7.559   7.837   0.50 8.62   ? 302 EM5 B C6  1 
HETATM 8568 C  C6  B EM5 K  3 .   ? -10.031 7.556   7.841   0.50 10.31  ? 302 EM5 B C6  1 
HETATM 8569 C  C7  A EM5 K  3 .   ? -10.693 8.763   7.600   0.50 9.31   ? 302 EM5 B C7  1 
HETATM 8570 C  C7  B EM5 K  3 .   ? -10.690 8.756   7.609   0.50 11.17  ? 302 EM5 B C7  1 
HETATM 8571 C  C8  A EM5 K  3 .   ? -10.527 9.374   6.371   0.50 9.53   ? 302 EM5 B C8  1 
HETATM 8572 C  C8  B EM5 K  3 .   ? -10.525 9.386   6.387   0.50 11.90  ? 302 EM5 B C8  1 
HETATM 8573 C  C9  A EM5 K  3 .   ? -9.674  8.782   5.406   0.50 9.71   ? 302 EM5 B C9  1 
HETATM 8574 C  C9  B EM5 K  3 .   ? -9.659  8.809   5.427   0.50 11.99  ? 302 EM5 B C9  1 
HETATM 8575 C  C10 A EM5 K  3 .   ? -8.985  7.629   5.701   0.50 9.99   ? 302 EM5 B C10 1 
HETATM 8576 C  C10 B EM5 K  3 .   ? -8.975  7.640   5.712   0.50 10.65  ? 302 EM5 B C10 1 
HETATM 8577 C  C12 A EM5 K  3 .   ? -9.522  9.404   4.075   0.50 12.24  ? 302 EM5 B C12 1 
HETATM 8578 C  C12 B EM5 K  3 .   ? -9.511  9.386   4.084   0.50 13.80  ? 302 EM5 B C12 1 
HETATM 8579 C  C2  A EM5 K  3 .   ? -9.126  6.985   6.938   0.50 8.67   ? 302 EM5 B C2  1 
HETATM 8580 C  C2  B EM5 K  3 .   ? -9.123  6.987   6.941   0.50 9.17   ? 302 EM5 B C2  1 
HETATM 8581 N  N5  A EM5 K  3 .   ? -7.477  5.098   6.016   0.50 11.14  ? 302 EM5 B N5  1 
HETATM 8582 N  N5  B EM5 K  3 .   ? -7.441  5.083   5.989   0.50 7.09   ? 302 EM5 B N5  1 
HETATM 8583 C  C15 A EM5 K  3 .   ? -8.036  10.413  2.417   0.50 18.17  ? 302 EM5 B C15 1 
HETATM 8584 C  C15 B EM5 K  3 .   ? -7.939  10.149  2.317   0.50 15.64  ? 302 EM5 B C15 1 
HETATM 8585 C  C16 A EM5 K  3 .   ? -7.282  9.532   1.556   0.50 16.59  ? 302 EM5 B C16 1 
HETATM 8586 C  C16 B EM5 K  3 .   ? -7.629  11.631  2.461   0.50 17.65  ? 302 EM5 B C16 1 
HETATM 8587 O  O13 A EM5 K  3 .   ? -10.523 9.627   3.347   0.50 13.75  ? 302 EM5 B O13 1 
HETATM 8588 O  O13 B EM5 K  3 .   ? -10.544 9.678   3.400   0.50 20.17  ? 302 EM5 B O13 1 
HETATM 8589 N  N14 A EM5 K  3 .   ? -8.302  9.667   3.657   0.50 12.19  ? 302 EM5 B N14 1 
HETATM 8590 N  N14 B EM5 K  3 .   ? -8.288  9.571   3.622   0.50 13.23  ? 302 EM5 B N14 1 
HETATM 8591 O  O17 A EM5 K  3 .   ? -8.180  8.630   1.077   0.50 23.45  ? 302 EM5 B O17 1 
HETATM 8592 O  O17 B EM5 K  3 .   ? -7.650  11.997  1.165   0.50 27.04  ? 302 EM5 B O17 1 
HETATM 8593 S  S1  A EM5 K  3 .   ? -8.376  5.430   7.251   0.50 8.20   ? 302 EM5 B S1  1 
HETATM 8594 S  S1  B EM5 K  3 .   ? -8.373  5.431   7.252   0.50 8.85   ? 302 EM5 B S1  1 
HETATM 8595 O  O4  A EM5 K  3 .   ? -7.573  5.609   8.437   0.50 8.53   ? 302 EM5 B O4  1 
HETATM 8596 O  O4  B EM5 K  3 .   ? -7.572  5.609   8.437   0.50 9.01   ? 302 EM5 B O4  1 
HETATM 8597 O  O3  A EM5 K  3 .   ? -9.462  4.498   7.341   0.50 9.75   ? 302 EM5 B O3  1 
HETATM 8598 O  O3  B EM5 K  3 .   ? -9.470  4.490   7.340   0.50 8.71   ? 302 EM5 B O3  1 
HETATM 8599 CL CL1 A EM5 K  3 .   ? -10.307 6.878   9.422   0.50 9.62   ? 302 EM5 B CL1 1 
HETATM 8600 CL CL1 B EM5 K  3 .   ? -10.300 6.874   9.426   0.50 11.62  ? 302 EM5 B CL1 1 
HETATM 8601 N  N18 A EM5 K  3 .   ? -11.143 10.575  6.046   0.50 13.18  ? 302 EM5 B N18 1 
HETATM 8602 N  N18 B EM5 K  3 .   ? -11.145 10.594  6.083   0.50 15.26  ? 302 EM5 B N18 1 
HETATM 8603 C  C19 A EM5 K  3 .   ? -12.004 11.271  6.965   0.50 14.05  ? 302 EM5 B C19 1 
HETATM 8604 C  C19 B EM5 K  3 .   ? -11.965 11.270  7.060   0.50 18.31  ? 302 EM5 B C19 1 
HETATM 8605 C  C23 A EM5 K  3 .   ? -12.071 12.777  6.556   0.50 16.67  ? 302 EM5 B C23 1 
HETATM 8606 C  C23 B EM5 K  3 .   ? -11.985 12.785  6.679   0.50 21.11  ? 302 EM5 B C23 1 
HETATM 8607 C  C24 A EM5 K  3 .   ? -13.026 13.492  7.453   0.50 15.07  ? 302 EM5 B C24 1 
HETATM 8608 C  C24 B EM5 K  3 .   ? -12.954 13.498  7.543   0.50 22.07  ? 302 EM5 B C24 1 
HETATM 8609 C  C22 A EM5 K  3 .   ? -14.405 12.893  7.422   0.50 15.56  ? 302 EM5 B C22 1 
HETATM 8610 C  C22 B EM5 K  3 .   ? -14.343 12.906  7.489   0.50 21.38  ? 302 EM5 B C22 1 
HETATM 8611 C  C21 A EM5 K  3 .   ? -14.312 11.401  7.849   0.50 18.79  ? 302 EM5 B C21 1 
HETATM 8612 C  C21 B EM5 K  3 .   ? -14.266 11.436  7.937   0.50 21.99  ? 302 EM5 B C21 1 
HETATM 8613 C  C20 A EM5 K  3 .   ? -13.406 10.672  6.888   0.50 15.13  ? 302 EM5 B C20 1 
HETATM 8614 C  C20 B EM5 K  3 .   ? -13.368 10.664  7.000   0.50 18.42  ? 302 EM5 B C20 1 
HETATM 8615 C  C1  . EDO L  4 .   ? -16.424 -13.444 2.376   1.00 23.47  ? 303 EDO B C1  1 
HETATM 8616 O  O1  . EDO L  4 .   ? -17.357 -12.675 3.319   1.00 22.40  ? 303 EDO B O1  1 
HETATM 8617 C  C2  . EDO L  4 .   ? -15.694 -14.577 3.232   1.00 31.77  ? 303 EDO B C2  1 
HETATM 8618 O  O2  . EDO L  4 .   ? -16.221 -14.736 4.563   1.00 51.38  ? 303 EDO B O2  1 
HETATM 8619 C  C1  . EDO M  4 .   ? -17.478 -3.791  21.575  1.00 68.16  ? 304 EDO B C1  1 
HETATM 8620 O  O1  . EDO M  4 .   ? -16.343 -3.739  20.589  1.00 22.49  ? 304 EDO B O1  1 
HETATM 8621 C  C2  . EDO M  4 .   ? -17.061 -3.430  23.049  1.00 50.17  ? 304 EDO B C2  1 
HETATM 8622 O  O2  . EDO M  4 .   ? -16.016 -2.423  23.062  1.00 49.91  ? 304 EDO B O2  1 
HETATM 8623 C  C1  . EDO N  4 .   ? -4.227  1.688   24.092  1.00 30.55  ? 305 EDO B C1  1 
HETATM 8624 O  O1  . EDO N  4 .   ? -4.444  3.132   24.367  1.00 62.63  ? 305 EDO B O1  1 
HETATM 8625 C  C2  . EDO N  4 .   ? -3.342  1.049   25.161  1.00 21.18  ? 305 EDO B C2  1 
HETATM 8626 O  O2  . EDO N  4 .   ? -2.671  -0.279  25.042  1.00 28.41  ? 305 EDO B O2  1 
HETATM 8627 C  C1  . EDO O  4 .   ? -12.874 11.616  2.590   1.00 40.33  ? 306 EDO B C1  1 
HETATM 8628 O  O1  . EDO O  4 .   ? -14.196 11.137  3.413   1.00 25.16  ? 306 EDO B O1  1 
HETATM 8629 C  C2  . EDO O  4 .   ? -11.855 11.205  1.368   1.00 24.14  ? 306 EDO B C2  1 
HETATM 8630 O  O2  . EDO O  4 .   ? -12.243 12.167  0.262   1.00 26.10  ? 306 EDO B O2  1 
HETATM 8631 ZN ZN  . ZN  P  2 .   ? 37.375  2.633   -30.951 1.00 13.41  ? 301 ZN  C ZN  1 
HETATM 8632 C  C6  . EM5 Q  3 .   ? 40.194  6.103   -33.916 1.00 15.46  ? 302 EM5 C C6  1 
HETATM 8633 C  C7  . EM5 Q  3 .   ? 41.032  7.162   -33.661 1.00 17.55  ? 302 EM5 C C7  1 
HETATM 8634 C  C8  . EM5 Q  3 .   ? 40.830  7.853   -32.418 1.00 16.92  ? 302 EM5 C C8  1 
HETATM 8635 C  C9  . EM5 Q  3 .   ? 39.839  7.456   -31.548 1.00 16.13  ? 302 EM5 C C9  1 
HETATM 8636 C  C10 . EM5 Q  3 .   ? 39.023  6.377   -31.853 1.00 14.59  ? 302 EM5 C C10 1 
HETATM 8637 C  C12 . EM5 Q  3 .   ? 39.697  8.112   -30.234 1.00 17.98  ? 302 EM5 C C12 1 
HETATM 8638 C  C2  . EM5 Q  3 .   ? 39.170  5.645   -33.043 1.00 14.78  ? 302 EM5 C C2  1 
HETATM 8639 N  N5  . EM5 Q  3 .   ? 37.085  4.141   -32.179 1.00 12.74  ? 302 EM5 C N5  1 
HETATM 8640 C  C15 . EM5 Q  3 .   ? 38.274  9.141   -28.484 1.00 29.02  ? 302 EM5 C C15 1 
HETATM 8641 C  C16 . EM5 Q  3 .   ? 38.955  10.454  -28.087 1.00 44.13  ? 302 EM5 C C16 1 
HETATM 8642 O  O13 . EM5 Q  3 .   ? 40.710  8.195   -29.425 1.00 23.69  ? 302 EM5 C O13 1 
HETATM 8643 N  N14 . EM5 Q  3 .   ? 38.574  8.456   -29.788 1.00 21.51  ? 302 EM5 C N14 1 
HETATM 8644 O  O17 . EM5 Q  3 .   ? 38.971  11.338  -29.177 1.00 47.85  ? 302 EM5 C O17 1 
HETATM 8645 S  S1  . EM5 Q  3 .   ? 38.145  4.269   -33.379 1.00 13.24  ? 302 EM5 C S1  1 
HETATM 8646 O  O4  . EM5 Q  3 .   ? 37.479  4.451   -34.629 1.00 12.72  ? 302 EM5 C O4  1 
HETATM 8647 O  O3  . EM5 Q  3 .   ? 38.930  3.176   -33.333 1.00 13.56  ? 302 EM5 C O3  1 
HETATM 8648 CL CL1 . EM5 Q  3 .   ? 40.434  5.260   -35.424 1.00 15.86  ? 302 EM5 C CL1 1 
HETATM 8649 N  N18 . EM5 Q  3 .   ? 41.600  8.975   -32.132 1.00 20.02  ? 302 EM5 C N18 1 
HETATM 8650 C  C19 . EM5 Q  3 .   ? 42.601  9.635   -32.962 1.00 21.37  ? 302 EM5 C C19 1 
HETATM 8651 C  C23 . EM5 Q  3 .   ? 42.899  11.061  -32.412 1.00 27.87  ? 302 EM5 C C23 1 
HETATM 8652 C  C24 . EM5 Q  3 .   ? 43.902  11.677  -33.359 1.00 24.12  ? 302 EM5 C C24 1 
HETATM 8653 C  C22 . EM5 Q  3 .   ? 45.182  10.863  -33.319 1.00 27.25  ? 302 EM5 C C22 1 
HETATM 8654 C  C21 . EM5 Q  3 .   ? 44.921  9.462   -33.838 1.00 25.94  ? 302 EM5 C C21 1 
HETATM 8655 C  C20 . EM5 Q  3 .   ? 43.859  8.756   -32.948 1.00 23.60  ? 302 EM5 C C20 1 
HETATM 8656 C  C1  . EDO R  4 .   ? 39.861  17.447  -36.758 1.00 37.67  ? 303 EDO C C1  1 
HETATM 8657 O  O1  . EDO R  4 .   ? 40.649  16.276  -36.817 1.00 32.76  ? 303 EDO C O1  1 
HETATM 8658 C  C2  . EDO R  4 .   ? 39.422  17.568  -38.172 1.00 20.84  ? 303 EDO C C2  1 
HETATM 8659 O  O2  . EDO R  4 .   ? 38.445  16.703  -38.543 1.00 25.45  ? 303 EDO C O2  1 
HETATM 8660 ZN ZN  . ZN  S  2 .   ? 6.559   5.605   -38.601 1.00 9.12   ? 301 ZN  D ZN  1 
HETATM 8661 C  C6  . EM5 T  3 .   ? 4.669   9.711   -35.756 1.00 10.85  ? 302 EM5 D C6  1 
HETATM 8662 C  C7  . EM5 T  3 .   ? 4.006   10.892  -36.111 1.00 11.72  ? 302 EM5 D C7  1 
HETATM 8663 C  C8  . EM5 T  3 .   ? 4.216   11.439  -37.376 1.00 12.38  ? 302 EM5 D C8  1 
HETATM 8664 C  C9  . EM5 T  3 .   ? 5.064   10.806  -38.279 1.00 11.55  ? 302 EM5 D C9  1 
HETATM 8665 C  C10 . EM5 T  3 .   ? 5.705   9.667   -37.922 1.00 11.49  ? 302 EM5 D C10 1 
HETATM 8666 C  C12 . EM5 T  3 .   ? 5.275   11.347  -39.640 1.00 13.64  ? 302 EM5 D C12 1 
HETATM 8667 C  C2  . EM5 T  3 .   ? 5.564   9.076   -36.657 1.00 10.72  ? 302 EM5 D C2  1 
HETATM 8668 N  N5  . EM5 T  3 .   ? 7.224   7.101   -37.525 1.00 10.30  ? 302 EM5 D N5  1 
HETATM 8669 C  C15 . EM5 T  3 .   ? 6.834   12.121  -41.379 1.00 18.24  ? 302 EM5 D C15 1 
HETATM 8670 C  C16 . EM5 T  3 .   ? 7.351   13.518  -41.234 1.00 31.57  ? 302 EM5 D C16 1 
HETATM 8671 O  O13 . EM5 T  3 .   ? 4.261   11.550  -40.354 1.00 18.48  ? 302 EM5 D O13 1 
HETATM 8672 N  N14 . EM5 T  3 .   ? 6.476   11.562  -40.051 1.00 14.48  ? 302 EM5 D N14 1 
HETATM 8673 O  O17 . EM5 T  3 .   ? 6.392   14.308  -40.762 1.00 34.24  ? 302 EM5 D O17 1 
HETATM 8674 S  S1  . EM5 T  3 .   ? 6.285   7.497   -36.274 1.00 9.94   ? 302 EM5 D S1  1 
HETATM 8675 O  O4  . EM5 T  3 .   ? 7.116   7.696   -35.082 1.00 10.06  ? 302 EM5 D O4  1 
HETATM 8676 O  O3  . EM5 T  3 .   ? 5.176   6.576   -36.168 1.00 10.60  ? 302 EM5 D O3  1 
HETATM 8677 CL CL1 . EM5 T  3 .   ? 4.389   9.039   -34.177 1.00 11.95  ? 302 EM5 D CL1 1 
HETATM 8678 N  N18 . EM5 T  3 .   ? 3.564   12.652  -37.733 1.00 15.25  ? 302 EM5 D N18 1 
HETATM 8679 C  C19 . EM5 T  3 .   ? 2.766   13.388  -36.786 1.00 15.90  ? 302 EM5 D C19 1 
HETATM 8680 C  C23 . EM5 T  3 .   ? 2.714   14.850  -37.330 1.00 16.87  ? 302 EM5 D C23 1 
HETATM 8681 C  C24 . EM5 T  3 .   ? 1.763   15.673  -36.447 1.00 18.59  ? 302 EM5 D C24 1 
HETATM 8682 C  C22 . EM5 T  3 .   ? 0.372   15.091  -36.439 1.00 17.98  ? 302 EM5 D C22 1 
HETATM 8683 C  C21 . EM5 T  3 .   ? 0.459   13.646  -35.859 1.00 22.83  ? 302 EM5 D C21 1 
HETATM 8684 C  C20 . EM5 T  3 .   ? 1.334   12.801  -36.782 1.00 17.44  ? 302 EM5 D C20 1 
HETATM 8685 C  C1  . EDO U  4 .   ? 17.108  -11.246 -27.369 1.00 18.17  ? 303 EDO D C1  1 
HETATM 8686 O  O1  . EDO U  4 .   ? 16.085  -12.122 -26.982 1.00 58.18  ? 303 EDO D O1  1 
HETATM 8687 C  C2  . EDO U  4 .   ? 18.276  -12.012 -27.270 1.00 22.26  ? 303 EDO D C2  1 
HETATM 8688 O  O2  . EDO U  4 .   ? 19.503  -11.268 -27.607 1.00 37.64  ? 303 EDO D O2  1 
HETATM 8689 C  C1  . EDO V  4 .   ? -2.384  -1.256  -20.409 1.00 37.40  ? 304 EDO D C1  1 
HETATM 8690 O  O1  . EDO V  4 .   ? -1.438  -0.067  -20.391 1.00 37.30  ? 304 EDO D O1  1 
HETATM 8691 C  C2  . EDO V  4 .   ? -2.869  -1.221  -21.890 1.00 26.65  ? 304 EDO D C2  1 
HETATM 8692 O  O2  . EDO V  4 .   ? -1.842  -1.416  -22.791 1.00 21.66  ? 304 EDO D O2  1 
HETATM 8693 C  C1  . EDO W  4 .   ? 8.546   20.837  -33.212 1.00 42.72  ? 305 EDO D C1  1 
HETATM 8694 O  O1  . EDO W  4 .   ? 8.899   20.098  -32.027 1.00 25.43  ? 305 EDO D O1  1 
HETATM 8695 C  C2  . EDO W  4 .   ? 7.115   20.594  -33.755 1.00 37.09  ? 305 EDO D C2  1 
HETATM 8696 O  O2  . EDO W  4 .   ? 6.253   19.684  -33.046 1.00 58.68  ? 305 EDO D O2  1 
HETATM 8697 C  C1  . EDO X  4 .   ? -8.427  8.095   -56.401 1.00 44.76  ? 306 EDO D C1  1 
HETATM 8698 O  O1  . EDO X  4 .   ? -8.635  9.447   -55.806 1.00 31.19  ? 306 EDO D O1  1 
HETATM 8699 C  C2  . EDO X  4 .   ? -7.866  8.285   -57.802 1.00 64.18  ? 306 EDO D C2  1 
HETATM 8700 O  O2  . EDO X  4 .   ? -6.488  7.885   -57.750 1.00 44.36  ? 306 EDO D O2  1 
HETATM 8701 C  C1  . PEG Y  5 .   ? 12.025  3.241   -17.856 1.00 49.81  ? 307 PEG D C1  1 
HETATM 8702 O  O1  . PEG Y  5 .   ? 11.995  1.879   -18.113 1.00 27.16  ? 307 PEG D O1  1 
HETATM 8703 C  C2  . PEG Y  5 .   ? 10.548  3.460   -17.953 1.00 48.87  ? 307 PEG D C2  1 
HETATM 8704 O  O2  . PEG Y  5 .   ? 10.293  3.970   -19.290 1.00 38.00  ? 307 PEG D O2  1 
HETATM 8705 C  C3  . PEG Y  5 .   ? 9.947   5.414   -19.288 1.00 63.76  ? 307 PEG D C3  1 
HETATM 8706 C  C4  . PEG Y  5 .   ? 10.860  6.474   -18.611 1.00 59.82  ? 307 PEG D C4  1 
HETATM 8707 O  O4  . PEG Y  5 .   ? 12.133  6.491   -19.218 1.00 59.21  ? 307 PEG D O4  1 
HETATM 8708 C  C1  . EDO Z  4 .   ? 21.995  2.227   -23.738 1.00 34.95  ? 308 EDO D C1  1 
HETATM 8709 O  O1  . EDO Z  4 .   ? 22.029  3.708   -23.546 1.00 28.16  ? 308 EDO D O1  1 
HETATM 8710 C  C2  . EDO Z  4 .   ? 21.998  1.705   -25.174 1.00 26.78  ? 308 EDO D C2  1 
HETATM 8711 O  O2  . EDO Z  4 .   ? 21.264  0.672   -25.893 1.00 31.66  ? 308 EDO D O2  1 
HETATM 8712 O  O   . HOH AA 6 .   ? 23.247  3.764   15.211  1.00 21.47  ? 401 HOH A O   1 
HETATM 8713 O  O   . HOH AA 6 .   ? 44.956  1.576   12.258  1.00 40.53  ? 402 HOH A O   1 
HETATM 8714 O  O   . HOH AA 6 .   ? 13.569  -14.845 29.515  1.00 32.45  ? 403 HOH A O   1 
HETATM 8715 O  O   . HOH AA 6 .   ? 22.532  7.246   -4.164  1.00 39.72  ? 404 HOH A O   1 
HETATM 8716 O  O   . HOH AA 6 .   ? 25.826  4.596   16.373  1.00 25.66  ? 405 HOH A O   1 
HETATM 8717 O  O   . HOH AA 6 .   ? 28.651  8.836   17.699  1.00 38.42  ? 406 HOH A O   1 
HETATM 8718 O  O   . HOH AA 6 .   ? 12.072  16.443  15.327  1.00 35.92  ? 407 HOH A O   1 
HETATM 8719 O  O   . HOH AA 6 .   ? 43.275  -5.743  0.948   1.00 36.53  ? 408 HOH A O   1 
HETATM 8720 O  O   . HOH AA 6 .   ? 43.140  6.243   9.567   1.00 50.12  ? 409 HOH A O   1 
HETATM 8721 O  O   . HOH AA 6 .   ? 42.880  -10.100 19.150  1.00 28.98  ? 410 HOH A O   1 
HETATM 8722 O  O   . HOH AA 6 .   ? 41.654  6.090   5.266   1.00 29.52  ? 411 HOH A O   1 
HETATM 8723 O  O   . HOH AA 6 .   ? 6.029   -3.549  21.058  1.00 31.89  ? 412 HOH A O   1 
HETATM 8724 O  O   . HOH AA 6 .   ? 14.541  -9.995  26.066  1.00 16.75  ? 413 HOH A O   1 
HETATM 8725 O  O   . HOH AA 6 .   ? 24.831  9.476   11.402  1.00 34.59  ? 414 HOH A O   1 
HETATM 8726 O  O   . HOH AA 6 .   ? 14.490  4.728   23.934  1.00 27.16  ? 415 HOH A O   1 
HETATM 8727 O  O   . HOH AA 6 .   ? 17.941  3.197   12.860  1.00 11.75  ? 416 HOH A O   1 
HETATM 8728 O  O   . HOH AA 6 .   ? 10.732  12.460  20.476  1.00 28.89  ? 417 HOH A O   1 
HETATM 8729 O  O   . HOH AA 6 .   ? 34.000  1.594   -5.907  1.00 71.50  ? 418 HOH A O   1 
HETATM 8730 O  O   . HOH AA 6 .   ? 6.402   15.811  16.036  1.00 34.22  ? 419 HOH A O   1 
HETATM 8731 O  O   . HOH AA 6 .   ? 17.715  7.927   19.605  1.00 29.39  ? 420 HOH A O   1 
HETATM 8732 O  O   . HOH AA 6 .   ? 32.314  -16.948 10.375  1.00 30.79  ? 421 HOH A O   1 
HETATM 8733 O  O   . HOH AA 6 .   ? 7.702   -8.210  11.840  1.00 24.46  ? 422 HOH A O   1 
HETATM 8734 O  O   . HOH AA 6 .   ? 9.497   -14.332 1.815   1.00 31.49  ? 423 HOH A O   1 
HETATM 8735 O  O   . HOH AA 6 .   ? 35.249  -1.011  30.659  1.00 31.36  ? 424 HOH A O   1 
HETATM 8736 O  O   . HOH AA 6 .   ? 35.934  -14.876 4.105   1.00 34.53  ? 425 HOH A O   1 
HETATM 8737 O  O   . HOH AA 6 .   ? 11.287  3.406   19.344  1.00 21.04  ? 426 HOH A O   1 
HETATM 8738 O  O   . HOH AA 6 .   ? 19.771  14.002  28.598  1.00 25.03  ? 427 HOH A O   1 
HETATM 8739 O  O   . HOH AA 6 .   ? 24.989  -0.183  31.849  1.00 24.83  ? 428 HOH A O   1 
HETATM 8740 O  O   . HOH AA 6 .   ? 24.359  -7.666  -7.576  1.00 43.62  ? 429 HOH A O   1 
HETATM 8741 O  O   . HOH AA 6 .   ? 23.835  -16.171 29.707  1.00 29.27  ? 430 HOH A O   1 
HETATM 8742 O  O   . HOH AA 6 .   ? 39.647  -12.630 19.940  1.00 26.05  ? 431 HOH A O   1 
HETATM 8743 O  O   . HOH AA 6 .   ? 32.936  4.997   20.135  1.00 22.73  ? 432 HOH A O   1 
HETATM 8744 O  O   . HOH AA 6 .   ? 36.984  6.181   11.433  1.00 21.83  ? 433 HOH A O   1 
HETATM 8745 O  O   . HOH AA 6 .   ? 29.294  -16.874 14.945  1.00 25.80  ? 434 HOH A O   1 
HETATM 8746 O  O   . HOH AA 6 .   ? 18.067  -15.152 6.289   1.00 20.70  ? 435 HOH A O   1 
HETATM 8747 O  O   . HOH AA 6 .   ? 18.366  -3.138  -5.701  1.00 26.56  ? 436 HOH A O   1 
HETATM 8748 O  O   . HOH AA 6 .   ? 45.152  -4.572  7.540   1.00 27.92  ? 437 HOH A O   1 
HETATM 8749 O  O   . HOH AA 6 .   ? 19.354  9.759   32.430  1.00 20.64  ? 438 HOH A O   1 
HETATM 8750 O  O   . HOH AA 6 .   ? 10.284  4.766   8.762   1.00 12.95  ? 439 HOH A O   1 
HETATM 8751 O  O   . HOH AA 6 .   ? 41.984  2.269   0.856   1.00 17.75  ? 440 HOH A O   1 
HETATM 8752 O  O   . HOH AA 6 .   ? 39.420  -15.681 16.987  1.00 30.30  ? 441 HOH A O   1 
HETATM 8753 O  O   . HOH AA 6 .   ? 10.625  6.238   15.419  1.00 13.49  ? 442 HOH A O   1 
HETATM 8754 O  O   . HOH AA 6 .   ? 11.627  2.283   -6.722  1.00 32.36  ? 443 HOH A O   1 
HETATM 8755 O  O   . HOH AA 6 .   ? 26.172  2.769   -2.514  1.00 26.80  ? 444 HOH A O   1 
HETATM 8756 O  O   . HOH AA 6 .   ? 45.180  -1.124  14.369  1.00 34.85  ? 445 HOH A O   1 
HETATM 8757 O  O   . HOH AA 6 .   ? 25.650  -18.538 12.603  1.00 25.32  ? 446 HOH A O   1 
HETATM 8758 O  O   . HOH AA 6 .   ? 27.698  14.895  -1.232  1.00 43.25  ? 447 HOH A O   1 
HETATM 8759 O  O   . HOH AA 6 .   ? 32.943  6.939   15.735  1.00 27.32  ? 448 HOH A O   1 
HETATM 8760 O  O   . HOH AA 6 .   ? 12.770  -12.332 16.547  1.00 22.32  ? 449 HOH A O   1 
HETATM 8761 O  O   . HOH AA 6 .   ? 10.486  -3.342  2.788   1.00 14.33  ? 450 HOH A O   1 
HETATM 8762 O  O   . HOH AA 6 .   ? 10.807  -4.565  -5.220  1.00 25.67  ? 451 HOH A O   1 
HETATM 8763 O  O   . HOH AA 6 .   ? 15.255  -6.870  21.186  1.00 13.01  ? 452 HOH A O   1 
HETATM 8764 O  O   . HOH AA 6 .   ? 11.448  5.297   2.276   1.00 12.29  ? 453 HOH A O   1 
HETATM 8765 O  O   . HOH AA 6 .   ? 7.494   -6.762  2.460   1.00 26.78  ? 454 HOH A O   1 
HETATM 8766 O  O   . HOH AA 6 .   ? 32.346  -16.651 17.235  1.00 36.75  ? 455 HOH A O   1 
HETATM 8767 O  O   . HOH AA 6 .   ? 36.295  -7.081  26.387  1.00 22.18  ? 456 HOH A O   1 
HETATM 8768 O  O   . HOH AA 6 .   ? 33.939  -13.301 26.694  1.00 26.51  ? 457 HOH A O   1 
HETATM 8769 O  O   . HOH AA 6 .   ? 38.625  -5.673  -3.218  1.00 36.10  ? 458 HOH A O   1 
HETATM 8770 O  O   . HOH AA 6 .   ? 31.996  -16.846 20.766  1.00 35.71  ? 459 HOH A O   1 
HETATM 8771 O  O   . HOH AA 6 .   ? 31.808  5.605   32.499  1.00 35.98  ? 460 HOH A O   1 
HETATM 8772 O  O   . HOH AA 6 .   ? 15.390  -15.503 2.642   1.00 26.77  ? 461 HOH A O   1 
HETATM 8773 O  O   . HOH AA 6 .   ? 9.255   11.357  1.236   1.00 17.22  ? 462 HOH A O   1 
HETATM 8774 O  O   . HOH AA 6 .   ? 28.495  -4.221  2.591   1.00 12.31  ? 463 HOH A O   1 
HETATM 8775 O  O   . HOH AA 6 .   ? 16.761  -18.461 12.618  1.00 37.69  ? 464 HOH A O   1 
HETATM 8776 O  O   . HOH AA 6 .   ? 14.001  1.571   -0.225  1.00 16.62  ? 465 HOH A O   1 
HETATM 8777 O  O   . HOH AA 6 .   ? 17.182  0.757   -0.548  1.00 16.13  ? 466 HOH A O   1 
HETATM 8778 O  O   . HOH AA 6 .   ? 36.718  -4.439  -0.820  1.00 21.83  ? 467 HOH A O   1 
HETATM 8779 O  O   . HOH AA 6 .   ? 18.777  -6.675  -11.989 1.00 42.54  ? 468 HOH A O   1 
HETATM 8780 O  O   . HOH AA 6 .   ? 12.482  -2.654  11.047  1.00 10.74  ? 469 HOH A O   1 
HETATM 8781 O  O   . HOH AA 6 .   ? 33.119  -14.952 3.590   1.00 26.45  ? 470 HOH A O   1 
HETATM 8782 O  O   . HOH AA 6 .   ? 20.860  4.068   16.439  1.00 17.06  ? 471 HOH A O   1 
HETATM 8783 O  O   . HOH AA 6 .   ? 16.011  -12.127 26.944  1.00 19.16  ? 472 HOH A O   1 
HETATM 8784 O  O   . HOH AA 6 .   ? 28.610  2.391   -1.273  1.00 22.54  ? 473 HOH A O   1 
HETATM 8785 O  O   . HOH AA 6 .   ? 15.687  4.464   21.393  1.00 29.32  ? 474 HOH A O   1 
HETATM 8786 O  O   . HOH AA 6 .   ? 39.972  -12.217 11.690  1.00 22.71  ? 475 HOH A O   1 
HETATM 8787 O  O   . HOH AA 6 .   ? 5.582   -12.025 13.344  1.00 21.89  ? 476 HOH A O   1 
HETATM 8788 O  O   . HOH AA 6 .   ? 19.377  -18.433 26.207  1.00 29.05  ? 477 HOH A O   1 
HETATM 8789 O  O   . HOH AA 6 .   ? 13.128  14.130  14.167  1.00 24.02  ? 478 HOH A O   1 
HETATM 8790 O  O   . HOH AA 6 .   ? 32.876  6.874   12.879  1.00 23.98  ? 479 HOH A O   1 
HETATM 8791 O  O   . HOH AA 6 .   ? 12.152  -10.585 27.310  1.00 18.09  ? 480 HOH A O   1 
HETATM 8792 O  O   . HOH AA 6 .   ? 30.371  -8.895  -2.566  1.00 20.23  ? 481 HOH A O   1 
HETATM 8793 O  O   . HOH AA 6 .   ? 38.138  -7.602  24.507  1.00 25.19  ? 482 HOH A O   1 
HETATM 8794 O  O   . HOH AA 6 .   ? 19.688  -0.602  26.713  1.00 15.56  ? 483 HOH A O   1 
HETATM 8795 O  O   . HOH AA 6 .   ? 20.624  18.040  7.643   1.00 31.95  ? 484 HOH A O   1 
HETATM 8796 O  O   . HOH AA 6 .   ? 12.546  14.559  2.340   1.00 14.60  ? 485 HOH A O   1 
HETATM 8797 O  O   . HOH AA 6 .   ? 41.102  -10.458 9.821   1.00 19.65  ? 486 HOH A O   1 
HETATM 8798 O  O   . HOH AA 6 .   ? 38.591  4.027   11.332  1.00 20.78  ? 487 HOH A O   1 
HETATM 8799 O  O   . HOH AA 6 .   ? 9.524   -5.048  16.750  1.00 31.66  ? 488 HOH A O   1 
HETATM 8800 O  O   . HOH AA 6 .   ? 27.725  -21.220 24.649  1.00 34.43  ? 489 HOH A O   1 
HETATM 8801 O  O   . HOH AA 6 .   ? 8.648   2.942   7.369   1.00 10.25  ? 490 HOH A O   1 
HETATM 8802 O  O   . HOH AA 6 .   ? 27.979  -2.389  37.039  1.00 40.64  ? 491 HOH A O   1 
HETATM 8803 O  O   . HOH AA 6 .   ? 46.351  -8.872  16.289  1.00 50.24  ? 492 HOH A O   1 
HETATM 8804 O  O   . HOH AA 6 .   ? 28.150  -21.572 2.317   1.00 38.83  ? 493 HOH A O   1 
HETATM 8805 O  O   . HOH AA 6 .   ? 8.803   -6.457  7.541   1.00 18.67  ? 494 HOH A O   1 
HETATM 8806 O  O   . HOH AA 6 .   ? 7.400   4.964   11.258  1.00 11.79  ? 495 HOH A O   1 
HETATM 8807 O  O   . HOH AA 6 .   ? 20.857  -9.950  31.889  1.00 21.36  ? 496 HOH A O   1 
HETATM 8808 O  O   . HOH AA 6 .   ? 13.700  16.512  11.839  1.00 16.29  ? 497 HOH A O   1 
HETATM 8809 O  O   . HOH AA 6 .   ? 22.547  -19.525 12.510  1.00 33.74  ? 498 HOH A O   1 
HETATM 8810 O  O   . HOH AA 6 .   ? 25.901  11.166  30.947  1.00 24.25  ? 499 HOH A O   1 
HETATM 8811 O  O   . HOH AA 6 .   ? 39.813  -12.001 23.010  1.00 37.05  ? 500 HOH A O   1 
HETATM 8812 O  O   . HOH AA 6 .   ? 13.727  -12.542 20.906  1.00 18.64  ? 501 HOH A O   1 
HETATM 8813 O  O   . HOH AA 6 .   ? 4.918   -9.262  25.629  1.00 29.81  ? 502 HOH A O   1 
HETATM 8814 O  O   . HOH AA 6 .   ? 9.619   -5.256  -1.482  1.00 38.14  ? 503 HOH A O   1 
HETATM 8815 O  O   . HOH AA 6 .   ? 23.090  -12.378 9.831   1.00 12.09  ? 504 HOH A O   1 
HETATM 8816 O  O   . HOH AA 6 .   ? 7.912   -1.783  15.246  1.00 26.02  ? 505 HOH A O   1 
HETATM 8817 O  O   . HOH AA 6 .   ? 19.431  14.211  5.150   1.00 13.19  ? 506 HOH A O   1 
HETATM 8818 O  O   . HOH AA 6 .   ? 26.499  5.331   -3.700  1.00 27.88  ? 507 HOH A O   1 
HETATM 8819 O  O   . HOH AA 6 .   ? 31.168  -20.976 8.636   1.00 32.72  ? 508 HOH A O   1 
HETATM 8820 O  O   . HOH AA 6 .   ? 11.040  11.179  8.115   1.00 12.43  ? 509 HOH A O   1 
HETATM 8821 O  O   . HOH AA 6 .   ? 11.072  -5.062  0.718   1.00 21.42  ? 510 HOH A O   1 
HETATM 8822 O  O   . HOH AA 6 .   ? 26.023  -9.948  29.030  1.00 28.41  ? 511 HOH A O   1 
HETATM 8823 O  O   . HOH AA 6 .   ? 19.060  11.885  -0.700  1.00 20.36  ? 512 HOH A O   1 
HETATM 8824 O  O   . HOH AA 6 .   ? 11.947  -15.358 8.538   1.00 23.74  ? 513 HOH A O   1 
HETATM 8825 O  O   . HOH AA 6 .   ? 29.183  -14.953 17.083  1.00 19.86  ? 514 HOH A O   1 
HETATM 8826 O  O   . HOH AA 6 .   ? 29.820  -15.664 -1.726  1.00 21.64  ? 515 HOH A O   1 
HETATM 8827 O  O   . HOH AA 6 .   ? 11.372  3.940   -0.017  1.00 21.60  ? 516 HOH A O   1 
HETATM 8828 O  O   . HOH AA 6 .   ? 36.804  5.242   14.379  1.00 29.90  ? 517 HOH A O   1 
HETATM 8829 O  O   . HOH AA 6 .   ? 6.667   -9.807  4.444   1.00 26.97  ? 518 HOH A O   1 
HETATM 8830 O  O   . HOH AA 6 .   ? 13.941  1.876   -2.979  1.00 23.51  ? 519 HOH A O   1 
HETATM 8831 O  O   . HOH AA 6 .   ? 31.490  -13.237 2.512   1.00 23.82  ? 520 HOH A O   1 
HETATM 8832 O  O   . HOH AA 6 .   ? 8.196   -10.514 26.486  1.00 27.46  ? 521 HOH A O   1 
HETATM 8833 O  O   . HOH AA 6 .   ? 44.251  -9.701  8.142   1.00 28.04  ? 522 HOH A O   1 
HETATM 8834 O  O   . HOH AA 6 .   ? 10.054  2.919   22.494  1.00 34.16  ? 523 HOH A O   1 
HETATM 8835 O  O   . HOH AA 6 .   ? 28.210  3.940   33.420  1.00 27.68  ? 524 HOH A O   1 
HETATM 8836 O  O   . HOH AA 6 .   ? 37.811  10.106  -5.157  1.00 29.07  ? 525 HOH A O   1 
HETATM 8837 O  O   . HOH AA 6 .   ? 38.635  6.393   18.722  1.00 34.11  ? 526 HOH A O   1 
HETATM 8838 O  O   . HOH AA 6 .   ? 11.992  7.503   8.675   1.00 12.21  ? 527 HOH A O   1 
HETATM 8839 O  O   . HOH AA 6 .   ? 41.973  8.759   -3.604  1.00 34.83  ? 528 HOH A O   1 
HETATM 8840 O  O   . HOH AA 6 .   ? 10.261  -4.054  19.644  1.00 23.60  ? 529 HOH A O   1 
HETATM 8841 O  O   . HOH AA 6 .   ? 17.268  -3.912  -8.335  1.00 30.40  ? 530 HOH A O   1 
HETATM 8842 O  O   . HOH AA 6 .   ? 17.802  9.615   0.203   1.00 13.46  ? 531 HOH A O   1 
HETATM 8843 O  O   . HOH AA 6 .   ? 11.973  -17.208 4.867   1.00 47.64  ? 532 HOH A O   1 
HETATM 8844 O  O   . HOH AA 6 .   ? 20.803  -2.681  -5.179  1.00 23.42  ? 533 HOH A O   1 
HETATM 8845 O  O   . HOH AA 6 .   ? 31.261  10.453  16.362  1.00 41.27  ? 534 HOH A O   1 
HETATM 8846 O  O   . HOH AA 6 .   ? 15.055  -15.824 15.211  1.00 24.04  ? 535 HOH A O   1 
HETATM 8847 O  O   . HOH AA 6 .   ? 16.681  11.005  -3.092  1.00 28.67  ? 536 HOH A O   1 
HETATM 8848 O  O   . HOH AA 6 .   ? 18.398  -15.781 34.052  1.00 31.34  ? 537 HOH A O   1 
HETATM 8849 O  O   . HOH AA 6 .   ? 27.723  7.726   15.764  1.00 33.81  ? 538 HOH A O   1 
HETATM 8850 O  O   . HOH AA 6 .   ? 14.489  4.348   -4.011  1.00 21.90  ? 539 HOH A O   1 
HETATM 8851 O  O   . HOH AA 6 .   ? 9.743   -2.588  10.419  1.00 17.52  ? 540 HOH A O   1 
HETATM 8852 O  O   . HOH AA 6 .   ? 9.294   -10.808 14.198  1.00 31.47  ? 541 HOH A O   1 
HETATM 8853 O  O   . HOH AA 6 .   ? 17.363  0.250   28.681  1.00 20.01  ? 542 HOH A O   1 
HETATM 8854 O  O   . HOH AA 6 .   ? 26.152  -17.815 17.518  1.00 22.56  ? 543 HOH A O   1 
HETATM 8855 O  O   . HOH AA 6 .   ? 23.444  3.324   -2.009  1.00 17.19  ? 544 HOH A O   1 
HETATM 8856 O  O   . HOH AA 6 .   ? 39.252  3.785   19.503  1.00 25.36  ? 545 HOH A O   1 
HETATM 8857 O  O   . HOH AA 6 .   ? 12.442  4.787   29.888  1.00 38.91  ? 546 HOH A O   1 
HETATM 8858 O  O   . HOH AA 6 .   ? 19.948  10.886  22.303  1.00 38.63  ? 547 HOH A O   1 
HETATM 8859 O  O   . HOH AA 6 .   ? 23.195  11.987  14.881  1.00 30.45  ? 548 HOH A O   1 
HETATM 8860 O  O   . HOH AA 6 .   ? 38.533  12.462  -1.893  1.00 41.64  ? 549 HOH A O   1 
HETATM 8861 O  O   . HOH AA 6 .   ? 38.729  2.040   -6.067  1.00 22.93  ? 550 HOH A O   1 
HETATM 8862 O  O   . HOH AA 6 .   ? 7.698   9.057   14.170  1.00 16.71  ? 551 HOH A O   1 
HETATM 8863 O  O   . HOH AA 6 .   ? 29.958  9.883   14.131  1.00 39.27  ? 552 HOH A O   1 
HETATM 8864 O  O   . HOH AA 6 .   ? 15.234  -14.408 19.376  1.00 16.46  ? 553 HOH A O   1 
HETATM 8865 O  O   . HOH AA 6 .   ? 29.772  10.184  33.692  1.00 39.05  ? 554 HOH A O   1 
HETATM 8866 O  O   . HOH AA 6 .   ? 8.434   -0.253  24.366  1.00 32.21  ? 555 HOH A O   1 
HETATM 8867 O  O   . HOH AA 6 .   ? 11.419  1.692   -4.008  1.00 28.32  ? 556 HOH A O   1 
HETATM 8868 O  O   . HOH AA 6 .   ? 11.452  9.709   -2.072  1.00 40.11  ? 557 HOH A O   1 
HETATM 8869 O  O   . HOH AA 6 .   ? 25.621  -15.995 6.590   1.00 15.17  ? 558 HOH A O   1 
HETATM 8870 O  O   . HOH AA 6 .   ? 23.803  -21.603 -2.965  1.00 44.89  ? 559 HOH A O   1 
HETATM 8871 O  O   . HOH AA 6 .   ? 17.260  -16.447 -7.842  1.00 38.06  ? 560 HOH A O   1 
HETATM 8872 O  O   . HOH AA 6 .   ? 24.203  -20.975 26.857  1.00 32.35  ? 561 HOH A O   1 
HETATM 8873 O  O   . HOH AA 6 .   ? 27.348  -5.573  -5.216  1.00 25.73  ? 562 HOH A O   1 
HETATM 8874 O  O   . HOH AA 6 .   ? 14.685  7.119   21.075  1.00 27.22  ? 563 HOH A O   1 
HETATM 8875 O  O   . HOH AA 6 .   ? 19.485  9.488   35.247  1.00 36.63  ? 564 HOH A O   1 
HETATM 8876 O  O   . HOH AA 6 .   ? 41.744  7.973   -0.776  1.00 32.76  ? 565 HOH A O   1 
HETATM 8877 O  O   . HOH AA 6 .   ? 21.100  -4.459  32.626  1.00 38.53  ? 566 HOH A O   1 
HETATM 8878 O  O   . HOH AA 6 .   ? 13.552  5.111   -0.578  1.00 22.32  ? 567 HOH A O   1 
HETATM 8879 O  O   . HOH AA 6 .   ? 43.486  -9.532  11.389  1.00 26.05  ? 568 HOH A O   1 
HETATM 8880 O  O   . HOH AA 6 .   ? 14.731  -12.426 29.447  1.00 19.71  ? 569 HOH A O   1 
HETATM 8881 O  O   . HOH AA 6 .   ? 8.992   4.042   2.689   1.00 14.06  ? 570 HOH A O   1 
HETATM 8882 O  O   . HOH AA 6 .   ? 32.083  -18.271 7.300   1.00 37.36  ? 571 HOH A O   1 
HETATM 8883 O  O   . HOH AA 6 .   ? 26.883  -18.986 -1.275  1.00 44.97  ? 572 HOH A O   1 
HETATM 8884 O  O   . HOH AA 6 .   ? 26.171  -18.498 20.633  1.00 19.90  ? 573 HOH A O   1 
HETATM 8885 O  O   . HOH AA 6 .   ? 28.136  -4.684  31.367  1.00 24.85  ? 574 HOH A O   1 
HETATM 8886 O  O   . HOH AA 6 .   ? 41.767  7.005   2.816   1.00 33.17  ? 575 HOH A O   1 
HETATM 8887 O  O   . HOH AA 6 .   ? 42.040  4.258   12.781  1.00 38.10  ? 576 HOH A O   1 
HETATM 8888 O  O   . HOH AA 6 .   ? 32.499  7.791   30.792  1.00 24.65  ? 577 HOH A O   1 
HETATM 8889 O  O   . HOH AA 6 .   ? 11.673  7.992   1.663   1.00 14.75  ? 578 HOH A O   1 
HETATM 8890 O  O   . HOH AA 6 .   ? 7.840   -7.090  16.958  1.00 26.47  ? 579 HOH A O   1 
HETATM 8891 O  O   . HOH AA 6 .   ? 7.468   -1.956  -0.677  1.00 25.33  ? 580 HOH A O   1 
HETATM 8892 O  O   . HOH AA 6 .   ? 29.500  11.957  -4.652  1.00 32.09  ? 581 HOH A O   1 
HETATM 8893 O  O   . HOH AA 6 .   ? 24.197  12.024  0.546   1.00 32.61  ? 582 HOH A O   1 
HETATM 8894 O  O   . HOH AA 6 .   ? 31.717  -2.537  -4.731  1.00 38.12  ? 583 HOH A O   1 
HETATM 8895 O  O   . HOH AA 6 .   ? 37.506  7.969   9.403   1.00 24.81  ? 584 HOH A O   1 
HETATM 8896 O  O   . HOH AA 6 .   ? 31.358  -4.216  38.300  1.00 47.60  ? 585 HOH A O   1 
HETATM 8897 O  O   . HOH AA 6 .   ? 14.421  -2.001  29.016  1.00 27.00  ? 586 HOH A O   1 
HETATM 8898 O  O   . HOH AA 6 .   ? 38.464  -15.504 12.508  1.00 33.42  ? 587 HOH A O   1 
HETATM 8899 O  O   . HOH AA 6 .   ? 17.789  -1.586  -7.632  1.00 38.98  ? 588 HOH A O   1 
HETATM 8900 O  O   . HOH AA 6 .   ? 31.459  -19.012 4.323   1.00 26.06  ? 589 HOH A O   1 
HETATM 8901 O  O   . HOH AA 6 .   ? 23.921  -15.432 -11.672 1.00 32.76  ? 590 HOH A O   1 
HETATM 8902 O  O   . HOH AA 6 .   ? 9.919   -2.048  27.608  1.00 37.07  ? 591 HOH A O   1 
HETATM 8903 O  O   . HOH AA 6 .   ? 38.370  -13.484 5.511   1.00 27.75  ? 592 HOH A O   1 
HETATM 8904 O  O   . HOH AA 6 .   ? 11.129  2.416   28.992  1.00 51.62  ? 593 HOH A O   1 
HETATM 8905 O  O   . HOH AA 6 .   ? 15.170  -13.564 16.791  1.00 16.18  ? 594 HOH A O   1 
HETATM 8906 O  O   . HOH AA 6 .   ? 27.338  6.048   35.458  1.00 26.42  ? 595 HOH A O   1 
HETATM 8907 O  O   . HOH AA 6 .   ? 15.507  13.841  -0.365  1.00 29.74  ? 596 HOH A O   1 
HETATM 8908 O  O   . HOH AA 6 .   ? 7.557   -15.722 7.372   1.00 38.22  ? 597 HOH A O   1 
HETATM 8909 O  O   . HOH AA 6 .   ? 41.540  12.352  7.665   1.00 35.63  ? 598 HOH A O   1 
HETATM 8910 O  O   . HOH AA 6 .   ? 24.879  16.061  2.519   1.00 40.23  ? 599 HOH A O   1 
HETATM 8911 O  O   . HOH AA 6 .   ? 12.472  4.484   22.141  1.00 30.86  ? 600 HOH A O   1 
HETATM 8912 O  O   . HOH AA 6 .   ? 45.448  1.629   21.814  1.00 38.25  ? 601 HOH A O   1 
HETATM 8913 O  O   . HOH AA 6 .   ? 30.337  7.145   13.741  1.00 22.97  ? 602 HOH A O   1 
HETATM 8914 O  O   . HOH AA 6 .   ? 6.271   -2.891  13.372  1.00 20.42  ? 603 HOH A O   1 
HETATM 8915 O  O   . HOH AA 6 .   ? 35.671  10.180  10.083  1.00 27.96  ? 604 HOH A O   1 
HETATM 8916 O  O   . HOH AA 6 .   ? 39.180  -3.894  -7.719  1.00 55.26  ? 605 HOH A O   1 
HETATM 8917 O  O   . HOH AA 6 .   ? 13.188  -14.350 2.392   1.00 34.28  ? 606 HOH A O   1 
HETATM 8918 O  O   . HOH AA 6 .   ? 17.824  -6.303  33.649  1.00 37.24  ? 607 HOH A O   1 
HETATM 8919 O  O   . HOH AA 6 .   ? 26.389  -8.313  -11.228 1.00 47.87  ? 608 HOH A O   1 
HETATM 8920 O  O   . HOH AA 6 .   ? 7.313   -0.772  8.314   1.00 32.61  ? 609 HOH A O   1 
HETATM 8921 O  O   . HOH AA 6 .   ? 13.249  -14.411 13.067  1.00 27.06  ? 610 HOH A O   1 
HETATM 8922 O  O   . HOH AA 6 .   ? 41.132  10.364  -0.130  1.00 37.92  ? 611 HOH A O   1 
HETATM 8923 O  O   . HOH AA 6 .   ? 19.652  13.522  19.006  1.00 45.46  ? 612 HOH A O   1 
HETATM 8924 O  O   . HOH AA 6 .   ? 39.208  4.970   15.150  1.00 35.17  ? 613 HOH A O   1 
HETATM 8925 O  O   . HOH AA 6 .   ? 21.092  -25.665 -6.303  1.00 23.57  ? 614 HOH A O   1 
HETATM 8926 O  O   . HOH AA 6 .   ? 38.296  -5.905  29.293  1.00 41.11  ? 615 HOH A O   1 
HETATM 8927 O  O   . HOH AA 6 .   ? 34.136  -10.627 28.183  1.00 45.06  ? 616 HOH A O   1 
HETATM 8928 O  O   . HOH AA 6 .   ? 20.253  -7.371  32.460  1.00 28.47  ? 617 HOH A O   1 
HETATM 8929 O  O   . HOH AA 6 .   ? 29.498  -3.505  -5.730  1.00 48.74  ? 618 HOH A O   1 
HETATM 8930 O  O   . HOH AA 6 .   ? 17.982  5.651   20.854  1.00 27.44  ? 619 HOH A O   1 
HETATM 8931 O  O   . HOH AA 6 .   ? 24.640  -2.559  33.196  1.00 35.96  ? 620 HOH A O   1 
HETATM 8932 O  O   . HOH AA 6 .   ? 21.568  12.066  -2.296  1.00 61.58  ? 621 HOH A O   1 
HETATM 8933 O  O   . HOH AA 6 .   ? 39.556  3.030   16.678  1.00 37.43  ? 622 HOH A O   1 
HETATM 8934 O  O   . HOH AA 6 .   ? 28.867  -18.634 20.687  1.00 26.51  ? 623 HOH A O   1 
HETATM 8935 O  O   . HOH AA 6 .   ? 24.510  -11.556 30.336  1.00 29.72  ? 624 HOH A O   1 
HETATM 8936 O  O   . HOH AA 6 .   ? 30.285  -17.560 18.607  1.00 38.86  ? 625 HOH A O   1 
HETATM 8937 O  O   . HOH AA 6 .   ? 46.592  1.860   10.551  1.00 39.40  ? 626 HOH A O   1 
HETATM 8938 O  O   . HOH AA 6 .   ? 45.627  1.870   7.811   1.00 31.90  ? 627 HOH A O   1 
HETATM 8939 O  O   . HOH AA 6 .   ? 8.069   -3.995  11.887  1.00 30.23  ? 628 HOH A O   1 
HETATM 8940 O  O   . HOH AA 6 .   ? 4.150   13.276  19.776  1.00 40.28  ? 629 HOH A O   1 
HETATM 8941 O  O   . HOH AA 6 .   ? 7.280   -5.699  5.239   1.00 30.52  ? 630 HOH A O   1 
HETATM 8942 O  O   . HOH AA 6 .   ? 8.956   2.815   20.298  1.00 32.38  ? 631 HOH A O   1 
HETATM 8943 O  O   . HOH AA 6 .   ? 33.841  9.390   16.283  1.00 39.88  ? 632 HOH A O   1 
HETATM 8944 O  O   . HOH AA 6 .   ? 40.183  8.830   -5.771  1.00 29.27  ? 633 HOH A O   1 
HETATM 8945 O  O   . HOH AA 6 .   ? 14.077  -16.033 27.039  1.00 39.56  ? 634 HOH A O   1 
HETATM 8946 O  O   . HOH AA 6 .   ? 11.061  -14.715 17.098  1.00 32.22  ? 635 HOH A O   1 
HETATM 8947 O  O   . HOH AA 6 .   ? 13.170  13.667  -1.863  1.00 30.27  ? 636 HOH A O   1 
HETATM 8948 O  O   . HOH AA 6 .   ? 45.426  0.082   6.002   1.00 30.36  ? 637 HOH A O   1 
HETATM 8949 O  O   . HOH AA 6 .   ? 33.523  -17.657 2.965   1.00 33.96  ? 638 HOH A O   1 
HETATM 8950 O  O   . HOH AA 6 .   ? 40.058  -4.226  -2.056  1.00 40.24  ? 639 HOH A O   1 
HETATM 8951 O  O   . HOH AA 6 .   ? 45.436  -6.763  5.971   1.00 29.82  ? 640 HOH A O   1 
HETATM 8952 O  O   . HOH AA 6 .   ? 10.403  -4.366  30.201  1.00 37.59  ? 641 HOH A O   1 
HETATM 8953 O  O   . HOH AA 6 .   ? 42.128  -13.861 11.930  1.00 43.36  ? 642 HOH A O   1 
HETATM 8954 O  O   . HOH AA 6 .   ? 27.310  -18.090 15.057  1.00 47.59  ? 643 HOH A O   1 
HETATM 8955 O  O   . HOH AA 6 .   ? 7.899   6.588   15.605  1.00 16.11  ? 644 HOH A O   1 
HETATM 8956 O  O   . HOH AA 6 .   ? 20.893  -0.841  -7.243  1.00 42.92  ? 645 HOH A O   1 
HETATM 8957 O  O   . HOH AA 6 .   ? 39.404  -9.917  24.782  1.00 40.13  ? 646 HOH A O   1 
HETATM 8958 O  O   . HOH AA 6 .   ? 23.587  3.309   -4.986  1.00 47.52  ? 647 HOH A O   1 
HETATM 8959 O  O   . HOH AA 6 .   ? 22.458  12.862  39.158  1.00 35.95  ? 648 HOH A O   1 
HETATM 8960 O  O   . HOH AA 6 .   ? 36.622  -15.605 25.685  1.00 37.43  ? 649 HOH A O   1 
HETATM 8961 O  O   . HOH AA 6 .   ? 29.911  -18.198 -2.569  1.00 36.34  ? 650 HOH A O   1 
HETATM 8962 O  O   . HOH AA 6 .   ? 23.677  -10.215 32.646  1.00 33.72  ? 651 HOH A O   1 
HETATM 8963 O  O   . HOH AA 6 .   ? 33.887  9.452   12.136  1.00 31.01  ? 652 HOH A O   1 
HETATM 8964 O  O   . HOH AA 6 .   ? 45.020  1.882   15.255  1.00 49.50  ? 653 HOH A O   1 
HETATM 8965 O  O   . HOH AA 6 .   ? 23.586  -4.215  -5.707  1.00 43.22  ? 654 HOH A O   1 
HETATM 8966 O  O   . HOH AA 6 .   ? 16.351  -16.428 7.897   1.00 34.29  ? 655 HOH A O   1 
HETATM 8967 O  O   . HOH AA 6 .   ? 31.662  10.100  31.952  1.00 37.06  ? 656 HOH A O   1 
HETATM 8968 O  O   . HOH AA 6 .   ? 31.988  11.508  12.272  1.00 38.26  ? 657 HOH A O   1 
HETATM 8969 O  O   . HOH AA 6 .   ? 32.651  -15.018 28.344  1.00 34.47  ? 658 HOH A O   1 
HETATM 8970 O  O   . HOH AA 6 .   ? 25.521  6.671   37.426  1.00 31.45  ? 659 HOH A O   1 
HETATM 8971 O  O   . HOH AA 6 .   ? 43.851  9.081   2.408   1.00 48.03  ? 660 HOH A O   1 
HETATM 8972 O  O   . HOH AA 6 .   ? 22.959  -3.361  -8.389  1.00 37.50  ? 661 HOH A O   1 
HETATM 8973 O  O   . HOH AA 6 .   ? 9.853   -16.921 8.516   1.00 41.18  ? 662 HOH A O   1 
HETATM 8974 O  O   . HOH AA 6 .   ? 11.036  -14.978 30.221  1.00 27.22  ? 663 HOH A O   1 
HETATM 8975 O  O   . HOH AA 6 .   ? 20.016  7.938   -4.522  1.00 38.91  ? 664 HOH A O   1 
HETATM 8976 O  O   . HOH AA 6 .   ? 36.429  13.709  -1.004  1.00 39.17  ? 665 HOH A O   1 
HETATM 8977 O  O   . HOH AA 6 .   ? 8.177   -4.730  9.381   1.00 32.52  ? 666 HOH A O   1 
HETATM 8978 O  O   . HOH AA 6 .   ? 12.554  -10.712 30.132  1.00 19.57  ? 667 HOH A O   1 
HETATM 8979 O  O   . HOH AA 6 .   ? 19.495  -11.268 33.881  1.00 25.82  ? 668 HOH A O   1 
HETATM 8980 O  O   . HOH AA 6 .   ? 14.382  -17.779 11.532  1.00 36.54  ? 669 HOH A O   1 
HETATM 8981 O  O   . HOH AA 6 .   ? 21.408  16.097  5.359   1.00 25.61  ? 670 HOH A O   1 
HETATM 8982 O  O   . HOH AA 6 .   ? 40.303  7.063   17.001  1.00 46.27  ? 671 HOH A O   1 
HETATM 8983 O  O   . HOH AA 6 .   ? 11.648  -13.084 25.894  1.00 27.10  ? 672 HOH A O   1 
HETATM 8984 O  O   . HOH AA 6 .   ? 12.122  5.469   -4.215  1.00 30.29  ? 673 HOH A O   1 
HETATM 8985 O  O   . HOH AA 6 .   ? 30.673  -21.358 3.340   1.00 42.68  ? 674 HOH A O   1 
HETATM 8986 O  O   . HOH AA 6 .   ? 12.598  -15.723 11.187  1.00 36.55  ? 675 HOH A O   1 
HETATM 8987 O  O   . HOH AA 6 .   ? 13.782  -17.054 7.278   1.00 30.00  ? 676 HOH A O   1 
HETATM 8988 O  O   . HOH AA 6 .   ? 19.297  10.384  -4.380  1.00 32.71  ? 677 HOH A O   1 
HETATM 8989 O  O   . HOH AA 6 .   ? 25.440  -18.502 30.297  1.00 40.69  ? 678 HOH A O   1 
HETATM 8990 O  O   . HOH AA 6 .   ? 8.267   -13.026 27.847  1.00 30.18  ? 679 HOH A O   1 
HETATM 8991 O  O   . HOH AA 6 .   ? 22.689  16.379  8.006   1.00 43.68  ? 680 HOH A O   1 
HETATM 8992 O  O   . HOH AA 6 .   ? 21.708  2.396   -6.731  1.00 48.82  ? 681 HOH A O   1 
HETATM 8993 O  O   . HOH AA 6 .   ? 31.634  -19.847 -1.464  1.00 43.83  ? 682 HOH A O   1 
HETATM 8994 O  O   . HOH AA 6 .   ? 13.360  -5.764  32.200  1.00 27.62  ? 683 HOH A O   1 
HETATM 8995 O  O   . HOH AA 6 .   ? 47.995  0.603   17.209  1.00 32.06  ? 684 HOH A O   1 
HETATM 8996 O  O   . HOH BA 6 .   ? 8.802   14.721  8.264   1.00 27.65  ? 401 HOH B O   1 
HETATM 8997 O  O   . HOH BA 6 .   ? 2.671   6.580   16.814  1.00 29.16  ? 402 HOH B O   1 
HETATM 8998 O  O   . HOH BA 6 .   ? -0.049  16.605  -11.196 1.00 36.30  ? 403 HOH B O   1 
HETATM 8999 O  O   . HOH BA 6 .   ? -7.849  6.511   1.997   1.00 17.81  ? 404 HOH B O   1 
HETATM 9000 O  O   . HOH BA 6 .   ? 6.295   6.888   17.683  1.00 39.67  ? 405 HOH B O   1 
HETATM 9001 O  O   . HOH BA 6 .   ? 3.990   17.889  -15.365 1.00 31.77  ? 406 HOH B O   1 
HETATM 9002 O  O   . HOH BA 6 .   ? -20.111 -12.034 8.174   1.00 31.84  ? 407 HOH B O   1 
HETATM 9003 O  O   . HOH BA 6 .   ? -10.481 7.710   1.150   1.00 25.98  ? 408 HOH B O   1 
HETATM 9004 O  O   . HOH BA 6 .   ? -16.932 -0.112  23.465  1.00 41.57  ? 409 HOH B O   1 
HETATM 9005 O  O   . HOH BA 6 .   ? -28.730 -6.700  15.575  1.00 43.15  ? 410 HOH B O   1 
HETATM 9006 O  O   . HOH BA 6 .   ? -10.735 -19.843 25.164  1.00 48.39  ? 411 HOH B O   1 
HETATM 9007 O  O   . HOH BA 6 .   ? -27.040 -3.668  -5.979  1.00 30.46  ? 412 HOH B O   1 
HETATM 9008 O  O   . HOH BA 6 .   ? -29.247 2.286   5.775   1.00 25.67  ? 413 HOH B O   1 
HETATM 9009 O  O   . HOH BA 6 .   ? -13.991 -14.844 5.886   1.00 20.46  ? 414 HOH B O   1 
HETATM 9010 O  O   . HOH BA 6 .   ? 3.711   -2.172  22.592  1.00 26.85  ? 415 HOH B O   1 
HETATM 9011 O  O   . HOH BA 6 .   ? -18.641 6.537   23.669  1.00 42.34  ? 416 HOH B O   1 
HETATM 9012 O  O   . HOH BA 6 .   ? -2.628  5.161   4.056   1.00 11.09  ? 417 HOH B O   1 
HETATM 9013 O  O   . HOH BA 6 .   ? -3.568  19.116  -20.065 1.00 28.29  ? 418 HOH B O   1 
HETATM 9014 O  O   . HOH BA 6 .   ? -1.588  20.627  8.413   1.00 39.14  ? 419 HOH B O   1 
HETATM 9015 O  O   . HOH BA 6 .   ? -26.461 -7.196  -1.731  1.00 31.27  ? 420 HOH B O   1 
HETATM 9016 O  O   . HOH BA 6 .   ? -13.365 4.889   -18.916 1.00 40.64  ? 421 HOH B O   1 
HETATM 9017 O  O   . HOH BA 6 .   ? -4.210  11.529  -15.043 1.00 28.71  ? 422 HOH B O   1 
HETATM 9018 O  O   . HOH BA 6 .   ? -13.314 7.561   -15.590 1.00 24.70  ? 423 HOH B O   1 
HETATM 9019 O  O   . HOH BA 6 .   ? 5.843   12.163  -4.314  1.00 20.92  ? 424 HOH B O   1 
HETATM 9020 O  O   . HOH BA 6 .   ? -13.848 -15.085 28.466  1.00 28.69  ? 425 HOH B O   1 
HETATM 9021 O  O   . HOH BA 6 .   ? -20.915 -5.153  21.940  1.00 24.16  ? 426 HOH B O   1 
HETATM 9022 O  O   . HOH BA 6 .   ? 3.793   3.454   -2.437  1.00 17.84  ? 427 HOH B O   1 
HETATM 9023 O  O   . HOH BA 6 .   ? -1.869  9.544   -2.973  1.00 24.90  ? 428 HOH B O   1 
HETATM 9024 O  O   . HOH BA 6 .   ? 6.190   -6.843  6.890   1.00 40.77  ? 429 HOH B O   1 
HETATM 9025 O  O   . HOH BA 6 .   ? -5.718  -12.608 11.836  1.00 18.85  ? 430 HOH B O   1 
HETATM 9026 O  O   . HOH BA 6 .   ? 9.177   7.164   8.469   1.00 16.20  ? 431 HOH B O   1 
HETATM 9027 O  O   . HOH BA 6 .   ? -13.908 0.210   15.123  1.00 10.74  ? 432 HOH B O   1 
HETATM 9028 O  O   . HOH BA 6 .   ? -14.374 -1.901  -13.599 1.00 51.30  ? 433 HOH B O   1 
HETATM 9029 O  O   . HOH BA 6 .   ? -5.627  -11.702 -15.003 1.00 29.82  ? 434 HOH B O   1 
HETATM 9030 O  O   . HOH BA 6 .   ? -19.873 -7.672  -11.702 1.00 38.50  ? 435 HOH B O   1 
HETATM 9031 O  O   . HOH BA 6 .   ? 5.195   6.345   1.051   1.00 12.90  ? 436 HOH B O   1 
HETATM 9032 O  O   . HOH BA 6 .   ? -26.315 9.108   16.609  1.00 28.37  ? 437 HOH B O   1 
HETATM 9033 O  O   . HOH BA 6 .   ? -20.155 -12.126 -2.430  1.00 32.17  ? 438 HOH B O   1 
HETATM 9034 O  O   . HOH BA 6 .   ? -21.368 -9.977  9.745   1.00 33.68  ? 439 HOH B O   1 
HETATM 9035 O  O   . HOH BA 6 .   ? 3.213   15.184  -5.197  1.00 48.45  ? 440 HOH B O   1 
HETATM 9036 O  O   . HOH BA 6 .   ? 6.256   16.767  0.864   1.00 28.61  ? 441 HOH B O   1 
HETATM 9037 O  O   . HOH BA 6 .   ? -3.849  16.131  -11.191 1.00 20.07  ? 442 HOH B O   1 
HETATM 9038 O  O   . HOH BA 6 .   ? -3.278  -8.540  -9.161  1.00 27.86  ? 443 HOH B O   1 
HETATM 9039 O  O   . HOH BA 6 .   ? 6.495   0.488   22.193  1.00 31.28  ? 444 HOH B O   1 
HETATM 9040 O  O   . HOH BA 6 .   ? -17.156 11.240  1.606   1.00 30.20  ? 445 HOH B O   1 
HETATM 9041 O  O   . HOH BA 6 .   ? -29.686 -4.655  -0.885  1.00 22.38  ? 446 HOH B O   1 
HETATM 9042 O  O   . HOH BA 6 .   ? 4.667   -9.765  -12.457 1.00 29.97  ? 447 HOH B O   1 
HETATM 9043 O  O   . HOH BA 6 .   ? 5.918   -9.458  13.523  1.00 17.93  ? 448 HOH B O   1 
HETATM 9044 O  O   . HOH BA 6 .   ? 5.359   5.470   7.744   1.00 12.46  ? 449 HOH B O   1 
HETATM 9045 O  O   . HOH BA 6 .   ? 4.386   6.468   14.160  1.00 11.80  ? 450 HOH B O   1 
HETATM 9046 O  O   . HOH BA 6 .   ? -27.200 -10.032 1.533   1.00 27.09  ? 451 HOH B O   1 
HETATM 9047 O  O   . HOH BA 6 .   ? 1.695   14.389  -11.464 1.00 33.23  ? 452 HOH B O   1 
HETATM 9048 O  O   . HOH BA 6 .   ? -16.921 11.059  4.421   1.00 26.80  ? 453 HOH B O   1 
HETATM 9049 O  O   . HOH BA 6 .   ? 5.152   15.967  13.515  1.00 27.78  ? 454 HOH B O   1 
HETATM 9050 O  O   . HOH BA 6 .   ? -16.359 -12.348 25.750  1.00 24.69  ? 455 HOH B O   1 
HETATM 9051 O  O   . HOH BA 6 .   ? -21.974 1.472   18.691  1.00 22.36  ? 456 HOH B O   1 
HETATM 9052 O  O   . HOH BA 6 .   ? 7.867   11.806  14.754  1.00 23.01  ? 457 HOH B O   1 
HETATM 9053 O  O   . HOH BA 6 .   ? 5.488   -8.100  -1.522  1.00 37.60  ? 458 HOH B O   1 
HETATM 9054 O  O   . HOH BA 6 .   ? -21.666 -8.752  -8.485  1.00 20.18  ? 459 HOH B O   1 
HETATM 9055 O  O   . HOH BA 6 .   ? -17.745 9.225   -2.599  1.00 19.86  ? 460 HOH B O   1 
HETATM 9056 O  O   . HOH BA 6 .   ? -20.620 -11.223 5.745   1.00 44.15  ? 461 HOH B O   1 
HETATM 9057 O  O   . HOH BA 6 .   ? 7.352   -11.466 24.201  1.00 33.21  ? 462 HOH B O   1 
HETATM 9058 O  O   . HOH BA 6 .   ? -9.313  15.252  9.850   1.00 34.83  ? 463 HOH B O   1 
HETATM 9059 O  O   . HOH BA 6 .   ? -13.401 -6.951  -11.242 1.00 20.14  ? 464 HOH B O   1 
HETATM 9060 O  O   . HOH BA 6 .   ? 4.555   17.129  3.699   1.00 24.43  ? 465 HOH B O   1 
HETATM 9061 O  O   . HOH BA 6 .   ? 2.810   -13.268 15.896  1.00 22.24  ? 466 HOH B O   1 
HETATM 9062 O  O   . HOH BA 6 .   ? -2.821  -5.417  -4.173  1.00 13.61  ? 467 HOH B O   1 
HETATM 9063 O  O   . HOH BA 6 .   ? -11.866 -17.591 13.275  1.00 43.57  ? 468 HOH B O   1 
HETATM 9064 O  O   . HOH BA 6 .   ? -12.203 -13.590 -11.353 1.00 18.62  ? 469 HOH B O   1 
HETATM 9065 O  O   . HOH BA 6 .   ? 3.712   -2.159  13.947  1.00 15.29  ? 470 HOH B O   1 
HETATM 9066 O  O   . HOH BA 6 .   ? 4.144   14.778  1.781   1.00 26.98  ? 471 HOH B O   1 
HETATM 9067 O  O   . HOH BA 6 .   ? 4.792   -5.876  9.192   1.00 23.48  ? 472 HOH B O   1 
HETATM 9068 O  O   . HOH BA 6 .   ? -17.601 -3.831  26.789  1.00 28.43  ? 473 HOH B O   1 
HETATM 9069 O  O   . HOH BA 6 .   ? -20.243 -9.604  15.073  1.00 20.29  ? 474 HOH B O   1 
HETATM 9070 O  O   . HOH BA 6 .   ? -3.879  12.658  -18.257 1.00 21.99  ? 475 HOH B O   1 
HETATM 9071 O  O   . HOH BA 6 .   ? -18.210 -8.174  16.081  1.00 19.84  ? 476 HOH B O   1 
HETATM 9072 O  O   . HOH BA 6 .   ? -23.129 11.379  -1.231  1.00 27.43  ? 477 HOH B O   1 
HETATM 9073 O  O   . HOH BA 6 .   ? -26.914 -6.331  6.532   1.00 16.66  ? 478 HOH B O   1 
HETATM 9074 O  O   . HOH BA 6 .   ? -16.817 2.586   22.295  1.00 45.06  ? 479 HOH B O   1 
HETATM 9075 O  O   . HOH BA 6 .   ? -5.514  6.469   0.575   1.00 14.10  ? 480 HOH B O   1 
HETATM 9076 O  O   . HOH BA 6 .   ? -24.527 -2.466  -6.644  1.00 18.23  ? 481 HOH B O   1 
HETATM 9077 O  O   . HOH BA 6 .   ? -6.526  -11.515 29.150  1.00 34.35  ? 482 HOH B O   1 
HETATM 9078 O  O   . HOH BA 6 .   ? -7.733  -15.628 -7.863  1.00 13.62  ? 483 HOH B O   1 
HETATM 9079 O  O   . HOH BA 6 .   ? -17.408 13.268  -4.005  1.00 31.65  ? 484 HOH B O   1 
HETATM 9080 O  O   . HOH BA 6 .   ? -23.081 9.514   6.461   1.00 18.57  ? 485 HOH B O   1 
HETATM 9081 O  O   . HOH BA 6 .   ? -5.566  1.611   -9.793  1.00 15.04  ? 486 HOH B O   1 
HETATM 9082 O  O   . HOH BA 6 .   ? -21.599 -2.302  -12.743 1.00 40.54  ? 487 HOH B O   1 
HETATM 9083 O  O   . HOH BA 6 .   ? -20.852 3.808   -13.084 1.00 23.63  ? 488 HOH B O   1 
HETATM 9084 O  O   . HOH BA 6 .   ? -16.455 5.487   22.118  1.00 38.63  ? 489 HOH B O   1 
HETATM 9085 O  O   . HOH BA 6 .   ? -5.647  -15.477 13.489  1.00 25.91  ? 490 HOH B O   1 
HETATM 9086 O  O   . HOH BA 6 .   ? -17.297 9.846   -14.209 1.00 45.60  ? 491 HOH B O   1 
HETATM 9087 O  O   . HOH BA 6 .   ? -1.602  16.596  11.083  1.00 13.73  ? 492 HOH B O   1 
HETATM 9088 O  O   . HOH BA 6 .   ? -22.768 -2.139  -8.763  1.00 18.60  ? 493 HOH B O   1 
HETATM 9089 O  O   . HOH BA 6 .   ? 1.781   -1.648  5.855   1.00 10.87  ? 494 HOH B O   1 
HETATM 9090 O  O   . HOH BA 6 .   ? 1.367   18.113  -14.023 1.00 27.07  ? 495 HOH B O   1 
HETATM 9091 O  O   . HOH BA 6 .   ? -27.557 -4.396  8.474   1.00 16.33  ? 496 HOH B O   1 
HETATM 9092 O  O   . HOH BA 6 .   ? -24.046 0.586   21.157  1.00 28.77  ? 497 HOH B O   1 
HETATM 9093 O  O   . HOH BA 6 .   ? -16.700 -16.843 16.651  1.00 47.87  ? 498 HOH B O   1 
HETATM 9094 O  O   . HOH BA 6 .   ? -14.573 -13.602 23.925  1.00 27.63  ? 499 HOH B O   1 
HETATM 9095 O  O   . HOH BA 6 .   ? -17.771 -16.470 -6.580  1.00 30.25  ? 500 HOH B O   1 
HETATM 9096 O  O   . HOH BA 6 .   ? -3.630  2.220   -12.014 1.00 18.79  ? 501 HOH B O   1 
HETATM 9097 O  O   . HOH BA 6 .   ? -16.814 -10.802 1.257   1.00 14.61  ? 502 HOH B O   1 
HETATM 9098 O  O   . HOH BA 6 .   ? 6.930   -11.522 17.303  1.00 28.86  ? 503 HOH B O   1 
HETATM 9099 O  O   . HOH BA 6 .   ? -5.978  -16.616 5.429   1.00 35.76  ? 504 HOH B O   1 
HETATM 9100 O  O   . HOH BA 6 .   ? -1.811  -12.542 24.958  1.00 40.36  ? 505 HOH B O   1 
HETATM 9101 O  O   . HOH BA 6 .   ? 6.002   11.719  7.941   1.00 11.80  ? 506 HOH B O   1 
HETATM 9102 O  O   . HOH BA 6 .   ? 8.155   4.601   5.199   1.00 11.56  ? 507 HOH B O   1 
HETATM 9103 O  O   . HOH BA 6 .   ? -21.292 20.702  11.734  1.00 38.17  ? 508 HOH B O   1 
HETATM 9104 O  O   . HOH BA 6 .   ? -10.249 -9.053  8.197   1.00 10.15  ? 509 HOH B O   1 
HETATM 9105 O  O   . HOH BA 6 .   ? -3.258  2.497   21.359  1.00 27.58  ? 510 HOH B O   1 
HETATM 9106 O  O   . HOH BA 6 .   ? -19.154 -0.610  -16.586 1.00 40.90  ? 511 HOH B O   1 
HETATM 9107 O  O   . HOH BA 6 .   ? -31.735 5.254   -7.587  1.00 22.69  ? 512 HOH B O   1 
HETATM 9108 O  O   . HOH BA 6 .   ? -8.935  -8.007  -14.498 1.00 18.69  ? 513 HOH B O   1 
HETATM 9109 O  O   . HOH BA 6 .   ? -1.890  -11.493 -3.145  1.00 18.82  ? 514 HOH B O   1 
HETATM 9110 O  O   . HOH BA 6 .   ? -6.032  11.335  20.733  1.00 35.74  ? 515 HOH B O   1 
HETATM 9111 O  O   . HOH BA 6 .   ? 6.633   3.303   9.177   1.00 10.10  ? 516 HOH B O   1 
HETATM 9112 O  O   . HOH BA 6 .   ? -16.916 -10.546 20.262  1.00 16.18  ? 517 HOH B O   1 
HETATM 9113 O  O   . HOH BA 6 .   ? -1.316  -0.662  -12.697 1.00 22.17  ? 518 HOH B O   1 
HETATM 9114 O  O   . HOH BA 6 .   ? -0.674  4.030   -16.963 1.00 29.86  ? 519 HOH B O   1 
HETATM 9115 O  O   . HOH BA 6 .   ? 4.102   -14.981 10.019  1.00 38.27  ? 520 HOH B O   1 
HETATM 9116 O  O   . HOH BA 6 .   ? 4.180   -2.375  -3.081  1.00 32.62  ? 521 HOH B O   1 
HETATM 9117 O  O   . HOH BA 6 .   ? -26.538 9.156   -2.958  1.00 30.25  ? 522 HOH B O   1 
HETATM 9118 O  O   . HOH BA 6 .   ? -1.365  14.569  17.012  1.00 24.53  ? 523 HOH B O   1 
HETATM 9119 O  O   . HOH BA 6 .   ? -29.087 7.172   -1.616  1.00 30.04  ? 524 HOH B O   1 
HETATM 9120 O  O   . HOH BA 6 .   ? -34.739 5.445   -5.319  1.00 39.18  ? 525 HOH B O   1 
HETATM 9121 O  O   . HOH BA 6 .   ? -15.795 -0.315  -14.993 1.00 27.66  ? 526 HOH B O   1 
HETATM 9122 O  O   . HOH BA 6 .   ? -0.815  5.772   -4.671  1.00 20.73  ? 527 HOH B O   1 
HETATM 9123 O  O   . HOH BA 6 .   ? -27.299 6.934   -11.899 1.00 29.67  ? 528 HOH B O   1 
HETATM 9124 O  O   . HOH BA 6 .   ? -12.345 17.252  6.557   1.00 34.87  ? 529 HOH B O   1 
HETATM 9125 O  O   . HOH BA 6 .   ? 5.390   19.931  10.755  1.00 23.62  ? 530 HOH B O   1 
HETATM 9126 O  O   . HOH BA 6 .   ? -10.392 14.274  -13.541 1.00 19.49  ? 531 HOH B O   1 
HETATM 9127 O  O   . HOH BA 6 .   ? 8.911   16.561  0.866   1.00 20.63  ? 532 HOH B O   1 
HETATM 9128 O  O   . HOH BA 6 .   ? -23.816 -8.029  20.295  1.00 34.15  ? 533 HOH B O   1 
HETATM 9129 O  O   . HOH BA 6 .   ? -0.697  11.936  16.232  1.00 15.22  ? 534 HOH B O   1 
HETATM 9130 O  O   . HOH BA 6 .   ? 0.077   -13.988 8.861   1.00 34.81  ? 535 HOH B O   1 
HETATM 9131 O  O   . HOH BA 6 .   ? -10.523 -10.494 29.775  1.00 24.22  ? 536 HOH B O   1 
HETATM 9132 O  O   . HOH BA 6 .   ? 8.654   8.657   2.040   1.00 18.48  ? 537 HOH B O   1 
HETATM 9133 O  O   . HOH BA 6 .   ? -9.128  16.990  -15.727 1.00 38.92  ? 538 HOH B O   1 
HETATM 9134 O  O   . HOH BA 6 .   ? -5.831  -15.684 25.725  1.00 21.68  ? 539 HOH B O   1 
HETATM 9135 O  O   . HOH BA 6 .   ? -12.599 -0.536  22.757  1.00 22.60  ? 540 HOH B O   1 
HETATM 9136 O  O   . HOH BA 6 .   ? 2.402   4.938   -5.611  1.00 29.57  ? 541 HOH B O   1 
HETATM 9137 O  O   . HOH BA 6 .   ? 0.838   13.173  19.382  1.00 33.11  ? 542 HOH B O   1 
HETATM 9138 O  O   . HOH BA 6 .   ? -23.279 -9.148  14.037  1.00 36.55  ? 543 HOH B O   1 
HETATM 9139 O  O   . HOH BA 6 .   ? -14.510 -14.151 0.630   1.00 18.37  ? 544 HOH B O   1 
HETATM 9140 O  O   . HOH BA 6 .   ? 8.377   17.805  -3.017  1.00 38.78  ? 545 HOH B O   1 
HETATM 9141 O  O   . HOH BA 6 .   ? 4.258   8.209   7.749   1.00 11.85  ? 546 HOH B O   1 
HETATM 9142 O  O   . HOH BA 6 .   ? -29.229 8.230   6.368   1.00 33.69  ? 547 HOH B O   1 
HETATM 9143 O  O   . HOH BA 6 .   ? -16.578 6.424   -18.152 1.00 37.61  ? 548 HOH B O   1 
HETATM 9144 O  O   . HOH BA 6 .   ? -16.138 -5.870  -12.862 1.00 27.43  ? 549 HOH B O   1 
HETATM 9145 O  O   . HOH BA 6 .   ? -14.337 -14.588 19.823  1.00 35.55  ? 550 HOH B O   1 
HETATM 9146 O  O   . HOH BA 6 .   ? -20.767 13.504  7.989   1.00 24.34  ? 551 HOH B O   1 
HETATM 9147 O  O   . HOH BA 6 .   ? -13.291 -12.098 11.723  1.00 12.37  ? 552 HOH B O   1 
HETATM 9148 O  O   . HOH BA 6 .   ? -6.073  14.652  1.774   1.00 36.33  ? 553 HOH B O   1 
HETATM 9149 O  O   . HOH BA 6 .   ? 4.890   9.175   14.434  1.00 17.38  ? 554 HOH B O   1 
HETATM 9150 O  O   . HOH BA 6 .   ? 2.327   6.023   -12.647 1.00 38.60  ? 555 HOH B O   1 
HETATM 9151 O  O   . HOH BA 6 .   ? 7.014   -0.984  17.760  1.00 24.18  ? 556 HOH B O   1 
HETATM 9152 O  O   . HOH BA 6 .   ? 6.560   4.832   13.816  1.00 13.04  ? 557 HOH B O   1 
HETATM 9153 O  O   . HOH BA 6 .   ? 11.479  14.432  -0.112  1.00 26.12  ? 558 HOH B O   1 
HETATM 9154 O  O   . HOH BA 6 .   ? -29.892 -3.058  6.858   1.00 28.92  ? 559 HOH B O   1 
HETATM 9155 O  O   . HOH BA 6 .   ? 0.794   7.976   -4.465  1.00 23.94  ? 560 HOH B O   1 
HETATM 9156 O  O   . HOH BA 6 .   ? 4.463   3.166   -5.800  1.00 29.09  ? 561 HOH B O   1 
HETATM 9157 O  O   . HOH BA 6 .   ? 1.912   8.743   -7.141  1.00 32.48  ? 562 HOH B O   1 
HETATM 9158 O  O   . HOH BA 6 .   ? -7.227  6.953   19.131  1.00 27.08  ? 563 HOH B O   1 
HETATM 9159 O  O   . HOH BA 6 .   ? -4.771  0.253   21.928  1.00 23.29  ? 564 HOH B O   1 
HETATM 9160 O  O   . HOH BA 6 .   ? -17.388 12.818  -12.515 1.00 49.84  ? 565 HOH B O   1 
HETATM 9161 O  O   . HOH BA 6 .   ? -0.361  -13.333 22.325  1.00 37.86  ? 566 HOH B O   1 
HETATM 9162 O  O   . HOH BA 6 .   ? 4.432   -2.125  6.532   1.00 17.63  ? 567 HOH B O   1 
HETATM 9163 O  O   . HOH BA 6 .   ? -3.841  13.160  -5.333  1.00 26.42  ? 568 HOH B O   1 
HETATM 9164 O  O   . HOH BA 6 .   ? -8.114  12.603  5.259   1.00 30.72  ? 569 HOH B O   1 
HETATM 9165 O  O   . HOH BA 6 .   ? -26.156 -9.737  6.011   1.00 24.46  ? 570 HOH B O   1 
HETATM 9166 O  O   . HOH BA 6 .   ? -30.784 7.178   -4.531  1.00 31.29  ? 571 HOH B O   1 
HETATM 9167 O  O   . HOH BA 6 .   ? 6.020   -2.373  1.870   1.00 23.62  ? 572 HOH B O   1 
HETATM 9168 O  O   . HOH BA 6 .   ? 4.113   -9.354  3.112   1.00 23.47  ? 573 HOH B O   1 
HETATM 9169 O  O   . HOH BA 6 .   ? -26.455 10.298  5.148   1.00 38.17  ? 574 HOH B O   1 
HETATM 9170 O  O   . HOH BA 6 .   ? -24.125 8.932   -1.724  1.00 19.26  ? 575 HOH B O   1 
HETATM 9171 O  O   . HOH BA 6 .   ? 6.028   -6.070  14.857  1.00 27.02  ? 576 HOH B O   1 
HETATM 9172 O  O   . HOH BA 6 .   ? -32.473 -3.978  -2.039  1.00 29.78  ? 577 HOH B O   1 
HETATM 9173 O  O   . HOH BA 6 .   ? -14.343 -2.933  25.426  1.00 35.84  ? 578 HOH B O   1 
HETATM 9174 O  O   . HOH BA 6 .   ? -25.148 -7.614  12.686  1.00 24.37  ? 579 HOH B O   1 
HETATM 9175 O  O   . HOH BA 6 .   ? -14.101 -10.985 23.895  1.00 22.49  ? 580 HOH B O   1 
HETATM 9176 O  O   . HOH BA 6 .   ? -19.496 -13.758 14.462  1.00 23.38  ? 581 HOH B O   1 
HETATM 9177 O  O   . HOH BA 6 .   ? -30.737 2.033   1.920   1.00 23.74  ? 582 HOH B O   1 
HETATM 9178 O  O   . HOH BA 6 .   ? 4.161   10.026  -6.798  1.00 35.51  ? 583 HOH B O   1 
HETATM 9179 O  O   . HOH BA 6 .   ? -22.626 6.265   -12.554 1.00 31.83  ? 584 HOH B O   1 
HETATM 9180 O  O   . HOH BA 6 .   ? -13.617 -18.684 -0.729  1.00 38.14  ? 585 HOH B O   1 
HETATM 9181 O  O   . HOH BA 6 .   ? -11.316 -15.904 3.203   1.00 30.10  ? 586 HOH B O   1 
HETATM 9182 O  O   . HOH BA 6 .   ? 8.802   6.472   -1.818  1.00 31.28  ? 587 HOH B O   1 
HETATM 9183 O  O   . HOH BA 6 .   ? -27.405 -5.841  -4.829  1.00 39.51  ? 588 HOH B O   1 
HETATM 9184 O  O   . HOH BA 6 .   ? 4.173   -5.988  24.876  1.00 39.11  ? 589 HOH B O   1 
HETATM 9185 O  O   . HOH BA 6 .   ? -2.910  7.152   -3.708  1.00 19.08  ? 590 HOH B O   1 
HETATM 9186 O  O   . HOH BA 6 .   ? -30.711 8.100   -11.510 1.00 27.98  ? 591 HOH B O   1 
HETATM 9187 O  O   . HOH BA 6 .   ? 4.186   -4.771  0.809   1.00 29.52  ? 592 HOH B O   1 
HETATM 9188 O  O   . HOH BA 6 .   ? 3.411   21.304  9.598   1.00 26.38  ? 593 HOH B O   1 
HETATM 9189 O  O   . HOH BA 6 .   ? 7.823   -3.288  3.617   1.00 20.54  ? 594 HOH B O   1 
HETATM 9190 O  O   . HOH BA 6 .   ? 1.310   -0.476  -12.352 1.00 32.07  ? 595 HOH B O   1 
HETATM 9191 O  O   . HOH BA 6 .   ? 10.022  8.278   -0.565  1.00 32.19  ? 596 HOH B O   1 
HETATM 9192 O  O   . HOH BA 6 .   ? -20.206 -13.431 11.737  1.00 32.11  ? 597 HOH B O   1 
HETATM 9193 O  O   . HOH BA 6 .   ? -14.756 -14.744 -2.466  1.00 16.75  ? 598 HOH B O   1 
HETATM 9194 O  O   . HOH BA 6 .   ? -19.823 -14.369 9.445   1.00 30.54  ? 599 HOH B O   1 
HETATM 9195 O  O   . HOH BA 6 .   ? -30.122 -3.900  10.031  1.00 26.63  ? 600 HOH B O   1 
HETATM 9196 O  O   . HOH BA 6 .   ? -6.563  15.475  16.011  1.00 34.38  ? 601 HOH B O   1 
HETATM 9197 O  O   . HOH BA 6 .   ? 4.397   -13.241 22.540  1.00 38.32  ? 602 HOH B O   1 
HETATM 9198 O  O   . HOH BA 6 .   ? -26.852 9.411   12.455  1.00 38.48  ? 603 HOH B O   1 
HETATM 9199 O  O   . HOH BA 6 .   ? -0.932  -12.850 4.566   1.00 38.09  ? 604 HOH B O   1 
HETATM 9200 O  O   . HOH BA 6 .   ? -0.012  -8.643  27.186  1.00 54.91  ? 605 HOH B O   1 
HETATM 9201 O  O   . HOH BA 6 .   ? -2.807  -10.933 -15.009 1.00 32.12  ? 606 HOH B O   1 
HETATM 9202 O  O   . HOH BA 6 .   ? -8.286  -19.331 27.629  1.00 24.17  ? 607 HOH B O   1 
HETATM 9203 O  O   . HOH BA 6 .   ? 7.470   1.409   19.791  1.00 29.02  ? 608 HOH B O   1 
HETATM 9204 O  O   . HOH BA 6 .   ? -7.937  17.617  10.909  1.00 39.19  ? 609 HOH B O   1 
HETATM 9205 O  O   . HOH BA 6 .   ? -1.481  -12.151 15.168  1.00 45.26  ? 610 HOH B O   1 
HETATM 9206 O  O   . HOH BA 6 .   ? -12.798 -16.599 24.128  1.00 45.91  ? 611 HOH B O   1 
HETATM 9207 O  O   . HOH BA 6 .   ? -24.475 -1.110  -11.742 1.00 33.78  ? 612 HOH B O   1 
HETATM 9208 O  O   . HOH BA 6 .   ? -20.212 -4.156  26.164  1.00 34.39  ? 613 HOH B O   1 
HETATM 9209 O  O   . HOH BA 6 .   ? 5.654   17.543  -13.603 1.00 44.21  ? 614 HOH B O   1 
HETATM 9210 O  O   . HOH BA 6 .   ? -7.763  -5.720  28.911  1.00 43.93  ? 615 HOH B O   1 
HETATM 9211 O  O   . HOH BA 6 .   ? -22.837 -4.447  -10.248 1.00 32.93  ? 616 HOH B O   1 
HETATM 9212 O  O   . HOH BA 6 .   ? -4.568  -13.510 21.012  1.00 50.99  ? 617 HOH B O   1 
HETATM 9213 O  O   . HOH BA 6 .   ? -13.903 -4.911  -13.018 1.00 34.85  ? 618 HOH B O   1 
HETATM 9214 O  O   . HOH BA 6 .   ? -17.530 -14.300 -2.259  1.00 28.77  ? 619 HOH B O   1 
HETATM 9215 O  O   . HOH BA 6 .   ? -21.485 -6.610  -9.965  1.00 33.54  ? 620 HOH B O   1 
HETATM 9216 O  O   . HOH BA 6 .   ? -31.498 8.946   1.053   1.00 50.72  ? 621 HOH B O   1 
HETATM 9217 O  O   . HOH BA 6 .   ? -24.733 8.177   0.978   1.00 26.19  ? 622 HOH B O   1 
HETATM 9218 O  O   . HOH BA 6 .   ? 1.125   22.510  9.999   1.00 41.35  ? 623 HOH B O   1 
HETATM 9219 O  O   . HOH BA 6 .   ? -13.255 13.626  -2.890  1.00 46.56  ? 624 HOH B O   1 
HETATM 9220 O  O   . HOH BA 6 .   ? -3.753  20.893  -18.341 1.00 41.86  ? 625 HOH B O   1 
HETATM 9221 O  O   . HOH BA 6 .   ? -15.695 8.477   -16.810 1.00 33.91  ? 626 HOH B O   1 
HETATM 9222 O  O   . HOH BA 6 .   ? -0.310  -13.375 -4.188  1.00 39.91  ? 627 HOH B O   1 
HETATM 9223 O  O   . HOH BA 6 .   ? -14.812 1.376   23.330  1.00 35.63  ? 628 HOH B O   1 
HETATM 9224 O  O   . HOH BA 6 .   ? -10.189 -3.996  -15.726 1.00 31.86  ? 629 HOH B O   1 
HETATM 9225 O  O   . HOH BA 6 .   ? 12.743  11.414  -3.549  1.00 34.05  ? 630 HOH B O   1 
HETATM 9226 O  O   . HOH BA 6 .   ? -11.067 14.737  -5.333  1.00 38.31  ? 631 HOH B O   1 
HETATM 9227 O  O   . HOH BA 6 .   ? 5.985   2.180   -3.524  1.00 26.80  ? 632 HOH B O   1 
HETATM 9228 O  O   . HOH BA 6 .   ? -29.225 -7.742  6.296   1.00 30.36  ? 633 HOH B O   1 
HETATM 9229 O  O   . HOH BA 6 .   ? 7.839   6.008   0.909   1.00 18.10  ? 634 HOH B O   1 
HETATM 9230 O  O   . HOH BA 6 .   ? -16.595 -14.234 27.797  1.00 23.57  ? 635 HOH B O   1 
HETATM 9231 O  O   . HOH BA 6 .   ? -21.310 -12.088 15.748  1.00 26.35  ? 636 HOH B O   1 
HETATM 9232 O  O   . HOH BA 6 .   ? -8.220  -5.745  -15.711 1.00 27.84  ? 637 HOH B O   1 
HETATM 9233 O  O   . HOH BA 6 .   ? -17.821 3.758   -20.791 1.00 38.63  ? 638 HOH B O   1 
HETATM 9234 O  O   . HOH BA 6 .   ? -30.050 4.709   2.290   1.00 34.01  ? 639 HOH B O   1 
HETATM 9235 O  O   . HOH BA 6 .   ? -13.533 -16.461 1.712   1.00 37.74  ? 640 HOH B O   1 
HETATM 9236 O  O   . HOH BA 6 .   ? -24.135 -11.046 5.351   1.00 43.90  ? 641 HOH B O   1 
HETATM 9237 O  O   . HOH BA 6 .   ? -19.256 -16.418 -4.120  1.00 37.72  ? 642 HOH B O   1 
HETATM 9238 O  O   . HOH BA 6 .   ? -12.982 -9.156  -12.726 1.00 28.67  ? 643 HOH B O   1 
HETATM 9239 O  O   . HOH BA 6 .   ? -11.513 -8.322  -14.993 1.00 26.83  ? 644 HOH B O   1 
HETATM 9240 O  O   . HOH BA 6 .   ? 5.749   -4.358  7.381   1.00 35.80  ? 645 HOH B O   1 
HETATM 9241 O  O   . HOH BA 6 .   ? 4.738   -12.021 24.594  1.00 44.28  ? 646 HOH B O   1 
HETATM 9242 O  O   . HOH BA 6 .   ? 7.613   -9.403  15.731  1.00 20.58  ? 647 HOH B O   1 
HETATM 9243 O  O   . HOH BA 6 .   ? -11.641 -1.769  24.844  1.00 38.95  ? 648 HOH B O   1 
HETATM 9244 O  O   . HOH BA 6 .   ? 5.258   -13.176 15.783  1.00 29.59  ? 649 HOH B O   1 
HETATM 9245 O  O   . HOH BA 6 .   ? -3.248  16.213  -8.589  1.00 35.36  ? 650 HOH B O   1 
HETATM 9246 O  O   . HOH BA 6 .   ? -18.397 -12.001 23.876  1.00 32.82  ? 651 HOH B O   1 
HETATM 9247 O  O   . HOH BA 6 .   ? 5.102   -7.355  1.186   1.00 22.72  ? 652 HOH B O   1 
HETATM 9248 O  O   . HOH BA 6 .   ? 5.874   -0.536  -2.302  1.00 35.21  ? 653 HOH B O   1 
HETATM 9249 O  O   . HOH BA 6 .   ? -17.555 -12.945 21.272  1.00 26.90  ? 654 HOH B O   1 
HETATM 9250 O  O   . HOH BA 6 .   ? -17.393 -12.565 29.941  1.00 24.52  ? 655 HOH B O   1 
HETATM 9251 O  O   . HOH BA 6 .   ? -15.285 -16.885 -0.884  1.00 37.44  ? 656 HOH B O   1 
HETATM 9252 O  O   . HOH BA 6 .   ? -4.215  -13.913 9.781   1.00 34.39  ? 657 HOH B O   1 
HETATM 9253 O  O   . HOH BA 6 .   ? -3.617  15.273  18.538  1.00 38.35  ? 658 HOH B O   1 
HETATM 9254 O  O   . HOH BA 6 .   ? -20.814 -10.789 -9.933  1.00 27.73  ? 659 HOH B O   1 
HETATM 9255 O  O   . HOH BA 6 .   ? 0.260   20.461  -15.010 1.00 32.59  ? 660 HOH B O   1 
HETATM 9256 O  O   . HOH BA 6 .   ? 6.320   18.747  2.190   1.00 27.72  ? 661 HOH B O   1 
HETATM 9257 O  O   . HOH BA 6 .   ? -27.358 8.754   1.361   1.00 35.32  ? 662 HOH B O   1 
HETATM 9258 O  O   . HOH BA 6 .   ? -2.940  18.918  10.621  1.00 37.65  ? 663 HOH B O   1 
HETATM 9259 O  O   . HOH BA 6 .   ? -13.296 -11.889 -13.161 1.00 26.67  ? 664 HOH B O   1 
HETATM 9260 O  O   . HOH BA 6 .   ? -29.423 7.018   1.170   1.00 33.11  ? 665 HOH B O   1 
HETATM 9261 O  O   . HOH BA 6 .   ? -9.569  15.898  7.063   1.00 38.11  ? 666 HOH B O   1 
HETATM 9262 O  O   . HOH BA 6 .   ? -0.743  -14.313 6.489   1.00 40.69  ? 667 HOH B O   1 
HETATM 9263 O  O   . HOH BA 6 .   ? -19.067 -16.203 15.493  1.00 41.06  ? 668 HOH B O   1 
HETATM 9264 O  O   . HOH BA 6 .   ? -1.953  21.227  -16.548 1.00 36.40  ? 669 HOH B O   1 
HETATM 9265 O  O   . HOH BA 6 .   ? 12.807  11.439  -6.414  1.00 39.70  ? 670 HOH B O   1 
HETATM 9266 O  O   . HOH BA 6 .   ? -7.691  -10.055 -15.990 1.00 21.96  ? 671 HOH B O   1 
HETATM 9267 O  O   . HOH BA 6 .   ? -13.881 -15.852 -11.465 1.00 29.51  ? 672 HOH B O   1 
HETATM 9268 O  O   . HOH BA 6 .   ? -10.253 -13.212 30.646  1.00 24.55  ? 673 HOH B O   1 
HETATM 9269 O  O   . HOH BA 6 .   ? -33.470 2.611   2.682   1.00 45.83  ? 674 HOH B O   1 
HETATM 9270 O  O   . HOH BA 6 .   ? -5.555  19.056  9.594   1.00 49.52  ? 675 HOH B O   1 
HETATM 9271 O  O   . HOH BA 6 .   ? -1.990  -15.323 10.846  1.00 34.76  ? 676 HOH B O   1 
HETATM 9272 O  O   . HOH BA 6 .   ? -25.602 -6.018  -9.087  1.00 46.79  ? 677 HOH B O   1 
HETATM 9273 O  O   . HOH BA 6 .   ? -21.704 -13.592 18.152  1.00 45.41  ? 678 HOH B O   1 
HETATM 9274 O  O   . HOH CA 6 .   ? 20.473  3.935   -46.975 1.00 28.81  ? 401 HOH C O   1 
HETATM 9275 O  O   . HOH CA 6 .   ? 33.667  18.291  -27.891 1.00 52.96  ? 402 HOH C O   1 
HETATM 9276 O  O   . HOH CA 6 .   ? 28.679  6.803   -19.327 1.00 40.45  ? 403 HOH C O   1 
HETATM 9277 O  O   . HOH CA 6 .   ? 27.157  25.317  -32.308 1.00 21.15  ? 404 HOH C O   1 
HETATM 9278 O  O   . HOH CA 6 .   ? 20.584  -1.773  -50.995 1.00 43.02  ? 405 HOH C O   1 
HETATM 9279 O  O   . HOH CA 6 .   ? 40.707  13.863  -36.813 1.00 26.35  ? 406 HOH C O   1 
HETATM 9280 O  O   . HOH CA 6 .   ? 20.177  1.155   -45.348 1.00 30.98  ? 407 HOH C O   1 
HETATM 9281 O  O   . HOH CA 6 .   ? 35.529  -21.294 -51.180 1.00 20.99  ? 408 HOH C O   1 
HETATM 9282 O  O   . HOH CA 6 .   ? 56.140  8.265   -37.828 1.00 35.33  ? 409 HOH C O   1 
HETATM 9283 O  O   . HOH CA 6 .   ? 24.318  -3.524  -44.918 1.00 29.59  ? 410 HOH C O   1 
HETATM 9284 O  O   . HOH CA 6 .   ? 22.165  -6.246  -31.604 1.00 24.68  ? 411 HOH C O   1 
HETATM 9285 O  O   . HOH CA 6 .   ? 22.001  -8.601  -39.919 1.00 30.13  ? 412 HOH C O   1 
HETATM 9286 O  O   . HOH CA 6 .   ? 26.166  3.442   -47.351 1.00 25.85  ? 413 HOH C O   1 
HETATM 9287 O  O   . HOH CA 6 .   ? 32.375  5.155   -30.519 1.00 15.90  ? 414 HOH C O   1 
HETATM 9288 O  O   . HOH CA 6 .   ? 24.379  -12.878 -41.610 1.00 33.28  ? 415 HOH C O   1 
HETATM 9289 O  O   . HOH CA 6 .   ? 61.424  -1.106  -33.126 1.00 31.61  ? 416 HOH C O   1 
HETATM 9290 O  O   . HOH CA 6 .   ? 47.001  9.195   -27.339 1.00 30.11  ? 417 HOH C O   1 
HETATM 9291 O  O   . HOH CA 6 .   ? 31.547  -20.802 -48.385 1.00 43.50  ? 418 HOH C O   1 
HETATM 9292 O  O   . HOH CA 6 .   ? 40.710  -5.345  -52.421 1.00 46.01  ? 419 HOH C O   1 
HETATM 9293 O  O   . HOH CA 6 .   ? 45.061  -7.011  -45.653 1.00 21.29  ? 420 HOH C O   1 
HETATM 9294 O  O   . HOH CA 6 .   ? 43.704  -5.608  -50.364 1.00 27.62  ? 421 HOH C O   1 
HETATM 9295 O  O   . HOH CA 6 .   ? 36.120  -9.564  -53.725 1.00 30.61  ? 422 HOH C O   1 
HETATM 9296 O  O   . HOH CA 6 .   ? 41.895  -17.709 -53.686 1.00 32.43  ? 423 HOH C O   1 
HETATM 9297 O  O   . HOH CA 6 .   ? 51.323  8.426   -31.550 1.00 26.10  ? 424 HOH C O   1 
HETATM 9298 O  O   . HOH CA 6 .   ? 23.932  13.085  -42.342 1.00 19.83  ? 425 HOH C O   1 
HETATM 9299 O  O   . HOH CA 6 .   ? 60.127  1.614   -28.828 1.00 36.83  ? 426 HOH C O   1 
HETATM 9300 O  O   . HOH CA 6 .   ? 28.579  -8.006  -17.326 1.00 28.95  ? 427 HOH C O   1 
HETATM 9301 O  O   . HOH CA 6 .   ? 27.134  -10.203 -26.761 1.00 28.27  ? 428 HOH C O   1 
HETATM 9302 O  O   . HOH CA 6 .   ? 33.091  -1.417  -49.028 1.00 20.25  ? 429 HOH C O   1 
HETATM 9303 O  O   . HOH CA 6 .   ? 29.558  -4.843  -22.172 1.00 19.24  ? 430 HOH C O   1 
HETATM 9304 O  O   . HOH CA 6 .   ? 38.861  -2.750  -11.666 1.00 38.24  ? 431 HOH C O   1 
HETATM 9305 O  O   . HOH CA 6 .   ? 29.880  6.460   -22.133 1.00 37.30  ? 432 HOH C O   1 
HETATM 9306 O  O   . HOH CA 6 .   ? 27.266  16.367  -41.256 1.00 17.27  ? 433 HOH C O   1 
HETATM 9307 O  O   . HOH CA 6 .   ? 53.086  14.526  -44.922 1.00 39.85  ? 434 HOH C O   1 
HETATM 9308 O  O   . HOH CA 6 .   ? 22.465  -2.011  -31.440 1.00 37.19  ? 435 HOH C O   1 
HETATM 9309 O  O   . HOH CA 6 .   ? 24.892  6.627   -34.744 1.00 13.40  ? 436 HOH C O   1 
HETATM 9310 O  O   . HOH CA 6 .   ? 56.540  4.510   -42.234 1.00 23.91  ? 437 HOH C O   1 
HETATM 9311 O  O   . HOH CA 6 .   ? 46.261  11.090  -13.017 1.00 71.53  ? 438 HOH C O   1 
HETATM 9312 O  O   . HOH CA 6 .   ? 33.341  11.994  -10.962 1.00 27.90  ? 439 HOH C O   1 
HETATM 9313 O  O   . HOH CA 6 .   ? 25.142  8.268   -28.085 1.00 18.55  ? 440 HOH C O   1 
HETATM 9314 O  O   . HOH CA 6 .   ? 39.112  11.376  -31.915 1.00 34.49  ? 441 HOH C O   1 
HETATM 9315 O  O   . HOH CA 6 .   ? 26.039  7.090   -41.210 1.00 12.79  ? 442 HOH C O   1 
HETATM 9316 O  O   . HOH CA 6 .   ? 47.842  -13.073 -39.346 1.00 32.17  ? 443 HOH C O   1 
HETATM 9317 O  O   . HOH CA 6 .   ? 35.406  17.121  -41.386 1.00 35.85  ? 444 HOH C O   1 
HETATM 9318 O  O   . HOH CA 6 .   ? 47.035  7.500   -22.996 1.00 26.13  ? 445 HOH C O   1 
HETATM 9319 O  O   . HOH CA 6 .   ? 52.046  -4.958  -18.338 1.00 38.53  ? 446 HOH C O   1 
HETATM 9320 O  O   . HOH CA 6 .   ? 46.693  2.150   -47.437 1.00 37.44  ? 447 HOH C O   1 
HETATM 9321 O  O   . HOH CA 6 .   ? 26.310  -8.527  -16.111 1.00 31.12  ? 448 HOH C O   1 
HETATM 9322 O  O   . HOH CA 6 .   ? 35.252  19.761  -36.007 1.00 38.55  ? 449 HOH C O   1 
HETATM 9323 O  O   . HOH CA 6 .   ? 25.983  5.640   -43.478 1.00 19.77  ? 450 HOH C O   1 
HETATM 9324 O  O   . HOH CA 6 .   ? 32.584  -13.294 -37.043 1.00 25.01  ? 451 HOH C O   1 
HETATM 9325 O  O   . HOH CA 6 .   ? 22.739  -11.314 -44.759 1.00 30.17  ? 452 HOH C O   1 
HETATM 9326 O  O   . HOH CA 6 .   ? 23.893  -3.182  -26.663 1.00 46.16  ? 453 HOH C O   1 
HETATM 9327 O  O   . HOH CA 6 .   ? 59.687  -2.135  -35.619 1.00 32.89  ? 454 HOH C O   1 
HETATM 9328 O  O   . HOH CA 6 .   ? 43.148  -2.281  -40.504 1.00 14.83  ? 455 HOH C O   1 
HETATM 9329 O  O   . HOH CA 6 .   ? 25.147  -1.570  -40.701 1.00 14.38  ? 456 HOH C O   1 
HETATM 9330 O  O   . HOH CA 6 .   ? 25.537  -2.853  -48.467 1.00 18.77  ? 457 HOH C O   1 
HETATM 9331 O  O   . HOH CA 6 .   ? 35.233  6.144   -26.925 1.00 23.44  ? 458 HOH C O   1 
HETATM 9332 O  O   . HOH CA 6 .   ? 47.196  9.234   -30.334 1.00 29.24  ? 459 HOH C O   1 
HETATM 9333 O  O   . HOH CA 6 .   ? 51.366  -2.425  -43.782 1.00 30.41  ? 460 HOH C O   1 
HETATM 9334 O  O   . HOH CA 6 .   ? 28.573  3.350   -43.599 1.00 14.93  ? 461 HOH C O   1 
HETATM 9335 O  O   . HOH CA 6 .   ? 28.225  18.457  -31.734 1.00 19.05  ? 462 HOH C O   1 
HETATM 9336 O  O   . HOH CA 6 .   ? 50.350  -4.381  -16.353 1.00 38.46  ? 463 HOH C O   1 
HETATM 9337 O  O   . HOH CA 6 .   ? 25.744  -3.341  -42.665 1.00 18.24  ? 464 HOH C O   1 
HETATM 9338 O  O   . HOH CA 6 .   ? 23.343  -4.541  -36.018 1.00 19.54  ? 465 HOH C O   1 
HETATM 9339 O  O   . HOH CA 6 .   ? 26.962  -0.767  -32.348 1.00 12.05  ? 466 HOH C O   1 
HETATM 9340 O  O   . HOH CA 6 .   ? 34.022  16.070  -38.346 1.00 16.28  ? 467 HOH C O   1 
HETATM 9341 O  O   . HOH CA 6 .   ? 24.655  -2.068  -23.783 1.00 30.50  ? 468 HOH C O   1 
HETATM 9342 O  O   . HOH CA 6 .   ? 51.135  7.404   -28.590 1.00 28.49  ? 469 HOH C O   1 
HETATM 9343 O  O   . HOH CA 6 .   ? 41.696  6.812   -9.890  1.00 32.51  ? 470 HOH C O   1 
HETATM 9344 O  O   . HOH CA 6 .   ? 53.111  -11.086 -37.119 1.00 40.68  ? 471 HOH C O   1 
HETATM 9345 O  O   . HOH CA 6 .   ? 24.217  -14.286 -48.298 1.00 46.23  ? 472 HOH C O   1 
HETATM 9346 O  O   . HOH CA 6 .   ? 33.761  13.669  -44.128 1.00 20.83  ? 473 HOH C O   1 
HETATM 9347 O  O   . HOH CA 6 .   ? 29.529  -13.940 -28.126 1.00 32.10  ? 474 HOH C O   1 
HETATM 9348 O  O   . HOH CA 6 .   ? 54.708  9.709   -34.424 1.00 37.35  ? 475 HOH C O   1 
HETATM 9349 O  O   . HOH CA 6 .   ? 25.665  5.423   -24.039 1.00 27.28  ? 476 HOH C O   1 
HETATM 9350 O  O   . HOH CA 6 .   ? 48.035  -11.064 -16.136 1.00 40.40  ? 477 HOH C O   1 
HETATM 9351 O  O   . HOH CA 6 .   ? 42.189  10.179  -28.176 1.00 65.09  ? 478 HOH C O   1 
HETATM 9352 O  O   . HOH CA 6 .   ? 46.763  -13.023 -53.122 1.00 20.64  ? 479 HOH C O   1 
HETATM 9353 O  O   . HOH CA 6 .   ? 47.506  -1.567  -10.162 1.00 36.16  ? 480 HOH C O   1 
HETATM 9354 O  O   . HOH CA 6 .   ? 44.585  -13.799 -44.705 1.00 22.71  ? 481 HOH C O   1 
HETATM 9355 O  O   . HOH CA 6 .   ? 47.698  -8.894  -51.408 1.00 34.21  ? 482 HOH C O   1 
HETATM 9356 O  O   . HOH CA 6 .   ? 27.586  16.166  -29.452 1.00 34.05  ? 483 HOH C O   1 
HETATM 9357 O  O   . HOH CA 6 .   ? 43.485  4.241   -44.409 1.00 21.36  ? 484 HOH C O   1 
HETATM 9358 O  O   . HOH CA 6 .   ? 38.201  -14.185 -13.541 1.00 44.59  ? 485 HOH C O   1 
HETATM 9359 O  O   . HOH CA 6 .   ? 52.863  6.364   -31.618 1.00 24.62  ? 486 HOH C O   1 
HETATM 9360 O  O   . HOH CA 6 .   ? 48.108  18.880  -41.369 1.00 41.20  ? 487 HOH C O   1 
HETATM 9361 O  O   . HOH CA 6 .   ? 41.515  -8.383  -55.080 1.00 22.03  ? 488 HOH C O   1 
HETATM 9362 O  O   . HOH CA 6 .   ? 33.773  1.627   -16.562 1.00 23.22  ? 489 HOH C O   1 
HETATM 9363 O  O   . HOH CA 6 .   ? 43.643  -12.591 -25.967 1.00 26.76  ? 490 HOH C O   1 
HETATM 9364 O  O   . HOH CA 6 .   ? 21.964  6.899   -32.264 1.00 12.89  ? 491 HOH C O   1 
HETATM 9365 O  O   . HOH CA 6 .   ? 40.294  -16.449 -30.346 1.00 35.27  ? 492 HOH C O   1 
HETATM 9366 O  O   . HOH CA 6 .   ? 58.260  -1.942  -30.085 1.00 30.85  ? 493 HOH C O   1 
HETATM 9367 O  O   . HOH CA 6 .   ? 42.149  16.860  -44.638 1.00 31.55  ? 494 HOH C O   1 
HETATM 9368 O  O   . HOH CA 6 .   ? 20.674  13.662  -35.691 1.00 13.35  ? 495 HOH C O   1 
HETATM 9369 O  O   . HOH CA 6 .   ? 33.166  16.325  -14.657 1.00 38.55  ? 496 HOH C O   1 
HETATM 9370 O  O   . HOH CA 6 .   ? 37.315  9.032   -47.513 1.00 34.68  ? 497 HOH C O   1 
HETATM 9371 O  O   . HOH CA 6 .   ? 37.602  -10.331 -33.339 1.00 17.67  ? 498 HOH C O   1 
HETATM 9372 O  O   . HOH CA 6 .   ? 46.109  -11.386 -40.578 1.00 29.45  ? 499 HOH C O   1 
HETATM 9373 O  O   . HOH CA 6 .   ? 41.049  7.370   -46.885 1.00 27.41  ? 500 HOH C O   1 
HETATM 9374 O  O   . HOH CA 6 .   ? 26.405  -13.411 -34.673 1.00 26.24  ? 501 HOH C O   1 
HETATM 9375 O  O   . HOH CA 6 .   ? 22.204  -5.011  -41.106 1.00 25.43  ? 502 HOH C O   1 
HETATM 9376 O  O   . HOH CA 6 .   ? 54.567  -9.789  -31.019 1.00 29.54  ? 503 HOH C O   1 
HETATM 9377 O  O   . HOH CA 6 .   ? 55.620  -8.160  -32.807 1.00 28.00  ? 504 HOH C O   1 
HETATM 9378 O  O   . HOH CA 6 .   ? 31.863  2.596   -43.803 1.00 15.17  ? 505 HOH C O   1 
HETATM 9379 O  O   . HOH CA 6 .   ? 24.203  -0.646  -33.011 1.00 19.55  ? 506 HOH C O   1 
HETATM 9380 O  O   . HOH CA 6 .   ? 23.252  4.821   -36.104 1.00 10.70  ? 507 HOH C O   1 
HETATM 9381 O  O   . HOH CA 6 .   ? 21.952  -13.599 -35.801 1.00 38.32  ? 508 HOH C O   1 
HETATM 9382 O  O   . HOH CA 6 .   ? 52.716  8.819   -24.119 1.00 35.23  ? 509 HOH C O   1 
HETATM 9383 O  O   . HOH CA 6 .   ? 35.951  18.022  -38.284 1.00 27.59  ? 510 HOH C O   1 
HETATM 9384 O  O   . HOH CA 6 .   ? 44.380  -15.176 -50.652 1.00 34.63  ? 511 HOH C O   1 
HETATM 9385 O  O   . HOH CA 6 .   ? 43.132  -1.358  -10.975 1.00 39.91  ? 512 HOH C O   1 
HETATM 9386 O  O   . HOH CA 6 .   ? 26.585  9.434   -34.817 1.00 13.75  ? 513 HOH C O   1 
HETATM 9387 O  O   . HOH CA 6 .   ? 51.209  11.021  -16.256 1.00 51.41  ? 514 HOH C O   1 
HETATM 9388 O  O   . HOH CA 6 .   ? 32.451  11.434  -43.278 1.00 14.21  ? 515 HOH C O   1 
HETATM 9389 O  O   . HOH CA 6 .   ? 35.673  -0.884  -48.474 1.00 19.91  ? 516 HOH C O   1 
HETATM 9390 O  O   . HOH CA 6 .   ? 52.472  5.047   -48.985 1.00 33.34  ? 517 HOH C O   1 
HETATM 9391 O  O   . HOH CA 6 .   ? 38.836  -19.613 -45.993 1.00 40.49  ? 518 HOH C O   1 
HETATM 9392 O  O   . HOH CA 6 .   ? 40.925  4.398   -45.794 1.00 30.02  ? 519 HOH C O   1 
HETATM 9393 O  O   . HOH CA 6 .   ? 22.284  10.998  -29.437 1.00 18.17  ? 520 HOH C O   1 
HETATM 9394 O  O   . HOH CA 6 .   ? 28.782  9.092   -22.425 1.00 32.49  ? 521 HOH C O   1 
HETATM 9395 O  O   . HOH CA 6 .   ? 37.600  14.059  -28.619 1.00 41.52  ? 522 HOH C O   1 
HETATM 9396 O  O   . HOH CA 6 .   ? 23.681  -8.770  -29.191 1.00 32.50  ? 523 HOH C O   1 
HETATM 9397 O  O   . HOH CA 6 .   ? 26.258  6.768   -13.923 1.00 42.53  ? 524 HOH C O   1 
HETATM 9398 O  O   . HOH CA 6 .   ? 28.568  -0.190  -14.426 1.00 35.19  ? 525 HOH C O   1 
HETATM 9399 O  O   . HOH CA 6 .   ? 38.211  5.151   -45.226 1.00 18.59  ? 526 HOH C O   1 
HETATM 9400 O  O   . HOH CA 6 .   ? 53.768  -10.027 -22.621 1.00 38.89  ? 527 HOH C O   1 
HETATM 9401 O  O   . HOH CA 6 .   ? 22.188  -0.271  -44.168 1.00 22.43  ? 528 HOH C O   1 
HETATM 9402 O  O   . HOH CA 6 .   ? 34.758  -7.903  -11.246 1.00 52.31  ? 529 HOH C O   1 
HETATM 9403 O  O   . HOH CA 6 .   ? 44.145  15.082  -35.063 1.00 35.11  ? 530 HOH C O   1 
HETATM 9404 O  O   . HOH CA 6 .   ? 31.435  12.866  -46.504 1.00 26.37  ? 531 HOH C O   1 
HETATM 9405 O  O   . HOH CA 6 .   ? 46.666  13.955  -47.831 1.00 38.76  ? 532 HOH C O   1 
HETATM 9406 O  O   . HOH CA 6 .   ? 28.310  6.911   -44.082 1.00 19.58  ? 533 HOH C O   1 
HETATM 9407 O  O   . HOH CA 6 .   ? 29.147  6.176   -47.409 1.00 18.98  ? 534 HOH C O   1 
HETATM 9408 O  O   . HOH CA 6 .   ? 39.757  -12.080 -55.283 1.00 27.31  ? 535 HOH C O   1 
HETATM 9409 O  O   . HOH CA 6 .   ? 40.551  -15.686 -25.379 1.00 32.28  ? 536 HOH C O   1 
HETATM 9410 O  O   . HOH CA 6 .   ? 27.984  -10.575 -22.481 1.00 28.03  ? 537 HOH C O   1 
HETATM 9411 O  O   . HOH CA 6 .   ? 31.843  -2.068  -51.787 1.00 32.43  ? 538 HOH C O   1 
HETATM 9412 O  O   . HOH CA 6 .   ? 41.912  -3.831  -48.470 1.00 25.27  ? 539 HOH C O   1 
HETATM 9413 O  O   . HOH CA 6 .   ? 28.656  3.767   -46.237 1.00 18.04  ? 540 HOH C O   1 
HETATM 9414 O  O   . HOH CA 6 .   ? 46.718  -16.515 -35.851 1.00 36.14  ? 541 HOH C O   1 
HETATM 9415 O  O   . HOH CA 6 .   ? 27.648  2.540   -52.534 1.00 36.45  ? 542 HOH C O   1 
HETATM 9416 O  O   . HOH CA 6 .   ? 26.326  11.833  -45.824 1.00 35.66  ? 543 HOH C O   1 
HETATM 9417 O  O   . HOH CA 6 .   ? 43.845  14.010  -47.714 1.00 32.69  ? 544 HOH C O   1 
HETATM 9418 O  O   . HOH CA 6 .   ? 23.603  5.828   -40.803 1.00 13.87  ? 545 HOH C O   1 
HETATM 9419 O  O   . HOH CA 6 .   ? 39.524  18.123  -40.860 1.00 36.74  ? 546 HOH C O   1 
HETATM 9420 O  O   . HOH CA 6 .   ? 31.465  2.301   -14.551 1.00 28.40  ? 547 HOH C O   1 
HETATM 9421 O  O   . HOH CA 6 .   ? 26.351  9.779   -41.861 1.00 16.10  ? 548 HOH C O   1 
HETATM 9422 O  O   . HOH CA 6 .   ? 19.410  -7.643  -17.514 1.00 37.42  ? 549 HOH C O   1 
HETATM 9423 O  O   . HOH CA 6 .   ? 58.066  -7.157  -31.199 1.00 31.66  ? 550 HOH C O   1 
HETATM 9424 O  O   . HOH CA 6 .   ? 30.336  15.627  -43.812 1.00 35.75  ? 551 HOH C O   1 
HETATM 9425 O  O   . HOH CA 6 .   ? 53.289  6.213   -23.525 1.00 30.05  ? 552 HOH C O   1 
HETATM 9426 O  O   . HOH CA 6 .   ? 51.840  10.138  -33.493 1.00 27.73  ? 553 HOH C O   1 
HETATM 9427 O  O   . HOH CA 6 .   ? 29.580  -12.361 -23.904 1.00 29.97  ? 554 HOH C O   1 
HETATM 9428 O  O   . HOH CA 6 .   ? 42.345  11.881  -25.341 1.00 40.30  ? 555 HOH C O   1 
HETATM 9429 O  O   . HOH CA 6 .   ? 39.117  -26.671 -44.282 1.00 26.60  ? 556 HOH C O   1 
HETATM 9430 O  O   . HOH CA 6 .   ? 49.955  12.274  -33.001 1.00 32.15  ? 557 HOH C O   1 
HETATM 9431 O  O   . HOH CA 6 .   ? 32.529  0.422   -50.964 1.00 33.80  ? 558 HOH C O   1 
HETATM 9432 O  O   . HOH CA 6 .   ? 40.228  -13.971 -36.439 1.00 19.96  ? 559 HOH C O   1 
HETATM 9433 O  O   . HOH CA 6 .   ? 26.912  4.053   -50.073 1.00 34.07  ? 560 HOH C O   1 
HETATM 9434 O  O   . HOH CA 6 .   ? 42.076  -13.930 -48.796 1.00 29.61  ? 561 HOH C O   1 
HETATM 9435 O  O   . HOH CA 6 .   ? 40.184  6.705   -26.882 1.00 41.90  ? 562 HOH C O   1 
HETATM 9436 O  O   . HOH CA 6 .   ? 29.003  -12.098 -40.928 1.00 35.33  ? 563 HOH C O   1 
HETATM 9437 O  O   . HOH CA 6 .   ? 30.146  -10.547 -16.839 1.00 51.04  ? 564 HOH C O   1 
HETATM 9438 O  O   . HOH CA 6 .   ? 38.647  13.975  -42.891 1.00 26.25  ? 565 HOH C O   1 
HETATM 9439 O  O   . HOH CA 6 .   ? 46.150  -17.035 -38.550 1.00 36.49  ? 566 HOH C O   1 
HETATM 9440 O  O   . HOH CA 6 .   ? 40.698  4.005   -6.662  1.00 28.28  ? 567 HOH C O   1 
HETATM 9441 O  O   . HOH CA 6 .   ? 29.560  -11.595 -26.553 1.00 23.11  ? 568 HOH C O   1 
HETATM 9442 O  O   . HOH CA 6 .   ? 53.697  7.098   -27.987 1.00 32.23  ? 569 HOH C O   1 
HETATM 9443 O  O   . HOH CA 6 .   ? 27.477  -12.427 -30.024 1.00 34.45  ? 570 HOH C O   1 
HETATM 9444 O  O   . HOH CA 6 .   ? 26.626  6.583   -21.148 1.00 37.04  ? 571 HOH C O   1 
HETATM 9445 O  O   . HOH CA 6 .   ? 20.835  -1.054  -30.090 1.00 23.58  ? 572 HOH C O   1 
HETATM 9446 O  O   . HOH CA 6 .   ? 27.970  -10.349 -51.820 1.00 47.77  ? 573 HOH C O   1 
HETATM 9447 O  O   . HOH CA 6 .   ? 56.059  14.250  -35.388 1.00 44.24  ? 574 HOH C O   1 
HETATM 9448 O  O   . HOH CA 6 .   ? 48.563  11.458  -24.333 1.00 35.27  ? 575 HOH C O   1 
HETATM 9449 O  O   . HOH CA 6 .   ? 44.663  9.437   -29.415 1.00 32.28  ? 576 HOH C O   1 
HETATM 9450 O  O   . HOH CA 6 .   ? 39.400  -5.041  -49.603 1.00 33.92  ? 577 HOH C O   1 
HETATM 9451 O  O   . HOH CA 6 .   ? 32.305  7.799   -22.538 1.00 33.30  ? 578 HOH C O   1 
HETATM 9452 O  O   . HOH CA 6 .   ? 45.219  -5.956  -48.126 1.00 39.64  ? 579 HOH C O   1 
HETATM 9453 O  O   . HOH CA 6 .   ? 44.199  -4.254  -9.228  1.00 41.46  ? 580 HOH C O   1 
HETATM 9454 O  O   . HOH CA 6 .   ? 37.661  5.843   -27.973 1.00 27.25  ? 581 HOH C O   1 
HETATM 9455 O  O   . HOH CA 6 .   ? 41.476  14.131  -34.291 1.00 47.80  ? 582 HOH C O   1 
HETATM 9456 O  O   . HOH CA 6 .   ? 44.705  -5.058  -52.862 1.00 31.99  ? 583 HOH C O   1 
HETATM 9457 O  O   . HOH CA 6 .   ? 55.686  11.890  -43.451 1.00 46.93  ? 584 HOH C O   1 
HETATM 9458 O  O   . HOH CA 6 .   ? 26.356  -4.616  -52.426 1.00 52.54  ? 585 HOH C O   1 
HETATM 9459 O  O   . HOH CA 6 .   ? 40.581  6.709   -7.469  1.00 33.71  ? 586 HOH C O   1 
HETATM 9460 O  O   . HOH CA 6 .   ? 54.001  5.222   -26.049 1.00 35.15  ? 587 HOH C O   1 
HETATM 9461 O  O   . HOH CA 6 .   ? 22.971  -3.936  -48.330 1.00 27.88  ? 588 HOH C O   1 
HETATM 9462 O  O   . HOH CA 6 .   ? 28.073  15.346  -45.495 1.00 30.56  ? 589 HOH C O   1 
HETATM 9463 O  O   . HOH CA 6 .   ? 35.438  1.311   -50.335 1.00 35.80  ? 590 HOH C O   1 
HETATM 9464 O  O   . HOH CA 6 .   ? 47.875  11.927  -26.747 1.00 41.63  ? 591 HOH C O   1 
HETATM 9465 O  O   . HOH CA 6 .   ? 48.238  -15.886 -39.969 1.00 36.88  ? 592 HOH C O   1 
HETATM 9466 O  O   . HOH CA 6 .   ? 58.375  4.883   -40.561 1.00 80.63  ? 593 HOH C O   1 
HETATM 9467 O  O   . HOH CA 6 .   ? 20.979  -3.766  -32.260 1.00 32.69  ? 594 HOH C O   1 
HETATM 9468 O  O   . HOH CA 6 .   ? 22.552  -2.706  -34.054 1.00 29.59  ? 595 HOH C O   1 
HETATM 9469 O  O   . HOH CA 6 .   ? 22.376  8.675   -27.947 1.00 19.79  ? 596 HOH C O   1 
HETATM 9470 O  O   . HOH CA 6 .   ? 21.770  -3.881  -38.059 1.00 26.73  ? 597 HOH C O   1 
HETATM 9471 O  O   . HOH CA 6 .   ? 38.136  -2.494  -48.760 1.00 34.24  ? 598 HOH C O   1 
HETATM 9472 O  O   . HOH CA 6 .   ? 39.537  11.745  -46.732 1.00 44.73  ? 599 HOH C O   1 
HETATM 9473 O  O   . HOH CA 6 .   ? 44.865  -16.128 -45.813 1.00 38.75  ? 600 HOH C O   1 
HETATM 9474 O  O   . HOH CA 6 .   ? 17.325  -5.035  -15.748 1.00 35.41  ? 601 HOH C O   1 
HETATM 9475 O  O   . HOH CA 6 .   ? 36.301  13.899  -45.409 1.00 47.96  ? 602 HOH C O   1 
HETATM 9476 O  O   . HOH CA 6 .   ? 30.867  -14.480 -35.414 1.00 42.45  ? 603 HOH C O   1 
HETATM 9477 O  O   . HOH CA 6 .   ? 41.729  -26.056 -44.606 1.00 36.15  ? 604 HOH C O   1 
HETATM 9478 O  O   . HOH CA 6 .   ? 46.985  -12.955 -14.862 1.00 41.15  ? 605 HOH C O   1 
HETATM 9479 O  O   . HOH CA 6 .   ? 24.067  -15.020 -34.825 1.00 44.96  ? 606 HOH C O   1 
HETATM 9480 O  O   . HOH CA 6 .   ? 26.840  7.403   -47.626 1.00 29.15  ? 607 HOH C O   1 
HETATM 9481 O  O   . HOH CA 6 .   ? 33.947  12.191  -47.696 1.00 32.59  ? 608 HOH C O   1 
HETATM 9482 O  O   . HOH CA 6 .   ? 30.005  6.011   -50.012 1.00 32.30  ? 609 HOH C O   1 
HETATM 9483 O  O   . HOH CA 6 .   ? 28.070  -15.235 -35.787 1.00 35.23  ? 610 HOH C O   1 
HETATM 9484 O  O   . HOH CA 6 .   ? 38.244  -7.487  -10.303 1.00 39.73  ? 611 HOH C O   1 
HETATM 9485 O  O   . HOH CA 6 .   ? 26.921  -13.840 -31.967 1.00 40.78  ? 612 HOH C O   1 
HETATM 9486 O  O   . HOH DA 6 .   ? -14.643 4.722   -37.454 1.00 25.37  ? 401 HOH D O   1 
HETATM 9487 O  O   . HOH DA 6 .   ? 22.308  0.344   -28.023 1.00 28.52  ? 402 HOH D O   1 
HETATM 9488 O  O   . HOH DA 6 .   ? 5.746   17.475  -33.832 1.00 31.82  ? 403 HOH D O   1 
HETATM 9489 O  O   . HOH DA 6 .   ? 2.401   14.171  -43.552 1.00 27.58  ? 404 HOH D O   1 
HETATM 9490 O  O   . HOH DA 6 .   ? 12.666  11.387  -46.342 1.00 30.03  ? 405 HOH D O   1 
HETATM 9491 O  O   . HOH DA 6 .   ? 14.213  19.806  -43.009 1.00 34.18  ? 406 HOH D O   1 
HETATM 9492 O  O   . HOH DA 6 .   ? -5.666  -5.612  -53.966 1.00 32.22  ? 407 HOH D O   1 
HETATM 9493 O  O   . HOH DA 6 .   ? -6.998  11.151  -19.731 1.00 21.08  ? 408 HOH D O   1 
HETATM 9494 O  O   . HOH DA 6 .   ? 2.454   19.313  -37.054 1.00 38.06  ? 409 HOH D O   1 
HETATM 9495 O  O   . HOH DA 6 .   ? -2.188  11.434  -58.359 1.00 55.01  ? 410 HOH D O   1 
HETATM 9496 O  O   . HOH DA 6 .   ? -0.313  -10.425 -18.355 1.00 30.25  ? 411 HOH D O   1 
HETATM 9497 O  O   . HOH DA 6 .   ? 18.205  -0.179  -20.652 1.00 26.27  ? 412 HOH D O   1 
HETATM 9498 O  O   . HOH DA 6 .   ? -8.257  13.612  -44.311 1.00 40.73  ? 413 HOH D O   1 
HETATM 9499 O  O   . HOH DA 6 .   ? 11.248  17.739  -54.821 1.00 26.82  ? 414 HOH D O   1 
HETATM 9500 O  O   . HOH DA 6 .   ? 8.735   -14.558 -37.710 1.00 35.92  ? 415 HOH D O   1 
HETATM 9501 O  O   . HOH DA 6 .   ? 12.003  7.046   -39.507 1.00 11.84  ? 416 HOH D O   1 
HETATM 9502 O  O   . HOH DA 6 .   ? -12.711 -7.797  -41.559 1.00 31.72  ? 417 HOH D O   1 
HETATM 9503 O  O   . HOH DA 6 .   ? -15.421 -2.271  -44.017 1.00 31.20  ? 418 HOH D O   1 
HETATM 9504 O  O   . HOH DA 6 .   ? -9.839  8.595   -20.768 1.00 32.04  ? 419 HOH D O   1 
HETATM 9505 O  O   . HOH DA 6 .   ? -12.120 5.817   -53.330 1.00 38.75  ? 420 HOH D O   1 
HETATM 9506 O  O   . HOH DA 6 .   ? 10.829  13.537  -58.652 1.00 24.31  ? 421 HOH D O   1 
HETATM 9507 O  O   . HOH DA 6 .   ? 20.283  -6.419  -44.402 1.00 38.59  ? 422 HOH D O   1 
HETATM 9508 O  O   . HOH DA 6 .   ? -6.165  13.699  -37.297 1.00 24.48  ? 423 HOH D O   1 
HETATM 9509 O  O   . HOH DA 6 .   ? -6.491  5.256   -56.489 1.00 29.35  ? 424 HOH D O   1 
HETATM 9510 O  O   . HOH DA 6 .   ? 6.550   14.725  -38.172 1.00 28.75  ? 425 HOH D O   1 
HETATM 9511 O  O   . HOH DA 6 .   ? 0.466   19.252  -21.934 1.00 34.59  ? 426 HOH D O   1 
HETATM 9512 O  O   . HOH DA 6 .   ? 20.061  -10.119 -29.913 1.00 21.44  ? 427 HOH D O   1 
HETATM 9513 O  O   . HOH DA 6 .   ? 20.769  9.356   -25.871 1.00 39.06  ? 428 HOH D O   1 
HETATM 9514 O  O   . HOH DA 6 .   ? 11.773  -6.921  -52.259 1.00 24.34  ? 429 HOH D O   1 
HETATM 9515 O  O   . HOH DA 6 .   ? 17.241  -6.543  -56.337 1.00 25.96  ? 430 HOH D O   1 
HETATM 9516 O  O   . HOH DA 6 .   ? 2.137   -15.315 -29.848 1.00 31.85  ? 431 HOH D O   1 
HETATM 9517 O  O   . HOH DA 6 .   ? 17.569  2.462   -56.213 1.00 40.53  ? 432 HOH D O   1 
HETATM 9518 O  O   . HOH DA 6 .   ? -6.490  -2.525  -21.223 1.00 30.42  ? 433 HOH D O   1 
HETATM 9519 O  O   . HOH DA 6 .   ? -3.018  -10.471 -39.650 1.00 23.15  ? 434 HOH D O   1 
HETATM 9520 O  O   . HOH DA 6 .   ? 22.615  13.791  -28.749 1.00 25.34  ? 435 HOH D O   1 
HETATM 9521 O  O   . HOH DA 6 .   ? 1.058   9.385   -59.349 1.00 31.64  ? 436 HOH D O   1 
HETATM 9522 O  O   . HOH DA 6 .   ? -13.056 -1.853  -34.556 1.00 23.88  ? 437 HOH D O   1 
HETATM 9523 O  O   . HOH DA 6 .   ? 20.355  -7.500  -29.846 1.00 19.22  ? 438 HOH D O   1 
HETATM 9524 O  O   . HOH DA 6 .   ? 20.400  -6.843  -38.460 1.00 41.72  ? 439 HOH D O   1 
HETATM 9525 O  O   . HOH DA 6 .   ? 17.750  7.439   -27.231 1.00 21.31  ? 440 HOH D O   1 
HETATM 9526 O  O   . HOH DA 6 .   ? -2.011  -9.025  -16.918 1.00 24.47  ? 441 HOH D O   1 
HETATM 9527 O  O   . HOH DA 6 .   ? -10.136 15.351  -20.858 1.00 32.25  ? 442 HOH D O   1 
HETATM 9528 O  O   . HOH DA 6 .   ? 12.336  20.073  -29.438 1.00 30.04  ? 443 HOH D O   1 
HETATM 9529 O  O   . HOH DA 6 .   ? -11.004 11.778  -26.406 1.00 30.84  ? 444 HOH D O   1 
HETATM 9530 O  O   . HOH DA 6 .   ? 19.834  8.160   -42.466 1.00 13.96  ? 445 HOH D O   1 
HETATM 9531 O  O   . HOH DA 6 .   ? 18.336  5.250   -45.935 1.00 18.58  ? 446 HOH D O   1 
HETATM 9532 O  O   . HOH DA 6 .   ? -5.739  -9.592  -34.875 1.00 33.66  ? 447 HOH D O   1 
HETATM 9533 O  O   . HOH DA 6 .   ? -7.197  -6.875  -51.724 1.00 27.20  ? 448 HOH D O   1 
HETATM 9534 O  O   . HOH DA 6 .   ? -5.622  19.597  -21.786 1.00 40.67  ? 449 HOH D O   1 
HETATM 9535 O  O   . HOH DA 6 .   ? 23.744  9.070   -35.072 1.00 16.34  ? 450 HOH D O   1 
HETATM 9536 O  O   . HOH DA 6 .   ? 19.045  8.471   -29.351 1.00 14.98  ? 451 HOH D O   1 
HETATM 9537 O  O   . HOH DA 6 .   ? -12.354 -4.896  -44.785 1.00 28.39  ? 452 HOH D O   1 
HETATM 9538 O  O   . HOH DA 6 .   ? 21.081  18.531  -42.753 1.00 28.86  ? 453 HOH D O   1 
HETATM 9539 O  O   . HOH DA 6 .   ? 8.622   -10.633 -31.394 1.00 20.14  ? 454 HOH D O   1 
HETATM 9540 O  O   . HOH DA 6 .   ? -8.494  -0.085  -51.965 1.00 21.12  ? 455 HOH D O   1 
HETATM 9541 O  O   . HOH DA 6 .   ? 5.552   -0.185  -57.915 1.00 26.48  ? 456 HOH D O   1 
HETATM 9542 O  O   . HOH DA 6 .   ? -6.312  -9.003  -37.384 1.00 39.67  ? 457 HOH D O   1 
HETATM 9543 O  O   . HOH DA 6 .   ? 4.546   16.039  -57.181 1.00 22.11  ? 458 HOH D O   1 
HETATM 9544 O  O   . HOH DA 6 .   ? 8.904   3.349   -53.154 1.00 15.82  ? 459 HOH D O   1 
HETATM 9545 O  O   . HOH DA 6 .   ? 0.352   -12.655 -37.097 1.00 19.55  ? 460 HOH D O   1 
HETATM 9546 O  O   . HOH DA 6 .   ? 20.846  2.462   -21.326 1.00 33.86  ? 461 HOH D O   1 
HETATM 9547 O  O   . HOH DA 6 .   ? 0.759   2.519   -28.306 1.00 13.99  ? 462 HOH D O   1 
HETATM 9548 O  O   . HOH DA 6 .   ? 14.083  -8.367  -52.596 1.00 26.21  ? 463 HOH D O   1 
HETATM 9549 O  O   . HOH DA 6 .   ? -8.710  -6.508  -28.837 1.00 42.73  ? 464 HOH D O   1 
HETATM 9550 O  O   . HOH DA 6 .   ? -2.389  -14.186 -26.504 1.00 42.25  ? 465 HOH D O   1 
HETATM 9551 O  O   . HOH DA 6 .   ? 11.862  -3.637  -47.377 1.00 14.14  ? 466 HOH D O   1 
HETATM 9552 O  O   . HOH DA 6 .   ? -5.786  -7.095  -27.957 1.00 23.99  ? 467 HOH D O   1 
HETATM 9553 O  O   . HOH DA 6 .   ? 20.605  14.033  -47.925 1.00 22.35  ? 468 HOH D O   1 
HETATM 9554 O  O   . HOH DA 6 .   ? 13.086  22.491  -35.070 1.00 31.95  ? 469 HOH D O   1 
HETATM 9555 O  O   . HOH DA 6 .   ? -12.322 -4.610  -32.219 1.00 47.86  ? 470 HOH D O   1 
HETATM 9556 O  O   . HOH DA 6 .   ? -2.060  13.335  -39.209 1.00 27.38  ? 471 HOH D O   1 
HETATM 9557 O  O   . HOH DA 6 .   ? 19.993  7.441   -35.782 1.00 13.49  ? 472 HOH D O   1 
HETATM 9558 O  O   . HOH DA 6 .   ? -2.494  13.361  -41.952 1.00 31.42  ? 473 HOH D O   1 
HETATM 9559 O  O   . HOH DA 6 .   ? 19.237  -3.911  -34.329 1.00 24.42  ? 474 HOH D O   1 
HETATM 9560 O  O   . HOH DA 6 .   ? 4.706   -0.802  -14.746 1.00 39.39  ? 475 HOH D O   1 
HETATM 9561 O  O   . HOH DA 6 .   ? 5.773   -6.465  -57.652 1.00 18.33  ? 476 HOH D O   1 
HETATM 9562 O  O   . HOH DA 6 .   ? 16.306  0.288   -37.546 1.00 11.50  ? 477 HOH D O   1 
HETATM 9563 O  O   . HOH DA 6 .   ? 9.143   8.363   -42.983 1.00 14.76  ? 478 HOH D O   1 
HETATM 9564 O  O   . HOH DA 6 .   ? -12.497 -3.862  -36.539 1.00 26.71  ? 479 HOH D O   1 
HETATM 9565 O  O   . HOH DA 6 .   ? 9.895   2.428   -21.533 1.00 24.91  ? 480 HOH D O   1 
HETATM 9566 O  O   . HOH DA 6 .   ? -15.817 4.519   -32.574 1.00 44.69  ? 481 HOH D O   1 
HETATM 9567 O  O   . HOH DA 6 .   ? 19.318  19.011  -40.087 1.00 26.25  ? 482 HOH D O   1 
HETATM 9568 O  O   . HOH DA 6 .   ? 6.667   -13.840 -51.035 1.00 14.59  ? 483 HOH D O   1 
HETATM 9569 O  O   . HOH DA 6 .   ? 10.842  13.842  -61.347 1.00 37.18  ? 484 HOH D O   1 
HETATM 9570 O  O   . HOH DA 6 .   ? 18.589  -0.737  -46.382 1.00 27.91  ? 485 HOH D O   1 
HETATM 9571 O  O   . HOH DA 6 .   ? -3.314  -14.562 -49.700 1.00 28.57  ? 486 HOH D O   1 
HETATM 9572 O  O   . HOH DA 6 .   ? -8.273  11.869  -37.141 1.00 22.23  ? 487 HOH D O   1 
HETATM 9573 O  O   . HOH DA 6 .   ? -12.663 -4.428  -47.669 1.00 32.03  ? 488 HOH D O   1 
HETATM 9574 O  O   . HOH DA 6 .   ? -3.029  11.205  -46.243 1.00 21.74  ? 489 HOH D O   1 
HETATM 9575 O  O   . HOH DA 6 .   ? -5.496  -10.136 -45.399 1.00 33.70  ? 490 HOH D O   1 
HETATM 9576 O  O   . HOH DA 6 .   ? 21.216  5.208   -34.313 1.00 11.17  ? 491 HOH D O   1 
HETATM 9577 O  O   . HOH DA 6 .   ? 16.961  7.699   -56.070 1.00 42.95  ? 492 HOH D O   1 
HETATM 9578 O  O   . HOH DA 6 .   ? -14.590 10.377  -37.165 1.00 34.10  ? 493 HOH D O   1 
HETATM 9579 O  O   . HOH DA 6 .   ? 16.270  19.808  -57.473 1.00 38.41  ? 494 HOH D O   1 
HETATM 9580 O  O   . HOH DA 6 .   ? -10.896 19.510  -31.097 1.00 26.69  ? 495 HOH D O   1 
HETATM 9581 O  O   . HOH DA 6 .   ? 18.278  -0.163  -29.476 1.00 15.29  ? 496 HOH D O   1 
HETATM 9582 O  O   . HOH DA 6 .   ? 15.755  15.197  -24.181 1.00 33.36  ? 497 HOH D O   1 
HETATM 9583 O  O   . HOH DA 6 .   ? -3.581  -5.616  -26.934 1.00 21.49  ? 498 HOH D O   1 
HETATM 9584 O  O   . HOH DA 6 .   ? -1.531  2.652   -19.822 1.00 56.49  ? 499 HOH D O   1 
HETATM 9585 O  O   . HOH DA 6 .   ? -2.530  -8.702  -41.898 1.00 17.42  ? 500 HOH D O   1 
HETATM 9586 O  O   . HOH DA 6 .   ? -10.175 -0.408  -49.723 1.00 21.19  ? 501 HOH D O   1 
HETATM 9587 O  O   . HOH DA 6 .   ? 4.217   -6.927  -34.988 1.00 12.51  ? 502 HOH D O   1 
HETATM 9588 O  O   . HOH DA 6 .   ? 22.777  6.460   -38.311 1.00 12.29  ? 503 HOH D O   1 
HETATM 9589 O  O   . HOH DA 6 .   ? 18.801  16.693  -41.861 1.00 27.27  ? 504 HOH D O   1 
HETATM 9590 O  O   . HOH DA 6 .   ? 8.553   21.668  -29.752 1.00 25.20  ? 505 HOH D O   1 
HETATM 9591 O  O   . HOH DA 6 .   ? 0.520   -11.947 -14.028 1.00 38.88  ? 506 HOH D O   1 
HETATM 9592 O  O   . HOH DA 6 .   ? -12.752 8.493   -55.520 1.00 35.45  ? 507 HOH D O   1 
HETATM 9593 O  O   . HOH DA 6 .   ? 19.532  11.226  -29.223 1.00 18.09  ? 508 HOH D O   1 
HETATM 9594 O  O   . HOH DA 6 .   ? 8.462   -9.106  -14.197 1.00 33.55  ? 509 HOH D O   1 
HETATM 9595 O  O   . HOH DA 6 .   ? -13.888 -1.298  -49.463 1.00 26.87  ? 510 HOH D O   1 
HETATM 9596 O  O   . HOH DA 6 .   ? 8.183   -16.409 -45.274 1.00 29.38  ? 511 HOH D O   1 
HETATM 9597 O  O   . HOH DA 6 .   ? 13.210  18.593  -32.597 1.00 13.63  ? 512 HOH D O   1 
HETATM 9598 O  O   . HOH DA 6 .   ? -5.958  -10.028 -41.988 1.00 38.25  ? 513 HOH D O   1 
HETATM 9599 O  O   . HOH DA 6 .   ? -2.353  -7.875  -22.692 1.00 21.92  ? 514 HOH D O   1 
HETATM 9600 O  O   . HOH DA 6 .   ? 5.168   12.139  -23.143 1.00 30.02  ? 515 HOH D O   1 
HETATM 9601 O  O   . HOH DA 6 .   ? 19.797  21.837  -32.946 1.00 30.62  ? 516 HOH D O   1 
HETATM 9602 O  O   . HOH DA 6 .   ? -7.247  -3.081  -53.575 1.00 40.20  ? 517 HOH D O   1 
HETATM 9603 O  O   . HOH DA 6 .   ? 25.647  13.102  -35.496 1.00 13.68  ? 518 HOH D O   1 
HETATM 9604 O  O   . HOH DA 6 .   ? 0.528   -8.209  -19.071 1.00 22.49  ? 519 HOH D O   1 
HETATM 9605 O  O   . HOH DA 6 .   ? 13.753  7.554   -48.259 1.00 23.29  ? 520 HOH D O   1 
HETATM 9606 O  O   . HOH DA 6 .   ? 3.213   -13.846 -39.509 1.00 32.05  ? 521 HOH D O   1 
HETATM 9607 O  O   . HOH DA 6 .   ? -17.932 8.361   -50.438 1.00 48.37  ? 522 HOH D O   1 
HETATM 9608 O  O   . HOH DA 6 .   ? -6.888  0.407   -56.247 1.00 30.95  ? 523 HOH D O   1 
HETATM 9609 O  O   . HOH DA 6 .   ? 9.513   -13.463 -55.612 1.00 35.23  ? 524 HOH D O   1 
HETATM 9610 O  O   . HOH DA 6 .   ? 7.418   -5.092  -14.572 1.00 30.66  ? 525 HOH D O   1 
HETATM 9611 O  O   . HOH DA 6 .   ? -9.330  -5.623  -23.012 1.00 45.87  ? 526 HOH D O   1 
HETATM 9612 O  O   . HOH DA 6 .   ? 2.271   9.414   -25.022 1.00 21.38  ? 527 HOH D O   1 
HETATM 9613 O  O   . HOH DA 6 .   ? 26.241  16.181  -43.681 1.00 26.46  ? 528 HOH D O   1 
HETATM 9614 O  O   . HOH DA 6 .   ? 14.420  -11.993 -34.394 1.00 31.11  ? 529 HOH D O   1 
HETATM 9615 O  O   . HOH DA 6 .   ? 14.072  5.815   -60.433 1.00 33.90  ? 530 HOH D O   1 
HETATM 9616 O  O   . HOH DA 6 .   ? -6.330  23.448  -32.062 1.00 21.72  ? 531 HOH D O   1 
HETATM 9617 O  O   . HOH DA 6 .   ? 11.240  4.530   -22.085 1.00 38.13  ? 532 HOH D O   1 
HETATM 9618 O  O   . HOH DA 6 .   ? 23.643  18.546  -42.819 1.00 23.18  ? 533 HOH D O   1 
HETATM 9619 O  O   . HOH DA 6 .   ? -14.253 9.539   -44.879 1.00 31.39  ? 534 HOH D O   1 
HETATM 9620 O  O   . HOH DA 6 .   ? -5.453  -13.680 -32.487 1.00 35.51  ? 535 HOH D O   1 
HETATM 9621 O  O   . HOH DA 6 .   ? 5.840   18.881  -59.148 1.00 35.36  ? 536 HOH D O   1 
HETATM 9622 O  O   . HOH DA 6 .   ? 14.121  13.963  -27.346 1.00 17.80  ? 537 HOH D O   1 
HETATM 9623 O  O   . HOH DA 6 .   ? -10.692 -4.878  -30.131 1.00 37.98  ? 538 HOH D O   1 
HETATM 9624 O  O   . HOH DA 6 .   ? 4.332   9.697   -42.651 1.00 23.67  ? 539 HOH D O   1 
HETATM 9625 O  O   . HOH DA 6 .   ? -15.885 9.645   -47.772 1.00 34.28  ? 540 HOH D O   1 
HETATM 9626 O  O   . HOH DA 6 .   ? 11.075  3.774   -55.384 1.00 20.07  ? 541 HOH D O   1 
HETATM 9627 O  O   . HOH DA 6 .   ? 8.823   -10.127 -58.210 1.00 25.59  ? 542 HOH D O   1 
HETATM 9628 O  O   . HOH DA 6 .   ? 12.606  -9.708  -46.206 1.00 20.73  ? 543 HOH D O   1 
HETATM 9629 O  O   . HOH DA 6 .   ? 8.734   16.742  -41.927 1.00 30.91  ? 544 HOH D O   1 
HETATM 9630 O  O   . HOH DA 6 .   ? 15.601  9.719   -48.041 1.00 24.17  ? 545 HOH D O   1 
HETATM 9631 O  O   . HOH DA 6 .   ? 16.990  6.760   -48.955 1.00 29.64  ? 546 HOH D O   1 
HETATM 9632 O  O   . HOH DA 6 .   ? 18.669  -13.189 -33.124 1.00 32.70  ? 547 HOH D O   1 
HETATM 9633 O  O   . HOH DA 6 .   ? -20.821 9.217   -40.319 1.00 47.58  ? 548 HOH D O   1 
HETATM 9634 O  O   . HOH DA 6 .   ? -6.832  -7.716  -33.320 1.00 48.01  ? 549 HOH D O   1 
HETATM 9635 O  O   . HOH DA 6 .   ? 18.928  -0.195  -36.887 1.00 17.45  ? 550 HOH D O   1 
HETATM 9636 O  O   . HOH DA 6 .   ? -0.151  -12.140 -42.473 1.00 19.72  ? 551 HOH D O   1 
HETATM 9637 O  O   . HOH DA 6 .   ? 13.884  -11.223 -20.788 1.00 34.47  ? 552 HOH D O   1 
HETATM 9638 O  O   . HOH DA 6 .   ? 8.673   -13.636 -29.698 1.00 42.90  ? 553 HOH D O   1 
HETATM 9639 O  O   . HOH DA 6 .   ? 13.466  1.204   -55.814 1.00 27.10  ? 554 HOH D O   1 
HETATM 9640 O  O   . HOH DA 6 .   ? 23.492  8.289   -45.369 1.00 32.19  ? 555 HOH D O   1 
HETATM 9641 O  O   . HOH DA 6 .   ? 7.522   9.195   -24.482 1.00 23.33  ? 556 HOH D O   1 
HETATM 9642 O  O   . HOH DA 6 .   ? 23.340  10.389  -41.506 1.00 20.28  ? 557 HOH D O   1 
HETATM 9643 O  O   . HOH DA 6 .   ? -3.003  -0.783  -16.921 1.00 33.15  ? 558 HOH D O   1 
HETATM 9644 O  O   . HOH DA 6 .   ? 0.674   24.242  -29.965 1.00 40.21  ? 559 HOH D O   1 
HETATM 9645 O  O   . HOH DA 6 .   ? -15.684 -0.359  -36.563 1.00 72.35  ? 560 HOH D O   1 
HETATM 9646 O  O   . HOH DA 6 .   ? 18.686  -3.267  -43.055 1.00 25.59  ? 561 HOH D O   1 
HETATM 9647 O  O   . HOH DA 6 .   ? 18.900  10.127  -35.823 1.00 12.73  ? 562 HOH D O   1 
HETATM 9648 O  O   . HOH DA 6 .   ? 18.996  11.559  -50.299 1.00 35.13  ? 563 HOH D O   1 
HETATM 9649 O  O   . HOH DA 6 .   ? 21.159  6.836   -29.709 1.00 14.48  ? 564 HOH D O   1 
HETATM 9650 O  O   . HOH DA 6 .   ? -16.819 4.092   -52.024 1.00 37.00  ? 565 HOH D O   1 
HETATM 9651 O  O   . HOH DA 6 .   ? 17.857  -10.642 -48.169 1.00 43.26  ? 566 HOH D O   1 
HETATM 9652 O  O   . HOH DA 6 .   ? 22.221  -4.944  -26.534 1.00 35.86  ? 567 HOH D O   1 
HETATM 9653 O  O   . HOH DA 6 .   ? -0.036  0.192   -57.110 1.00 46.17  ? 568 HOH D O   1 
HETATM 9654 O  O   . HOH DA 6 .   ? 1.112   -9.908  -31.409 1.00 14.68  ? 569 HOH D O   1 
HETATM 9655 O  O   . HOH DA 6 .   ? 18.462  -7.599  -40.154 1.00 23.41  ? 570 HOH D O   1 
HETATM 9656 O  O   . HOH DA 6 .   ? -16.259 4.326   -41.409 1.00 25.86  ? 571 HOH D O   1 
HETATM 9657 O  O   . HOH DA 6 .   ? 13.498  16.481  -26.537 1.00 26.44  ? 572 HOH D O   1 
HETATM 9658 O  O   . HOH DA 6 .   ? 18.519  -4.327  -18.267 1.00 33.84  ? 573 HOH D O   1 
HETATM 9659 O  O   . HOH DA 6 .   ? 19.073  4.829   -49.296 1.00 30.29  ? 574 HOH D O   1 
HETATM 9660 O  O   . HOH DA 6 .   ? -9.323  11.223  -45.289 1.00 22.16  ? 575 HOH D O   1 
HETATM 9661 O  O   . HOH DA 6 .   ? -2.281  -4.105  -56.240 1.00 36.70  ? 576 HOH D O   1 
HETATM 9662 O  O   . HOH DA 6 .   ? 4.820   9.355   -23.870 1.00 27.19  ? 577 HOH D O   1 
HETATM 9663 O  O   . HOH DA 6 .   ? -3.169  22.452  -35.176 1.00 21.14  ? 578 HOH D O   1 
HETATM 9664 O  O   . HOH DA 6 .   ? -11.898 12.695  -38.255 1.00 31.13  ? 579 HOH D O   1 
HETATM 9665 O  O   . HOH DA 6 .   ? 0.987   -5.025  -54.593 1.00 28.06  ? 580 HOH D O   1 
HETATM 9666 O  O   . HOH DA 6 .   ? 24.842  10.230  -44.140 1.00 32.00  ? 581 HOH D O   1 
HETATM 9667 O  O   . HOH DA 6 .   ? -9.579  15.972  -29.883 1.00 35.98  ? 582 HOH D O   1 
HETATM 9668 O  O   . HOH DA 6 .   ? 10.260  -10.732 -17.075 1.00 35.46  ? 583 HOH D O   1 
HETATM 9669 O  O   . HOH DA 6 .   ? -2.668  13.946  -56.695 1.00 29.49  ? 584 HOH D O   1 
HETATM 9670 O  O   . HOH DA 6 .   ? -5.122  -11.254 -28.445 1.00 27.31  ? 585 HOH D O   1 
HETATM 9671 O  O   . HOH DA 6 .   ? 13.714  -10.583 -27.928 1.00 33.96  ? 586 HOH D O   1 
HETATM 9672 O  O   . HOH DA 6 .   ? 4.057   19.245  -22.725 1.00 29.39  ? 587 HOH D O   1 
HETATM 9673 O  O   . HOH DA 6 .   ? -0.350  -12.730 -45.539 1.00 17.89  ? 588 HOH D O   1 
HETATM 9674 O  O   . HOH DA 6 .   ? 15.996  24.233  -34.363 1.00 26.20  ? 589 HOH D O   1 
HETATM 9675 O  O   . HOH DA 6 .   ? -5.783  -11.011 -31.120 1.00 31.58  ? 590 HOH D O   1 
HETATM 9676 O  O   . HOH DA 6 .   ? 22.554  1.871   -19.073 1.00 32.17  ? 591 HOH D O   1 
HETATM 9677 O  O   . HOH DA 6 .   ? 20.489  -4.035  -28.670 1.00 29.33  ? 592 HOH D O   1 
HETATM 9678 O  O   . HOH DA 6 .   ? 13.331  -11.120 -39.018 1.00 43.85  ? 593 HOH D O   1 
HETATM 9679 O  O   . HOH DA 6 .   ? -21.398 0.729   -46.677 1.00 37.83  ? 594 HOH D O   1 
HETATM 9680 O  O   . HOH DA 6 .   ? 0.561   13.235  -40.270 1.00 24.48  ? 595 HOH D O   1 
HETATM 9681 O  O   . HOH DA 6 .   ? 14.594  22.741  -43.609 1.00 51.03  ? 596 HOH D O   1 
HETATM 9682 O  O   . HOH DA 6 .   ? -18.305 -1.665  -45.395 1.00 39.41  ? 597 HOH D O   1 
HETATM 9683 O  O   . HOH DA 6 .   ? 11.704  8.992   -47.290 1.00 23.20  ? 598 HOH D O   1 
HETATM 9684 O  O   . HOH DA 6 .   ? -11.825 -7.381  -36.992 1.00 36.02  ? 599 HOH D O   1 
HETATM 9685 O  O   . HOH DA 6 .   ? 11.800  20.867  -32.823 1.00 27.34  ? 600 HOH D O   1 
HETATM 9686 O  O   . HOH DA 6 .   ? -16.227 3.119   -38.818 1.00 36.48  ? 601 HOH D O   1 
HETATM 9687 O  O   . HOH DA 6 .   ? -3.946  9.981   -17.586 1.00 21.76  ? 602 HOH D O   1 
HETATM 9688 O  O   . HOH DA 6 .   ? -9.124  16.722  -34.407 1.00 48.05  ? 603 HOH D O   1 
HETATM 9689 O  O   . HOH DA 6 .   ? 22.459  -1.510  -39.956 1.00 23.06  ? 604 HOH D O   1 
HETATM 9690 O  O   . HOH DA 6 .   ? -11.903 12.190  -30.813 1.00 40.94  ? 605 HOH D O   1 
HETATM 9691 O  O   . HOH DA 6 .   ? 11.237  -10.583 -43.580 1.00 29.63  ? 606 HOH D O   1 
HETATM 9692 O  O   . HOH DA 6 .   ? -13.883 11.201  -27.575 1.00 45.23  ? 607 HOH D O   1 
HETATM 9693 O  O   . HOH DA 6 .   ? 13.194  -12.942 -30.059 1.00 43.22  ? 608 HOH D O   1 
HETATM 9694 O  O   . HOH DA 6 .   ? -8.766  19.421  -26.203 1.00 37.74  ? 609 HOH D O   1 
HETATM 9695 O  O   . HOH DA 6 .   ? 13.031  -3.357  -12.828 1.00 38.83  ? 610 HOH D O   1 
HETATM 9696 O  O   . HOH DA 6 .   ? 20.616  -0.883  -41.890 1.00 31.62  ? 611 HOH D O   1 
HETATM 9697 O  O   . HOH DA 6 .   ? -15.311 7.083   -40.942 1.00 35.18  ? 612 HOH D O   1 
HETATM 9698 O  O   . HOH DA 6 .   ? 6.740   8.505   -41.614 1.00 17.60  ? 613 HOH D O   1 
HETATM 9699 O  O   . HOH DA 6 .   ? 0.822   15.347  -46.250 1.00 48.30  ? 614 HOH D O   1 
HETATM 9700 O  O   . HOH DA 6 .   ? 11.487  -10.149 -57.997 1.00 23.07  ? 615 HOH D O   1 
HETATM 9701 O  O   . HOH DA 6 .   ? -0.796  23.212  -34.310 1.00 48.89  ? 616 HOH D O   1 
HETATM 9702 O  O   . HOH DA 6 .   ? -3.159  -12.294 -45.454 1.00 29.12  ? 617 HOH D O   1 
HETATM 9703 O  O   . HOH DA 6 .   ? -1.304  10.145  -60.474 1.00 48.79  ? 618 HOH D O   1 
HETATM 9704 O  O   . HOH DA 6 .   ? 6.885   -4.086  -58.617 1.00 29.28  ? 619 HOH D O   1 
HETATM 9705 O  O   . HOH DA 6 .   ? 27.406  13.062  -47.304 1.00 37.44  ? 620 HOH D O   1 
HETATM 9706 O  O   . HOH DA 6 .   ? -14.708 -5.375  -36.843 1.00 55.06  ? 621 HOH D O   1 
HETATM 9707 O  O   . HOH DA 6 .   ? 20.055  -2.575  -36.374 1.00 32.80  ? 622 HOH D O   1 
HETATM 9708 O  O   . HOH DA 6 .   ? 1.803   -7.392  -55.875 1.00 27.69  ? 623 HOH D O   1 
HETATM 9709 O  O   . HOH DA 6 .   ? 22.009  -7.309  -27.619 1.00 26.25  ? 624 HOH D O   1 
HETATM 9710 O  O   . HOH DA 6 .   ? 10.464  -10.840 -20.322 1.00 46.96  ? 625 HOH D O   1 
HETATM 9711 O  O   . HOH DA 6 .   ? -4.497  24.695  -29.952 1.00 47.37  ? 626 HOH D O   1 
HETATM 9712 O  O   . HOH DA 6 .   ? -17.299 2.278   -37.123 1.00 37.29  ? 627 HOH D O   1 
HETATM 9713 O  O   . HOH DA 6 .   ? 22.472  7.771   -42.607 1.00 18.14  ? 628 HOH D O   1 
HETATM 9714 O  O   . HOH DA 6 .   ? 12.319  -6.221  -10.827 1.00 45.18  ? 629 HOH D O   1 
HETATM 9715 O  O   . HOH DA 6 .   ? 3.134   -6.758  -58.202 1.00 24.62  ? 630 HOH D O   1 
HETATM 9716 O  O   . HOH DA 6 .   ? 0.765   -3.356  -56.524 1.00 37.29  ? 631 HOH D O   1 
HETATM 9717 O  O   . HOH DA 6 .   ? 14.087  -11.551 -47.374 1.00 42.31  ? 632 HOH D O   1 
HETATM 9718 O  O   . HOH DA 6 .   ? 5.262   17.942  -36.564 1.00 39.58  ? 633 HOH D O   1 
HETATM 9719 O  O   . HOH DA 6 .   ? -6.967  -9.346  -26.919 1.00 32.36  ? 634 HOH D O   1 
HETATM 9720 O  O   . HOH DA 6 .   ? 0.806   -14.600 -41.656 1.00 42.15  ? 635 HOH D O   1 
HETATM 9721 O  O   . HOH DA 6 .   ? -1.193  -12.538 -39.296 1.00 29.48  ? 636 HOH D O   1 
HETATM 9722 O  O   . HOH DA 6 .   ? -11.643 -2.490  -49.929 1.00 27.70  ? 637 HOH D O   1 
HETATM 9723 O  O   . HOH DA 6 .   ? 4.925   -2.474  -59.170 1.00 30.87  ? 638 HOH D O   1 
HETATM 9724 O  O   . HOH DA 6 .   ? -3.257  -9.979  -21.325 1.00 26.31  ? 639 HOH D O   1 
HETATM 9725 O  O   . HOH DA 6 .   ? -4.050  -8.962  -18.778 1.00 27.34  ? 640 HOH D O   1 
HETATM 9726 O  O   . HOH DA 6 .   ? -14.856 9.502   -42.383 1.00 34.14  ? 641 HOH D O   1 
HETATM 9727 O  O   . HOH DA 6 .   ? 9.997   -12.008 -33.447 1.00 32.90  ? 642 HOH D O   1 
HETATM 9728 O  O   . HOH DA 6 .   ? 19.643  -5.669  -42.027 1.00 24.33  ? 643 HOH D O   1 
HETATM 9729 O  O   . HOH DA 6 .   ? 0.986   -10.122 -56.190 1.00 25.50  ? 644 HOH D O   1 
HETATM 9730 O  O   . HOH DA 6 .   ? -6.594  -9.138  -53.099 1.00 31.16  ? 645 HOH D O   1 
HETATM 9731 O  O   . HOH DA 6 .   ? -8.136  -6.743  -18.328 1.00 36.47  ? 646 HOH D O   1 
HETATM 9732 O  O   . HOH DA 6 .   ? 5.241   -15.502 -36.690 1.00 45.45  ? 647 HOH D O   1 
HETATM 9733 O  O   . HOH DA 6 .   ? 14.670  26.377  -35.384 1.00 34.23  ? 648 HOH D O   1 
HETATM 9734 O  O   . HOH DA 6 .   ? 27.531  13.128  -49.845 1.00 39.26  ? 649 HOH D O   1 
HETATM 9735 O  O   . HOH DA 6 .   ? 11.019  -13.907 -52.551 1.00 24.94  ? 650 HOH D O   1 
HETATM 9736 O  O   . HOH DA 6 .   ? 12.441  -13.558 -32.177 1.00 38.26  ? 651 HOH D O   1 
HETATM 9737 O  O   . HOH DA 6 .   ? -13.012 3.936   -55.221 1.00 34.86  ? 652 HOH D O   1 
HETATM 9738 O  O   . HOH DA 6 .   ? 12.698  22.809  -30.869 1.00 27.68  ? 653 HOH D O   1 
HETATM 9739 O  O   . HOH DA 6 .   ? 6.918   -8.534  -59.123 1.00 24.78  ? 654 HOH D O   1 
HETATM 9740 O  O   . HOH DA 6 .   ? 13.592  -12.495 -36.870 1.00 47.42  ? 655 HOH D O   1 
HETATM 9741 O  O   . HOH DA 6 .   ? -6.744  -8.852  -18.393 1.00 29.17  ? 656 HOH D O   1 
HETATM 9742 O  O   . HOH DA 6 .   ? 15.026  24.769  -31.818 1.00 29.90  ? 657 HOH D O   1 
HETATM 9743 O  O   . HOH DA 6 .   ? -7.897  -10.364 -20.653 1.00 42.85  ? 658 HOH D O   1 
HETATM 9744 O  O   . HOH DA 6 .   ? -2.752  -14.659 -39.760 1.00 41.14  ? 659 HOH D O   1 
HETATM 9745 O  O   . HOH DA 6 .   ? -7.144  -11.081 -24.569 1.00 51.22  ? 660 HOH D O   1 
HETATM 9746 O  O   . HOH DA 6 .   ? -11.495 -3.899  -52.376 1.00 35.79  ? 661 HOH D O   1 
HETATM 9747 O  O   . HOH DA 6 .   ? 2.968   -9.202  -59.802 1.00 42.62  ? 662 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   ? 0.7032 0.5765 0.4654 -0.2409 0.0780  -0.2245 3   LYS A N   
2    C  CA  . LYS A  3   ? 0.6066 0.4935 0.4455 -0.2339 -0.0134 -0.1430 3   LYS A CA  
3    C  C   . LYS A  3   ? 0.4121 0.3279 0.7864 -0.0057 -0.1016 -0.2870 3   LYS A C   
4    O  O   . LYS A  3   ? 0.5801 0.4814 0.7532 -0.0715 0.1040  -0.2086 3   LYS A O   
5    C  CB  . LYS A  3   ? 0.6624 0.7794 0.5886 -0.4295 0.0498  -0.2367 3   LYS A CB  
6    C  CG  . LYS A  3   ? 0.5674 0.4371 0.8007 -0.2049 0.2955  0.1270  3   LYS A CG  
7    N  N   . TRP A  4   ? 0.2785 0.1957 0.2448 -0.0126 -0.0543 -0.0143 4   TRP A N   
8    C  CA  . TRP A  4   ? 0.2219 0.1475 0.2343 -0.0113 -0.0373 -0.0063 4   TRP A CA  
9    C  C   . TRP A  4   ? 0.2177 0.1746 0.2197 0.0222  -0.0422 0.0049  4   TRP A C   
10   O  O   . TRP A  4   ? 0.2311 0.2110 0.2265 0.0003  -0.0502 0.0019  4   TRP A O   
11   C  CB  . TRP A  4   ? 0.1787 0.1640 0.2263 0.0008  -0.0381 -0.0018 4   TRP A CB  
12   C  CG  . TRP A  4   ? 0.1845 0.1362 0.1918 -0.0200 -0.0291 -0.0058 4   TRP A CG  
13   C  CD1 . TRP A  4   ? 0.1967 0.1651 0.2352 -0.0301 0.0021  0.0017  4   TRP A CD1 
14   C  CD2 . TRP A  4   ? 0.1527 0.1445 0.1846 -0.0050 -0.0381 -0.0033 4   TRP A CD2 
15   N  NE1 . TRP A  4   ? 0.1807 0.1708 0.2460 -0.0345 -0.0241 -0.0282 4   TRP A NE1 
16   C  CE2 . TRP A  4   ? 0.1575 0.1536 0.1916 -0.0151 -0.0455 -0.0211 4   TRP A CE2 
17   C  CE3 . TRP A  4   ? 0.1590 0.1465 0.1742 -0.0181 -0.0394 -0.0011 4   TRP A CE3 
18   C  CZ2 . TRP A  4   ? 0.2175 0.1595 0.1829 0.0085  -0.0316 0.0042  4   TRP A CZ2 
19   C  CZ3 . TRP A  4   ? 0.1990 0.1715 0.1518 0.0251  -0.0298 0.0085  4   TRP A CZ3 
20   C  CH2 . TRP A  4   ? 0.1931 0.1680 0.1538 0.0277  -0.0223 0.0020  4   TRP A CH2 
21   N  N   . THR A  5   ? 0.2148 0.1603 0.2141 0.0126  -0.0417 0.0136  5   THR A N   
22   C  CA  . THR A  5   ? 0.2352 0.1841 0.1844 0.0183  -0.0186 -0.0058 5   THR A CA  
23   C  C   . THR A  5   ? 0.1540 0.1827 0.1570 0.0201  -0.0010 0.0019  5   THR A C   
24   O  O   . THR A  5   ? 0.1807 0.1569 0.1718 0.0109  -0.0241 0.0189  5   THR A O   
25   C  CB  . THR A  5   ? 0.2674 0.1876 0.2078 -0.0023 -0.0085 -0.0542 5   THR A CB  
26   O  OG1 . THR A  5   ? 0.2468 0.2352 0.2648 -0.0063 0.0291  -0.0288 5   THR A OG1 
27   C  CG2 . THR A  5   ? 0.3301 0.2244 0.2586 -0.0261 -0.0288 -0.0719 5   THR A CG2 
28   N  N   . TYR A  6   ? 0.2333 0.1718 0.1731 0.0346  0.0049  -0.0055 6   TYR A N   
29   C  CA  . TYR A  6   ? 0.2288 0.1324 0.2028 0.0137  0.0322  0.0011  6   TYR A CA  
30   C  C   . TYR A  6   ? 0.2160 0.1487 0.2072 0.0366  0.0027  -0.0054 6   TYR A C   
31   O  O   . TYR A  6   ? 0.2509 0.1861 0.1934 0.0186  -0.0364 0.0163  6   TYR A O   
32   C  CB  . TYR A  6   ? 0.2811 0.1659 0.2192 0.0565  0.0939  0.0251  6   TYR A CB  
33   C  CG  . TYR A  6   ? 0.1996 0.1085 0.2075 0.0027  0.0345  0.0205  6   TYR A CG  
34   C  CD1 . TYR A  6   ? 0.2009 0.1145 0.1790 -0.0044 0.0314  0.0156  6   TYR A CD1 
35   C  CD2 . TYR A  6   ? 0.2389 0.1430 0.2112 -0.0424 0.0237  0.0125  6   TYR A CD2 
36   C  CE1 . TYR A  6   ? 0.1676 0.1071 0.1773 -0.0089 0.0159  0.0275  6   TYR A CE1 
37   C  CE2 . TYR A  6   ? 0.2219 0.1827 0.1762 -0.0331 0.0140  0.0268  6   TYR A CE2 
38   C  CZ  . TYR A  6   ? 0.1866 0.1357 0.1680 -0.0451 0.0157  0.0190  6   TYR A CZ  
39   O  OH  . TYR A  6   ? 0.1639 0.1580 0.1578 -0.0317 -0.0048 0.0185  6   TYR A OH  
40   N  N   . PHE A  7   ? 0.3199 0.2115 0.4011 0.0016  0.1729  -0.0921 7   PHE A N   
41   C  CA  . PHE A  7   ? 0.3425 0.2636 0.4518 -0.0516 0.1842  -0.1218 7   PHE A CA  
42   C  C   . PHE A  7   ? 0.3889 0.2365 0.6214 -0.0403 0.2435  -0.0598 7   PHE A C   
43   O  O   . PHE A  7   ? 0.4086 0.2638 0.7052 -0.1119 0.3143  -0.1342 7   PHE A O   
44   C  CB  . PHE A  7   ? 0.8265 0.5630 0.4958 -0.3650 0.1192  -0.2039 7   PHE A CB  
45   C  CG  . PHE A  7   ? 0.7076 0.6384 0.3434 -0.2235 0.0895  -0.2247 7   PHE A CG  
46   C  CD1 . PHE A  7   ? 0.6400 0.6715 0.3036 -0.1046 0.1362  -0.0370 7   PHE A CD1 
47   C  CD2 . PHE A  7   ? 0.9998 1.0261 0.3318 -0.2546 0.3001  -0.3119 7   PHE A CD2 
48   C  CE1 . PHE A  7   ? 0.6649 0.7461 0.1955 -0.1322 0.0276  0.0385  7   PHE A CE1 
49   C  CE2 . PHE A  7   ? 1.1207 1.1883 0.7384 -0.1421 0.0098  -0.4860 7   PHE A CE2 
50   C  CZ  . PHE A  7   ? 0.9816 1.0734 0.5996 0.0391  0.1700  -0.1973 7   PHE A CZ  
51   N  N   . GLY A  8   ? 0.2779 0.4892 0.3415 0.0413  0.0293  -0.0279 8   GLY A N   
52   C  CA  . GLY A  8   ? 0.4309 0.3441 0.2561 -0.0661 -0.0264 -0.0253 8   GLY A CA  
53   C  C   . GLY A  8   ? 0.5813 0.2701 0.3132 -0.1041 -0.0199 -0.0276 8   GLY A C   
54   O  O   . GLY A  8   ? 0.6243 0.3100 0.3322 0.1614  0.0274  -0.0624 8   GLY A O   
55   N  N   . PRO A  9   ? 0.3294 0.2632 0.3671 0.0606  0.0480  -0.0445 9   PRO A N   
56   C  CA  . PRO A  9   ? 0.3485 0.3046 0.4292 0.1088  0.1017  -0.0048 9   PRO A CA  
57   C  C   . PRO A  9   ? 0.2973 0.2293 0.4243 0.0356  0.0533  -0.0271 9   PRO A C   
58   O  O   . PRO A  9   ? 0.2823 0.2364 0.3486 0.0087  -0.0006 -0.0428 9   PRO A O   
59   C  CB  . PRO A  9   ? 0.3599 0.3911 0.4901 0.1134  -0.1181 -0.2273 9   PRO A CB  
60   C  CG  . PRO A  9   ? 0.3538 0.3403 0.3914 0.1327  -0.1392 -0.1723 9   PRO A CG  
61   C  CD  . PRO A  9   ? 0.3849 0.4349 0.4363 0.1062  0.0908  -0.1490 9   PRO A CD  
62   N  N   . ASP A  10  ? 0.3395 0.2627 0.2860 0.0520  0.0601  -0.0324 10  ASP A N   
63   C  CA  . ASP A  10  ? 0.2585 0.1891 0.3050 0.0135  0.0197  -0.0557 10  ASP A CA  
64   C  C   . ASP A  10  ? 0.2259 0.1389 0.2481 -0.0197 -0.0078 -0.0176 10  ASP A C   
65   O  O   . ASP A  10  ? 0.2103 0.1958 0.2359 0.0006  -0.0500 -0.0539 10  ASP A O   
66   C  CB  . ASP A  10  ? 0.3792 0.2164 0.2887 -0.0266 -0.0819 -0.0514 10  ASP A CB  
67   C  CG  . ASP A  10  ? 0.6822 0.2737 0.4441 0.0035  -0.0945 -0.1521 10  ASP A CG  
68   O  OD1 . ASP A  10  ? 0.6925 0.2497 0.5238 0.0260  0.0271  -0.1316 10  ASP A OD1 
69   O  OD2 . ASP A  10  ? 0.8571 0.4112 0.4235 0.0719  -0.1100 -0.1949 10  ASP A OD2 
70   N  N   . GLY A  11  ? 0.2072 0.1647 0.2708 0.0257  -0.0212 -0.0331 11  GLY A N   
71   C  CA  . GLY A  11  ? 0.2210 0.1332 0.1895 0.0319  -0.0334 -0.0227 11  GLY A CA  
72   C  C   . GLY A  11  ? 0.1247 0.1611 0.1817 0.0306  -0.0339 0.0084  11  GLY A C   
73   O  O   . GLY A  11  ? 0.1612 0.1247 0.2121 0.0060  -0.0446 -0.0009 11  GLY A O   
74   N  N   . GLU A  12  ? 0.1509 0.1062 0.2046 -0.0069 -0.0252 0.0009  12  GLU A N   
75   C  CA  . GLU A  12  ? 0.1249 0.1060 0.1869 0.0013  -0.0234 0.0069  12  GLU A CA  
76   C  C   . GLU A  12  ? 0.1231 0.1075 0.1712 -0.0004 -0.0082 -0.0152 12  GLU A C   
77   O  O   . GLU A  12  ? 0.1312 0.1145 0.1745 0.0113  -0.0082 0.0168  12  GLU A O   
78   C  CB  . GLU A  12  ? 0.1238 0.1066 0.1930 -0.0043 -0.0249 0.0166  12  GLU A CB  
79   C  CG  . GLU A  12  ? 0.1332 0.0937 0.1975 0.0013  -0.0197 0.0170  12  GLU A CG  
80   C  CD  . GLU A  12  ? 0.1212 0.1201 0.1609 -0.0067 -0.0172 0.0035  12  GLU A CD  
81   O  OE1 . GLU A  12  ? 0.1229 0.1116 0.1630 0.0030  -0.0046 0.0034  12  GLU A OE1 
82   O  OE2 . GLU A  12  ? 0.1793 0.1320 0.1734 -0.0001 -0.0151 -0.0020 12  GLU A OE2 
83   N  N   . ASN A  13  ? 0.1249 0.1033 0.1886 -0.0087 -0.0216 0.0168  13  ASN A N   
84   C  CA  . ASN A  13  ? 0.1120 0.0933 0.2040 -0.0100 -0.0188 0.0313  13  ASN A CA  
85   C  C   . ASN A  13  ? 0.1245 0.1172 0.1622 -0.0070 -0.0219 0.0228  13  ASN A C   
86   O  O   . ASN A  13  ? 0.1538 0.1078 0.1932 -0.0047 -0.0350 0.0214  13  ASN A O   
87   C  CB  . ASN A  13  ? 0.1100 0.1100 0.2102 -0.0048 -0.0201 0.0150  13  ASN A CB  
88   C  CG  . ASN A  13  ? 0.1237 0.1050 0.1723 0.0038  -0.0098 0.0082  13  ASN A CG  
89   O  OD1 . ASN A  13  ? 0.1216 0.1066 0.2163 -0.0115 -0.0068 0.0130  13  ASN A OD1 
90   N  ND2 . ASN A  13  ? 0.1213 0.1247 0.1763 -0.0093 -0.0030 0.0113  13  ASN A ND2 
91   N  N   . SER A  14  ? 0.1531 0.0876 0.1887 0.0000  -0.0188 0.0068  14  SER A N   
92   C  CA  . SER A  14  ? 0.1478 0.0860 0.2030 -0.0031 -0.0013 -0.0027 14  SER A CA  
93   C  C   . SER A  14  ? 0.1337 0.1003 0.1967 -0.0172 -0.0225 -0.0026 14  SER A C   
94   O  O   . SER A  14  ? 0.1513 0.1082 0.2096 -0.0174 -0.0167 0.0022  14  SER A O   
95   C  CB  . SER A  14  ? 0.1731 0.1209 0.2814 -0.0210 0.0399  -0.0413 14  SER A CB  
96   O  OG  . SER A  14  ? 0.2211 0.2515 0.3499 0.0080  0.0387  -0.0444 14  SER A OG  
97   N  N   . TRP A  15  ? 0.1175 0.0942 0.1861 -0.0021 -0.0193 0.0067  15  TRP A N   
98   C  CA  . TRP A  15  ? 0.1192 0.0947 0.1782 0.0008  -0.0113 0.0277  15  TRP A CA  
99   C  C   . TRP A  15  ? 0.1378 0.1045 0.1762 -0.0171 -0.0234 0.0087  15  TRP A C   
100  O  O   . TRP A  15  ? 0.1202 0.0965 0.2003 -0.0120 -0.0171 0.0058  15  TRP A O   
101  C  CB  . TRP A  15  ? 0.1322 0.1044 0.1676 0.0174  -0.0048 0.0110  15  TRP A CB  
102  C  CG  . TRP A  15  ? 0.1155 0.1116 0.1590 -0.0017 -0.0144 0.0175  15  TRP A CG  
103  C  CD1 . TRP A  15  ? 0.1201 0.1316 0.1707 -0.0148 -0.0320 0.0208  15  TRP A CD1 
104  C  CD2 . TRP A  15  ? 0.1069 0.1039 0.1660 -0.0015 -0.0257 0.0036  15  TRP A CD2 
105  N  NE1 . TRP A  15  ? 0.1298 0.1348 0.1727 -0.0179 -0.0230 0.0205  15  TRP A NE1 
106  C  CE2 . TRP A  15  ? 0.1089 0.1137 0.1764 -0.0137 -0.0256 0.0024  15  TRP A CE2 
107  C  CE3 . TRP A  15  ? 0.1203 0.1150 0.1565 -0.0008 -0.0146 0.0089  15  TRP A CE3 
108  C  CZ2 . TRP A  15  ? 0.1100 0.1253 0.1665 -0.0161 -0.0319 0.0166  15  TRP A CZ2 
109  C  CZ3 . TRP A  15  ? 0.1085 0.1249 0.1734 -0.0021 -0.0289 0.0086  15  TRP A CZ3 
110  C  CH2 . TRP A  15  ? 0.1018 0.1308 0.1731 -0.0212 -0.0183 -0.0001 15  TRP A CH2 
111  N  N   . SER A  16  ? 0.1366 0.1055 0.1573 -0.0078 -0.0205 0.0100  16  SER A N   
112  C  CA  . SER A  16  ? 0.1612 0.0891 0.1800 -0.0252 -0.0205 0.0061  16  SER A CA  
113  C  C   . SER A  16  ? 0.1335 0.1324 0.1802 0.0048  -0.0154 0.0120  16  SER A C   
114  O  O   . SER A  16  ? 0.1487 0.1220 0.1874 -0.0006 -0.0083 0.0218  16  SER A O   
115  C  CB  . SER A  16  ? 0.1456 0.1435 0.1651 -0.0065 -0.0105 -0.0037 16  SER A CB  
116  O  OG  . SER A  16  ? 0.1818 0.1242 0.2300 -0.0200 -0.0389 0.0178  16  SER A OG  
117  N  N   A LYS A  17  ? 0.1463 0.0873 0.2116 -0.0111 -0.0171 0.0227  17  LYS A N   
118  N  N   B LYS A  17  ? 0.1295 0.0855 0.1920 -0.0023 -0.0299 0.0009  17  LYS A N   
119  C  CA  A LYS A  17  ? 0.1539 0.0904 0.1585 -0.0139 -0.0167 0.0239  17  LYS A CA  
120  C  CA  B LYS A  17  ? 0.1441 0.0885 0.1335 -0.0279 -0.0035 -0.0013 17  LYS A CA  
121  C  C   A LYS A  17  ? 0.1481 0.1060 0.1852 -0.0054 -0.0100 0.0187  17  LYS A C   
122  C  C   B LYS A  17  ? 0.1270 0.0851 0.1473 -0.0020 0.0012  -0.0006 17  LYS A C   
123  O  O   A LYS A  17  ? 0.1739 0.0881 0.1830 0.0091  -0.0017 0.0257  17  LYS A O   
124  O  O   B LYS A  17  ? 0.1272 0.0895 0.1430 -0.0128 -0.0034 -0.0016 17  LYS A O   
125  C  CB  A LYS A  17  ? 0.1655 0.0884 0.1877 -0.0095 0.0057  0.0009  17  LYS A CB  
126  C  CB  B LYS A  17  ? 0.1293 0.0960 0.1506 0.0127  0.0037  0.0089  17  LYS A CB  
127  C  CG  A LYS A  17  ? 0.1719 0.1640 0.2977 -0.0430 0.0193  -0.0710 17  LYS A CG  
128  C  CG  B LYS A  17  ? 0.1879 0.1120 0.2062 0.0247  -0.0253 -0.0321 17  LYS A CG  
129  C  CD  A LYS A  17  ? 0.2325 0.1958 0.3114 -0.0930 0.0284  -0.0846 17  LYS A CD  
130  C  CD  B LYS A  17  ? 0.2111 0.0992 0.2489 -0.0414 0.0121  -0.0428 17  LYS A CD  
131  C  CE  A LYS A  17  ? 0.1658 0.2822 0.4014 -0.0617 -0.0434 0.1430  17  LYS A CE  
132  C  CE  B LYS A  17  ? 0.2028 0.1831 0.2379 -0.0745 0.0274  -0.0389 17  LYS A CE  
133  N  NZ  A LYS A  17  ? 0.2128 0.2304 0.4553 -0.0604 0.0397  0.0091  17  LYS A NZ  
134  N  NZ  B LYS A  17  ? 0.2318 0.1741 0.2681 -0.0105 -0.0089 -0.0730 17  LYS A NZ  
135  N  N   . LYS A  18  ? 0.1492 0.1036 0.1803 -0.0122 -0.0249 0.0198  18  LYS A N   
136  C  CA  . LYS A  18  ? 0.1618 0.1346 0.1911 -0.0458 -0.0209 0.0150  18  LYS A CA  
137  C  C   . LYS A  18  ? 0.1415 0.1357 0.2248 -0.0339 -0.0118 0.0124  18  LYS A C   
138  O  O   . LYS A  18  ? 0.1919 0.1455 0.2962 -0.0502 0.0396  -0.0211 18  LYS A O   
139  C  CB  . LYS A  18  ? 0.1710 0.1713 0.2170 -0.0280 -0.0352 0.0118  18  LYS A CB  
140  C  CG  . LYS A  18  ? 0.2549 0.2652 0.3554 -0.0750 -0.1034 -0.0003 18  LYS A CG  
141  C  CD  . LYS A  18  ? 0.3605 0.3880 0.3836 -0.0941 -0.1169 -0.0344 18  LYS A CD  
142  C  CE  . LYS A  18  ? 0.3183 0.6615 0.5236 -0.0982 -0.2240 0.0330  18  LYS A CE  
143  N  NZ  . LYS A  18  ? 0.6219 0.5218 0.8954 0.0377  -0.0948 -0.1479 18  LYS A NZ  
144  N  N   . TYR A  19  ? 0.1443 0.1089 0.1918 -0.0125 -0.0227 0.0113  19  TYR A N   
145  C  CA  . TYR A  19  ? 0.1446 0.1265 0.1999 -0.0083 -0.0156 0.0341  19  TYR A CA  
146  C  C   . TYR A  19  ? 0.1333 0.1240 0.2030 -0.0100 -0.0200 0.0060  19  TYR A C   
147  O  O   . TYR A  19  ? 0.1340 0.1173 0.1929 -0.0053 -0.0109 0.0155  19  TYR A O   
148  C  CB  . TYR A  19  ? 0.1532 0.1042 0.1995 -0.0140 -0.0208 0.0190  19  TYR A CB  
149  C  CG  . TYR A  19  ? 0.1689 0.1116 0.2016 -0.0094 -0.0475 0.0163  19  TYR A CG  
150  C  CD1 . TYR A  19  ? 0.1543 0.1131 0.2452 -0.0001 -0.0417 -0.0039 19  TYR A CD1 
151  C  CD2 . TYR A  19  ? 0.1866 0.1159 0.2093 -0.0040 -0.0466 0.0299  19  TYR A CD2 
152  C  CE1 . TYR A  19  ? 0.2177 0.1480 0.2369 -0.0337 -0.0472 0.0039  19  TYR A CE1 
153  C  CE2 . TYR A  19  ? 0.2054 0.1204 0.2000 -0.0089 -0.0325 0.0015  19  TYR A CE2 
154  C  CZ  . TYR A  19  ? 0.2390 0.1384 0.2090 -0.0181 -0.0584 0.0255  19  TYR A CZ  
155  O  OH  . TYR A  19  ? 0.2939 0.2196 0.2358 -0.0469 -0.0930 -0.0021 19  TYR A OH  
156  N  N   . PRO A  20  ? 0.1543 0.1188 0.1935 -0.0096 -0.0118 0.0120  20  PRO A N   
157  C  CA  . PRO A  20  ? 0.1726 0.1035 0.1768 0.0010  -0.0155 0.0222  20  PRO A CA  
158  C  C   . PRO A  20  ? 0.1448 0.0987 0.2005 -0.0081 -0.0188 0.0185  20  PRO A C   
159  O  O   . PRO A  20  ? 0.1429 0.1080 0.2011 -0.0023 -0.0234 0.0223  20  PRO A O   
160  C  CB  . PRO A  20  ? 0.2521 0.0942 0.2247 -0.0104 -0.0240 0.0571  20  PRO A CB  
161  C  CG  . PRO A  20  ? 0.2250 0.1787 0.2472 -0.0455 -0.0370 0.0379  20  PRO A CG  
162  C  CD  . PRO A  20  ? 0.1674 0.1107 0.2337 -0.0212 -0.0118 0.0312  20  PRO A CD  
163  N  N   . SER A  21  ? 0.1298 0.1152 0.1967 -0.0068 0.0041  0.0242  21  SER A N   
164  C  CA  . SER A  21  ? 0.1307 0.1046 0.1842 0.0051  -0.0064 0.0164  21  SER A CA  
165  C  C   . SER A  21  ? 0.1110 0.1292 0.1513 0.0081  -0.0200 0.0303  21  SER A C   
166  O  O   . SER A  21  ? 0.1235 0.1254 0.1683 0.0009  -0.0093 0.0117  21  SER A O   
167  C  CB  . SER A  21  ? 0.1181 0.1578 0.1806 -0.0181 0.0034  0.0397  21  SER A CB  
168  O  OG  . SER A  21  ? 0.1535 0.1745 0.2395 -0.0278 0.0086  0.0605  21  SER A OG  
169  N  N   . CYS A  22  ? 0.1138 0.1201 0.1641 -0.0114 -0.0116 0.0209  22  CYS A N   
170  C  CA  . CYS A  22  ? 0.1036 0.1209 0.1887 -0.0309 -0.0068 0.0254  22  CYS A CA  
171  C  C   . CYS A  22  ? 0.1216 0.1070 0.1744 -0.0095 -0.0044 0.0314  22  CYS A C   
172  O  O   . CYS A  22  ? 0.1226 0.1269 0.1952 -0.0142 -0.0185 0.0330  22  CYS A O   
173  C  CB  . CYS A  22  ? 0.1125 0.1155 0.1910 0.0002  -0.0086 0.0120  22  CYS A CB  
174  S  SG  . CYS A  22  ? 0.1360 0.1264 0.1825 -0.0126 -0.0113 0.0179  22  CYS A SG  
175  N  N   . GLY A  23  ? 0.1215 0.1408 0.1875 -0.0055 -0.0218 0.0477  23  GLY A N   
176  C  CA  . GLY A  23  ? 0.1123 0.1484 0.1922 -0.0027 -0.0176 0.0320  23  GLY A CA  
177  C  C   . GLY A  23  ? 0.1554 0.1036 0.1874 -0.0133 -0.0086 0.0324  23  GLY A C   
178  O  O   . GLY A  23  ? 0.1601 0.1456 0.1930 0.0131  -0.0242 0.0324  23  GLY A O   
179  N  N   . GLY A  24  ? 0.1469 0.1415 0.1815 -0.0105 -0.0044 0.0381  24  GLY A N   
180  C  CA  . GLY A  24  ? 0.1561 0.1659 0.1954 0.0027  -0.0096 0.0369  24  GLY A CA  
181  C  C   . GLY A  24  ? 0.1917 0.1498 0.1541 -0.0008 -0.0365 0.0348  24  GLY A C   
182  O  O   . GLY A  24  ? 0.1916 0.1881 0.2187 -0.0173 -0.0325 0.0609  24  GLY A O   
183  N  N   . LEU A  25  ? 0.2071 0.1562 0.1728 0.0266  -0.0228 0.0341  25  LEU A N   
184  C  CA  . LEU A  25  ? 0.2071 0.1906 0.1905 0.0386  -0.0420 0.0085  25  LEU A CA  
185  C  C   . LEU A  25  ? 0.1811 0.1701 0.1870 0.0000  -0.0245 0.0295  25  LEU A C   
186  O  O   . LEU A  25  ? 0.1932 0.1587 0.1876 -0.0017 -0.0111 0.0317  25  LEU A O   
187  C  CB  . LEU A  25  ? 0.4070 0.1812 0.1425 0.0245  -0.0376 0.0381  25  LEU A CB  
188  C  CG  . LEU A  25  ? 0.4237 0.2353 0.3077 0.0593  -0.0748 0.0619  25  LEU A CG  
189  C  CD1 . LEU A  25  ? 0.6380 0.2655 0.2474 0.0165  -0.0286 0.0623  25  LEU A CD1 
190  C  CD2 . LEU A  25  ? 0.5040 0.3168 0.3156 0.0637  -0.2078 0.0633  25  LEU A CD2 
191  N  N   . LEU A  26  ? 0.2238 0.1630 0.1620 0.0001  -0.0355 0.0234  26  LEU A N   
192  C  CA  . LEU A  26  ? 0.1923 0.1885 0.1627 0.0181  -0.0241 0.0341  26  LEU A CA  
193  C  C   . LEU A  26  ? 0.1517 0.1679 0.1617 0.0092  -0.0342 0.0122  26  LEU A C   
194  O  O   . LEU A  26  ? 0.1480 0.2112 0.1819 0.0265  -0.0119 0.0298  26  LEU A O   
195  C  CB  . LEU A  26  ? 0.2226 0.2048 0.1998 -0.0009 0.0206  0.0291  26  LEU A CB  
196  C  CG  . LEU A  26  ? 0.2755 0.2735 0.2219 -0.0167 0.0129  0.0150  26  LEU A CG  
197  C  CD1 . LEU A  26  ? 0.2705 0.4606 0.2976 -0.0597 0.0697  -0.0277 26  LEU A CD1 
198  C  CD2 . LEU A  26  ? 0.2663 0.3486 0.2457 -0.0490 -0.0168 -0.0119 26  LEU A CD2 
199  N  N   . GLN A  27  ? 0.1389 0.1342 0.1566 -0.0038 -0.0131 0.0365  27  GLN A N   
200  C  CA  . GLN A  27  ? 0.1237 0.1087 0.1566 -0.0109 -0.0136 0.0215  27  GLN A CA  
201  C  C   . GLN A  27  ? 0.1225 0.1031 0.1466 -0.0167 -0.0207 0.0103  27  GLN A C   
202  O  O   . GLN A  27  ? 0.1808 0.1358 0.1667 -0.0127 -0.0541 0.0324  27  GLN A O   
203  C  CB  . GLN A  27  ? 0.1184 0.1140 0.1667 0.0037  -0.0205 0.0209  27  GLN A CB  
204  C  CG  . GLN A  27  ? 0.1188 0.1242 0.1772 -0.0116 -0.0294 0.0346  27  GLN A CG  
205  C  CD  . GLN A  27  ? 0.1254 0.1139 0.1614 0.0058  -0.0031 0.0322  27  GLN A CD  
206  O  OE1 . GLN A  27  ? 0.1213 0.1042 0.1518 -0.0099 0.0027  0.0251  27  GLN A OE1 
207  N  NE2 . GLN A  27  ? 0.1218 0.1217 0.1627 0.0017  0.0044  0.0301  27  GLN A NE2 
208  N  N   . SER A  28  ? 0.1089 0.1164 0.1374 0.0004  -0.0095 0.0161  28  SER A N   
209  C  CA  . SER A  28  ? 0.1003 0.1193 0.1339 0.0039  0.0001  0.0247  28  SER A CA  
210  C  C   . SER A  28  ? 0.0992 0.1159 0.1330 -0.0010 -0.0217 0.0133  28  SER A C   
211  O  O   . SER A  28  ? 0.1125 0.1137 0.1361 0.0063  -0.0031 0.0100  28  SER A O   
212  C  CB  . SER A  28  ? 0.1107 0.1395 0.1319 0.0033  0.0071  0.0199  28  SER A CB  
213  O  OG  . SER A  28  ? 0.1098 0.1303 0.1324 0.0058  0.0024  0.0229  28  SER A OG  
214  N  N   . PRO A  29  ? 0.0931 0.1200 0.1326 -0.0047 -0.0069 0.0114  29  PRO A N   
215  C  CA  . PRO A  29  ? 0.1186 0.0931 0.1299 -0.0079 -0.0057 0.0163  29  PRO A CA  
216  C  C   . PRO A  29  ? 0.0945 0.1064 0.1271 -0.0081 -0.0034 0.0054  29  PRO A C   
217  O  O   . PRO A  29  ? 0.1100 0.1263 0.1429 0.0006  -0.0175 0.0183  29  PRO A O   
218  C  CB  . PRO A  29  ? 0.1118 0.1186 0.1290 0.0036  0.0036  0.0286  29  PRO A CB  
219  C  CG  . PRO A  29  ? 0.1143 0.1018 0.1593 0.0089  0.0024  0.0175  29  PRO A CG  
220  C  CD  . PRO A  29  ? 0.1084 0.1091 0.1199 0.0011  -0.0052 0.0144  29  PRO A CD  
221  N  N   . ILE A  30  ? 0.1168 0.1077 0.1437 -0.0030 -0.0081 0.0064  30  ILE A N   
222  C  CA  . ILE A  30  ? 0.1198 0.1134 0.1521 -0.0243 -0.0248 0.0160  30  ILE A CA  
223  C  C   . ILE A  30  ? 0.1133 0.1207 0.1400 -0.0021 -0.0010 -0.0039 30  ILE A C   
224  O  O   . ILE A  30  ? 0.1119 0.1286 0.1784 -0.0055 -0.0158 0.0142  30  ILE A O   
225  C  CB  . ILE A  30  ? 0.1305 0.1365 0.1472 -0.0078 -0.0027 0.0156  30  ILE A CB  
226  C  CG1 . ILE A  30  ? 0.1089 0.1894 0.1500 -0.0052 -0.0157 -0.0232 30  ILE A CG1 
227  C  CG2 . ILE A  30  ? 0.2208 0.1442 0.1421 -0.0416 -0.0076 0.0237  30  ILE A CG2 
228  C  CD1 . ILE A  30  ? 0.1649 0.1923 0.1535 -0.0034 -0.0049 -0.0346 30  ILE A CD1 
229  N  N   . ASP A  31  ? 0.1221 0.1363 0.1571 -0.0171 -0.0182 -0.0073 31  ASP A N   
230  C  CA  . ASP A  31  ? 0.1179 0.1260 0.1702 -0.0331 -0.0229 0.0092  31  ASP A CA  
231  C  C   . ASP A  31  ? 0.1427 0.1098 0.1498 -0.0259 -0.0255 0.0182  31  ASP A C   
232  O  O   . ASP A  31  ? 0.2158 0.1437 0.1676 -0.0023 -0.0236 0.0115  31  ASP A O   
233  C  CB  . ASP A  31  ? 0.1195 0.1554 0.1934 -0.0215 -0.0317 0.0209  31  ASP A CB  
234  C  CG  . ASP A  31  ? 0.1471 0.1823 0.1762 -0.0337 -0.0146 0.0232  31  ASP A CG  
235  O  OD1 . ASP A  31  ? 0.1432 0.1513 0.2182 -0.0299 -0.0351 0.0363  31  ASP A OD1 
236  O  OD2 . ASP A  31  ? 0.1947 0.2064 0.2714 -0.0727 -0.0784 0.0694  31  ASP A OD2 
237  N  N   . LEU A  32  ? 0.1450 0.1474 0.1724 -0.0016 -0.0020 0.0192  32  LEU A N   
238  C  CA  . LEU A  32  ? 0.1323 0.1590 0.1855 -0.0032 0.0044  0.0008  32  LEU A CA  
239  C  C   . LEU A  32  ? 0.1876 0.1976 0.1465 -0.0370 0.0160  -0.0079 32  LEU A C   
240  O  O   . LEU A  32  ? 0.2105 0.1560 0.2104 -0.0268 -0.0192 0.0052  32  LEU A O   
241  C  CB  . LEU A  32  ? 0.1564 0.1493 0.2172 -0.0010 -0.0036 -0.0024 32  LEU A CB  
242  C  CG  . LEU A  32  ? 0.1578 0.1468 0.1461 0.0089  0.0010  0.0064  32  LEU A CG  
243  C  CD1 . LEU A  32  ? 0.1429 0.1958 0.2151 0.0212  -0.0182 0.0070  32  LEU A CD1 
244  C  CD2 . LEU A  32  ? 0.1948 0.2387 0.2162 -0.0337 0.0346  0.0403  32  LEU A CD2 
245  N  N   . HIS A  33  ? 0.2336 0.3240 0.1835 -0.1086 -0.0278 0.0027  33  HIS A N   
246  C  CA  . HIS A  33  ? 0.2594 0.4405 0.2148 -0.1517 -0.0187 0.0046  33  HIS A CA  
247  C  C   . HIS A  33  ? 0.2474 0.3346 0.2443 -0.1452 -0.0464 0.0193  33  HIS A C   
248  O  O   . HIS A  33  ? 0.1843 0.3141 0.2243 -0.0792 -0.0190 0.0060  33  HIS A O   
249  C  CB  . HIS A  33  ? 0.2944 0.3166 0.3436 -0.0572 -0.0691 0.0434  33  HIS A CB  
250  C  CG  . HIS A  33  ? 0.2237 0.3281 0.2401 -0.0131 -0.0306 -0.0161 33  HIS A CG  
251  N  ND1 . HIS A  33  ? 0.3984 0.3552 0.3516 0.0443  -0.0650 0.0232  33  HIS A ND1 
252  C  CD2 . HIS A  33  ? 0.2542 0.5712 0.4202 -0.0027 -0.1891 0.0336  33  HIS A CD2 
253  C  CE1 . HIS A  33  ? 0.3157 0.4492 0.4095 -0.1202 -0.1076 0.0998  33  HIS A CE1 
254  N  NE2 . HIS A  33  ? 0.3854 0.6030 0.4479 -0.0184 -0.1945 0.0072  33  HIS A NE2 
255  N  N   . SER A  34  ? 0.2518 0.3147 0.3573 -0.1107 -0.0414 -0.0032 34  SER A N   
256  C  CA  . SER A  34  ? 0.3770 0.3098 0.4221 -0.1674 -0.0027 -0.0108 34  SER A CA  
257  C  C   . SER A  34  ? 0.2881 0.2947 0.4170 -0.0738 -0.0282 -0.0450 34  SER A C   
258  O  O   . SER A  34  ? 0.3181 0.4772 0.4654 -0.1207 -0.0179 -0.2365 34  SER A O   
259  C  CB  . SER A  34  ? 0.5335 0.3097 0.7447 -0.2134 0.0329  -0.0156 34  SER A CB  
260  O  OG  . SER A  34  ? 0.6736 0.4954 0.7152 -0.2831 0.0367  -0.1293 34  SER A OG  
261  N  N   . ASP A  35  ? 0.2349 0.3314 0.3307 -0.0954 -0.0505 0.0334  35  ASP A N   
262  C  CA  . ASP A  35  ? 0.3225 0.4168 0.4000 -0.0681 -0.1053 0.0707  35  ASP A CA  
263  C  C   . ASP A  35  ? 0.2326 0.4563 0.3156 -0.0593 -0.0670 -0.0080 35  ASP A C   
264  O  O   . ASP A  35  ? 0.3648 0.6042 0.3252 -0.0714 -0.1428 0.0372  35  ASP A O   
265  C  CB  . ASP A  35  ? 0.3074 0.6778 0.4470 -0.0031 0.0595  0.0575  35  ASP A CB  
266  C  CG  . ASP A  35  ? 0.5581 0.8500 0.8356 -0.1141 -0.0170 0.2791  35  ASP A CG  
267  O  OD1 . ASP A  35  ? 0.3902 0.9990 1.4852 -0.0525 -0.3156 0.2351  35  ASP A OD1 
268  O  OD2 . ASP A  35  ? 0.5914 0.7853 0.8805 -0.0089 -0.2830 0.0368  35  ASP A OD2 
269  N  N   . ILE A  36  ? 0.2266 0.3764 0.2760 -0.0613 -0.0767 0.0491  36  ILE A N   
270  C  CA  . ILE A  36  ? 0.2292 0.3324 0.2112 -0.0177 -0.0278 0.0135  36  ILE A CA  
271  C  C   . ILE A  36  ? 0.2252 0.2755 0.2025 -0.0229 -0.0558 -0.0033 36  ILE A C   
272  O  O   . ILE A  36  ? 0.2154 0.3307 0.2684 -0.0369 -0.0259 0.0731  36  ILE A O   
273  C  CB  . ILE A  36  ? 0.2977 0.3581 0.2300 0.0851  -0.0115 0.0358  36  ILE A CB  
274  C  CG1 . ILE A  36  ? 0.3608 0.3549 0.1936 -0.0972 0.0178  0.0355  36  ILE A CG1 
275  C  CG2 . ILE A  36  ? 0.2595 0.4034 0.3172 0.0557  -0.0237 0.1123  36  ILE A CG2 
276  C  CD1 . ILE A  36  ? 0.2948 0.3218 0.3070 -0.0358 0.0209  0.0017  36  ILE A CD1 
277  N  N   . LEU A  37  ? 0.2631 0.3137 0.1967 -0.0457 -0.0436 0.0016  37  LEU A N   
278  C  CA  . LEU A  37  ? 0.2292 0.3009 0.2053 -0.0476 -0.0480 -0.0071 37  LEU A CA  
279  C  C   . LEU A  37  ? 0.2190 0.3357 0.2113 -0.0154 -0.0416 -0.0332 37  LEU A C   
280  O  O   . LEU A  37  ? 0.3217 0.3328 0.2734 -0.0949 -0.0521 -0.0697 37  LEU A O   
281  C  CB  . LEU A  37  ? 0.2284 0.2953 0.2447 -0.0480 -0.0374 -0.0131 37  LEU A CB  
282  C  CG  . LEU A  37  ? 0.2479 0.3008 0.2922 -0.0519 0.0133  0.0188  37  LEU A CG  
283  C  CD1 . LEU A  37  ? 0.2725 0.3450 0.2814 -0.0467 -0.0621 0.0447  37  LEU A CD1 
284  C  CD2 . LEU A  37  ? 0.2161 0.2784 0.2358 -0.0166 -0.0063 0.0048  37  LEU A CD2 
285  N  N   . GLN A  38  ? 0.2169 0.2828 0.2179 -0.0353 -0.0133 -0.0059 38  GLN A N   
286  C  CA  . GLN A  38  ? 0.2401 0.2973 0.1955 -0.0497 -0.0084 0.0076  38  GLN A CA  
287  C  C   . GLN A  38  ? 0.2434 0.2640 0.1757 -0.0346 0.0058  -0.0346 38  GLN A C   
288  O  O   . GLN A  38  ? 0.2488 0.2232 0.1878 -0.0445 -0.0164 -0.0385 38  GLN A O   
289  C  CB  . GLN A  38  ? 0.3483 0.4128 0.1861 -0.0227 0.0212  0.0691  38  GLN A CB  
290  C  CG  . GLN A  38  ? 0.4554 0.5623 0.1831 0.1703  0.0381  0.0829  38  GLN A CG  
291  C  CD  . GLN A  38  ? 0.5290 0.4084 0.2998 -0.0205 0.0109  0.0473  38  GLN A CD  
292  O  OE1 . GLN A  38  ? 0.5837 0.7525 0.4266 0.1270  -0.0021 0.0220  38  GLN A OE1 
293  N  NE2 . GLN A  38  ? 0.4069 0.5403 0.3995 0.0063  0.0293  0.1571  38  GLN A NE2 
294  N  N   . TYR A  39  ? 0.2683 0.2786 0.2119 -0.0624 -0.0121 -0.0579 39  TYR A N   
295  C  CA  . TYR A  39  ? 0.2984 0.2190 0.1986 -0.0900 -0.0159 -0.0105 39  TYR A CA  
296  C  C   . TYR A  39  ? 0.2507 0.2846 0.1808 -0.0606 0.0270  -0.0256 39  TYR A C   
297  O  O   . TYR A  39  ? 0.3323 0.3098 0.1766 -0.0558 -0.0160 -0.0350 39  TYR A O   
298  C  CB  . TYR A  39  ? 0.3062 0.1798 0.2472 -0.0630 -0.0195 -0.0333 39  TYR A CB  
299  C  CG  . TYR A  39  ? 0.3301 0.2367 0.2813 -0.0430 -0.0168 -0.0752 39  TYR A CG  
300  C  CD1 . TYR A  39  ? 0.3596 0.2795 0.3319 -0.0012 -0.0982 -0.0763 39  TYR A CD1 
301  C  CD2 . TYR A  39  ? 0.4115 0.2445 0.2602 0.0196  -0.0560 -0.1064 39  TYR A CD2 
302  C  CE1 . TYR A  39  ? 0.3299 0.3157 0.3652 -0.0732 -0.0013 -0.1383 39  TYR A CE1 
303  C  CE2 . TYR A  39  ? 0.4224 0.3265 0.3615 -0.0518 0.0783  -0.1810 39  TYR A CE2 
304  C  CZ  . TYR A  39  ? 0.4209 0.2965 0.4603 0.0625  -0.0423 -0.1688 39  TYR A CZ  
305  O  OH  . TYR A  39  ? 0.4996 0.3823 0.4714 0.1417  -0.0948 -0.2054 39  TYR A OH  
306  N  N   . ASP A  40  ? 0.2363 0.2301 0.1999 -0.0266 0.0190  -0.0571 40  ASP A N   
307  C  CA  . ASP A  40  ? 0.2603 0.2854 0.1707 -0.0423 0.0052  -0.0010 40  ASP A CA  
308  C  C   . ASP A  40  ? 0.3001 0.2974 0.2241 0.0219  0.0361  0.0208  40  ASP A C   
309  O  O   . ASP A  40  ? 0.2724 0.2830 0.2130 -0.0461 0.0197  -0.0271 40  ASP A O   
310  C  CB  . ASP A  40  ? 0.3565 0.2830 0.2528 -0.1095 0.0018  0.0135  40  ASP A CB  
311  C  CG  . ASP A  40  ? 0.4492 0.4393 0.3570 -0.1085 0.1116  -0.0348 40  ASP A CG  
312  O  OD1 . ASP A  40  ? 0.3265 0.4898 0.2809 -0.0154 -0.0003 0.1123  40  ASP A OD1 
313  O  OD2 . ASP A  40  ? 0.6848 0.4058 0.7043 -0.1615 0.2348  0.1645  40  ASP A OD2 
314  N  N   . ALA A  41  ? 0.3502 0.3964 0.2303 0.0070  0.0564  -0.0633 41  ALA A N   
315  C  CA  . ALA A  41  ? 0.4394 0.4697 0.2394 0.0550  0.0201  -0.1015 41  ALA A CA  
316  C  C   . ALA A  41  ? 0.3541 0.3180 0.2434 0.0478  0.1151  -0.0820 41  ALA A C   
317  O  O   . ALA A  41  ? 0.4717 0.5484 0.3647 0.1846  0.0921  -0.1080 41  ALA A O   
318  C  CB  . ALA A  41  ? 0.4372 0.5236 0.2863 0.0740  -0.0084 -0.1787 41  ALA A CB  
319  N  N   . SER A  42  ? 0.4142 0.3054 0.2413 0.0139  0.1045  -0.0227 42  SER A N   
320  C  CA  . SER A  42  ? 0.3617 0.3871 0.3290 -0.0663 0.0580  0.0639  42  SER A CA  
321  C  C   . SER A  42  ? 0.3439 0.4317 0.3620 -0.0516 0.1134  0.0403  42  SER A C   
322  O  O   . SER A  42  ? 0.2351 0.5083 0.3770 -0.0209 0.0675  0.1772  42  SER A O   
323  C  CB  . SER A  42  ? 0.4416 0.4047 0.5104 -0.0408 0.1262  0.1271  42  SER A CB  
324  O  OG  . SER A  42  ? 0.4408 0.5720 0.5292 -0.0018 0.1404  0.1720  42  SER A OG  
325  N  N   . LEU A  43  ? 0.2480 0.2745 0.2627 -0.0352 0.0461  0.0175  43  LEU A N   
326  C  CA  . LEU A  43  ? 0.2418 0.2461 0.2828 -0.0135 0.0197  -0.0145 43  LEU A CA  
327  C  C   . LEU A  43  ? 0.2198 0.2789 0.2356 -0.0269 0.0527  -0.0146 43  LEU A C   
328  O  O   . LEU A  43  ? 0.2341 0.2615 0.3040 -0.0105 0.0408  -0.0068 43  LEU A O   
329  C  CB  . LEU A  43  ? 0.2099 0.2049 0.2661 -0.0127 0.0194  -0.0433 43  LEU A CB  
330  C  CG  . LEU A  43  ? 0.2300 0.2060 0.2256 -0.0124 0.0179  -0.0493 43  LEU A CG  
331  C  CD1 . LEU A  43  ? 0.2366 0.2168 0.2144 -0.0223 0.0136  -0.0061 43  LEU A CD1 
332  C  CD2 . LEU A  43  ? 0.2735 0.2196 0.2518 -0.0336 0.0066  0.0019  43  LEU A CD2 
333  N  N   . THR A  44  ? 0.2170 0.3424 0.2236 -0.0234 0.0488  -0.0546 44  THR A N   
334  C  CA  . THR A  44  ? 0.2104 0.3847 0.2262 0.0253  0.0365  -0.0467 44  THR A CA  
335  C  C   . THR A  44  ? 0.2522 0.2716 0.2375 0.0151  0.0603  -0.0554 44  THR A C   
336  O  O   . THR A  44  ? 0.1997 0.2517 0.2319 0.0062  0.0328  -0.0332 44  THR A O   
337  C  CB  . THR A  44  ? 0.2626 0.4710 0.3170 0.0115  0.0981  -0.0766 44  THR A CB  
338  O  OG1 . THR A  44  ? 0.2438 0.4920 0.4353 -0.0133 0.1218  0.0285  44  THR A OG1 
339  C  CG2 . THR A  44  ? 0.4977 0.7006 0.3361 0.0878  0.1412  -0.1735 44  THR A CG2 
340  N  N   . PRO A  45  ? 0.2555 0.2400 0.2399 0.0276  0.0378  -0.0286 45  PRO A N   
341  C  CA  . PRO A  45  ? 0.1873 0.2906 0.2349 0.0137  0.0193  -0.0474 45  PRO A CA  
342  C  C   . PRO A  45  ? 0.2253 0.2579 0.2046 0.0192  0.0201  -0.0046 45  PRO A C   
343  O  O   . PRO A  45  ? 0.2555 0.3440 0.2698 -0.0095 0.0719  -0.0591 45  PRO A O   
344  C  CB  . PRO A  45  ? 0.3219 0.2969 0.2788 0.0348  0.0145  -0.0358 45  PRO A CB  
345  C  CG  . PRO A  45  ? 0.3319 0.3353 0.3361 0.0708  -0.0345 -0.0671 45  PRO A CG  
346  C  CD  . PRO A  45  ? 0.2816 0.2944 0.3274 0.0757  0.0851  -0.0781 45  PRO A CD  
347  N  N   . LEU A  46  ? 0.2170 0.2332 0.2119 0.0174  0.0245  -0.0166 46  LEU A N   
348  C  CA  . LEU A  46  ? 0.1838 0.2524 0.2088 0.0258  0.0076  0.0159  46  LEU A CA  
349  C  C   . LEU A  46  ? 0.2294 0.2231 0.1896 0.0283  0.0124  -0.0196 46  LEU A C   
350  O  O   . LEU A  46  ? 0.2423 0.2671 0.2498 -0.0039 -0.0165 0.0277  46  LEU A O   
351  C  CB  . LEU A  46  ? 0.1987 0.1964 0.2262 0.0564  -0.0105 0.0013  46  LEU A CB  
352  C  CG  . LEU A  46  ? 0.1718 0.2334 0.2354 0.0165  0.0168  0.0558  46  LEU A CG  
353  C  CD1 . LEU A  46  ? 0.1680 0.2646 0.3046 0.0350  0.0282  0.0251  46  LEU A CD1 
354  C  CD2 . LEU A  46  ? 0.2544 0.3190 0.2884 0.0378  0.0118  0.0987  46  LEU A CD2 
355  N  N   . GLU A  47  ? 0.2018 0.2465 0.1941 0.0196  0.0088  -0.0295 47  GLU A N   
356  C  CA  . GLU A  47  ? 0.1665 0.2685 0.2563 0.0335  -0.0284 -0.0508 47  GLU A CA  
357  C  C   . GLU A  47  ? 0.1942 0.2208 0.1974 0.0507  -0.0273 -0.0156 47  GLU A C   
358  O  O   . GLU A  47  ? 0.2585 0.2640 0.2183 0.0381  -0.0013 0.0269  47  GLU A O   
359  C  CB  . GLU A  47  ? 0.2404 0.3890 0.2873 0.0954  0.0458  -0.0521 47  GLU A CB  
360  C  CG  . GLU A  47  ? 0.3327 0.4417 0.4492 0.1141  0.0618  -0.0973 47  GLU A CG  
361  C  CD  . GLU A  47  ? 0.4243 0.8123 0.6276 0.2137  0.1646  -0.0798 47  GLU A CD  
362  O  OE1 . GLU A  47  ? 0.5896 1.1224 0.6470 0.2484  0.2121  -0.1787 47  GLU A OE1 
363  O  OE2 . GLU A  47  ? 0.3470 0.8704 0.9858 0.2530  0.0759  0.1211  47  GLU A OE2 
364  N  N   . PHE A  48  ? 0.1548 0.2302 0.2287 0.0488  0.0017  0.0298  48  PHE A N   
365  C  CA  . PHE A  48  ? 0.1373 0.2353 0.2164 0.0128  0.0074  0.0200  48  PHE A CA  
366  C  C   . PHE A  48  ? 0.1358 0.2247 0.2304 0.0344  -0.0276 0.0545  48  PHE A C   
367  O  O   . PHE A  48  ? 0.2133 0.2551 0.3357 0.0171  -0.0804 0.0740  48  PHE A O   
368  C  CB  . PHE A  48  ? 0.1917 0.2274 0.1998 -0.0193 0.0037  0.0546  48  PHE A CB  
369  C  CG  . PHE A  48  ? 0.1939 0.2121 0.1674 0.0074  -0.0003 0.0034  48  PHE A CG  
370  C  CD1 . PHE A  48  ? 0.1824 0.2249 0.1931 0.0309  0.0269  0.0057  48  PHE A CD1 
371  C  CD2 . PHE A  48  ? 0.2449 0.2168 0.2093 -0.0176 -0.0050 0.0234  48  PHE A CD2 
372  C  CE1 . PHE A  48  ? 0.1854 0.2302 0.1760 0.0231  0.0183  -0.0097 48  PHE A CE1 
373  C  CE2 . PHE A  48  ? 0.2229 0.2416 0.2122 -0.0239 0.0491  -0.0201 48  PHE A CE2 
374  C  CZ  . PHE A  48  ? 0.2028 0.2475 0.2263 0.0008  0.0657  -0.0348 48  PHE A CZ  
375  N  N   . GLN A  49  ? 0.1845 0.2363 0.1863 -0.0085 -0.0083 0.0322  49  GLN A N   
376  C  CA  . GLN A  49  ? 0.1775 0.2209 0.2355 0.0177  -0.0068 0.0148  49  GLN A CA  
377  C  C   . GLN A  49  ? 0.1202 0.1956 0.2015 -0.0019 0.0008  0.0559  49  GLN A C   
378  O  O   . GLN A  49  ? 0.1451 0.2143 0.1825 0.0119  -0.0024 0.0428  49  GLN A O   
379  C  CB  . GLN A  49  ? 0.2019 0.3253 0.1658 0.0035  0.0312  0.0124  49  GLN A CB  
380  C  CG  . GLN A  49  ? 0.2898 0.3141 0.2666 -0.0317 0.0153  -0.0165 49  GLN A CG  
381  C  CD  . GLN A  49  ? 0.3495 0.4583 0.5983 -0.0140 0.1679  -0.0866 49  GLN A CD  
382  O  OE1 . GLN A  49  ? 0.6597 0.5499 0.4785 0.1419  0.1972  -0.1238 49  GLN A OE1 
383  N  NE2 . GLN A  49  ? 0.6179 0.2957 0.8047 -0.0352 0.0419  -0.1004 49  GLN A NE2 
384  N  N   . GLY A  50  ? 0.1368 0.2732 0.1940 0.0312  0.0008  0.0310  50  GLY A N   
385  C  CA  . GLY A  50  ? 0.1128 0.2842 0.1881 -0.0040 0.0029  0.0283  50  GLY A CA  
386  C  C   . GLY A  50  ? 0.1669 0.2000 0.1995 0.0134  0.0052  0.0177  50  GLY A C   
387  O  O   . GLY A  50  ? 0.1419 0.2426 0.2088 -0.0122 0.0011  0.0205  50  GLY A O   
388  N  N   . TYR A  51  ? 0.1345 0.2232 0.2035 0.0234  0.0098  0.0402  51  TYR A N   
389  C  CA  . TYR A  51  ? 0.1235 0.2470 0.1825 -0.0055 -0.0124 0.0507  51  TYR A CA  
390  C  C   . TYR A  51  ? 0.1371 0.2508 0.1985 0.0396  -0.0125 0.0446  51  TYR A C   
391  O  O   . TYR A  51  ? 0.1464 0.2698 0.1908 0.0337  -0.0011 0.0342  51  TYR A O   
392  C  CB  . TYR A  51  ? 0.1368 0.1813 0.1996 0.0243  -0.0196 0.0361  51  TYR A CB  
393  C  CG  . TYR A  51  ? 0.1367 0.2085 0.1688 0.0243  -0.0095 0.0347  51  TYR A CG  
394  C  CD1 . TYR A  51  ? 0.1269 0.2249 0.1685 0.0178  -0.0170 0.0425  51  TYR A CD1 
395  C  CD2 . TYR A  51  ? 0.1256 0.1773 0.2062 0.0106  -0.0023 0.0391  51  TYR A CD2 
396  C  CE1 . TYR A  51  ? 0.1455 0.2017 0.1617 0.0204  -0.0083 0.0134  51  TYR A CE1 
397  C  CE2 . TYR A  51  ? 0.1345 0.1877 0.1873 0.0122  -0.0027 0.0411  51  TYR A CE2 
398  C  CZ  . TYR A  51  ? 0.1240 0.1688 0.2234 0.0174  -0.0394 0.0374  51  TYR A CZ  
399  O  OH  . TYR A  51  ? 0.1408 0.2031 0.2049 0.0038  -0.0272 0.0480  51  TYR A OH  
400  N  N   . ASN A  52  ? 0.1350 0.2617 0.2431 0.0353  -0.0276 0.0657  52  ASN A N   
401  C  CA  . ASN A  52  ? 0.1935 0.2921 0.2073 0.0564  -0.0211 0.0132  52  ASN A CA  
402  C  C   . ASN A  52  ? 0.1494 0.2728 0.2699 0.0425  -0.0304 0.0163  52  ASN A C   
403  O  O   . ASN A  52  ? 0.1306 0.3966 0.3348 0.0363  -0.0257 -0.0149 52  ASN A O   
404  C  CB  . ASN A  52  ? 0.2250 0.2702 0.2602 0.0625  -0.0096 0.0643  52  ASN A CB  
405  C  CG  . ASN A  52  ? 0.2640 0.3745 0.3322 0.1137  -0.0384 0.0964  52  ASN A CG  
406  O  OD1 . ASN A  52  ? 0.2605 0.3939 0.2836 0.0773  -0.0494 0.0766  52  ASN A OD1 
407  N  ND2 . ASN A  52  ? 0.2931 0.4605 0.3799 0.1503  -0.0139 0.1102  52  ASN A ND2 
408  N  N   . LEU A  53  ? 0.1941 0.3070 0.2195 0.0245  -0.0094 -0.0053 53  LEU A N   
409  C  CA  . LEU A  53  ? 0.2033 0.3273 0.2188 0.0809  -0.0394 -0.0150 53  LEU A CA  
410  C  C   . LEU A  53  ? 0.1926 0.4154 0.2946 -0.0160 -0.1036 -0.0351 53  LEU A C   
411  O  O   . LEU A  53  ? 0.3019 0.4003 0.3120 0.1144  -0.1389 0.0011  53  LEU A O   
412  C  CB  . LEU A  53  ? 0.1541 0.2439 0.2319 0.0043  -0.0364 0.0010  53  LEU A CB  
413  C  CG  . LEU A  53  ? 0.1694 0.2449 0.1877 -0.0055 -0.0173 0.0418  53  LEU A CG  
414  C  CD1 . LEU A  53  ? 0.1939 0.2714 0.2276 0.0370  -0.0304 0.0403  53  LEU A CD1 
415  C  CD2 . LEU A  53  ? 0.2665 0.2623 0.2079 -0.0652 -0.0239 0.0434  53  LEU A CD2 
416  N  N   . SER A  54  ? 0.1609 0.3932 0.3562 0.0507  -0.0551 -0.0778 54  SER A N   
417  C  CA  . SER A  54  ? 0.3068 0.4886 0.3798 0.0547  -0.1389 -0.0363 54  SER A CA  
418  C  C   . SER A  54  ? 0.2781 0.3585 0.4270 0.0400  -0.1195 -0.0087 54  SER A C   
419  O  O   . SER A  54  ? 0.1705 0.4165 0.3066 0.0230  -0.0544 -0.0243 54  SER A O   
420  C  CB  . SER A  54  ? 0.2133 0.5401 0.2988 -0.0076 -0.0596 -0.0297 54  SER A CB  
421  O  OG  . SER A  54  ? 0.2326 0.6779 0.3737 0.0518  -0.0791 -0.1747 54  SER A OG  
422  N  N   . ALA A  55  ? 0.3459 0.4820 0.4941 0.0533  -0.1482 0.0710  55  ALA A N   
423  C  CA  . ALA A  55  ? 0.2869 0.4164 0.4355 -0.0094 -0.1669 0.0525  55  ALA A CA  
424  C  C   . ALA A  55  ? 0.2778 0.4315 0.3787 -0.0639 -0.1447 0.1042  55  ALA A C   
425  O  O   . ALA A  55  ? 0.3224 0.6128 0.3260 -0.0111 -0.1235 0.0656  55  ALA A O   
426  C  CB  . ALA A  55  ? 0.7531 0.5268 0.5247 -0.0002 -0.3380 0.1534  55  ALA A CB  
427  N  N   . ASN A  56  ? 0.2523 0.5133 0.4315 0.0177  -0.1766 0.1256  56  ASN A N   
428  C  CA  . ASN A  56  ? 0.1585 0.4883 0.3940 -0.0025 -0.0928 0.0474  56  ASN A CA  
429  C  C   . ASN A  56  ? 0.2457 0.4452 0.3134 0.0000  -0.0834 0.0038  56  ASN A C   
430  O  O   . ASN A  56  ? 0.3248 0.5348 0.4534 -0.0365 -0.1944 -0.0543 56  ASN A O   
431  C  CB  . ASN A  56  ? 0.1870 0.4515 0.3723 0.0209  -0.0835 0.0248  56  ASN A CB  
432  C  CG  . ASN A  56  ? 0.3856 0.4887 0.4928 0.1324  0.0263  0.0392  56  ASN A CG  
433  O  OD1 . ASN A  56  ? 0.3211 0.6250 0.4598 0.1065  -0.1760 0.0649  56  ASN A OD1 
434  N  ND2 . ASN A  56  ? 0.2778 0.5978 0.5198 -0.0153 -0.0122 -0.1114 56  ASN A ND2 
435  N  N   . LYS A  57  ? 0.2057 0.4036 0.2629 -0.0306 -0.0614 -0.0149 57  LYS A N   
436  C  CA  . LYS A  57  ? 0.1474 0.3734 0.2159 -0.0346 0.0188  0.0266  57  LYS A CA  
437  C  C   . LYS A  57  ? 0.1972 0.3257 0.1941 -0.0245 -0.0146 0.0040  57  LYS A C   
438  O  O   . LYS A  57  ? 0.1813 0.3507 0.2424 -0.0190 -0.0212 0.0538  57  LYS A O   
439  C  CB  . LYS A  57  ? 0.1748 0.3432 0.2089 -0.0436 0.0038  0.0058  57  LYS A CB  
440  C  CG  . LYS A  57  ? 0.2030 0.4351 0.2234 -0.0265 0.0266  0.0038  57  LYS A CG  
441  C  CD  . LYS A  57  ? 0.2150 0.5073 0.2321 -0.0069 -0.0221 0.0695  57  LYS A CD  
442  C  CE  . LYS A  57  ? 0.3844 0.5664 0.4807 0.0015  0.0781  0.0869  57  LYS A CE  
443  N  N   . GLN A  58  ? 0.1711 0.3671 0.2692 -0.0124 -0.0380 -0.0186 58  GLN A N   
444  C  CA  . GLN A  58  ? 0.1486 0.4037 0.2216 0.0173  0.0067  0.0119  58  GLN A CA  
445  C  C   . GLN A  58  ? 0.1464 0.3201 0.2830 -0.0187 -0.0103 0.0309  58  GLN A C   
446  O  O   . GLN A  58  ? 0.1939 0.4203 0.3295 -0.0574 -0.0828 0.0806  58  GLN A O   
447  C  CB  . GLN A  58  ? 0.1443 0.4992 0.2116 0.0672  -0.0241 0.0145  58  GLN A CB  
448  C  CG  . GLN A  58  ? 0.3216 0.4374 0.2096 0.0377  -0.0292 -0.0311 58  GLN A CG  
449  C  CD  . GLN A  58  ? 0.2856 0.3674 0.2408 -0.0333 -0.0829 -0.0052 58  GLN A CD  
450  O  OE1 . GLN A  58  ? 0.5098 0.4666 0.2812 0.0605  -0.0247 0.0359  58  GLN A OE1 
451  N  NE2 . GLN A  58  ? 0.3638 0.4784 0.4099 0.0268  -0.1720 -0.1250 58  GLN A NE2 
452  N  N   . PHE A  59  ? 0.1505 0.3439 0.1786 -0.0114 -0.0192 -0.0151 59  PHE A N   
453  C  CA  . PHE A  59  ? 0.1438 0.3367 0.1863 0.0050  -0.0225 0.0128  59  PHE A CA  
454  C  C   . PHE A  59  ? 0.1525 0.2626 0.2020 -0.0250 -0.0143 -0.0104 59  PHE A C   
455  O  O   . PHE A  59  ? 0.1475 0.3352 0.1963 -0.0106 -0.0257 0.0178  59  PHE A O   
456  C  CB  . PHE A  59  ? 0.1433 0.3298 0.2014 0.0093  -0.0016 -0.0039 59  PHE A CB  
457  C  CG  . PHE A  59  ? 0.1410 0.3079 0.2075 0.0025  -0.0170 -0.0059 59  PHE A CG  
458  C  CD1 . PHE A  59  ? 0.1526 0.3748 0.2107 -0.0197 -0.0195 0.0026  59  PHE A CD1 
459  C  CD2 . PHE A  59  ? 0.1405 0.2969 0.2148 -0.0084 -0.0186 -0.0108 59  PHE A CD2 
460  C  CE1 . PHE A  59  ? 0.1590 0.3190 0.2428 -0.0190 -0.0046 0.0060  59  PHE A CE1 
461  C  CE2 . PHE A  59  ? 0.1600 0.2755 0.2201 -0.0027 -0.0225 0.0150  59  PHE A CE2 
462  C  CZ  . PHE A  59  ? 0.1661 0.3101 0.2173 -0.0314 -0.0037 0.0221  59  PHE A CZ  
463  N  N   . LEU A  60  ? 0.1582 0.2818 0.2103 -0.0055 -0.0099 0.0055  60  LEU A N   
464  C  CA  . LEU A  60  ? 0.1662 0.2698 0.1911 -0.0367 -0.0495 -0.0344 60  LEU A CA  
465  C  C   . LEU A  60  ? 0.1743 0.2762 0.1540 -0.0083 -0.0462 -0.0353 60  LEU A C   
466  O  O   . LEU A  60  ? 0.1664 0.3044 0.1507 -0.0237 -0.0435 -0.0268 60  LEU A O   
467  C  CB  . LEU A  60  ? 0.1508 0.3006 0.2823 -0.0309 -0.0641 -0.0022 60  LEU A CB  
468  C  CG  . LEU A  60  ? 0.2205 0.3034 0.2590 -0.0383 0.0195  -0.0001 60  LEU A CG  
469  C  CD1 . LEU A  60  ? 0.2916 0.4486 0.2541 -0.0152 0.0307  -0.0797 60  LEU A CD1 
470  C  CD2 . LEU A  60  ? 0.2786 0.3167 0.2833 -0.0479 -0.0449 0.0091  60  LEU A CD2 
471  N  N   . LEU A  61  ? 0.1273 0.2984 0.1629 0.0047  -0.0303 -0.0099 61  LEU A N   
472  C  CA  . LEU A  61  ? 0.1405 0.2746 0.1701 -0.0022 -0.0259 -0.0055 61  LEU A CA  
473  C  C   . LEU A  61  ? 0.1587 0.2949 0.1481 -0.0200 -0.0326 -0.0343 61  LEU A C   
474  O  O   . LEU A  61  ? 0.1838 0.2967 0.1565 -0.0159 -0.0310 -0.0409 61  LEU A O   
475  C  CB  . LEU A  61  ? 0.1650 0.3164 0.1912 -0.0094 -0.0425 0.0318  61  LEU A CB  
476  C  CG  . LEU A  61  ? 0.1817 0.3290 0.1913 -0.0400 -0.0043 0.0272  61  LEU A CG  
477  C  CD1 . LEU A  61  ? 0.1791 0.2601 0.2201 -0.0026 -0.0138 0.0019  61  LEU A CD1 
478  C  CD2 . LEU A  61  ? 0.1988 0.3309 0.3036 0.0250  0.0348  0.0987  61  LEU A CD2 
479  N  N   A THR A  62  ? 0.1520 0.2286 0.1561 -0.0173 -0.0122 -0.0157 62  THR A N   
480  N  N   B THR A  62  ? 0.1525 0.2369 0.1613 -0.0155 -0.0144 -0.0190 62  THR A N   
481  C  CA  A THR A  62  ? 0.1818 0.2399 0.1491 -0.0017 -0.0179 -0.0251 62  THR A CA  
482  C  CA  B THR A  62  ? 0.1763 0.2437 0.1767 -0.0027 -0.0134 -0.0324 62  THR A CA  
483  C  C   A THR A  62  ? 0.1735 0.2049 0.1586 -0.0008 -0.0675 -0.0071 62  THR A C   
484  C  C   B THR A  62  ? 0.1749 0.3026 0.1836 0.0195  -0.0184 -0.0212 62  THR A C   
485  O  O   A THR A  62  ? 0.1766 0.2258 0.1535 -0.0367 -0.0278 -0.0177 62  THR A O   
486  O  O   B THR A  62  ? 0.1863 0.2395 0.1698 -0.0004 -0.0009 -0.0006 62  THR A O   
487  C  CB  A THR A  62  ? 0.1819 0.2130 0.2744 -0.0264 0.0248  -0.0024 62  THR A CB  
488  C  CB  B THR A  62  ? 0.2441 0.2700 0.2358 -0.0283 0.0269  -0.0226 62  THR A CB  
489  O  OG1 A THR A  62  ? 0.1865 0.2922 0.2807 -0.0560 0.0122  -0.0089 62  THR A OG1 
490  O  OG1 B THR A  62  ? 0.2107 0.3497 0.2076 0.0447  -0.0091 -0.0085 62  THR A OG1 
491  C  CG2 A THR A  62  ? 0.2638 0.2034 0.3468 0.0368  0.0610  0.0781  62  THR A CG2 
492  C  CG2 B THR A  62  ? 0.2422 0.2849 0.3827 0.0406  -0.0519 -0.1017 62  THR A CG2 
493  N  N   . ASN A  63  ? 0.1742 0.2619 0.1730 -0.0004 -0.0141 -0.0182 63  ASN A N   
494  C  CA  . ASN A  63  ? 0.1752 0.2228 0.1833 -0.0326 0.0042  -0.0120 63  ASN A CA  
495  C  C   . ASN A  63  ? 0.2079 0.2231 0.1757 -0.0454 -0.0177 -0.0183 63  ASN A C   
496  O  O   . ASN A  63  ? 0.1805 0.2443 0.2291 -0.0368 -0.0296 -0.0261 63  ASN A O   
497  C  CB  . ASN A  63  ? 0.1688 0.2801 0.1612 -0.0029 -0.0173 -0.0657 63  ASN A CB  
498  C  CG  . ASN A  63  ? 0.1602 0.2019 0.1932 -0.0447 -0.0119 -0.0239 63  ASN A CG  
499  O  OD1 . ASN A  63  ? 0.1935 0.2348 0.1952 -0.0135 0.0122  -0.0176 63  ASN A OD1 
500  N  ND2 . ASN A  63  ? 0.1984 0.2314 0.1897 -0.0403 0.0152  -0.0348 63  ASN A ND2 
501  N  N   . ASN A  64  ? 0.2031 0.2308 0.1786 -0.0407 -0.0061 -0.0010 64  ASN A N   
502  C  CA  . ASN A  64  ? 0.2120 0.1996 0.2228 -0.0240 -0.0072 0.0188  64  ASN A CA  
503  C  C   . ASN A  64  ? 0.2342 0.1989 0.2099 -0.0297 -0.0154 -0.0236 64  ASN A C   
504  O  O   . ASN A  64  ? 0.2192 0.2487 0.2735 -0.0097 -0.0422 0.0006  64  ASN A O   
505  C  CB  . ASN A  64  ? 0.2477 0.2185 0.2148 -0.0469 -0.0083 -0.0299 64  ASN A CB  
506  C  CG  . ASN A  64  ? 0.1917 0.2498 0.2188 -0.0675 -0.0317 -0.0047 64  ASN A CG  
507  O  OD1 . ASN A  64  ? 0.2026 0.2141 0.1917 -0.0284 -0.0138 -0.0032 64  ASN A OD1 
508  N  ND2 . ASN A  64  ? 0.3271 0.3261 0.1995 -0.0567 0.0037  0.0026  64  ASN A ND2 
509  N  N   . GLY A  65  ? 0.1949 0.2219 0.1975 -0.0138 -0.0283 -0.0329 65  GLY A N   
510  C  CA  . GLY A  65  ? 0.1791 0.2539 0.2588 -0.0351 -0.0011 -0.0337 65  GLY A CA  
511  C  C   . GLY A  65  ? 0.1694 0.2394 0.2458 -0.0017 -0.0163 -0.0367 65  GLY A C   
512  O  O   . GLY A  65  ? 0.2031 0.4016 0.2551 0.0063  -0.0179 -0.0658 65  GLY A O   
513  N  N   . HIS A  66  ? 0.1766 0.1989 0.2095 0.0018  -0.0281 0.0035  66  HIS A N   
514  C  CA  . HIS A  66  ? 0.1368 0.2072 0.2058 0.0105  -0.0220 0.0275  66  HIS A CA  
515  C  C   . HIS A  66  ? 0.1615 0.1757 0.1978 -0.0119 0.0025  0.0177  66  HIS A C   
516  O  O   . HIS A  66  ? 0.1898 0.1938 0.2702 -0.0376 -0.0305 0.0200  66  HIS A O   
517  C  CB  . HIS A  66  ? 0.2694 0.1772 0.1877 -0.0311 -0.0362 0.0027  66  HIS A CB  
518  C  CG  . HIS A  66  ? 0.2709 0.2159 0.2002 0.0070  -0.0688 0.0041  66  HIS A CG  
519  N  ND1 . HIS A  66  ? 0.2893 0.2242 0.2190 -0.0058 -0.0473 0.0193  66  HIS A ND1 
520  C  CD2 . HIS A  66  ? 0.2716 0.2132 0.2455 0.0025  -0.0621 -0.0160 66  HIS A CD2 
521  C  CE1 . HIS A  66  ? 0.2447 0.1967 0.2251 0.0212  -0.0519 0.0135  66  HIS A CE1 
522  N  NE2 . HIS A  66  ? 0.2433 0.2303 0.2443 0.0212  -0.0436 -0.0171 66  HIS A NE2 
523  N  N   . SER A  67  ? 0.1591 0.1932 0.1782 -0.0108 -0.0175 -0.0151 67  SER A N   
524  C  CA  . SER A  67  ? 0.1406 0.1881 0.1649 -0.0081 -0.0149 0.0100  67  SER A CA  
525  C  C   . SER A  67  ? 0.1542 0.1833 0.1646 -0.0064 -0.0087 -0.0226 67  SER A C   
526  O  O   . SER A  67  ? 0.1816 0.2065 0.1946 -0.0212 -0.0283 -0.0139 67  SER A O   
527  C  CB  . SER A  67  ? 0.1807 0.1907 0.1674 -0.0376 -0.0003 -0.0016 67  SER A CB  
528  O  OG  . SER A  67  ? 0.1620 0.1982 0.1726 0.0004  -0.0193 -0.0097 67  SER A OG  
529  N  N   . VAL A  68  ? 0.1524 0.1780 0.1726 -0.0077 -0.0005 -0.0103 68  VAL A N   
530  C  CA  . VAL A  68  ? 0.1333 0.2095 0.1388 -0.0322 -0.0078 0.0043  68  VAL A CA  
531  C  C   . VAL A  68  ? 0.1459 0.1955 0.1522 -0.0179 0.0008  -0.0154 68  VAL A C   
532  O  O   . VAL A  68  ? 0.1656 0.2202 0.1455 -0.0012 0.0020  0.0062  68  VAL A O   
533  C  CB  . VAL A  68  ? 0.1583 0.2532 0.1562 -0.0138 0.0141  0.0290  68  VAL A CB  
534  C  CG1 . VAL A  68  ? 0.2309 0.2451 0.1825 0.0012  0.0055  0.0083  68  VAL A CG1 
535  C  CG2 . VAL A  68  ? 0.1703 0.3679 0.1976 -0.0043 -0.0376 0.0381  68  VAL A CG2 
536  N  N   A LYS A  69  ? 0.1568 0.2485 0.1491 -0.0234 -0.0170 -0.0320 69  LYS A N   
537  N  N   B LYS A  69  ? 0.1096 0.2230 0.1692 -0.0018 -0.0073 0.0167  69  LYS A N   
538  C  CA  A LYS A  69  ? 0.1342 0.2244 0.1721 -0.0006 -0.0127 0.0077  69  LYS A CA  
539  C  CA  B LYS A  69  ? 0.1209 0.1920 0.1369 0.0060  -0.0218 0.0205  69  LYS A CA  
540  C  C   A LYS A  69  ? 0.1251 0.2130 0.1389 -0.0188 -0.0144 -0.0279 69  LYS A C   
541  C  C   B LYS A  69  ? 0.1240 0.2006 0.1710 -0.0088 -0.0477 -0.0193 69  LYS A C   
542  O  O   A LYS A  69  ? 0.1479 0.2163 0.1538 0.0107  -0.0341 -0.0165 69  LYS A O   
543  O  O   B LYS A  69  ? 0.1817 0.2394 0.1711 0.0009  -0.0230 -0.0348 69  LYS A O   
544  C  CB  A LYS A  69  ? 0.1949 0.1976 0.2640 0.0046  -0.0405 0.0119  69  LYS A CB  
545  C  CB  B LYS A  69  ? 0.1071 0.1879 0.1573 0.0055  -0.0194 -0.0062 69  LYS A CB  
546  C  CG  A LYS A  69  ? 0.2035 0.2070 0.3348 -0.0098 -0.0859 -0.0040 69  LYS A CG  
547  C  CG  B LYS A  69  ? 0.1381 0.2500 0.1211 0.0048  -0.0263 0.0392  69  LYS A CG  
548  C  CD  A LYS A  69  ? 0.2865 0.2619 0.3756 -0.0287 -0.0159 0.0508  69  LYS A CD  
549  C  CD  B LYS A  69  ? 0.1736 0.2130 0.2118 0.0015  -0.0339 0.0366  69  LYS A CD  
550  C  CE  A LYS A  69  ? 0.5056 0.3032 0.4957 -0.0869 0.0151  0.0502  69  LYS A CE  
551  C  CE  B LYS A  69  ? 0.2367 0.2435 0.2680 0.0063  -0.0446 0.0281  69  LYS A CE  
552  N  NZ  A LYS A  69  ? 0.4578 0.3561 0.4515 -0.0210 -0.0389 0.0882  69  LYS A NZ  
553  N  NZ  B LYS A  69  ? 0.2925 0.2112 0.2291 -0.0372 -0.0063 0.0187  69  LYS A NZ  
554  N  N   . LEU A  70  ? 0.1064 0.2031 0.1423 -0.0106 -0.0216 -0.0103 70  LEU A N   
555  C  CA  . LEU A  70  ? 0.1161 0.2005 0.1369 -0.0050 -0.0198 -0.0001 70  LEU A CA  
556  C  C   . LEU A  70  ? 0.1122 0.2114 0.1231 -0.0199 -0.0135 -0.0089 70  LEU A C   
557  O  O   . LEU A  70  ? 0.1252 0.2120 0.1496 -0.0092 -0.0216 -0.0033 70  LEU A O   
558  C  CB  . LEU A  70  ? 0.1149 0.2080 0.1672 -0.0071 -0.0073 0.0244  70  LEU A CB  
559  C  CG  . LEU A  70  ? 0.1226 0.2359 0.1668 0.0117  -0.0302 0.0198  70  LEU A CG  
560  C  CD1 . LEU A  70  ? 0.1368 0.2824 0.1923 0.0006  -0.0446 0.0188  70  LEU A CD1 
561  C  CD2 . LEU A  70  ? 0.1798 0.2330 0.2161 0.0337  -0.0092 0.0283  70  LEU A CD2 
562  N  N   . ASN A  71  ? 0.1442 0.1850 0.1579 -0.0150 -0.0040 -0.0072 71  ASN A N   
563  C  CA  . ASN A  71  ? 0.1258 0.2008 0.1542 -0.0129 -0.0162 0.0109  71  ASN A CA  
564  C  C   . ASN A  71  ? 0.1218 0.2201 0.1569 -0.0085 -0.0102 0.0104  71  ASN A C   
565  O  O   . ASN A  71  ? 0.1556 0.2718 0.1747 0.0164  -0.0267 0.0335  71  ASN A O   
566  C  CB  . ASN A  71  ? 0.1877 0.2270 0.1873 -0.0475 -0.0140 -0.0050 71  ASN A CB  
567  C  CG  . ASN A  71  ? 0.2432 0.2515 0.2808 -0.0627 -0.0307 -0.0259 71  ASN A CG  
568  O  OD1 . ASN A  71  ? 0.2548 0.3650 0.3164 0.0012  -0.0189 -0.0625 71  ASN A OD1 
569  N  ND2 . ASN A  71  ? 0.3209 0.2838 0.4133 -0.0367 0.0003  -0.0535 71  ASN A ND2 
570  N  N   . LEU A  72  ? 0.1432 0.2091 0.1414 -0.0285 -0.0044 0.0059  72  LEU A N   
571  C  CA  . LEU A  72  ? 0.1139 0.2276 0.1630 -0.0065 0.0000  0.0032  72  LEU A CA  
572  C  C   . LEU A  72  ? 0.1567 0.1967 0.1772 -0.0086 -0.0122 0.0203  72  LEU A C   
573  O  O   . LEU A  72  ? 0.1571 0.2186 0.2065 -0.0157 0.0103  0.0237  72  LEU A O   
574  C  CB  . LEU A  72  ? 0.1238 0.1966 0.1626 -0.0178 -0.0214 0.0013  72  LEU A CB  
575  C  CG  . LEU A  72  ? 0.1379 0.1975 0.1384 0.0106  -0.0087 0.0153  72  LEU A CG  
576  C  CD1 . LEU A  72  ? 0.1112 0.2219 0.1860 0.0109  -0.0148 0.0037  72  LEU A CD1 
577  C  CD2 . LEU A  72  ? 0.1610 0.2135 0.2089 -0.0162 -0.0146 0.0599  72  LEU A CD2 
578  N  N   . PRO A  73  ? 0.1446 0.2147 0.1896 -0.0084 0.0071  0.0257  73  PRO A N   
579  C  CA  . PRO A  73  ? 0.1289 0.2634 0.2043 0.0003  0.0110  0.0344  73  PRO A CA  
580  C  C   . PRO A  73  ? 0.1728 0.2277 0.2207 0.0027  0.0216  0.0181  73  PRO A C   
581  O  O   . PRO A  73  ? 0.1269 0.2402 0.2138 0.0223  0.0070  0.0175  73  PRO A O   
582  C  CB  . PRO A  73  ? 0.1606 0.2625 0.2020 0.0042  -0.0008 0.0377  73  PRO A CB  
583  C  CG  . PRO A  73  ? 0.1236 0.2622 0.2151 0.0217  0.0032  0.0383  73  PRO A CG  
584  C  CD  . PRO A  73  ? 0.1170 0.2317 0.2189 0.0042  -0.0071 0.0422  73  PRO A CD  
585  N  N   . SER A  74  ? 0.1807 0.2740 0.2034 -0.0114 0.0190  0.0282  74  SER A N   
586  C  CA  . SER A  74  ? 0.2649 0.2730 0.2001 0.0446  0.0345  0.0345  74  SER A CA  
587  C  C   . SER A  74  ? 0.1949 0.2733 0.1749 0.0106  0.0011  0.0335  74  SER A C   
588  O  O   . SER A  74  ? 0.2110 0.3670 0.1954 0.0232  0.0051  0.0305  74  SER A O   
589  C  CB  . SER A  74  ? 0.3169 0.3606 0.3439 -0.0149 0.0203  0.1208  74  SER A CB  
590  O  OG  . SER A  74  ? 0.3603 0.4264 0.2599 -0.0691 0.0436  0.0788  74  SER A OG  
591  N  N   . ASP A  75  ? 0.1535 0.2845 0.1874 0.0208  -0.0024 0.0047  75  ASP A N   
592  C  CA  . ASP A  75  ? 0.1536 0.2953 0.2818 0.0244  -0.0442 -0.0351 75  ASP A CA  
593  C  C   . ASP A  75  ? 0.1430 0.2675 0.2113 0.0100  0.0117  -0.0102 75  ASP A C   
594  O  O   . ASP A  75  ? 0.1150 0.3385 0.3086 0.0012  0.0129  -0.0646 75  ASP A O   
595  C  CB  . ASP A  75  ? 0.1581 0.3707 0.2664 0.0298  -0.0408 -0.0008 75  ASP A CB  
596  C  CG  . ASP A  75  ? 0.2026 0.3362 0.3005 0.0732  -0.0743 -0.0226 75  ASP A CG  
597  O  OD1 . ASP A  75  ? 0.2949 0.4842 0.2705 0.1282  -0.0531 -0.0131 75  ASP A OD1 
598  O  OD2 . ASP A  75  ? 0.2470 0.4199 0.3517 0.0209  0.0402  0.0195  75  ASP A OD2 
599  N  N   . MET A  76  ? 0.1480 0.2715 0.1711 0.0221  -0.0160 0.0439  76  MET A N   
600  C  CA  . MET A  76  ? 0.1535 0.2450 0.1388 0.0255  0.0124  0.0484  76  MET A CA  
601  C  C   . MET A  76  ? 0.1159 0.2019 0.1676 0.0006  0.0190  0.0326  76  MET A C   
602  O  O   . MET A  76  ? 0.1354 0.2113 0.1881 0.0158  0.0051  0.0215  76  MET A O   
603  C  CB  . MET A  76  ? 0.1504 0.2860 0.1922 -0.0088 0.0122  0.0646  76  MET A CB  
604  C  CG  . MET A  76  ? 0.1618 0.2250 0.1898 0.0128  0.0185  0.0304  76  MET A CG  
605  S  SD  . MET A  76  ? 0.1507 0.2357 0.2103 -0.0025 0.0302  0.0347  76  MET A SD  
606  C  CE  . MET A  76  ? 0.1745 0.1940 0.2045 -0.0288 0.0392  0.0049  76  MET A CE  
607  N  N   . HIS A  77  ? 0.1240 0.2120 0.1565 -0.0107 -0.0057 0.0374  77  HIS A N   
608  C  CA  . HIS A  77  ? 0.1391 0.2251 0.1626 -0.0208 -0.0059 0.0482  77  HIS A CA  
609  C  C   . HIS A  77  ? 0.1470 0.1657 0.1723 0.0152  0.0134  0.0342  77  HIS A C   
610  O  O   . HIS A  77  ? 0.1476 0.1996 0.2008 0.0172  0.0008  0.0335  77  HIS A O   
611  C  CB  . HIS A  77  ? 0.1775 0.2043 0.1978 -0.0104 0.0356  0.0369  77  HIS A CB  
612  C  CG  . HIS A  77  ? 0.1752 0.2645 0.1909 0.0197  0.0172  0.0545  77  HIS A CG  
613  N  ND1 . HIS A  77  ? 0.1846 0.3620 0.2117 -0.0212 0.0211  0.0520  77  HIS A ND1 
614  C  CD2 . HIS A  77  ? 0.1824 0.3267 0.2220 0.0162  0.0425  0.0314  77  HIS A CD2 
615  C  CE1 . HIS A  77  ? 0.1738 0.3330 0.1990 -0.0104 0.0310  0.0544  77  HIS A CE1 
616  N  NE2 . HIS A  77  ? 0.1672 0.2952 0.2931 -0.0111 0.0515  0.0315  77  HIS A NE2 
617  N  N   . ILE A  78  ? 0.1582 0.1976 0.1694 0.0054  -0.0086 0.0205  78  ILE A N   
618  C  CA  . ILE A  78  ? 0.1818 0.1996 0.1720 0.0151  0.0131  0.0040  78  ILE A CA  
619  C  C   . ILE A  78  ? 0.1784 0.2256 0.1587 0.0305  -0.0055 0.0200  78  ILE A C   
620  O  O   . ILE A  78  ? 0.1886 0.2620 0.1982 0.0049  -0.0001 0.0512  78  ILE A O   
621  C  CB  . ILE A  78  ? 0.1522 0.2623 0.1746 -0.0364 0.0080  -0.0280 78  ILE A CB  
622  C  CG1 . ILE A  78  ? 0.1852 0.2928 0.1662 -0.0491 0.0082  0.0128  78  ILE A CG1 
623  C  CG2 . ILE A  78  ? 0.2244 0.2816 0.2129 0.0133  -0.0208 -0.0361 78  ILE A CG2 
624  C  CD1 . ILE A  78  ? 0.1503 0.2662 0.2558 -0.0084 0.0039  0.0023  78  ILE A CD1 
625  N  N   . GLN A  79  ? 0.1881 0.2168 0.1966 0.0097  0.0280  0.0080  79  GLN A N   
626  C  CA  . GLN A  79  ? 0.1957 0.2956 0.2152 0.0295  0.0231  0.0081  79  GLN A CA  
627  C  C   . GLN A  79  ? 0.1958 0.2784 0.2207 0.0411  0.0144  -0.0209 79  GLN A C   
628  O  O   . GLN A  79  ? 0.2172 0.3058 0.2320 -0.0011 0.0060  -0.0050 79  GLN A O   
629  C  CB  . GLN A  79  ? 0.2182 0.3151 0.3418 0.0447  0.0003  -0.0259 79  GLN A CB  
630  C  CG  . GLN A  79  ? 0.2480 0.4352 0.4175 -0.0140 0.0800  -0.1119 79  GLN A CG  
631  C  CD  . GLN A  79  ? 0.3560 0.6547 0.5493 0.1102  0.1613  0.0227  79  GLN A CD  
632  O  OE1 . GLN A  79  ? 0.7959 1.2882 0.5845 -0.3622 0.2554  0.1272  79  GLN A OE1 
633  N  NE2 . GLN A  79  ? 0.4897 0.6876 0.7069 0.1571  0.0558  0.1350  79  GLN A NE2 
634  N  N   . GLY A  80  ? 0.3019 0.3151 0.1838 -0.0104 0.0340  -0.0040 80  GLY A N   
635  C  CA  . GLY A  80  ? 0.2443 0.3695 0.2536 -0.0044 0.0091  -0.0127 80  GLY A CA  
636  C  C   . GLY A  80  ? 0.2480 0.3063 0.2196 -0.0443 0.0524  -0.0379 80  GLY A C   
637  O  O   . GLY A  80  ? 0.3170 0.4011 0.2393 -0.0784 -0.0155 -0.0806 80  GLY A O   
638  N  N   . LEU A  81  ? 0.2459 0.2322 0.2010 -0.0357 -0.0175 0.0151  81  LEU A N   
639  C  CA  . LEU A  81  ? 0.2564 0.2869 0.2656 -0.0630 -0.0275 0.0776  81  LEU A CA  
640  C  C   . LEU A  81  ? 0.2965 0.3079 0.2476 -0.1456 -0.0555 0.0398  81  LEU A C   
641  O  O   . LEU A  81  ? 0.3725 0.3852 0.2238 -0.0939 0.0389  0.0160  81  LEU A O   
642  C  CB  . LEU A  81  ? 0.1988 0.2655 0.2776 -0.0329 -0.0340 0.0684  81  LEU A CB  
643  C  CG  . LEU A  81  ? 0.2136 0.2394 0.2771 -0.0625 -0.0422 0.0487  81  LEU A CG  
644  C  CD1 . LEU A  81  ? 0.2463 0.2661 0.2894 -0.0472 -0.0033 -0.0227 81  LEU A CD1 
645  C  CD2 . LEU A  81  ? 0.1913 0.2800 0.3625 -0.0403 -0.0872 0.0456  81  LEU A CD2 
646  N  N   . GLN A  82  ? 0.4065 0.4418 0.2229 -0.1896 -0.1014 0.1221  82  GLN A N   
647  C  CA  . GLN A  82  ? 0.4709 0.4994 0.2065 -0.2362 -0.0556 0.0807  82  GLN A CA  
648  C  C   . GLN A  82  ? 0.4231 0.4558 0.2063 -0.2220 0.0469  0.0653  82  GLN A C   
649  O  O   . GLN A  82  ? 0.4271 0.4216 0.2360 -0.1690 0.0168  -0.0242 82  GLN A O   
650  C  CB  . GLN A  82  ? 0.7048 0.5448 0.3605 -0.3543 -0.3499 0.2660  82  GLN A CB  
651  C  CG  . GLN A  82  ? 0.8414 0.7849 0.6635 -0.1762 -0.3371 -0.0634 82  GLN A CG  
652  C  CD  . GLN A  82  ? 1.0833 0.8259 0.8667 -0.1345 -0.1923 0.0917  82  GLN A CD  
653  O  OE1 . GLN A  82  ? 0.8686 0.7926 0.3813 -0.1078 -0.2545 0.1155  82  GLN A OE1 
654  N  NE2 . GLN A  82  ? 0.9215 0.5470 0.8465 0.0060  -0.6393 0.0775  82  GLN A NE2 
655  N  N   . SER A  83  ? 0.2177 0.3251 0.1814 -0.0694 -0.0231 0.0541  83  SER A N   
656  C  CA  . SER A  83  ? 0.1771 0.2840 0.1610 -0.0326 -0.0454 0.0379  83  SER A CA  
657  C  C   . SER A  83  ? 0.1655 0.2723 0.1374 -0.0455 -0.0157 0.0273  83  SER A C   
658  O  O   . SER A  83  ? 0.1460 0.2461 0.1692 -0.0266 -0.0150 0.0491  83  SER A O   
659  C  CB  . SER A  83  ? 0.1855 0.2762 0.1830 -0.0348 -0.0359 0.0577  83  SER A CB  
660  O  OG  . SER A  83  ? 0.2694 0.2894 0.1890 -0.0025 -0.0444 0.0572  83  SER A OG  
661  N  N   . ARG A  84  ? 0.1359 0.2785 0.1444 -0.0120 -0.0315 0.0264  84  ARG A N   
662  C  CA  . ARG A  84  ? 0.1228 0.2265 0.1438 -0.0024 -0.0188 0.0074  84  ARG A CA  
663  C  C   . ARG A  84  ? 0.1295 0.2126 0.1612 -0.0049 -0.0172 0.0425  84  ARG A C   
664  O  O   . ARG A  84  ? 0.1213 0.2072 0.1738 -0.0125 -0.0041 0.0413  84  ARG A O   
665  C  CB  . ARG A  84  ? 0.1186 0.2722 0.1566 -0.0152 -0.0221 0.0552  84  ARG A CB  
666  C  CG  . ARG A  84  ? 0.1143 0.2610 0.1495 -0.0095 -0.0217 0.0487  84  ARG A CG  
667  C  CD  . ARG A  84  ? 0.1054 0.2531 0.2027 0.0147  -0.0326 0.0190  84  ARG A CD  
668  N  NE  . ARG A  84  ? 0.1327 0.2277 0.1819 0.0069  -0.0092 0.0527  84  ARG A NE  
669  C  CZ  . ARG A  84  ? 0.1385 0.2288 0.1595 0.0048  -0.0163 0.0255  84  ARG A CZ  
670  N  NH1 . ARG A  84  ? 0.1488 0.2621 0.2065 -0.0049 -0.0181 0.0241  84  ARG A NH1 
671  N  NH2 . ARG A  84  ? 0.1650 0.2472 0.2270 0.0054  0.0322  0.0094  84  ARG A NH2 
672  N  N   . TYR A  85  ? 0.1071 0.2253 0.1470 -0.0156 -0.0129 0.0332  85  TYR A N   
673  C  CA  . TYR A  85  ? 0.1010 0.2168 0.1476 0.0026  -0.0134 0.0278  85  TYR A CA  
674  C  C   . TYR A  85  ? 0.1023 0.1730 0.1710 -0.0074 0.0006  0.0284  85  TYR A C   
675  O  O   . TYR A  85  ? 0.1661 0.1762 0.1654 -0.0226 -0.0376 0.0337  85  TYR A O   
676  C  CB  . TYR A  85  ? 0.1064 0.2095 0.1499 -0.0164 -0.0108 0.0358  85  TYR A CB  
677  C  CG  . TYR A  85  ? 0.0933 0.2096 0.1546 -0.0201 -0.0127 0.0289  85  TYR A CG  
678  C  CD1 . TYR A  85  ? 0.1542 0.2496 0.1684 -0.0403 -0.0265 0.0337  85  TYR A CD1 
679  C  CD2 . TYR A  85  ? 0.1299 0.1828 0.1670 -0.0359 0.0053  0.0432  85  TYR A CD2 
680  C  CE1 . TYR A  85  ? 0.1412 0.2356 0.1772 -0.0270 -0.0258 0.0139  85  TYR A CE1 
681  C  CE2 . TYR A  85  ? 0.1489 0.2099 0.1574 -0.0477 -0.0044 0.0601  85  TYR A CE2 
682  C  CZ  . TYR A  85  ? 0.1463 0.2173 0.1907 -0.0289 -0.0270 0.0562  85  TYR A CZ  
683  O  OH  . TYR A  85  ? 0.2029 0.3273 0.2068 0.0267  -0.0511 0.0602  85  TYR A OH  
684  N  N   . SER A  86  ? 0.1215 0.1943 0.1458 -0.0109 -0.0016 0.0221  86  SER A N   
685  C  CA  . SER A  86  ? 0.0971 0.2188 0.1341 -0.0140 -0.0082 0.0182  86  SER A CA  
686  C  C   . SER A  86  ? 0.1116 0.1692 0.1452 -0.0077 0.0002  0.0189  86  SER A C   
687  O  O   . SER A  86  ? 0.1107 0.1567 0.1641 -0.0114 0.0031  0.0280  86  SER A O   
688  C  CB  . SER A  86  ? 0.1247 0.2346 0.1606 -0.0291 0.0231  0.0376  86  SER A CB  
689  O  OG  . SER A  86  ? 0.1104 0.2886 0.1647 -0.0121 0.0066  0.0644  86  SER A OG  
690  N  N   . ALA A  87  ? 0.1200 0.1938 0.1434 -0.0001 -0.0008 0.0321  87  ALA A N   
691  C  CA  . ALA A  87  ? 0.1442 0.1612 0.1394 -0.0053 0.0177  0.0142  87  ALA A CA  
692  C  C   . ALA A  87  ? 0.1161 0.1750 0.1596 -0.0072 -0.0016 0.0012  87  ALA A C   
693  O  O   . ALA A  87  ? 0.1179 0.2191 0.1932 -0.0205 -0.0017 0.0055  87  ALA A O   
694  C  CB  . ALA A  87  ? 0.1682 0.1907 0.1713 0.0091  0.0053  0.0440  87  ALA A CB  
695  N  N   . THR A  88  ? 0.1229 0.1682 0.1602 -0.0024 0.0171  0.0185  88  THR A N   
696  C  CA  . THR A  88  ? 0.1062 0.1821 0.1575 -0.0077 0.0155  0.0162  88  THR A CA  
697  C  C   . THR A  88  ? 0.1087 0.1397 0.1502 -0.0003 -0.0083 0.0089  88  THR A C   
698  O  O   . THR A  88  ? 0.1339 0.1712 0.1597 -0.0330 -0.0159 0.0098  88  THR A O   
699  C  CB  . THR A  88  ? 0.1567 0.1581 0.1685 -0.0228 -0.0140 -0.0006 88  THR A CB  
700  O  OG1 . THR A  88  ? 0.1878 0.1873 0.1873 -0.0155 -0.0157 -0.0069 88  THR A OG1 
701  C  CG2 . THR A  88  ? 0.1336 0.1741 0.1877 -0.0038 -0.0066 0.0236  88  THR A CG2 
702  N  N   . GLN A  89  ? 0.1095 0.1644 0.1467 -0.0130 0.0026  0.0214  89  GLN A N   
703  C  CA  . GLN A  89  ? 0.1213 0.1371 0.1527 -0.0214 0.0061  0.0085  89  GLN A CA  
704  C  C   . GLN A  89  ? 0.1168 0.1439 0.1394 0.0010  -0.0144 0.0104  89  GLN A C   
705  O  O   . GLN A  89  ? 0.1145 0.1676 0.1382 -0.0058 -0.0135 0.0055  89  GLN A O   
706  C  CB  . GLN A  89  ? 0.1284 0.1863 0.1618 0.0079  -0.0288 -0.0036 89  GLN A CB  
707  C  CG  . GLN A  89  ? 0.1230 0.2379 0.2122 0.0376  0.0149  0.0310  89  GLN A CG  
708  C  CD  . GLN A  89  ? 0.1470 0.1868 0.2026 -0.0139 -0.0351 0.0359  89  GLN A CD  
709  O  OE1 . GLN A  89  ? 0.1454 0.2132 0.1800 -0.0346 -0.0156 0.0111  89  GLN A OE1 
710  N  NE2 . GLN A  89  ? 0.1661 0.2359 0.3067 0.0189  -0.0254 -0.0435 89  GLN A NE2 
711  N  N   . LEU A  90  ? 0.0996 0.1575 0.1518 -0.0070 -0.0020 0.0204  90  LEU A N   
712  C  CA  . LEU A  90  ? 0.0987 0.1446 0.1346 -0.0033 0.0035  0.0232  90  LEU A CA  
713  C  C   . LEU A  90  ? 0.1200 0.1430 0.1307 -0.0100 -0.0134 0.0096  90  LEU A C   
714  O  O   . LEU A  90  ? 0.1123 0.1581 0.1279 -0.0006 -0.0086 0.0081  90  LEU A O   
715  C  CB  . LEU A  90  ? 0.1146 0.1538 0.1508 0.0051  -0.0198 0.0156  90  LEU A CB  
716  C  CG  . LEU A  90  ? 0.1203 0.1617 0.1481 -0.0012 -0.0109 0.0089  90  LEU A CG  
717  C  CD1 . LEU A  90  ? 0.1382 0.2037 0.1512 -0.0189 -0.0149 0.0380  90  LEU A CD1 
718  C  CD2 . LEU A  90  ? 0.1367 0.1767 0.2026 0.0397  0.0004  0.0332  90  LEU A CD2 
719  N  N   . HIS A  91  ? 0.1132 0.1513 0.1342 -0.0002 -0.0078 0.0251  91  HIS A N   
720  C  CA  . HIS A  91  ? 0.1046 0.1287 0.1366 -0.0039 0.0035  0.0055  91  HIS A CA  
721  C  C   . HIS A  91  ? 0.0944 0.1437 0.1211 0.0018  -0.0120 -0.0051 91  HIS A C   
722  O  O   . HIS A  91  ? 0.1084 0.1403 0.1233 0.0002  -0.0062 0.0038  91  HIS A O   
723  C  CB  . HIS A  91  ? 0.1254 0.1411 0.1279 -0.0132 -0.0240 0.0096  91  HIS A CB  
724  C  CG  . HIS A  91  ? 0.1098 0.1420 0.1109 0.0033  -0.0132 0.0030  91  HIS A CG  
725  N  ND1 . HIS A  91  ? 0.1159 0.1394 0.1247 -0.0107 -0.0166 0.0173  91  HIS A ND1 
726  C  CD2 . HIS A  91  ? 0.1060 0.1420 0.1158 0.0159  -0.0276 0.0067  91  HIS A CD2 
727  C  CE1 . HIS A  91  ? 0.0921 0.1439 0.1344 -0.0048 -0.0021 0.0137  91  HIS A CE1 
728  N  NE2 . HIS A  91  ? 0.0871 0.1222 0.1340 0.0021  -0.0176 0.0198  91  HIS A NE2 
729  N  N   . LEU A  92  ? 0.1025 0.1595 0.1306 -0.0110 0.0003  0.0081  92  LEU A N   
730  C  CA  . LEU A  92  ? 0.1078 0.1240 0.1262 0.0084  -0.0105 0.0173  92  LEU A CA  
731  C  C   . LEU A  92  ? 0.1152 0.1095 0.1210 0.0052  0.0032  0.0122  92  LEU A C   
732  O  O   . LEU A  92  ? 0.1061 0.1361 0.1418 -0.0006 -0.0018 -0.0072 92  LEU A O   
733  C  CB  . LEU A  92  ? 0.1254 0.1701 0.1780 0.0181  0.0111  0.0499  92  LEU A CB  
734  C  CG  . LEU A  92  ? 0.1469 0.1418 0.1289 0.0297  -0.0044 0.0293  92  LEU A CG  
735  C  CD1 . LEU A  92  ? 0.2113 0.3154 0.2948 0.0620  -0.1150 -0.0197 92  LEU A CD1 
736  C  CD2 . LEU A  92  ? 0.1998 0.1476 0.2961 0.0141  0.0156  -0.0201 92  LEU A CD2 
737  N  N   . HIS A  93  ? 0.1093 0.1228 0.1197 0.0000  0.0027  0.0095  93  HIS A N   
738  C  CA  . HIS A  93  ? 0.1028 0.1321 0.1302 -0.0063 0.0049  0.0331  93  HIS A CA  
739  C  C   . HIS A  93  ? 0.1066 0.1078 0.1179 -0.0012 -0.0107 0.0097  93  HIS A C   
740  O  O   . HIS A  93  ? 0.1183 0.1181 0.1346 0.0011  0.0154  0.0109  93  HIS A O   
741  C  CB  . HIS A  93  ? 0.1035 0.1525 0.1266 -0.0082 -0.0091 0.0255  93  HIS A CB  
742  C  CG  . HIS A  93  ? 0.1036 0.1120 0.1277 -0.0043 -0.0119 0.0096  93  HIS A CG  
743  N  ND1 . HIS A  93  ? 0.1156 0.1252 0.1497 0.0057  0.0081  0.0124  93  HIS A ND1 
744  C  CD2 . HIS A  93  ? 0.1044 0.1231 0.1084 -0.0118 -0.0146 0.0143  93  HIS A CD2 
745  C  CE1 . HIS A  93  ? 0.0936 0.1299 0.1307 0.0024  -0.0046 -0.0002 93  HIS A CE1 
746  N  NE2 . HIS A  93  ? 0.0942 0.1226 0.1370 -0.0013 -0.0102 0.0050  93  HIS A NE2 
747  N  N   . TRP A  94  ? 0.1021 0.1353 0.1448 -0.0071 0.0114  0.0249  94  TRP A N   
748  C  CA  . TRP A  94  ? 0.1066 0.1177 0.1435 -0.0066 0.0156  0.0146  94  TRP A CA  
749  C  C   . TRP A  94  ? 0.1368 0.1344 0.1237 0.0021  -0.0046 0.0154  94  TRP A C   
750  O  O   . TRP A  94  ? 0.1159 0.1322 0.1444 -0.0081 0.0178  0.0096  94  TRP A O   
751  C  CB  . TRP A  94  ? 0.1344 0.1387 0.1380 -0.0060 -0.0102 0.0126  94  TRP A CB  
752  C  CG  . TRP A  94  ? 0.1365 0.1263 0.1381 -0.0072 0.0116  0.0126  94  TRP A CG  
753  C  CD1 . TRP A  94  ? 0.1390 0.1650 0.1411 0.0013  0.0099  0.0142  94  TRP A CD1 
754  C  CD2 . TRP A  94  ? 0.1330 0.1421 0.1271 -0.0098 0.0023  0.0236  94  TRP A CD2 
755  N  NE1 . TRP A  94  ? 0.1204 0.1888 0.1408 -0.0133 0.0116  0.0004  94  TRP A NE1 
756  C  CE2 . TRP A  94  ? 0.1224 0.1844 0.1199 -0.0049 -0.0047 0.0077  94  TRP A CE2 
757  C  CE3 . TRP A  94  ? 0.1184 0.1556 0.1302 -0.0066 0.0000  0.0143  94  TRP A CE3 
758  C  CZ2 . TRP A  94  ? 0.1298 0.1832 0.1478 -0.0122 0.0071  0.0113  94  TRP A CZ2 
759  C  CZ3 . TRP A  94  ? 0.1197 0.1515 0.1500 0.0024  -0.0107 0.0167  94  TRP A CZ3 
760  C  CH2 . TRP A  94  ? 0.1190 0.1753 0.1535 0.0080  -0.0049 0.0042  94  TRP A CH2 
761  N  N   . GLY A  95  ? 0.1201 0.1359 0.1332 -0.0024 0.0193  0.0189  95  GLY A N   
762  C  CA  . GLY A  95  ? 0.1116 0.1615 0.1447 0.0075  0.0132  0.0064  95  GLY A CA  
763  C  C   . GLY A  95  ? 0.1374 0.1570 0.1421 -0.0138 0.0211  0.0165  95  GLY A C   
764  O  O   . GLY A  95  ? 0.1261 0.1659 0.1478 -0.0120 0.0195  0.0111  95  GLY A O   
765  N  N   . ASN A  96  ? 0.1321 0.1582 0.1437 0.0042  0.0241  0.0212  96  ASN A N   
766  C  CA  . ASN A  96  ? 0.1659 0.1609 0.1405 -0.0055 0.0344  0.0150  96  ASN A CA  
767  C  C   . ASN A  96  ? 0.1356 0.2078 0.1621 -0.0085 0.0494  0.0113  96  ASN A C   
768  O  O   . ASN A  96  ? 0.1535 0.1724 0.1618 -0.0178 0.0203  0.0179  96  ASN A O   
769  C  CB  . ASN A  96  ? 0.1763 0.1668 0.1962 0.0027  0.0373  0.0105  96  ASN A CB  
770  C  CG  . ASN A  96  ? 0.1657 0.2037 0.2404 0.0258  0.0646  0.0548  96  ASN A CG  
771  O  OD1 . ASN A  96  ? 0.2015 0.2368 0.3221 0.0379  0.1012  0.1105  96  ASN A OD1 
772  N  ND2 . ASN A  96  ? 0.1597 0.2314 0.2600 0.0120  0.0259  0.0124  96  ASN A ND2 
773  N  N   . PRO A  97  ? 0.1518 0.1759 0.1526 -0.0166 0.0186  0.0072  97  PRO A N   
774  C  CA  . PRO A  97  ? 0.1694 0.2126 0.1584 -0.0193 -0.0050 0.0452  97  PRO A CA  
775  C  C   . PRO A  97  ? 0.1902 0.1827 0.1419 -0.0165 0.0260  0.0200  97  PRO A C   
776  O  O   . PRO A  97  ? 0.1751 0.1999 0.2500 -0.0204 0.0143  0.0574  97  PRO A O   
777  C  CB  . PRO A  97  ? 0.2277 0.2192 0.1707 -0.0303 -0.0096 0.0510  97  PRO A CB  
778  C  CG  . PRO A  97  ? 0.2309 0.2317 0.2070 -0.0395 -0.0069 0.0446  97  PRO A CG  
779  C  CD  . PRO A  97  ? 0.1737 0.2204 0.1778 -0.0252 -0.0107 -0.0047 97  PRO A CD  
780  N  N   . ASN A  98  ? 0.1394 0.2131 0.1747 -0.0119 0.0251  0.0226  98  ASN A N   
781  C  CA  . ASN A  98  ? 0.1571 0.2394 0.1913 -0.0012 0.0193  0.0207  98  ASN A CA  
782  C  C   . ASN A  98  ? 0.1444 0.2178 0.2089 -0.0236 -0.0071 0.0204  98  ASN A C   
783  O  O   . ASN A  98  ? 0.1582 0.3328 0.1979 -0.0618 0.0212  0.0177  98  ASN A O   
784  C  CB  . ASN A  98  ? 0.1841 0.2425 0.2266 0.0008  0.0473  0.0212  98  ASN A CB  
785  C  CG  . ASN A  98  ? 0.3637 0.3499 0.2602 0.0888  0.0618  0.0078  98  ASN A CG  
786  O  OD1 . ASN A  98  ? 0.4717 0.5072 0.2522 0.0965  0.0662  0.0861  98  ASN A OD1 
787  N  ND2 . ASN A  98  ? 0.6407 0.4156 0.3225 0.0775  0.0831  -0.0929 98  ASN A ND2 
788  N  N   . ASP A  99  ? 0.1588 0.2133 0.1644 0.0006  0.0268  0.0255  99  ASP A N   
789  C  CA  . ASP A  99  ? 0.1436 0.2383 0.1781 0.0229  0.0287  0.0312  99  ASP A CA  
790  C  C   . ASP A  99  ? 0.1188 0.1825 0.1937 -0.0068 0.0073  0.0282  99  ASP A C   
791  O  O   . ASP A  99  ? 0.1517 0.1758 0.1735 0.0032  0.0107  0.0122  99  ASP A O   
792  C  CB  . ASP A  99  ? 0.1486 0.2229 0.2036 0.0175  0.0055  -0.0137 99  ASP A CB  
793  C  CG  . ASP A  99  ? 0.1620 0.2040 0.2164 -0.0125 0.0089  0.0086  99  ASP A CG  
794  O  OD1 . ASP A  99  ? 0.3347 0.2401 0.1956 -0.0074 -0.0029 0.0095  99  ASP A OD1 
795  O  OD2 . ASP A  99  ? 0.2608 0.3106 0.3173 0.0530  -0.1163 0.0006  99  ASP A OD2 
796  N  N   . PRO A  100 ? 0.1302 0.1843 0.1611 -0.0004 0.0345  0.0319  100 PRO A N   
797  C  CA  . PRO A  100 ? 0.1353 0.1740 0.1707 -0.0216 0.0120  0.0252  100 PRO A CA  
798  C  C   . PRO A  100 ? 0.1263 0.1592 0.1924 -0.0003 0.0310  0.0166  100 PRO A C   
799  O  O   . PRO A  100 ? 0.1685 0.1582 0.2307 -0.0023 0.0489  0.0381  100 PRO A O   
800  C  CB  . PRO A  100 ? 0.1545 0.1712 0.2247 -0.0249 0.0241  0.0709  100 PRO A CB  
801  C  CG  . PRO A  100 ? 0.1518 0.1688 0.2382 -0.0097 0.0118  0.0379  100 PRO A CG  
802  C  CD  . PRO A  100 ? 0.1833 0.1857 0.1793 0.0040  0.0495  0.0454  100 PRO A CD  
803  N  N   . HIS A  101 ? 0.1424 0.1658 0.1638 0.0013  0.0109  0.0168  101 HIS A N   
804  C  CA  . HIS A  101 ? 0.1553 0.1713 0.1719 -0.0280 0.0295  0.0233  101 HIS A CA  
805  C  C   . HIS A  101 ? 0.1587 0.1459 0.1672 0.0016  0.0071  0.0391  101 HIS A C   
806  O  O   . HIS A  101 ? 0.1779 0.2023 0.2807 -0.0108 -0.0520 0.0512  101 HIS A O   
807  C  CB  . HIS A  101 ? 0.1771 0.2365 0.1891 -0.0673 0.0245  0.0047  101 HIS A CB  
808  C  CG  . HIS A  101 ? 0.1798 0.2136 0.2181 -0.0219 0.0253  -0.0122 101 HIS A CG  
809  N  ND1 . HIS A  101 ? 0.1981 0.2493 0.2516 -0.0381 0.0163  -0.0019 101 HIS A ND1 
810  C  CD2 . HIS A  101 ? 0.2247 0.1981 0.2214 -0.0376 0.0493  -0.0031 101 HIS A CD2 
811  C  CE1 . HIS A  101 ? 0.1789 0.2216 0.3003 -0.0528 0.0155  0.0041  101 HIS A CE1 
812  N  NE2 . HIS A  101 ? 0.2256 0.2220 0.2469 -0.0478 -0.0026 -0.0057 101 HIS A NE2 
813  N  N   . GLY A  102 ? 0.1407 0.1543 0.1548 -0.0252 0.0168  0.0125  102 GLY A N   
814  C  CA  . GLY A  102 ? 0.1702 0.1254 0.1601 -0.0019 0.0260  0.0292  102 GLY A CA  
815  C  C   . GLY A  102 ? 0.1107 0.1335 0.1439 0.0022  -0.0023 0.0125  102 GLY A C   
816  O  O   . GLY A  102 ? 0.1457 0.1377 0.1563 -0.0008 -0.0008 0.0036  102 GLY A O   
817  N  N   . SER A  103 ? 0.1278 0.1194 0.1355 0.0050  0.0088  0.0166  103 SER A N   
818  C  CA  . SER A  103 ? 0.1303 0.0989 0.1480 0.0133  0.0010  0.0255  103 SER A CA  
819  C  C   . SER A  103 ? 0.0942 0.1289 0.1504 0.0092  0.0036  0.0204  103 SER A C   
820  O  O   . SER A  103 ? 0.1243 0.1523 0.1659 0.0085  0.0044  0.0413  103 SER A O   
821  C  CB  . SER A  103 ? 0.1059 0.1093 0.1689 -0.0105 -0.0047 0.0051  103 SER A CB  
822  O  OG  . SER A  103 ? 0.1243 0.1231 0.1504 -0.0083 0.0006  0.0227  103 SER A OG  
823  N  N   . GLU A  104 ? 0.1161 0.1132 0.1122 -0.0051 0.0026  0.0173  104 GLU A N   
824  C  CA  . GLU A  104 ? 0.1168 0.1210 0.1474 -0.0050 -0.0205 0.0210  104 GLU A CA  
825  C  C   . GLU A  104 ? 0.1049 0.1179 0.1494 -0.0094 0.0005  0.0284  104 GLU A C   
826  O  O   . GLU A  104 ? 0.1163 0.1122 0.1455 -0.0027 -0.0109 0.0178  104 GLU A O   
827  C  CB  . GLU A  104 ? 0.1262 0.1301 0.1224 -0.0249 -0.0166 0.0160  104 GLU A CB  
828  C  CG  . GLU A  104 ? 0.1233 0.1087 0.1658 -0.0206 0.0083  0.0080  104 GLU A CG  
829  C  CD  . GLU A  104 ? 0.1146 0.1195 0.1270 -0.0009 -0.0051 0.0053  104 GLU A CD  
830  O  OE1 . GLU A  104 ? 0.1182 0.1206 0.1618 0.0063  0.0116  0.0269  104 GLU A OE1 
831  O  OE2 . GLU A  104 ? 0.1044 0.1357 0.1781 -0.0019 -0.0040 0.0137  104 GLU A OE2 
832  N  N   . HIS A  105 ? 0.0974 0.1253 0.1378 -0.0100 0.0061  0.0065  105 HIS A N   
833  C  CA  . HIS A  105 ? 0.1222 0.1019 0.1375 -0.0027 0.0076  0.0193  105 HIS A CA  
834  C  C   . HIS A  105 ? 0.1130 0.1295 0.1259 -0.0081 -0.0054 0.0195  105 HIS A C   
835  O  O   . HIS A  105 ? 0.1240 0.1345 0.1468 -0.0117 -0.0076 0.0217  105 HIS A O   
836  C  CB  . HIS A  105 ? 0.1041 0.1150 0.1434 0.0044  0.0001  0.0114  105 HIS A CB  
837  C  CG  . HIS A  105 ? 0.1021 0.1321 0.1383 0.0048  -0.0018 0.0119  105 HIS A CG  
838  N  ND1 . HIS A  105 ? 0.1082 0.1271 0.1386 -0.0096 0.0044  0.0163  105 HIS A ND1 
839  C  CD2 . HIS A  105 ? 0.1067 0.1259 0.1454 0.0080  -0.0041 0.0107  105 HIS A CD2 
840  C  CE1 . HIS A  105 ? 0.1105 0.1458 0.1294 0.0087  -0.0081 0.0238  105 HIS A CE1 
841  N  NE2 . HIS A  105 ? 0.1059 0.1521 0.1446 0.0021  0.0002  0.0346  105 HIS A NE2 
842  N  N   . THR A  106 ? 0.1112 0.1088 0.1503 -0.0150 -0.0135 0.0120  106 THR A N   
843  C  CA  . THR A  106 ? 0.1218 0.1143 0.1671 -0.0173 0.0097  0.0190  106 THR A CA  
844  C  C   . THR A  106 ? 0.1202 0.1229 0.1406 -0.0097 -0.0145 0.0184  106 THR A C   
845  O  O   . THR A  106 ? 0.1260 0.1260 0.1495 -0.0128 -0.0078 0.0177  106 THR A O   
846  C  CB  . THR A  106 ? 0.1142 0.1450 0.1473 0.0006  0.0094  0.0173  106 THR A CB  
847  O  OG1 . THR A  106 ? 0.1298 0.1447 0.1801 -0.0075 -0.0082 0.0348  106 THR A OG1 
848  C  CG2 . THR A  106 ? 0.1373 0.1611 0.1844 0.0240  0.0125  0.0072  106 THR A CG2 
849  N  N   . VAL A  107 ? 0.1392 0.1143 0.1711 -0.0072 -0.0134 0.0029  107 VAL A N   
850  C  CA  . VAL A  107 ? 0.1430 0.1161 0.1728 -0.0001 -0.0152 -0.0010 107 VAL A CA  
851  C  C   . VAL A  107 ? 0.1515 0.1049 0.1676 -0.0204 0.0058  0.0059  107 VAL A C   
852  O  O   . VAL A  107 ? 0.1517 0.1336 0.1843 -0.0261 -0.0078 0.0172  107 VAL A O   
853  C  CB  . VAL A  107 ? 0.1406 0.1281 0.1899 -0.0033 -0.0165 0.0138  107 VAL A CB  
854  C  CG1 . VAL A  107 ? 0.1881 0.1505 0.2355 -0.0011 -0.0128 -0.0255 107 VAL A CG1 
855  C  CG2 . VAL A  107 ? 0.1376 0.1914 0.2283 -0.0211 -0.0264 0.0238  107 VAL A CG2 
856  N  N   . SER A  108 ? 0.1430 0.1508 0.1942 -0.0131 -0.0206 -0.0015 108 SER A N   
857  C  CA  . SER A  108 ? 0.1503 0.1511 0.2128 -0.0279 -0.0232 -0.0171 108 SER A CA  
858  C  C   . SER A  108 ? 0.1361 0.1551 0.1830 -0.0255 -0.0296 0.0078  108 SER A C   
859  O  O   . SER A  108 ? 0.1527 0.1572 0.2277 -0.0353 -0.0098 0.0029  108 SER A O   
860  C  CB  . SER A  108 ? 0.1926 0.1675 0.2734 -0.0362 0.0126  -0.0714 108 SER A CB  
861  O  OG  . SER A  108 ? 0.2279 0.2515 0.3055 -0.0878 -0.0057 -0.0557 108 SER A OG  
862  N  N   . GLY A  109 ? 0.1438 0.1493 0.1861 0.0022  -0.0130 0.0088  109 GLY A N   
863  C  CA  . GLY A  109 ? 0.1397 0.1703 0.1956 -0.0037 -0.0178 -0.0016 109 GLY A CA  
864  C  C   . GLY A  109 ? 0.1280 0.1922 0.2282 -0.0122 0.0084  0.0195  109 GLY A C   
865  O  O   . GLY A  109 ? 0.1593 0.2351 0.2453 0.0128  -0.0130 -0.0195 109 GLY A O   
866  N  N   . GLN A  110 ? 0.1394 0.1453 0.2204 -0.0204 -0.0218 0.0453  110 GLN A N   
867  C  CA  . GLN A  110 ? 0.1675 0.1318 0.1953 -0.0398 -0.0227 0.0132  110 GLN A CA  
868  C  C   . GLN A  110 ? 0.1404 0.1286 0.1702 -0.0204 0.0027  0.0291  110 GLN A C   
869  O  O   . GLN A  110 ? 0.1414 0.1257 0.1770 -0.0181 0.0072  0.0062  110 GLN A O   
870  C  CB  . GLN A  110 ? 0.1682 0.1384 0.2392 -0.0181 -0.0358 0.0203  110 GLN A CB  
871  C  CG  . GLN A  110 ? 0.1790 0.1566 0.2475 -0.0364 -0.0061 0.0160  110 GLN A CG  
872  C  CD  . GLN A  110 ? 0.1899 0.2198 0.2342 -0.0281 -0.0001 0.0228  110 GLN A CD  
873  O  OE1 . GLN A  110 ? 0.2078 0.2069 0.2757 -0.0335 0.0262  0.0356  110 GLN A OE1 
874  N  NE2 . GLN A  110 ? 0.2076 0.2261 0.3094 -0.0351 -0.0387 -0.0168 110 GLN A NE2 
875  N  N   . HIS A  111 ? 0.1207 0.1553 0.1690 0.0037  0.0085  0.0294  111 HIS A N   
876  C  CA  . HIS A  111 ? 0.1428 0.1527 0.1694 -0.0087 -0.0308 0.0126  111 HIS A CA  
877  C  C   . HIS A  111 ? 0.1517 0.1664 0.1542 -0.0442 -0.0342 0.0563  111 HIS A C   
878  O  O   . HIS A  111 ? 0.1582 0.2201 0.2818 -0.0590 -0.0374 0.0882  111 HIS A O   
879  C  CB  . HIS A  111 ? 0.1714 0.1593 0.1878 -0.0244 0.0265  0.0179  111 HIS A CB  
880  C  CG  . HIS A  111 ? 0.1330 0.1694 0.1839 -0.0093 0.0231  0.0040  111 HIS A CG  
881  N  ND1 . HIS A  111 ? 0.1919 0.1641 0.2721 0.0091  0.0155  0.0223  111 HIS A ND1 
882  C  CD2 . HIS A  111 ? 0.1351 0.1252 0.1756 -0.0211 0.0215  0.0078  111 HIS A CD2 
883  C  CE1 . HIS A  111 ? 0.1244 0.1543 0.2718 0.0126  0.0377  0.0425  111 HIS A CE1 
884  N  NE2 . HIS A  111 ? 0.1610 0.1827 0.2698 0.0094  0.0412  0.0117  111 HIS A NE2 
885  N  N   . PHE A  112 ? 0.1324 0.1394 0.1602 -0.0160 -0.0122 0.0147  112 PHE A N   
886  C  CA  . PHE A  112 ? 0.1349 0.1417 0.1400 -0.0122 -0.0081 0.0237  112 PHE A CA  
887  C  C   . PHE A  112 ? 0.1333 0.1068 0.1511 -0.0063 0.0201  0.0186  112 PHE A C   
888  O  O   . PHE A  112 ? 0.1404 0.1213 0.1508 0.0034  0.0153  0.0103  112 PHE A O   
889  C  CB  . PHE A  112 ? 0.1265 0.1305 0.1628 -0.0088 0.0153  -0.0054 112 PHE A CB  
890  C  CG  . PHE A  112 ? 0.1495 0.1538 0.1712 -0.0199 0.0156  0.0071  112 PHE A CG  
891  C  CD1 . PHE A  112 ? 0.2286 0.2329 0.1778 -0.0637 -0.0037 -0.0104 112 PHE A CD1 
892  C  CD2 . PHE A  112 ? 0.2066 0.1410 0.2514 -0.0233 0.0491  -0.0069 112 PHE A CD2 
893  C  CE1 . PHE A  112 ? 0.2791 0.2786 0.2428 -0.0403 0.0298  -0.0508 112 PHE A CE1 
894  C  CE2 . PHE A  112 ? 0.2623 0.1736 0.3210 -0.0375 0.0534  -0.0344 112 PHE A CE2 
895  C  CZ  . PHE A  112 ? 0.3028 0.2620 0.2879 -0.0583 0.0337  -0.1012 112 PHE A CZ  
896  N  N   . ALA A  113 ? 0.1191 0.1306 0.1415 -0.0097 0.0029  0.0146  113 ALA A N   
897  C  CA  . ALA A  113 ? 0.1268 0.1386 0.1465 -0.0188 0.0155  0.0240  113 ALA A CA  
898  C  C   . ALA A  113 ? 0.1249 0.1426 0.1212 0.0044  0.0062  0.0203  113 ALA A C   
899  O  O   . ALA A  113 ? 0.1186 0.1398 0.1499 -0.0008 0.0189  0.0210  113 ALA A O   
900  C  CB  . ALA A  113 ? 0.1837 0.1494 0.1514 0.0025  -0.0048 0.0434  113 ALA A CB  
901  N  N   . ALA A  114 ? 0.1091 0.1386 0.1420 -0.0084 0.0113  0.0262  114 ALA A N   
902  C  CA  . ALA A  114 ? 0.1295 0.1268 0.1177 -0.0158 0.0183  0.0050  114 ALA A CA  
903  C  C   . ALA A  114 ? 0.0967 0.1163 0.1409 0.0093  0.0019  0.0097  114 ALA A C   
904  O  O   . ALA A  114 ? 0.1236 0.1149 0.1286 0.0044  0.0100  0.0070  114 ALA A O   
905  C  CB  . ALA A  114 ? 0.1294 0.1547 0.1468 -0.0149 -0.0055 0.0122  114 ALA A CB  
906  N  N   . GLU A  115 ? 0.1024 0.1289 0.1301 -0.0076 -0.0050 0.0264  115 GLU A N   
907  C  CA  . GLU A  115 ? 0.1132 0.1320 0.1181 -0.0083 0.0073  0.0270  115 GLU A CA  
908  C  C   . GLU A  115 ? 0.1245 0.1269 0.1113 0.0004  0.0046  0.0125  115 GLU A C   
909  O  O   . GLU A  115 ? 0.1088 0.1417 0.1568 -0.0015 0.0164  -0.0076 115 GLU A O   
910  C  CB  . GLU A  115 ? 0.1125 0.1576 0.1155 -0.0070 0.0064  0.0203  115 GLU A CB  
911  C  CG  . GLU A  115 ? 0.1130 0.1338 0.1200 0.0104  -0.0054 0.0133  115 GLU A CG  
912  C  CD  . GLU A  115 ? 0.1119 0.1158 0.1380 0.0044  0.0081  0.0132  115 GLU A CD  
913  O  OE1 . GLU A  115 ? 0.1089 0.1371 0.1409 -0.0053 -0.0082 0.0222  115 GLU A OE1 
914  O  OE2 . GLU A  115 ? 0.1170 0.1436 0.1400 -0.0186 -0.0033 0.0208  115 GLU A OE2 
915  N  N   . LEU A  116 ? 0.1046 0.1289 0.1212 0.0004  0.0015  0.0216  116 LEU A N   
916  C  CA  . LEU A  116 ? 0.0974 0.1247 0.1438 -0.0081 0.0006  0.0373  116 LEU A CA  
917  C  C   . LEU A  116 ? 0.0895 0.1253 0.1161 0.0016  -0.0088 0.0053  116 LEU A C   
918  O  O   . LEU A  116 ? 0.1091 0.1193 0.1233 -0.0020 0.0015  0.0022  116 LEU A O   
919  C  CB  . LEU A  116 ? 0.0964 0.1514 0.1608 0.0137  -0.0148 0.0422  116 LEU A CB  
920  C  CG  . LEU A  116 ? 0.1152 0.1233 0.1705 -0.0033 -0.0435 0.0312  116 LEU A CG  
921  C  CD1 . LEU A  116 ? 0.1385 0.1883 0.1833 0.0036  -0.0206 -0.0036 116 LEU A CD1 
922  C  CD2 . LEU A  116 ? 0.1269 0.1676 0.2142 0.0358  -0.0027 0.0216  116 LEU A CD2 
923  N  N   . HIS A  117 ? 0.0903 0.1161 0.1231 0.0017  -0.0103 0.0162  117 HIS A N   
924  C  CA  . HIS A  117 ? 0.0973 0.1170 0.1209 0.0083  -0.0042 0.0242  117 HIS A CA  
925  C  C   . HIS A  117 ? 0.1042 0.1152 0.1053 -0.0044 0.0016  0.0120  117 HIS A C   
926  O  O   . HIS A  117 ? 0.0999 0.1509 0.1181 0.0017  -0.0040 0.0088  117 HIS A O   
927  C  CB  . HIS A  117 ? 0.0985 0.1291 0.1416 0.0085  -0.0106 0.0195  117 HIS A CB  
928  C  CG  . HIS A  117 ? 0.1009 0.0936 0.1362 0.0024  0.0083  0.0122  117 HIS A CG  
929  N  ND1 . HIS A  117 ? 0.1174 0.0971 0.1220 0.0000  -0.0013 -0.0042 117 HIS A ND1 
930  C  CD2 . HIS A  117 ? 0.1054 0.1177 0.1290 -0.0006 -0.0188 0.0265  117 HIS A CD2 
931  C  CE1 . HIS A  117 ? 0.1107 0.1069 0.1156 -0.0188 -0.0019 0.0036  117 HIS A CE1 
932  N  NE2 . HIS A  117 ? 0.0960 0.1195 0.1324 -0.0027 -0.0192 -0.0096 117 HIS A NE2 
933  N  N   . ILE A  118 ? 0.1007 0.1175 0.1269 0.0005  0.0092  0.0148  118 ILE A N   
934  C  CA  . ILE A  118 ? 0.0982 0.1116 0.1302 0.0039  0.0000  0.0239  118 ILE A CA  
935  C  C   . ILE A  118 ? 0.0814 0.1358 0.1344 0.0001  -0.0001 0.0077  118 ILE A C   
936  O  O   . ILE A  118 ? 0.1133 0.1365 0.1210 -0.0102 -0.0030 0.0125  118 ILE A O   
937  C  CB  . ILE A  118 ? 0.0940 0.1346 0.1623 0.0115  -0.0085 0.0301  118 ILE A CB  
938  C  CG1 . ILE A  118 ? 0.1263 0.1492 0.1398 0.0274  -0.0118 0.0280  118 ILE A CG1 
939  C  CG2 . ILE A  118 ? 0.1060 0.1820 0.2057 0.0096  -0.0190 0.0259  118 ILE A CG2 
940  C  CD1 . ILE A  118 ? 0.1437 0.1711 0.1787 0.0495  -0.0141 0.0312  118 ILE A CD1 
941  N  N   . VAL A  119 ? 0.0944 0.1243 0.1304 -0.0087 0.0049  0.0142  119 VAL A N   
942  C  CA  . VAL A  119 ? 0.1027 0.1154 0.1439 -0.0153 -0.0058 0.0142  119 VAL A CA  
943  C  C   . VAL A  119 ? 0.0899 0.1445 0.1292 -0.0088 0.0048  0.0140  119 VAL A C   
944  O  O   . VAL A  119 ? 0.1078 0.1693 0.1518 -0.0172 -0.0178 0.0181  119 VAL A O   
945  C  CB  . VAL A  119 ? 0.1062 0.1240 0.1494 -0.0077 -0.0027 -0.0001 119 VAL A CB  
946  C  CG1 . VAL A  119 ? 0.1290 0.1514 0.1733 -0.0068 0.0111  0.0297  119 VAL A CG1 
947  C  CG2 . VAL A  119 ? 0.0996 0.1588 0.1524 -0.0055 -0.0036 0.0188  119 VAL A CG2 
948  N  N   . HIS A  120 ? 0.1027 0.1577 0.1536 -0.0094 0.0000  0.0375  120 HIS A N   
949  C  CA  . HIS A  120 ? 0.0992 0.1497 0.1496 -0.0190 0.0043  0.0271  120 HIS A CA  
950  C  C   . HIS A  120 ? 0.0985 0.1296 0.1570 -0.0065 0.0027  0.0304  120 HIS A C   
951  O  O   . HIS A  120 ? 0.1061 0.1592 0.1633 -0.0200 -0.0072 0.0424  120 HIS A O   
952  C  CB  . HIS A  120 ? 0.1195 0.1531 0.1471 -0.0015 -0.0006 0.0168  120 HIS A CB  
953  C  CG  . HIS A  120 ? 0.1207 0.1520 0.1345 -0.0027 0.0053  0.0428  120 HIS A CG  
954  N  ND1 . HIS A  120 ? 0.1195 0.1581 0.1512 -0.0034 0.0158  0.0190  120 HIS A ND1 
955  C  CD2 . HIS A  120 ? 0.1416 0.1365 0.1802 -0.0046 -0.0067 0.0273  120 HIS A CD2 
956  C  CE1 . HIS A  120 ? 0.1243 0.1756 0.1633 0.0040  0.0100  0.0313  120 HIS A CE1 
957  N  NE2 . HIS A  120 ? 0.1361 0.1559 0.1662 0.0091  -0.0087 0.0409  120 HIS A NE2 
958  N  N   . TYR A  121 ? 0.1161 0.1577 0.1625 -0.0203 0.0069  0.0369  121 TYR A N   
959  C  CA  . TYR A  121 ? 0.1324 0.1767 0.1493 -0.0010 0.0089  0.0365  121 TYR A CA  
960  C  C   . TYR A  121 ? 0.1185 0.1641 0.1767 -0.0081 -0.0004 0.0409  121 TYR A C   
961  O  O   . TYR A  121 ? 0.1309 0.1663 0.1640 -0.0030 -0.0016 0.0435  121 TYR A O   
962  C  CB  . TYR A  121 ? 0.1400 0.1852 0.1906 -0.0197 -0.0132 0.0311  121 TYR A CB  
963  C  CG  . TYR A  121 ? 0.1474 0.1801 0.1823 -0.0289 0.0097  0.0301  121 TYR A CG  
964  C  CD1 . TYR A  121 ? 0.1546 0.2194 0.1683 -0.0234 -0.0051 0.0152  121 TYR A CD1 
965  C  CD2 . TYR A  121 ? 0.1709 0.2193 0.1893 -0.0656 0.0104  0.0084  121 TYR A CD2 
966  C  CE1 . TYR A  121 ? 0.1834 0.2323 0.2449 -0.0476 -0.0261 -0.0006 121 TYR A CE1 
967  C  CE2 . TYR A  121 ? 0.1497 0.2337 0.2640 -0.0553 0.0223  0.0106  121 TYR A CE2 
968  C  CZ  . TYR A  121 ? 0.1317 0.2778 0.2769 -0.0494 -0.0114 0.0204  121 TYR A CZ  
969  O  OH  . TYR A  121 ? 0.1703 0.3423 0.3141 -0.0511 -0.0584 -0.0097 121 TYR A OH  
970  N  N   . ASN A  122 ? 0.1321 0.1755 0.1615 -0.0110 -0.0075 0.0398  122 ASN A N   
971  C  CA  . ASN A  122 ? 0.1054 0.2399 0.1698 -0.0312 -0.0006 0.0533  122 ASN A CA  
972  C  C   . ASN A  122 ? 0.1346 0.2023 0.1575 -0.0080 -0.0153 0.0548  122 ASN A C   
973  O  O   . ASN A  122 ? 0.1295 0.1972 0.2054 -0.0175 -0.0055 0.0566  122 ASN A O   
974  C  CB  . ASN A  122 ? 0.1191 0.2408 0.1537 -0.0034 -0.0197 0.0320  122 ASN A CB  
975  C  CG  . ASN A  122 ? 0.1411 0.2673 0.1509 -0.0122 -0.0107 0.0528  122 ASN A CG  
976  O  OD1 . ASN A  122 ? 0.1391 0.2666 0.1617 -0.0120 -0.0034 0.0552  122 ASN A OD1 
977  N  ND2 . ASN A  122 ? 0.1993 0.2972 0.1595 -0.0038 -0.0293 0.0424  122 ASN A ND2 
978  N  N   . SER A  123 ? 0.0996 0.2163 0.1702 -0.0114 -0.0016 0.0577  123 SER A N   
979  C  CA  . SER A  123 ? 0.0885 0.2523 0.1920 -0.0283 0.0097  0.0640  123 SER A CA  
980  C  C   . SER A  123 ? 0.1293 0.2128 0.1956 -0.0402 0.0217  0.0268  123 SER A C   
981  O  O   . SER A  123 ? 0.1278 0.2750 0.2151 -0.0483 0.0109  0.0690  123 SER A O   
982  C  CB  . SER A  123 ? 0.1270 0.2184 0.1692 -0.0099 -0.0128 0.0420  123 SER A CB  
983  O  OG  . SER A  123 ? 0.1492 0.2254 0.1777 0.0008  -0.0065 0.0443  123 SER A OG  
984  N  N   . ASP A  124 ? 0.1469 0.2322 0.1619 -0.0147 0.0053  0.0341  124 ASP A N   
985  C  CA  . ASP A  124 ? 0.1605 0.2770 0.1855 0.0282  0.0466  0.0778  124 ASP A CA  
986  C  C   . ASP A  124 ? 0.1703 0.2359 0.2683 -0.0237 0.0528  0.0434  124 ASP A C   
987  O  O   . ASP A  124 ? 0.1767 0.3693 0.2861 -0.0175 0.0444  0.1347  124 ASP A O   
988  C  CB  . ASP A  124 ? 0.2102 0.2825 0.2020 0.0009  0.0102  0.0697  124 ASP A CB  
989  C  CG  . ASP A  124 ? 0.2012 0.2418 0.1427 -0.0303 0.0275  0.0450  124 ASP A CG  
990  O  OD1 . ASP A  124 ? 0.1668 0.2831 0.1784 0.0068  -0.0199 0.0491  124 ASP A OD1 
991  O  OD2 . ASP A  124 ? 0.1991 0.2697 0.1786 -0.0220 0.0332  0.0378  124 ASP A OD2 
992  N  N   . LEU A  125 ? 0.1797 0.2378 0.1864 0.0291  0.0207  0.0749  125 LEU A N   
993  C  CA  . LEU A  125 ? 0.1728 0.2129 0.2428 0.0092  0.0216  0.0381  125 LEU A CA  
994  C  C   . LEU A  125 ? 0.1652 0.2210 0.1885 -0.0073 0.0331  0.0475  125 LEU A C   
995  O  O   . LEU A  125 ? 0.2219 0.2744 0.2845 -0.0049 0.0179  0.0930  125 LEU A O   
996  C  CB  . LEU A  125 ? 0.1795 0.2126 0.2252 0.0099  0.0006  0.0430  125 LEU A CB  
997  C  CG  . LEU A  125 ? 0.2150 0.2838 0.2440 -0.0159 -0.0163 -0.0066 125 LEU A CG  
998  C  CD1 . LEU A  125 ? 0.2541 0.3495 0.2297 -0.0546 -0.0493 0.0537  125 LEU A CD1 
999  C  CD2 . LEU A  125 ? 0.3628 0.4393 0.2393 0.0207  0.0405  0.0430  125 LEU A CD2 
1000 N  N   . TYR A  126 ? 0.1855 0.2254 0.2022 -0.0181 0.0323  0.0126  126 TYR A N   
1001 C  CA  . TYR A  126 ? 0.1848 0.1963 0.1939 -0.0418 0.0233  0.0247  126 TYR A CA  
1002 C  C   . TYR A  126 ? 0.2178 0.2358 0.2408 -0.0593 0.0274  0.0447  126 TYR A C   
1003 O  O   . TYR A  126 ? 0.1912 0.2310 0.2605 -0.0261 -0.0030 0.0634  126 TYR A O   
1004 C  CB  . TYR A  126 ? 0.1549 0.2524 0.2948 -0.0479 0.0128  0.0510  126 TYR A CB  
1005 C  CG  . TYR A  126 ? 0.1637 0.2226 0.2769 -0.0249 -0.0006 0.0912  126 TYR A CG  
1006 C  CD1 . TYR A  126 ? 0.3051 0.2061 0.3253 -0.0871 0.0049  0.0929  126 TYR A CD1 
1007 C  CD2 . TYR A  126 ? 0.1729 0.2411 0.2610 -0.0627 0.0001  0.0787  126 TYR A CD2 
1008 C  CE1 . TYR A  126 ? 0.1500 0.3093 0.3565 -0.0211 -0.0137 0.1301  126 TYR A CE1 
1009 C  CE2 . TYR A  126 ? 0.1838 0.2283 0.2602 -0.0127 -0.0153 0.0624  126 TYR A CE2 
1010 C  CZ  . TYR A  126 ? 0.1897 0.2619 0.3026 -0.0212 -0.0271 0.1179  126 TYR A CZ  
1011 O  OH  . TYR A  126 ? 0.2124 0.2901 0.3510 -0.0299 -0.0337 0.1550  126 TYR A OH  
1012 N  N   . PRO A  127 ? 0.1887 0.2444 0.3016 -0.0248 -0.0233 0.0171  127 PRO A N   
1013 C  CA  . PRO A  127 ? 0.2638 0.2518 0.2678 -0.0650 -0.0490 0.0117  127 PRO A CA  
1014 C  C   . PRO A  127 ? 0.2188 0.2810 0.2483 -0.0286 -0.0315 -0.0158 127 PRO A C   
1015 O  O   . PRO A  127 ? 0.2186 0.3974 0.3388 -0.0258 -0.0474 0.0234  127 PRO A O   
1016 C  CB  . PRO A  127 ? 0.2373 0.2554 0.4282 -0.0888 -0.0094 0.0509  127 PRO A CB  
1017 C  CG  . PRO A  127 ? 0.2883 0.3057 0.2492 0.0005  -0.0177 0.0168  127 PRO A CG  
1018 C  CD  . PRO A  127 ? 0.2660 0.2452 0.3003 -0.0288 -0.0024 0.0385  127 PRO A CD  
1019 N  N   . ASP A  128 ? 0.2197 0.2476 0.2498 -0.0633 0.0138  0.0122  128 ASP A N   
1020 C  CA  . ASP A  128 ? 0.2065 0.2834 0.2365 -0.0531 -0.0023 -0.0329 128 ASP A CA  
1021 C  C   . ASP A  128 ? 0.2101 0.2567 0.2198 -0.0337 -0.0366 0.0212  128 ASP A C   
1022 O  O   . ASP A  128 ? 0.1730 0.2151 0.2327 -0.0215 -0.0052 0.0067  128 ASP A O   
1023 C  CB  . ASP A  128 ? 0.2780 0.2193 0.3547 -0.0163 -0.0311 -0.0247 128 ASP A CB  
1024 C  CG  . ASP A  128 ? 0.2546 0.2660 0.3556 -0.0704 -0.0012 0.0055  128 ASP A CG  
1025 O  OD1 . ASP A  128 ? 0.3294 0.2615 0.4238 -0.0534 -0.0910 -0.0160 128 ASP A OD1 
1026 O  OD2 . ASP A  128 ? 0.3231 0.3797 0.6399 -0.1569 -0.0526 0.0245  128 ASP A OD2 
1027 N  N   . ALA A  129 ? 0.1896 0.2028 0.2518 -0.0093 0.0078  0.0040  129 ALA A N   
1028 C  CA  . ALA A  129 ? 0.1976 0.1719 0.2456 -0.0013 0.0195  0.0610  129 ALA A CA  
1029 C  C   . ALA A  129 ? 0.2701 0.1895 0.2321 -0.0005 0.0001  0.0688  129 ALA A C   
1030 O  O   . ALA A  129 ? 0.2236 0.2271 0.2838 -0.0181 -0.0065 0.0502  129 ALA A O   
1031 C  CB  . ALA A  129 ? 0.2894 0.2451 0.2201 0.0268  0.0386  0.0681  129 ALA A CB  
1032 N  N   . SER A  130 ? 0.3337 0.1772 0.2474 0.0132  0.0084  0.0033  130 SER A N   
1033 C  CA  . SER A  130 ? 0.3217 0.2348 0.2895 0.0582  0.0259  0.0273  130 SER A CA  
1034 C  C   . SER A  130 ? 0.2867 0.1759 0.2943 0.0237  0.0414  0.0064  130 SER A C   
1035 O  O   . SER A  130 ? 0.2638 0.2540 0.3767 0.0458  0.0435  0.0820  130 SER A O   
1036 C  CB  . SER A  130 ? 0.5851 0.2101 0.2662 0.0736  0.0079  0.0084  130 SER A CB  
1037 O  OG  . SER A  130 ? 0.6722 0.3551 0.5177 0.1650  -0.0132 -0.1201 130 SER A OG  
1038 N  N   . THR A  131 ? 0.2557 0.1963 0.2802 -0.0491 0.0116  -0.0151 131 THR A N   
1039 C  CA  . THR A  131 ? 0.2066 0.2770 0.3527 -0.0240 -0.0376 0.0593  131 THR A CA  
1040 C  C   . THR A  131 ? 0.2328 0.1844 0.2888 -0.0366 0.0151  0.0699  131 THR A C   
1041 O  O   . THR A  131 ? 0.2753 0.1809 0.2960 -0.0098 -0.0137 0.0788  131 THR A O   
1042 C  CB  . THR A  131 ? 0.2018 0.3064 0.3012 -0.1065 -0.0261 0.0234  131 THR A CB  
1043 O  OG1 . THR A  131 ? 0.3100 0.2209 0.3868 -0.0758 -0.0158 -0.0019 131 THR A OG1 
1044 C  CG2 . THR A  131 ? 0.2754 0.2599 0.3546 -0.0659 -0.0197 0.1179  131 THR A CG2 
1045 N  N   . ALA A  132 ? 0.2283 0.1524 0.2804 -0.0157 0.0059  0.0540  132 ALA A N   
1046 C  CA  . ALA A  132 ? 0.1534 0.1750 0.2260 -0.0165 -0.0043 0.0270  132 ALA A CA  
1047 C  C   . ALA A  132 ? 0.1848 0.1946 0.2308 -0.0263 -0.0113 0.0433  132 ALA A C   
1048 O  O   . ALA A  132 ? 0.1630 0.1773 0.2415 -0.0080 -0.0031 0.0446  132 ALA A O   
1049 C  CB  . ALA A  132 ? 0.1755 0.1795 0.2618 -0.0193 0.0197  0.0234  132 ALA A CB  
1050 N  N   . SER A  133 ? 0.1676 0.1549 0.2676 -0.0099 0.0106  0.0351  133 SER A N   
1051 C  CA  . SER A  133 ? 0.1669 0.1980 0.2583 0.0089  0.0162  0.0309  133 SER A CA  
1052 C  C   . SER A  133 ? 0.1606 0.1429 0.2694 -0.0162 0.0109  0.0144  133 SER A C   
1053 O  O   . SER A  133 ? 0.1961 0.1833 0.2506 -0.0668 0.0025  0.0096  133 SER A O   
1054 C  CB  . SER A  133 ? 0.1909 0.2109 0.2630 -0.0078 0.0384  0.0219  133 SER A CB  
1055 O  OG  . SER A  133 ? 0.2304 0.2262 0.3497 -0.0073 0.0038  -0.0080 133 SER A OG  
1056 N  N   . ASN A  134 ? 0.1733 0.1709 0.2811 -0.0285 -0.0164 0.0661  134 ASN A N   
1057 C  CA  . ASN A  134 ? 0.2004 0.1485 0.3131 -0.0211 -0.0638 0.0443  134 ASN A CA  
1058 C  C   . ASN A  134 ? 0.1976 0.1770 0.2901 -0.0072 0.0122  0.0717  134 ASN A C   
1059 O  O   . ASN A  134 ? 0.2889 0.3112 0.3255 0.0579  -0.0398 0.0837  134 ASN A O   
1060 C  CB  . ASN A  134 ? 0.1995 0.1656 0.4021 -0.0055 -0.0356 0.0431  134 ASN A CB  
1061 C  CG  . ASN A  134 ? 0.2319 0.2509 0.6440 -0.0630 0.0617  0.0414  134 ASN A CG  
1062 O  OD1 . ASN A  134 ? 0.2751 0.1997 0.5012 -0.0604 0.0629  0.0502  134 ASN A OD1 
1063 N  ND2 . ASN A  134 ? 0.3468 0.2451 0.6221 -0.0841 0.0156  0.0507  134 ASN A ND2 
1064 N  N   . LYS A  135 ? 0.1810 0.1841 0.2976 -0.0168 0.0062  0.0559  135 LYS A N   
1065 C  CA  . LYS A  135 ? 0.1694 0.2186 0.2999 -0.0012 0.0086  0.0766  135 LYS A CA  
1066 C  C   . LYS A  135 ? 0.2083 0.2298 0.2207 0.0018  -0.0510 0.0270  135 LYS A C   
1067 O  O   . LYS A  135 ? 0.1797 0.2236 0.2561 0.0122  0.0048  0.0699  135 LYS A O   
1068 C  CB  . LYS A  135 ? 0.2004 0.3274 0.3048 -0.0567 0.0044  0.0469  135 LYS A CB  
1069 C  CG  . LYS A  135 ? 0.2409 0.3683 0.3612 -0.0746 -0.0104 -0.0423 135 LYS A CG  
1070 C  CD  . LYS A  135 ? 0.2757 0.3003 0.4497 -0.0993 -0.0234 0.0856  135 LYS A CD  
1071 C  CE  . LYS A  135 ? 0.3331 0.3149 0.3518 0.0120  0.0091  0.0959  135 LYS A CE  
1072 N  NZ  . LYS A  135 ? 0.2685 0.2584 0.3825 0.0252  -0.0023 0.1110  135 LYS A NZ  
1073 N  N   . SER A  136 ? 0.2868 0.2586 0.2367 0.0337  -0.0384 0.0715  136 SER A N   
1074 C  CA  . SER A  136 ? 0.3753 0.2338 0.2647 -0.0037 -0.1028 0.0900  136 SER A CA  
1075 C  C   . SER A  136 ? 0.1954 0.2279 0.2193 -0.0432 -0.0500 0.0990  136 SER A C   
1076 O  O   . SER A  136 ? 0.2029 0.2728 0.2665 -0.0569 -0.0212 0.1125  136 SER A O   
1077 C  CB  . SER A  136 ? 0.4663 0.3074 0.2316 0.0414  -0.0783 0.1313  136 SER A CB  
1078 O  OG  . SER A  136 ? 0.6721 0.3944 0.3249 -0.0118 -0.0611 0.1122  136 SER A OG  
1079 N  N   . GLU A  137 ? 0.2163 0.2028 0.2503 -0.0354 -0.0269 0.0763  137 GLU A N   
1080 C  CA  . GLU A  137 ? 0.1941 0.2087 0.1989 -0.0042 -0.0359 0.0782  137 GLU A CA  
1081 C  C   . GLU A  137 ? 0.1817 0.2053 0.1826 -0.0107 -0.0032 0.0421  137 GLU A C   
1082 O  O   . GLU A  137 ? 0.1889 0.2445 0.2007 0.0215  -0.0171 0.0447  137 GLU A O   
1083 C  CB  . GLU A  137 ? 0.2513 0.3466 0.2316 0.0124  -0.0392 0.0409  137 GLU A CB  
1084 C  CG  . GLU A  137 ? 0.4443 0.4151 0.2956 0.1172  -0.1690 0.0126  137 GLU A CG  
1085 C  CD  . GLU A  137 ? 0.9721 0.5125 0.3341 0.0617  0.1404  -0.0367 137 GLU A CD  
1086 O  OE1 . GLU A  137 ? 0.7743 1.0623 0.7178 0.1716  0.2535  0.2034  137 GLU A OE1 
1087 O  OE2 . GLU A  137 ? 1.2072 0.5873 0.4959 -0.0499 -0.3383 0.1966  137 GLU A OE2 
1088 N  N   . GLY A  138 ? 0.1600 0.1837 0.1787 -0.0244 -0.0121 0.0471  138 GLY A N   
1089 C  CA  . GLY A  138 ? 0.1834 0.1724 0.1886 -0.0047 -0.0005 0.0532  138 GLY A CA  
1090 C  C   . GLY A  138 ? 0.1479 0.1321 0.1729 -0.0189 -0.0143 0.0258  138 GLY A C   
1091 O  O   . GLY A  138 ? 0.1195 0.1714 0.2023 -0.0092 -0.0088 0.0494  138 GLY A O   
1092 N  N   . LEU A  139 ? 0.1351 0.1567 0.1771 -0.0329 -0.0147 0.0401  139 LEU A N   
1093 C  CA  . LEU A  139 ? 0.1353 0.1610 0.1473 -0.0060 0.0046  0.0255  139 LEU A CA  
1094 C  C   . LEU A  139 ? 0.1129 0.1378 0.1627 -0.0185 0.0076  0.0183  139 LEU A C   
1095 O  O   . LEU A  139 ? 0.1310 0.1542 0.1448 -0.0126 -0.0077 0.0265  139 LEU A O   
1096 C  CB  . LEU A  139 ? 0.1067 0.1460 0.1764 -0.0070 -0.0046 0.0088  139 LEU A CB  
1097 C  CG  . LEU A  139 ? 0.1134 0.1545 0.1912 -0.0126 0.0036  0.0198  139 LEU A CG  
1098 C  CD1 . LEU A  139 ? 0.1631 0.1718 0.2349 -0.0278 0.0463  -0.0054 139 LEU A CD1 
1099 C  CD2 . LEU A  139 ? 0.1375 0.1920 0.1989 -0.0105 -0.0163 -0.0255 139 LEU A CD2 
1100 N  N   . ALA A  140 ? 0.1125 0.1578 0.1496 -0.0046 -0.0001 0.0402  140 ALA A N   
1101 C  CA  . ALA A  140 ? 0.1425 0.1318 0.1375 -0.0245 -0.0133 0.0359  140 ALA A CA  
1102 C  C   . ALA A  140 ? 0.1067 0.1515 0.1412 -0.0142 -0.0194 0.0314  140 ALA A C   
1103 O  O   . ALA A  140 ? 0.1269 0.1716 0.1394 -0.0350 -0.0187 0.0407  140 ALA A O   
1104 C  CB  . ALA A  140 ? 0.1035 0.1446 0.1804 -0.0100 0.0008  0.0215  140 ALA A CB  
1105 N  N   . VAL A  141 ? 0.1136 0.1282 0.1345 -0.0092 0.0033  0.0341  141 VAL A N   
1106 C  CA  . VAL A  141 ? 0.1125 0.1340 0.1311 -0.0049 0.0054  0.0099  141 VAL A CA  
1107 C  C   . VAL A  141 ? 0.1079 0.1365 0.1264 -0.0174 0.0119  -0.0031 141 VAL A C   
1108 O  O   . VAL A  141 ? 0.1303 0.1377 0.1342 -0.0199 -0.0067 0.0078  141 VAL A O   
1109 C  CB  . VAL A  141 ? 0.1218 0.1298 0.1304 0.0154  0.0018  0.0091  141 VAL A CB  
1110 C  CG1 . VAL A  141 ? 0.1203 0.1816 0.1298 0.0166  -0.0044 0.0165  141 VAL A CG1 
1111 C  CG2 . VAL A  141 ? 0.1492 0.1430 0.1733 0.0163  -0.0348 0.0058  141 VAL A CG2 
1112 N  N   . LEU A  142 ? 0.1033 0.1411 0.1303 0.0102  0.0049  0.0179  142 LEU A N   
1113 C  CA  . LEU A  142 ? 0.1138 0.1318 0.1592 0.0075  0.0239  0.0173  142 LEU A CA  
1114 C  C   . LEU A  142 ? 0.1268 0.1286 0.1031 -0.0027 -0.0078 0.0234  142 LEU A C   
1115 O  O   . LEU A  142 ? 0.1342 0.1507 0.1176 -0.0187 -0.0004 0.0097  142 LEU A O   
1116 C  CB  . LEU A  142 ? 0.1385 0.1279 0.1492 0.0061  0.0104  0.0069  142 LEU A CB  
1117 C  CG  . LEU A  142 ? 0.1133 0.1611 0.1697 0.0115  0.0136  0.0281  142 LEU A CG  
1118 C  CD1 . LEU A  142 ? 0.1368 0.2128 0.1956 0.0279  -0.0185 0.0337  142 LEU A CD1 
1119 C  CD2 . LEU A  142 ? 0.1702 0.1945 0.1522 0.0106  0.0103  -0.0118 142 LEU A CD2 
1120 N  N   . ALA A  143 ? 0.1159 0.1281 0.1410 -0.0064 0.0087  0.0127  143 ALA A N   
1121 C  CA  . ALA A  143 ? 0.1018 0.1152 0.1452 0.0103  0.0060  0.0148  143 ALA A CA  
1122 C  C   . ALA A  143 ? 0.1041 0.1185 0.1354 -0.0006 -0.0072 0.0006  143 ALA A C   
1123 O  O   . ALA A  143 ? 0.1445 0.1174 0.1337 -0.0016 0.0026  0.0139  143 ALA A O   
1124 C  CB  . ALA A  143 ? 0.1055 0.1272 0.1454 0.0055  -0.0100 0.0156  143 ALA A CB  
1125 N  N   . VAL A  144 ? 0.1040 0.1300 0.1258 0.0050  0.0111  0.0174  144 VAL A N   
1126 C  CA  . VAL A  144 ? 0.1177 0.1324 0.1429 0.0054  0.0106  0.0405  144 VAL A CA  
1127 C  C   . VAL A  144 ? 0.1227 0.1080 0.1243 0.0054  0.0029  0.0236  144 VAL A C   
1128 O  O   . VAL A  144 ? 0.1311 0.1259 0.1366 0.0023  0.0078  0.0058  144 VAL A O   
1129 C  CB  . VAL A  144 ? 0.1249 0.1458 0.1468 0.0105  -0.0041 0.0411  144 VAL A CB  
1130 C  CG1 . VAL A  144 ? 0.1623 0.1606 0.1797 0.0105  -0.0038 0.0610  144 VAL A CG1 
1131 C  CG2 . VAL A  144 ? 0.1206 0.1740 0.1725 0.0237  0.0058  0.0516  144 VAL A CG2 
1132 N  N   . LEU A  145 ? 0.1134 0.1226 0.1404 0.0055  0.0052  0.0268  145 LEU A N   
1133 C  CA  . LEU A  145 ? 0.1183 0.1406 0.1367 0.0000  0.0034  0.0185  145 LEU A CA  
1134 C  C   . LEU A  145 ? 0.1152 0.1240 0.1419 0.0116  0.0042  0.0200  145 LEU A C   
1135 O  O   . LEU A  145 ? 0.1474 0.1400 0.1500 0.0334  0.0195  0.0236  145 LEU A O   
1136 C  CB  . LEU A  145 ? 0.1537 0.1561 0.1354 -0.0275 -0.0047 0.0286  145 LEU A CB  
1137 C  CG  . LEU A  145 ? 0.1615 0.1482 0.1675 0.0006  -0.0306 0.0192  145 LEU A CG  
1138 C  CD1 . LEU A  145 ? 0.1757 0.1993 0.1822 -0.0260 -0.0039 -0.0061 145 LEU A CD1 
1139 C  CD2 . LEU A  145 ? 0.1811 0.1673 0.2079 0.0012  -0.0490 0.0294  145 LEU A CD2 
1140 N  N   . ILE A  146 ? 0.1257 0.1298 0.1291 -0.0023 0.0179  0.0223  146 ILE A N   
1141 C  CA  . ILE A  146 ? 0.1164 0.1459 0.1351 -0.0006 -0.0013 0.0295  146 ILE A CA  
1142 C  C   . ILE A  146 ? 0.1260 0.1290 0.1521 0.0065  0.0047  0.0365  146 ILE A C   
1143 O  O   . ILE A  146 ? 0.1298 0.1375 0.1664 0.0091  0.0200  0.0307  146 ILE A O   
1144 C  CB  . ILE A  146 ? 0.1419 0.1261 0.1297 0.0027  0.0048  0.0228  146 ILE A CB  
1145 C  CG1 . ILE A  146 ? 0.1315 0.1656 0.1527 -0.0010 0.0078  -0.0003 146 ILE A CG1 
1146 C  CG2 . ILE A  146 ? 0.1673 0.1449 0.1294 -0.0004 -0.0026 0.0278  146 ILE A CG2 
1147 C  CD1 . ILE A  146 ? 0.1436 0.1533 0.1586 -0.0017 -0.0151 0.0164  146 ILE A CD1 
1148 N  N   . GLU A  147 ? 0.1552 0.1342 0.1674 0.0149  0.0234  0.0469  147 GLU A N   
1149 C  CA  . GLU A  147 ? 0.1466 0.1604 0.2066 -0.0222 0.0183  0.0648  147 GLU A CA  
1150 C  C   . GLU A  147 ? 0.1403 0.1428 0.1870 -0.0036 0.0087  0.0446  147 GLU A C   
1151 O  O   . GLU A  147 ? 0.1588 0.1405 0.1920 0.0091  0.0113  0.0428  147 GLU A O   
1152 C  CB  . GLU A  147 ? 0.2044 0.1556 0.2291 -0.0087 0.0390  0.0234  147 GLU A CB  
1153 C  CG  . GLU A  147 ? 0.2001 0.1646 0.2314 -0.0188 0.0117  0.0512  147 GLU A CG  
1154 C  CD  . GLU A  147 ? 0.2313 0.2105 0.2626 -0.0067 -0.0031 0.0396  147 GLU A CD  
1155 O  OE1 . GLU A  147 ? 0.2421 0.2639 0.2734 -0.0282 -0.0098 0.0136  147 GLU A OE1 
1156 O  OE2 . GLU A  147 ? 0.2896 0.1824 0.3766 -0.0242 0.0182  -0.0212 147 GLU A OE2 
1157 N  N   A MET A  148 ? 0.1816 0.1534 0.1634 0.0209  0.0222  0.0458  148 MET A N   
1158 N  N   B MET A  148 ? 0.1868 0.1392 0.2370 -0.0201 0.0510  0.0652  148 MET A N   
1159 C  CA  A MET A  148 ? 0.1688 0.1494 0.1725 0.0016  0.0373  0.0543  148 MET A CA  
1160 C  CA  B MET A  148 ? 0.2193 0.2325 0.2266 -0.0151 0.0343  0.0518  148 MET A CA  
1161 C  C   A MET A  148 ? 0.1852 0.1674 0.1956 -0.0072 0.0171  0.0144  148 MET A C   
1162 C  C   B MET A  148 ? 0.1760 0.2389 0.2170 -0.0285 0.0270  0.0595  148 MET A C   
1163 O  O   A MET A  148 ? 0.2342 0.1448 0.2107 -0.0149 -0.0194 0.0284  148 MET A O   
1164 O  O   B MET A  148 ? 0.2480 0.1883 0.2366 -0.0201 0.0561  0.0474  148 MET A O   
1165 C  CB  A MET A  148 ? 0.1303 0.1842 0.1748 0.0134  0.0106  0.0226  148 MET A CB  
1166 C  CB  B MET A  148 ? 0.2597 0.2288 0.2196 -0.0442 0.0593  0.0762  148 MET A CB  
1167 C  CG  A MET A  148 ? 0.2782 0.1653 0.1766 0.0002  0.0458  0.0523  148 MET A CG  
1168 C  CG  B MET A  148 ? 0.2662 0.2020 0.3125 -0.0743 -0.0210 0.0598  148 MET A CG  
1169 S  SD  A MET A  148 ? 0.2649 0.2338 0.2447 0.0143  0.0460  0.0627  148 MET A SD  
1170 S  SD  B MET A  148 ? 0.3897 0.4707 0.4140 0.0847  0.1902  0.0721  148 MET A SD  
1171 C  CE  A MET A  148 ? 0.1840 0.1498 0.2257 -0.0060 -0.0220 0.0603  148 MET A CE  
1172 C  CE  B MET A  148 ? 0.1647 0.3662 0.1810 0.0272  0.0377  0.1023  148 MET A CE  
1173 N  N   . GLY A  149 ? 0.1901 0.1823 0.2275 0.0042  0.0098  0.0633  149 GLY A N   
1174 C  CA  . GLY A  149 ? 0.2611 0.1763 0.2056 0.0019  0.0031  0.0263  149 GLY A CA  
1175 C  C   . GLY A  149 ? 0.2380 0.1518 0.2231 0.0063  0.0291  0.0679  149 GLY A C   
1176 O  O   . GLY A  149 ? 0.2356 0.1879 0.2195 0.0245  0.0253  0.0637  149 GLY A O   
1177 N  N   A SER A  150 ? 0.2237 0.1612 0.2382 0.0241  -0.0002 0.0792  150 SER A N   
1178 N  N   B SER A  150 ? 0.2426 0.1710 0.2604 0.0043  0.0350  0.0166  150 SER A N   
1179 C  CA  A SER A  150 ? 0.2722 0.1788 0.2411 0.0397  -0.0446 0.0488  150 SER A CA  
1180 C  CA  B SER A  150 ? 0.2397 0.1929 0.2265 0.0257  0.0505  0.0642  150 SER A CA  
1181 C  C   A SER A  150 ? 0.1911 0.1988 0.2285 0.0232  0.0234  0.0630  150 SER A C   
1182 C  C   B SER A  150 ? 0.2564 0.2194 0.2341 0.0258  0.0337  0.0328  150 SER A C   
1183 O  O   A SER A  150 ? 0.1879 0.1729 0.2195 -0.0006 0.0131  0.0405  150 SER A O   
1184 O  O   B SER A  150 ? 0.2311 0.1920 0.2241 0.0641  0.0033  0.0368  150 SER A O   
1185 C  CB  A SER A  150 ? 0.3523 0.2385 0.1518 0.0245  0.0152  0.0554  150 SER A CB  
1186 C  CB  B SER A  150 ? 0.3104 0.1553 0.2984 0.0840  -0.0822 -0.0208 150 SER A CB  
1187 O  OG  A SER A  150 ? 0.3051 0.2210 0.4943 0.0543  -0.0037 0.0172  150 SER A OG  
1188 O  OG  B SER A  150 ? 0.2722 0.2869 0.3747 0.0790  0.0973  -0.0656 150 SER A OG  
1189 N  N   . PHE A  151 ? 0.2592 0.2270 0.2272 0.0453  0.0190  0.0691  151 PHE A N   
1190 C  CA  . PHE A  151 ? 0.1921 0.2477 0.2366 0.0538  0.0076  0.0881  151 PHE A CA  
1191 C  C   . PHE A  151 ? 0.1995 0.2271 0.2329 0.0256  0.0168  0.0242  151 PHE A C   
1192 O  O   . PHE A  151 ? 0.2426 0.2155 0.2355 0.0558  0.0226  0.0714  151 PHE A O   
1193 C  CB  . PHE A  151 ? 0.2140 0.2367 0.2482 0.0390  -0.0172 0.0917  151 PHE A CB  
1194 C  CG  . PHE A  151 ? 0.2518 0.2224 0.2374 0.0347  -0.0117 0.0886  151 PHE A CG  
1195 C  CD1 . PHE A  151 ? 0.3489 0.2409 0.2216 0.0133  -0.0383 0.1189  151 PHE A CD1 
1196 C  CD2 . PHE A  151 ? 0.2480 0.3072 0.2576 0.0435  -0.0232 0.0702  151 PHE A CD2 
1197 C  CE1 . PHE A  151 ? 0.3092 0.3080 0.1913 0.0044  -0.0305 0.1077  151 PHE A CE1 
1198 C  CE2 . PHE A  151 ? 0.2742 0.3091 0.2096 0.0310  -0.0057 0.0735  151 PHE A CE2 
1199 C  CZ  . PHE A  151 ? 0.2825 0.2682 0.1962 -0.0089 -0.0299 0.0785  151 PHE A CZ  
1200 N  N   . ASN A  152 ? 0.2000 0.2152 0.1721 0.0237  0.0156  0.0566  152 ASN A N   
1201 C  CA  . ASN A  152 ? 0.1897 0.2042 0.2055 0.0578  0.0012  0.0648  152 ASN A CA  
1202 C  C   . ASN A  152 ? 0.2013 0.2515 0.1918 0.0584  0.0132  0.0399  152 ASN A C   
1203 O  O   . ASN A  152 ? 0.1766 0.2343 0.1892 0.0366  -0.0141 0.0414  152 ASN A O   
1204 C  CB  . ASN A  152 ? 0.1840 0.2107 0.1839 0.0510  0.0265  0.0658  152 ASN A CB  
1205 C  CG  . ASN A  152 ? 0.1845 0.1797 0.1740 0.0348  -0.0131 0.0538  152 ASN A CG  
1206 O  OD1 . ASN A  152 ? 0.1798 0.2202 0.1990 0.0357  -0.0001 0.0405  152 ASN A OD1 
1207 N  ND2 . ASN A  152 ? 0.2021 0.1802 0.1667 0.0326  0.0006  0.0267  152 ASN A ND2 
1208 N  N   . PRO A  153 ? 0.1908 0.2508 0.2146 0.0605  -0.0161 0.0637  153 PRO A N   
1209 C  CA  . PRO A  153 ? 0.2070 0.2632 0.2189 0.0538  -0.0305 0.0914  153 PRO A CA  
1210 C  C   . PRO A  153 ? 0.1836 0.2346 0.1954 0.0557  0.0059  0.0240  153 PRO A C   
1211 O  O   . PRO A  153 ? 0.2389 0.2776 0.2070 0.0345  -0.0317 0.0364  153 PRO A O   
1212 C  CB  . PRO A  153 ? 0.2155 0.2748 0.3829 0.0775  -0.0346 0.1036  153 PRO A CB  
1213 C  CG  . PRO A  153 ? 0.2492 0.3064 0.4073 0.0801  -0.1015 0.0330  153 PRO A CG  
1214 C  CD  . PRO A  153 ? 0.2178 0.2700 0.2499 0.0766  -0.0359 0.0441  153 PRO A CD  
1215 N  N   . SER A  154 ? 0.1655 0.2293 0.2058 0.0416  -0.0102 0.0509  154 SER A N   
1216 C  CA  . SER A  154 ? 0.2070 0.2133 0.2006 0.0514  0.0103  0.0445  154 SER A CA  
1217 C  C   . SER A  154 ? 0.1799 0.2067 0.1503 0.0117  -0.0122 0.0230  154 SER A C   
1218 O  O   . SER A  154 ? 0.1657 0.2454 0.1800 0.0150  -0.0079 0.0296  154 SER A O   
1219 C  CB  . SER A  154 ? 0.2275 0.2551 0.2127 0.0780  0.0244  0.0299  154 SER A CB  
1220 O  OG  . SER A  154 ? 0.2841 0.2735 0.2886 0.0876  0.0617  0.0610  154 SER A OG  
1221 N  N   . TYR A  155 ? 0.1591 0.2046 0.1915 0.0336  -0.0071 0.0236  155 TYR A N   
1222 C  CA  . TYR A  155 ? 0.1691 0.2042 0.1593 0.0190  -0.0125 0.0024  155 TYR A CA  
1223 C  C   . TYR A  155 ? 0.1559 0.2171 0.1772 0.0106  -0.0186 0.0192  155 TYR A C   
1224 O  O   . TYR A  155 ? 0.1769 0.2153 0.1675 0.0118  -0.0205 0.0142  155 TYR A O   
1225 C  CB  . TYR A  155 ? 0.1746 0.2111 0.1538 0.0119  -0.0049 0.0296  155 TYR A CB  
1226 C  CG  . TYR A  155 ? 0.1400 0.2011 0.1635 0.0302  -0.0012 0.0302  155 TYR A CG  
1227 C  CD1 . TYR A  155 ? 0.1529 0.1634 0.1816 0.0128  0.0103  0.0487  155 TYR A CD1 
1228 C  CD2 . TYR A  155 ? 0.1475 0.1926 0.1622 0.0325  0.0122  0.0354  155 TYR A CD2 
1229 C  CE1 . TYR A  155 ? 0.1471 0.1556 0.1578 0.0097  -0.0113 0.0392  155 TYR A CE1 
1230 C  CE2 . TYR A  155 ? 0.1520 0.1719 0.1509 0.0207  0.0064  0.0179  155 TYR A CE2 
1231 C  CZ  . TYR A  155 ? 0.1363 0.1516 0.1489 0.0116  -0.0017 0.0075  155 TYR A CZ  
1232 O  OH  . TYR A  155 ? 0.1457 0.1909 0.1542 0.0141  -0.0150 0.0278  155 TYR A OH  
1233 N  N   . ASP A  156 ? 0.1690 0.2151 0.1644 0.0257  -0.0104 0.0316  156 ASP A N   
1234 C  CA  . ASP A  156 ? 0.1984 0.2483 0.1909 0.0314  -0.0057 0.0435  156 ASP A CA  
1235 C  C   . ASP A  156 ? 0.1859 0.2108 0.1919 0.0250  -0.0241 0.0378  156 ASP A C   
1236 O  O   . ASP A  156 ? 0.2226 0.2861 0.1835 -0.0026 -0.0295 0.0074  156 ASP A O   
1237 C  CB  . ASP A  156 ? 0.2199 0.3288 0.2178 0.0592  -0.0273 0.0866  156 ASP A CB  
1238 C  CG  . ASP A  156 ? 0.2643 0.3149 0.2123 0.0183  -0.0347 0.0556  156 ASP A CG  
1239 O  OD1 . ASP A  156 ? 0.2531 0.2926 0.1887 -0.0038 0.0026  0.0436  156 ASP A OD1 
1240 O  OD2 . ASP A  156 ? 0.3621 0.3863 0.2197 0.0554  -0.0513 0.0413  156 ASP A OD2 
1241 N  N   . LYS A  157 ? 0.1870 0.2537 0.1766 0.0166  -0.0245 0.0346  157 LYS A N   
1242 C  CA  . LYS A  157 ? 0.2469 0.2457 0.1763 -0.0380 -0.0253 0.0092  157 LYS A CA  
1243 C  C   . LYS A  157 ? 0.1976 0.2619 0.1941 -0.0122 0.0102  0.0297  157 LYS A C   
1244 O  O   . LYS A  157 ? 0.2360 0.2776 0.2989 -0.0264 -0.0102 0.0141  157 LYS A O   
1245 C  CB  . LYS A  157 ? 0.1682 0.2784 0.2158 -0.0205 -0.0059 0.0311  157 LYS A CB  
1246 C  CG  . LYS A  157 ? 0.2770 0.2947 0.2309 0.0275  0.0469  0.0414  157 LYS A CG  
1247 C  CD  . LYS A  157 ? 0.2215 0.3294 0.2124 0.0443  -0.0164 0.0355  157 LYS A CD  
1248 C  CE  . LYS A  157 ? 0.2742 0.3600 0.3181 0.0950  -0.0493 0.0329  157 LYS A CE  
1249 N  NZ  . LYS A  157 ? 0.3238 0.3960 0.2661 0.1206  -0.0573 0.0126  157 LYS A NZ  
1250 N  N   . ILE A  158 ? 0.2376 0.2599 0.1556 0.0074  0.0066  0.0339  158 ILE A N   
1251 C  CA  . ILE A  158 ? 0.2479 0.2289 0.1568 0.0074  0.0126  0.0367  158 ILE A CA  
1252 C  C   . ILE A  158 ? 0.2432 0.1898 0.1835 -0.0233 -0.0240 0.0040  158 ILE A C   
1253 O  O   . ILE A  158 ? 0.2463 0.2277 0.1635 -0.0174 -0.0074 0.0178  158 ILE A O   
1254 C  CB  . ILE A  158 ? 0.2868 0.2204 0.1743 0.0092  0.0086  0.0430  158 ILE A CB  
1255 C  CG1 . ILE A  158 ? 0.3718 0.2870 0.1843 0.0610  0.0555  0.0102  158 ILE A CG1 
1256 C  CG2 . ILE A  158 ? 0.2925 0.2436 0.1930 0.0447  -0.0203 0.0436  158 ILE A CG2 
1257 C  CD1 . ILE A  158 ? 0.4470 0.2666 0.1888 0.0463  -0.0061 0.0486  158 ILE A CD1 
1258 N  N   . PHE A  159 ? 0.1970 0.1961 0.1734 0.0006  -0.0138 0.0262  159 PHE A N   
1259 C  CA  . PHE A  159 ? 0.1923 0.2701 0.1655 -0.0271 -0.0122 0.0179  159 PHE A CA  
1260 C  C   . PHE A  159 ? 0.2270 0.2106 0.1726 0.0029  0.0055  0.0343  159 PHE A C   
1261 O  O   . PHE A  159 ? 0.2078 0.2499 0.1860 -0.0003 -0.0013 0.0134  159 PHE A O   
1262 C  CB  . PHE A  159 ? 0.1844 0.2140 0.1581 0.0055  -0.0251 0.0031  159 PHE A CB  
1263 C  CG  . PHE A  159 ? 0.1816 0.2161 0.1790 0.0076  -0.0190 -0.0020 159 PHE A CG  
1264 C  CD1 . PHE A  159 ? 0.2396 0.2594 0.2079 0.0256  -0.0497 0.0288  159 PHE A CD1 
1265 C  CD2 . PHE A  159 ? 0.1879 0.2769 0.1980 -0.0242 -0.0174 -0.0103 159 PHE A CD2 
1266 C  CE1 . PHE A  159 ? 0.2776 0.2467 0.1924 0.0790  -0.0598 0.0039  159 PHE A CE1 
1267 C  CE2 . PHE A  159 ? 0.1527 0.3211 0.1958 -0.0468 0.0049  0.0010  159 PHE A CE2 
1268 C  CZ  . PHE A  159 ? 0.2043 0.2843 0.1986 0.0527  0.0383  0.0117  159 PHE A CZ  
1269 N  N   . SER A  160 ? 0.2292 0.2314 0.1804 -0.0175 -0.0222 0.0523  160 SER A N   
1270 C  CA  . SER A  160 ? 0.2404 0.2812 0.1891 -0.0049 -0.0491 0.0282  160 SER A CA  
1271 C  C   . SER A  160 ? 0.2428 0.3269 0.1791 -0.0087 0.0005  0.0005  160 SER A C   
1272 O  O   . SER A  160 ? 0.2889 0.3317 0.1832 -0.0159 -0.0525 0.0020  160 SER A O   
1273 C  CB  . SER A  160 ? 0.2224 0.3321 0.2260 0.0023  -0.0457 0.0661  160 SER A CB  
1274 O  OG  . SER A  160 ? 0.2492 0.3614 0.2433 0.0179  0.0000  0.0422  160 SER A OG  
1275 N  N   . HIS A  161 ? 0.1960 0.2722 0.1927 -0.0414 -0.0251 0.0027  161 HIS A N   
1276 C  CA  . HIS A  161 ? 0.2338 0.2615 0.1731 -0.0409 -0.0038 0.0115  161 HIS A CA  
1277 C  C   . HIS A  161 ? 0.2646 0.2671 0.1813 -0.0187 -0.0021 -0.0001 161 HIS A C   
1278 O  O   . HIS A  161 ? 0.2370 0.2722 0.2098 -0.0268 0.0137  -0.0285 161 HIS A O   
1279 C  CB  . HIS A  161 ? 0.2217 0.2667 0.1831 0.0088  0.0075  0.0254  161 HIS A CB  
1280 C  CG  . HIS A  161 ? 0.1908 0.2545 0.2509 -0.0234 -0.0016 -0.0189 161 HIS A CG  
1281 N  ND1 . HIS A  161 ? 0.2906 0.3723 0.2852 -0.0406 -0.0664 -0.0259 161 HIS A ND1 
1282 C  CD2 . HIS A  161 ? 0.2241 0.2748 0.2870 0.0104  0.0076  -0.0085 161 HIS A CD2 
1283 C  CE1 . HIS A  161 ? 0.2800 0.3480 0.3326 -0.0300 -0.0079 -0.0380 161 HIS A CE1 
1284 N  NE2 . HIS A  161 ? 0.2294 0.2810 0.3420 0.0150  -0.0061 -0.0079 161 HIS A NE2 
1285 N  N   . LEU A  162 ? 0.2270 0.2298 0.2026 -0.0043 -0.0143 0.0041  162 LEU A N   
1286 C  CA  . LEU A  162 ? 0.2309 0.2133 0.1945 -0.0144 0.0242  -0.0111 162 LEU A CA  
1287 C  C   . LEU A  162 ? 0.2508 0.2750 0.1910 -0.0206 0.0345  0.0016  162 LEU A C   
1288 O  O   . LEU A  162 ? 0.2218 0.2452 0.2229 -0.0315 0.0092  -0.0141 162 LEU A O   
1289 C  CB  . LEU A  162 ? 0.2527 0.2892 0.2096 -0.0008 0.0225  -0.0325 162 LEU A CB  
1290 C  CG  . LEU A  162 ? 0.2575 0.2039 0.2246 0.0113  -0.0391 -0.0122 162 LEU A CG  
1291 C  CD1 . LEU A  162 ? 0.2764 0.2646 0.3238 0.0036  -0.0440 -0.1126 162 LEU A CD1 
1292 C  CD2 . LEU A  162 ? 0.4682 0.3032 0.2541 0.0965  -0.0735 0.0277  162 LEU A CD2 
1293 N  N   . GLN A  163 ? 0.2603 0.2713 0.2111 -0.0762 -0.0051 -0.0044 163 GLN A N   
1294 C  CA  . GLN A  163 ? 0.3326 0.3324 0.1608 -0.0787 -0.0027 0.0010  163 GLN A CA  
1295 C  C   . GLN A  163 ? 0.3495 0.3255 0.2449 -0.0653 0.0443  -0.0337 163 GLN A C   
1296 O  O   . GLN A  163 ? 0.4545 0.4764 0.4066 -0.2330 0.2167  -0.1934 163 GLN A O   
1297 C  CB  . GLN A  163 ? 0.3916 0.4014 0.2855 -0.0779 -0.0034 0.1037  163 GLN A CB  
1298 C  CG  . GLN A  163 ? 0.3445 0.3660 0.3798 -0.0165 -0.0607 0.0986  163 GLN A CG  
1299 C  CD  . GLN A  163 ? 0.4352 0.6504 0.4574 0.0732  -0.0944 0.1472  163 GLN A CD  
1300 O  OE1 . GLN A  163 ? 0.4950 0.3739 0.3930 -0.1083 -0.1000 0.0097  163 GLN A OE1 
1301 N  NE2 . GLN A  163 ? 0.6388 0.5860 0.5035 0.1105  -0.0174 0.1631  163 GLN A NE2 
1302 N  N   . HIS A  164 ? 0.2238 0.2669 0.2169 -0.0207 -0.0385 -0.0215 164 HIS A N   
1303 C  CA  . HIS A  164 ? 0.2789 0.2557 0.1898 -0.0072 -0.0522 -0.0369 164 HIS A CA  
1304 C  C   . HIS A  164 ? 0.2667 0.2486 0.1949 -0.0392 -0.0644 -0.0022 164 HIS A C   
1305 O  O   . HIS A  164 ? 0.2649 0.3143 0.2364 -0.0762 -0.0571 -0.0029 164 HIS A O   
1306 C  CB  . HIS A  164 ? 0.2267 0.3033 0.2328 -0.0317 -0.0106 -0.0082 164 HIS A CB  
1307 C  CG  . HIS A  164 ? 0.2168 0.2592 0.2247 -0.0326 -0.0015 -0.0068 164 HIS A CG  
1308 N  ND1 . HIS A  164 ? 0.2078 0.3033 0.2527 -0.0251 -0.0414 -0.0023 164 HIS A ND1 
1309 C  CD2 . HIS A  164 ? 0.2744 0.2785 0.2544 0.0128  -0.0586 -0.0271 164 HIS A CD2 
1310 C  CE1 . HIS A  164 ? 0.2424 0.2170 0.2702 -0.0184 -0.0329 0.0061  164 HIS A CE1 
1311 N  NE2 . HIS A  164 ? 0.4856 0.3680 0.3925 0.0933  0.0212  0.0564  164 HIS A NE2 
1312 N  N   . VAL A  165 ? 0.1981 0.2637 0.1916 -0.0294 -0.0222 -0.0058 165 VAL A N   
1313 C  CA  . VAL A  165 ? 0.2053 0.2267 0.2132 -0.0285 -0.0089 0.0107  165 VAL A CA  
1314 C  C   . VAL A  165 ? 0.2090 0.2232 0.1717 -0.0188 -0.0328 -0.0142 165 VAL A C   
1315 O  O   . VAL A  165 ? 0.2040 0.2446 0.1770 -0.0209 0.0061  -0.0100 165 VAL A O   
1316 C  CB  . VAL A  165 ? 0.2209 0.2773 0.2258 0.0366  0.0403  0.0290  165 VAL A CB  
1317 C  CG1 . VAL A  165 ? 0.1953 0.2723 0.2748 0.0002  0.0041  -0.0217 165 VAL A CG1 
1318 C  CG2 . VAL A  165 ? 0.2146 0.3087 0.1639 -0.0186 0.0006  -0.0383 165 VAL A CG2 
1319 N  N   . LYS A  166 ? 0.1775 0.2795 0.1947 -0.0342 0.0012  -0.0240 166 LYS A N   
1320 C  CA  . LYS A  166 ? 0.1914 0.2797 0.1865 -0.0320 -0.0121 0.0010  166 LYS A CA  
1321 C  C   . LYS A  166 ? 0.1947 0.2206 0.1648 -0.0526 -0.0125 -0.0149 166 LYS A C   
1322 O  O   . LYS A  166 ? 0.1949 0.2461 0.2224 -0.0214 -0.0124 -0.0347 166 LYS A O   
1323 C  CB  . LYS A  166 ? 0.2263 0.2834 0.1940 -0.0609 0.0495  0.0153  166 LYS A CB  
1324 C  CG  . LYS A  166 ? 0.2761 0.2694 0.1914 -0.0566 0.0154  -0.0302 166 LYS A CG  
1325 C  CD  . LYS A  166 ? 0.2978 0.3545 0.2244 -0.0864 -0.0073 -0.0092 166 LYS A CD  
1326 C  CE  . LYS A  166 ? 0.5811 0.4492 0.1778 -0.0659 -0.0107 0.0256  166 LYS A CE  
1327 N  NZ  . LYS A  166 ? 0.8433 0.7108 0.6196 -0.1899 -0.0988 -0.1675 166 LYS A NZ  
1328 N  N   . TYR A  167 ? 0.2552 0.1857 0.1861 -0.0395 0.0095  -0.0337 167 TYR A N   
1329 C  CA  . TYR A  167 ? 0.2548 0.1962 0.1784 -0.0551 -0.0157 -0.0105 167 TYR A CA  
1330 C  C   . TYR A  167 ? 0.2067 0.2401 0.1617 -0.0299 -0.0238 -0.0080 167 TYR A C   
1331 O  O   . TYR A  167 ? 0.2111 0.2630 0.1730 -0.0163 -0.0234 -0.0044 167 TYR A O   
1332 C  CB  . TYR A  167 ? 0.2922 0.2314 0.1426 -0.0396 0.0203  -0.0197 167 TYR A CB  
1333 C  CG  . TYR A  167 ? 0.2135 0.2217 0.1858 -0.0350 0.0074  -0.0434 167 TYR A CG  
1334 C  CD1 . TYR A  167 ? 0.2300 0.2600 0.2005 -0.0359 0.0061  -0.0697 167 TYR A CD1 
1335 C  CD2 . TYR A  167 ? 0.3054 0.2271 0.1596 -0.0471 -0.0105 -0.0099 167 TYR A CD2 
1336 C  CE1 . TYR A  167 ? 0.2303 0.2863 0.2205 -0.0151 0.0324  -0.0343 167 TYR A CE1 
1337 C  CE2 . TYR A  167 ? 0.2901 0.3067 0.2520 -0.0908 0.0345  -0.0688 167 TYR A CE2 
1338 C  CZ  . TYR A  167 ? 0.3013 0.2696 0.1895 -0.0673 0.0088  -0.0333 167 TYR A CZ  
1339 O  OH  . TYR A  167 ? 0.3180 0.3262 0.2360 -0.0622 0.0361  -0.0183 167 TYR A OH  
1340 N  N   . LYS A  168 ? 0.2306 0.2224 0.2017 -0.0211 -0.0310 -0.0043 168 LYS A N   
1341 C  CA  . LYS A  168 ? 0.2604 0.2070 0.2576 -0.0388 -0.0281 0.0361  168 LYS A CA  
1342 C  C   . LYS A  168 ? 0.3333 0.1973 0.2195 -0.0766 0.0165  -0.0184 168 LYS A C   
1343 O  O   . LYS A  168 ? 0.2848 0.2185 0.2509 -0.0271 -0.0177 -0.0284 168 LYS A O   
1344 C  CB  . LYS A  168 ? 0.2618 0.2396 0.2338 0.0020  -0.0027 -0.0353 168 LYS A CB  
1345 C  CG  . LYS A  168 ? 0.2599 0.2238 0.2727 -0.0403 -0.0508 0.0199  168 LYS A CG  
1346 C  CD  . LYS A  168 ? 0.3405 0.2961 0.3100 -0.0197 -0.0751 0.0776  168 LYS A CD  
1347 C  CE  . LYS A  168 ? 0.6381 0.4261 0.3951 -0.0170 -0.1398 0.2422  168 LYS A CE  
1348 N  NZ  . LYS A  168 ? 0.6118 0.4684 0.3811 0.0701  -0.0093 0.0886  168 LYS A NZ  
1349 N  N   . GLY A  169 ? 0.2558 0.2612 0.2068 -0.0487 -0.0026 0.0257  169 GLY A N   
1350 C  CA  . GLY A  169 ? 0.2904 0.2329 0.2981 -0.0647 0.0138  0.0145  169 GLY A CA  
1351 C  C   . GLY A  169 ? 0.2872 0.2633 0.3138 -0.0715 -0.0044 0.0326  169 GLY A C   
1352 O  O   . GLY A  169 ? 0.2922 0.2949 0.4498 -0.0796 -0.0222 0.0704  169 GLY A O   
1353 N  N   . GLN A  170 ? 0.2540 0.2499 0.1858 -0.0256 -0.0147 0.0009  170 GLN A N   
1354 C  CA  . GLN A  170 ? 0.2245 0.2399 0.2103 -0.0431 -0.0271 0.0043  170 GLN A CA  
1355 C  C   . GLN A  170 ? 0.2070 0.2963 0.1900 -0.0391 -0.0234 -0.0137 170 GLN A C   
1356 O  O   . GLN A  170 ? 0.2212 0.3162 0.1846 -0.0174 -0.0504 -0.0183 170 GLN A O   
1357 C  CB  . GLN A  170 ? 0.2087 0.2322 0.2046 -0.0398 0.0136  -0.0161 170 GLN A CB  
1358 C  CG  . GLN A  170 ? 0.2503 0.2459 0.1958 -0.0311 0.0033  -0.0244 170 GLN A CG  
1359 C  CD  . GLN A  170 ? 0.2752 0.2218 0.2079 -0.0462 0.0006  -0.0326 170 GLN A CD  
1360 O  OE1 . GLN A  170 ? 0.2244 0.2717 0.2049 -0.0548 -0.0366 0.0040  170 GLN A OE1 
1361 N  NE2 . GLN A  170 ? 0.3240 0.3516 0.2093 -0.1233 0.0249  -0.1021 170 GLN A NE2 
1362 N  N   A GLU A  171 ? 0.1822 0.3547 0.1886 -0.0697 -0.0738 -0.0848 171 GLU A N   
1363 N  N   B GLU A  171 ? 0.1993 0.3500 0.1710 0.0074  0.0097  -0.0093 171 GLU A N   
1364 C  CA  A GLU A  171 ? 0.1905 0.3225 0.1554 -0.0266 -0.0565 -0.0093 171 GLU A CA  
1365 C  CA  B GLU A  171 ? 0.2359 0.2964 0.1737 -0.0062 0.0563  0.0378  171 GLU A CA  
1366 C  C   A GLU A  171 ? 0.2503 0.2622 0.1321 -0.0344 -0.0289 0.0427  171 GLU A C   
1367 C  C   B GLU A  171 ? 0.1751 0.3121 0.1454 -0.0097 -0.0407 -0.0345 171 GLU A C   
1368 O  O   A GLU A  171 ? 0.2419 0.2949 0.1779 -0.0524 -0.0691 0.0212  171 GLU A O   
1369 O  O   B GLU A  171 ? 0.2293 0.2969 0.1565 -0.0318 -0.0256 -0.0074 171 GLU A O   
1370 C  CB  A GLU A  171 ? 0.3211 0.2864 0.2085 -0.0602 0.0159  -0.0866 171 GLU A CB  
1371 C  CB  B GLU A  171 ? 0.1995 0.3413 0.2678 -0.0558 0.0194  -0.0013 171 GLU A CB  
1372 C  CG  A GLU A  171 ? 0.3299 0.4068 0.3006 -0.0864 0.0212  0.0647  171 GLU A CG  
1373 C  CG  B GLU A  171 ? 0.2250 0.4041 0.2087 -0.0497 -0.0111 -0.0286 171 GLU A CG  
1374 C  CD  A GLU A  171 ? 0.4095 0.2274 0.2913 -0.0006 0.0690  0.0005  171 GLU A CD  
1375 C  CD  B GLU A  171 ? 0.2491 0.4294 0.3050 -0.0183 -0.0817 0.0875  171 GLU A CD  
1376 O  OE1 A GLU A  171 ? 0.3729 0.3855 0.4309 0.0151  0.0267  0.0932  171 GLU A OE1 
1377 O  OE1 B GLU A  171 ? 0.3033 0.3210 0.3034 -0.0207 -0.1004 0.0443  171 GLU A OE1 
1378 O  OE2 A GLU A  171 ? 0.3948 0.3079 0.2861 -0.0039 0.0289  0.0314  171 GLU A OE2 
1379 O  OE2 B GLU A  171 ? 0.2478 0.4845 0.2070 -0.1322 -0.0729 -0.0110 171 GLU A OE2 
1380 N  N   . ALA A  172 ? 0.2197 0.3383 0.1564 0.0159  -0.0186 0.0049  172 ALA A N   
1381 C  CA  . ALA A  172 ? 0.2041 0.2829 0.2086 -0.0031 -0.0453 0.0244  172 ALA A CA  
1382 C  C   . ALA A  172 ? 0.1842 0.3421 0.1903 -0.0026 -0.0237 0.0203  172 ALA A C   
1383 O  O   . ALA A  172 ? 0.2126 0.3901 0.1604 0.0238  -0.0501 0.0083  172 ALA A O   
1384 C  CB  . ALA A  172 ? 0.2321 0.3003 0.2615 0.0263  -0.0069 0.0867  172 ALA A CB  
1385 N  N   . PHE A  173 ? 0.2193 0.3671 0.1527 0.0340  -0.0314 0.0149  173 PHE A N   
1386 C  CA  . PHE A  173 ? 0.1662 0.3492 0.2121 -0.0006 -0.0322 0.0055  173 PHE A CA  
1387 C  C   . PHE A  173 ? 0.2314 0.3362 0.2116 0.0367  -0.0435 0.0185  173 PHE A C   
1388 O  O   . PHE A  173 ? 0.3540 0.4370 0.2010 -0.0017 -0.0590 0.0641  173 PHE A O   
1389 C  CB  . PHE A  173 ? 0.1720 0.4171 0.2696 -0.0237 -0.0329 -0.0165 173 PHE A CB  
1390 C  CG  . PHE A  173 ? 0.1999 0.3571 0.3026 -0.0535 -0.1017 -0.0374 173 PHE A CG  
1391 C  CD1 . PHE A  173 ? 0.2825 0.3793 0.3829 -0.0199 -0.0701 0.1175  173 PHE A CD1 
1392 C  CD2 . PHE A  173 ? 0.3224 0.4539 0.5319 0.0800  -0.2319 -0.0995 173 PHE A CD2 
1393 C  CE1 . PHE A  173 ? 0.2874 0.3560 0.3263 0.0395  -0.1245 0.0373  173 PHE A CE1 
1394 C  CE2 . PHE A  173 ? 0.4855 0.3772 0.3831 0.0351  -0.0535 -0.0842 173 PHE A CE2 
1395 C  CZ  . PHE A  173 ? 0.4124 0.6026 0.3458 -0.0261 -0.0229 -0.1061 173 PHE A CZ  
1396 N  N   . VAL A  174 ? 0.2122 0.3018 0.1936 0.0051  -0.0168 -0.0039 174 VAL A N   
1397 C  CA  . VAL A  174 ? 0.1732 0.3037 0.1998 -0.0157 -0.0145 0.0288  174 VAL A CA  
1398 C  C   . VAL A  174 ? 0.1502 0.3590 0.2025 -0.0150 -0.0286 0.0763  174 VAL A C   
1399 O  O   . VAL A  174 ? 0.1690 0.3899 0.2087 -0.0249 -0.0231 0.0493  174 VAL A O   
1400 C  CB  . VAL A  174 ? 0.1854 0.3383 0.1784 0.0200  -0.0294 -0.0054 174 VAL A CB  
1401 C  CG1 . VAL A  174 ? 0.2203 0.3615 0.2289 -0.0111 -0.0353 -0.0190 174 VAL A CG1 
1402 C  CG2 . VAL A  174 ? 0.2068 0.3468 0.2356 0.0144  0.0206  0.0643  174 VAL A CG2 
1403 N  N   . PRO A  175 ? 0.1924 0.3449 0.2036 0.0456  -0.0258 0.0238  175 PRO A N   
1404 C  CA  . PRO A  175 ? 0.1930 0.3595 0.1821 0.0346  -0.0367 0.0207  175 PRO A CA  
1405 C  C   . PRO A  175 ? 0.1924 0.3741 0.1229 -0.0145 -0.0473 0.0463  175 PRO A C   
1406 O  O   . PRO A  175 ? 0.1910 0.3224 0.2071 -0.0067 -0.0441 0.0167  175 PRO A O   
1407 C  CB  . PRO A  175 ? 0.2388 0.4527 0.1936 0.0665  -0.0078 0.0978  175 PRO A CB  
1408 C  CG  . PRO A  175 ? 0.2549 0.4927 0.2652 0.1242  -0.0196 0.0987  175 PRO A CG  
1409 C  CD  . PRO A  175 ? 0.2243 0.3068 0.2654 0.0281  -0.0546 0.0991  175 PRO A CD  
1410 N  N   . GLY A  176 ? 0.1775 0.3689 0.1822 0.0166  -0.0414 0.0179  176 GLY A N   
1411 C  CA  . GLY A  176 ? 0.1838 0.2975 0.1743 -0.0113 -0.0323 0.0357  176 GLY A CA  
1412 C  C   . GLY A  176 ? 0.2032 0.2904 0.2014 0.0073  -0.0348 0.0558  176 GLY A C   
1413 O  O   . GLY A  176 ? 0.1990 0.3249 0.2772 0.0149  -0.0695 0.0638  176 GLY A O   
1414 N  N   . PHE A  177 ? 0.1548 0.2864 0.2253 -0.0109 -0.0491 0.0311  177 PHE A N   
1415 C  CA  . PHE A  177 ? 0.1627 0.3181 0.1840 0.0083  -0.0267 0.0429  177 PHE A CA  
1416 C  C   . PHE A  177 ? 0.1593 0.2543 0.1907 0.0201  -0.0055 0.0297  177 PHE A C   
1417 O  O   . PHE A  177 ? 0.1644 0.2676 0.2233 0.0126  -0.0156 0.0578  177 PHE A O   
1418 C  CB  . PHE A  177 ? 0.1809 0.3406 0.2110 0.0113  -0.0464 0.0517  177 PHE A CB  
1419 C  CG  . PHE A  177 ? 0.1852 0.2909 0.1992 -0.0096 -0.0301 0.0378  177 PHE A CG  
1420 C  CD1 . PHE A  177 ? 0.1622 0.2996 0.1917 0.0044  -0.0100 0.0637  177 PHE A CD1 
1421 C  CD2 . PHE A  177 ? 0.1985 0.3243 0.1972 -0.0013 -0.0179 0.0537  177 PHE A CD2 
1422 C  CE1 . PHE A  177 ? 0.1750 0.3438 0.2187 0.0162  -0.0296 0.0483  177 PHE A CE1 
1423 C  CE2 . PHE A  177 ? 0.2033 0.3396 0.1657 -0.0091 -0.0063 0.0266  177 PHE A CE2 
1424 C  CZ  . PHE A  177 ? 0.1829 0.3089 0.1665 0.0053  -0.0204 0.0343  177 PHE A CZ  
1425 N  N   . ASN A  178 ? 0.1701 0.2919 0.2299 0.0405  -0.0411 0.0294  178 ASN A N   
1426 C  CA  . ASN A  178 ? 0.1645 0.2474 0.2186 0.0523  -0.0227 -0.0033 178 ASN A CA  
1427 C  C   . ASN A  178 ? 0.1878 0.2129 0.2200 0.0122  -0.0357 0.0505  178 ASN A C   
1428 O  O   . ASN A  178 ? 0.1785 0.2250 0.1931 0.0439  -0.0131 0.0403  178 ASN A O   
1429 C  CB  . ASN A  178 ? 0.2115 0.2366 0.2542 0.0721  -0.0480 0.0190  178 ASN A CB  
1430 C  CG  . ASN A  178 ? 0.1769 0.2779 0.2310 0.0807  0.0104  0.0365  178 ASN A CG  
1431 O  OD1 . ASN A  178 ? 0.1938 0.2800 0.2512 0.0792  -0.0023 0.0555  178 ASN A OD1 
1432 N  ND2 . ASN A  178 ? 0.2931 0.2606 0.3446 0.1042  -0.0040 0.0434  178 ASN A ND2 
1433 N  N   . ILE A  179 ? 0.1398 0.2256 0.1891 0.0307  -0.0071 0.0400  179 ILE A N   
1434 C  CA  . ILE A  179 ? 0.1283 0.2091 0.2066 0.0219  -0.0176 0.0575  179 ILE A CA  
1435 C  C   . ILE A  179 ? 0.1267 0.1827 0.1923 0.0218  -0.0078 0.0373  179 ILE A C   
1436 O  O   . ILE A  179 ? 0.1235 0.1917 0.1840 0.0018  -0.0059 0.0419  179 ILE A O   
1437 C  CB  . ILE A  179 ? 0.1370 0.2090 0.1911 0.0183  -0.0253 0.0377  179 ILE A CB  
1438 C  CG1 . ILE A  179 ? 0.1358 0.2259 0.2146 0.0197  0.0237  0.0006  179 ILE A CG1 
1439 C  CG2 . ILE A  179 ? 0.1301 0.2424 0.2154 0.0485  0.0122  0.0640  179 ILE A CG2 
1440 C  CD1 . ILE A  179 ? 0.1733 0.2315 0.2050 -0.0009 -0.0042 0.0144  179 ILE A CD1 
1441 N  N   . GLU A  180 ? 0.1499 0.2144 0.1749 0.0401  0.0032  0.0362  180 GLU A N   
1442 C  CA  . GLU A  180 ? 0.1558 0.1930 0.2052 0.0367  0.0179  0.0381  180 GLU A CA  
1443 C  C   . GLU A  180 ? 0.1799 0.1915 0.1958 0.0446  0.0274  0.0109  180 GLU A C   
1444 O  O   . GLU A  180 ? 0.1689 0.2062 0.2313 0.0396  0.0218  0.0184  180 GLU A O   
1445 C  CB  . GLU A  180 ? 0.1791 0.2531 0.2077 0.0469  0.0385  0.0006  180 GLU A CB  
1446 C  CG  . GLU A  180 ? 0.2579 0.2675 0.2672 0.0876  0.0121  0.0102  180 GLU A CG  
1447 C  CD  . GLU A  180 ? 0.2963 0.2319 0.2717 0.0844  0.0192  0.0277  180 GLU A CD  
1448 O  OE1 . GLU A  180 ? 0.3044 0.3621 0.3386 0.0863  0.1035  0.0072  180 GLU A OE1 
1449 O  OE2 . GLU A  180 ? 0.3583 0.3653 0.2822 0.1064  0.0376  -0.0304 180 GLU A OE2 
1450 N  N   . GLU A  181 ? 0.1687 0.2166 0.1755 0.0471  0.0195  0.0499  181 GLU A N   
1451 C  CA  . GLU A  181 ? 0.1394 0.2090 0.2306 0.0269  0.0133  0.0491  181 GLU A CA  
1452 C  C   . GLU A  181 ? 0.1604 0.1488 0.1886 0.0363  0.0197  0.0250  181 GLU A C   
1453 O  O   . GLU A  181 ? 0.1668 0.1741 0.2490 0.0314  0.0168  0.0487  181 GLU A O   
1454 C  CB  . GLU A  181 ? 0.1782 0.2854 0.2144 0.0748  0.0072  0.0838  181 GLU A CB  
1455 C  CG  . GLU A  181 ? 0.2041 0.2521 0.2435 0.0717  -0.0059 0.0857  181 GLU A CG  
1456 C  CD  . GLU A  181 ? 0.2460 0.3145 0.2837 0.0889  -0.0111 0.0683  181 GLU A CD  
1457 O  OE1 . GLU A  181 ? 0.2684 0.4353 0.2536 0.1015  -0.0286 0.0332  181 GLU A OE1 
1458 O  OE2 . GLU A  181 ? 0.2414 0.3632 0.3667 0.0863  -0.0147 0.1542  181 GLU A OE2 
1459 N  N   . LEU A  182 ? 0.1333 0.1634 0.1784 0.0354  0.0059  0.0309  182 LEU A N   
1460 C  CA  . LEU A  182 ? 0.1339 0.1576 0.1553 0.0365  -0.0057 0.0144  182 LEU A CA  
1461 C  C   . LEU A  182 ? 0.1572 0.1469 0.1688 0.0208  -0.0075 0.0223  182 LEU A C   
1462 O  O   . LEU A  182 ? 0.1550 0.1723 0.1566 0.0187  0.0046  0.0270  182 LEU A O   
1463 C  CB  . LEU A  182 ? 0.1525 0.1435 0.1485 0.0295  -0.0089 0.0228  182 LEU A CB  
1464 C  CG  . LEU A  182 ? 0.1656 0.1512 0.1379 0.0073  -0.0036 0.0193  182 LEU A CG  
1465 C  CD1 . LEU A  182 ? 0.1642 0.1723 0.1909 -0.0032 -0.0068 0.0176  182 LEU A CD1 
1466 C  CD2 . LEU A  182 ? 0.1788 0.2053 0.1647 0.0195  -0.0055 0.0221  182 LEU A CD2 
1467 N  N   . LEU A  183 ? 0.1615 0.1750 0.1609 0.0242  0.0031  0.0049  183 LEU A N   
1468 C  CA  . LEU A  183 ? 0.1621 0.1628 0.1841 0.0297  -0.0012 0.0192  183 LEU A CA  
1469 C  C   . LEU A  183 ? 0.1565 0.1707 0.1737 0.0212  0.0081  0.0150  183 LEU A C   
1470 O  O   . LEU A  183 ? 0.2304 0.1567 0.1878 0.0412  -0.0095 0.0193  183 LEU A O   
1471 C  CB  . LEU A  183 ? 0.2112 0.1681 0.1873 0.0175  0.0286  0.0306  183 LEU A CB  
1472 C  CG  . LEU A  183 ? 0.2241 0.1645 0.1759 0.0121  0.0323  0.0020  183 LEU A CG  
1473 C  CD1 . LEU A  183 ? 0.2573 0.2324 0.2222 0.0013  0.0730  0.0294  183 LEU A CD1 
1474 C  CD2 . LEU A  183 ? 0.2085 0.1592 0.2465 0.0153  0.0280  0.0070  183 LEU A CD2 
1475 N  N   . PRO A  184 ? 0.1638 0.1764 0.1673 0.0155  0.0096  0.0254  184 PRO A N   
1476 C  CA  . PRO A  184 ? 0.1823 0.1797 0.1996 0.0035  0.0082  0.0398  184 PRO A CA  
1477 C  C   . PRO A  184 ? 0.2787 0.1840 0.2593 0.0060  0.0073  0.0682  184 PRO A C   
1478 O  O   . PRO A  184 ? 0.2971 0.1573 0.2434 0.0198  0.0447  0.0105  184 PRO A O   
1479 C  CB  . PRO A  184 ? 0.2243 0.2403 0.2500 -0.0259 -0.0403 0.0688  184 PRO A CB  
1480 C  CG  . PRO A  184 ? 0.2185 0.2053 0.1992 -0.0048 -0.0142 0.0268  184 PRO A CG  
1481 C  CD  . PRO A  184 ? 0.1536 0.1909 0.1948 0.0632  -0.0138 0.0209  184 PRO A CD  
1482 N  N   . GLU A  185 ? 0.2618 0.1675 0.3114 0.0329  -0.0015 0.0059  185 GLU A N   
1483 C  CA  . GLU A  185 ? 0.3000 0.1949 0.2787 0.0188  -0.0127 0.0127  185 GLU A CA  
1484 C  C   . GLU A  185 ? 0.3001 0.2214 0.2335 0.0463  0.0152  0.0452  185 GLU A C   
1485 O  O   . GLU A  185 ? 0.2517 0.2136 0.3222 0.0384  -0.0179 0.0001  185 GLU A O   
1486 C  CB  . GLU A  185 ? 0.4947 0.2311 0.2638 -0.0325 0.0375  0.0337  185 GLU A CB  
1487 C  CG  . GLU A  185 ? 0.6991 0.3477 0.3190 0.1544  0.0211  0.0274  185 GLU A CG  
1488 C  CD  . GLU A  185 ? 0.8072 0.4691 0.5659 0.0504  -0.1380 -0.0668 185 GLU A CD  
1489 O  OE1 . GLU A  185 ? 1.1140 0.7709 0.4503 0.2901  -0.0857 0.0999  185 GLU A OE1 
1490 O  OE2 . GLU A  185 ? 0.6682 0.6613 0.6106 0.0958  -0.1148 -0.2075 185 GLU A OE2 
1491 N  N   . ARG A  186 ? 0.2387 0.1561 0.3089 0.0340  0.0305  -0.0018 186 ARG A N   
1492 C  CA  . ARG A  186 ? 0.2966 0.1840 0.3386 0.0197  0.0340  -0.0002 186 ARG A CA  
1493 C  C   . ARG A  186 ? 0.1856 0.2108 0.3531 0.0428  0.0359  0.0088  186 ARG A C   
1494 O  O   . ARG A  186 ? 0.2309 0.2030 0.2413 0.0013  0.0197  -0.0147 186 ARG A O   
1495 C  CB  . ARG A  186 ? 0.2724 0.1894 0.4329 0.0362  0.0555  -0.0225 186 ARG A CB  
1496 C  CG  . ARG A  186 ? 0.5266 0.1807 0.5928 -0.0345 -0.0566 -0.0234 186 ARG A CG  
1497 C  CD  . ARG A  186 ? 0.4877 0.2034 0.5360 -0.0436 -0.0249 -0.0551 186 ARG A CD  
1498 N  NE  . ARG A  186 ? 0.5765 0.3163 0.5668 -0.0316 0.0111  0.0256  186 ARG A NE  
1499 C  CZ  . ARG A  186 ? 0.5674 0.3204 0.6220 0.1446  0.1113  -0.0278 186 ARG A CZ  
1500 N  NH1 . ARG A  186 ? 0.7808 0.4145 0.5392 -0.0575 0.0133  0.1782  186 ARG A NH1 
1501 N  NH2 . ARG A  186 ? 0.4666 0.2614 0.9000 -0.0333 0.1596  -0.0609 186 ARG A NH2 
1502 N  N   . THR A  187 ? 0.2022 0.1837 0.2137 0.0308  0.0370  -0.0146 187 THR A N   
1503 C  CA  . THR A  187 ? 0.2146 0.1770 0.2037 0.0410  0.0039  -0.0053 187 THR A CA  
1504 C  C   . THR A  187 ? 0.2039 0.2212 0.2138 0.0605  -0.0020 -0.0266 187 THR A C   
1505 O  O   . THR A  187 ? 0.2346 0.2061 0.1875 0.0403  0.0195  -0.0055 187 THR A O   
1506 C  CB  . THR A  187 ? 0.1684 0.2330 0.2008 0.0236  0.0251  -0.0121 187 THR A CB  
1507 O  OG1 . THR A  187 ? 0.1952 0.2474 0.2751 0.0434  -0.0003 -0.0201 187 THR A OG1 
1508 C  CG2 . THR A  187 ? 0.2615 0.2063 0.1786 -0.0086 0.0139  -0.0227 187 THR A CG2 
1509 N  N   . ALA A  188 ? 0.2493 0.2365 0.1990 0.0739  0.0058  -0.0100 188 ALA A N   
1510 C  CA  . ALA A  188 ? 0.2357 0.2499 0.2032 0.0991  -0.0027 -0.0257 188 ALA A CA  
1511 C  C   . ALA A  188 ? 0.2187 0.2018 0.1884 0.0418  0.0175  -0.0438 188 ALA A C   
1512 O  O   . ALA A  188 ? 0.2058 0.2101 0.2010 0.0271  0.0211  -0.0270 188 ALA A O   
1513 C  CB  . ALA A  188 ? 0.3323 0.2573 0.2341 0.1263  0.0286  -0.0494 188 ALA A CB  
1514 N  N   . GLU A  189 ? 0.2238 0.1661 0.2086 0.0636  0.0323  -0.0175 189 GLU A N   
1515 C  CA  . GLU A  189 ? 0.2049 0.1370 0.2515 0.0339  0.0376  0.0042  189 GLU A CA  
1516 C  C   . GLU A  189 ? 0.1821 0.1425 0.1860 0.0176  0.0251  0.0025  189 GLU A C   
1517 O  O   . GLU A  189 ? 0.1729 0.1504 0.1865 0.0179  0.0177  0.0047  189 GLU A O   
1518 C  CB  . GLU A  189 ? 0.2852 0.1608 0.2613 0.0205  0.0837  0.0154  189 GLU A CB  
1519 C  CG  . GLU A  189 ? 0.3734 0.1886 0.4194 0.0282  0.1074  -0.0449 189 GLU A CG  
1520 C  CD  . GLU A  189 ? 0.4205 0.2297 0.3607 -0.0810 0.1495  -0.0806 189 GLU A CD  
1521 O  OE1 . GLU A  189 ? 0.3772 0.2678 0.3441 0.0439  0.0647  0.0052  189 GLU A OE1 
1522 O  OE2 . GLU A  189 ? 0.4809 0.3387 0.5097 -0.0128 0.0996  -0.1638 189 GLU A OE2 
1523 N  N   . TYR A  190 ? 0.1966 0.1477 0.1634 0.0156  0.0255  -0.0013 190 TYR A N   
1524 C  CA  . TYR A  190 ? 0.1516 0.1344 0.1643 0.0046  0.0048  -0.0095 190 TYR A CA  
1525 C  C   . TYR A  190 ? 0.1644 0.1383 0.1487 -0.0055 0.0082  -0.0100 190 TYR A C   
1526 O  O   . TYR A  190 ? 0.1982 0.1573 0.1554 -0.0052 0.0124  -0.0091 190 TYR A O   
1527 C  CB  . TYR A  190 ? 0.1593 0.1508 0.1400 0.0063  0.0136  -0.0138 190 TYR A CB  
1528 C  CG  . TYR A  190 ? 0.1750 0.1484 0.1288 0.0061  0.0113  -0.0157 190 TYR A CG  
1529 C  CD1 . TYR A  190 ? 0.1822 0.1446 0.1679 -0.0160 0.0201  -0.0125 190 TYR A CD1 
1530 C  CD2 . TYR A  190 ? 0.1712 0.1898 0.1886 0.0115  0.0400  -0.0021 190 TYR A CD2 
1531 C  CE1 . TYR A  190 ? 0.1904 0.1592 0.1555 0.0083  0.0065  -0.0205 190 TYR A CE1 
1532 C  CE2 . TYR A  190 ? 0.1831 0.1861 0.1961 0.0095  0.0562  -0.0035 190 TYR A CE2 
1533 C  CZ  . TYR A  190 ? 0.1869 0.1739 0.1734 -0.0081 0.0197  -0.0352 190 TYR A CZ  
1534 O  OH  . TYR A  190 ? 0.2025 0.2021 0.1836 -0.0234 0.0491  -0.0298 190 TYR A OH  
1535 N  N   . TYR A  191 ? 0.1697 0.1258 0.1430 -0.0032 0.0099  -0.0065 191 TYR A N   
1536 C  CA  . TYR A  191 ? 0.1483 0.1294 0.1574 -0.0048 0.0025  0.0227  191 TYR A CA  
1537 C  C   . TYR A  191 ? 0.1358 0.1429 0.1273 -0.0034 -0.0074 -0.0132 191 TYR A C   
1538 O  O   . TYR A  191 ? 0.1584 0.1576 0.1361 -0.0241 -0.0076 -0.0054 191 TYR A O   
1539 C  CB  . TYR A  191 ? 0.1630 0.1492 0.1534 -0.0205 0.0058  0.0055  191 TYR A CB  
1540 C  CG  . TYR A  191 ? 0.1312 0.1671 0.1723 -0.0199 0.0000  0.0053  191 TYR A CG  
1541 C  CD1 . TYR A  191 ? 0.1676 0.1810 0.1670 -0.0299 0.0119  -0.0182 191 TYR A CD1 
1542 C  CD2 . TYR A  191 ? 0.1586 0.1426 0.1773 -0.0027 0.0089  0.0015  191 TYR A CD2 
1543 C  CE1 . TYR A  191 ? 0.1973 0.1845 0.1790 -0.0092 0.0105  -0.0038 191 TYR A CE1 
1544 C  CE2 . TYR A  191 ? 0.1601 0.1464 0.2085 -0.0099 0.0093  0.0063  191 TYR A CE2 
1545 C  CZ  . TYR A  191 ? 0.1852 0.1500 0.1708 -0.0072 0.0219  0.0039  191 TYR A CZ  
1546 O  OH  . TYR A  191 ? 0.1945 0.1855 0.2437 -0.0391 0.0251  0.0265  191 TYR A OH  
1547 N  N   . ARG A  192 ? 0.1463 0.1500 0.1383 -0.0144 -0.0053 0.0117  192 ARG A N   
1548 C  CA  . ARG A  192 ? 0.1508 0.1345 0.1509 -0.0033 -0.0091 0.0163  192 ARG A CA  
1549 C  C   . ARG A  192 ? 0.1418 0.1464 0.1292 0.0039  -0.0075 -0.0021 192 ARG A C   
1550 O  O   . ARG A  192 ? 0.1740 0.1512 0.1435 -0.0167 -0.0211 -0.0087 192 ARG A O   
1551 C  CB  . ARG A  192 ? 0.1552 0.1887 0.1669 0.0004  0.0150  0.0095  192 ARG A CB  
1552 C  CG  . ARG A  192 ? 0.1839 0.1923 0.1639 -0.0291 0.0141  0.0025  192 ARG A CG  
1553 C  CD  . ARG A  192 ? 0.1938 0.2028 0.1822 -0.0036 0.0049  0.0063  192 ARG A CD  
1554 N  NE  . ARG A  192 ? 0.1850 0.2214 0.1864 -0.0244 0.0003  -0.0029 192 ARG A NE  
1555 C  CZ  . ARG A  192 ? 0.1812 0.2211 0.1411 -0.0058 -0.0173 -0.0228 192 ARG A CZ  
1556 N  NH1 . ARG A  192 ? 0.1864 0.2757 0.1788 -0.0524 0.0015  -0.0245 192 ARG A NH1 
1557 N  NH2 . ARG A  192 ? 0.1665 0.2263 0.2286 -0.0330 0.0125  0.0272  192 ARG A NH2 
1558 N  N   . TYR A  193 ? 0.1236 0.1320 0.1397 0.0025  -0.0031 0.0052  193 TYR A N   
1559 C  CA  . TYR A  193 ? 0.1385 0.1389 0.1381 -0.0002 -0.0069 -0.0024 193 TYR A CA  
1560 C  C   . TYR A  193 ? 0.1402 0.1430 0.1347 -0.0126 0.0074  0.0157  193 TYR A C   
1561 O  O   . TYR A  193 ? 0.1556 0.1571 0.1425 -0.0241 -0.0170 0.0141  193 TYR A O   
1562 C  CB  . TYR A  193 ? 0.1387 0.1661 0.1400 -0.0082 -0.0132 -0.0013 193 TYR A CB  
1563 C  CG  . TYR A  193 ? 0.1216 0.1660 0.1407 -0.0190 -0.0035 0.0080  193 TYR A CG  
1564 C  CD1 . TYR A  193 ? 0.1266 0.1389 0.1385 -0.0264 -0.0044 0.0114  193 TYR A CD1 
1565 C  CD2 . TYR A  193 ? 0.1401 0.1668 0.1520 0.0021  -0.0196 0.0198  193 TYR A CD2 
1566 C  CE1 . TYR A  193 ? 0.1049 0.1359 0.1393 -0.0063 -0.0071 -0.0037 193 TYR A CE1 
1567 C  CE2 . TYR A  193 ? 0.1287 0.1493 0.1572 -0.0268 -0.0122 0.0126  193 TYR A CE2 
1568 C  CZ  . TYR A  193 ? 0.1106 0.1494 0.1353 -0.0155 -0.0021 0.0006  193 TYR A CZ  
1569 O  OH  . TYR A  193 ? 0.1210 0.1209 0.1465 -0.0076 -0.0059 0.0077  193 TYR A OH  
1570 N  N   . ARG A  194 ? 0.1581 0.1349 0.1383 -0.0066 -0.0111 0.0205  194 ARG A N   
1571 C  CA  . ARG A  194 ? 0.1574 0.1310 0.1319 -0.0147 -0.0055 0.0231  194 ARG A CA  
1572 C  C   . ARG A  194 ? 0.1505 0.1590 0.1350 0.0064  -0.0126 0.0446  194 ARG A C   
1573 O  O   . ARG A  194 ? 0.1673 0.1594 0.1657 0.0017  -0.0370 0.0159  194 ARG A O   
1574 C  CB  . ARG A  194 ? 0.2447 0.1854 0.1502 -0.0035 0.0414  0.0390  194 ARG A CB  
1575 C  CG  . ARG A  194 ? 0.2414 0.2581 0.1909 -0.0126 0.0450  0.0619  194 ARG A CG  
1576 C  CD  . ARG A  194 ? 0.2833 0.5061 0.3121 -0.0127 0.0168  -0.0914 194 ARG A CD  
1577 N  NE  . ARG A  194 ? 0.4287 0.7700 0.7456 -0.1037 0.3184  -0.0758 194 ARG A NE  
1578 C  CZ  . ARG A  194 ? 0.2535 0.6269 0.6763 0.0167  0.1863  0.2002  194 ARG A CZ  
1579 N  NH1 . ARG A  194 ? 0.7455 0.5562 0.8049 -0.0134 0.2989  0.0801  194 ARG A NH1 
1580 N  NH2 . ARG A  194 ? 0.3514 0.7195 0.5756 0.0475  0.1860  0.0986  194 ARG A NH2 
1581 N  N   . GLY A  195 ? 0.1414 0.1315 0.1306 0.0002  -0.0027 0.0221  195 GLY A N   
1582 C  CA  . GLY A  195 ? 0.1258 0.1496 0.1318 -0.0027 -0.0053 0.0111  195 GLY A CA  
1583 C  C   . GLY A  195 ? 0.1134 0.1377 0.1430 0.0017  -0.0151 0.0174  195 GLY A C   
1584 O  O   . GLY A  195 ? 0.1249 0.1379 0.1484 -0.0025 -0.0023 0.0335  195 GLY A O   
1585 N  N   . SER A  196 ? 0.1161 0.1388 0.1277 -0.0066 -0.0161 0.0075  196 SER A N   
1586 C  CA  . SER A  196 ? 0.1131 0.1252 0.1477 -0.0027 -0.0111 0.0055  196 SER A CA  
1587 C  C   . SER A  196 ? 0.1080 0.1237 0.1465 -0.0049 -0.0036 0.0212  196 SER A C   
1588 O  O   . SER A  196 ? 0.1238 0.1130 0.1442 0.0079  0.0015  0.0234  196 SER A O   
1589 C  CB  . SER A  196 ? 0.1107 0.1497 0.1476 0.0051  -0.0069 0.0508  196 SER A CB  
1590 O  OG  . SER A  196 ? 0.1036 0.1141 0.1659 0.0006  -0.0059 0.0351  196 SER A OG  
1591 N  N   . LEU A  197 ? 0.1087 0.1297 0.1330 -0.0097 -0.0063 0.0238  197 LEU A N   
1592 C  CA  . LEU A  197 ? 0.1026 0.1364 0.1455 -0.0098 -0.0041 -0.0044 197 LEU A CA  
1593 C  C   . LEU A  197 ? 0.0969 0.1037 0.1400 0.0008  -0.0118 0.0229  197 LEU A C   
1594 O  O   . LEU A  197 ? 0.1112 0.1227 0.1402 -0.0013 -0.0157 0.0261  197 LEU A O   
1595 C  CB  . LEU A  197 ? 0.1206 0.1380 0.1622 -0.0286 -0.0132 0.0079  197 LEU A CB  
1596 C  CG  . LEU A  197 ? 0.1208 0.1668 0.2122 -0.0140 -0.0436 0.0370  197 LEU A CG  
1597 C  CD1 . LEU A  197 ? 0.1437 0.2215 0.2746 -0.0606 0.0521  -0.0333 197 LEU A CD1 
1598 C  CD2 . LEU A  197 ? 0.1592 0.1884 0.2390 -0.0574 -0.0212 0.0085  197 LEU A CD2 
1599 N  N   . THR A  198 ? 0.1109 0.1156 0.1405 -0.0032 -0.0157 0.0226  198 THR A N   
1600 C  CA  . THR A  198 ? 0.1107 0.1102 0.1572 0.0021  0.0124  0.0162  198 THR A CA  
1601 C  C   . THR A  198 ? 0.0958 0.1156 0.1451 0.0042  -0.0143 0.0249  198 THR A C   
1602 O  O   . THR A  198 ? 0.1157 0.1231 0.1587 0.0009  -0.0004 0.0018  198 THR A O   
1603 C  CB  . THR A  198 ? 0.1146 0.1049 0.1329 -0.0055 -0.0184 0.0234  198 THR A CB  
1604 O  OG1 . THR A  198 ? 0.0996 0.1094 0.1504 -0.0065 -0.0201 0.0161  198 THR A OG1 
1605 C  CG2 . THR A  198 ? 0.1177 0.1260 0.1475 -0.0105 -0.0113 -0.0029 198 THR A CG2 
1606 N  N   . THR A  199 ? 0.1231 0.1039 0.1508 -0.0074 -0.0221 0.0160  199 THR A N   
1607 C  CA  . THR A  199 ? 0.1369 0.1145 0.1439 -0.0088 -0.0214 0.0145  199 THR A CA  
1608 C  C   . THR A  199 ? 0.1271 0.1204 0.1527 0.0000  -0.0422 0.0079  199 THR A C   
1609 O  O   . THR A  199 ? 0.1284 0.1159 0.1600 -0.0018 -0.0114 0.0232  199 THR A O   
1610 C  CB  . THR A  199 ? 0.1251 0.1234 0.1684 0.0002  -0.0270 0.0220  199 THR A CB  
1611 O  OG1 . THR A  199 ? 0.1309 0.1662 0.1671 -0.0150 -0.0274 0.0209  199 THR A OG1 
1612 C  CG2 . THR A  199 ? 0.1729 0.1188 0.1626 -0.0204 -0.0342 0.0373  199 THR A CG2 
1613 N  N   . PRO A  200 ? 0.1216 0.1179 0.1433 -0.0163 -0.0152 0.0094  200 PRO A N   
1614 C  CA  . PRO A  200 ? 0.1261 0.1183 0.1924 -0.0230 -0.0025 0.0021  200 PRO A CA  
1615 C  C   . PRO A  200 ? 0.1489 0.1265 0.1789 -0.0153 -0.0232 0.0041  200 PRO A C   
1616 O  O   . PRO A  200 ? 0.1321 0.1382 0.1966 -0.0211 -0.0329 0.0275  200 PRO A O   
1617 C  CB  . PRO A  200 ? 0.1473 0.1330 0.1808 -0.0152 -0.0055 0.0128  200 PRO A CB  
1618 C  CG  . PRO A  200 ? 0.1318 0.1060 0.1865 0.0048  -0.0050 0.0119  200 PRO A CG  
1619 C  CD  . PRO A  200 ? 0.1328 0.1086 0.1773 0.0006  -0.0107 0.0024  200 PRO A CD  
1620 N  N   . PRO A  201 ? 0.1140 0.1390 0.1782 -0.0152 -0.0204 0.0236  201 PRO A N   
1621 C  CA  . PRO A  201 ? 0.1417 0.1111 0.1974 -0.0150 -0.0148 0.0339  201 PRO A CA  
1622 C  C   . PRO A  201 ? 0.1227 0.1213 0.1791 -0.0179 -0.0232 0.0447  201 PRO A C   
1623 O  O   . PRO A  201 ? 0.1424 0.1279 0.2043 -0.0171 -0.0166 0.0396  201 PRO A O   
1624 C  CB  . PRO A  201 ? 0.1260 0.1351 0.2263 -0.0254 -0.0113 0.0403  201 PRO A CB  
1625 C  CG  . PRO A  201 ? 0.1753 0.2167 0.2927 -0.0462 -0.0510 0.0947  201 PRO A CG  
1626 C  CD  . PRO A  201 ? 0.1192 0.1461 0.2304 -0.0201 -0.0266 0.0212  201 PRO A CD  
1627 N  N   . CYS A  202 ? 0.1098 0.1190 0.1699 -0.0106 -0.0154 0.0165  202 CYS A N   
1628 C  CA  . CYS A  202 ? 0.1161 0.1270 0.1560 0.0027  -0.0187 0.0142  202 CYS A CA  
1629 C  C   . CYS A  202 ? 0.1247 0.0911 0.1703 -0.0018 -0.0137 0.0366  202 CYS A C   
1630 O  O   . CYS A  202 ? 0.1237 0.1266 0.1715 -0.0126 -0.0145 0.0323  202 CYS A O   
1631 C  CB  . CYS A  202 ? 0.1106 0.1484 0.1641 0.0114  -0.0115 0.0203  202 CYS A CB  
1632 S  SG  . CYS A  202 ? 0.1177 0.1268 0.1745 -0.0074 -0.0159 0.0221  202 CYS A SG  
1633 N  N   . ASN A  203 ? 0.1272 0.1276 0.1714 -0.0197 0.0066  0.0331  203 ASN A N   
1634 C  CA  . ASN A  203 ? 0.1254 0.1509 0.1822 -0.0140 -0.0105 0.0411  203 ASN A CA  
1635 C  C   . ASN A  203 ? 0.1114 0.1552 0.1621 -0.0196 0.0006  0.0331  203 ASN A C   
1636 O  O   . ASN A  203 ? 0.1211 0.1410 0.1578 -0.0159 -0.0006 0.0348  203 ASN A O   
1637 C  CB  . ASN A  203 ? 0.1380 0.1970 0.2233 -0.0631 0.0134  0.0145  203 ASN A CB  
1638 C  CG  . ASN A  203 ? 0.1663 0.2267 0.2278 -0.0949 -0.0147 0.0412  203 ASN A CG  
1639 O  OD1 . ASN A  203 ? 0.2164 0.2663 0.2869 -0.0661 -0.0097 -0.0044 203 ASN A OD1 
1640 N  ND2 . ASN A  203 ? 0.2669 0.2134 0.3944 -0.0457 0.0414  0.0443  203 ASN A ND2 
1641 N  N   . PRO A  204 ? 0.1227 0.1479 0.1631 -0.0119 -0.0055 0.0356  204 PRO A N   
1642 C  CA  . PRO A  204 ? 0.1278 0.1562 0.1499 -0.0093 -0.0018 0.0402  204 PRO A CA  
1643 C  C   . PRO A  204 ? 0.1212 0.1470 0.1581 -0.0188 0.0078  0.0241  204 PRO A C   
1644 O  O   . PRO A  204 ? 0.1523 0.1866 0.1714 0.0072  -0.0052 0.0383  204 PRO A O   
1645 C  CB  . PRO A  204 ? 0.1544 0.1972 0.1660 0.0117  -0.0305 0.0547  204 PRO A CB  
1646 C  CG  . PRO A  204 ? 0.1988 0.2050 0.2044 -0.0048 -0.0288 0.0744  204 PRO A CG  
1647 C  CD  . PRO A  204 ? 0.1820 0.1518 0.1958 0.0064  -0.0087 0.0719  204 PRO A CD  
1648 N  N   . THR A  205 ? 0.1206 0.1687 0.1678 -0.0168 -0.0130 0.0378  205 THR A N   
1649 C  CA  . THR A  205 ? 0.1084 0.1485 0.1865 -0.0201 0.0074  0.0518  205 THR A CA  
1650 C  C   . THR A  205 ? 0.1249 0.1473 0.1588 -0.0115 -0.0102 0.0458  205 THR A C   
1651 O  O   . THR A  205 ? 0.1215 0.1760 0.1973 -0.0115 0.0051  0.0511  205 THR A O   
1652 C  CB  . THR A  205 ? 0.1666 0.1318 0.2085 -0.0214 0.0114  0.0385  205 THR A CB  
1653 O  OG1 . THR A  205 ? 0.1473 0.1543 0.1954 -0.0188 -0.0115 0.0408  205 THR A OG1 
1654 C  CG2 . THR A  205 ? 0.1848 0.1375 0.2266 -0.0238 -0.0247 0.0660  205 THR A CG2 
1655 N  N   . VAL A  206 ? 0.1181 0.1399 0.1565 -0.0106 -0.0010 0.0319  206 VAL A N   
1656 C  CA  . VAL A  206 ? 0.1340 0.1329 0.1675 0.0013  0.0073  0.0381  206 VAL A CA  
1657 C  C   . VAL A  206 ? 0.1226 0.1451 0.1560 -0.0243 -0.0141 0.0308  206 VAL A C   
1658 O  O   . VAL A  206 ? 0.1269 0.1586 0.1721 -0.0113 -0.0198 0.0201  206 VAL A O   
1659 C  CB  . VAL A  206 ? 0.1280 0.1279 0.1523 -0.0013 0.0094  0.0266  206 VAL A CB  
1660 C  CG1 . VAL A  206 ? 0.1330 0.1526 0.1670 0.0044  -0.0150 0.0367  206 VAL A CG1 
1661 C  CG2 . VAL A  206 ? 0.1201 0.1679 0.1580 -0.0100 0.0077  0.0106  206 VAL A CG2 
1662 N  N   . LEU A  207 ? 0.1351 0.1377 0.1442 -0.0021 0.0083  0.0279  207 LEU A N   
1663 C  CA  . LEU A  207 ? 0.1457 0.1530 0.1533 -0.0013 0.0082  0.0292  207 LEU A CA  
1664 C  C   . LEU A  207 ? 0.1390 0.1395 0.1351 -0.0100 -0.0134 0.0059  207 LEU A C   
1665 O  O   . LEU A  207 ? 0.1222 0.1493 0.1385 -0.0031 -0.0086 0.0200  207 LEU A O   
1666 C  CB  . LEU A  207 ? 0.1724 0.1742 0.1746 0.0182  0.0265  0.0227  207 LEU A CB  
1667 C  CG  . LEU A  207 ? 0.2471 0.1739 0.1840 0.0562  0.0006  0.0156  207 LEU A CG  
1668 C  CD1 . LEU A  207 ? 0.3700 0.2414 0.1914 0.0082  -0.0477 -0.0162 207 LEU A CD1 
1669 C  CD2 . LEU A  207 ? 0.2298 0.4018 0.2997 0.0416  0.0272  -0.0837 207 LEU A CD2 
1670 N  N   . TRP A  208 ? 0.1347 0.1194 0.1407 -0.0124 -0.0021 0.0157  208 TRP A N   
1671 C  CA  . TRP A  208 ? 0.1254 0.1105 0.1332 0.0082  0.0035  0.0178  208 TRP A CA  
1672 C  C   . TRP A  208 ? 0.1335 0.1097 0.1121 -0.0192 -0.0055 0.0121  208 TRP A C   
1673 O  O   . TRP A  208 ? 0.1596 0.1406 0.1356 -0.0044 -0.0143 0.0132  208 TRP A O   
1674 C  CB  . TRP A  208 ? 0.1264 0.1324 0.1416 0.0079  -0.0025 0.0111  208 TRP A CB  
1675 C  CG  . TRP A  208 ? 0.1125 0.1268 0.1165 -0.0066 -0.0102 0.0158  208 TRP A CG  
1676 C  CD1 . TRP A  208 ? 0.1077 0.1296 0.1316 -0.0047 -0.0126 0.0286  208 TRP A CD1 
1677 C  CD2 . TRP A  208 ? 0.0891 0.1318 0.1389 -0.0053 0.0048  0.0245  208 TRP A CD2 
1678 N  NE1 . TRP A  208 ? 0.1039 0.1451 0.1345 0.0006  -0.0062 0.0249  208 TRP A NE1 
1679 C  CE2 . TRP A  208 ? 0.1000 0.1298 0.1332 0.0000  -0.0030 0.0214  208 TRP A CE2 
1680 C  CE3 . TRP A  208 ? 0.1039 0.1447 0.1110 -0.0071 -0.0061 0.0238  208 TRP A CE3 
1681 C  CZ2 . TRP A  208 ? 0.0996 0.1375 0.1482 -0.0122 0.0122  0.0292  208 TRP A CZ2 
1682 C  CZ3 . TRP A  208 ? 0.1329 0.1190 0.1296 0.0011  -0.0050 0.0142  208 TRP A CZ3 
1683 C  CH2 . TRP A  208 ? 0.1291 0.1190 0.1429 -0.0245 -0.0024 0.0230  208 TRP A CH2 
1684 N  N   . THR A  209 ? 0.1119 0.1198 0.1254 0.0054  0.0003  0.0187  209 THR A N   
1685 C  CA  . THR A  209 ? 0.1278 0.1271 0.1377 0.0046  0.0032  0.0053  209 THR A CA  
1686 C  C   . THR A  209 ? 0.1585 0.1152 0.1111 0.0017  -0.0109 0.0061  209 THR A C   
1687 O  O   . THR A  209 ? 0.1369 0.1495 0.1303 -0.0223 -0.0025 0.0043  209 THR A O   
1688 C  CB  . THR A  209 ? 0.1209 0.1357 0.1507 0.0116  0.0085  0.0189  209 THR A CB  
1689 O  OG1 . THR A  209 ? 0.1347 0.1727 0.1435 0.0054  0.0165  0.0044  209 THR A OG1 
1690 C  CG2 . THR A  209 ? 0.1659 0.1362 0.1901 0.0298  0.0269  0.0051  209 THR A CG2 
1691 N  N   . VAL A  210 ? 0.1296 0.1202 0.1272 -0.0082 0.0081  0.0186  210 VAL A N   
1692 C  CA  . VAL A  210 ? 0.1170 0.1395 0.1301 0.0072  0.0030  0.0137  210 VAL A CA  
1693 C  C   . VAL A  210 ? 0.1253 0.1338 0.1049 -0.0049 0.0062  0.0111  210 VAL A C   
1694 O  O   . VAL A  210 ? 0.1509 0.1367 0.1224 0.0043  0.0104  0.0006  210 VAL A O   
1695 C  CB  . VAL A  210 ? 0.1179 0.1292 0.1511 0.0083  0.0064  0.0059  210 VAL A CB  
1696 C  CG1 . VAL A  210 ? 0.1342 0.1512 0.1369 -0.0132 0.0172  0.0020  210 VAL A CG1 
1697 C  CG2 . VAL A  210 ? 0.1355 0.1224 0.1693 0.0080  -0.0089 0.0008  210 VAL A CG2 
1698 N  N   . PHE A  211 ? 0.1264 0.1192 0.1326 0.0025  0.0033  0.0209  211 PHE A N   
1699 C  CA  . PHE A  211 ? 0.1525 0.1112 0.1472 -0.0060 -0.0031 0.0110  211 PHE A CA  
1700 C  C   . PHE A  211 ? 0.1293 0.1267 0.1514 -0.0042 0.0077  -0.0034 211 PHE A C   
1701 O  O   . PHE A  211 ? 0.1500 0.1384 0.1516 -0.0002 0.0073  0.0034  211 PHE A O   
1702 C  CB  . PHE A  211 ? 0.1405 0.1287 0.1457 0.0203  0.0012  0.0120  211 PHE A CB  
1703 C  CG  . PHE A  211 ? 0.1378 0.1315 0.1546 0.0114  0.0029  0.0065  211 PHE A CG  
1704 C  CD1 . PHE A  211 ? 0.1480 0.1564 0.1615 0.0292  0.0063  0.0242  211 PHE A CD1 
1705 C  CD2 . PHE A  211 ? 0.1377 0.1154 0.1978 0.0218  -0.0232 0.0084  211 PHE A CD2 
1706 C  CE1 . PHE A  211 ? 0.1264 0.2094 0.2149 0.0201  0.0083  0.0222  211 PHE A CE1 
1707 C  CE2 . PHE A  211 ? 0.1438 0.1634 0.1854 0.0074  -0.0128 0.0245  211 PHE A CE2 
1708 C  CZ  . PHE A  211 ? 0.1490 0.1782 0.2104 0.0223  -0.0044 0.0255  211 PHE A CZ  
1709 N  N   . ARG A  212 ? 0.1663 0.1133 0.1537 -0.0129 -0.0038 0.0031  212 ARG A N   
1710 C  CA  . ARG A  212 ? 0.1652 0.1136 0.1689 -0.0161 0.0036  -0.0022 212 ARG A CA  
1711 C  C   . ARG A  212 ? 0.1549 0.1403 0.1527 -0.0100 0.0111  0.0062  212 ARG A C   
1712 O  O   . ARG A  212 ? 0.1615 0.1569 0.1883 -0.0063 0.0100  0.0110  212 ARG A O   
1713 C  CB  . ARG A  212 ? 0.1998 0.1453 0.1739 -0.0306 0.0256  -0.0069 212 ARG A CB  
1714 C  CG  . ARG A  212 ? 0.2235 0.1826 0.2183 -0.0367 -0.0041 -0.0373 212 ARG A CG  
1715 C  CD  . ARG A  212 ? 0.3087 0.1935 0.2397 -0.0511 0.0471  -0.0296 212 ARG A CD  
1716 N  NE  . ARG A  212 ? 0.4381 0.3594 0.2821 -0.2011 0.0800  -0.1225 212 ARG A NE  
1717 C  CZ  . ARG A  212 ? 0.5755 0.4234 0.3307 -0.2208 0.1293  -0.1161 212 ARG A CZ  
1718 N  NH1 . ARG A  212 ? 0.5677 0.2370 0.3995 -0.0660 0.0509  -0.0614 212 ARG A NH1 
1719 N  NH2 . ARG A  212 ? 0.6034 0.4994 0.6047 -0.3231 0.0550  -0.0471 212 ARG A NH2 
1720 N  N   . ASN A  213 ? 0.1788 0.1282 0.1672 0.0013  -0.0080 0.0222  213 ASN A N   
1721 C  CA  . ASN A  213 ? 0.2147 0.1152 0.1791 0.0069  0.0150  0.0047  213 ASN A CA  
1722 C  C   . ASN A  213 ? 0.1879 0.1618 0.1694 -0.0178 -0.0035 0.0190  213 ASN A C   
1723 O  O   . ASN A  213 ? 0.1636 0.1391 0.1817 0.0013  0.0022  -0.0020 213 ASN A O   
1724 C  CB  . ASN A  213 ? 0.2127 0.1531 0.1938 0.0212  0.0096  0.0124  213 ASN A CB  
1725 C  CG  . ASN A  213 ? 0.2274 0.1634 0.2665 -0.0086 0.0579  -0.0264 213 ASN A CG  
1726 O  OD1 . ASN A  213 ? 0.3353 0.2250 0.2597 -0.0281 0.0495  -0.0648 213 ASN A OD1 
1727 N  ND2 . ASN A  213 ? 0.2685 0.1934 0.2565 -0.0228 0.0324  -0.0760 213 ASN A ND2 
1728 N  N   . PRO A  214 ? 0.1776 0.1313 0.1571 -0.0023 -0.0025 0.0197  214 PRO A N   
1729 C  CA  . PRO A  214 ? 0.1721 0.1463 0.1851 0.0172  0.0018  0.0227  214 PRO A CA  
1730 C  C   . PRO A  214 ? 0.1615 0.1200 0.1670 0.0154  0.0070  0.0218  214 PRO A C   
1731 O  O   . PRO A  214 ? 0.2228 0.1281 0.1997 0.0108  0.0126  0.0356  214 PRO A O   
1732 C  CB  . PRO A  214 ? 0.1832 0.1718 0.2186 0.0018  0.0291  0.0059  214 PRO A CB  
1733 C  CG  . PRO A  214 ? 0.1744 0.2105 0.2254 -0.0188 0.0237  0.0015  214 PRO A CG  
1734 C  CD  . PRO A  214 ? 0.1923 0.1749 0.2330 -0.0473 0.0458  0.0018  214 PRO A CD  
1735 N  N   . VAL A  215 ? 0.1507 0.1574 0.1498 0.0190  0.0013  0.0153  215 VAL A N   
1736 C  CA  . VAL A  215 ? 0.1569 0.1740 0.1423 0.0312  0.0130  0.0136  215 VAL A CA  
1737 C  C   . VAL A  215 ? 0.1628 0.1348 0.1538 0.0092  0.0111  0.0201  215 VAL A C   
1738 O  O   . VAL A  215 ? 0.1578 0.1568 0.1767 0.0232  0.0165  0.0278  215 VAL A O   
1739 C  CB  . VAL A  215 ? 0.1567 0.1562 0.1716 0.0268  0.0051  0.0388  215 VAL A CB  
1740 C  CG1 . VAL A  215 ? 0.1759 0.2220 0.1827 0.0182  0.0289  0.0557  215 VAL A CG1 
1741 C  CG2 . VAL A  215 ? 0.1577 0.1385 0.2071 0.0236  -0.0025 0.0476  215 VAL A CG2 
1742 N  N   A GLN A  216 ? 0.1833 0.1466 0.1683 0.0419  0.0221  0.0466  216 GLN A N   
1743 N  N   B GLN A  216 ? 0.1593 0.1805 0.1409 0.0103  0.0321  0.0344  216 GLN A N   
1744 C  CA  A GLN A  216 ? 0.1909 0.1717 0.1483 0.0227  0.0098  0.0184  216 GLN A CA  
1745 C  CA  B GLN A  216 ? 0.1904 0.1666 0.1452 0.0115  0.0359  0.0412  216 GLN A CA  
1746 C  C   A GLN A  216 ? 0.1757 0.1956 0.1351 0.0236  0.0130  0.0467  216 GLN A C   
1747 C  C   B GLN A  216 ? 0.1744 0.1873 0.1561 0.0165  0.0280  0.0439  216 GLN A C   
1748 O  O   A GLN A  216 ? 0.1533 0.2137 0.2046 0.0208  0.0316  0.0455  216 GLN A O   
1749 O  O   B GLN A  216 ? 0.1639 0.2043 0.1948 0.0532  0.0223  0.0143  216 GLN A O   
1750 C  CB  A GLN A  216 ? 0.1912 0.1971 0.1543 0.0279  -0.0182 0.0509  216 GLN A CB  
1751 C  CB  B GLN A  216 ? 0.2034 0.1629 0.1743 -0.0044 0.0205  0.0201  216 GLN A CB  
1752 C  CG  A GLN A  216 ? 0.2078 0.2034 0.1694 0.0236  0.0128  0.0057  216 GLN A CG  
1753 C  CG  B GLN A  216 ? 0.2558 0.1439 0.2096 -0.0560 -0.0044 0.0121  216 GLN A CG  
1754 C  CD  A GLN A  216 ? 0.2882 0.1925 0.2498 -0.0370 -0.0100 -0.0675 216 GLN A CD  
1755 C  CD  B GLN A  216 ? 0.2326 0.1604 0.2323 0.0541  0.0229  0.0776  216 GLN A CD  
1756 O  OE1 A GLN A  216 ? 0.2904 0.2082 0.2504 -0.0161 0.0578  -0.0125 216 GLN A OE1 
1757 O  OE1 B GLN A  216 ? 0.2217 0.2021 0.2632 0.0337  -0.0148 0.0271  216 GLN A OE1 
1758 N  NE2 A GLN A  216 ? 0.4998 0.3094 0.2044 -0.1153 -0.1154 0.0767  216 GLN A NE2 
1759 N  NE2 B GLN A  216 ? 0.2902 0.1665 0.2500 0.0060  -0.0343 0.0604  216 GLN A NE2 
1760 N  N   . ILE A  217 ? 0.1728 0.1618 0.1597 0.0200  0.0179  0.0237  217 ILE A N   
1761 C  CA  . ILE A  217 ? 0.1714 0.1615 0.1667 0.0162  0.0062  0.0368  217 ILE A CA  
1762 C  C   . ILE A  217 ? 0.1756 0.1721 0.1806 0.0442  0.0054  0.0411  217 ILE A C   
1763 O  O   . ILE A  217 ? 0.1694 0.1813 0.1664 0.0137  0.0165  0.0304  217 ILE A O   
1764 C  CB  . ILE A  217 ? 0.1293 0.1737 0.1764 0.0114  0.0064  0.0430  217 ILE A CB  
1765 C  CG1 . ILE A  217 ? 0.1658 0.1663 0.1723 0.0197  0.0135  0.0420  217 ILE A CG1 
1766 C  CG2 . ILE A  217 ? 0.1825 0.1906 0.1800 0.0476  0.0412  0.0599  217 ILE A CG2 
1767 C  CD1 . ILE A  217 ? 0.1840 0.1760 0.1588 0.0200  0.0307  0.0482  217 ILE A CD1 
1768 N  N   . SER A  218 ? 0.1793 0.1944 0.1649 0.0232  0.0189  0.0468  218 SER A N   
1769 C  CA  . SER A  218 ? 0.1849 0.2144 0.1727 0.0301  0.0398  0.0487  218 SER A CA  
1770 C  C   . SER A  218 ? 0.2164 0.1770 0.1509 0.0200  0.0351  0.0508  218 SER A C   
1771 O  O   . SER A  218 ? 0.1761 0.1713 0.1752 0.0189  0.0302  0.0433  218 SER A O   
1772 C  CB  . SER A  218 ? 0.2471 0.2094 0.1736 0.0197  0.0022  0.0841  218 SER A CB  
1773 O  OG  . SER A  218 ? 0.2166 0.2056 0.1967 0.0282  0.0160  0.0621  218 SER A OG  
1774 N  N   . GLN A  219 ? 0.2356 0.1889 0.2235 0.0209  0.0960  0.0476  219 GLN A N   
1775 C  CA  . GLN A  219 ? 0.2050 0.2091 0.2345 -0.0058 0.0614  0.0276  219 GLN A CA  
1776 C  C   . GLN A  219 ? 0.2029 0.2188 0.2030 0.0152  0.0361  0.0197  219 GLN A C   
1777 O  O   . GLN A  219 ? 0.1985 0.2148 0.1833 0.0082  0.0550  0.0423  219 GLN A O   
1778 C  CB  . GLN A  219 ? 0.2539 0.3470 0.3461 -0.0987 0.1485  -0.0527 219 GLN A CB  
1779 C  CG  . GLN A  219 ? 0.6914 0.4958 0.3929 -0.2409 0.0963  0.1217  219 GLN A CG  
1780 C  CD  . GLN A  219 ? 0.7334 0.5023 0.5899 -0.3617 0.1456  -0.0563 219 GLN A CD  
1781 O  OE1 . GLN A  219 ? 0.3730 0.2918 0.2274 0.0275  0.0242  0.0396  219 GLN A OE1 
1782 N  NE2 . GLN A  219 ? 0.4266 0.8734 0.8455 -0.3027 0.0904  0.2440  219 GLN A NE2 
1783 N  N   . GLU A  220 ? 0.1942 0.2224 0.1841 0.0082  0.0423  0.0666  220 GLU A N   
1784 C  CA  . GLU A  220 ? 0.2582 0.2125 0.1754 0.0221  0.0245  0.0673  220 GLU A CA  
1785 C  C   . GLU A  220 ? 0.2101 0.1945 0.1415 0.0188  -0.0061 0.0368  220 GLU A C   
1786 O  O   . GLU A  220 ? 0.2017 0.2211 0.1509 0.0267  0.0232  0.0122  220 GLU A O   
1787 C  CB  . GLU A  220 ? 0.2680 0.2601 0.1573 0.0581  0.0234  0.0936  220 GLU A CB  
1788 C  CG  . GLU A  220 ? 0.4038 0.3422 0.1957 0.0417  0.0739  0.1216  220 GLU A CG  
1789 C  CD  . GLU A  220 ? 0.4835 0.3719 0.2913 0.0884  0.0751  0.1568  220 GLU A CD  
1790 O  OE1 . GLU A  220 ? 0.4338 0.2634 0.3080 0.0848  0.0912  0.1187  220 GLU A OE1 
1791 O  OE2 . GLU A  220 ? 0.5617 0.4591 0.4026 0.0864  0.1470  0.1639  220 GLU A OE2 
1792 N  N   . GLN A  221 ? 0.1819 0.2347 0.1469 0.0531  0.0226  0.0434  221 GLN A N   
1793 C  CA  . GLN A  221 ? 0.1806 0.1933 0.1451 0.0311  -0.0091 0.0240  221 GLN A CA  
1794 C  C   . GLN A  221 ? 0.1637 0.2111 0.1421 0.0189  0.0043  0.0073  221 GLN A C   
1795 O  O   . GLN A  221 ? 0.1696 0.1902 0.1421 0.0127  -0.0143 0.0170  221 GLN A O   
1796 C  CB  . GLN A  221 ? 0.1526 0.1953 0.1524 0.0408  0.0111  0.0403  221 GLN A CB  
1797 C  CG  . GLN A  221 ? 0.1685 0.2461 0.1565 0.0449  -0.0027 0.0348  221 GLN A CG  
1798 C  CD  . GLN A  221 ? 0.1914 0.1899 0.1562 0.0170  -0.0048 0.0530  221 GLN A CD  
1799 O  OE1 . GLN A  221 ? 0.1705 0.2160 0.1743 0.0223  0.0070  0.0456  221 GLN A OE1 
1800 N  NE2 . GLN A  221 ? 0.1991 0.2200 0.1768 0.0208  0.0031  0.0605  221 GLN A NE2 
1801 N  N   . LEU A  222 ? 0.1571 0.1825 0.1341 0.0021  0.0109  0.0230  222 LEU A N   
1802 C  CA  . LEU A  222 ? 0.1497 0.1832 0.1499 0.0125  -0.0024 0.0078  222 LEU A CA  
1803 C  C   . LEU A  222 ? 0.1459 0.1933 0.1789 -0.0153 0.0142  0.0238  222 LEU A C   
1804 O  O   . LEU A  222 ? 0.1643 0.1722 0.1524 -0.0008 0.0152  0.0064  222 LEU A O   
1805 C  CB  . LEU A  222 ? 0.1731 0.1800 0.1487 -0.0081 -0.0069 0.0490  222 LEU A CB  
1806 C  CG  . LEU A  222 ? 0.1438 0.1996 0.1539 0.0071  -0.0063 0.0078  222 LEU A CG  
1807 C  CD1 . LEU A  222 ? 0.1544 0.1915 0.1776 -0.0058 -0.0066 0.0381  222 LEU A CD1 
1808 C  CD2 . LEU A  222 ? 0.1634 0.2443 0.1915 -0.0189 -0.0030 0.0444  222 LEU A CD2 
1809 N  N   . LEU A  223 ? 0.1614 0.2114 0.1536 -0.0076 0.0194  0.0030  223 LEU A N   
1810 C  CA  . LEU A  223 ? 0.1794 0.2039 0.1469 0.0040  0.0264  0.0254  223 LEU A CA  
1811 C  C   . LEU A  223 ? 0.1912 0.1996 0.1276 0.0181  0.0145  0.0071  223 LEU A C   
1812 O  O   . LEU A  223 ? 0.2171 0.1901 0.1530 0.0077  0.0238  -0.0064 223 LEU A O   
1813 C  CB  . LEU A  223 ? 0.1868 0.2351 0.1644 0.0444  0.0292  0.0541  223 LEU A CB  
1814 C  CG  . LEU A  223 ? 0.2102 0.2611 0.2133 0.0190  0.0395  0.0361  223 LEU A CG  
1815 C  CD1 . LEU A  223 ? 0.2301 0.2085 0.2386 0.0612  0.0669  0.0738  223 LEU A CD1 
1816 C  CD2 . LEU A  223 ? 0.2656 0.3374 0.2080 0.0504  0.0515  0.1008  223 LEU A CD2 
1817 N  N   . ALA A  224 ? 0.1828 0.1998 0.1632 0.0115  -0.0075 0.0186  224 ALA A N   
1818 C  CA  . ALA A  224 ? 0.2273 0.2093 0.2004 0.0086  -0.0179 0.0036  224 ALA A CA  
1819 C  C   . ALA A  224 ? 0.1627 0.2266 0.2075 0.0035  -0.0146 0.0048  224 ALA A C   
1820 O  O   . ALA A  224 ? 0.2000 0.2336 0.2255 -0.0039 -0.0139 -0.0128 224 ALA A O   
1821 C  CB  . ALA A  224 ? 0.2032 0.2685 0.2461 0.0286  -0.0146 0.0409  224 ALA A CB  
1822 N  N   . LEU A  225 ? 0.1681 0.2145 0.1692 0.0039  -0.0160 0.0142  225 LEU A N   
1823 C  CA  . LEU A  225 ? 0.1475 0.1994 0.1963 0.0070  -0.0020 0.0106  225 LEU A CA  
1824 C  C   . LEU A  225 ? 0.1900 0.1835 0.1764 0.0061  0.0218  0.0234  225 LEU A C   
1825 O  O   . LEU A  225 ? 0.1737 0.1799 0.2447 -0.0064 0.0152  -0.0119 225 LEU A O   
1826 C  CB  . LEU A  225 ? 0.1612 0.1800 0.1521 0.0092  0.0068  0.0140  225 LEU A CB  
1827 C  CG  . LEU A  225 ? 0.1611 0.1839 0.1961 0.0040  0.0155  0.0458  225 LEU A CG  
1828 C  CD1 . LEU A  225 ? 0.1641 0.1986 0.2327 -0.0086 -0.0179 0.0493  225 LEU A CD1 
1829 C  CD2 . LEU A  225 ? 0.2119 0.1908 0.1754 0.0228  0.0052  0.0306  225 LEU A CD2 
1830 N  N   . GLU A  226 ? 0.1474 0.1900 0.1495 0.0163  -0.0009 0.0118  226 GLU A N   
1831 C  CA  . GLU A  226 ? 0.1667 0.1681 0.1845 0.0063  -0.0047 0.0130  226 GLU A CA  
1832 C  C   . GLU A  226 ? 0.1626 0.1923 0.2018 0.0068  -0.0125 -0.0031 226 GLU A C   
1833 O  O   . GLU A  226 ? 0.2418 0.2011 0.2111 0.0409  -0.0223 -0.0241 226 GLU A O   
1834 C  CB  . GLU A  226 ? 0.1533 0.1810 0.1643 0.0020  0.0138  -0.0027 226 GLU A CB  
1835 C  CG  . GLU A  226 ? 0.1565 0.1948 0.1566 -0.0261 0.0194  0.0024  226 GLU A CG  
1836 C  CD  . GLU A  226 ? 0.1640 0.1887 0.1590 -0.0201 0.0057  0.0229  226 GLU A CD  
1837 O  OE1 . GLU A  226 ? 0.1825 0.2293 0.1512 -0.0218 0.0192  0.0346  226 GLU A OE1 
1838 O  OE2 . GLU A  226 ? 0.1780 0.2086 0.1606 -0.0145 0.0077  0.0310  226 GLU A OE2 
1839 N  N   . THR A  227 ? 0.1810 0.1961 0.1636 -0.0042 0.0105  -0.0109 227 THR A N   
1840 C  CA  . THR A  227 ? 0.2447 0.2357 0.1507 -0.0441 0.0222  -0.0298 227 THR A CA  
1841 C  C   . THR A  227 ? 0.2141 0.2382 0.1645 0.0013  -0.0019 -0.0142 227 THR A C   
1842 O  O   . THR A  227 ? 0.2672 0.2873 0.2004 -0.0537 0.0408  -0.0615 227 THR A O   
1843 C  CB  . THR A  227 ? 0.2143 0.2322 0.1972 0.0170  0.0367  -0.0273 227 THR A CB  
1844 O  OG1 . THR A  227 ? 0.2617 0.2776 0.1526 0.0020  0.0377  0.0150  227 THR A OG1 
1845 C  CG2 . THR A  227 ? 0.2528 0.2838 0.2666 -0.0983 0.0446  -0.0258 227 THR A CG2 
1846 N  N   . ALA A  228 ? 0.1835 0.2164 0.1857 -0.0222 -0.0148 -0.0098 228 ALA A N   
1847 C  CA  . ALA A  228 ? 0.2089 0.2144 0.1867 -0.0416 -0.0328 -0.0161 228 ALA A CA  
1848 C  C   . ALA A  228 ? 0.2037 0.2250 0.2100 -0.0212 -0.0237 -0.0325 228 ALA A C   
1849 O  O   . ALA A  228 ? 0.2636 0.2454 0.2094 -0.0377 -0.0436 -0.0466 228 ALA A O   
1850 C  CB  . ALA A  228 ? 0.1445 0.3033 0.4008 -0.0341 -0.0162 -0.0287 228 ALA A CB  
1851 N  N   . LEU A  229 ? 0.1892 0.1958 0.1833 -0.0042 0.0053  -0.0063 229 LEU A N   
1852 C  CA  . LEU A  229 ? 0.1962 0.2051 0.1833 -0.0074 0.0044  -0.0147 229 LEU A CA  
1853 C  C   . LEU A  229 ? 0.1909 0.2069 0.1588 -0.0111 -0.0172 -0.0453 229 LEU A C   
1854 O  O   . LEU A  229 ? 0.1839 0.2142 0.2021 -0.0364 -0.0181 -0.0302 229 LEU A O   
1855 C  CB  . LEU A  229 ? 0.2073 0.2175 0.1802 -0.0009 -0.0127 -0.0072 229 LEU A CB  
1856 C  CG  . LEU A  229 ? 0.1832 0.2606 0.1809 0.0142  0.0057  -0.0117 229 LEU A CG  
1857 C  CD1 . LEU A  229 ? 0.2322 0.3738 0.1716 0.0537  0.0055  0.0082  229 LEU A CD1 
1858 C  CD2 . LEU A  229 ? 0.1917 0.2689 0.2559 -0.0049 -0.0344 -0.0195 229 LEU A CD2 
1859 N  N   . TYR A  230 ? 0.2023 0.1939 0.2310 -0.0226 0.0088  -0.0515 230 TYR A N   
1860 C  CA  . TYR A  230 ? 0.2325 0.2034 0.2105 -0.0179 0.0141  -0.0614 230 TYR A CA  
1861 C  C   . TYR A  230 ? 0.2028 0.2199 0.2276 -0.0241 0.0195  -0.0554 230 TYR A C   
1862 O  O   . TYR A  230 ? 0.1992 0.2278 0.2750 -0.0307 0.0132  -0.0322 230 TYR A O   
1863 C  CB  . TYR A  230 ? 0.2362 0.2366 0.2092 -0.0236 0.0022  -0.0442 230 TYR A CB  
1864 C  CG  . TYR A  230 ? 0.2537 0.2942 0.2155 0.0046  0.0288  -0.0452 230 TYR A CG  
1865 C  CD1 . TYR A  230 ? 0.3851 0.3260 0.3353 -0.0063 0.0071  0.0319  230 TYR A CD1 
1866 C  CD2 . TYR A  230 ? 0.2583 0.3502 0.3239 0.0212  0.0686  0.0022  230 TYR A CD2 
1867 C  CE1 . TYR A  230 ? 0.5198 0.4719 0.3305 0.1482  0.0961  0.0990  230 TYR A CE1 
1868 C  CE2 . TYR A  230 ? 0.3270 0.4349 0.2924 0.0249  0.1052  -0.0303 230 TYR A CE2 
1869 C  CZ  . TYR A  230 ? 0.3172 0.4698 0.4900 -0.0002 0.0648  0.0781  230 TYR A CZ  
1870 O  OH  . TYR A  230 ? 0.7429 0.4075 0.4419 -0.0744 0.0763  -0.0029 230 TYR A OH  
1871 N  N   . CYS A  231 ? 0.2305 0.2300 0.2463 -0.0107 0.0203  -0.0321 231 CYS A N   
1872 C  CA  . CYS A  231 ? 0.2242 0.2567 0.2149 0.0093  -0.0212 -0.0445 231 CYS A CA  
1873 C  C   . CYS A  231 ? 0.2163 0.2522 0.2176 -0.0063 0.0036  -0.0274 231 CYS A C   
1874 O  O   . CYS A  231 ? 0.2904 0.2820 0.2080 -0.0359 0.0080  -0.0380 231 CYS A O   
1875 C  CB  . CYS A  231 ? 0.2640 0.4570 0.2381 -0.1278 -0.0634 -0.0234 231 CYS A CB  
1876 S  SG  . CYS A  231 ? 0.2881 0.6124 0.5465 -0.0594 -0.0993 0.2044  231 CYS A SG  
1877 N  N   . THR A  232 ? 0.2454 0.2290 0.2254 0.0102  -0.0176 -0.0523 232 THR A N   
1878 C  CA  . THR A  232 ? 0.2509 0.1945 0.2536 -0.0016 0.0344  -0.0282 232 THR A CA  
1879 C  C   . THR A  232 ? 0.2579 0.2040 0.1944 -0.0225 0.0125  -0.0337 232 THR A C   
1880 O  O   . THR A  232 ? 0.2396 0.2439 0.2418 -0.0034 -0.0016 -0.0217 232 THR A O   
1881 C  CB  . THR A  232 ? 0.2785 0.2582 0.2502 0.0167  0.0153  -0.0571 232 THR A CB  
1882 O  OG1 . THR A  232 ? 0.2913 0.2279 0.2423 0.0012  0.0442  -0.0585 232 THR A OG1 
1883 C  CG2 . THR A  232 ? 0.2699 0.2640 0.2846 0.0197  0.0296  -0.0515 232 THR A CG2 
1884 N  N   . HIS A  233 ? 0.2590 0.2346 0.2351 -0.0144 -0.0064 -0.0282 233 HIS A N   
1885 C  CA  . HIS A  233 ? 0.2812 0.2263 0.2190 -0.0447 -0.0253 -0.0344 233 HIS A CA  
1886 C  C   . HIS A  233 ? 0.2762 0.1813 0.2626 -0.0290 0.0088  -0.0599 233 HIS A C   
1887 O  O   . HIS A  233 ? 0.2611 0.2431 0.2046 -0.0041 -0.0016 -0.0458 233 HIS A O   
1888 C  CB  . HIS A  233 ? 0.3453 0.1988 0.2590 -0.0036 -0.0458 -0.0058 233 HIS A CB  
1889 C  CG  . HIS A  233 ? 0.4376 0.3889 0.2976 -0.0130 -0.0050 0.0264  233 HIS A CG  
1890 N  ND1 . HIS A  233 ? 0.4521 0.5186 0.5090 0.0094  0.0526  0.1306  233 HIS A ND1 
1891 C  CD2 . HIS A  233 ? 0.4878 0.2228 0.4418 0.0237  0.0850  0.0322  233 HIS A CD2 
1892 C  CE1 . HIS A  233 ? 0.4246 0.5255 0.4452 -0.0655 0.0015  0.2213  233 HIS A CE1 
1893 N  NE2 . HIS A  233 ? 0.5450 0.2366 0.5008 -0.0712 0.0914  0.0432  233 HIS A NE2 
1894 N  N   . MET A  234 ? 0.2931 0.2673 0.2441 -0.0158 -0.0452 -0.0151 234 MET A N   
1895 C  CA  . MET A  234 ? 0.3480 0.2852 0.1916 0.0613  -0.0372 -0.0477 234 MET A CA  
1896 C  C   . MET A  234 ? 0.2977 0.2873 0.2290 0.0194  -0.0159 -0.0392 234 MET A C   
1897 O  O   . MET A  234 ? 0.3789 0.2526 0.2331 0.0177  0.0170  -0.0364 234 MET A O   
1898 C  CB  . MET A  234 ? 0.3851 0.2465 0.2518 -0.0118 -0.0651 -0.0057 234 MET A CB  
1899 C  CG  . MET A  234 ? 0.3256 0.3831 0.1838 -0.0580 -0.0640 -0.0113 234 MET A CG  
1900 S  SD  . MET A  234 ? 0.4591 0.6347 0.2913 -0.0215 -0.1013 0.0418  234 MET A SD  
1901 C  CE  . MET A  234 ? 0.5013 0.6641 0.4492 -0.0922 -0.0463 0.1288  234 MET A CE  
1902 N  N   . ASP A  235 ? 0.3638 0.2536 0.2854 -0.0122 0.0040  -0.0780 235 ASP A N   
1903 C  CA  . ASP A  235 ? 0.4598 0.1888 0.4145 0.0017  0.0210  -0.0913 235 ASP A CA  
1904 C  C   . ASP A  235 ? 0.4159 0.3449 0.2943 0.0102  0.0221  -0.1082 235 ASP A C   
1905 O  O   . ASP A  235 ? 0.4588 0.3504 0.2971 0.0623  0.0115  -0.1011 235 ASP A O   
1906 C  CB  . ASP A  235 ? 0.6148 0.2822 0.5004 -0.1199 0.0561  -0.1377 235 ASP A CB  
1907 C  CG  . ASP A  235 ? 0.9129 0.7433 0.6901 -0.2220 0.0666  0.0550  235 ASP A CG  
1908 O  OD1 . ASP A  235 ? 1.1098 0.2676 0.7276 -0.1655 -0.0203 0.0565  235 ASP A OD1 
1909 O  OD2 . ASP A  235 ? 1.1931 0.9703 1.0975 -0.2606 -0.0690 -0.6169 235 ASP A OD2 
1910 N  N   . ASP A  236 ? 0.3490 0.2550 0.3046 0.0066  -0.0188 -0.0260 236 ASP A N   
1911 C  CA  . ASP A  236 ? 0.3488 0.2229 0.2886 0.0038  0.0054  -0.0212 236 ASP A CA  
1912 C  C   . ASP A  236 ? 0.3860 0.2046 0.2777 0.0104  0.0139  -0.0619 236 ASP A C   
1913 O  O   . ASP A  236 ? 0.4847 0.2299 0.2478 0.0475  0.0446  -0.0347 236 ASP A O   
1914 C  CB  . ASP A  236 ? 0.3942 0.2759 0.2507 0.0496  -0.0456 -0.0270 236 ASP A CB  
1915 C  CG  . ASP A  236 ? 0.4453 0.2317 0.2874 0.0761  0.0096  0.0416  236 ASP A CG  
1916 O  OD1 . ASP A  236 ? 0.4591 0.4110 0.3265 0.1270  0.0525  -0.0278 236 ASP A OD1 
1917 O  OD2 . ASP A  236 ? 0.4525 0.2996 0.2889 0.0392  0.0310  0.0250  236 ASP A OD2 
1918 N  N   . PRO A  237 ? 0.4592 0.2235 0.2442 0.0247  0.0588  -0.0321 237 PRO A N   
1919 C  CA  . PRO A  237 ? 0.4162 0.2682 0.3276 0.0325  0.1096  -0.1043 237 PRO A CA  
1920 C  C   . PRO A  237 ? 0.4681 0.2163 0.3331 0.0137  0.0634  -0.0435 237 PRO A C   
1921 O  O   . PRO A  237 ? 0.4467 0.3201 0.3259 0.1121  0.1162  -0.0292 237 PRO A O   
1922 C  CB  . PRO A  237 ? 0.5662 0.2593 0.4135 0.0539  0.1523  -0.0506 237 PRO A CB  
1923 C  CG  . PRO A  237 ? 0.5298 0.3916 0.4540 0.2327  0.0653  0.0581  237 PRO A CG  
1924 C  CD  . PRO A  237 ? 0.4832 0.2214 0.4315 0.1170  0.0739  0.0544  237 PRO A CD  
1925 N  N   . SER A  238 ? 0.3844 0.2628 0.2988 0.0886  0.0265  -0.0498 238 SER A N   
1926 C  CA  . SER A  238 ? 0.3538 0.2793 0.2852 0.0941  0.0122  -0.0836 238 SER A CA  
1927 C  C   . SER A  238 ? 0.3625 0.2867 0.3334 0.0983  0.0554  -0.0458 238 SER A C   
1928 O  O   . SER A  238 ? 0.3143 0.3504 0.3059 0.0600  0.0312  -0.0185 238 SER A O   
1929 C  CB  . SER A  238 ? 0.4323 0.3793 0.3749 0.2130  -0.0047 -0.0494 238 SER A CB  
1930 O  OG  . SER A  238 ? 0.5613 0.3556 0.5851 0.1749  0.0937  -0.0679 238 SER A OG  
1931 N  N   . PRO A  239 ? 0.2946 0.2463 0.3237 0.0440  0.0474  -0.0673 239 PRO A N   
1932 C  CA  . PRO A  239 ? 0.3529 0.2712 0.2219 0.0359  0.0576  -0.0961 239 PRO A CA  
1933 C  C   . PRO A  239 ? 0.2515 0.2830 0.3181 0.0462  0.0673  -0.0668 239 PRO A C   
1934 O  O   . PRO A  239 ? 0.2741 0.3333 0.3308 0.0188  0.0722  -0.0647 239 PRO A O   
1935 C  CB  . PRO A  239 ? 0.2908 0.3121 0.3279 0.0502  0.0540  -0.0463 239 PRO A CB  
1936 C  CG  . PRO A  239 ? 0.4170 0.3093 0.3559 0.0483  0.0929  -0.0845 239 PRO A CG  
1937 C  CD  . PRO A  239 ? 0.3670 0.2688 0.3475 0.0691  0.0268  -0.0472 239 PRO A CD  
1938 N  N   . ARG A  240 ? 0.2660 0.2847 0.2786 0.0196  0.0556  -0.0935 240 ARG A N   
1939 C  CA  . ARG A  240 ? 0.2405 0.2614 0.3039 0.0100  0.0663  -0.1039 240 ARG A CA  
1940 C  C   . ARG A  240 ? 0.2499 0.2097 0.2776 0.0040  0.0557  -0.0525 240 ARG A C   
1941 O  O   . ARG A  240 ? 0.2167 0.2639 0.3356 -0.0186 0.0542  -0.0546 240 ARG A O   
1942 C  CB  . ARG A  240 ? 0.4668 0.4126 0.3847 0.1516  0.1437  0.0409  240 ARG A CB  
1943 C  CG  . ARG A  240 ? 0.7738 0.5545 0.4534 0.2132  0.0558  -0.0449 240 ARG A CG  
1944 C  CD  . ARG A  240 ? 1.0599 1.0671 0.4155 0.0120  0.2116  0.2238  240 ARG A CD  
1945 N  NE  . ARG A  240 ? 1.2160 0.7194 0.3310 -0.1603 -0.1844 0.0584  240 ARG A NE  
1946 C  CZ  . ARG A  240 ? 0.8357 0.7600 0.6614 0.1280  -0.1011 0.3062  240 ARG A CZ  
1947 N  NH1 . ARG A  240 ? 1.5791 1.3248 1.0058 0.0178  -0.0999 -0.2593 240 ARG A NH1 
1948 N  NH2 . ARG A  240 ? 0.5319 0.9707 0.6810 0.1702  -0.0688 0.2637  240 ARG A NH2 
1949 N  N   . GLU A  241 ? 0.1955 0.2233 0.2762 -0.0069 0.0373  -0.0498 241 GLU A N   
1950 C  CA  . GLU A  241 ? 0.2160 0.2429 0.2606 -0.0012 0.0337  -0.0762 241 GLU A CA  
1951 C  C   . GLU A  241 ? 0.1707 0.2925 0.2559 -0.0114 0.0110  -0.0546 241 GLU A C   
1952 O  O   . GLU A  241 ? 0.2216 0.3053 0.2869 0.0420  -0.0052 -0.0880 241 GLU A O   
1953 C  CB  . GLU A  241 ? 0.2582 0.2920 0.3799 -0.0535 0.0892  -0.0498 241 GLU A CB  
1954 C  CG  . GLU A  241 ? 0.3638 0.3894 0.4535 -0.0188 0.1712  0.0309  241 GLU A CG  
1955 C  CD  . GLU A  241 ? 0.5723 0.5646 0.5307 -0.2321 0.1620  0.0384  241 GLU A CD  
1956 O  OE1 . GLU A  241 ? 1.1108 0.7343 0.6452 -0.4227 0.2391  -0.0170 241 GLU A OE1 
1957 O  OE2 . GLU A  241 ? 0.7530 0.5761 0.5668 0.0649  0.2007  0.1535  241 GLU A OE2 
1958 N  N   . MET A  242 ? 0.1922 0.2001 0.2056 -0.0161 0.0198  -0.0270 242 MET A N   
1959 C  CA  . MET A  242 ? 0.1785 0.1861 0.1976 -0.0080 -0.0071 -0.0447 242 MET A CA  
1960 C  C   . MET A  242 ? 0.1672 0.1676 0.1480 -0.0026 -0.0164 -0.0048 242 MET A C   
1961 O  O   . MET A  242 ? 0.1739 0.1879 0.1741 0.0153  -0.0097 -0.0265 242 MET A O   
1962 C  CB  . MET A  242 ? 0.1609 0.2234 0.1700 -0.0233 0.0070  -0.0176 242 MET A CB  
1963 C  CG  . MET A  242 ? 0.1913 0.1983 0.1597 -0.0350 -0.0063 0.0139  242 MET A CG  
1964 S  SD  . MET A  242 ? 0.2116 0.2178 0.1854 -0.0324 0.0160  -0.0234 242 MET A SD  
1965 C  CE  . MET A  242 ? 0.2561 0.1974 0.2316 -0.0604 0.0392  -0.0052 242 MET A CE  
1966 N  N   . ILE A  243 ? 0.1558 0.1801 0.1424 -0.0072 -0.0161 -0.0122 243 ILE A N   
1967 C  CA  . ILE A  243 ? 0.1417 0.1691 0.1363 -0.0117 0.0054  -0.0100 243 ILE A CA  
1968 C  C   . ILE A  243 ? 0.1266 0.1615 0.1689 0.0052  0.0257  0.0179  243 ILE A C   
1969 O  O   . ILE A  243 ? 0.1507 0.1516 0.1629 -0.0013 0.0207  0.0058  243 ILE A O   
1970 C  CB  . ILE A  243 ? 0.1600 0.1826 0.1657 0.0160  0.0176  0.0165  243 ILE A CB  
1971 C  CG1 . ILE A  243 ? 0.1801 0.2394 0.1790 0.0106  0.0334  0.0001  243 ILE A CG1 
1972 C  CG2 . ILE A  243 ? 0.1953 0.2509 0.1781 -0.0254 -0.0075 0.0248  243 ILE A CG2 
1973 C  CD1 . ILE A  243 ? 0.1825 0.3009 0.2509 0.0107  0.0570  0.0092  243 ILE A CD1 
1974 N  N   . ASN A  244 ? 0.1264 0.1661 0.1392 -0.0022 0.0016  -0.0102 244 ASN A N   
1975 C  CA  . ASN A  244 ? 0.1082 0.1484 0.1500 -0.0059 0.0074  0.0021  244 ASN A CA  
1976 C  C   . ASN A  244 ? 0.1282 0.1434 0.1481 -0.0012 0.0032  -0.0013 244 ASN A C   
1977 O  O   . ASN A  244 ? 0.1283 0.1429 0.1711 0.0111  0.0168  0.0148  244 ASN A O   
1978 C  CB  . ASN A  244 ? 0.1209 0.1967 0.1775 0.0081  0.0131  0.0173  244 ASN A CB  
1979 C  CG  . ASN A  244 ? 0.1320 0.1928 0.1861 0.0146  0.0133  0.0205  244 ASN A CG  
1980 O  OD1 . ASN A  244 ? 0.1507 0.2138 0.2096 -0.0111 0.0314  0.0212  244 ASN A OD1 
1981 N  ND2 . ASN A  244 ? 0.1683 0.2913 0.2275 0.0216  0.0516  -0.0089 244 ASN A ND2 
1982 N  N   . ASN A  245 ? 0.1185 0.1358 0.1407 0.0042  0.0129  -0.0044 245 ASN A N   
1983 C  CA  . ASN A  245 ? 0.1154 0.1213 0.1446 -0.0085 0.0062  0.0177  245 ASN A CA  
1984 C  C   . ASN A  245 ? 0.1156 0.1062 0.1439 -0.0052 0.0103  0.0120  245 ASN A C   
1985 O  O   . ASN A  245 ? 0.1191 0.1606 0.1448 -0.0107 0.0157  -0.0135 245 ASN A O   
1986 C  CB  . ASN A  245 ? 0.1177 0.1342 0.1684 0.0060  -0.0069 -0.0085 245 ASN A CB  
1987 C  CG  . ASN A  245 ? 0.1096 0.1194 0.1445 -0.0053 -0.0091 -0.0146 245 ASN A CG  
1988 O  OD1 . ASN A  245 ? 0.1256 0.1309 0.1828 0.0015  -0.0096 -0.0098 245 ASN A OD1 
1989 N  ND2 . ASN A  245 ? 0.1158 0.1606 0.1976 -0.0068 -0.0197 0.0017  245 ASN A ND2 
1990 N  N   . PHE A  246 ? 0.1236 0.1246 0.1249 0.0039  -0.0122 0.0172  246 PHE A N   
1991 C  CA  . PHE A  246 ? 0.1282 0.1121 0.1388 0.0122  -0.0176 0.0175  246 PHE A CA  
1992 C  C   . PHE A  246 ? 0.1019 0.1191 0.1242 0.0052  -0.0044 0.0033  246 PHE A C   
1993 O  O   . PHE A  246 ? 0.1142 0.1320 0.1463 0.0110  0.0024  0.0081  246 PHE A O   
1994 C  CB  . PHE A  246 ? 0.1463 0.1317 0.1523 0.0066  0.0095  0.0078  246 PHE A CB  
1995 C  CG  . PHE A  246 ? 0.1523 0.1075 0.1321 0.0047  -0.0077 0.0011  246 PHE A CG  
1996 C  CD1 . PHE A  246 ? 0.1372 0.1346 0.1517 -0.0015 -0.0033 0.0321  246 PHE A CD1 
1997 C  CD2 . PHE A  246 ? 0.1675 0.1262 0.1673 -0.0201 -0.0251 0.0164  246 PHE A CD2 
1998 C  CE1 . PHE A  246 ? 0.1411 0.1333 0.1732 -0.0197 -0.0024 0.0031  246 PHE A CE1 
1999 C  CE2 . PHE A  246 ? 0.1527 0.1690 0.1907 -0.0124 -0.0499 0.0257  246 PHE A CE2 
2000 C  CZ  . PHE A  246 ? 0.1313 0.1308 0.1870 -0.0092 -0.0231 0.0084  246 PHE A CZ  
2001 N  N   . ARG A  247 ? 0.1256 0.1042 0.1259 0.0003  -0.0089 0.0206  247 ARG A N   
2002 C  CA  . ARG A  247 ? 0.1066 0.1071 0.1319 -0.0095 -0.0048 0.0254  247 ARG A CA  
2003 C  C   . ARG A  247 ? 0.1186 0.0969 0.1267 0.0020  -0.0043 0.0081  247 ARG A C   
2004 O  O   . ARG A  247 ? 0.1159 0.1028 0.1493 -0.0082 -0.0060 0.0081  247 ARG A O   
2005 C  CB  . ARG A  247 ? 0.1118 0.1185 0.1370 -0.0076 -0.0055 0.0356  247 ARG A CB  
2006 C  CG  . ARG A  247 ? 0.1164 0.1109 0.1341 -0.0065 -0.0073 0.0359  247 ARG A CG  
2007 C  CD  . ARG A  247 ? 0.1150 0.0944 0.1563 0.0064  0.0000  0.0245  247 ARG A CD  
2008 N  NE  . ARG A  247 ? 0.1181 0.1000 0.1430 -0.0024 -0.0057 0.0233  247 ARG A NE  
2009 C  CZ  . ARG A  247 ? 0.1087 0.1195 0.1412 -0.0019 -0.0185 0.0220  247 ARG A CZ  
2010 N  NH1 . ARG A  247 ? 0.1286 0.1172 0.1597 -0.0092 0.0115  -0.0010 247 ARG A NH1 
2011 N  NH2 . ARG A  247 ? 0.1186 0.1055 0.1800 -0.0060 -0.0243 0.0209  247 ARG A NH2 
2012 N  N   . GLN A  248 ? 0.1106 0.1107 0.1392 -0.0006 -0.0049 0.0078  248 GLN A N   
2013 C  CA  . GLN A  248 ? 0.0987 0.0937 0.1466 -0.0001 -0.0118 0.0071  248 GLN A CA  
2014 C  C   . GLN A  248 ? 0.1091 0.1036 0.1408 0.0053  -0.0105 0.0139  248 GLN A C   
2015 O  O   . GLN A  248 ? 0.1080 0.1188 0.1401 0.0004  -0.0061 0.0168  248 GLN A O   
2016 C  CB  . GLN A  248 ? 0.1147 0.1175 0.1505 -0.0020 -0.0114 0.0058  248 GLN A CB  
2017 C  CG  . GLN A  248 ? 0.1091 0.1280 0.1389 0.0086  0.0036  0.0305  248 GLN A CG  
2018 C  CD  . GLN A  248 ? 0.1089 0.1233 0.1400 -0.0047 -0.0041 0.0122  248 GLN A CD  
2019 O  OE1 . GLN A  248 ? 0.1483 0.1432 0.1655 -0.0188 -0.0193 0.0303  248 GLN A OE1 
2020 N  NE2 . GLN A  248 ? 0.1396 0.1715 0.1751 -0.0300 -0.0281 0.0325  248 GLN A NE2 
2021 N  N   . VAL A  249 ? 0.1071 0.1107 0.1291 0.0062  -0.0117 0.0110  249 VAL A N   
2022 C  CA  . VAL A  249 ? 0.1246 0.1173 0.1304 0.0040  -0.0215 0.0117  249 VAL A CA  
2023 C  C   . VAL A  249 ? 0.1018 0.1080 0.1285 0.0126  -0.0212 -0.0048 249 VAL A C   
2024 O  O   . VAL A  249 ? 0.1130 0.1204 0.1498 0.0094  -0.0055 0.0148  249 VAL A O   
2025 C  CB  . VAL A  249 ? 0.1425 0.1025 0.1817 0.0062  -0.0312 0.0147  249 VAL A CB  
2026 C  CG1 . VAL A  249 ? 0.1523 0.1080 0.1779 0.0143  -0.0256 0.0091  249 VAL A CG1 
2027 C  CG2 . VAL A  249 ? 0.1498 0.1436 0.2101 -0.0172 -0.0361 0.0106  249 VAL A CG2 
2028 N  N   . GLN A  250 ? 0.1128 0.1102 0.1274 0.0031  -0.0143 0.0006  250 GLN A N   
2029 C  CA  . GLN A  250 ? 0.1251 0.1260 0.1367 -0.0016 -0.0190 0.0190  250 GLN A CA  
2030 C  C   . GLN A  250 ? 0.1351 0.1215 0.1463 -0.0084 -0.0149 0.0118  250 GLN A C   
2031 O  O   . GLN A  250 ? 0.1814 0.1378 0.1638 -0.0063 -0.0212 0.0020  250 GLN A O   
2032 C  CB  . GLN A  250 ? 0.1183 0.1226 0.1511 -0.0187 -0.0089 0.0150  250 GLN A CB  
2033 C  CG  . GLN A  250 ? 0.1226 0.1093 0.1601 0.0020  -0.0002 0.0017  250 GLN A CG  
2034 C  CD  . GLN A  250 ? 0.1168 0.0987 0.1568 -0.0063 -0.0237 0.0111  250 GLN A CD  
2035 O  OE1 . GLN A  250 ? 0.1229 0.1102 0.1750 0.0140  -0.0063 0.0279  250 GLN A OE1 
2036 N  NE2 . GLN A  250 ? 0.1173 0.1086 0.1381 -0.0131 -0.0143 0.0058  250 GLN A NE2 
2037 N  N   . LYS A  251 ? 0.1307 0.1702 0.1451 -0.0076 -0.0071 0.0212  251 LYS A N   
2038 C  CA  . LYS A  251 ? 0.1215 0.1867 0.1516 -0.0181 -0.0138 0.0198  251 LYS A CA  
2039 C  C   . LYS A  251 ? 0.1351 0.1706 0.1548 -0.0006 -0.0092 0.0247  251 LYS A C   
2040 O  O   . LYS A  251 ? 0.1254 0.2035 0.1843 -0.0013 -0.0013 0.0172  251 LYS A O   
2041 C  CB  . LYS A  251 ? 0.1114 0.2865 0.1595 0.0436  0.0039  0.0290  251 LYS A CB  
2042 C  CG  . LYS A  251 ? 0.1464 0.3224 0.1969 0.0391  0.0252  0.0031  251 LYS A CG  
2043 C  CD  . LYS A  251 ? 0.1574 0.3212 0.1849 0.0521  0.0519  0.0432  251 LYS A CD  
2044 C  CE  . LYS A  251 ? 0.1238 0.1804 0.1592 0.0004  -0.0061 0.0121  251 LYS A CE  
2045 N  NZ  . LYS A  251 ? 0.1141 0.1359 0.1610 -0.0126 -0.0058 0.0197  251 LYS A NZ  
2046 N  N   . PHE A  252 ? 0.1567 0.2062 0.1899 0.0070  -0.0020 0.0120  252 PHE A N   
2047 C  CA  . PHE A  252 ? 0.1824 0.2239 0.1560 0.0325  -0.0174 -0.0095 252 PHE A CA  
2048 C  C   . PHE A  252 ? 0.2187 0.2737 0.1820 0.0000  -0.0122 0.0075  252 PHE A C   
2049 O  O   . PHE A  252 ? 0.2530 0.3052 0.3076 -0.0310 -0.0368 0.0127  252 PHE A O   
2050 C  CB  . PHE A  252 ? 0.2338 0.1770 0.1907 0.0513  0.0082  -0.0065 252 PHE A CB  
2051 C  CG  . PHE A  252 ? 0.1934 0.2122 0.1868 0.0298  -0.0306 0.0113  252 PHE A CG  
2052 C  CD1 . PHE A  252 ? 0.1897 0.2735 0.1558 0.0212  -0.0179 0.0181  252 PHE A CD1 
2053 C  CD2 . PHE A  252 ? 0.2587 0.2106 0.1870 0.0252  0.0064  0.0227  252 PHE A CD2 
2054 C  CE1 . PHE A  252 ? 0.2086 0.2675 0.1988 0.0328  -0.0088 0.0179  252 PHE A CE1 
2055 C  CE2 . PHE A  252 ? 0.2678 0.2268 0.2155 0.0394  0.0294  0.0303  252 PHE A CE2 
2056 C  CZ  . PHE A  252 ? 0.2706 0.2649 0.1812 0.0323  0.0355  0.0318  252 PHE A CZ  
2057 N  N   . ASP A  253 ? 0.3337 0.3447 0.2076 0.0254  -0.0541 0.0250  253 ASP A N   
2058 C  CA  . ASP A  253 ? 0.2578 0.3986 0.1556 0.0435  -0.0612 0.0167  253 ASP A CA  
2059 C  C   . ASP A  253 ? 0.2627 0.2753 0.2500 0.0245  -0.0296 -0.0512 253 ASP A C   
2060 O  O   . ASP A  253 ? 0.2939 0.3297 0.2300 0.0153  -0.0266 -0.0153 253 ASP A O   
2061 C  CB  . ASP A  253 ? 0.3656 0.3941 0.2744 0.1140  -0.0431 0.0032  253 ASP A CB  
2062 C  CG  . ASP A  253 ? 0.5791 0.6809 0.7231 -0.0407 -0.1393 -0.1327 253 ASP A CG  
2063 O  OD1 . ASP A  253 ? 0.3797 0.6760 0.7154 0.1252  -0.1613 -0.0476 253 ASP A OD1 
2064 O  OD2 . ASP A  253 ? 0.9530 0.6301 0.6412 0.1877  0.2857  0.0850  253 ASP A OD2 
2065 N  N   . GLU A  254 ? 0.2746 0.3125 0.2328 0.0418  -0.0408 -0.0272 254 GLU A N   
2066 C  CA  . GLU A  254 ? 0.2639 0.3453 0.2477 0.0568  -0.0140 -0.0306 254 GLU A CA  
2067 C  C   . GLU A  254 ? 0.2489 0.3813 0.2545 -0.0088 -0.0479 0.0432  254 GLU A C   
2068 O  O   . GLU A  254 ? 0.3259 0.4193 0.2437 0.0197  -0.0208 0.0561  254 GLU A O   
2069 C  CB  . GLU A  254 ? 0.2922 0.4182 0.2474 0.0158  0.0031  0.0454  254 GLU A CB  
2070 C  CG  . GLU A  254 ? 0.2735 0.5440 0.3565 0.0521  -0.0212 -0.0529 254 GLU A CG  
2071 C  CD  . GLU A  254 ? 0.6296 0.5866 0.2902 -0.1513 -0.0396 0.1376  254 GLU A CD  
2072 O  OE1 . GLU A  254 ? 0.7989 1.1166 0.4528 -0.0524 -0.0792 -0.1376 254 GLU A OE1 
2073 O  OE2 . GLU A  254 ? 0.4761 0.8456 0.6362 -0.0489 0.0328  0.1003  254 GLU A OE2 
2074 N  N   . ARG A  255 ? 0.2815 0.2597 0.2582 0.0289  -0.0395 0.0200  255 ARG A N   
2075 C  CA  . ARG A  255 ? 0.2570 0.3164 0.2290 0.0388  -0.0249 -0.0019 255 ARG A CA  
2076 C  C   . ARG A  255 ? 0.2967 0.3216 0.2352 0.0593  0.0134  0.0287  255 ARG A C   
2077 O  O   . ARG A  255 ? 0.2540 0.3132 0.2820 0.0161  -0.0364 0.0017  255 ARG A O   
2078 C  CB  . ARG A  255 ? 0.2429 0.2840 0.2218 0.0223  -0.0376 -0.0072 255 ARG A CB  
2079 C  CG  . ARG A  255 ? 0.3182 0.2676 0.2097 0.0341  -0.0378 -0.0196 255 ARG A CG  
2080 C  CD  . ARG A  255 ? 0.2445 0.2508 0.2863 -0.0046 -0.0604 0.0125  255 ARG A CD  
2081 N  NE  . ARG A  255 ? 0.2766 0.2992 0.2505 -0.0302 -0.0581 0.0221  255 ARG A NE  
2082 C  CZ  . ARG A  255 ? 0.2468 0.2606 0.2209 -0.0502 -0.0324 0.0244  255 ARG A CZ  
2083 N  NH1 . ARG A  255 ? 0.2833 0.2065 0.2722 -0.0158 -0.0798 -0.0088 255 ARG A NH1 
2084 N  NH2 . ARG A  255 ? 0.1919 0.2523 0.2184 -0.0179 -0.0505 0.0226  255 ARG A NH2 
2085 N  N   . LEU A  256 ? 0.2776 0.3146 0.2689 0.0457  -0.0084 0.0016  256 LEU A N   
2086 C  CA  . LEU A  256 ? 0.2870 0.3018 0.2175 0.0507  -0.0575 -0.0053 256 LEU A CA  
2087 C  C   . LEU A  256 ? 0.2427 0.2527 0.2186 0.0359  -0.0118 -0.0042 256 LEU A C   
2088 O  O   . LEU A  256 ? 0.2757 0.2769 0.2565 0.0483  -0.0495 -0.0005 256 LEU A O   
2089 C  CB  . LEU A  256 ? 0.3389 0.3167 0.1773 0.0519  -0.0634 0.0221  256 LEU A CB  
2090 C  CG  . LEU A  256 ? 0.2946 0.3865 0.2462 0.0157  -0.0590 -0.0098 256 LEU A CG  
2091 C  CD1 . LEU A  256 ? 0.5276 0.3921 0.2365 0.1023  -0.0312 -0.0468 256 LEU A CD1 
2092 C  CD2 . LEU A  256 ? 0.4722 0.4840 0.2809 -0.0858 0.0391  0.0113  256 LEU A CD2 
2093 N  N   . VAL A  257 ? 0.2017 0.2483 0.1986 0.0209  -0.0188 -0.0015 257 VAL A N   
2094 C  CA  . VAL A  257 ? 0.1988 0.2166 0.2280 0.0233  -0.0477 -0.0282 257 VAL A CA  
2095 C  C   . VAL A  257 ? 0.1952 0.1955 0.1840 0.0105  -0.0314 -0.0409 257 VAL A C   
2096 O  O   . VAL A  257 ? 0.1998 0.2294 0.2348 -0.0218 -0.0339 -0.0730 257 VAL A O   
2097 C  CB  . VAL A  257 ? 0.1988 0.2454 0.1994 0.0165  -0.0225 -0.0159 257 VAL A CB  
2098 C  CG1 . VAL A  257 ? 0.1940 0.2557 0.2079 0.0303  -0.0286 0.0089  257 VAL A CG1 
2099 C  CG2 . VAL A  257 ? 0.2247 0.3018 0.2231 0.0621  -0.0446 -0.0548 257 VAL A CG2 
2100 N  N   . TYR A  258 ? 0.2058 0.1967 0.1770 -0.0125 -0.0102 0.0010  258 TYR A N   
2101 C  CA  . TYR A  258 ? 0.2190 0.1699 0.1775 -0.0203 0.0059  0.0003  258 TYR A CA  
2102 C  C   . TYR A  258 ? 0.1849 0.1814 0.1727 -0.0055 -0.0126 -0.0053 258 TYR A C   
2103 O  O   . TYR A  258 ? 0.2380 0.1992 0.1852 0.0040  -0.0638 -0.0278 258 TYR A O   
2104 C  CB  . TYR A  258 ? 0.2251 0.2165 0.1606 -0.0325 -0.0190 0.0361  258 TYR A CB  
2105 C  CG  . TYR A  258 ? 0.2493 0.2603 0.1856 -0.0408 -0.0095 0.0381  258 TYR A CG  
2106 C  CD1 . TYR A  258 ? 0.3198 0.3529 0.1672 -0.0510 -0.0261 0.0227  258 TYR A CD1 
2107 C  CD2 . TYR A  258 ? 0.3567 0.2312 0.2072 -0.0552 0.0201  0.0422  258 TYR A CD2 
2108 C  CE1 . TYR A  258 ? 0.3255 0.3066 0.2558 0.0035  -0.0185 0.0710  258 TYR A CE1 
2109 C  CE2 . TYR A  258 ? 0.3696 0.3694 0.2752 -0.0287 0.0139  0.1147  258 TYR A CE2 
2110 C  CZ  . TYR A  258 ? 0.3753 0.3141 0.2410 0.0126  -0.0152 0.0897  258 TYR A CZ  
2111 O  OH  . TYR A  258 ? 0.5230 0.3963 0.3561 0.0494  -0.1043 0.1157  258 TYR A OH  
2112 N  N   . THR A  259 ? 0.2096 0.1688 0.1835 -0.0276 -0.0226 -0.0198 259 THR A N   
2113 C  CA  . THR A  259 ? 0.2050 0.1742 0.1699 -0.0288 -0.0145 -0.0027 259 THR A CA  
2114 C  C   . THR A  259 ? 0.1827 0.1801 0.1682 -0.0301 0.0087  -0.0190 259 THR A C   
2115 O  O   . THR A  259 ? 0.2537 0.1882 0.1593 -0.0194 0.0004  -0.0315 259 THR A O   
2116 C  CB  . THR A  259 ? 0.2067 0.2342 0.1725 -0.0361 0.0150  -0.0330 259 THR A CB  
2117 O  OG1 . THR A  259 ? 0.2692 0.2663 0.1857 -0.0767 0.0097  -0.0373 259 THR A OG1 
2118 C  CG2 . THR A  259 ? 0.2048 0.2338 0.2089 -0.0264 0.0245  -0.0110 259 THR A CG2 
2119 N  N   . SER A  260 ? 0.2123 0.1520 0.1920 0.0009  0.0015  -0.0357 260 SER A N   
2120 C  CA  . SER A  260 ? 0.2507 0.2123 0.1909 0.0158  0.0238  -0.0489 260 SER A CA  
2121 C  C   . SER A  260 ? 0.2730 0.2155 0.1952 0.0364  0.0287  -0.0508 260 SER A C   
2122 O  O   . SER A  260 ? 0.3270 0.2685 0.3098 0.0807  0.0283  -0.0862 260 SER A O   
2123 C  CB  . SER A  260 ? 0.2170 0.2341 0.1918 0.0050  0.0407  -0.0068 260 SER A CB  
2124 O  OG  . SER A  260 ? 0.2049 0.1952 0.1817 0.0099  0.0302  -0.0334 260 SER A OG  
2125 N  N   . PHE A  261 ? 0.2743 0.1784 0.2431 -0.0124 0.0116  -0.0374 261 PHE A N   
2126 C  CA  . PHE A  261 ? 0.2995 0.1762 0.3039 -0.0223 0.0203  -0.0189 261 PHE A CA  
2127 C  C   . PHE A  261 ? 0.2730 0.1920 0.3184 -0.0488 0.0128  -0.0396 261 PHE A C   
2128 O  O   . PHE A  261 ? 0.3218 0.2508 0.3195 -0.0300 -0.0058 -0.0359 261 PHE A O   
2129 C  CB  . PHE A  261 ? 0.3413 0.1659 0.3306 -0.0154 0.0784  -0.0046 261 PHE A CB  
2130 C  CG  . PHE A  261 ? 0.3285 0.2053 0.2417 -0.0124 0.0283  -0.0140 261 PHE A CG  
2131 C  CD1 . PHE A  261 ? 0.3452 0.1881 0.3182 -0.0068 0.0211  -0.0274 261 PHE A CD1 
2132 C  CD2 . PHE A  261 ? 0.2789 0.1596 0.2389 0.0129  -0.0073 -0.0130 261 PHE A CD2 
2133 C  CE1 . PHE A  261 ? 0.3475 0.2480 0.3544 -0.0406 0.0555  -0.0900 261 PHE A CE1 
2134 C  CE2 . PHE A  261 ? 0.2514 0.1777 0.2162 -0.0069 0.0239  0.0115  261 PHE A CE2 
2135 C  CZ  . PHE A  261 ? 0.2739 0.1852 0.2527 0.0075  0.0238  0.0075  261 PHE A CZ  
2136 N  N   . SER A  262 ? 0.4768 0.2402 0.3471 -0.1014 -0.0572 -0.0811 262 SER A N   
2137 C  CA  . SER A  262 ? 0.4025 0.3666 0.3840 -0.1497 0.0230  -0.0611 262 SER A CA  
2138 C  C   . SER A  262 ? 0.4825 0.4258 0.6876 -0.1980 -0.0093 0.0770  262 SER A C   
2139 O  O   . SER A  262 ? 0.4938 0.3213 1.0468 -0.0982 0.2253  -0.0432 262 SER A O   
2140 C  CB  . SER A  262 ? 0.8374 0.3112 0.5141 -0.1036 0.1333  -0.0746 262 SER A CB  
2141 O  OG  . SER A  262 ? 1.0681 0.4087 0.5794 0.0091  -0.1289 -0.1521 262 SER A OG  
2142 N  N   . GLN A  263 ? 1.0726 0.4518 0.3520 -0.1131 -0.0588 0.1233  263 GLN A N   
2143 C  CA  . GLN A  263 ? 1.0171 0.5727 0.8003 -0.0333 0.3028  0.1984  263 GLN A CA  
2144 C  C   . GLN A  263 ? 1.5259 0.7016 0.9113 0.3515  0.4307  -0.1335 263 GLN A C   
2145 O  O   . GLN A  263 ? 1.2525 0.2552 1.1763 0.1080  0.1564  0.1060  263 GLN A O   
2146 C  CB  . GLN A  263 ? 1.4448 0.2831 1.1528 0.1316  0.1962  0.1079  263 GLN A CB  
2147 C  CG  . GLN A  263 ? 1.7374 0.2611 1.0990 -0.3323 0.3203  -0.1193 263 GLN A CG  
2148 C  CD  . GLN A  263 ? 0.6248 0.5289 0.7393 -0.1717 -0.2411 -0.0342 263 GLN A CD  
2149 O  OE1 . GLN A  263 ? 0.5464 0.7052 0.4661 -0.0378 -0.0228 0.2678  263 GLN A OE1 
2150 N  NE2 . GLN A  263 ? 0.4553 0.2369 0.4103 -0.1423 0.0207  -0.0277 263 GLN A NE2 
2151 N  N   . LYS B  3   ? 1.1100 0.1058 1.6308 -0.0734 -0.0967 0.2069  3   LYS B N   
2152 C  CA  . LYS B  3   ? 0.7532 0.2245 0.5950 -0.1017 -0.2997 0.1587  3   LYS B CA  
2153 C  C   . LYS B  3   ? 0.6454 0.3069 0.4227 0.0580  0.1103  0.1214  3   LYS B C   
2154 O  O   . LYS B  3   ? 0.5554 0.3801 0.3416 -0.0564 0.0881  0.0652  3   LYS B O   
2155 C  CB  . LYS B  3   ? 1.4519 0.2694 1.1785 0.0429  -0.4973 0.1375  3   LYS B CB  
2156 C  CG  . LYS B  3   ? 0.5554 0.6242 1.0470 0.0781  -0.4274 -0.0462 3   LYS B CG  
2157 C  CD  . LYS B  3   ? 0.7368 0.4242 0.8646 -0.0719 0.0447  -0.1644 3   LYS B CD  
2158 C  CE  . LYS B  3   ? 0.6135 0.3053 0.5958 -0.0809 0.0560  -0.0195 3   LYS B CE  
2159 N  NZ  . LYS B  3   ? 0.8096 0.4606 0.7728 0.0785  0.0479  0.2991  3   LYS B NZ  
2160 N  N   . TRP B  4   ? 0.2500 0.1484 0.2547 -0.0081 -0.0046 0.0469  4   TRP B N   
2161 C  CA  . TRP B  4   ? 0.2117 0.1454 0.2007 -0.0223 -0.0121 0.0330  4   TRP B CA  
2162 C  C   . TRP B  4   ? 0.1674 0.1464 0.1881 -0.0308 -0.0020 0.0355  4   TRP B C   
2163 O  O   . TRP B  4   ? 0.1857 0.1626 0.2196 -0.0082 -0.0173 0.0243  4   TRP B O   
2164 C  CB  . TRP B  4   ? 0.1796 0.1224 0.1858 -0.0113 -0.0147 0.0029  4   TRP B CB  
2165 C  CG  . TRP B  4   ? 0.1656 0.1231 0.1739 -0.0034 -0.0489 0.0195  4   TRP B CG  
2166 C  CD1 . TRP B  4   ? 0.1843 0.1493 0.2104 -0.0011 -0.0212 0.0434  4   TRP B CD1 
2167 C  CD2 . TRP B  4   ? 0.1360 0.1179 0.1684 -0.0079 -0.0211 0.0243  4   TRP B CD2 
2168 N  NE1 . TRP B  4   ? 0.1866 0.1400 0.1924 0.0085  -0.0070 0.0308  4   TRP B NE1 
2169 C  CE2 . TRP B  4   ? 0.1628 0.1295 0.1737 0.0079  -0.0218 0.0337  4   TRP B CE2 
2170 C  CE3 . TRP B  4   ? 0.1629 0.1247 0.1702 0.0024  -0.0102 0.0216  4   TRP B CE3 
2171 C  CZ2 . TRP B  4   ? 0.1781 0.1682 0.1658 -0.0261 -0.0399 0.0294  4   TRP B CZ2 
2172 C  CZ3 . TRP B  4   ? 0.1634 0.1514 0.1470 -0.0192 -0.0075 0.0057  4   TRP B CZ3 
2173 C  CH2 . TRP B  4   ? 0.1556 0.1569 0.1421 -0.0228 -0.0167 0.0309  4   TRP B CH2 
2174 N  N   . THR B  5   ? 0.1725 0.1359 0.1979 -0.0179 -0.0128 0.0310  5   THR B N   
2175 C  CA  . THR B  5   ? 0.2054 0.1615 0.1813 -0.0288 -0.0229 0.0140  5   THR B CA  
2176 C  C   . THR B  5   ? 0.1544 0.1429 0.1481 -0.0315 -0.0061 0.0114  5   THR B C   
2177 O  O   . THR B  5   ? 0.1638 0.1349 0.1610 -0.0288 -0.0030 0.0148  5   THR B O   
2178 C  CB  . THR B  5   ? 0.2116 0.1653 0.2120 -0.0205 0.0022  0.0528  5   THR B CB  
2179 O  OG1 . THR B  5   ? 0.2060 0.1996 0.2319 -0.0130 0.0231  0.0582  5   THR B OG1 
2180 C  CG2 . THR B  5   ? 0.3037 0.1708 0.1822 -0.0291 0.0052  0.0597  5   THR B CG2 
2181 N  N   . TYR B  6   ? 0.1804 0.1554 0.1539 -0.0362 0.0029  0.0185  6   TYR B N   
2182 C  CA  . TYR B  6   ? 0.1491 0.1545 0.2115 -0.0290 0.0256  0.0348  6   TYR B CA  
2183 C  C   . TYR B  6   ? 0.1743 0.1539 0.1890 -0.0332 0.0207  0.0145  6   TYR B C   
2184 O  O   . TYR B  6   ? 0.1734 0.1672 0.2057 -0.0290 0.0009  0.0049  6   TYR B O   
2185 C  CB  . TYR B  6   ? 0.1681 0.1509 0.1912 -0.0487 0.0293  0.0023  6   TYR B CB  
2186 C  CG  . TYR B  6   ? 0.1615 0.1064 0.1537 -0.0278 -0.0023 0.0017  6   TYR B CG  
2187 C  CD1 . TYR B  6   ? 0.1801 0.1114 0.1622 -0.0161 0.0016  0.0050  6   TYR B CD1 
2188 C  CD2 . TYR B  6   ? 0.1615 0.0964 0.1679 -0.0365 0.0122  0.0037  6   TYR B CD2 
2189 C  CE1 . TYR B  6   ? 0.1798 0.1021 0.1568 -0.0048 0.0172  0.0023  6   TYR B CE1 
2190 C  CE2 . TYR B  6   ? 0.1372 0.0947 0.1605 -0.0116 0.0001  0.0144  6   TYR B CE2 
2191 C  CZ  . TYR B  6   ? 0.1372 0.1129 0.1526 -0.0022 0.0026  0.0042  6   TYR B CZ  
2192 O  OH  . TYR B  6   ? 0.1494 0.1360 0.1565 0.0206  0.0126  -0.0019 6   TYR B OH  
2193 N  N   . PHE B  7   ? 0.1606 0.2015 0.2138 -0.0232 0.0168  0.0420  7   PHE B N   
2194 C  CA  . PHE B  7   ? 0.1588 0.2232 0.2791 -0.0440 0.0292  -0.0127 7   PHE B CA  
2195 C  C   . PHE B  7   ? 0.1887 0.3012 0.3397 -0.0320 0.0484  0.1013  7   PHE B C   
2196 O  O   . PHE B  7   ? 0.2528 0.2591 0.3738 -0.0454 0.0229  0.0527  7   PHE B O   
2197 C  CB  . PHE B  7   ? 0.2694 0.3172 0.2778 0.0305  0.0410  -0.0063 7   PHE B CB  
2198 C  CG  . PHE B  7   ? 0.2956 0.3551 0.2675 0.0134  0.0449  0.0449  7   PHE B CG  
2199 C  CD1 . PHE B  7   ? 0.3116 0.4173 0.3711 0.1301  0.0753  -0.0114 7   PHE B CD1 
2200 C  CD2 . PHE B  7   ? 0.3280 0.7490 0.3801 0.0520  0.0782  0.2263  7   PHE B CD2 
2201 C  CE1 . PHE B  7   ? 0.4084 0.5662 0.3338 0.0572  0.1533  -0.0182 7   PHE B CE1 
2202 C  CE2 . PHE B  7   ? 0.5941 0.8112 0.4565 0.1402  0.3071  0.2085  7   PHE B CE2 
2203 C  CZ  . PHE B  7   ? 0.4082 0.7440 0.6904 0.0628  0.2509  0.1887  7   PHE B CZ  
2204 N  N   . GLY B  8   ? 0.2023 0.3607 0.3095 -0.1034 0.0322  0.0495  8   GLY B N   
2205 C  CA  . GLY B  8   ? 0.2274 0.2850 0.2834 -0.0546 0.0343  0.0318  8   GLY B CA  
2206 C  C   . GLY B  8   ? 0.1984 0.2795 0.2378 -0.0397 0.0033  0.0561  8   GLY B C   
2207 O  O   . GLY B  8   ? 0.2026 0.3074 0.2283 -0.0663 -0.0102 0.0479  8   GLY B O   
2208 N  N   . PRO B  9   ? 0.2176 0.2535 0.2768 -0.0734 0.0139  0.0111  9   PRO B N   
2209 C  CA  . PRO B  9   ? 0.2931 0.2557 0.2652 -0.1044 0.0201  0.0276  9   PRO B CA  
2210 C  C   . PRO B  9   ? 0.2611 0.2271 0.2121 -0.0447 -0.0582 0.0339  9   PRO B C   
2211 O  O   . PRO B  9   ? 0.2460 0.2425 0.2274 -0.0735 -0.0461 0.0352  9   PRO B O   
2212 C  CB  . PRO B  9   ? 0.3067 0.3299 0.3276 -0.1839 -0.0094 0.1145  9   PRO B CB  
2213 C  CG  . PRO B  9   ? 0.4649 0.2482 0.3468 -0.0038 -0.0403 0.0620  9   PRO B CG  
2214 C  CD  . PRO B  9   ? 0.2877 0.3847 0.2731 -0.1309 0.0256  0.1297  9   PRO B CD  
2215 N  N   . ASP B  10  ? 0.2255 0.2157 0.2433 -0.0626 0.0003  0.0886  10  ASP B N   
2216 C  CA  . ASP B  10  ? 0.2382 0.1344 0.2205 -0.0271 -0.0245 0.0562  10  ASP B CA  
2217 C  C   . ASP B  10  ? 0.2103 0.1333 0.1976 -0.0521 -0.0236 0.0209  10  ASP B C   
2218 O  O   . ASP B  10  ? 0.1946 0.1583 0.2039 -0.0501 -0.0406 0.0397  10  ASP B O   
2219 C  CB  . ASP B  10  ? 0.2467 0.1602 0.2387 -0.0436 -0.0451 0.0598  10  ASP B CB  
2220 C  CG  . ASP B  10  ? 0.3455 0.1761 0.3328 -0.0743 -0.0706 0.0866  10  ASP B CG  
2221 O  OD1 . ASP B  10  ? 0.3905 0.1659 0.3673 -0.0819 -0.0749 0.0531  10  ASP B OD1 
2222 O  OD2 . ASP B  10  ? 0.5292 0.3072 0.3398 -0.1097 -0.1038 0.1526  10  ASP B OD2 
2223 N  N   . GLY B  11  ? 0.1811 0.1451 0.2314 -0.0604 -0.0337 0.0328  11  GLY B N   
2224 C  CA  . GLY B  11  ? 0.1757 0.1317 0.1811 -0.0523 -0.0040 0.0323  11  GLY B CA  
2225 C  C   . GLY B  11  ? 0.1273 0.1303 0.1708 -0.0095 -0.0216 0.0192  11  GLY B C   
2226 O  O   . GLY B  11  ? 0.1467 0.1194 0.1660 -0.0088 -0.0201 0.0268  11  GLY B O   
2227 N  N   . GLU B  12  ? 0.1193 0.1118 0.1728 -0.0037 -0.0094 0.0234  12  GLU B N   
2228 C  CA  . GLU B  12  ? 0.1155 0.0987 0.1597 -0.0150 -0.0174 0.0072  12  GLU B CA  
2229 C  C   . GLU B  12  ? 0.1179 0.0883 0.1573 0.0012  -0.0114 0.0173  12  GLU B C   
2230 O  O   . GLU B  12  ? 0.1293 0.1016 0.1580 -0.0176 -0.0077 0.0087  12  GLU B O   
2231 C  CB  . GLU B  12  ? 0.1114 0.0960 0.1864 -0.0059 -0.0142 0.0283  12  GLU B CB  
2232 C  CG  . GLU B  12  ? 0.1146 0.0992 0.1810 -0.0133 -0.0085 0.0111  12  GLU B CG  
2233 C  CD  . GLU B  12  ? 0.1104 0.1155 0.1533 -0.0054 -0.0055 0.0076  12  GLU B CD  
2234 O  OE1 . GLU B  12  ? 0.1170 0.1046 0.1662 -0.0075 -0.0070 0.0110  12  GLU B OE1 
2235 O  OE2 . GLU B  12  ? 0.1624 0.1201 0.1591 -0.0194 -0.0114 0.0165  12  GLU B OE2 
2236 N  N   . ASN B  13  ? 0.1124 0.0976 0.1721 -0.0119 -0.0062 0.0261  13  ASN B N   
2237 C  CA  . ASN B  13  ? 0.1170 0.0743 0.1967 -0.0035 -0.0128 -0.0035 13  ASN B CA  
2238 C  C   . ASN B  13  ? 0.1245 0.0996 0.1770 -0.0203 -0.0152 0.0172  13  ASN B C   
2239 O  O   . ASN B  13  ? 0.1540 0.0956 0.2037 -0.0220 -0.0372 0.0198  13  ASN B O   
2240 C  CB  . ASN B  13  ? 0.1240 0.0949 0.2026 0.0120  -0.0098 0.0419  13  ASN B CB  
2241 C  CG  . ASN B  13  ? 0.1181 0.1034 0.1727 -0.0097 -0.0141 0.0212  13  ASN B CG  
2242 O  OD1 . ASN B  13  ? 0.1190 0.1064 0.1947 -0.0102 -0.0040 0.0289  13  ASN B OD1 
2243 N  ND2 . ASN B  13  ? 0.1150 0.1183 0.1957 -0.0002 -0.0032 0.0198  13  ASN B ND2 
2244 N  N   . SER B  14  ? 0.1134 0.0878 0.1834 -0.0055 -0.0048 0.0234  14  SER B N   
2245 C  CA  . SER B  14  ? 0.1231 0.0838 0.2068 -0.0107 0.0064  0.0263  14  SER B CA  
2246 C  C   . SER B  14  ? 0.1237 0.0907 0.1630 -0.0072 -0.0091 0.0247  14  SER B C   
2247 O  O   . SER B  14  ? 0.1377 0.0926 0.1896 -0.0089 -0.0149 0.0208  14  SER B O   
2248 C  CB  . SER B  14  ? 0.1166 0.1368 0.2154 -0.0027 0.0145  0.0662  14  SER B CB  
2249 O  OG  . SER B  14  ? 0.1374 0.1345 0.2430 -0.0094 0.0322  0.0254  14  SER B OG  
2250 N  N   . TRP B  15  ? 0.1010 0.1058 0.1647 -0.0100 -0.0076 0.0163  15  TRP B N   
2251 C  CA  . TRP B  15  ? 0.1198 0.1057 0.1687 -0.0162 -0.0030 0.0114  15  TRP B CA  
2252 C  C   . TRP B  15  ? 0.1166 0.1068 0.1710 0.0001  -0.0021 0.0099  15  TRP B C   
2253 O  O   . TRP B  15  ? 0.1272 0.0992 0.1973 -0.0038 0.0055  0.0006  15  TRP B O   
2254 C  CB  . TRP B  15  ? 0.1175 0.1103 0.1567 -0.0245 -0.0124 0.0185  15  TRP B CB  
2255 C  CG  . TRP B  15  ? 0.1088 0.1028 0.1563 -0.0089 -0.0170 0.0041  15  TRP B CG  
2256 C  CD1 . TRP B  15  ? 0.1219 0.1266 0.1685 0.0124  -0.0328 0.0117  15  TRP B CD1 
2257 C  CD2 . TRP B  15  ? 0.1060 0.0851 0.1543 0.0099  -0.0036 0.0141  15  TRP B CD2 
2258 N  NE1 . TRP B  15  ? 0.1302 0.1027 0.1517 -0.0043 -0.0217 0.0248  15  TRP B NE1 
2259 C  CE2 . TRP B  15  ? 0.1082 0.1107 0.1570 0.0051  -0.0141 0.0159  15  TRP B CE2 
2260 C  CE3 . TRP B  15  ? 0.1069 0.1075 0.1641 0.0010  -0.0091 0.0163  15  TRP B CE3 
2261 C  CZ2 . TRP B  15  ? 0.1141 0.1098 0.1808 0.0000  -0.0280 0.0201  15  TRP B CZ2 
2262 C  CZ3 . TRP B  15  ? 0.1030 0.1134 0.1742 -0.0054 -0.0179 0.0192  15  TRP B CZ3 
2263 C  CH2 . TRP B  15  ? 0.1346 0.1023 0.1592 0.0055  -0.0258 0.0157  15  TRP B CH2 
2264 N  N   . SER B  16  ? 0.1363 0.0992 0.1667 -0.0201 -0.0171 -0.0055 16  SER B N   
2265 C  CA  . SER B  16  ? 0.1559 0.1157 0.1780 -0.0150 -0.0207 0.0139  16  SER B CA  
2266 C  C   . SER B  16  ? 0.1364 0.1159 0.1657 -0.0033 -0.0168 0.0118  16  SER B C   
2267 O  O   . SER B  16  ? 0.1685 0.1195 0.2057 -0.0125 -0.0135 -0.0003 16  SER B O   
2268 C  CB  . SER B  16  ? 0.1793 0.1051 0.2232 -0.0222 -0.0201 0.0367  16  SER B CB  
2269 O  OG  . SER B  16  ? 0.1953 0.1771 0.2746 -0.0055 -0.0295 0.0118  16  SER B OG  
2270 N  N   . LYS B  17  ? 0.1254 0.1007 0.1989 -0.0258 -0.0072 0.0149  17  LYS B N   
2271 C  CA  . LYS B  17  ? 0.1385 0.0907 0.2034 -0.0118 -0.0021 0.0109  17  LYS B CA  
2272 C  C   . LYS B  17  ? 0.1588 0.1033 0.2082 -0.0070 -0.0099 0.0106  17  LYS B C   
2273 O  O   . LYS B  17  ? 0.1735 0.1017 0.2506 -0.0064 0.0053  -0.0038 17  LYS B O   
2274 C  CB  . LYS B  17  ? 0.1467 0.1103 0.2250 -0.0057 0.0255  0.0047  17  LYS B CB  
2275 C  CG  . LYS B  17  ? 0.1333 0.1098 0.2358 -0.0111 -0.0020 0.0080  17  LYS B CG  
2276 C  CD  . LYS B  17  ? 0.1468 0.0994 0.2409 0.0059  0.0162  0.0243  17  LYS B CD  
2277 C  CE  . LYS B  17  ? 0.1389 0.1167 0.2189 -0.0082 -0.0114 0.0181  17  LYS B CE  
2278 N  NZ  . LYS B  17  ? 0.1521 0.1299 0.2287 -0.0099 0.0052  -0.0086 17  LYS B NZ  
2279 N  N   . LYS B  18  ? 0.1512 0.0971 0.2192 -0.0065 0.0055  -0.0120 18  LYS B N   
2280 C  CA  . LYS B  18  ? 0.1548 0.1295 0.2050 0.0150  0.0156  0.0179  18  LYS B CA  
2281 C  C   . LYS B  18  ? 0.1533 0.1087 0.2138 0.0051  0.0197  0.0244  18  LYS B C   
2282 O  O   . LYS B  18  ? 0.1895 0.1244 0.2754 0.0155  0.0392  0.0419  18  LYS B O   
2283 C  CB  . LYS B  18  ? 0.1860 0.1560 0.2206 -0.0209 -0.0002 0.0221  18  LYS B CB  
2284 C  CG  . LYS B  18  ? 0.2514 0.3720 0.2264 -0.1133 -0.0108 0.0745  18  LYS B CG  
2285 C  CD  . LYS B  18  ? 0.3538 0.4856 0.2142 -0.0665 -0.0226 0.0916  18  LYS B CD  
2286 C  CE  . LYS B  18  ? 0.4763 0.5684 0.2742 -0.2284 -0.0879 0.0504  18  LYS B CE  
2287 N  NZ  . LYS B  18  ? 0.4722 1.0527 0.3968 -0.3022 -0.2111 0.0485  18  LYS B NZ  
2288 N  N   . TYR B  19  ? 0.1555 0.0964 0.2139 -0.0177 0.0041  0.0185  19  TYR B N   
2289 C  CA  . TYR B  19  ? 0.1687 0.1195 0.1942 -0.0049 0.0010  0.0061  19  TYR B CA  
2290 C  C   . TYR B  19  ? 0.1418 0.1014 0.1857 -0.0093 0.0052  0.0100  19  TYR B C   
2291 O  O   . TYR B  19  ? 0.1565 0.1057 0.2071 0.0027  0.0000  0.0027  19  TYR B O   
2292 C  CB  . TYR B  19  ? 0.1486 0.1218 0.1990 -0.0231 -0.0130 0.0114  19  TYR B CB  
2293 C  CG  . TYR B  19  ? 0.1503 0.1035 0.1732 -0.0074 -0.0095 0.0055  19  TYR B CG  
2294 C  CD1 . TYR B  19  ? 0.1861 0.1387 0.2296 0.0230  -0.0148 0.0062  19  TYR B CD1 
2295 C  CD2 . TYR B  19  ? 0.1725 0.1254 0.1852 -0.0274 0.0005  0.0178  19  TYR B CD2 
2296 C  CE1 . TYR B  19  ? 0.2013 0.1640 0.2482 0.0188  -0.0377 0.0293  19  TYR B CE1 
2297 C  CE2 . TYR B  19  ? 0.2065 0.1360 0.2300 -0.0330 -0.0156 0.0234  19  TYR B CE2 
2298 C  CZ  . TYR B  19  ? 0.2414 0.1781 0.2256 0.0229  -0.0375 0.0450  19  TYR B CZ  
2299 O  OH  . TYR B  19  ? 0.3132 0.2355 0.2748 0.0420  -0.1014 0.0504  19  TYR B OH  
2300 N  N   . PRO B  20  ? 0.1845 0.1186 0.2004 -0.0286 -0.0243 -0.0060 20  PRO B N   
2301 C  CA  . PRO B  20  ? 0.1915 0.1161 0.2097 -0.0440 -0.0316 -0.0067 20  PRO B CA  
2302 C  C   . PRO B  20  ? 0.1757 0.1234 0.1761 -0.0156 -0.0161 -0.0039 20  PRO B C   
2303 O  O   . PRO B  20  ? 0.1681 0.1209 0.2123 -0.0116 -0.0186 -0.0081 20  PRO B O   
2304 C  CB  . PRO B  20  ? 0.2534 0.1269 0.2688 -0.0392 -0.0449 -0.0201 20  PRO B CB  
2305 C  CG  . PRO B  20  ? 0.3655 0.1866 0.2536 0.0308  -0.0340 -0.0453 20  PRO B CG  
2306 C  CD  . PRO B  20  ? 0.2575 0.0840 0.2561 -0.0161 -0.0201 -0.0022 20  PRO B CD  
2307 N  N   . SER B  21  ? 0.1780 0.0963 0.1879 -0.0177 -0.0041 -0.0126 21  SER B N   
2308 C  CA  . SER B  21  ? 0.1640 0.1078 0.1964 -0.0038 0.0025  -0.0066 21  SER B CA  
2309 C  C   . SER B  21  ? 0.1415 0.0920 0.1508 -0.0086 -0.0085 -0.0089 21  SER B C   
2310 O  O   . SER B  21  ? 0.1479 0.1358 0.1750 -0.0179 -0.0280 0.0222  21  SER B O   
2311 C  CB  . SER B  21  ? 0.1629 0.1459 0.1816 0.0047  -0.0015 -0.0143 21  SER B CB  
2312 O  OG  . SER B  21  ? 0.1918 0.1800 0.2326 0.0208  0.0023  -0.0454 21  SER B OG  
2313 N  N   . CYS B  22  ? 0.1340 0.1054 0.1511 -0.0102 -0.0022 0.0006  22  CYS B N   
2314 C  CA  . CYS B  22  ? 0.1417 0.1001 0.1691 0.0155  -0.0031 -0.0098 22  CYS B CA  
2315 C  C   . CYS B  22  ? 0.1359 0.1091 0.2045 -0.0074 -0.0137 -0.0149 22  CYS B C   
2316 O  O   . CYS B  22  ? 0.1513 0.1124 0.2132 -0.0020 -0.0168 -0.0094 22  CYS B O   
2317 C  CB  . CYS B  22  ? 0.1298 0.1188 0.1679 -0.0085 -0.0083 0.0016  22  CYS B CB  
2318 S  SG  . CYS B  22  ? 0.1520 0.1087 0.1788 -0.0004 -0.0061 0.0047  22  CYS B SG  
2319 N  N   . GLY B  23  ? 0.1392 0.1222 0.2026 -0.0016 -0.0344 0.0066  23  GLY B N   
2320 C  CA  . GLY B  23  ? 0.1541 0.1254 0.2289 -0.0024 -0.0383 -0.0072 23  GLY B CA  
2321 C  C   . GLY B  23  ? 0.1798 0.1158 0.2037 -0.0140 -0.0505 -0.0173 23  GLY B C   
2322 O  O   . GLY B  23  ? 0.2052 0.1779 0.2406 -0.0021 -0.0739 -0.0211 23  GLY B O   
2323 N  N   . GLY B  24  ? 0.1983 0.1596 0.1907 -0.0193 -0.0281 0.0116  24  GLY B N   
2324 C  CA  . GLY B  24  ? 0.2500 0.1905 0.1893 -0.0506 -0.0357 0.0143  24  GLY B CA  
2325 C  C   . GLY B  24  ? 0.2358 0.2149 0.1923 -0.0671 -0.0512 -0.0263 24  GLY B C   
2326 O  O   . GLY B  24  ? 0.3473 0.1776 0.2279 -0.0524 -0.0829 0.0094  24  GLY B O   
2327 N  N   . LEU B  25  ? 0.3423 0.2150 0.2139 -0.1292 -0.0753 0.0011  25  LEU B N   
2328 C  CA  . LEU B  25  ? 0.4411 0.2322 0.2320 -0.1703 -0.1021 0.0395  25  LEU B CA  
2329 C  C   . LEU B  25  ? 0.3495 0.1971 0.1939 -0.1129 -0.0714 -0.0049 25  LEU B C   
2330 O  O   . LEU B  25  ? 0.2889 0.1773 0.1813 -0.0486 -0.0259 -0.0286 25  LEU B O   
2331 C  CB  . LEU B  25  ? 0.4925 0.3023 0.2030 -0.1788 -0.0500 -0.0519 25  LEU B CB  
2332 C  CG  . LEU B  25  ? 0.3477 0.3728 0.2374 -0.0223 -0.0871 0.0037  25  LEU B CG  
2333 C  CD1 . LEU B  25  ? 0.5509 0.5090 0.3301 -0.0642 0.0872  -0.1590 25  LEU B CD1 
2334 C  CD2 . LEU B  25  ? 0.4993 0.4335 0.4093 0.0988  -0.1727 -0.0047 25  LEU B CD2 
2335 N  N   . LEU B  26  ? 0.3431 0.2014 0.2008 -0.1079 -0.0411 0.0132  26  LEU B N   
2336 C  CA  . LEU B  26  ? 0.2985 0.2615 0.1513 -0.0621 -0.0521 0.0088  26  LEU B CA  
2337 C  C   . LEU B  26  ? 0.2218 0.1482 0.1447 0.0036  -0.0248 0.0239  26  LEU B C   
2338 O  O   . LEU B  26  ? 0.2095 0.1608 0.1657 -0.0047 -0.0046 0.0156  26  LEU B O   
2339 C  CB  . LEU B  26  ? 0.3594 0.2283 0.1564 -0.0674 0.0205  -0.0183 26  LEU B CB  
2340 C  CG  . LEU B  26  ? 0.5478 0.3085 0.1938 0.0005  0.0301  0.0142  26  LEU B CG  
2341 C  CD1 . LEU B  26  ? 0.6987 0.5744 0.1958 0.0757  0.0946  0.0295  26  LEU B CD1 
2342 C  CD2 . LEU B  26  ? 0.5729 0.2999 0.1836 -0.0352 -0.0168 0.0531  26  LEU B CD2 
2343 N  N   . GLN B  27  ? 0.1706 0.1412 0.1720 -0.0308 -0.0258 0.0182  27  GLN B N   
2344 C  CA  . GLN B  27  ? 0.1360 0.1278 0.1430 -0.0135 -0.0296 0.0152  27  GLN B CA  
2345 C  C   . GLN B  27  ? 0.1443 0.1119 0.1355 -0.0060 -0.0135 0.0115  27  GLN B C   
2346 O  O   . GLN B  27  ? 0.1650 0.1303 0.1917 0.0001  -0.0403 0.0232  27  GLN B O   
2347 C  CB  . GLN B  27  ? 0.1269 0.1129 0.2122 -0.0132 -0.0174 0.0096  27  GLN B CB  
2348 C  CG  . GLN B  27  ? 0.1448 0.1127 0.2059 -0.0196 -0.0363 0.0006  27  GLN B CG  
2349 C  CD  . GLN B  27  ? 0.1446 0.1064 0.1492 -0.0100 -0.0205 -0.0081 27  GLN B CD  
2350 O  OE1 . GLN B  27  ? 0.1562 0.1068 0.1676 -0.0066 -0.0142 -0.0026 27  GLN B OE1 
2351 N  NE2 . GLN B  27  ? 0.1720 0.0971 0.1567 -0.0140 -0.0132 -0.0122 27  GLN B NE2 
2352 N  N   . SER B  28  ? 0.1238 0.1079 0.1411 -0.0098 -0.0058 0.0074  28  SER B N   
2353 C  CA  . SER B  28  ? 0.1085 0.1005 0.1414 -0.0050 -0.0165 -0.0026 28  SER B CA  
2354 C  C   . SER B  28  ? 0.1046 0.1037 0.1421 -0.0055 -0.0074 0.0190  28  SER B C   
2355 O  O   . SER B  28  ? 0.1130 0.0987 0.1749 -0.0034 -0.0050 0.0203  28  SER B O   
2356 C  CB  . SER B  28  ? 0.1017 0.1274 0.1418 0.0006  -0.0053 -0.0049 28  SER B CB  
2357 O  OG  . SER B  28  ? 0.1280 0.1154 0.1426 0.0062  -0.0024 0.0077  28  SER B OG  
2358 N  N   . PRO B  29  ? 0.0989 0.0933 0.1382 -0.0019 -0.0063 0.0125  29  PRO B N   
2359 C  CA  . PRO B  29  ? 0.1034 0.0903 0.1439 -0.0136 -0.0150 0.0239  29  PRO B CA  
2360 C  C   . PRO B  29  ? 0.1014 0.0919 0.1479 -0.0072 -0.0082 0.0073  29  PRO B C   
2361 O  O   . PRO B  29  ? 0.0998 0.1070 0.1560 -0.0099 -0.0146 0.0210  29  PRO B O   
2362 C  CB  . PRO B  29  ? 0.1115 0.1091 0.1277 -0.0107 0.0020  0.0119  29  PRO B CB  
2363 C  CG  . PRO B  29  ? 0.1118 0.1061 0.1478 0.0010  0.0024  0.0102  29  PRO B CG  
2364 C  CD  . PRO B  29  ? 0.1058 0.1001 0.1537 -0.0058 -0.0006 0.0147  29  PRO B CD  
2365 N  N   . ILE B  30  ? 0.1073 0.1070 0.1450 0.0009  0.0034  0.0245  30  ILE B N   
2366 C  CA  . ILE B  30  ? 0.1076 0.1008 0.1386 0.0067  -0.0095 0.0164  30  ILE B CA  
2367 C  C   . ILE B  30  ? 0.1025 0.1201 0.1463 -0.0047 0.0052  0.0185  30  ILE B C   
2368 O  O   . ILE B  30  ? 0.1091 0.1176 0.1538 -0.0019 -0.0091 0.0252  30  ILE B O   
2369 C  CB  . ILE B  30  ? 0.1328 0.1165 0.1559 -0.0150 -0.0120 0.0134  30  ILE B CB  
2370 C  CG1 . ILE B  30  ? 0.1315 0.1769 0.1568 0.0300  -0.0031 0.0089  30  ILE B CG1 
2371 C  CG2 . ILE B  30  ? 0.2200 0.1297 0.1468 0.0117  -0.0057 0.0176  30  ILE B CG2 
2372 C  CD1 . ILE B  30  ? 0.1758 0.2078 0.1808 0.0234  0.0142  0.0419  30  ILE B CD1 
2373 N  N   . ASP B  31  ? 0.1037 0.1168 0.1498 0.0055  -0.0011 0.0225  31  ASP B N   
2374 C  CA  . ASP B  31  ? 0.1114 0.1140 0.1630 0.0060  0.0008  0.0316  31  ASP B CA  
2375 C  C   . ASP B  31  ? 0.1375 0.1128 0.1557 -0.0091 -0.0251 0.0291  31  ASP B C   
2376 O  O   . ASP B  31  ? 0.1735 0.1626 0.1777 -0.0395 -0.0171 0.0425  31  ASP B O   
2377 C  CB  . ASP B  31  ? 0.1244 0.1329 0.1827 0.0362  0.0152  0.0266  31  ASP B CB  
2378 C  CG  . ASP B  31  ? 0.1450 0.1719 0.1666 0.0414  -0.0150 0.0022  31  ASP B CG  
2379 O  OD1 . ASP B  31  ? 0.1595 0.1345 0.2069 0.0293  -0.0267 0.0104  31  ASP B OD1 
2380 O  OD2 . ASP B  31  ? 0.2377 0.1769 0.2074 0.0543  -0.0276 0.0146  31  ASP B OD2 
2381 N  N   . LEU B  32  ? 0.1301 0.1161 0.1736 -0.0135 -0.0037 0.0368  32  LEU B N   
2382 C  CA  . LEU B  32  ? 0.1323 0.1655 0.1786 -0.0120 0.0004  0.0640  32  LEU B CA  
2383 C  C   . LEU B  32  ? 0.1655 0.1497 0.1710 -0.0141 -0.0092 0.0145  32  LEU B C   
2384 O  O   . LEU B  32  ? 0.2046 0.1611 0.1951 0.0055  -0.0317 0.0396  32  LEU B O   
2385 C  CB  . LEU B  32  ? 0.1364 0.1800 0.2000 -0.0033 -0.0102 0.0440  32  LEU B CB  
2386 C  CG  . LEU B  32  ? 0.1159 0.1789 0.1826 -0.0038 0.0035  0.0341  32  LEU B CG  
2387 C  CD1 . LEU B  32  ? 0.1112 0.2301 0.2222 -0.0069 0.0006  0.0558  32  LEU B CD1 
2388 C  CD2 . LEU B  32  ? 0.1882 0.2331 0.2297 -0.0099 -0.0122 0.0057  32  LEU B CD2 
2389 N  N   . HIS B  33  ? 0.1636 0.1535 0.1895 -0.0369 -0.0158 0.0491  33  HIS B N   
2390 C  CA  . HIS B  33  ? 0.1502 0.1805 0.1907 0.0111  0.0034  0.0467  33  HIS B CA  
2391 C  C   . HIS B  33  ? 0.1597 0.1684 0.1925 -0.0157 -0.0233 0.0290  33  HIS B C   
2392 O  O   . HIS B  33  ? 0.1463 0.1844 0.1885 -0.0125 -0.0118 0.0543  33  HIS B O   
2393 C  CB  . HIS B  33  ? 0.1813 0.2102 0.1935 -0.0161 0.0027  0.0592  33  HIS B CB  
2394 C  CG  . HIS B  33  ? 0.1588 0.2391 0.2191 -0.0547 -0.0259 0.0990  33  HIS B CG  
2395 N  ND1 . HIS B  33  ? 0.2652 0.2459 0.2329 -0.1165 -0.0682 0.0994  33  HIS B ND1 
2396 C  CD2 . HIS B  33  ? 0.1767 0.2518 0.1626 0.0096  -0.0152 0.0664  33  HIS B CD2 
2397 C  CE1 . HIS B  33  ? 0.2912 0.2775 0.2620 -0.0841 -0.0968 0.0732  33  HIS B CE1 
2398 N  NE2 . HIS B  33  ? 0.1892 0.2847 0.2427 -0.0223 -0.0266 0.0502  33  HIS B NE2 
2399 N  N   . SER B  34  ? 0.1646 0.1733 0.2269 -0.0030 -0.0275 0.0568  34  SER B N   
2400 C  CA  . SER B  34  ? 0.1928 0.2199 0.2179 -0.0074 -0.0179 0.0628  34  SER B CA  
2401 C  C   . SER B  34  ? 0.1725 0.1814 0.1869 -0.0094 0.0044  0.0792  34  SER B C   
2402 O  O   . SER B  34  ? 0.1750 0.2215 0.1974 -0.0026 0.0013  0.0751  34  SER B O   
2403 C  CB  . SER B  34  ? 0.2485 0.2299 0.3358 0.0405  0.0059  0.1469  34  SER B CB  
2404 O  OG  . SER B  34  ? 0.2766 0.2559 0.3166 0.0308  -0.0119 0.0731  34  SER B OG  
2405 N  N   . ASP B  35  ? 0.1533 0.2490 0.1769 -0.0249 -0.0223 0.0751  35  ASP B N   
2406 C  CA  . ASP B  35  ? 0.1522 0.2360 0.1858 -0.0063 -0.0071 0.0681  35  ASP B CA  
2407 C  C   . ASP B  35  ? 0.1834 0.2309 0.1760 0.0047  -0.0297 0.0218  35  ASP B C   
2408 O  O   . ASP B  35  ? 0.1989 0.3531 0.1754 0.0149  -0.0252 0.0355  35  ASP B O   
2409 C  CB  . ASP B  35  ? 0.1392 0.3152 0.2223 -0.0286 -0.0001 0.0298  35  ASP B CB  
2410 C  CG  . ASP B  35  ? 0.1943 0.2353 0.2019 -0.0151 -0.0240 0.0410  35  ASP B CG  
2411 O  OD1 . ASP B  35  ? 0.1718 0.2821 0.2471 -0.0073 -0.0160 0.0249  35  ASP B OD1 
2412 O  OD2 . ASP B  35  ? 0.1755 0.3328 0.2405 -0.0047 -0.0053 0.0985  35  ASP B OD2 
2413 N  N   . ILE B  36  ? 0.1324 0.2064 0.1997 0.0033  -0.0185 0.0565  36  ILE B N   
2414 C  CA  . ILE B  36  ? 0.1545 0.2116 0.1971 -0.0272 -0.0220 0.0370  36  ILE B CA  
2415 C  C   . ILE B  36  ? 0.1721 0.1958 0.1717 -0.0220 -0.0346 0.0238  36  ILE B C   
2416 O  O   . ILE B  36  ? 0.1788 0.2284 0.2155 0.0164  -0.0295 0.0447  36  ILE B O   
2417 C  CB  . ILE B  36  ? 0.1785 0.2516 0.2013 -0.0475 -0.0117 0.0552  36  ILE B CB  
2418 C  CG1 . ILE B  36  ? 0.2754 0.2297 0.2271 -0.0097 -0.0025 0.0660  36  ILE B CG1 
2419 C  CG2 . ILE B  36  ? 0.1732 0.3245 0.3069 -0.0451 -0.0097 -0.0285 36  ILE B CG2 
2420 C  CD1 . ILE B  36  ? 0.2218 0.2443 0.3014 -0.0053 -0.0242 0.0675  36  ILE B CD1 
2421 N  N   . LEU B  37  ? 0.1284 0.1942 0.1750 -0.0053 -0.0226 0.0408  37  LEU B N   
2422 C  CA  . LEU B  37  ? 0.1470 0.1798 0.1874 0.0149  0.0098  0.0457  37  LEU B CA  
2423 C  C   . LEU B  37  ? 0.1854 0.1989 0.1741 0.0188  -0.0104 0.0819  37  LEU B C   
2424 O  O   . LEU B  37  ? 0.1762 0.3181 0.2283 0.0425  0.0038  0.1363  37  LEU B O   
2425 C  CB  . LEU B  37  ? 0.1562 0.1648 0.2161 0.0048  -0.0183 0.0508  37  LEU B CB  
2426 C  CG  . LEU B  37  ? 0.1482 0.2279 0.2354 0.0175  -0.0100 0.0370  37  LEU B CG  
2427 C  CD1 . LEU B  37  ? 0.2410 0.2435 0.2680 0.0312  -0.0851 0.0113  37  LEU B CD1 
2428 C  CD2 . LEU B  37  ? 0.2010 0.2515 0.1945 -0.0032 -0.0100 0.0646  37  LEU B CD2 
2429 N  N   . GLN B  38  ? 0.1574 0.2058 0.1799 0.0105  0.0019  0.0585  38  GLN B N   
2430 C  CA  . GLN B  38  ? 0.1680 0.2670 0.1476 -0.0015 -0.0195 0.0454  38  GLN B CA  
2431 C  C   . GLN B  38  ? 0.1605 0.2106 0.1416 -0.0005 -0.0152 0.0578  38  GLN B C   
2432 O  O   . GLN B  38  ? 0.1663 0.1948 0.1446 0.0071  -0.0207 0.0571  38  GLN B O   
2433 C  CB  . GLN B  38  ? 0.1929 0.3637 0.1734 -0.0026 -0.0302 0.0103  38  GLN B CB  
2434 C  CG  . GLN B  38  ? 0.2674 0.4739 0.1854 0.0091  0.0266  -0.0403 38  GLN B CG  
2435 C  CD  . GLN B  38  ? 0.3534 0.5582 0.1527 -0.0425 -0.0315 0.0079  38  GLN B CD  
2436 O  OE1 . GLN B  38  ? 0.5486 0.8685 0.3306 -0.2167 -0.0279 0.0032  38  GLN B OE1 
2437 N  NE2 . GLN B  38  ? 0.4029 0.7579 0.5396 -0.0597 0.0864  -0.0580 38  GLN B NE2 
2438 N  N   . TYR B  39  ? 0.1618 0.1770 0.1544 0.0155  -0.0030 0.0553  39  TYR B N   
2439 C  CA  . TYR B  39  ? 0.1569 0.1635 0.1612 0.0190  0.0078  0.0421  39  TYR B CA  
2440 C  C   . TYR B  39  ? 0.1698 0.2116 0.1236 0.0215  -0.0085 0.0374  39  TYR B C   
2441 O  O   . TYR B  39  ? 0.1907 0.2312 0.1404 0.0384  -0.0158 0.0369  39  TYR B O   
2442 C  CB  . TYR B  39  ? 0.1816 0.1824 0.2140 0.0320  0.0168  0.0644  39  TYR B CB  
2443 C  CG  . TYR B  39  ? 0.2058 0.1587 0.1755 0.0215  0.0344  0.0597  39  TYR B CG  
2444 C  CD1 . TYR B  39  ? 0.2100 0.1890 0.1752 0.0016  0.0136  0.0260  39  TYR B CD1 
2445 C  CD2 . TYR B  39  ? 0.2680 0.1979 0.1796 -0.0241 0.0412  0.0641  39  TYR B CD2 
2446 C  CE1 . TYR B  39  ? 0.2437 0.1888 0.1565 -0.0055 0.0348  0.0323  39  TYR B CE1 
2447 C  CE2 . TYR B  39  ? 0.2511 0.2857 0.1826 -0.0221 0.0208  0.0750  39  TYR B CE2 
2448 C  CZ  . TYR B  39  ? 0.2151 0.2327 0.2036 -0.0029 0.0227  0.0812  39  TYR B CZ  
2449 O  OH  . TYR B  39  ? 0.2309 0.2931 0.2331 -0.0340 0.0265  0.0607  39  TYR B OH  
2450 N  N   . ASP B  40  ? 0.1558 0.1981 0.1231 0.0209  0.0089  0.0225  40  ASP B N   
2451 C  CA  . ASP B  40  ? 0.1684 0.1929 0.1568 0.0334  0.0138  0.0245  40  ASP B CA  
2452 C  C   . ASP B  40  ? 0.1759 0.1970 0.1228 0.0044  -0.0068 0.0287  40  ASP B C   
2453 O  O   . ASP B  40  ? 0.1735 0.2273 0.1297 0.0179  0.0053  0.0170  40  ASP B O   
2454 C  CB  . ASP B  40  ? 0.1961 0.1884 0.1711 0.0289  0.0012  0.0135  40  ASP B CB  
2455 C  CG  . ASP B  40  ? 0.2468 0.2414 0.1850 0.0004  0.0074  -0.0244 40  ASP B CG  
2456 O  OD1 . ASP B  40  ? 0.2507 0.2709 0.1898 0.0288  0.0186  -0.0245 40  ASP B OD1 
2457 O  OD2 . ASP B  40  ? 0.3049 0.2494 0.3653 0.0050  0.0619  0.0032  40  ASP B OD2 
2458 N  N   . ALA B  41  ? 0.1776 0.2355 0.1448 -0.0046 0.0145  0.0489  41  ALA B N   
2459 C  CA  . ALA B  41  ? 0.2243 0.2312 0.1697 -0.0110 0.0502  0.0358  41  ALA B CA  
2460 C  C   . ALA B  41  ? 0.1913 0.2579 0.1918 0.0070  0.0625  0.0242  41  ALA B C   
2461 O  O   . ALA B  41  ? 0.2369 0.2632 0.2136 0.0002  0.0453  0.0233  41  ALA B O   
2462 C  CB  . ALA B  41  ? 0.2948 0.2628 0.1872 -0.0179 0.0646  0.0499  41  ALA B CB  
2463 N  N   A SER B  42  ? 0.1689 0.2288 0.1386 0.0351  0.0147  0.0237  42  SER B N   
2464 N  N   B SER B  42  ? 0.2207 0.2578 0.1471 0.0358  0.0146  0.0058  42  SER B N   
2465 C  CA  A SER B  42  ? 0.1660 0.1989 0.1511 0.0145  0.0137  -0.0053 42  SER B CA  
2466 C  CA  B SER B  42  ? 0.2191 0.2780 0.2095 0.0428  0.0283  -0.0192 42  SER B CA  
2467 C  C   A SER B  42  ? 0.1796 0.1939 0.1465 -0.0075 0.0048  -0.0077 42  SER B C   
2468 C  C   B SER B  42  ? 0.2096 0.2094 0.1951 0.0725  -0.0078 -0.0688 42  SER B C   
2469 O  O   A SER B  42  ? 0.1897 0.1721 0.1580 -0.0131 0.0432  -0.0256 42  SER B O   
2470 O  O   B SER B  42  ? 0.1990 0.2248 0.2895 0.0361  -0.0251 -0.0103 42  SER B O   
2471 C  CB  A SER B  42  ? 0.2597 0.2206 0.1911 -0.0030 0.0164  -0.0324 42  SER B CB  
2472 C  CB  B SER B  42  ? 0.5105 0.4440 0.2108 -0.0114 -0.0455 -0.1176 42  SER B CB  
2473 O  OG  A SER B  42  ? 0.2346 0.2032 0.2320 -0.0198 -0.0106 -0.0628 42  SER B OG  
2474 O  OG  B SER B  42  ? 0.3277 0.3934 0.2600 0.0740  0.0520  -0.0473 42  SER B OG  
2475 N  N   . LEU B  43  ? 0.1758 0.2077 0.1448 0.0242  0.0037  0.0057  43  LEU B N   
2476 C  CA  . LEU B  43  ? 0.2051 0.2108 0.1452 -0.0011 -0.0059 0.0424  43  LEU B CA  
2477 C  C   . LEU B  43  ? 0.1758 0.2027 0.1720 0.0186  0.0033  0.0392  43  LEU B C   
2478 O  O   . LEU B  43  ? 0.1849 0.2190 0.1971 0.0121  -0.0047 0.0336  43  LEU B O   
2479 C  CB  . LEU B  43  ? 0.1869 0.1687 0.1475 0.0046  0.0094  0.0130  43  LEU B CB  
2480 C  CG  . LEU B  43  ? 0.1818 0.1496 0.1660 0.0114  -0.0128 0.0200  43  LEU B CG  
2481 C  CD1 . LEU B  43  ? 0.1822 0.2361 0.1730 0.0348  0.0049  0.0281  43  LEU B CD1 
2482 C  CD2 . LEU B  43  ? 0.2299 0.1723 0.1734 0.0298  0.0052  0.0190  43  LEU B CD2 
2483 N  N   . THR B  44  ? 0.1725 0.2159 0.1839 0.0107  0.0455  0.0520  44  THR B N   
2484 C  CA  . THR B  44  ? 0.1969 0.2559 0.1819 -0.0106 0.0291  0.0608  44  THR B CA  
2485 C  C   . THR B  44  ? 0.1435 0.2069 0.2023 -0.0033 0.0256  0.0531  44  THR B C   
2486 O  O   . THR B  44  ? 0.1327 0.2112 0.1932 0.0051  0.0200  0.0528  44  THR B O   
2487 C  CB  . THR B  44  ? 0.2438 0.3190 0.1852 -0.0176 0.0807  0.0509  44  THR B CB  
2488 O  OG1 . THR B  44  ? 0.2031 0.4020 0.2815 0.0753  0.0761  0.0344  44  THR B OG1 
2489 C  CG2 . THR B  44  ? 0.2367 0.4128 0.1642 -0.0222 0.0727  0.0476  44  THR B CG2 
2490 N  N   . PRO B  45  ? 0.1697 0.2169 0.1778 0.0119  0.0086  0.0703  45  PRO B N   
2491 C  CA  . PRO B  45  ? 0.1426 0.2308 0.2081 -0.0085 -0.0121 0.0607  45  PRO B CA  
2492 C  C   . PRO B  45  ? 0.1240 0.2403 0.1775 0.0228  -0.0018 0.0434  45  PRO B C   
2493 O  O   . PRO B  45  ? 0.1599 0.3009 0.2256 0.0512  0.0319  0.0904  45  PRO B O   
2494 C  CB  . PRO B  45  ? 0.2515 0.2181 0.2381 -0.0621 -0.0155 0.0602  45  PRO B CB  
2495 C  CG  . PRO B  45  ? 0.1999 0.2055 0.2892 -0.0381 -0.0166 0.0695  45  PRO B CG  
2496 C  CD  . PRO B  45  ? 0.2003 0.3097 0.2202 -0.0828 0.0177  0.0776  45  PRO B CD  
2497 N  N   . LEU B  46  ? 0.1513 0.2110 0.1466 0.0105  -0.0105 0.0344  46  LEU B N   
2498 C  CA  . LEU B  46  ? 0.1291 0.1991 0.1773 0.0239  0.0015  0.0440  46  LEU B CA  
2499 C  C   . LEU B  46  ? 0.1452 0.1781 0.1643 0.0153  0.0002  0.0331  46  LEU B C   
2500 O  O   . LEU B  46  ? 0.1429 0.1897 0.2208 0.0068  -0.0030 0.0431  46  LEU B O   
2501 C  CB  . LEU B  46  ? 0.1397 0.2268 0.1949 -0.0050 0.0022  0.0261  46  LEU B CB  
2502 C  CG  . LEU B  46  ? 0.1535 0.2667 0.2270 -0.0267 0.0121  0.0105  46  LEU B CG  
2503 C  CD1 . LEU B  46  ? 0.1826 0.2483 0.2669 -0.0093 0.0375  0.0669  46  LEU B CD1 
2504 C  CD2 . LEU B  46  ? 0.1872 0.3409 0.2634 0.0179  -0.0324 -0.0421 46  LEU B CD2 
2505 N  N   . GLU B  47  ? 0.1434 0.1928 0.1791 0.0046  -0.0099 0.0485  47  GLU B N   
2506 C  CA  . GLU B  47  ? 0.1529 0.2435 0.1638 -0.0284 -0.0214 0.0632  47  GLU B CA  
2507 C  C   . GLU B  47  ? 0.1737 0.1768 0.1568 0.0058  -0.0013 0.0201  47  GLU B C   
2508 O  O   . GLU B  47  ? 0.2216 0.1918 0.1843 0.0116  0.0025  0.0236  47  GLU B O   
2509 C  CB  . GLU B  47  ? 0.1380 0.2803 0.2578 -0.0208 0.0059  0.0946  47  GLU B CB  
2510 C  CG  . GLU B  47  ? 0.2081 0.3696 0.3100 -0.0233 0.0414  0.1811  47  GLU B CG  
2511 C  CD  . GLU B  47  ? 0.3276 0.4691 0.3436 -0.0165 0.0625  0.2088  47  GLU B CD  
2512 O  OE1 . GLU B  47  ? 0.5324 0.8965 0.5053 -0.3488 0.2117  -0.0547 47  GLU B OE1 
2513 O  OE2 . GLU B  47  ? 0.2672 0.7693 0.4951 0.0454  0.0819  0.1160  47  GLU B OE2 
2514 N  N   . PHE B  48  ? 0.1301 0.1924 0.1656 0.0077  -0.0132 0.0331  48  PHE B N   
2515 C  CA  . PHE B  48  ? 0.1489 0.1734 0.1683 0.0403  0.0102  0.0505  48  PHE B CA  
2516 C  C   . PHE B  48  ? 0.1475 0.1715 0.1819 -0.0015 -0.0238 0.0321  48  PHE B C   
2517 O  O   . PHE B  48  ? 0.1869 0.2155 0.2345 0.0214  -0.0392 0.0040  48  PHE B O   
2518 C  CB  . PHE B  48  ? 0.1859 0.1738 0.2049 0.0330  0.0145  0.0410  48  PHE B CB  
2519 C  CG  . PHE B  48  ? 0.1779 0.1720 0.1636 0.0370  0.0106  0.0166  48  PHE B CG  
2520 C  CD1 . PHE B  48  ? 0.1628 0.2484 0.1879 -0.0019 0.0268  0.0557  48  PHE B CD1 
2521 C  CD2 . PHE B  48  ? 0.1833 0.1802 0.2011 0.0390  0.0135  0.0261  48  PHE B CD2 
2522 C  CE1 . PHE B  48  ? 0.1504 0.2306 0.1834 0.0041  0.0375  0.0434  48  PHE B CE1 
2523 C  CE2 . PHE B  48  ? 0.1884 0.1976 0.2000 0.0314  0.0181  0.0341  48  PHE B CE2 
2524 C  CZ  . PHE B  48  ? 0.1557 0.2239 0.1893 0.0071  0.0225  0.0666  48  PHE B CZ  
2525 N  N   . GLN B  49  ? 0.1315 0.1877 0.1807 0.0268  0.0167  0.0386  49  GLN B N   
2526 C  CA  . GLN B  49  ? 0.1392 0.2020 0.1900 0.0333  0.0198  0.0377  49  GLN B CA  
2527 C  C   . GLN B  49  ? 0.1331 0.1965 0.1603 0.0152  0.0091  0.0162  49  GLN B C   
2528 O  O   . GLN B  49  ? 0.1195 0.1938 0.1839 0.0121  -0.0015 0.0398  49  GLN B O   
2529 C  CB  . GLN B  49  ? 0.1937 0.2569 0.1780 0.0368  0.0392  0.0389  49  GLN B CB  
2530 C  CG  . GLN B  49  ? 0.2172 0.2861 0.2179 0.0234  0.0337  0.0672  49  GLN B CG  
2531 C  CD  . GLN B  49  ? 0.1884 0.3414 0.2646 -0.0217 0.0097  0.0826  49  GLN B CD  
2532 O  OE1 . GLN B  49  ? 0.3396 0.3427 0.5092 -0.0286 -0.1154 0.1500  49  GLN B OE1 
2533 N  NE2 . GLN B  49  ? 0.1733 0.4247 0.4270 -0.0130 -0.0048 0.0954  49  GLN B NE2 
2534 N  N   . GLY B  50  ? 0.1142 0.2315 0.1945 -0.0078 0.0144  0.0403  50  GLY B N   
2535 C  CA  . GLY B  50  ? 0.1331 0.2027 0.2034 0.0243  0.0324  0.0477  50  GLY B CA  
2536 C  C   . GLY B  50  ? 0.1005 0.2083 0.1714 0.0052  0.0030  0.0493  50  GLY B C   
2537 O  O   . GLY B  50  ? 0.1150 0.2056 0.2261 0.0179  0.0075  0.0589  50  GLY B O   
2538 N  N   . TYR B  51  ? 0.0958 0.1962 0.1685 0.0151  -0.0035 0.0317  51  TYR B N   
2539 C  CA  . TYR B  51  ? 0.1095 0.1999 0.1512 0.0151  0.0015  0.0488  51  TYR B CA  
2540 C  C   . TYR B  51  ? 0.1145 0.1759 0.1513 0.0029  -0.0044 0.0431  51  TYR B C   
2541 O  O   . TYR B  51  ? 0.1104 0.1585 0.1651 -0.0110 -0.0103 0.0311  51  TYR B O   
2542 C  CB  . TYR B  51  ? 0.1069 0.1500 0.1776 -0.0044 -0.0168 0.0403  51  TYR B CB  
2543 C  CG  . TYR B  51  ? 0.1148 0.1500 0.1359 -0.0062 0.0011  0.0321  51  TYR B CG  
2544 C  CD1 . TYR B  51  ? 0.1102 0.1682 0.1603 -0.0069 -0.0049 0.0183  51  TYR B CD1 
2545 C  CD2 . TYR B  51  ? 0.0966 0.1577 0.1490 -0.0130 -0.0030 0.0359  51  TYR B CD2 
2546 C  CE1 . TYR B  51  ? 0.1426 0.1518 0.1373 0.0239  0.0078  0.0177  51  TYR B CE1 
2547 C  CE2 . TYR B  51  ? 0.1207 0.1527 0.1389 0.0013  -0.0006 0.0042  51  TYR B CE2 
2548 C  CZ  . TYR B  51  ? 0.1150 0.1620 0.1599 -0.0022 -0.0181 -0.0011 51  TYR B CZ  
2549 O  OH  . TYR B  51  ? 0.1361 0.1636 0.2058 0.0178  -0.0405 0.0011  51  TYR B OH  
2550 N  N   . ASN B  52  ? 0.1284 0.1755 0.1795 -0.0220 -0.0055 0.0355  52  ASN B N   
2551 C  CA  . ASN B  52  ? 0.1203 0.1730 0.1857 -0.0295 -0.0259 0.0452  52  ASN B CA  
2552 C  C   . ASN B  52  ? 0.1286 0.1863 0.1949 -0.0081 0.0087  0.0447  52  ASN B C   
2553 O  O   . ASN B  52  ? 0.1194 0.2718 0.2556 0.0062  -0.0072 0.0993  52  ASN B O   
2554 C  CB  . ASN B  52  ? 0.1394 0.1987 0.2412 -0.0500 -0.0418 0.0578  52  ASN B CB  
2555 C  CG  . ASN B  52  ? 0.1767 0.2857 0.2648 -0.0746 -0.0763 0.0650  52  ASN B CG  
2556 O  OD1 . ASN B  52  ? 0.4366 0.4037 0.2683 -0.2505 -0.0826 0.0648  52  ASN B OD1 
2557 N  ND2 . ASN B  52  ? 0.2005 0.2884 0.4981 -0.0882 -0.0231 -0.0048 52  ASN B ND2 
2558 N  N   . LEU B  53  ? 0.1333 0.1901 0.1414 -0.0099 -0.0173 0.0333  53  LEU B N   
2559 C  CA  . LEU B  53  ? 0.1365 0.1881 0.1603 -0.0143 -0.0217 0.0354  53  LEU B CA  
2560 C  C   . LEU B  53  ? 0.1292 0.1503 0.1690 0.0009  -0.0267 0.0138  53  LEU B C   
2561 O  O   . LEU B  53  ? 0.1507 0.1999 0.1927 0.0080  -0.0261 0.0044  53  LEU B O   
2562 C  CB  . LEU B  53  ? 0.1230 0.1621 0.1863 -0.0057 -0.0364 0.0331  53  LEU B CB  
2563 C  CG  . LEU B  53  ? 0.1555 0.1709 0.2034 -0.0114 -0.0365 0.0518  53  LEU B CG  
2564 C  CD1 . LEU B  53  ? 0.1993 0.1927 0.2392 -0.0381 -0.0643 0.0901  53  LEU B CD1 
2565 C  CD2 . LEU B  53  ? 0.2569 0.2736 0.1757 -0.0203 -0.0694 0.0171  53  LEU B CD2 
2566 N  N   . SER B  54  ? 0.1363 0.1879 0.1500 0.0116  -0.0113 0.0366  54  SER B N   
2567 C  CA  . SER B  54  ? 0.1344 0.2566 0.1721 0.0234  -0.0326 0.0273  54  SER B CA  
2568 C  C   . SER B  54  ? 0.1423 0.1786 0.1770 0.0077  -0.0004 0.0275  54  SER B C   
2569 O  O   . SER B  54  ? 0.1368 0.1970 0.1691 0.0104  -0.0263 0.0254  54  SER B O   
2570 C  CB  . SER B  54  ? 0.1430 0.2757 0.1597 0.0331  -0.0232 0.0440  54  SER B CB  
2571 O  OG  . SER B  54  ? 0.1445 0.2868 0.1939 -0.0124 -0.0111 0.0430  54  SER B OG  
2572 N  N   . ALA B  55  ? 0.1571 0.2100 0.1948 -0.0114 -0.0161 0.0249  55  ALA B N   
2573 C  CA  . ALA B  55  ? 0.1740 0.2020 0.2112 0.0117  -0.0164 0.0005  55  ALA B CA  
2574 C  C   . ALA B  55  ? 0.1655 0.2194 0.1739 -0.0074 -0.0118 0.0195  55  ALA B C   
2575 O  O   . ALA B  55  ? 0.1994 0.2732 0.1764 0.0116  0.0094  0.0021  55  ALA B O   
2576 C  CB  . ALA B  55  ? 0.2763 0.1879 0.3195 0.0304  -0.0836 -0.0100 55  ALA B CB  
2577 N  N   . ASN B  56  ? 0.1426 0.2334 0.1623 -0.0066 -0.0496 0.0130  56  ASN B N   
2578 C  CA  . ASN B  56  ? 0.1347 0.2581 0.1861 -0.0174 -0.0215 0.0272  56  ASN B CA  
2579 C  C   . ASN B  56  ? 0.1790 0.2118 0.1715 0.0177  -0.0164 0.0291  56  ASN B C   
2580 O  O   . ASN B  56  ? 0.2328 0.2120 0.2523 0.0124  -0.0652 0.0423  56  ASN B O   
2581 C  CB  . ASN B  56  ? 0.1186 0.3046 0.1951 0.0005  -0.0241 0.0040  56  ASN B CB  
2582 C  CG  . ASN B  56  ? 0.1547 0.3080 0.2725 -0.0036 -0.0229 -0.0340 56  ASN B CG  
2583 O  OD1 . ASN B  56  ? 0.2286 0.2926 0.2591 0.0122  -0.0318 -0.0486 56  ASN B OD1 
2584 N  ND2 . ASN B  56  ? 0.2615 0.4717 0.4693 -0.1456 0.0958  -0.1278 56  ASN B ND2 
2585 N  N   . LYS B  57  ? 0.1369 0.2146 0.1692 -0.0006 -0.0043 0.0051  57  LYS B N   
2586 C  CA  . LYS B  57  ? 0.1455 0.1927 0.1743 0.0239  0.0027  0.0326  57  LYS B CA  
2587 C  C   . LYS B  57  ? 0.1469 0.1655 0.1760 0.0217  -0.0179 0.0403  57  LYS B C   
2588 O  O   . LYS B  57  ? 0.1509 0.1790 0.1983 0.0272  0.0010  0.0396  57  LYS B O   
2589 C  CB  . LYS B  57  ? 0.1568 0.2518 0.2039 0.0184  0.0117  -0.0159 57  LYS B CB  
2590 C  CG  . LYS B  57  ? 0.1840 0.3046 0.2703 0.0701  0.0447  0.0144  57  LYS B CG  
2591 C  CD  . LYS B  57  ? 0.4124 0.5089 0.2328 0.1031  0.1112  0.0460  57  LYS B CD  
2592 C  CE  . LYS B  57  ? 0.6698 0.4224 0.5754 0.1559  0.1219  0.0795  57  LYS B CE  
2593 N  NZ  . LYS B  57  ? 0.9222 0.4449 0.4448 0.2491  -0.0851 -0.0050 57  LYS B NZ  
2594 N  N   . GLN B  58  ? 0.1380 0.1956 0.1998 -0.0025 -0.0275 0.0270  58  GLN B N   
2595 C  CA  . GLN B  58  ? 0.1608 0.2344 0.1539 0.0085  -0.0181 0.0092  58  GLN B CA  
2596 C  C   . GLN B  58  ? 0.1588 0.1703 0.1707 0.0135  -0.0294 0.0288  58  GLN B C   
2597 O  O   . GLN B  58  ? 0.1475 0.1688 0.2368 0.0253  -0.0402 0.0287  58  GLN B O   
2598 C  CB  . GLN B  58  ? 0.2265 0.3497 0.1542 -0.0406 -0.0479 0.0073  58  GLN B CB  
2599 C  CG  . GLN B  58  ? 0.4354 0.3259 0.2906 0.0195  0.0731  0.1024  58  GLN B CG  
2600 C  CD  . GLN B  58  ? 0.4779 0.4921 0.3124 0.1052  0.0025  0.0769  58  GLN B CD  
2601 O  OE1 . GLN B  58  ? 0.3051 0.4240 0.3806 0.0845  -0.0895 0.0854  58  GLN B OE1 
2602 N  NE2 . GLN B  58  ? 0.4454 0.5941 0.3547 0.1624  0.0142  0.2297  58  GLN B NE2 
2603 N  N   . PHE B  59  ? 0.1310 0.1709 0.1535 -0.0040 -0.0258 0.0446  59  PHE B N   
2604 C  CA  . PHE B  59  ? 0.1349 0.1782 0.1306 -0.0186 -0.0207 0.0358  59  PHE B CA  
2605 C  C   . PHE B  59  ? 0.1297 0.1530 0.1329 0.0068  -0.0263 0.0144  59  PHE B C   
2606 O  O   . PHE B  59  ? 0.1391 0.1661 0.1505 -0.0079 -0.0118 0.0184  59  PHE B O   
2607 C  CB  . PHE B  59  ? 0.1342 0.1727 0.1550 -0.0086 -0.0245 0.0502  59  PHE B CB  
2608 C  CG  . PHE B  59  ? 0.1341 0.1685 0.1244 -0.0001 -0.0100 0.0294  59  PHE B CG  
2609 C  CD1 . PHE B  59  ? 0.1412 0.1667 0.1741 0.0022  -0.0247 0.0560  59  PHE B CD1 
2610 C  CD2 . PHE B  59  ? 0.1544 0.1875 0.1358 0.0098  -0.0190 0.0225  59  PHE B CD2 
2611 C  CE1 . PHE B  59  ? 0.1304 0.1852 0.1618 0.0144  -0.0241 0.0506  59  PHE B CE1 
2612 C  CE2 . PHE B  59  ? 0.1558 0.1960 0.1726 0.0035  -0.0017 0.0292  59  PHE B CE2 
2613 C  CZ  . PHE B  59  ? 0.1649 0.1804 0.1700 0.0026  -0.0239 0.0515  59  PHE B CZ  
2614 N  N   . LEU B  60  ? 0.1336 0.1402 0.1493 -0.0034 -0.0231 0.0271  60  LEU B N   
2615 C  CA  . LEU B  60  ? 0.1500 0.1412 0.1425 -0.0159 -0.0285 0.0458  60  LEU B CA  
2616 C  C   . LEU B  60  ? 0.1369 0.1421 0.1195 0.0037  -0.0245 0.0214  60  LEU B C   
2617 O  O   . LEU B  60  ? 0.1488 0.1749 0.1267 0.0012  -0.0247 0.0225  60  LEU B O   
2618 C  CB  . LEU B  60  ? 0.1567 0.1458 0.2171 -0.0099 -0.0225 0.0337  60  LEU B CB  
2619 C  CG  . LEU B  60  ? 0.2248 0.1627 0.3161 0.0037  0.0085  0.0790  60  LEU B CG  
2620 C  CD1 . LEU B  60  ? 0.2854 0.2455 0.2977 0.0307  0.0120  0.1032  60  LEU B CD1 
2621 C  CD2 . LEU B  60  ? 0.3396 0.1679 0.4683 -0.0718 0.0570  0.0006  60  LEU B CD2 
2622 N  N   . LEU B  61  ? 0.1439 0.1711 0.1204 -0.0018 -0.0253 0.0113  61  LEU B N   
2623 C  CA  . LEU B  61  ? 0.1479 0.1563 0.1411 -0.0146 -0.0100 0.0403  61  LEU B CA  
2624 C  C   . LEU B  61  ? 0.1518 0.1556 0.1379 -0.0040 -0.0303 0.0313  61  LEU B C   
2625 O  O   . LEU B  61  ? 0.1773 0.2203 0.1564 -0.0319 -0.0310 0.0772  61  LEU B O   
2626 C  CB  . LEU B  61  ? 0.1477 0.1820 0.1573 -0.0186 -0.0079 -0.0015 61  LEU B CB  
2627 C  CG  . LEU B  61  ? 0.1624 0.1847 0.1534 -0.0234 -0.0016 -0.0037 61  LEU B CG  
2628 C  CD1 . LEU B  61  ? 0.2286 0.1726 0.1952 0.0319  0.0241  0.0254  61  LEU B CD1 
2629 C  CD2 . LEU B  61  ? 0.2022 0.2193 0.1879 -0.0519 0.0250  -0.0395 61  LEU B CD2 
2630 N  N   . THR B  62  ? 0.1333 0.1672 0.1347 -0.0146 -0.0201 0.0428  62  THR B N   
2631 C  CA  . THR B  62  ? 0.1584 0.2077 0.1595 -0.0341 -0.0029 0.0598  62  THR B CA  
2632 C  C   . THR B  62  ? 0.1620 0.1669 0.1585 -0.0346 0.0120  0.0432  62  THR B C   
2633 O  O   . THR B  62  ? 0.1709 0.2080 0.1787 -0.0111 0.0071  0.0697  62  THR B O   
2634 C  CB  . THR B  62  ? 0.1846 0.1386 0.4506 0.0024  0.0868  -0.0031 62  THR B CB  
2635 O  OG1 . THR B  62  ? 0.2355 0.2279 0.3409 0.0283  -0.0042 0.0023  62  THR B OG1 
2636 C  CG2 . THR B  62  ? 0.2099 0.2249 0.4947 -0.0326 0.1148  0.0372  62  THR B CG2 
2637 N  N   . ASN B  63  ? 0.1470 0.1859 0.1542 -0.0243 0.0159  0.0372  63  ASN B N   
2638 C  CA  . ASN B  63  ? 0.1487 0.1805 0.1626 -0.0402 0.0255  0.0077  63  ASN B CA  
2639 C  C   . ASN B  63  ? 0.1641 0.1624 0.1481 -0.0078 0.0036  0.0146  63  ASN B C   
2640 O  O   . ASN B  63  ? 0.1618 0.1595 0.1772 -0.0116 -0.0095 0.0282  63  ASN B O   
2641 C  CB  . ASN B  63  ? 0.1744 0.2046 0.1464 -0.0341 0.0328  0.0082  63  ASN B CB  
2642 C  CG  . ASN B  63  ? 0.1557 0.1337 0.1639 -0.0179 0.0063  0.0219  63  ASN B CG  
2643 O  OD1 . ASN B  63  ? 0.1734 0.1917 0.1608 -0.0447 0.0215  0.0140  63  ASN B OD1 
2644 N  ND2 . ASN B  63  ? 0.2107 0.1662 0.1490 -0.0150 0.0330  0.0363  63  ASN B ND2 
2645 N  N   . ASN B  64  ? 0.1694 0.1520 0.1424 -0.0100 -0.0041 0.0074  64  ASN B N   
2646 C  CA  . ASN B  64  ? 0.1867 0.1556 0.1856 -0.0082 0.0203  -0.0155 64  ASN B CA  
2647 C  C   . ASN B  64  ? 0.1929 0.1713 0.1654 -0.0200 -0.0155 0.0107  64  ASN B C   
2648 O  O   . ASN B  64  ? 0.2139 0.1659 0.1952 -0.0162 -0.0241 -0.0030 64  ASN B O   
2649 C  CB  . ASN B  64  ? 0.1791 0.1743 0.1856 0.0156  -0.0074 -0.0106 64  ASN B CB  
2650 C  CG  . ASN B  64  ? 0.2050 0.1909 0.1583 0.0100  0.0103  -0.0023 64  ASN B CG  
2651 O  OD1 . ASN B  64  ? 0.2000 0.1545 0.1780 -0.0027 0.0126  0.0023  64  ASN B OD1 
2652 N  ND2 . ASN B  64  ? 0.2632 0.2879 0.1577 0.0035  0.0032  0.0272  64  ASN B ND2 
2653 N  N   . GLY B  65  ? 0.1651 0.1679 0.1808 -0.0021 0.0194  0.0323  65  GLY B N   
2654 C  CA  . GLY B  65  ? 0.1572 0.1846 0.2115 -0.0119 0.0072  0.0433  65  GLY B CA  
2655 C  C   . GLY B  65  ? 0.1586 0.1719 0.1793 -0.0197 -0.0003 0.0046  65  GLY B C   
2656 O  O   . GLY B  65  ? 0.1614 0.2834 0.2597 -0.0190 0.0052  0.0756  65  GLY B O   
2657 N  N   . HIS B  66  ? 0.1733 0.1359 0.1789 -0.0091 -0.0003 0.0143  66  HIS B N   
2658 C  CA  . HIS B  66  ? 0.1980 0.1276 0.1971 -0.0062 -0.0221 0.0095  66  HIS B CA  
2659 C  C   . HIS B  66  ? 0.1631 0.1403 0.1722 0.0069  0.0094  0.0141  66  HIS B C   
2660 O  O   . HIS B  66  ? 0.1731 0.1333 0.2137 0.0162  -0.0086 0.0126  66  HIS B O   
2661 C  CB  . HIS B  66  ? 0.2573 0.1541 0.1900 -0.0245 -0.0363 0.0003  66  HIS B CB  
2662 C  CG  . HIS B  66  ? 0.1943 0.1805 0.1857 -0.0161 -0.0314 0.0106  66  HIS B CG  
2663 N  ND1 . HIS B  66  ? 0.2349 0.1935 0.2051 -0.0537 -0.0312 0.0139  66  HIS B ND1 
2664 C  CD2 . HIS B  66  ? 0.1884 0.1929 0.2141 0.0163  -0.0348 0.0310  66  HIS B CD2 
2665 C  CE1 . HIS B  66  ? 0.1967 0.1622 0.1900 -0.0425 -0.0207 0.0097  66  HIS B CE1 
2666 N  NE2 . HIS B  66  ? 0.2183 0.2087 0.2339 -0.0361 0.0040  0.0240  66  HIS B NE2 
2667 N  N   . SER B  67  ? 0.1549 0.1360 0.1759 0.0039  -0.0104 0.0107  67  SER B N   
2668 C  CA  . SER B  67  ? 0.1535 0.1595 0.1375 -0.0272 0.0004  0.0205  67  SER B CA  
2669 C  C   . SER B  67  ? 0.1811 0.1185 0.1399 -0.0117 -0.0079 0.0132  67  SER B C   
2670 O  O   . SER B  67  ? 0.1641 0.1442 0.1773 -0.0053 -0.0070 0.0226  67  SER B O   
2671 C  CB  . SER B  67  ? 0.1681 0.1489 0.1554 0.0089  -0.0048 0.0293  67  SER B CB  
2672 O  OG  . SER B  67  ? 0.1467 0.1634 0.1567 -0.0035 0.0020  0.0310  67  SER B OG  
2673 N  N   . VAL B  68  ? 0.1427 0.1516 0.1550 -0.0143 0.0095  0.0196  68  VAL B N   
2674 C  CA  . VAL B  68  ? 0.1452 0.1559 0.1527 -0.0127 0.0083  0.0154  68  VAL B CA  
2675 C  C   . VAL B  68  ? 0.1328 0.1329 0.1517 -0.0055 0.0154  0.0237  68  VAL B C   
2676 O  O   . VAL B  68  ? 0.1556 0.1623 0.1323 -0.0074 0.0073  0.0009  68  VAL B O   
2677 C  CB  . VAL B  68  ? 0.1731 0.2110 0.1445 -0.0100 0.0057  -0.0023 68  VAL B CB  
2678 C  CG1 . VAL B  68  ? 0.2044 0.2069 0.1527 -0.0172 -0.0177 -0.0080 68  VAL B CG1 
2679 C  CG2 . VAL B  68  ? 0.1852 0.3459 0.1735 -0.0244 -0.0242 -0.0113 68  VAL B CG2 
2680 N  N   . LYS B  69  ? 0.1461 0.1907 0.1384 -0.0022 0.0138  0.0281  69  LYS B N   
2681 C  CA  . LYS B  69  ? 0.1161 0.1799 0.1526 -0.0259 -0.0052 0.0209  69  LYS B CA  
2682 C  C   . LYS B  69  ? 0.1342 0.1338 0.1176 -0.0077 -0.0232 0.0251  69  LYS B C   
2683 O  O   . LYS B  69  ? 0.1355 0.2168 0.1373 -0.0107 -0.0134 0.0682  69  LYS B O   
2684 C  CB  . LYS B  69  ? 0.1798 0.1928 0.2694 -0.0161 -0.0594 -0.0038 69  LYS B CB  
2685 C  CG  . LYS B  69  ? 0.3325 0.2575 0.2913 -0.0439 -0.1251 -0.0170 69  LYS B CG  
2686 C  CD  . LYS B  69  ? 0.3540 0.1808 0.4734 -0.0528 -0.0024 -0.1513 69  LYS B CD  
2687 C  CE  . LYS B  69  ? 0.2764 0.2453 0.4382 -0.0183 0.0312  -0.0705 69  LYS B CE  
2688 N  NZ  . LYS B  69  ? 0.4417 0.2728 0.3664 -0.0680 0.0640  -0.1044 69  LYS B NZ  
2689 N  N   . LEU B  70  ? 0.1179 0.1224 0.1390 -0.0043 -0.0079 0.0230  70  LEU B N   
2690 C  CA  . LEU B  70  ? 0.1136 0.1278 0.1159 0.0085  -0.0065 0.0225  70  LEU B CA  
2691 C  C   . LEU B  70  ? 0.1358 0.1234 0.1067 0.0050  -0.0161 0.0176  70  LEU B C   
2692 O  O   . LEU B  70  ? 0.1303 0.1260 0.1208 0.0059  -0.0079 0.0147  70  LEU B O   
2693 C  CB  . LEU B  70  ? 0.1240 0.1148 0.1409 0.0010  -0.0070 0.0309  70  LEU B CB  
2694 C  CG  . LEU B  70  ? 0.1365 0.1315 0.1433 -0.0071 -0.0220 0.0171  70  LEU B CG  
2695 C  CD1 . LEU B  70  ? 0.1619 0.1566 0.1644 -0.0257 -0.0665 0.0332  70  LEU B CD1 
2696 C  CD2 . LEU B  70  ? 0.1957 0.1186 0.1741 -0.0361 -0.0184 0.0229  70  LEU B CD2 
2697 N  N   . ASN B  71  ? 0.1315 0.1242 0.1264 0.0118  -0.0115 0.0075  71  ASN B N   
2698 C  CA  . ASN B  71  ? 0.1580 0.1200 0.1444 0.0171  -0.0148 0.0145  71  ASN B CA  
2699 C  C   . ASN B  71  ? 0.1295 0.1708 0.1516 0.0137  -0.0116 0.0225  71  ASN B C   
2700 O  O   . ASN B  71  ? 0.1602 0.2251 0.1662 -0.0249 -0.0200 0.0283  71  ASN B O   
2701 C  CB  . ASN B  71  ? 0.1889 0.1484 0.1934 0.0342  0.0140  0.0354  71  ASN B CB  
2702 C  CG  . ASN B  71  ? 0.2439 0.1889 0.2155 0.0310  -0.0006 0.0250  71  ASN B CG  
2703 O  OD1 . ASN B  71  ? 0.2778 0.2017 0.3189 -0.0216 0.0534  0.0020  71  ASN B OD1 
2704 N  ND2 . ASN B  71  ? 0.4346 0.1908 0.2860 0.0626  -0.0241 0.0517  71  ASN B ND2 
2705 N  N   . LEU B  72  ? 0.1349 0.1497 0.1452 0.0122  -0.0096 0.0181  72  LEU B N   
2706 C  CA  . LEU B  72  ? 0.1111 0.1505 0.1481 0.0185  -0.0060 0.0102  72  LEU B CA  
2707 C  C   . LEU B  72  ? 0.1430 0.1532 0.1682 0.0310  -0.0118 0.0199  72  LEU B C   
2708 O  O   . LEU B  72  ? 0.1727 0.1624 0.1940 0.0194  0.0237  -0.0087 72  LEU B O   
2709 C  CB  . LEU B  72  ? 0.1206 0.1412 0.1532 0.0237  -0.0220 0.0174  72  LEU B CB  
2710 C  CG  . LEU B  72  ? 0.1400 0.1339 0.1509 0.0238  -0.0146 0.0120  72  LEU B CG  
2711 C  CD1 . LEU B  72  ? 0.1066 0.1421 0.1612 0.0138  -0.0198 0.0255  72  LEU B CD1 
2712 C  CD2 . LEU B  72  ? 0.1426 0.1419 0.1582 0.0011  -0.0083 0.0126  72  LEU B CD2 
2713 N  N   . PRO B  73  ? 0.1407 0.1348 0.1552 0.0318  -0.0099 0.0115  73  PRO B N   
2714 C  CA  . PRO B  73  ? 0.1594 0.1829 0.1799 0.0270  0.0141  0.0130  73  PRO B CA  
2715 C  C   . PRO B  73  ? 0.1781 0.1747 0.1975 0.0348  0.0296  0.0077  73  PRO B C   
2716 O  O   . PRO B  73  ? 0.1739 0.1972 0.1923 0.0100  0.0039  0.0408  73  PRO B O   
2717 C  CB  . PRO B  73  ? 0.1726 0.2018 0.2000 0.0245  0.0002  0.0185  73  PRO B CB  
2718 C  CG  . PRO B  73  ? 0.1179 0.1982 0.2185 0.0228  -0.0129 0.0245  73  PRO B CG  
2719 C  CD  . PRO B  73  ? 0.1445 0.1549 0.1817 0.0108  -0.0126 -0.0021 73  PRO B CD  
2720 N  N   . SER B  74  ? 0.2439 0.2262 0.2267 0.0194  0.0710  -0.0253 74  SER B N   
2721 C  CA  . SER B  74  ? 0.2286 0.2006 0.2397 0.0193  0.0605  -0.0013 74  SER B CA  
2722 C  C   . SER B  74  ? 0.1943 0.2116 0.2065 0.0269  0.0394  -0.0111 74  SER B C   
2723 O  O   . SER B  74  ? 0.2123 0.2422 0.2082 0.0085  0.0485  -0.0030 74  SER B O   
2724 C  CB  . SER B  74  ? 0.3373 0.2046 0.2985 0.0543  0.0362  0.0000  74  SER B CB  
2725 O  OG  . SER B  74  ? 0.4175 0.2649 0.3512 0.1132  0.0491  -0.0174 74  SER B OG  
2726 N  N   . ASP B  75  ? 0.1569 0.2113 0.2344 0.0313  0.0294  0.0270  75  ASP B N   
2727 C  CA  . ASP B  75  ? 0.1432 0.2062 0.2597 0.0427  0.0250  0.0385  75  ASP B CA  
2728 C  C   . ASP B  75  ? 0.1688 0.1934 0.2474 0.0301  0.0263  0.0475  75  ASP B C   
2729 O  O   . ASP B  75  ? 0.1767 0.2551 0.2802 0.0352  0.0352  0.0831  75  ASP B O   
2730 C  CB  . ASP B  75  ? 0.1636 0.2872 0.3991 0.0488  -0.0148 0.0842  75  ASP B CB  
2731 C  CG  . ASP B  75  ? 0.2282 0.5156 0.3943 -0.0374 -0.0374 0.1953  75  ASP B CG  
2732 O  OD1 . ASP B  75  ? 0.3380 0.6869 0.4388 -0.1703 0.0352  0.1492  75  ASP B OD1 
2733 O  OD2 . ASP B  75  ? 0.6434 0.8809 1.0246 -0.3446 -0.1881 -0.0041 75  ASP B OD2 
2734 N  N   . MET B  76  ? 0.1490 0.2078 0.1953 0.0421  0.0205  0.0355  76  MET B N   
2735 C  CA  . MET B  76  ? 0.1176 0.2007 0.1837 0.0118  0.0157  0.0189  76  MET B CA  
2736 C  C   . MET B  76  ? 0.1159 0.1606 0.1745 0.0242  0.0064  0.0312  76  MET B C   
2737 O  O   . MET B  76  ? 0.1321 0.1746 0.1864 0.0093  0.0156  0.0332  76  MET B O   
2738 C  CB  . MET B  76  ? 0.1948 0.2000 0.2082 0.0358  0.0280  0.0534  76  MET B CB  
2739 C  CG  . MET B  76  ? 0.1280 0.2186 0.1947 0.0226  0.0032  0.0515  76  MET B CG  
2740 S  SD  . MET B  76  ? 0.1599 0.1947 0.1995 -0.0025 0.0152  0.0034  76  MET B SD  
2741 C  CE  . MET B  76  ? 0.1456 0.1496 0.1829 0.0168  0.0309  0.0302  76  MET B CE  
2742 N  N   . HIS B  77  ? 0.1231 0.1676 0.1671 0.0313  0.0150  0.0256  77  HIS B N   
2743 C  CA  . HIS B  77  ? 0.1419 0.1777 0.1644 0.0409  0.0146  0.0269  77  HIS B CA  
2744 C  C   . HIS B  77  ? 0.1379 0.1479 0.1418 0.0175  0.0082  0.0083  77  HIS B C   
2745 O  O   . HIS B  77  ? 0.1411 0.1641 0.1756 0.0100  0.0036  0.0184  77  HIS B O   
2746 C  CB  . HIS B  77  ? 0.1536 0.2229 0.2211 0.0461  0.0518  0.0053  77  HIS B CB  
2747 C  CG  . HIS B  77  ? 0.1657 0.2416 0.2140 0.0387  0.0370  0.0091  77  HIS B CG  
2748 N  ND1 . HIS B  77  ? 0.1533 0.2600 0.2696 0.0248  0.0359  -0.0048 77  HIS B ND1 
2749 C  CD2 . HIS B  77  ? 0.2027 0.2705 0.2029 0.0161  0.0640  0.0209  77  HIS B CD2 
2750 C  CE1 . HIS B  77  ? 0.2207 0.2526 0.2196 0.0303  0.0513  -0.0048 77  HIS B CE1 
2751 N  NE2 . HIS B  77  ? 0.1988 0.3343 0.2486 -0.0154 0.0701  -0.0065 77  HIS B NE2 
2752 N  N   . ILE B  78  ? 0.1619 0.2016 0.1361 0.0378  -0.0055 0.0131  78  ILE B N   
2753 C  CA  . ILE B  78  ? 0.1782 0.2019 0.1448 0.0378  -0.0023 0.0499  78  ILE B CA  
2754 C  C   . ILE B  78  ? 0.1690 0.1828 0.1753 0.0515  -0.0052 -0.0025 78  ILE B C   
2755 O  O   . ILE B  78  ? 0.2060 0.2132 0.1794 0.0455  0.0242  0.0108  78  ILE B O   
2756 C  CB  . ILE B  78  ? 0.1662 0.2424 0.1573 0.0528  0.0115  0.0467  78  ILE B CB  
2757 C  CG1 . ILE B  78  ? 0.1722 0.2620 0.1839 0.0266  0.0298  0.0636  78  ILE B CG1 
2758 C  CG2 . ILE B  78  ? 0.1946 0.2815 0.1886 0.0692  0.0299  0.0840  78  ILE B CG2 
2759 C  CD1 . ILE B  78  ? 0.1554 0.2385 0.2147 0.0413  0.0279  0.0551  78  ILE B CD1 
2760 N  N   . GLN B  79  ? 0.1681 0.2112 0.1664 0.0388  0.0093  0.0465  79  GLN B N   
2761 C  CA  . GLN B  79  ? 0.1647 0.2600 0.1703 0.0299  0.0097  0.0345  79  GLN B CA  
2762 C  C   . GLN B  79  ? 0.2097 0.2397 0.1787 0.0198  0.0275  0.0381  79  GLN B C   
2763 O  O   . GLN B  79  ? 0.2413 0.2415 0.1754 0.0328  0.0128  0.0184  79  GLN B O   
2764 C  CB  . GLN B  79  ? 0.2060 0.3097 0.2499 -0.0057 0.0172  0.0478  79  GLN B CB  
2765 C  CG  . GLN B  79  ? 0.2969 0.4113 0.2949 -0.0416 0.0523  0.0849  79  GLN B CG  
2766 C  CD  . GLN B  79  ? 0.3377 0.4978 0.2924 0.1102  0.0025  0.0460  79  GLN B CD  
2767 O  OE1 . GLN B  79  ? 0.3376 0.3865 0.3886 0.0539  -0.0006 -0.0199 79  GLN B OE1 
2768 N  NE2 . GLN B  79  ? 0.5295 0.8562 0.2724 -0.0939 0.0332  0.0195  79  GLN B NE2 
2769 N  N   . GLY B  80  ? 0.2536 0.2673 0.1655 0.0657  0.0131  0.0365  80  GLY B N   
2770 C  CA  . GLY B  80  ? 0.2656 0.2517 0.1776 0.0209  0.0115  0.0424  80  GLY B CA  
2771 C  C   . GLY B  80  ? 0.2192 0.2809 0.1889 0.0374  0.0164  0.0425  80  GLY B C   
2772 O  O   . GLY B  80  ? 0.2428 0.3817 0.2163 0.0143  0.0085  0.1158  80  GLY B O   
2773 N  N   . LEU B  81  ? 0.2211 0.2404 0.1869 0.0212  0.0093  0.0243  81  LEU B N   
2774 C  CA  . LEU B  81  ? 0.2264 0.2902 0.1688 0.0435  -0.0035 0.0381  81  LEU B CA  
2775 C  C   . LEU B  81  ? 0.2573 0.3095 0.1700 0.0071  0.0223  0.0549  81  LEU B C   
2776 O  O   . LEU B  81  ? 0.2494 0.3151 0.1914 0.0153  0.0226  0.0210  81  LEU B O   
2777 C  CB  . LEU B  81  ? 0.2310 0.2489 0.2707 0.0644  0.0484  0.0581  81  LEU B CB  
2778 C  CG  . LEU B  81  ? 0.2094 0.2567 0.2360 0.0712  0.0210  0.0205  81  LEU B CG  
2779 C  CD1 . LEU B  81  ? 0.2578 0.2649 0.2404 0.0388  0.0529  0.0279  81  LEU B CD1 
2780 C  CD2 . LEU B  81  ? 0.2460 0.3294 0.2743 0.0875  -0.0182 0.1027  81  LEU B CD2 
2781 N  N   . GLN B  82  ? 0.3016 0.3604 0.2184 0.0350  -0.0617 -0.0406 82  GLN B N   
2782 C  CA  . GLN B  82  ? 0.2852 0.3716 0.2555 0.0168  -0.0659 -0.0194 82  GLN B CA  
2783 C  C   . GLN B  82  ? 0.3762 0.4541 0.2063 0.1285  -0.0015 0.0127  82  GLN B C   
2784 O  O   . GLN B  82  ? 0.4971 0.3991 0.1731 0.1227  0.0252  -0.0164 82  GLN B O   
2785 C  CB  . GLN B  82  ? 0.4519 0.3758 0.2926 0.0438  -0.1804 -0.0372 82  GLN B CB  
2786 C  CG  . GLN B  82  ? 0.2223 0.4106 0.3877 0.0066  -0.0182 0.0734  82  GLN B CG  
2787 C  CD  . GLN B  82  ? 0.4335 0.7677 0.4673 -0.1586 -0.1346 0.1199  82  GLN B CD  
2788 O  OE1 . GLN B  82  ? 0.4446 0.6970 0.4889 -0.1993 -0.0418 0.2332  82  GLN B OE1 
2789 N  NE2 . GLN B  82  ? 0.3902 0.4175 0.4103 0.0807  -0.0684 0.0187  82  GLN B NE2 
2790 N  N   . SER B  83  ? 0.3274 0.2770 0.2195 0.0451  0.0186  -0.0274 83  SER B N   
2791 C  CA  . SER B  83  ? 0.2703 0.2834 0.1699 0.0438  -0.0053 0.0006  83  SER B CA  
2792 C  C   . SER B  83  ? 0.2744 0.2752 0.1627 0.0545  0.0354  0.0232  83  SER B C   
2793 O  O   . SER B  83  ? 0.2190 0.2446 0.2032 0.0318  0.0379  -0.0165 83  SER B O   
2794 C  CB  . SER B  83  ? 0.3638 0.2739 0.1996 0.0354  -0.0079 -0.0318 83  SER B CB  
2795 O  OG  . SER B  83  ? 0.4158 0.4221 0.2332 0.0367  -0.0585 -0.0745 83  SER B OG  
2796 N  N   . ARG B  84  ? 0.2595 0.2948 0.1633 0.0538  0.0595  -0.0079 84  ARG B N   
2797 C  CA  . ARG B  84  ? 0.2150 0.2801 0.1670 0.0170  0.0535  -0.0215 84  ARG B CA  
2798 C  C   . ARG B  84  ? 0.2192 0.2187 0.1810 0.0378  0.0432  -0.0089 84  ARG B C   
2799 O  O   . ARG B  84  ? 0.2082 0.2368 0.1972 0.0394  0.0460  -0.0414 84  ARG B O   
2800 C  CB  . ARG B  84  ? 0.2588 0.3573 0.1958 0.0956  0.0487  0.0195  84  ARG B CB  
2801 C  CG  . ARG B  84  ? 0.2203 0.3270 0.2401 0.0434  0.0020  0.0452  84  ARG B CG  
2802 C  CD  . ARG B  84  ? 0.2280 0.3838 0.2906 0.0860  0.0228  0.0553  84  ARG B CD  
2803 N  NE  . ARG B  84  ? 0.2661 0.3202 0.2739 0.0763  0.0302  0.0067  84  ARG B NE  
2804 C  CZ  . ARG B  84  ? 0.2736 0.4052 0.2827 0.0555  0.0456  0.0693  84  ARG B CZ  
2805 N  NH1 . ARG B  84  ? 0.3263 0.6123 0.4154 0.1391  0.1576  0.0265  84  ARG B NH1 
2806 N  NH2 . ARG B  84  ? 0.5061 0.3764 0.2176 0.0687  0.0493  -0.0033 84  ARG B NH2 
2807 N  N   . TYR B  85  ? 0.1805 0.2167 0.1412 0.0433  0.0232  -0.0044 85  TYR B N   
2808 C  CA  . TYR B  85  ? 0.1563 0.1879 0.1312 0.0313  0.0307  0.0138  85  TYR B CA  
2809 C  C   . TYR B  85  ? 0.1488 0.1516 0.1705 0.0127  0.0387  -0.0013 85  TYR B C   
2810 O  O   . TYR B  85  ? 0.1747 0.1730 0.1879 0.0126  0.0036  0.0216  85  TYR B O   
2811 C  CB  . TYR B  85  ? 0.1674 0.2036 0.1484 0.0421  0.0096  -0.0196 85  TYR B CB  
2812 C  CG  . TYR B  85  ? 0.1546 0.1701 0.1424 0.0178  0.0210  -0.0165 85  TYR B CG  
2813 C  CD1 . TYR B  85  ? 0.1988 0.2076 0.1492 0.0201  0.0177  -0.0151 85  TYR B CD1 
2814 C  CD2 . TYR B  85  ? 0.1610 0.1547 0.1630 0.0228  0.0179  -0.0211 85  TYR B CD2 
2815 C  CE1 . TYR B  85  ? 0.2021 0.2087 0.1810 -0.0100 0.0006  -0.0029 85  TYR B CE1 
2816 C  CE2 . TYR B  85  ? 0.1717 0.1725 0.1649 0.0479  0.0092  -0.0284 85  TYR B CE2 
2817 C  CZ  . TYR B  85  ? 0.1809 0.1952 0.1658 0.0096  0.0026  -0.0348 85  TYR B CZ  
2818 O  OH  . TYR B  85  ? 0.2385 0.2566 0.1842 -0.0271 -0.0211 -0.0231 85  TYR B OH  
2819 N  N   . SER B  86  ? 0.1369 0.1713 0.1651 0.0348  0.0201  0.0162  86  SER B N   
2820 C  CA  . SER B  86  ? 0.1537 0.1848 0.1493 0.0528  0.0201  -0.0031 86  SER B CA  
2821 C  C   . SER B  86  ? 0.1221 0.1345 0.1612 0.0277  0.0136  0.0004  86  SER B C   
2822 O  O   . SER B  86  ? 0.1252 0.1420 0.1516 0.0217  0.0158  0.0006  86  SER B O   
2823 C  CB  . SER B  86  ? 0.1645 0.2161 0.2018 0.0829  0.0390  0.0109  86  SER B CB  
2824 O  OG  . SER B  86  ? 0.1683 0.2364 0.2390 0.0588  0.0619  -0.0025 86  SER B OG  
2825 N  N   . ALA B  87  ? 0.1323 0.1458 0.1464 0.0243  0.0132  0.0060  87  ALA B N   
2826 C  CA  . ALA B  87  ? 0.1247 0.1383 0.1504 0.0267  0.0154  0.0132  87  ALA B CA  
2827 C  C   . ALA B  87  ? 0.1203 0.1357 0.1487 0.0311  0.0068  0.0154  87  ALA B C   
2828 O  O   . ALA B  87  ? 0.1386 0.1642 0.1766 0.0392  0.0099  0.0333  87  ALA B O   
2829 C  CB  . ALA B  87  ? 0.1736 0.1555 0.1724 -0.0103 0.0109  -0.0121 87  ALA B CB  
2830 N  N   . THR B  88  ? 0.1259 0.1333 0.1277 0.0167  0.0109  0.0085  88  THR B N   
2831 C  CA  . THR B  88  ? 0.1460 0.1269 0.1406 0.0156  0.0013  0.0042  88  THR B CA  
2832 C  C   . THR B  88  ? 0.1405 0.1200 0.1310 0.0313  -0.0040 0.0019  88  THR B C   
2833 O  O   . THR B  88  ? 0.1238 0.1188 0.1444 0.0280  -0.0015 0.0118  88  THR B O   
2834 C  CB  . THR B  88  ? 0.1732 0.1271 0.1925 0.0067  -0.0048 0.0000  88  THR B CB  
2835 O  OG1 . THR B  88  ? 0.2875 0.1488 0.1962 -0.0002 0.0001  0.0172  88  THR B OG1 
2836 C  CG2 . THR B  88  ? 0.1596 0.1464 0.2192 0.0293  0.0115  -0.0055 88  THR B CG2 
2837 N  N   . GLN B  89  ? 0.1116 0.1107 0.1356 0.0222  0.0043  -0.0005 89  GLN B N   
2838 C  CA  . GLN B  89  ? 0.1165 0.1018 0.1249 0.0184  0.0082  0.0116  89  GLN B CA  
2839 C  C   . GLN B  89  ? 0.1021 0.1058 0.1226 0.0179  0.0013  0.0082  89  GLN B C   
2840 O  O   . GLN B  89  ? 0.1265 0.1170 0.1084 0.0239  -0.0052 0.0058  89  GLN B O   
2841 C  CB  . GLN B  89  ? 0.1295 0.1113 0.1502 0.0000  -0.0073 0.0171  89  GLN B CB  
2842 C  CG  . GLN B  89  ? 0.1322 0.1549 0.1779 -0.0218 0.0031  -0.0242 89  GLN B CG  
2843 C  CD  . GLN B  89  ? 0.1514 0.1300 0.1761 0.0055  -0.0211 0.0018  89  GLN B CD  
2844 O  OE1 . GLN B  89  ? 0.1428 0.1535 0.1891 0.0301  -0.0004 -0.0004 89  GLN B OE1 
2845 N  NE2 . GLN B  89  ? 0.1883 0.2268 0.2707 -0.0300 -0.0077 0.0790  89  GLN B NE2 
2846 N  N   . LEU B  90  ? 0.1037 0.1070 0.1035 0.0120  0.0000  -0.0012 90  LEU B N   
2847 C  CA  . LEU B  90  ? 0.1078 0.0851 0.1079 0.0162  0.0082  0.0138  90  LEU B CA  
2848 C  C   . LEU B  90  ? 0.1000 0.0963 0.1027 0.0080  0.0020  0.0109  90  LEU B C   
2849 O  O   . LEU B  90  ? 0.1105 0.1080 0.1121 0.0105  0.0033  0.0251  90  LEU B O   
2850 C  CB  . LEU B  90  ? 0.1082 0.0994 0.1127 0.0011  -0.0092 0.0149  90  LEU B CB  
2851 C  CG  . LEU B  90  ? 0.1170 0.1019 0.1208 -0.0010 -0.0133 0.0131  90  LEU B CG  
2852 C  CD1 . LEU B  90  ? 0.1411 0.1186 0.1359 -0.0080 -0.0144 -0.0055 90  LEU B CD1 
2853 C  CD2 . LEU B  90  ? 0.1281 0.1259 0.1477 -0.0096 -0.0122 0.0168  90  LEU B CD2 
2854 N  N   . HIS B  91  ? 0.0893 0.1064 0.1123 0.0059  0.0060  0.0055  91  HIS B N   
2855 C  CA  . HIS B  91  ? 0.0933 0.0971 0.1202 0.0086  0.0122  0.0121  91  HIS B CA  
2856 C  C   . HIS B  91  ? 0.0960 0.0938 0.1058 0.0027  0.0012  0.0212  91  HIS B C   
2857 O  O   . HIS B  91  ? 0.1143 0.0939 0.0996 0.0091  0.0054  0.0176  91  HIS B O   
2858 C  CB  . HIS B  91  ? 0.1165 0.0904 0.1210 -0.0032 -0.0063 0.0294  91  HIS B CB  
2859 C  CG  . HIS B  91  ? 0.0951 0.0919 0.1012 -0.0083 0.0057  0.0099  91  HIS B CG  
2860 N  ND1 . HIS B  91  ? 0.1057 0.0985 0.1161 -0.0057 -0.0052 -0.0004 91  HIS B ND1 
2861 C  CD2 . HIS B  91  ? 0.1096 0.1051 0.1079 -0.0095 -0.0158 0.0077  91  HIS B CD2 
2862 C  CE1 . HIS B  91  ? 0.0971 0.1098 0.1107 -0.0033 -0.0006 0.0010  91  HIS B CE1 
2863 N  NE2 . HIS B  91  ? 0.1028 0.0864 0.1137 -0.0006 0.0021  0.0041  91  HIS B NE2 
2864 N  N   . LEU B  92  ? 0.1070 0.0985 0.1032 0.0015  0.0114  0.0089  92  LEU B N   
2865 C  CA  . LEU B  92  ? 0.0920 0.1121 0.1254 0.0099  0.0119  0.0053  92  LEU B CA  
2866 C  C   . LEU B  92  ? 0.1019 0.0999 0.1088 0.0036  0.0121  0.0148  92  LEU B C   
2867 O  O   . LEU B  92  ? 0.1097 0.1094 0.1203 0.0105  0.0078  0.0133  92  LEU B O   
2868 C  CB  . LEU B  92  ? 0.1191 0.1532 0.1386 -0.0189 0.0149  -0.0255 92  LEU B CB  
2869 C  CG  . LEU B  92  ? 0.1235 0.1520 0.1410 -0.0233 -0.0050 -0.0118 92  LEU B CG  
2870 C  CD1 . LEU B  92  ? 0.1828 0.2079 0.2667 -0.0124 -0.0566 0.0291  92  LEU B CD1 
2871 C  CD2 . LEU B  92  ? 0.1374 0.1361 0.2781 -0.0166 0.0136  0.0578  92  LEU B CD2 
2872 N  N   . HIS B  93  ? 0.0958 0.1015 0.1082 0.0091  0.0145  -0.0029 93  HIS B N   
2873 C  CA  . HIS B  93  ? 0.0954 0.0951 0.1132 0.0111  0.0184  -0.0031 93  HIS B CA  
2874 C  C   . HIS B  93  ? 0.1051 0.0900 0.1139 0.0019  0.0105  0.0098  93  HIS B C   
2875 O  O   . HIS B  93  ? 0.1201 0.0964 0.1207 -0.0037 0.0243  0.0128  93  HIS B O   
2876 C  CB  . HIS B  93  ? 0.1009 0.1091 0.1337 0.0084  0.0089  -0.0017 93  HIS B CB  
2877 C  CG  . HIS B  93  ? 0.1003 0.0973 0.1073 0.0087  0.0000  0.0021  93  HIS B CG  
2878 N  ND1 . HIS B  93  ? 0.1012 0.1027 0.1238 -0.0005 0.0087  0.0019  93  HIS B ND1 
2879 C  CD2 . HIS B  93  ? 0.0949 0.1009 0.1111 0.0154  0.0033  -0.0012 93  HIS B CD2 
2880 C  CE1 . HIS B  93  ? 0.0998 0.1125 0.1188 0.0077  0.0131  0.0170  93  HIS B CE1 
2881 N  NE2 . HIS B  93  ? 0.0916 0.0882 0.1111 0.0016  0.0021  0.0162  93  HIS B NE2 
2882 N  N   . TRP B  94  ? 0.1168 0.0956 0.1247 0.0079  0.0326  0.0089  94  TRP B N   
2883 C  CA  . TRP B  94  ? 0.1202 0.1000 0.1242 0.0141  0.0444  0.0054  94  TRP B CA  
2884 C  C   . TRP B  94  ? 0.1323 0.1036 0.1237 -0.0020 0.0319  0.0215  94  TRP B C   
2885 O  O   . TRP B  94  ? 0.1238 0.1073 0.1311 0.0044  0.0397  0.0173  94  TRP B O   
2886 C  CB  . TRP B  94  ? 0.1465 0.0894 0.1267 0.0053  0.0245  0.0135  94  TRP B CB  
2887 C  CG  . TRP B  94  ? 0.1393 0.1007 0.1287 0.0065  0.0305  0.0010  94  TRP B CG  
2888 C  CD1 . TRP B  94  ? 0.1595 0.1125 0.1339 0.0117  0.0345  0.0054  94  TRP B CD1 
2889 C  CD2 . TRP B  94  ? 0.1328 0.1213 0.1048 0.0016  0.0036  0.0001  94  TRP B CD2 
2890 N  NE1 . TRP B  94  ? 0.1586 0.1222 0.1455 0.0128  0.0402  0.0126  94  TRP B NE1 
2891 C  CE2 . TRP B  94  ? 0.1349 0.1145 0.1159 0.0016  0.0291  0.0113  94  TRP B CE2 
2892 C  CE3 . TRP B  94  ? 0.1207 0.1209 0.1231 0.0000  0.0215  0.0000  94  TRP B CE3 
2893 C  CZ2 . TRP B  94  ? 0.1525 0.1143 0.1546 0.0041  0.0345  0.0099  94  TRP B CZ2 
2894 C  CZ3 . TRP B  94  ? 0.1323 0.1378 0.1194 0.0106  0.0046  -0.0003 94  TRP B CZ3 
2895 C  CH2 . TRP B  94  ? 0.1473 0.1351 0.1140 -0.0099 0.0194  0.0075  94  TRP B CH2 
2896 N  N   . GLY B  95  ? 0.1468 0.1075 0.1351 0.0066  0.0472  0.0039  95  GLY B N   
2897 C  CA  . GLY B  95  ? 0.1426 0.1377 0.1439 0.0268  0.0619  0.0243  95  GLY B CA  
2898 C  C   . GLY B  95  ? 0.1181 0.1450 0.1406 0.0179  0.0507  0.0136  95  GLY B C   
2899 O  O   . GLY B  95  ? 0.1595 0.1358 0.1404 0.0053  0.0544  0.0087  95  GLY B O   
2900 N  N   . ASN B  96  ? 0.1564 0.1584 0.1293 0.0128  0.0490  0.0088  96  ASN B N   
2901 C  CA  . ASN B  96  ? 0.1911 0.1866 0.1398 0.0095  0.0506  0.0046  96  ASN B CA  
2902 C  C   . ASN B  96  ? 0.1763 0.1671 0.1512 0.0149  0.0455  0.0189  96  ASN B C   
2903 O  O   . ASN B  96  ? 0.1700 0.1703 0.1576 0.0137  0.0551  -0.0044 96  ASN B O   
2904 C  CB  . ASN B  96  ? 0.2175 0.1797 0.2250 0.0030  0.0961  0.0038  96  ASN B CB  
2905 C  CG  . ASN B  96  ? 0.2193 0.1967 0.2575 -0.0334 0.0996  -0.0216 96  ASN B CG  
2906 O  OD1 . ASN B  96  ? 0.2293 0.2371 0.3683 -0.0152 0.1357  -0.1144 96  ASN B OD1 
2907 N  ND2 . ASN B  96  ? 0.1644 0.2549 0.3145 0.0221  0.0631  -0.0507 96  ASN B ND2 
2908 N  N   . PRO B  97  ? 0.1827 0.1673 0.1733 0.0248  0.0495  -0.0035 97  PRO B N   
2909 C  CA  . PRO B  97  ? 0.2200 0.2185 0.1693 0.0471  0.0000  -0.0306 97  PRO B CA  
2910 C  C   . PRO B  97  ? 0.2007 0.1758 0.1687 0.0111  0.0427  0.0015  97  PRO B C   
2911 O  O   . PRO B  97  ? 0.2370 0.2296 0.1924 -0.0365 0.0319  -0.0148 97  PRO B O   
2912 C  CB  . PRO B  97  ? 0.2268 0.3131 0.1906 0.1213  0.0275  0.0392  97  PRO B CB  
2913 C  CG  . PRO B  97  ? 0.2506 0.3097 0.1818 0.0972  0.0490  0.0035  97  PRO B CG  
2914 C  CD  . PRO B  97  ? 0.2537 0.2134 0.1872 0.0245  0.0636  0.0298  97  PRO B CD  
2915 N  N   . ASN B  98  ? 0.1673 0.1992 0.1478 0.0284  0.0305  -0.0125 98  ASN B N   
2916 C  CA  . ASN B  98  ? 0.1927 0.2342 0.1717 0.0557  0.0357  0.0413  98  ASN B CA  
2917 C  C   . ASN B  98  ? 0.1988 0.3467 0.1852 0.0661  0.0242  0.0010  98  ASN B C   
2918 O  O   . ASN B  98  ? 0.3668 0.4984 0.2335 0.2533  0.0850  0.0663  98  ASN B O   
2919 C  CB  . ASN B  98  ? 0.1890 0.3362 0.1689 0.0075  0.0297  0.0156  98  ASN B CB  
2920 C  CG  . ASN B  98  ? 0.2205 0.2845 0.1629 -0.0033 0.0271  0.0077  98  ASN B CG  
2921 O  OD1 . ASN B  98  ? 0.2705 0.2387 0.1770 0.0416  0.0528  0.0010  98  ASN B OD1 
2922 N  ND2 . ASN B  98  ? 0.3061 0.2924 0.2452 -0.0469 0.1085  0.0122  98  ASN B ND2 
2923 N  N   . ASP B  99  ? 0.2333 0.2636 0.1505 0.0539  0.0520  0.0315  99  ASP B N   
2924 C  CA  . ASP B  99  ? 0.2013 0.2949 0.1788 0.0541  0.0475  0.0554  99  ASP B CA  
2925 C  C   . ASP B  99  ? 0.1742 0.1956 0.1900 0.0168  0.0172  0.0310  99  ASP B C   
2926 O  O   . ASP B  99  ? 0.1947 0.2064 0.1818 -0.0089 0.0163  0.0282  99  ASP B O   
2927 C  CB  . ASP B  99  ? 0.2164 0.4223 0.2586 -0.0162 0.0116  0.0920  99  ASP B CB  
2928 C  CG  . ASP B  99  ? 0.3534 0.6032 0.2855 0.1632  -0.0400 0.0945  99  ASP B CG  
2929 O  OD1 . ASP B  99  ? 0.5133 0.9007 0.4172 0.2479  0.0789  0.1771  99  ASP B OD1 
2930 O  OD2 . ASP B  99  ? 0.7037 2.5804 2.4063 0.5583  -1.0655 -1.8370 99  ASP B OD2 
2931 N  N   . PRO B  100 ? 0.1866 0.1781 0.1705 0.0271  0.0190  0.0026  100 PRO B N   
2932 C  CA  . PRO B  100 ? 0.1760 0.1905 0.1778 0.0055  0.0323  -0.0172 100 PRO B CA  
2933 C  C   . PRO B  100 ? 0.1690 0.1296 0.1962 -0.0072 0.0504  -0.0138 100 PRO B C   
2934 O  O   . PRO B  100 ? 0.2199 0.1641 0.2195 -0.0401 0.0863  -0.0294 100 PRO B O   
2935 C  CB  . PRO B  100 ? 0.2098 0.1835 0.2196 -0.0081 -0.0142 -0.0174 100 PRO B CB  
2936 C  CG  . PRO B  100 ? 0.2610 0.2036 0.2669 0.0234  0.0352  -0.0265 100 PRO B CG  
2937 C  CD  . PRO B  100 ? 0.2597 0.2051 0.2394 0.0357  0.0563  -0.0513 100 PRO B CD  
2938 N  N   . HIS B  101 ? 0.1659 0.1839 0.1821 -0.0138 0.0346  -0.0311 101 HIS B N   
2939 C  CA  . HIS B  101 ? 0.1754 0.1521 0.1961 0.0190  0.0427  -0.0182 101 HIS B CA  
2940 C  C   . HIS B  101 ? 0.1641 0.1299 0.2383 -0.0245 0.0403  -0.0109 101 HIS B C   
2941 O  O   . HIS B  101 ? 0.1812 0.2153 0.3230 0.0041  0.0012  -0.0008 101 HIS B O   
2942 C  CB  . HIS B  101 ? 0.2482 0.2300 0.2109 0.0675  0.0351  0.0227  101 HIS B CB  
2943 C  CG  . HIS B  101 ? 0.2670 0.2209 0.3263 0.0653  -0.0050 0.0583  101 HIS B CG  
2944 N  ND1 . HIS B  101 ? 0.5073 0.2321 0.4592 0.0501  0.0071  0.0798  101 HIS B ND1 
2945 C  CD2 . HIS B  101 ? 0.3054 0.2481 0.3604 0.0726  -0.0344 -0.0949 101 HIS B CD2 
2946 C  CE1 . HIS B  101 ? 0.3301 0.4253 0.6496 -0.0038 0.0766  -0.1293 101 HIS B CE1 
2947 N  NE2 . HIS B  101 ? 0.5051 0.2293 0.5899 0.1575  0.0245  -0.0723 101 HIS B NE2 
2948 N  N   . GLY B  102 ? 0.1490 0.1141 0.1750 0.0024  0.0272  0.0049  102 GLY B N   
2949 C  CA  . GLY B  102 ? 0.1304 0.1071 0.1602 0.0029  0.0241  0.0042  102 GLY B CA  
2950 C  C   . GLY B  102 ? 0.1159 0.1096 0.1432 0.0019  0.0038  0.0006  102 GLY B C   
2951 O  O   . GLY B  102 ? 0.1382 0.1051 0.1550 0.0006  0.0127  0.0135  102 GLY B O   
2952 N  N   . SER B  103 ? 0.1146 0.1198 0.1308 0.0035  0.0223  0.0105  103 SER B N   
2953 C  CA  . SER B  103 ? 0.1082 0.1089 0.1435 -0.0038 0.0190  0.0040  103 SER B CA  
2954 C  C   . SER B  103 ? 0.1036 0.1119 0.1420 0.0039  0.0013  0.0179  103 SER B C   
2955 O  O   . SER B  103 ? 0.1112 0.1518 0.1785 -0.0111 0.0170  -0.0055 103 SER B O   
2956 C  CB  . SER B  103 ? 0.1098 0.1230 0.1426 0.0107  0.0093  0.0271  103 SER B CB  
2957 O  OG  . SER B  103 ? 0.1202 0.1088 0.1573 0.0108  0.0078  0.0187  103 SER B OG  
2958 N  N   . GLU B  104 ? 0.1046 0.1021 0.1333 0.0089  0.0002  0.0077  104 GLU B N   
2959 C  CA  . GLU B  104 ? 0.1079 0.0885 0.1500 0.0083  -0.0133 0.0102  104 GLU B CA  
2960 C  C   . GLU B  104 ? 0.0889 0.0912 0.1347 -0.0059 -0.0128 0.0098  104 GLU B C   
2961 O  O   . GLU B  104 ? 0.0951 0.1044 0.1582 -0.0008 -0.0062 0.0092  104 GLU B O   
2962 C  CB  . GLU B  104 ? 0.1247 0.1091 0.1249 0.0236  -0.0130 0.0071  104 GLU B CB  
2963 C  CG  . GLU B  104 ? 0.1313 0.0895 0.1389 0.0004  -0.0063 0.0212  104 GLU B CG  
2964 C  CD  . GLU B  104 ? 0.1052 0.1113 0.1107 -0.0020 0.0138  0.0168  104 GLU B CD  
2965 O  OE1 . GLU B  104 ? 0.1095 0.1084 0.1444 -0.0025 0.0136  -0.0008 104 GLU B OE1 
2966 O  OE2 . GLU B  104 ? 0.1138 0.1019 0.1716 -0.0003 0.0171  0.0133  104 GLU B OE2 
2967 N  N   . HIS B  105 ? 0.1115 0.1109 0.1337 0.0067  0.0059  0.0316  105 HIS B N   
2968 C  CA  . HIS B  105 ? 0.1131 0.0862 0.1507 0.0044  0.0000  0.0271  105 HIS B CA  
2969 C  C   . HIS B  105 ? 0.1062 0.1095 0.1179 0.0003  -0.0033 0.0082  105 HIS B C   
2970 O  O   . HIS B  105 ? 0.1284 0.1119 0.1342 0.0089  -0.0091 0.0027  105 HIS B O   
2971 C  CB  . HIS B  105 ? 0.1098 0.1138 0.1384 0.0109  0.0048  0.0250  105 HIS B CB  
2972 C  CG  . HIS B  105 ? 0.1089 0.1026 0.1382 0.0066  -0.0009 0.0230  105 HIS B CG  
2973 N  ND1 . HIS B  105 ? 0.1010 0.1302 0.1353 0.0065  -0.0105 0.0158  105 HIS B ND1 
2974 C  CD2 . HIS B  105 ? 0.1105 0.1089 0.1356 -0.0051 0.0179  0.0120  105 HIS B CD2 
2975 C  CE1 . HIS B  105 ? 0.1127 0.1486 0.1326 0.0000  -0.0100 -0.0046 105 HIS B CE1 
2976 N  NE2 . HIS B  105 ? 0.1150 0.1238 0.1342 0.0042  0.0008  0.0018  105 HIS B NE2 
2977 N  N   . THR B  106 ? 0.1071 0.1133 0.1472 0.0127  -0.0193 0.0241  106 THR B N   
2978 C  CA  . THR B  106 ? 0.1165 0.1157 0.1593 0.0153  -0.0022 0.0125  106 THR B CA  
2979 C  C   . THR B  106 ? 0.1172 0.1147 0.1748 0.0076  -0.0119 0.0118  106 THR B C   
2980 O  O   . THR B  106 ? 0.1341 0.1157 0.1585 0.0107  -0.0133 0.0201  106 THR B O   
2981 C  CB  . THR B  106 ? 0.1174 0.1319 0.1669 0.0092  -0.0058 -0.0044 106 THR B CB  
2982 O  OG1 . THR B  106 ? 0.1394 0.1301 0.1852 0.0260  -0.0187 -0.0008 106 THR B OG1 
2983 C  CG2 . THR B  106 ? 0.1653 0.1436 0.1876 -0.0055 0.0292  0.0151  106 THR B CG2 
2984 N  N   . VAL B  107 ? 0.1403 0.1048 0.1844 0.0124  -0.0212 0.0219  107 VAL B N   
2985 C  CA  . VAL B  107 ? 0.1516 0.1487 0.1970 0.0055  -0.0407 0.0466  107 VAL B CA  
2986 C  C   . VAL B  107 ? 0.1326 0.1549 0.1852 -0.0100 -0.0319 0.0081  107 VAL B C   
2987 O  O   . VAL B  107 ? 0.1811 0.1350 0.2432 0.0289  -0.0499 0.0247  107 VAL B O   
2988 C  CB  . VAL B  107 ? 0.1449 0.1116 0.2788 0.0013  -0.0355 0.0478  107 VAL B CB  
2989 C  CG1 . VAL B  107 ? 0.1975 0.1884 0.3070 -0.0060 -0.0223 0.1028  107 VAL B CG1 
2990 C  CG2 . VAL B  107 ? 0.1200 0.1533 0.2836 -0.0109 -0.0307 0.0474  107 VAL B CG2 
2991 N  N   . SER B  108 ? 0.1778 0.1310 0.2136 0.0079  -0.0365 0.0436  108 SER B N   
2992 C  CA  . SER B  108 ? 0.1817 0.1346 0.2302 0.0643  -0.0399 0.0179  108 SER B CA  
2993 C  C   . SER B  108 ? 0.1670 0.1877 0.2344 0.0497  -0.0420 -0.0058 108 SER B C   
2994 O  O   . SER B  108 ? 0.1687 0.1668 0.2736 0.0392  -0.0433 -0.0138 108 SER B O   
2995 C  CB  . SER B  108 ? 0.2463 0.1430 0.2885 0.0253  -0.0447 0.0530  108 SER B CB  
2996 O  OG  . SER B  108 ? 0.2339 0.1973 0.3083 0.0122  -0.0515 0.0945  108 SER B OG  
2997 N  N   . GLY B  109 ? 0.1481 0.1748 0.2117 0.0128  -0.0330 0.0144  109 GLY B N   
2998 C  CA  . GLY B  109 ? 0.1402 0.1892 0.2249 0.0455  -0.0238 0.0254  109 GLY B CA  
2999 C  C   . GLY B  109 ? 0.1566 0.2528 0.2233 0.0527  0.0086  0.0265  109 GLY B C   
3000 O  O   . GLY B  109 ? 0.2446 0.3418 0.2447 0.0570  0.0033  0.0241  109 GLY B O   
3001 N  N   . GLN B  110 ? 0.1825 0.1645 0.2190 0.0873  -0.0271 -0.0237 110 GLN B N   
3002 C  CA  . GLN B  110 ? 0.1836 0.1757 0.2320 0.0596  -0.0440 -0.0234 110 GLN B CA  
3003 C  C   . GLN B  110 ? 0.1583 0.1753 0.1796 0.0378  -0.0125 -0.0103 110 GLN B C   
3004 O  O   . GLN B  110 ? 0.1488 0.1342 0.1846 0.0075  -0.0044 0.0087  110 GLN B O   
3005 C  CB  . GLN B  110 ? 0.2174 0.1837 0.2837 0.0291  -0.0629 0.0207  110 GLN B CB  
3006 C  CG  . GLN B  110 ? 0.2489 0.1576 0.3518 0.0312  -0.0139 -0.0033 110 GLN B CG  
3007 C  CD  . GLN B  110 ? 0.2539 0.3009 0.3639 -0.0063 0.0200  0.0366  110 GLN B CD  
3008 O  OE1 . GLN B  110 ? 0.3914 0.3884 0.4051 0.0288  0.0158  -0.0474 110 GLN B OE1 
3009 N  NE2 . GLN B  110 ? 0.2639 0.4117 0.5015 0.0662  -0.0398 -0.0250 110 GLN B NE2 
3010 N  N   . HIS B  111 ? 0.1210 0.1852 0.2097 0.0322  0.0085  0.0005  111 HIS B N   
3011 C  CA  . HIS B  111 ? 0.1312 0.1414 0.2087 -0.0064 0.0087  0.0300  111 HIS B CA  
3012 C  C   . HIS B  111 ? 0.1333 0.1430 0.1891 0.0286  0.0083  -0.0119 111 HIS B C   
3013 O  O   . HIS B  111 ? 0.1534 0.2033 0.3410 0.0662  -0.0332 -0.0842 111 HIS B O   
3014 C  CB  . HIS B  111 ? 0.1832 0.1562 0.2290 -0.0153 0.0359  0.0103  111 HIS B CB  
3015 C  CG  . HIS B  111 ? 0.1434 0.1307 0.2019 0.0027  0.0375  0.0158  111 HIS B CG  
3016 N  ND1 . HIS B  111 ? 0.1748 0.1840 0.2091 0.0390  0.0273  -0.0152 111 HIS B ND1 
3017 C  CD2 . HIS B  111 ? 0.1465 0.1576 0.2702 -0.0216 0.0040  -0.0107 111 HIS B CD2 
3018 C  CE1 . HIS B  111 ? 0.1814 0.1705 0.2169 0.0089  0.0316  -0.0003 111 HIS B CE1 
3019 N  NE2 . HIS B  111 ? 0.2081 0.2027 0.3017 0.0046  0.0772  -0.0348 111 HIS B NE2 
3020 N  N   . PHE B  112 ? 0.1222 0.1192 0.1521 0.0223  0.0077  0.0280  112 PHE B N   
3021 C  CA  . PHE B  112 ? 0.1204 0.1347 0.1392 0.0201  -0.0029 0.0095  112 PHE B CA  
3022 C  C   . PHE B  112 ? 0.1134 0.1035 0.1487 0.0100  0.0239  0.0027  112 PHE B C   
3023 O  O   . PHE B  112 ? 0.1320 0.1212 0.1640 0.0025  0.0218  0.0033  112 PHE B O   
3024 C  CB  . PHE B  112 ? 0.1265 0.1461 0.1692 0.0104  0.0238  0.0394  112 PHE B CB  
3025 C  CG  . PHE B  112 ? 0.1436 0.1937 0.1860 0.0402  0.0291  0.0249  112 PHE B CG  
3026 C  CD1 . PHE B  112 ? 0.2344 0.2700 0.1817 0.0751  0.0353  0.0525  112 PHE B CD1 
3027 C  CD2 . PHE B  112 ? 0.2393 0.1649 0.2920 -0.0017 0.0563  0.0658  112 PHE B CD2 
3028 C  CE1 . PHE B  112 ? 0.2830 0.3564 0.2273 0.1212  0.0447  0.1164  112 PHE B CE1 
3029 C  CE2 . PHE B  112 ? 0.2922 0.2213 0.3263 0.0554  0.0951  0.0986  112 PHE B CE2 
3030 C  CZ  . PHE B  112 ? 0.3602 0.3213 0.2682 0.0789  0.0934  0.1577  112 PHE B CZ  
3031 N  N   . ALA B  113 ? 0.1238 0.1021 0.1345 0.0137  0.0151  0.0012  113 ALA B N   
3032 C  CA  . ALA B  113 ? 0.1340 0.1209 0.1468 0.0136  0.0227  0.0052  113 ALA B CA  
3033 C  C   . ALA B  113 ? 0.1121 0.1057 0.1333 -0.0083 0.0279  0.0018  113 ALA B C   
3034 O  O   . ALA B  113 ? 0.1372 0.1091 0.1418 0.0000  0.0376  -0.0001 113 ALA B O   
3035 C  CB  . ALA B  113 ? 0.1623 0.1271 0.1804 0.0093  0.0076  -0.0171 113 ALA B CB  
3036 N  N   . ALA B  114 ? 0.1213 0.0839 0.1328 0.0051  0.0222  -0.0032 114 ALA B N   
3037 C  CA  . ALA B  114 ? 0.1125 0.0908 0.1155 0.0062  0.0211  -0.0035 114 ALA B CA  
3038 C  C   . ALA B  114 ? 0.0939 0.1009 0.1041 -0.0108 0.0142  0.0098  114 ALA B C   
3039 O  O   . ALA B  114 ? 0.0967 0.1031 0.1179 -0.0021 0.0094  0.0159  114 ALA B O   
3040 C  CB  . ALA B  114 ? 0.1312 0.1064 0.1191 0.0032  0.0013  0.0071  114 ALA B CB  
3041 N  N   . GLU B  115 ? 0.1021 0.0996 0.1133 0.0068  0.0187  -0.0030 115 GLU B N   
3042 C  CA  . GLU B  115 ? 0.1037 0.1010 0.1027 0.0117  0.0144  0.0084  115 GLU B CA  
3043 C  C   . GLU B  115 ? 0.1026 0.0960 0.0969 0.0077  0.0096  0.0119  115 GLU B C   
3044 O  O   . GLU B  115 ? 0.1025 0.1076 0.1349 0.0129  0.0288  0.0370  115 GLU B O   
3045 C  CB  . GLU B  115 ? 0.1032 0.1136 0.1071 -0.0013 0.0069  -0.0029 115 GLU B CB  
3046 C  CG  . GLU B  115 ? 0.1010 0.1116 0.1121 -0.0074 0.0006  -0.0013 115 GLU B CG  
3047 C  CD  . GLU B  115 ? 0.1079 0.1023 0.1190 -0.0091 0.0053  0.0139  115 GLU B CD  
3048 O  OE1 . GLU B  115 ? 0.1046 0.1235 0.1448 0.0000  0.0043  0.0029  115 GLU B OE1 
3049 O  OE2 . GLU B  115 ? 0.1222 0.1231 0.1087 0.0030  -0.0063 0.0145  115 GLU B OE2 
3050 N  N   . LEU B  116 ? 0.0898 0.0861 0.1064 0.0025  0.0073  0.0084  116 LEU B N   
3051 C  CA  . LEU B  116 ? 0.0851 0.0937 0.1077 0.0100  0.0006  -0.0011 116 LEU B CA  
3052 C  C   . LEU B  116 ? 0.0854 0.1010 0.0969 0.0107  0.0049  0.0171  116 LEU B C   
3053 O  O   . LEU B  116 ? 0.0949 0.0917 0.1075 0.0027  0.0081  0.0170  116 LEU B O   
3054 C  CB  . LEU B  116 ? 0.1024 0.0850 0.1415 0.0071  -0.0076 0.0009  116 LEU B CB  
3055 C  CG  . LEU B  116 ? 0.0883 0.1095 0.1412 0.0029  -0.0222 0.0238  116 LEU B CG  
3056 C  CD1 . LEU B  116 ? 0.1157 0.1399 0.1583 0.0171  -0.0099 0.0253  116 LEU B CD1 
3057 C  CD2 . LEU B  116 ? 0.1093 0.1347 0.1753 -0.0095 -0.0022 0.0010  116 LEU B CD2 
3058 N  N   . HIS B  117 ? 0.0768 0.0856 0.1070 0.0063  0.0100  0.0075  117 HIS B N   
3059 C  CA  . HIS B  117 ? 0.0702 0.0937 0.1098 0.0037  0.0030  0.0016  117 HIS B CA  
3060 C  C   . HIS B  117 ? 0.0854 0.0963 0.0908 0.0092  -0.0035 0.0089  117 HIS B C   
3061 O  O   . HIS B  117 ? 0.0957 0.1183 0.1018 0.0098  0.0013  0.0163  117 HIS B O   
3062 C  CB  . HIS B  117 ? 0.0908 0.0908 0.1158 0.0004  -0.0010 0.0174  117 HIS B CB  
3063 C  CG  . HIS B  117 ? 0.0860 0.0851 0.1045 -0.0012 0.0044  0.0053  117 HIS B CG  
3064 N  ND1 . HIS B  117 ? 0.0870 0.0773 0.1064 -0.0013 0.0040  0.0117  117 HIS B ND1 
3065 C  CD2 . HIS B  117 ? 0.0978 0.0853 0.1098 0.0033  -0.0004 0.0053  117 HIS B CD2 
3066 C  CE1 . HIS B  117 ? 0.1116 0.0803 0.1086 0.0115  -0.0067 0.0065  117 HIS B CE1 
3067 N  NE2 . HIS B  117 ? 0.0946 0.0849 0.1226 -0.0041 -0.0026 0.0179  117 HIS B NE2 
3068 N  N   . ILE B  118 ? 0.0855 0.1033 0.0942 0.0072  0.0116  0.0059  118 ILE B N   
3069 C  CA  . ILE B  118 ? 0.0942 0.1031 0.1204 0.0158  0.0033  0.0046  118 ILE B CA  
3070 C  C   . ILE B  118 ? 0.0954 0.1087 0.1098 0.0229  0.0011  0.0075  118 ILE B C   
3071 O  O   . ILE B  118 ? 0.1129 0.1106 0.1079 0.0218  0.0077  0.0066  118 ILE B O   
3072 C  CB  . ILE B  118 ? 0.0845 0.1182 0.1326 0.0013  0.0047  0.0094  118 ILE B CB  
3073 C  CG1 . ILE B  118 ? 0.1200 0.1116 0.1337 -0.0122 0.0044  0.0104  118 ILE B CG1 
3074 C  CG2 . ILE B  118 ? 0.0987 0.1744 0.1332 0.0227  -0.0027 0.0353  118 ILE B CG2 
3075 C  CD1 . ILE B  118 ? 0.1321 0.1511 0.1542 -0.0440 0.0144  0.0080  118 ILE B CD1 
3076 N  N   . VAL B  119 ? 0.0967 0.1070 0.1100 0.0216  -0.0020 -0.0089 119 VAL B N   
3077 C  CA  . VAL B  119 ? 0.1019 0.0983 0.1163 0.0116  0.0013  0.0029  119 VAL B CA  
3078 C  C   . VAL B  119 ? 0.1079 0.1109 0.1157 0.0187  -0.0055 0.0159  119 VAL B C   
3079 O  O   . VAL B  119 ? 0.1120 0.1305 0.1330 0.0285  -0.0065 0.0137  119 VAL B O   
3080 C  CB  . VAL B  119 ? 0.1119 0.1139 0.1192 -0.0002 -0.0060 0.0079  119 VAL B CB  
3081 C  CG1 . VAL B  119 ? 0.1606 0.1230 0.1484 -0.0031 -0.0026 -0.0089 119 VAL B CG1 
3082 C  CG2 . VAL B  119 ? 0.1128 0.1356 0.1177 0.0150  0.0129  0.0040  119 VAL B CG2 
3083 N  N   . HIS B  120 ? 0.1155 0.1069 0.1247 0.0240  0.0096  0.0027  120 HIS B N   
3084 C  CA  . HIS B  120 ? 0.1216 0.1339 0.1382 0.0241  0.0194  -0.0060 120 HIS B CA  
3085 C  C   . HIS B  120 ? 0.1207 0.1279 0.1552 0.0289  0.0082  0.0117  120 HIS B C   
3086 O  O   . HIS B  120 ? 0.1387 0.1288 0.1439 0.0292  0.0013  -0.0111 120 HIS B O   
3087 C  CB  . HIS B  120 ? 0.1134 0.1358 0.1259 0.0024  0.0044  0.0027  120 HIS B CB  
3088 C  CG  . HIS B  120 ? 0.1243 0.1164 0.1177 0.0219  0.0004  0.0178  120 HIS B CG  
3089 N  ND1 . HIS B  120 ? 0.1235 0.1267 0.1306 0.0232  0.0145  0.0020  120 HIS B ND1 
3090 C  CD2 . HIS B  120 ? 0.1374 0.1319 0.1442 -0.0016 0.0064  0.0079  120 HIS B CD2 
3091 C  CE1 . HIS B  120 ? 0.1357 0.1378 0.1421 0.0012  0.0207  0.0161  120 HIS B CE1 
3092 N  NE2 . HIS B  120 ? 0.1290 0.1310 0.1410 0.0020  -0.0027 0.0109  120 HIS B NE2 
3093 N  N   . TYR B  121 ? 0.1342 0.1437 0.1676 0.0398  0.0134  -0.0234 121 TYR B N   
3094 C  CA  . TYR B  121 ? 0.1499 0.1545 0.1894 0.0305  0.0205  -0.0245 121 TYR B CA  
3095 C  C   . TYR B  121 ? 0.1693 0.1362 0.1829 0.0280  0.0063  -0.0181 121 TYR B C   
3096 O  O   . TYR B  121 ? 0.1662 0.1585 0.1662 0.0433  0.0073  -0.0313 121 TYR B O   
3097 C  CB  . TYR B  121 ? 0.1700 0.1486 0.2160 0.0535  0.0216  0.0159  121 TYR B CB  
3098 C  CG  . TYR B  121 ? 0.1878 0.1464 0.1892 0.0467  0.0038  0.0004  121 TYR B CG  
3099 C  CD1 . TYR B  121 ? 0.1903 0.1965 0.1838 0.0314  0.0039  0.0397  121 TYR B CD1 
3100 C  CD2 . TYR B  121 ? 0.2012 0.1878 0.2270 0.0688  0.0314  -0.0016 121 TYR B CD2 
3101 C  CE1 . TYR B  121 ? 0.1901 0.2359 0.2278 0.0466  0.0068  0.0567  121 TYR B CE1 
3102 C  CE2 . TYR B  121 ? 0.2327 0.2404 0.2791 0.1100  0.0218  0.0243  121 TYR B CE2 
3103 C  CZ  . TYR B  121 ? 0.2332 0.2222 0.3172 0.0867  0.0064  0.0316  121 TYR B CZ  
3104 O  OH  . TYR B  121 ? 0.2361 0.3935 0.4292 0.1035  -0.0110 0.1544  121 TYR B OH  
3105 N  N   . ASN B  122 ? 0.1740 0.1651 0.1732 0.0488  0.0154  -0.0396 122 ASN B N   
3106 C  CA  . ASN B  122 ? 0.1799 0.1882 0.1869 0.0600  0.0036  -0.0461 122 ASN B CA  
3107 C  C   . ASN B  122 ? 0.1674 0.2004 0.2151 0.0529  0.0200  -0.0643 122 ASN B C   
3108 O  O   . ASN B  122 ? 0.1981 0.1895 0.2204 0.0563  0.0396  -0.0158 122 ASN B O   
3109 C  CB  . ASN B  122 ? 0.1983 0.1856 0.1842 0.0413  -0.0008 -0.0324 122 ASN B CB  
3110 C  CG  . ASN B  122 ? 0.2992 0.2272 0.2259 0.0367  -0.0294 -0.0548 122 ASN B CG  
3111 O  OD1 . ASN B  122 ? 0.2889 0.2627 0.1864 0.0523  0.0342  -0.0491 122 ASN B OD1 
3112 N  ND2 . ASN B  122 ? 0.4651 0.2597 0.1985 0.0383  -0.0610 -0.0205 122 ASN B ND2 
3113 N  N   . SER B  123 ? 0.1568 0.2345 0.2342 0.0538  0.0201  -0.0417 123 SER B N   
3114 C  CA  . SER B  123 ? 0.1844 0.2768 0.2423 0.0857  0.0399  -0.0331 123 SER B CA  
3115 C  C   . SER B  123 ? 0.2856 0.2728 0.2872 0.1324  0.0740  0.0061  123 SER B C   
3116 O  O   . SER B  123 ? 0.2440 0.2566 0.2899 0.1080  0.0556  -0.0204 123 SER B O   
3117 C  CB  . SER B  123 ? 0.2119 0.2308 0.2275 0.0453  -0.0050 0.0019  123 SER B CB  
3118 O  OG  . SER B  123 ? 0.1903 0.2518 0.2967 0.0400  0.0369  -0.0004 123 SER B OG  
3119 N  N   . ASP B  124 ? 0.2088 0.2445 0.2513 0.0628  0.0810  -0.0186 124 ASP B N   
3120 C  CA  . ASP B  124 ? 0.2755 0.2551 0.2469 0.0464  0.0748  0.0140  124 ASP B CA  
3121 C  C   . ASP B  124 ? 0.2791 0.3188 0.2827 0.0596  0.0729  -0.1061 124 ASP B C   
3122 O  O   . ASP B  124 ? 0.3036 0.2805 0.2820 0.0873  0.0648  -0.0662 124 ASP B O   
3123 C  CB  . ASP B  124 ? 0.3010 0.3425 0.2420 0.1327  0.1145  0.0000  124 ASP B CB  
3124 C  CG  . ASP B  124 ? 0.3551 0.3648 0.2024 0.0301  0.0238  -0.0093 124 ASP B CG  
3125 O  OD1 . ASP B  124 ? 0.2924 0.3964 0.2858 0.0524  0.0869  -0.0485 124 ASP B OD1 
3126 O  OD2 . ASP B  124 ? 0.4193 0.3319 0.2692 0.1139  0.1547  0.0053  124 ASP B OD2 
3127 N  N   . LEU B  125 ? 0.2675 0.2368 0.2334 0.0572  0.0445  -0.0508 125 LEU B N   
3128 C  CA  . LEU B  125 ? 0.3327 0.2177 0.2175 0.0592  0.0540  -0.0411 125 LEU B CA  
3129 C  C   . LEU B  125 ? 0.3141 0.2289 0.2365 0.0083  0.0238  -0.0165 125 LEU B C   
3130 O  O   . LEU B  125 ? 0.4359 0.2147 0.2904 0.0759  0.0614  -0.0723 125 LEU B O   
3131 C  CB  . LEU B  125 ? 0.3554 0.2055 0.2212 0.0424  0.0256  -0.0120 125 LEU B CB  
3132 C  CG  . LEU B  125 ? 0.3652 0.2649 0.2417 0.0250  0.0572  0.0284  125 LEU B CG  
3133 C  CD1 . LEU B  125 ? 0.3532 0.2630 0.2471 0.0150  -0.0138 -0.0559 125 LEU B CD1 
3134 C  CD2 . LEU B  125 ? 0.4655 0.3001 0.2465 -0.0057 0.1265  -0.0153 125 LEU B CD2 
3135 N  N   . TYR B  126 ? 0.2934 0.2250 0.2318 0.0713  0.0378  -0.0392 126 TYR B N   
3136 C  CA  . TYR B  126 ? 0.3157 0.2332 0.2219 0.1145  0.0429  -0.0197 126 TYR B CA  
3137 C  C   . TYR B  126 ? 0.2990 0.2396 0.2503 0.0877  0.0263  -0.0008 126 TYR B C   
3138 O  O   . TYR B  126 ? 0.2789 0.2801 0.2956 0.1184  0.0223  -0.0113 126 TYR B O   
3139 C  CB  . TYR B  126 ? 0.3001 0.2805 0.2204 0.0540  0.0421  -0.0163 126 TYR B CB  
3140 C  CG  . TYR B  126 ? 0.2866 0.2029 0.2465 0.0639  0.0435  -0.0413 126 TYR B CG  
3141 C  CD1 . TYR B  126 ? 0.2967 0.2681 0.3340 0.0242  -0.0151 -0.0780 126 TYR B CD1 
3142 C  CD2 . TYR B  126 ? 0.2629 0.2533 0.2561 0.0564  0.0294  0.0289  126 TYR B CD2 
3143 C  CE1 . TYR B  126 ? 0.3412 0.2270 0.2505 0.0358  0.0117  -0.0593 126 TYR B CE1 
3144 C  CE2 . TYR B  126 ? 0.2986 0.2146 0.2438 0.0585  0.0573  -0.0306 126 TYR B CE2 
3145 C  CZ  . TYR B  126 ? 0.4276 0.2558 0.2648 0.0615  0.0105  -0.0673 126 TYR B CZ  
3146 O  OH  . TYR B  126 ? 0.4244 0.3316 0.3062 -0.0096 0.0106  -0.0889 126 TYR B OH  
3147 N  N   . PRO B  127 ? 0.3797 0.2569 0.2356 0.1088  0.0118  -0.0249 127 PRO B N   
3148 C  CA  . PRO B  127 ? 0.3606 0.3904 0.3333 0.1520  -0.0081 0.0682  127 PRO B CA  
3149 C  C   . PRO B  127 ? 0.3491 0.3402 0.3292 0.1368  -0.0712 0.0103  127 PRO B C   
3150 O  O   . PRO B  127 ? 0.3544 0.4332 0.3071 0.0763  -0.0376 0.1044  127 PRO B O   
3151 C  CB  . PRO B  127 ? 0.4161 0.3420 0.5635 0.1679  -0.0167 0.0366  127 PRO B CB  
3152 C  CG  . PRO B  127 ? 0.4529 0.2093 0.3619 0.1018  0.0704  0.0722  127 PRO B CG  
3153 C  CD  . PRO B  127 ? 0.3968 0.2273 0.3107 0.0813  0.0405  0.0022  127 PRO B CD  
3154 N  N   . ASP B  128 ? 0.3037 0.2701 0.2302 0.0577  -0.0201 0.0348  128 ASP B N   
3155 C  CA  . ASP B  128 ? 0.2470 0.3256 0.2080 0.0455  -0.0109 0.0398  128 ASP B CA  
3156 C  C   . ASP B  128 ? 0.2730 0.2131 0.2284 0.0268  -0.0284 -0.0105 128 ASP B C   
3157 O  O   . ASP B  128 ? 0.2544 0.2105 0.2318 0.0403  -0.0233 -0.0125 128 ASP B O   
3158 C  CB  . ASP B  128 ? 0.3400 0.1955 0.2948 0.0241  -0.0862 0.0462  128 ASP B CB  
3159 C  CG  . ASP B  128 ? 0.3207 0.2132 0.3813 0.0679  -0.0348 -0.0697 128 ASP B CG  
3160 O  OD1 . ASP B  128 ? 0.3832 0.3305 0.4280 0.0886  -0.0732 -0.1100 128 ASP B OD1 
3161 O  OD2 . ASP B  128 ? 0.3342 0.2605 0.3319 0.0466  0.0081  -0.0059 128 ASP B OD2 
3162 N  N   . ALA B  129 ? 0.2760 0.1881 0.2678 0.0084  0.0098  0.0013  129 ALA B N   
3163 C  CA  . ALA B  129 ? 0.2463 0.1753 0.2440 0.0195  0.0341  -0.0523 129 ALA B CA  
3164 C  C   . ALA B  129 ? 0.2392 0.1710 0.2117 0.0066  -0.0055 -0.0377 129 ALA B C   
3165 O  O   . ALA B  129 ? 0.2888 0.1617 0.2252 0.0310  -0.0008 -0.0248 129 ALA B O   
3166 C  CB  . ALA B  129 ? 0.3355 0.1882 0.2762 -0.0794 0.0703  -0.0541 129 ALA B CB  
3167 N  N   A SER B  130 ? 0.2904 0.1461 0.2855 0.0120  0.0154  -0.0200 130 SER B N   
3168 N  N   B SER B  130 ? 0.2706 0.1726 0.2473 -0.0095 -0.0176 -0.0142 130 SER B N   
3169 C  CA  A SER B  130 ? 0.3014 0.2283 0.2367 0.0003  0.0211  0.0227  130 SER B CA  
3170 C  CA  B SER B  130 ? 0.2365 0.2236 0.2268 0.0121  -0.0529 0.0359  130 SER B CA  
3171 C  C   A SER B  130 ? 0.2694 0.2028 0.2919 0.0287  -0.0100 -0.0330 130 SER B C   
3172 C  C   B SER B  130 ? 0.2433 0.1496 0.2582 0.0107  -0.0136 -0.0053 130 SER B C   
3173 O  O   A SER B  130 ? 0.3262 0.2472 0.2259 -0.0135 -0.0359 -0.0219 130 SER B O   
3174 O  O   B SER B  130 ? 0.2737 0.1125 0.2597 0.0279  -0.0205 0.0076  130 SER B O   
3175 C  CB  A SER B  130 ? 0.3677 0.1986 0.2980 0.0187  0.0767  0.0501  130 SER B CB  
3176 C  CB  B SER B  130 ? 0.2434 0.2396 0.2150 0.0113  -0.0564 0.0315  130 SER B CB  
3177 O  OG  A SER B  130 ? 0.3668 0.3581 0.3379 -0.0631 0.0447  0.0130  130 SER B OG  
3178 O  OG  B SER B  130 ? 0.2989 0.1908 0.3732 -0.0251 -0.0480 0.0594  130 SER B OG  
3179 N  N   . THR B  131 ? 0.3036 0.1482 0.3262 0.0208  0.0004  -0.0324 131 THR B N   
3180 C  CA  . THR B  131 ? 0.2788 0.2172 0.2564 0.0106  -0.0107 -0.0281 131 THR B CA  
3181 C  C   . THR B  131 ? 0.2495 0.2386 0.3168 0.0159  -0.0332 -0.0653 131 THR B C   
3182 O  O   . THR B  131 ? 0.2726 0.2557 0.2958 -0.0013 -0.0366 -0.0699 131 THR B O   
3183 C  CB  . THR B  131 ? 0.3271 0.2587 0.3263 0.1036  -0.0501 -0.0514 131 THR B CB  
3184 O  OG1 . THR B  131 ? 0.3856 0.2329 0.3700 0.0954  -0.0608 -0.0769 131 THR B OG1 
3185 C  CG2 . THR B  131 ? 0.3206 0.3198 0.3586 0.0510  -0.0771 -0.1103 131 THR B CG2 
3186 N  N   . ALA B  132 ? 0.2084 0.1891 0.2748 0.0392  0.0025  -0.0594 132 ALA B N   
3187 C  CA  . ALA B  132 ? 0.2389 0.2045 0.2369 0.0485  0.0122  -0.0314 132 ALA B CA  
3188 C  C   . ALA B  132 ? 0.2386 0.1875 0.2106 0.0343  0.0272  -0.0258 132 ALA B C   
3189 O  O   . ALA B  132 ? 0.2338 0.1955 0.2063 0.0332  0.0032  -0.0375 132 ALA B O   
3190 C  CB  . ALA B  132 ? 0.2048 0.1866 0.2452 0.0553  0.0036  -0.0331 132 ALA B CB  
3191 N  N   . SER B  133 ? 0.2141 0.1923 0.2096 0.0245  0.0296  -0.0485 133 SER B N   
3192 C  CA  . SER B  133 ? 0.1981 0.1640 0.2258 0.0091  0.0048  -0.0335 133 SER B CA  
3193 C  C   . SER B  133 ? 0.2177 0.1411 0.2471 0.0108  0.0192  0.0133  133 SER B C   
3194 O  O   . SER B  133 ? 0.2220 0.1976 0.2645 0.0362  0.0142  0.0121  133 SER B O   
3195 C  CB  . SER B  133 ? 0.2467 0.1917 0.2494 -0.0185 0.0486  -0.0077 133 SER B CB  
3196 O  OG  . SER B  133 ? 0.2482 0.1804 0.2595 -0.0089 0.0019  0.0172  133 SER B OG  
3197 N  N   . ASN B  134 ? 0.3152 0.1700 0.2678 0.0223  -0.0612 -0.0190 134 ASN B N   
3198 C  CA  . ASN B  134 ? 0.3206 0.1750 0.3032 -0.0331 -0.0373 -0.0145 134 ASN B CA  
3199 C  C   . ASN B  134 ? 0.3120 0.2161 0.2625 -0.0100 -0.0005 -0.0827 134 ASN B C   
3200 O  O   . ASN B  134 ? 0.3736 0.3167 0.3171 0.0033  -0.0740 -0.0996 134 ASN B O   
3201 C  CB  . ASN B  134 ? 0.3361 0.2432 0.6189 -0.0351 0.0104  -0.0324 134 ASN B CB  
3202 C  CG  . ASN B  134 ? 0.4974 0.1615 0.7610 0.0075  -0.1283 0.0784  134 ASN B CG  
3203 O  OD1 . ASN B  134 ? 0.5341 0.2364 0.6657 -0.0585 0.0484  -0.0842 134 ASN B OD1 
3204 N  ND2 . ASN B  134 ? 0.6357 0.2120 0.5545 -0.0223 0.1763  -0.0910 134 ASN B ND2 
3205 N  N   . LYS B  135 ? 0.2735 0.2264 0.2406 0.0378  0.0223  -0.0523 135 LYS B N   
3206 C  CA  . LYS B  135 ? 0.3573 0.2890 0.2433 -0.0230 0.0283  -0.1059 135 LYS B CA  
3207 C  C   . LYS B  135 ? 0.4158 0.3382 0.1996 -0.0179 0.0031  -0.0972 135 LYS B C   
3208 O  O   . LYS B  135 ? 0.2359 0.2991 0.2252 -0.0527 -0.0098 -0.0417 135 LYS B O   
3209 C  CB  . LYS B  135 ? 0.4005 0.3404 0.3365 0.0057  0.1100  -0.0513 135 LYS B CB  
3210 C  CG  . LYS B  135 ? 0.5784 0.3817 0.3859 0.0581  0.0155  -0.0395 135 LYS B CG  
3211 C  CD  . LYS B  135 ? 0.9151 0.4769 0.7665 -0.1697 -0.2124 -0.2397 135 LYS B CD  
3212 C  CE  . LYS B  135 ? 1.0580 0.9893 0.3817 -0.0326 0.0491  -0.0421 135 LYS B CE  
3213 N  NZ  . LYS B  135 ? 0.3926 0.4550 0.9568 0.1225  -0.3260 -0.3385 135 LYS B NZ  
3214 N  N   . SER B  136 ? 0.6750 0.5083 0.2134 -0.2500 -0.0802 -0.0187 136 SER B N   
3215 C  CA  . SER B  136 ? 0.7145 0.4286 0.3701 -0.2287 -0.2394 0.0218  136 SER B CA  
3216 C  C   . SER B  136 ? 0.3797 0.3013 0.2861 0.0274  -0.0901 -0.0310 136 SER B C   
3217 O  O   . SER B  136 ? 0.3294 0.3913 0.1483 -0.0814 -0.0103 0.0110  136 SER B O   
3218 C  CB  . SER B  136 ? 0.9605 0.6718 0.3917 -0.1940 -0.3361 -0.1273 136 SER B CB  
3219 N  N   . GLU B  137 ? 0.4351 0.2599 0.2478 0.0016  -0.0596 0.0141  137 GLU B N   
3220 C  CA  . GLU B  137 ? 0.3350 0.3023 0.2725 0.0406  -0.0359 -0.0351 137 GLU B CA  
3221 C  C   . GLU B  137 ? 0.2740 0.2938 0.2109 -0.0690 -0.0589 0.0111  137 GLU B C   
3222 O  O   . GLU B  137 ? 0.3075 0.3476 0.1972 -0.0996 -0.0265 0.0199  137 GLU B O   
3223 C  CB  . GLU B  137 ? 0.3737 0.6546 0.2357 -0.0021 -0.0429 0.0508  137 GLU B CB  
3224 N  N   . GLY B  138 ? 0.2401 0.2067 0.1507 -0.0414 -0.0044 -0.0111 138 GLY B N   
3225 C  CA  . GLY B  138 ? 0.1690 0.1955 0.1722 0.0135  0.0006  -0.0597 138 GLY B CA  
3226 C  C   . GLY B  138 ? 0.1600 0.1625 0.1634 0.0383  -0.0009 -0.0223 138 GLY B C   
3227 O  O   . GLY B  138 ? 0.1726 0.1860 0.1884 0.0603  0.0031  -0.0489 138 GLY B O   
3228 N  N   . LEU B  139 ? 0.1526 0.1226 0.1529 0.0201  0.0065  -0.0146 139 LEU B N   
3229 C  CA  . LEU B  139 ? 0.1469 0.1237 0.1414 0.0049  0.0120  -0.0094 139 LEU B CA  
3230 C  C   . LEU B  139 ? 0.1300 0.1305 0.1329 0.0302  0.0062  0.0011  139 LEU B C   
3231 O  O   . LEU B  139 ? 0.1429 0.1416 0.1438 0.0141  -0.0083 -0.0150 139 LEU B O   
3232 C  CB  . LEU B  139 ? 0.1442 0.1356 0.1590 0.0181  0.0175  0.0011  139 LEU B CB  
3233 C  CG  . LEU B  139 ? 0.1590 0.1218 0.1663 0.0244  0.0179  0.0013  139 LEU B CG  
3234 C  CD1 . LEU B  139 ? 0.1814 0.1688 0.2093 0.0231  0.0500  -0.0012 139 LEU B CD1 
3235 C  CD2 . LEU B  139 ? 0.1660 0.1707 0.1788 0.0330  -0.0016 -0.0008 139 LEU B CD2 
3236 N  N   . ALA B  140 ? 0.1403 0.1260 0.1476 0.0263  -0.0027 -0.0241 140 ALA B N   
3237 C  CA  . ALA B  140 ? 0.1451 0.1115 0.1136 0.0234  0.0002  -0.0133 140 ALA B CA  
3238 C  C   . ALA B  140 ? 0.1209 0.1394 0.1229 0.0206  -0.0055 -0.0174 140 ALA B C   
3239 O  O   . ALA B  140 ? 0.1521 0.1380 0.1315 0.0414  -0.0095 0.0013  140 ALA B O   
3240 C  CB  . ALA B  140 ? 0.1703 0.1562 0.1309 0.0290  0.0168  0.0002  140 ALA B CB  
3241 N  N   . VAL B  141 ? 0.1140 0.1097 0.1179 0.0063  0.0029  -0.0008 141 VAL B N   
3242 C  CA  . VAL B  141 ? 0.1172 0.1033 0.0899 0.0053  -0.0027 0.0043  141 VAL B CA  
3243 C  C   . VAL B  141 ? 0.1003 0.1159 0.1064 0.0205  0.0075  0.0049  141 VAL B C   
3244 O  O   . VAL B  141 ? 0.1203 0.1307 0.1121 0.0214  -0.0026 0.0087  141 VAL B O   
3245 C  CB  . VAL B  141 ? 0.1093 0.1300 0.1257 0.0074  0.0000  0.0075  141 VAL B CB  
3246 C  CG1 . VAL B  141 ? 0.1219 0.1826 0.1195 -0.0057 0.0049  0.0058  141 VAL B CG1 
3247 C  CG2 . VAL B  141 ? 0.1351 0.1380 0.1614 -0.0088 -0.0272 0.0357  141 VAL B CG2 
3248 N  N   . LEU B  142 ? 0.0985 0.1091 0.0951 0.0082  0.0020  0.0059  142 LEU B N   
3249 C  CA  . LEU B  142 ? 0.0965 0.1085 0.1113 0.0124  0.0000  -0.0054 142 LEU B CA  
3250 C  C   . LEU B  142 ? 0.1125 0.0850 0.0960 0.0004  -0.0057 0.0059  142 LEU B C   
3251 O  O   . LEU B  142 ? 0.1338 0.1297 0.1079 0.0347  0.0047  0.0159  142 LEU B O   
3252 C  CB  . LEU B  142 ? 0.1089 0.1309 0.1342 0.0095  0.0050  0.0150  142 LEU B CB  
3253 C  CG  . LEU B  142 ? 0.1168 0.1460 0.1320 0.0093  0.0083  0.0179  142 LEU B CG  
3254 C  CD1 . LEU B  142 ? 0.1148 0.1824 0.1984 -0.0290 0.0042  0.0168  142 LEU B CD1 
3255 C  CD2 . LEU B  142 ? 0.1167 0.1974 0.1285 0.0171  0.0051  0.0236  142 LEU B CD2 
3256 N  N   . ALA B  143 ? 0.1059 0.0940 0.1116 0.0062  0.0088  0.0070  143 ALA B N   
3257 C  CA  . ALA B  143 ? 0.1005 0.0890 0.1019 0.0051  0.0038  0.0058  143 ALA B CA  
3258 C  C   . ALA B  143 ? 0.0940 0.0790 0.1110 0.0075  -0.0009 0.0200  143 ALA B C   
3259 O  O   . ALA B  143 ? 0.1194 0.1001 0.1034 -0.0001 0.0042  0.0182  143 ALA B O   
3260 C  CB  . ALA B  143 ? 0.0978 0.1251 0.1273 -0.0027 -0.0122 0.0206  143 ALA B CB  
3261 N  N   . VAL B  144 ? 0.1009 0.0957 0.1055 -0.0013 -0.0004 -0.0006 144 VAL B N   
3262 C  CA  . VAL B  144 ? 0.1100 0.0954 0.0942 -0.0097 0.0091  -0.0037 144 VAL B CA  
3263 C  C   . VAL B  144 ? 0.0958 0.1003 0.1067 -0.0041 0.0067  0.0128  144 VAL B C   
3264 O  O   . VAL B  144 ? 0.1107 0.0969 0.1134 0.0013  0.0152  0.0092  144 VAL B O   
3265 C  CB  . VAL B  144 ? 0.1028 0.0994 0.1188 -0.0075 -0.0013 0.0113  144 VAL B CB  
3266 C  CG1 . VAL B  144 ? 0.1398 0.1059 0.1385 -0.0068 -0.0095 -0.0231 144 VAL B CG1 
3267 C  CG2 . VAL B  144 ? 0.1170 0.1265 0.1236 0.0070  0.0106  0.0079  144 VAL B CG2 
3268 N  N   . LEU B  145 ? 0.1005 0.1005 0.1014 0.0011  0.0064  0.0058  145 LEU B N   
3269 C  CA  . LEU B  145 ? 0.0839 0.1231 0.1140 -0.0013 -0.0010 0.0022  145 LEU B CA  
3270 C  C   . LEU B  145 ? 0.1015 0.0880 0.1173 -0.0001 0.0025  0.0087  145 LEU B C   
3271 O  O   . LEU B  145 ? 0.1206 0.1043 0.1213 -0.0147 0.0065  0.0031  145 LEU B O   
3272 C  CB  . LEU B  145 ? 0.1338 0.1158 0.1356 0.0121  -0.0211 0.0015  145 LEU B CB  
3273 C  CG  . LEU B  145 ? 0.1441 0.1231 0.1489 0.0113  -0.0339 -0.0015 145 LEU B CG  
3274 C  CD1 . LEU B  145 ? 0.1701 0.2109 0.1359 0.0343  -0.0444 0.0154  145 LEU B CD1 
3275 C  CD2 . LEU B  145 ? 0.1599 0.1782 0.2177 -0.0370 -0.0417 -0.0229 145 LEU B CD2 
3276 N  N   . ILE B  146 ? 0.1098 0.1143 0.1115 0.0070  0.0086  -0.0010 146 ILE B N   
3277 C  CA  . ILE B  146 ? 0.1240 0.1041 0.1120 0.0031  0.0018  -0.0044 146 ILE B CA  
3278 C  C   . ILE B  146 ? 0.1165 0.1161 0.1146 -0.0132 0.0055  -0.0017 146 ILE B C   
3279 O  O   . ILE B  146 ? 0.1220 0.1141 0.1430 -0.0009 0.0214  -0.0034 146 ILE B O   
3280 C  CB  . ILE B  146 ? 0.1200 0.1064 0.1163 0.0043  -0.0022 -0.0013 146 ILE B CB  
3281 C  CG1 . ILE B  146 ? 0.1175 0.1242 0.1346 0.0166  0.0114  0.0075  146 ILE B CG1 
3282 C  CG2 . ILE B  146 ? 0.1485 0.1388 0.1130 -0.0001 -0.0104 -0.0106 146 ILE B CG2 
3283 C  CD1 . ILE B  146 ? 0.1384 0.1158 0.1571 0.0184  -0.0124 0.0089  146 ILE B CD1 
3284 N  N   . GLU B  147 ? 0.1281 0.1014 0.1303 0.0006  0.0089  -0.0120 147 GLU B N   
3285 C  CA  . GLU B  147 ? 0.1439 0.1122 0.1492 0.0219  -0.0072 -0.0131 147 GLU B CA  
3286 C  C   . GLU B  147 ? 0.1249 0.0955 0.1466 -0.0051 0.0062  -0.0147 147 GLU B C   
3287 O  O   . GLU B  147 ? 0.1252 0.1365 0.1485 0.0059  0.0044  -0.0157 147 GLU B O   
3288 C  CB  . GLU B  147 ? 0.2447 0.1556 0.2471 0.0652  -0.0220 -0.0122 147 GLU B CB  
3289 C  CG  . GLU B  147 ? 0.2483 0.3816 0.3406 0.0212  0.0001  0.0665  147 GLU B CG  
3290 C  CD  . GLU B  147 ? 0.4515 0.3560 0.3277 0.0998  -0.0430 0.0237  147 GLU B CD  
3291 O  OE1 . GLU B  147 ? 0.3422 0.3183 0.3015 0.0859  0.0050  0.0840  147 GLU B OE1 
3292 O  OE2 . GLU B  147 ? 0.5885 0.3155 0.5096 0.1750  -0.3080 -0.1233 147 GLU B OE2 
3293 N  N   . MET B  148 ? 0.1305 0.0973 0.1399 -0.0020 0.0063  -0.0026 148 MET B N   
3294 C  CA  . MET B  148 ? 0.1287 0.1091 0.1471 0.0005  0.0185  -0.0032 148 MET B CA  
3295 C  C   . MET B  148 ? 0.1293 0.0987 0.1700 0.0240  -0.0122 -0.0078 148 MET B C   
3296 O  O   . MET B  148 ? 0.1582 0.1071 0.1900 -0.0001 -0.0389 -0.0024 148 MET B O   
3297 C  CB  . MET B  148 ? 0.1199 0.1476 0.1545 0.0009  0.0099  -0.0284 148 MET B CB  
3298 C  CG  . MET B  148 ? 0.1702 0.1478 0.1752 -0.0137 0.0396  -0.0195 148 MET B CG  
3299 S  SD  . MET B  148 ? 0.2064 0.1590 0.2245 -0.0143 0.0461  -0.0332 148 MET B SD  
3300 C  CE  . MET B  148 ? 0.2224 0.1654 0.2151 -0.0161 0.0624  -0.0181 148 MET B CE  
3301 N  N   . GLY B  149 ? 0.1289 0.0914 0.1562 0.0107  -0.0085 -0.0139 149 GLY B N   
3302 C  CA  . GLY B  149 ? 0.1274 0.0983 0.1795 0.0031  -0.0234 -0.0076 149 GLY B CA  
3303 C  C   . GLY B  149 ? 0.1432 0.0774 0.1428 0.0167  0.0103  -0.0139 149 GLY B C   
3304 O  O   . GLY B  149 ? 0.1430 0.1024 0.1457 0.0070  -0.0037 -0.0116 149 GLY B O   
3305 N  N   . SER B  150 ? 0.1320 0.0855 0.1606 0.0119  -0.0042 -0.0006 150 SER B N   
3306 C  CA  . SER B  150 ? 0.1367 0.0890 0.1539 0.0067  -0.0282 0.0021  150 SER B CA  
3307 C  C   . SER B  150 ? 0.1476 0.0851 0.1592 0.0015  -0.0211 -0.0138 150 SER B C   
3308 O  O   . SER B  150 ? 0.1608 0.0974 0.1655 0.0057  -0.0097 -0.0102 150 SER B O   
3309 C  CB  . SER B  150 ? 0.1421 0.0663 0.2065 -0.0029 0.0049  -0.0116 150 SER B CB  
3310 O  OG  . SER B  150 ? 0.1439 0.1005 0.2027 0.0039  -0.0083 0.0027  150 SER B OG  
3311 N  N   . PHE B  151 ? 0.1520 0.0931 0.1536 0.0078  -0.0290 -0.0023 151 PHE B N   
3312 C  CA  . PHE B  151 ? 0.1474 0.0924 0.1511 0.0114  -0.0185 -0.0049 151 PHE B CA  
3313 C  C   . PHE B  151 ? 0.1466 0.0969 0.1701 0.0004  -0.0126 0.0065  151 PHE B C   
3314 O  O   . PHE B  151 ? 0.1757 0.1079 0.2046 -0.0179 0.0106  -0.0006 151 PHE B O   
3315 C  CB  . PHE B  151 ? 0.1609 0.0978 0.1860 -0.0011 -0.0450 -0.0044 151 PHE B CB  
3316 C  CG  . PHE B  151 ? 0.1781 0.1059 0.1716 -0.0030 -0.0322 -0.0179 151 PHE B CG  
3317 C  CD1 . PHE B  151 ? 0.2053 0.1204 0.1506 -0.0098 -0.0414 -0.0116 151 PHE B CD1 
3318 C  CD2 . PHE B  151 ? 0.1903 0.1370 0.1683 0.0104  -0.0331 -0.0035 151 PHE B CD2 
3319 C  CE1 . PHE B  151 ? 0.2300 0.1237 0.1858 -0.0027 -0.0651 -0.0050 151 PHE B CE1 
3320 C  CE2 . PHE B  151 ? 0.2101 0.1398 0.2120 0.0119  -0.0609 -0.0068 151 PHE B CE2 
3321 C  CZ  . PHE B  151 ? 0.2294 0.1541 0.1693 0.0073  -0.0705 -0.0362 151 PHE B CZ  
3322 N  N   . ASN B  152 ? 0.1454 0.0885 0.1454 0.0035  -0.0125 -0.0046 152 ASN B N   
3323 C  CA  . ASN B  152 ? 0.1259 0.1055 0.1295 0.0048  -0.0190 -0.0040 152 ASN B CA  
3324 C  C   . ASN B  152 ? 0.1365 0.0942 0.1464 0.0041  -0.0104 -0.0088 152 ASN B C   
3325 O  O   . ASN B  152 ? 0.1293 0.0983 0.1486 -0.0034 -0.0179 0.0002  152 ASN B O   
3326 C  CB  . ASN B  152 ? 0.1299 0.1227 0.1294 -0.0006 -0.0115 -0.0072 152 ASN B CB  
3327 C  CG  . ASN B  152 ? 0.1368 0.0935 0.1538 0.0051  -0.0037 -0.0060 152 ASN B CG  
3328 O  OD1 . ASN B  152 ? 0.1369 0.1527 0.1708 0.0036  -0.0134 -0.0065 152 ASN B OD1 
3329 N  ND2 . ASN B  152 ? 0.1564 0.1150 0.1489 -0.0005 -0.0130 -0.0005 152 ASN B ND2 
3330 N  N   . PRO B  153 ? 0.1322 0.0973 0.1713 -0.0135 -0.0351 0.0042  153 PRO B N   
3331 C  CA  . PRO B  153 ? 0.1303 0.1084 0.1851 0.0059  -0.0223 -0.0089 153 PRO B CA  
3332 C  C   . PRO B  153 ? 0.1321 0.1463 0.1621 0.0091  -0.0262 0.0050  153 PRO B C   
3333 O  O   . PRO B  153 ? 0.1955 0.1420 0.1744 0.0140  -0.0464 0.0098  153 PRO B O   
3334 C  CB  . PRO B  153 ? 0.1818 0.1463 0.2653 -0.0227 -0.0624 -0.0256 153 PRO B CB  
3335 C  CG  . PRO B  153 ? 0.1918 0.1746 0.3450 -0.0294 -0.0910 0.0075  153 PRO B CG  
3336 C  CD  . PRO B  153 ? 0.1407 0.1033 0.2767 -0.0189 -0.0450 0.0003  153 PRO B CD  
3337 N  N   . SER B  154 ? 0.1228 0.1315 0.1633 -0.0044 -0.0162 -0.0001 154 SER B N   
3338 C  CA  . SER B  154 ? 0.1296 0.1633 0.1711 -0.0038 -0.0003 -0.0159 154 SER B CA  
3339 C  C   . SER B  154 ? 0.1200 0.1249 0.1517 0.0168  -0.0179 0.0063  154 SER B C   
3340 O  O   . SER B  154 ? 0.1337 0.1306 0.1551 0.0144  -0.0078 -0.0048 154 SER B O   
3341 C  CB  . SER B  154 ? 0.1739 0.1455 0.1982 -0.0250 0.0201  -0.0003 154 SER B CB  
3342 O  OG  . SER B  154 ? 0.2583 0.2909 0.2422 -0.1234 0.0532  -0.0200 154 SER B OG  
3343 N  N   . TYR B  155 ? 0.1142 0.1080 0.1490 -0.0063 -0.0152 0.0000  155 TYR B N   
3344 C  CA  . TYR B  155 ? 0.1300 0.1078 0.1298 0.0053  -0.0069 -0.0063 155 TYR B CA  
3345 C  C   . TYR B  155 ? 0.1207 0.1102 0.1359 -0.0022 -0.0044 0.0047  155 TYR B C   
3346 O  O   . TYR B  155 ? 0.1492 0.1031 0.1458 -0.0019 -0.0087 0.0041  155 TYR B O   
3347 C  CB  . TYR B  155 ? 0.1188 0.1062 0.1421 0.0036  -0.0013 -0.0146 155 TYR B CB  
3348 C  CG  . TYR B  155 ? 0.1272 0.0969 0.1374 0.0162  0.0067  -0.0012 155 TYR B CG  
3349 C  CD1 . TYR B  155 ? 0.1355 0.1033 0.1340 0.0152  0.0026  0.0070  155 TYR B CD1 
3350 C  CD2 . TYR B  155 ? 0.1306 0.1048 0.1433 0.0166  -0.0006 -0.0081 155 TYR B CD2 
3351 C  CE1 . TYR B  155 ? 0.1087 0.1243 0.1572 0.0124  -0.0126 -0.0036 155 TYR B CE1 
3352 C  CE2 . TYR B  155 ? 0.1324 0.1222 0.1364 0.0079  -0.0009 0.0019  155 TYR B CE2 
3353 C  CZ  . TYR B  155 ? 0.1277 0.1077 0.1448 0.0240  -0.0125 -0.0043 155 TYR B CZ  
3354 O  OH  . TYR B  155 ? 0.1256 0.1276 0.1450 0.0075  -0.0118 -0.0006 155 TYR B OH  
3355 N  N   . ASP B  156 ? 0.1275 0.1226 0.1307 0.0000  -0.0128 -0.0025 156 ASP B N   
3356 C  CA  . ASP B  156 ? 0.1562 0.1100 0.1366 0.0010  -0.0204 -0.0204 156 ASP B CA  
3357 C  C   . ASP B  156 ? 0.1635 0.1149 0.1322 -0.0143 -0.0242 0.0100  156 ASP B C   
3358 O  O   . ASP B  156 ? 0.1987 0.1226 0.1392 -0.0065 -0.0220 0.0067  156 ASP B O   
3359 C  CB  . ASP B  156 ? 0.2281 0.1480 0.1605 0.0100  -0.0104 -0.0373 156 ASP B CB  
3360 C  CG  . ASP B  156 ? 0.2109 0.1358 0.1643 0.0164  -0.0198 -0.0122 156 ASP B CG  
3361 O  OD1 . ASP B  156 ? 0.2071 0.1304 0.1595 0.0212  -0.0053 0.0076  156 ASP B OD1 
3362 O  OD2 . ASP B  156 ? 0.2845 0.2269 0.1630 -0.0189 -0.0525 -0.0016 156 ASP B OD2 
3363 N  N   . LYS B  157 ? 0.1347 0.1244 0.1678 0.0087  -0.0152 0.0057  157 LYS B N   
3364 C  CA  . LYS B  157 ? 0.1631 0.1329 0.2151 0.0205  -0.0049 0.0011  157 LYS B CA  
3365 C  C   . LYS B  157 ? 0.1612 0.1146 0.1879 0.0275  -0.0321 0.0150  157 LYS B C   
3366 O  O   . LYS B  157 ? 0.2351 0.1388 0.2292 0.0318  -0.0582 0.0336  157 LYS B O   
3367 C  CB  . LYS B  157 ? 0.1489 0.1545 0.2149 0.0367  -0.0022 -0.0062 157 LYS B CB  
3368 C  CG  . LYS B  157 ? 0.1904 0.1356 0.3749 -0.0089 0.0447  0.0388  157 LYS B CG  
3369 C  CD  . LYS B  157 ? 0.2247 0.2807 0.3862 -0.0239 0.0480  -0.0811 157 LYS B CD  
3370 C  CE  . LYS B  157 ? 0.2156 0.2890 0.5345 -0.0959 0.0601  -0.0898 157 LYS B CE  
3371 N  NZ  . LYS B  157 ? 0.3520 0.4598 0.5881 -0.1312 0.2076  -0.1280 157 LYS B NZ  
3372 N  N   . ILE B  158 ? 0.1503 0.1143 0.1464 0.0057  -0.0143 0.0027  158 ILE B N   
3373 C  CA  . ILE B  158 ? 0.1802 0.1097 0.1593 -0.0172 0.0019  -0.0255 158 ILE B CA  
3374 C  C   . ILE B  158 ? 0.1692 0.1204 0.1516 -0.0076 -0.0161 0.0141  158 ILE B C   
3375 O  O   . ILE B  158 ? 0.2122 0.1307 0.1507 -0.0136 -0.0135 0.0163  158 ILE B O   
3376 C  CB  . ILE B  158 ? 0.2153 0.1292 0.1420 -0.0311 -0.0013 -0.0264 158 ILE B CB  
3377 C  CG1 . ILE B  158 ? 0.2755 0.1368 0.1729 -0.0200 0.0190  -0.0160 158 ILE B CG1 
3378 C  CG2 . ILE B  158 ? 0.2305 0.1280 0.1768 -0.0310 -0.0230 0.0044  158 ILE B CG2 
3379 C  CD1 . ILE B  158 ? 0.3425 0.2270 0.1813 -0.0842 -0.0201 0.0008  158 ILE B CD1 
3380 N  N   . PHE B  159 ? 0.1745 0.1134 0.1498 0.0064  -0.0004 -0.0023 159 PHE B N   
3381 C  CA  . PHE B  159 ? 0.1958 0.1238 0.1737 -0.0148 0.0198  -0.0086 159 PHE B CA  
3382 C  C   . PHE B  159 ? 0.2096 0.1710 0.1480 -0.0324 0.0205  0.0047  159 PHE B C   
3383 O  O   . PHE B  159 ? 0.2759 0.1817 0.1623 -0.0474 0.0290  -0.0004 159 PHE B O   
3384 C  CB  . PHE B  159 ? 0.1946 0.1237 0.1730 -0.0091 0.0185  -0.0165 159 PHE B CB  
3385 C  CG  . PHE B  159 ? 0.1566 0.1367 0.1727 -0.0237 0.0212  -0.0067 159 PHE B CG  
3386 C  CD1 . PHE B  159 ? 0.1566 0.1537 0.1965 -0.0124 0.0005  0.0049  159 PHE B CD1 
3387 C  CD2 . PHE B  159 ? 0.1931 0.1659 0.1874 0.0155  0.0315  0.0100  159 PHE B CD2 
3388 C  CE1 . PHE B  159 ? 0.1846 0.1617 0.1983 -0.0153 -0.0137 -0.0063 159 PHE B CE1 
3389 C  CE2 . PHE B  159 ? 0.1809 0.1913 0.1919 0.0039  0.0403  0.0130  159 PHE B CE2 
3390 C  CZ  . PHE B  159 ? 0.1596 0.1548 0.2107 0.0175  0.0060  0.0096  159 PHE B CZ  
3391 N  N   . SER B  160 ? 0.2280 0.1628 0.1426 -0.0330 -0.0023 -0.0184 160 SER B N   
3392 C  CA  . SER B  160 ? 0.2413 0.1919 0.1482 -0.0399 -0.0103 0.0021  160 SER B CA  
3393 C  C   . SER B  160 ? 0.2773 0.2168 0.1397 -0.0298 -0.0190 0.0108  160 SER B C   
3394 O  O   . SER B  160 ? 0.3288 0.2563 0.1475 -0.0542 -0.0347 0.0232  160 SER B O   
3395 C  CB  . SER B  160 ? 0.2646 0.2733 0.1668 -0.0456 -0.0408 0.0052  160 SER B CB  
3396 O  OG  . SER B  160 ? 0.2498 0.2603 0.1821 -0.0416 -0.0412 0.0111  160 SER B OG  
3397 N  N   . HIS B  161 ? 0.2627 0.1401 0.1817 -0.0337 -0.0177 0.0124  161 HIS B N   
3398 C  CA  . HIS B  161 ? 0.2727 0.1666 0.1898 -0.0262 -0.0579 0.0083  161 HIS B CA  
3399 C  C   . HIS B  161 ? 0.2825 0.2030 0.1879 -0.0653 -0.0768 0.0159  161 HIS B C   
3400 O  O   . HIS B  161 ? 0.3990 0.2166 0.2029 -0.1001 -0.0642 0.0699  161 HIS B O   
3401 C  CB  . HIS B  161 ? 0.3071 0.1842 0.1700 0.0003  -0.0637 0.0207  161 HIS B CB  
3402 C  CG  . HIS B  161 ? 0.3004 0.1757 0.1907 0.0006  -0.0227 -0.0081 161 HIS B CG  
3403 N  ND1 . HIS B  161 ? 0.2922 0.2568 0.2482 0.0240  -0.0566 0.0113  161 HIS B ND1 
3404 C  CD2 . HIS B  161 ? 0.2511 0.1947 0.2406 0.0048  0.0044  0.0111  161 HIS B CD2 
3405 C  CE1 . HIS B  161 ? 0.3411 0.2351 0.2081 0.0284  -0.0390 -0.0222 161 HIS B CE1 
3406 N  NE2 . HIS B  161 ? 0.2974 0.1953 0.2601 0.0109  -0.0252 -0.0050 161 HIS B NE2 
3407 N  N   . LEU B  162 ? 0.2733 0.2303 0.2165 -0.0902 -0.0383 0.0433  162 LEU B N   
3408 C  CA  . LEU B  162 ? 0.3145 0.2419 0.2233 -0.1030 -0.0025 0.0622  162 LEU B CA  
3409 C  C   . LEU B  162 ? 0.4068 0.2900 0.1490 -0.1791 -0.0438 0.0406  162 LEU B C   
3410 O  O   . LEU B  162 ? 0.5432 0.2383 0.1885 -0.1993 -0.0331 0.0496  162 LEU B O   
3411 C  CB  . LEU B  162 ? 0.3204 0.2839 0.2181 -0.1208 -0.0116 0.0594  162 LEU B CB  
3412 C  CG  . LEU B  162 ? 0.4112 0.3289 0.2053 -0.1289 0.0287  0.0337  162 LEU B CG  
3413 C  CD1 . LEU B  162 ? 0.2222 0.4637 0.3849 -0.1211 0.0158  0.0741  162 LEU B CD1 
3414 C  CD2 . LEU B  162 ? 0.4801 0.3222 0.2300 -0.1597 -0.0790 0.0432  162 LEU B CD2 
3415 N  N   . GLN B  163 ? 0.4557 0.2196 0.1868 -0.1055 -0.0680 0.0261  163 GLN B N   
3416 C  CA  . GLN B  163 ? 0.4782 0.2277 0.1914 -0.1013 0.0040  0.0433  163 GLN B CA  
3417 C  C   . GLN B  163 ? 0.3953 0.2193 0.2356 -0.0605 -0.0502 -0.0168 163 GLN B C   
3418 O  O   . GLN B  163 ? 0.4206 0.4539 0.2708 -0.1221 -0.0924 0.1710  163 GLN B O   
3419 C  CB  . GLN B  163 ? 0.4205 0.3599 0.1805 -0.0250 -0.0249 -0.0263 163 GLN B CB  
3420 C  CG  . GLN B  163 ? 0.3403 0.4519 0.3694 0.0352  -0.0182 -0.0668 163 GLN B CG  
3421 C  CD  . GLN B  163 ? 0.3497 0.3202 0.5037 0.0396  0.0320  -0.0085 163 GLN B CD  
3422 O  OE1 . GLN B  163 ? 0.5013 0.3012 0.4277 -0.0587 0.0381  -0.0427 163 GLN B OE1 
3423 N  NE2 . GLN B  163 ? 0.4508 0.3034 0.3454 0.0312  -0.0464 -0.0408 163 GLN B NE2 
3424 N  N   . HIS B  164 ? 0.3896 0.2545 0.2149 -0.0663 -0.0384 -0.0122 164 HIS B N   
3425 C  CA  . HIS B  164 ? 0.2848 0.3234 0.1500 -0.0296 -0.0851 0.0026  164 HIS B CA  
3426 C  C   . HIS B  164 ? 0.2417 0.2644 0.2127 -0.0840 -0.0569 0.0491  164 HIS B C   
3427 O  O   . HIS B  164 ? 0.2383 0.3334 0.2227 -0.0661 -0.0533 0.0629  164 HIS B O   
3428 C  CB  . HIS B  164 ? 0.3805 0.3306 0.2877 -0.0732 -0.1445 0.0193  164 HIS B CB  
3429 C  CG  . HIS B  164 ? 0.4681 0.3095 0.2890 -0.0551 -0.2085 -0.0122 164 HIS B CG  
3430 N  ND1 . HIS B  164 ? 0.4897 0.2653 0.3808 -0.0775 -0.1811 -0.0009 164 HIS B ND1 
3431 C  CD2 . HIS B  164 ? 0.4622 0.2769 0.3295 -0.0109 -0.2230 -0.0432 164 HIS B CD2 
3432 C  CE1 . HIS B  164 ? 0.4381 0.3098 0.5080 -0.0607 -0.1650 -0.1176 164 HIS B CE1 
3433 N  NE2 . HIS B  164 ? 0.3968 0.4627 0.3500 0.0359  -0.2023 -0.0873 164 HIS B NE2 
3434 N  N   . VAL B  165 ? 0.2465 0.1936 0.1444 -0.0797 -0.0476 0.0490  165 VAL B N   
3435 C  CA  . VAL B  165 ? 0.2273 0.1629 0.1743 -0.0612 -0.0100 0.0274  165 VAL B CA  
3436 C  C   . VAL B  165 ? 0.2044 0.1295 0.1573 -0.0348 0.0118  0.0157  165 VAL B C   
3437 O  O   . VAL B  165 ? 0.1830 0.1649 0.1715 -0.0432 0.0146  0.0312  165 VAL B O   
3438 C  CB  . VAL B  165 ? 0.2272 0.2017 0.1685 -0.0785 0.0066  0.0009  165 VAL B CB  
3439 C  CG1 . VAL B  165 ? 0.2004 0.2172 0.2648 -0.0709 -0.0052 -0.0117 165 VAL B CG1 
3440 C  CG2 . VAL B  165 ? 0.2406 0.2258 0.1573 -0.0657 -0.0234 0.0609  165 VAL B CG2 
3441 N  N   A LYS B  166 ? 0.2277 0.1120 0.1676 -0.0432 0.0181  0.0196  166 LYS B N   
3442 N  N   B LYS B  166 ? 0.2111 0.1648 0.1825 -0.0033 0.0479  0.0394  166 LYS B N   
3443 C  CA  A LYS B  166 ? 0.2359 0.2030 0.1193 -0.0232 -0.0023 0.0282  166 LYS B CA  
3444 C  CA  B LYS B  166 ? 0.1696 0.1312 0.1383 -0.0087 -0.0155 0.0488  166 LYS B CA  
3445 C  C   A LYS B  166 ? 0.1941 0.1940 0.1046 0.0078  -0.0158 0.0264  166 LYS B C   
3446 C  C   B LYS B  166 ? 0.1676 0.1430 0.1494 -0.0038 0.0411  0.0171  166 LYS B C   
3447 O  O   A LYS B  166 ? 0.1931 0.1375 0.1357 -0.0387 -0.0146 -0.0118 166 LYS B O   
3448 O  O   B LYS B  166 ? 0.1471 0.1191 0.1471 -0.0168 0.0198  0.0155  166 LYS B O   
3449 C  CB  A LYS B  166 ? 0.2011 0.1467 0.1666 -0.0078 0.0376  -0.0133 166 LYS B CB  
3450 C  CB  B LYS B  166 ? 0.1628 0.1606 0.1574 -0.0013 -0.0223 0.0005  166 LYS B CB  
3451 C  CG  A LYS B  166 ? 0.1733 0.1749 0.1447 -0.0195 0.0407  0.0004  166 LYS B CG  
3452 C  CG  B LYS B  166 ? 0.1875 0.2155 0.2120 -0.0194 0.0273  -0.0002 166 LYS B CG  
3453 C  CD  A LYS B  166 ? 0.2545 0.2345 0.1204 0.0847  -0.0104 -0.0537 166 LYS B CD  
3454 C  CD  B LYS B  166 ? 0.2797 0.2222 0.2143 -0.0201 -0.0194 -0.0006 166 LYS B CD  
3455 C  CE  A LYS B  166 ? 0.2186 0.2109 0.1532 0.0248  -0.0183 -0.0079 166 LYS B CE  
3456 C  CE  B LYS B  166 ? 0.3951 0.2224 0.2303 0.0520  -0.0651 -0.0265 166 LYS B CE  
3457 N  NZ  A LYS B  166 ? 0.2386 0.1825 0.2430 -0.0335 0.0244  -0.0066 166 LYS B NZ  
3458 N  NZ  B LYS B  166 ? 0.2568 0.2408 0.2086 0.0117  -0.0223 0.0192  166 LYS B NZ  
3459 N  N   . TYR B  167 ? 0.2097 0.1423 0.1637 -0.0062 0.0621  0.0144  167 TYR B N   
3460 C  CA  . TYR B  167 ? 0.2007 0.1347 0.1622 -0.0223 0.0502  0.0198  167 TYR B CA  
3461 C  C   . TYR B  167 ? 0.1676 0.1427 0.1471 0.0044  0.0221  0.0144  167 TYR B C   
3462 O  O   . TYR B  167 ? 0.1703 0.1451 0.1683 0.0005  0.0369  0.0088  167 TYR B O   
3463 C  CB  . TYR B  167 ? 0.2415 0.1682 0.1654 0.0041  0.0864  0.0243  167 TYR B CB  
3464 C  CG  . TYR B  167 ? 0.3065 0.1569 0.2423 -0.0312 0.0838  0.0763  167 TYR B CG  
3465 C  CD1 . TYR B  167 ? 0.4075 0.1798 0.3401 0.0785  0.2322  0.0996  167 TYR B CD1 
3466 C  CD2 . TYR B  167 ? 0.4102 0.2212 0.2018 0.0041  0.0973  0.0293  167 TYR B CD2 
3467 C  CE1 . TYR B  167 ? 0.4118 0.1692 0.1492 -0.0411 0.0110  0.0148  167 TYR B CE1 
3468 C  CE2 . TYR B  167 ? 0.2168 0.3150 0.2377 -0.0181 0.0069  0.0108  167 TYR B CE2 
3469 C  CZ  . TYR B  167 ? 0.2477 0.2717 0.2500 0.0106  0.1099  -0.0126 167 TYR B CZ  
3470 O  OH  . TYR B  167 ? 0.3164 0.3395 0.2560 0.0011  0.0446  -0.0707 167 TYR B OH  
3471 N  N   . LYS B  168 ? 0.1909 0.1555 0.1637 -0.0182 0.0428  -0.0092 168 LYS B N   
3472 C  CA  . LYS B  168 ? 0.1744 0.1410 0.1946 -0.0069 0.0195  -0.0017 168 LYS B CA  
3473 C  C   . LYS B  168 ? 0.1925 0.1420 0.1843 -0.0121 0.0190  -0.0096 168 LYS B C   
3474 O  O   . LYS B  168 ? 0.2340 0.1573 0.2333 0.0084  0.0340  0.0258  168 LYS B O   
3475 C  CB  . LYS B  168 ? 0.2147 0.1935 0.2021 -0.0412 0.0324  -0.0433 168 LYS B CB  
3476 C  CG  . LYS B  168 ? 0.2435 0.1741 0.2263 -0.0126 0.0243  -0.0271 168 LYS B CG  
3477 C  CD  . LYS B  168 ? 0.2533 0.2140 0.3118 -0.0604 0.0128  -0.0421 168 LYS B CD  
3478 C  CE  . LYS B  168 ? 0.4029 0.3542 0.2988 -0.1450 0.0249  -0.0921 168 LYS B CE  
3479 N  NZ  . LYS B  168 ? 0.4271 0.4879 0.5070 -0.1218 -0.0354 -0.2026 168 LYS B NZ  
3480 N  N   . GLY B  169 ? 0.1931 0.1648 0.1676 0.0040  0.0376  -0.0154 169 GLY B N   
3481 C  CA  . GLY B  169 ? 0.2220 0.1741 0.2759 0.0161  -0.0135 -0.0227 169 GLY B CA  
3482 C  C   . GLY B  169 ? 0.1799 0.2055 0.2432 -0.0076 0.0381  -0.0264 169 GLY B C   
3483 O  O   . GLY B  169 ? 0.1895 0.2563 0.3846 0.0381  0.0345  -0.0134 169 GLY B O   
3484 N  N   . GLN B  170 ? 0.2129 0.1526 0.1992 -0.0177 0.0268  0.0233  170 GLN B N   
3485 C  CA  . GLN B  170 ? 0.2213 0.1791 0.1970 -0.0275 0.0111  0.0552  170 GLN B CA  
3486 C  C   . GLN B  170 ? 0.1652 0.1782 0.2039 -0.0042 0.0048  0.0403  170 GLN B C   
3487 O  O   . GLN B  170 ? 0.1997 0.2019 0.1856 -0.0243 -0.0027 0.0588  170 GLN B O   
3488 C  CB  . GLN B  170 ? 0.2077 0.1870 0.1960 0.0019  0.0260  0.0658  170 GLN B CB  
3489 C  CG  . GLN B  170 ? 0.2833 0.1721 0.2017 0.0066  0.0567  0.0600  170 GLN B CG  
3490 C  CD  . GLN B  170 ? 0.3834 0.2289 0.1657 0.0363  0.0136  0.0444  170 GLN B CD  
3491 O  OE1 . GLN B  170 ? 0.3491 0.2148 0.1536 0.0093  0.0143  0.0190  170 GLN B OE1 
3492 N  NE2 . GLN B  170 ? 0.4247 0.3365 0.2031 0.0083  -0.0312 0.1208  170 GLN B NE2 
3493 N  N   . GLU B  171 ? 0.1747 0.2193 0.2112 -0.0120 -0.0097 0.0884  171 GLU B N   
3494 C  CA  . GLU B  171 ? 0.2151 0.2490 0.1928 -0.0529 0.0087  0.0723  171 GLU B CA  
3495 C  C   . GLU B  171 ? 0.2043 0.3098 0.1844 -0.0677 -0.0416 0.0986  171 GLU B C   
3496 O  O   . GLU B  171 ? 0.2485 0.3801 0.1827 -0.0699 -0.0486 0.1238  171 GLU B O   
3497 C  CB  . GLU B  171 ? 0.2661 0.2691 0.3195 -0.0285 0.0239  0.0540  171 GLU B CB  
3498 C  CG  . GLU B  171 ? 0.3380 0.2578 0.3022 -0.0089 0.0699  0.0019  171 GLU B CG  
3499 C  CD  . GLU B  171 ? 0.4430 0.2594 0.4445 -0.0469 0.0722  0.0854  171 GLU B CD  
3500 O  OE1 . GLU B  171 ? 0.3912 0.4239 0.7837 0.0500  0.1919  0.2459  171 GLU B OE1 
3501 O  OE2 . GLU B  171 ? 0.4740 0.5392 0.3779 -0.0300 0.0862  -0.0741 171 GLU B OE2 
3502 N  N   . ALA B  172 ? 0.2014 0.2600 0.1609 -0.0788 -0.0265 0.0776  172 ALA B N   
3503 C  CA  . ALA B  172 ? 0.1407 0.3098 0.1989 -0.0613 -0.0463 0.0358  172 ALA B CA  
3504 C  C   . ALA B  172 ? 0.1946 0.2658 0.1539 -0.0644 -0.0395 0.0668  172 ALA B C   
3505 O  O   . ALA B  172 ? 0.1742 0.3406 0.1552 -0.0558 -0.0257 0.0520  172 ALA B O   
3506 C  CB  . ALA B  172 ? 0.2281 0.3922 0.1837 -0.0652 -0.0292 -0.0121 172 ALA B CB  
3507 N  N   . PHE B  173 ? 0.1906 0.2557 0.1508 -0.0564 -0.0423 0.0387  173 PHE B N   
3508 C  CA  . PHE B  173 ? 0.1819 0.2071 0.1570 -0.0419 -0.0194 0.0431  173 PHE B CA  
3509 C  C   . PHE B  173 ? 0.2260 0.2082 0.1719 -0.0560 -0.0409 0.0184  173 PHE B C   
3510 O  O   . PHE B  173 ? 0.3632 0.3080 0.1788 -0.0389 -0.0262 -0.0299 173 PHE B O   
3511 C  CB  . PHE B  173 ? 0.1866 0.2489 0.2489 -0.0302 -0.0403 0.0455  173 PHE B CB  
3512 C  CG  . PHE B  173 ? 0.1992 0.2417 0.2964 -0.0397 -0.0834 0.0408  173 PHE B CG  
3513 C  CD1 . PHE B  173 ? 0.2477 0.2984 0.3236 -0.0201 -0.0823 0.0013  173 PHE B CD1 
3514 C  CD2 . PHE B  173 ? 0.3791 0.2965 0.3508 -0.0122 -0.0974 0.0966  173 PHE B CD2 
3515 C  CE1 . PHE B  173 ? 0.3248 0.2700 0.4098 0.1331  -0.0815 0.0022  173 PHE B CE1 
3516 C  CE2 . PHE B  173 ? 0.4419 0.2603 0.4551 0.0951  -0.0978 0.0272  173 PHE B CE2 
3517 C  CZ  . PHE B  173 ? 0.2944 0.3859 0.4605 0.0929  -0.0630 0.0991  173 PHE B CZ  
3518 N  N   . VAL B  174 ? 0.1966 0.1799 0.1588 -0.0234 0.0233  0.0277  174 VAL B N   
3519 C  CA  . VAL B  174 ? 0.1925 0.1694 0.1857 -0.0131 0.0005  -0.0311 174 VAL B CA  
3520 C  C   . VAL B  174 ? 0.1640 0.1825 0.1699 -0.0260 0.0195  0.0006  174 VAL B C   
3521 O  O   . VAL B  174 ? 0.1638 0.1976 0.1842 -0.0247 0.0117  -0.0196 174 VAL B O   
3522 C  CB  . VAL B  174 ? 0.1380 0.1846 0.1889 0.0079  -0.0152 0.0068  174 VAL B CB  
3523 C  CG1 . VAL B  174 ? 0.1778 0.1826 0.2085 0.0067  -0.0285 0.0140  174 VAL B CG1 
3524 C  CG2 . VAL B  174 ? 0.1534 0.2353 0.2251 -0.0063 0.0175  -0.0222 174 VAL B CG2 
3525 N  N   . PRO B  175 ? 0.1402 0.1606 0.1539 -0.0004 -0.0046 0.0096  175 PRO B N   
3526 C  CA  . PRO B  175 ? 0.1437 0.1688 0.1465 -0.0279 -0.0062 0.0425  175 PRO B CA  
3527 C  C   . PRO B  175 ? 0.1368 0.1597 0.1507 -0.0019 -0.0062 0.0365  175 PRO B C   
3528 O  O   . PRO B  175 ? 0.1405 0.1960 0.1825 0.0127  -0.0060 0.0394  175 PRO B O   
3529 C  CB  . PRO B  175 ? 0.1909 0.1735 0.1966 -0.0332 -0.0386 0.0171  175 PRO B CB  
3530 C  CG  . PRO B  175 ? 0.1634 0.2210 0.2061 -0.0273 -0.0249 0.0228  175 PRO B CG  
3531 C  CD  . PRO B  175 ? 0.1522 0.2041 0.1517 -0.0091 -0.0268 -0.0046 175 PRO B CD  
3532 N  N   . GLY B  176 ? 0.1238 0.1911 0.1646 -0.0003 -0.0147 0.0458  176 GLY B N   
3533 C  CA  . GLY B  176 ? 0.1472 0.1678 0.1578 0.0031  0.0024  0.0392  176 GLY B CA  
3534 C  C   . GLY B  176 ? 0.1283 0.1689 0.1779 -0.0073 -0.0044 0.0078  176 GLY B C   
3535 O  O   . GLY B  176 ? 0.1522 0.1866 0.1787 -0.0088 -0.0258 0.0247  176 GLY B O   
3536 N  N   . PHE B  177 ? 0.1129 0.1591 0.1691 0.0018  -0.0229 0.0287  177 PHE B N   
3537 C  CA  . PHE B  177 ? 0.1441 0.1537 0.1912 0.0006  -0.0315 0.0297  177 PHE B CA  
3538 C  C   . PHE B  177 ? 0.1367 0.1583 0.1980 0.0048  -0.0392 0.0105  177 PHE B C   
3539 O  O   . PHE B  177 ? 0.1378 0.1726 0.1796 0.0011  -0.0303 0.0282  177 PHE B O   
3540 C  CB  . PHE B  177 ? 0.1514 0.1826 0.2001 0.0012  -0.0520 -0.0242 177 PHE B CB  
3541 C  CG  . PHE B  177 ? 0.1464 0.1813 0.1578 0.0322  -0.0287 -0.0116 177 PHE B CG  
3542 C  CD1 . PHE B  177 ? 0.1450 0.1781 0.1973 0.0133  -0.0200 -0.0185 177 PHE B CD1 
3543 C  CD2 . PHE B  177 ? 0.1507 0.1978 0.1827 0.0450  -0.0245 -0.0068 177 PHE B CD2 
3544 C  CE1 . PHE B  177 ? 0.1249 0.2423 0.2019 0.0249  -0.0132 0.0286  177 PHE B CE1 
3545 C  CE2 . PHE B  177 ? 0.1411 0.2251 0.1867 0.0729  -0.0277 -0.0026 177 PHE B CE2 
3546 C  CZ  . PHE B  177 ? 0.1465 0.2581 0.1578 0.0467  -0.0086 0.0139  177 PHE B CZ  
3547 N  N   . ASN B  178 ? 0.1725 0.1513 0.2058 -0.0100 -0.0564 0.0308  178 ASN B N   
3548 C  CA  . ASN B  178 ? 0.1552 0.1674 0.1915 -0.0343 -0.0465 0.0283  178 ASN B CA  
3549 C  C   . ASN B  178 ? 0.1344 0.1281 0.1596 -0.0122 -0.0212 0.0148  178 ASN B C   
3550 O  O   . ASN B  178 ? 0.1668 0.1511 0.1738 -0.0150 -0.0269 0.0168  178 ASN B O   
3551 C  CB  . ASN B  178 ? 0.1807 0.1850 0.2331 -0.0553 -0.0709 0.0423  178 ASN B CB  
3552 C  CG  . ASN B  178 ? 0.1597 0.1804 0.2052 -0.0071 -0.0060 0.0342  178 ASN B CG  
3553 O  OD1 . ASN B  178 ? 0.1544 0.1828 0.2200 -0.0196 -0.0013 0.0480  178 ASN B OD1 
3554 N  ND2 . ASN B  178 ? 0.2287 0.1892 0.2529 -0.0651 0.0158  0.0491  178 ASN B ND2 
3555 N  N   . ILE B  179 ? 0.1098 0.1268 0.1767 -0.0103 -0.0179 0.0144  179 ILE B N   
3556 C  CA  . ILE B  179 ? 0.1019 0.1362 0.1674 -0.0031 -0.0114 0.0149  179 ILE B CA  
3557 C  C   . ILE B  179 ? 0.1319 0.1238 0.1411 0.0100  0.0144  -0.0035 179 ILE B C   
3558 O  O   . ILE B  179 ? 0.1199 0.1475 0.1562 0.0119  0.0022  0.0054  179 ILE B O   
3559 C  CB  . ILE B  179 ? 0.1062 0.1355 0.1681 -0.0026 0.0083  0.0159  179 ILE B CB  
3560 C  CG1 . ILE B  179 ? 0.1583 0.1226 0.1693 -0.0070 0.0066  0.0096  179 ILE B CG1 
3561 C  CG2 . ILE B  179 ? 0.1036 0.1599 0.1926 -0.0208 -0.0094 -0.0263 179 ILE B CG2 
3562 C  CD1 . ILE B  179 ? 0.2004 0.1570 0.1653 -0.0017 0.0328  0.0148  179 ILE B CD1 
3563 N  N   . GLU B  180 ? 0.1184 0.1460 0.1597 -0.0013 -0.0048 0.0160  180 GLU B N   
3564 C  CA  . GLU B  180 ? 0.1524 0.1570 0.1543 0.0231  0.0062  0.0249  180 GLU B CA  
3565 C  C   . GLU B  180 ? 0.1322 0.1472 0.1725 0.0021  0.0087  0.0254  180 GLU B C   
3566 O  O   . GLU B  180 ? 0.1435 0.1638 0.1852 0.0019  0.0098  0.0538  180 GLU B O   
3567 C  CB  . GLU B  180 ? 0.1347 0.2175 0.1870 -0.0068 0.0242  0.0395  180 GLU B CB  
3568 C  CG  . GLU B  180 ? 0.2351 0.2919 0.2532 0.0241  0.0392  0.1141  180 GLU B CG  
3569 C  CD  . GLU B  180 ? 0.2264 0.2644 0.2429 0.0032  0.0165  0.0950  180 GLU B CD  
3570 O  OE1 . GLU B  180 ? 0.2564 0.3615 0.2389 0.0053  0.0479  0.1198  180 GLU B OE1 
3571 O  OE2 . GLU B  180 ? 0.2787 0.4202 0.2666 -0.0203 0.0475  0.1144  180 GLU B OE2 
3572 N  N   . GLU B  181 ? 0.1341 0.1347 0.1666 -0.0277 0.0087  0.0094  181 GLU B N   
3573 C  CA  . GLU B  181 ? 0.1650 0.1495 0.1619 -0.0187 -0.0139 0.0211  181 GLU B CA  
3574 C  C   . GLU B  181 ? 0.1305 0.1478 0.1585 0.0017  -0.0022 0.0036  181 GLU B C   
3575 O  O   . GLU B  181 ? 0.1516 0.1359 0.2079 -0.0052 -0.0039 -0.0134 181 GLU B O   
3576 C  CB  . GLU B  181 ? 0.1575 0.2238 0.2057 -0.0478 -0.0320 -0.0397 181 GLU B CB  
3577 C  CG  . GLU B  181 ? 0.1490 0.2886 0.3439 -0.0591 -0.0138 -0.1048 181 GLU B CG  
3578 C  CD  . GLU B  181 ? 0.2157 0.4352 0.3531 -0.0509 0.0032  -0.0949 181 GLU B CD  
3579 O  OE1 . GLU B  181 ? 0.2618 0.6723 0.3986 -0.0167 0.0534  0.0221  181 GLU B OE1 
3580 O  OE2 . GLU B  181 ? 0.2697 0.3828 0.4522 -0.0960 0.0190  -0.0567 181 GLU B OE2 
3581 N  N   . LEU B  182 ? 0.1103 0.1253 0.1516 -0.0012 -0.0132 0.0190  182 LEU B N   
3582 C  CA  . LEU B  182 ? 0.1179 0.1012 0.1521 -0.0082 -0.0225 0.0147  182 LEU B CA  
3583 C  C   . LEU B  182 ? 0.1177 0.1121 0.1316 0.0044  -0.0142 0.0064  182 LEU B C   
3584 O  O   . LEU B  182 ? 0.1198 0.1381 0.1384 0.0092  -0.0008 0.0094  182 LEU B O   
3585 C  CB  . LEU B  182 ? 0.1215 0.1211 0.1404 0.0044  -0.0119 0.0306  182 LEU B CB  
3586 C  CG  . LEU B  182 ? 0.1229 0.1077 0.1340 0.0040  -0.0082 0.0058  182 LEU B CG  
3587 C  CD1 . LEU B  182 ? 0.1547 0.0906 0.1513 -0.0067 -0.0039 0.0212  182 LEU B CD1 
3588 C  CD2 . LEU B  182 ? 0.1436 0.1592 0.1249 0.0135  -0.0019 0.0023  182 LEU B CD2 
3589 N  N   . LEU B  183 ? 0.1333 0.1349 0.1425 -0.0038 -0.0072 0.0356  183 LEU B N   
3590 C  CA  . LEU B  183 ? 0.1396 0.1278 0.1322 -0.0015 -0.0126 0.0207  183 LEU B CA  
3591 C  C   . LEU B  183 ? 0.1268 0.1503 0.1268 -0.0005 0.0027  0.0059  183 LEU B C   
3592 O  O   . LEU B  183 ? 0.1570 0.1328 0.1771 -0.0121 -0.0165 0.0146  183 LEU B O   
3593 C  CB  . LEU B  183 ? 0.1358 0.1729 0.1329 0.0069  -0.0054 0.0077  183 LEU B CB  
3594 C  CG  . LEU B  183 ? 0.1818 0.1619 0.1537 0.0066  0.0150  0.0134  183 LEU B CG  
3595 C  CD1 . LEU B  183 ? 0.2444 0.2090 0.1849 0.0614  0.0543  0.0225  183 LEU B CD1 
3596 C  CD2 . LEU B  183 ? 0.1823 0.1923 0.2285 0.0032  0.0031  0.0081  183 LEU B CD2 
3597 N  N   . PRO B  184 ? 0.1188 0.1267 0.1551 -0.0081 0.0057  0.0146  184 PRO B N   
3598 C  CA  . PRO B  184 ? 0.1515 0.1320 0.1788 -0.0121 -0.0020 0.0147  184 PRO B CA  
3599 C  C   . PRO B  184 ? 0.2328 0.1384 0.2601 -0.0452 0.0370  -0.0273 184 PRO B C   
3600 O  O   . PRO B  184 ? 0.2976 0.1620 0.2379 -0.0718 0.0966  -0.0084 184 PRO B O   
3601 C  CB  . PRO B  184 ? 0.2466 0.1734 0.1907 0.0502  -0.0845 -0.0321 184 PRO B CB  
3602 C  CG  . PRO B  184 ? 0.2087 0.1747 0.1639 0.0640  -0.0635 -0.0195 184 PRO B CG  
3603 C  CD  . PRO B  184 ? 0.1275 0.1400 0.1439 -0.0176 -0.0147 0.0205  184 PRO B CD  
3604 N  N   . GLU B  185 ? 0.2345 0.1596 0.2359 -0.0077 -0.0122 0.0117  185 GLU B N   
3605 C  CA  . GLU B  185 ? 0.2623 0.1266 0.2394 -0.0347 -0.0307 0.0042  185 GLU B CA  
3606 C  C   . GLU B  185 ? 0.1995 0.2125 0.1777 -0.0290 -0.0262 0.0270  185 GLU B C   
3607 O  O   . GLU B  185 ? 0.2086 0.2446 0.2615 -0.0809 -0.0721 0.1048  185 GLU B O   
3608 C  CB  . GLU B  185 ? 0.4710 0.1751 0.2110 0.0668  -0.0061 0.0113  185 GLU B CB  
3609 C  CG  . GLU B  185 ? 0.6069 0.2507 0.2935 -0.0767 -0.0181 -0.0798 185 GLU B CG  
3610 C  CD  . GLU B  185 ? 0.6335 0.5632 0.7572 -0.0151 -0.0159 -0.1676 185 GLU B CD  
3611 O  OE1 . GLU B  185 ? 0.6254 0.5576 0.3789 -0.0255 -0.1151 -0.1403 185 GLU B OE1 
3612 O  OE2 . GLU B  185 ? 1.4170 0.6246 1.0263 -0.2548 0.1720  -0.3070 185 GLU B OE2 
3613 N  N   . ARG B  186 ? 0.2081 0.1965 0.2091 -0.0274 0.0127  0.0260  186 ARG B N   
3614 C  CA  . ARG B  186 ? 0.2808 0.1711 0.2061 -0.0262 -0.0016 0.0348  186 ARG B CA  
3615 C  C   . ARG B  186 ? 0.1820 0.1973 0.2406 -0.0055 0.0245  0.0103  186 ARG B C   
3616 O  O   . ARG B  186 ? 0.2023 0.2195 0.2019 -0.0111 0.0107  0.0279  186 ARG B O   
3617 C  CB  . ARG B  186 ? 0.2565 0.2103 0.2768 -0.0196 -0.0449 0.0357  186 ARG B CB  
3618 C  CG  . ARG B  186 ? 0.6470 0.1613 0.3750 -0.0121 -0.1177 0.1088  186 ARG B CG  
3619 C  CD  . ARG B  186 ? 0.5683 0.3315 0.4204 0.0377  -0.0807 0.0824  186 ARG B CD  
3620 N  NE  . ARG B  186 ? 0.4865 0.2289 0.4914 -0.0311 -0.1158 0.1064  186 ARG B NE  
3621 C  CZ  . ARG B  186 ? 0.5772 0.6474 0.5087 -0.1254 0.0640  -0.0223 186 ARG B CZ  
3622 N  NH1 . ARG B  186 ? 1.0788 0.7063 0.4628 -0.2723 -0.3775 0.0504  186 ARG B NH1 
3623 N  NH2 . ARG B  186 ? 0.7819 0.5441 0.8293 -0.1800 0.2892  -0.3093 186 ARG B NH2 
3624 N  N   . THR B  187 ? 0.1472 0.1546 0.1767 -0.0016 0.0176  0.0316  187 THR B N   
3625 C  CA  . THR B  187 ? 0.1342 0.1410 0.1572 -0.0038 -0.0033 0.0294  187 THR B CA  
3626 C  C   . THR B  187 ? 0.1688 0.1509 0.1594 0.0035  0.0133  0.0458  187 THR B C   
3627 O  O   . THR B  187 ? 0.1601 0.1576 0.1648 -0.0143 0.0111  0.0365  187 THR B O   
3628 C  CB  . THR B  187 ? 0.1337 0.1696 0.1487 -0.0050 -0.0031 0.0300  187 THR B CB  
3629 O  OG1 . THR B  187 ? 0.1435 0.2090 0.2200 0.0046  -0.0094 0.0339  187 THR B OG1 
3630 C  CG2 . THR B  187 ? 0.2246 0.1846 0.1469 0.0431  -0.0185 0.0130  187 THR B CG2 
3631 N  N   . ALA B  188 ? 0.1442 0.2190 0.1652 -0.0468 -0.0042 0.0683  188 ALA B N   
3632 C  CA  . ALA B  188 ? 0.1467 0.1948 0.1563 -0.0290 0.0061  0.0543  188 ALA B CA  
3633 C  C   . ALA B  188 ? 0.1268 0.1499 0.1406 -0.0105 0.0142  0.0209  188 ALA B C   
3634 O  O   . ALA B  188 ? 0.1357 0.1723 0.1638 -0.0058 0.0154  0.0063  188 ALA B O   
3635 C  CB  . ALA B  188 ? 0.2032 0.2962 0.1655 -0.0950 -0.0063 0.0968  188 ALA B CB  
3636 N  N   . GLU B  189 ? 0.1465 0.1415 0.1466 -0.0223 0.0108  0.0397  189 GLU B N   
3637 C  CA  . GLU B  189 ? 0.1306 0.1220 0.1547 -0.0146 0.0184  0.0284  189 GLU B CA  
3638 C  C   . GLU B  189 ? 0.1177 0.1279 0.1254 -0.0018 0.0162  0.0178  189 GLU B C   
3639 O  O   . GLU B  189 ? 0.1316 0.1404 0.1274 -0.0018 0.0164  0.0196  189 GLU B O   
3640 C  CB  . GLU B  189 ? 0.1762 0.1357 0.1890 -0.0099 0.0049  0.0225  189 GLU B CB  
3641 C  CG  . GLU B  189 ? 0.2556 0.1376 0.2623 -0.0373 -0.0079 0.0476  189 GLU B CG  
3642 C  CD  . GLU B  189 ? 0.3563 0.2026 0.4852 -0.0585 0.0115  -0.0517 189 GLU B CD  
3643 O  OE1 . GLU B  189 ? 0.3231 0.2133 0.4143 -0.0361 0.0401  0.0351  189 GLU B OE1 
3644 O  OE2 . GLU B  189 ? 0.4596 0.2243 0.8041 -0.0635 0.1727  0.0983  189 GLU B OE2 
3645 N  N   . TYR B  190 ? 0.1165 0.1115 0.1285 0.0006  0.0005  0.0244  190 TYR B N   
3646 C  CA  . TYR B  190 ? 0.1134 0.1098 0.1204 0.0060  -0.0062 0.0237  190 TYR B CA  
3647 C  C   . TYR B  190 ? 0.1165 0.1270 0.1111 0.0033  0.0052  0.0215  190 TYR B C   
3648 O  O   . TYR B  190 ? 0.1259 0.1382 0.1149 0.0017  0.0025  0.0313  190 TYR B O   
3649 C  CB  . TYR B  190 ? 0.1176 0.1306 0.1142 0.0121  0.0091  0.0243  190 TYR B CB  
3650 C  CG  . TYR B  190 ? 0.1088 0.1294 0.1262 0.0150  0.0052  0.0321  190 TYR B CG  
3651 C  CD1 . TYR B  190 ? 0.1296 0.1260 0.1123 0.0008  0.0177  0.0198  190 TYR B CD1 
3652 C  CD2 . TYR B  190 ? 0.1213 0.1484 0.1322 0.0006  -0.0029 0.0313  190 TYR B CD2 
3653 C  CE1 . TYR B  190 ? 0.1316 0.1430 0.1242 0.0062  -0.0050 0.0367  190 TYR B CE1 
3654 C  CE2 . TYR B  190 ? 0.1327 0.1367 0.1327 0.0103  0.0162  0.0293  190 TYR B CE2 
3655 C  CZ  . TYR B  190 ? 0.1430 0.1579 0.1216 0.0149  0.0092  0.0383  190 TYR B CZ  
3656 O  OH  . TYR B  190 ? 0.1494 0.1914 0.1323 0.0209  0.0192  0.0233  190 TYR B OH  
3657 N  N   . TYR B  191 ? 0.1062 0.1256 0.1268 0.0013  0.0040  0.0250  191 TYR B N   
3658 C  CA  . TYR B  191 ? 0.1179 0.1148 0.1150 -0.0019 -0.0055 0.0111  191 TYR B CA  
3659 C  C   . TYR B  191 ? 0.1080 0.1263 0.1164 0.0040  0.0049  0.0334  191 TYR B C   
3660 O  O   . TYR B  191 ? 0.1485 0.1391 0.1133 0.0187  -0.0129 0.0201  191 TYR B O   
3661 C  CB  . TYR B  191 ? 0.1118 0.1298 0.1423 0.0030  0.0131  0.0227  191 TYR B CB  
3662 C  CG  . TYR B  191 ? 0.1181 0.1213 0.1337 -0.0044 0.0059  0.0434  191 TYR B CG  
3663 C  CD1 . TYR B  191 ? 0.1341 0.1289 0.1544 0.0147  0.0120  0.0438  191 TYR B CD1 
3664 C  CD2 . TYR B  191 ? 0.1055 0.1289 0.1454 -0.0015 0.0122  0.0284  191 TYR B CD2 
3665 C  CE1 . TYR B  191 ? 0.1195 0.1396 0.1771 0.0178  0.0216  0.0204  191 TYR B CE1 
3666 C  CE2 . TYR B  191 ? 0.1395 0.1285 0.1689 0.0034  0.0216  0.0311  191 TYR B CE2 
3667 C  CZ  . TYR B  191 ? 0.1364 0.1329 0.1731 0.0017  0.0201  0.0179  191 TYR B CZ  
3668 O  OH  . TYR B  191 ? 0.1794 0.1615 0.2471 0.0161  0.0162  -0.0089 191 TYR B OH  
3669 N  N   . ARG B  192 ? 0.1098 0.1195 0.1320 0.0000  0.0013  0.0088  192 ARG B N   
3670 C  CA  . ARG B  192 ? 0.1375 0.1174 0.1067 0.0038  -0.0017 0.0260  192 ARG B CA  
3671 C  C   . ARG B  192 ? 0.1360 0.1473 0.1061 -0.0036 -0.0218 0.0239  192 ARG B C   
3672 O  O   . ARG B  192 ? 0.1506 0.1457 0.1311 -0.0064 -0.0227 0.0339  192 ARG B O   
3673 C  CB  . ARG B  192 ? 0.1420 0.1549 0.1329 0.0113  0.0190  0.0179  192 ARG B CB  
3674 C  CG  . ARG B  192 ? 0.1489 0.1684 0.1483 0.0258  -0.0033 0.0232  192 ARG B CG  
3675 C  CD  . ARG B  192 ? 0.1845 0.2024 0.1360 0.0381  -0.0177 0.0089  192 ARG B CD  
3676 N  NE  . ARG B  192 ? 0.1644 0.1711 0.1604 0.0333  0.0128  0.0279  192 ARG B NE  
3677 C  CZ  . ARG B  192 ? 0.1523 0.1951 0.1336 0.0201  0.0079  0.0403  192 ARG B CZ  
3678 N  NH1 . ARG B  192 ? 0.1938 0.2003 0.1375 0.0482  0.0223  0.0381  192 ARG B NH1 
3679 N  NH2 . ARG B  192 ? 0.1525 0.2178 0.1593 0.0348  0.0111  0.0283  192 ARG B NH2 
3680 N  N   . TYR B  193 ? 0.1254 0.1412 0.1179 -0.0034 -0.0052 0.0199  193 TYR B N   
3681 C  CA  . TYR B  193 ? 0.1397 0.1436 0.1509 -0.0043 -0.0168 0.0204  193 TYR B CA  
3682 C  C   . TYR B  193 ? 0.1578 0.1405 0.1194 -0.0030 -0.0136 -0.0069 193 TYR B C   
3683 O  O   . TYR B  193 ? 0.1430 0.1430 0.1254 0.0128  -0.0089 0.0044  193 TYR B O   
3684 C  CB  . TYR B  193 ? 0.1252 0.1720 0.1602 -0.0002 -0.0267 0.0395  193 TYR B CB  
3685 C  CG  . TYR B  193 ? 0.1381 0.1213 0.1446 0.0023  -0.0289 0.0353  193 TYR B CG  
3686 C  CD1 . TYR B  193 ? 0.1254 0.1298 0.1450 0.0253  -0.0034 0.0171  193 TYR B CD1 
3687 C  CD2 . TYR B  193 ? 0.1207 0.1321 0.1712 0.0153  -0.0212 0.0307  193 TYR B CD2 
3688 C  CE1 . TYR B  193 ? 0.0992 0.1270 0.1548 0.0085  -0.0108 0.0134  193 TYR B CE1 
3689 C  CE2 . TYR B  193 ? 0.1152 0.1278 0.1289 0.0011  -0.0186 0.0140  193 TYR B CE2 
3690 C  CZ  . TYR B  193 ? 0.1082 0.1283 0.1231 -0.0005 -0.0074 0.0137  193 TYR B CZ  
3691 O  OH  . TYR B  193 ? 0.1247 0.1204 0.1427 0.0089  0.0039  0.0220  193 TYR B OH  
3692 N  N   . ARG B  194 ? 0.1944 0.1559 0.1488 -0.0288 -0.0352 0.0184  194 ARG B N   
3693 C  CA  . ARG B  194 ? 0.2119 0.1264 0.1337 -0.0167 -0.0149 -0.0078 194 ARG B CA  
3694 C  C   . ARG B  194 ? 0.1645 0.1285 0.1467 -0.0047 -0.0190 0.0067  194 ARG B C   
3695 O  O   . ARG B  194 ? 0.2037 0.1594 0.1778 -0.0243 -0.0690 0.0290  194 ARG B O   
3696 C  CB  . ARG B  194 ? 0.4369 0.1943 0.1152 -0.0423 0.0209  -0.0021 194 ARG B CB  
3697 C  CG  . ARG B  194 ? 0.5419 0.3431 0.1569 -0.1146 0.0531  -0.1035 194 ARG B CG  
3698 C  CD  . ARG B  194 ? 0.4452 0.6990 0.6502 -0.0948 0.1337  -0.0030 194 ARG B CD  
3699 N  N   . GLY B  195 ? 0.1822 0.1220 0.1318 -0.0043 -0.0210 0.0070  195 GLY B N   
3700 C  CA  . GLY B  195 ? 0.1358 0.1222 0.1555 -0.0148 -0.0216 0.0219  195 GLY B CA  
3701 C  C   . GLY B  195 ? 0.1287 0.1026 0.1349 -0.0064 -0.0128 -0.0093 195 GLY B C   
3702 O  O   . GLY B  195 ? 0.1572 0.1382 0.1313 -0.0019 -0.0002 -0.0140 195 GLY B O   
3703 N  N   . SER B  196 ? 0.1323 0.1106 0.1351 -0.0098 -0.0069 0.0039  196 SER B N   
3704 C  CA  . SER B  196 ? 0.1420 0.0960 0.1324 -0.0089 -0.0201 0.0137  196 SER B CA  
3705 C  C   . SER B  196 ? 0.1107 0.1071 0.1261 0.0077  0.0043  0.0052  196 SER B C   
3706 O  O   . SER B  196 ? 0.1346 0.1027 0.1387 -0.0066 -0.0063 -0.0004 196 SER B O   
3707 C  CB  . SER B  196 ? 0.1595 0.1186 0.1333 -0.0076 -0.0196 -0.0062 196 SER B CB  
3708 O  OG  . SER B  196 ? 0.1226 0.1057 0.1579 -0.0012 -0.0074 -0.0119 196 SER B OG  
3709 N  N   . LEU B  197 ? 0.1152 0.1115 0.1323 0.0082  -0.0087 0.0162  197 LEU B N   
3710 C  CA  . LEU B  197 ? 0.1124 0.1070 0.1348 0.0182  0.0051  0.0103  197 LEU B CA  
3711 C  C   . LEU B  197 ? 0.1019 0.0974 0.1327 0.0023  -0.0039 0.0130  197 LEU B C   
3712 O  O   . LEU B  197 ? 0.1120 0.1139 0.1491 -0.0080 -0.0111 0.0089  197 LEU B O   
3713 C  CB  . LEU B  197 ? 0.1240 0.0971 0.1374 0.0128  -0.0047 0.0035  197 LEU B CB  
3714 C  CG  . LEU B  197 ? 0.1371 0.1128 0.1851 0.0097  -0.0163 0.0179  197 LEU B CG  
3715 C  CD1 . LEU B  197 ? 0.1759 0.2143 0.2456 0.0617  0.0473  0.0780  197 LEU B CD1 
3716 C  CD2 . LEU B  197 ? 0.1788 0.1349 0.2111 0.0461  0.0079  0.0387  197 LEU B CD2 
3717 N  N   . THR B  198 ? 0.1130 0.1064 0.1332 0.0188  0.0034  -0.0055 198 THR B N   
3718 C  CA  . THR B  198 ? 0.0976 0.1156 0.1421 -0.0044 0.0000  0.0061  198 THR B CA  
3719 C  C   . THR B  198 ? 0.1077 0.1274 0.1297 0.0021  -0.0010 0.0061  198 THR B C   
3720 O  O   . THR B  198 ? 0.1149 0.1116 0.1439 -0.0066 -0.0042 0.0065  198 THR B O   
3721 C  CB  . THR B  198 ? 0.1085 0.1097 0.1337 -0.0083 -0.0061 0.0173  198 THR B CB  
3722 O  OG1 . THR B  198 ? 0.0982 0.1031 0.1359 -0.0008 -0.0054 0.0049  198 THR B OG1 
3723 C  CG2 . THR B  198 ? 0.1333 0.1161 0.1310 0.0094  0.0120  0.0194  198 THR B CG2 
3724 N  N   . THR B  199 ? 0.1167 0.1170 0.1358 0.0030  -0.0046 0.0285  199 THR B N   
3725 C  CA  . THR B  199 ? 0.1360 0.0911 0.1235 -0.0053 -0.0144 0.0073  199 THR B CA  
3726 C  C   . THR B  199 ? 0.1055 0.1167 0.1606 0.0163  -0.0036 0.0063  199 THR B C   
3727 O  O   . THR B  199 ? 0.1308 0.1165 0.1538 -0.0041 -0.0008 -0.0062 199 THR B O   
3728 C  CB  . THR B  199 ? 0.1271 0.1134 0.1406 0.0100  -0.0010 0.0057  199 THR B CB  
3729 O  OG1 . THR B  199 ? 0.1327 0.1505 0.1769 0.0200  -0.0142 -0.0178 199 THR B OG1 
3730 C  CG2 . THR B  199 ? 0.1425 0.1182 0.1805 0.0013  -0.0164 -0.0311 199 THR B CG2 
3731 N  N   . PRO B  200 ? 0.1267 0.1017 0.1411 -0.0087 -0.0168 0.0030  200 PRO B N   
3732 C  CA  . PRO B  200 ? 0.1275 0.0931 0.1690 0.0000  -0.0076 0.0146  200 PRO B CA  
3733 C  C   . PRO B  200 ? 0.1419 0.1046 0.1720 0.0006  -0.0170 -0.0055 200 PRO B C   
3734 O  O   . PRO B  200 ? 0.1479 0.1415 0.1811 0.0155  -0.0256 -0.0035 200 PRO B O   
3735 C  CB  . PRO B  200 ? 0.1417 0.1225 0.1696 -0.0095 -0.0057 0.0114  200 PRO B CB  
3736 C  CG  . PRO B  200 ? 0.1344 0.1057 0.1974 -0.0098 -0.0054 -0.0023 200 PRO B CG  
3737 C  CD  . PRO B  200 ? 0.1269 0.1085 0.1635 -0.0186 0.0034  0.0033  200 PRO B CD  
3738 N  N   A PRO B  201 ? 0.1384 0.1339 0.1477 0.0226  -0.0185 -0.0038 201 PRO B N   
3739 N  N   B PRO B  201 ? 0.1391 0.1262 0.1432 0.0207  -0.0177 0.0068  201 PRO B N   
3740 C  CA  A PRO B  201 ? 0.1465 0.0958 0.1439 -0.0016 0.0039  -0.0076 201 PRO B CA  
3741 C  CA  B PRO B  201 ? 0.1573 0.0898 0.1395 0.0348  -0.0179 -0.0046 201 PRO B CA  
3742 C  C   A PRO B  201 ? 0.1455 0.1053 0.1583 0.0118  0.0038  -0.0134 201 PRO B C   
3743 C  C   B PRO B  201 ? 0.1317 0.1133 0.1443 -0.0151 -0.0143 0.0108  201 PRO B C   
3744 O  O   A PRO B  201 ? 0.1472 0.0983 0.1481 -0.0117 0.0237  0.0000  201 PRO B O   
3745 O  O   B PRO B  201 ? 0.1370 0.1118 0.1360 0.0109  -0.0121 -0.0052 201 PRO B O   
3746 C  CB  A PRO B  201 ? 0.1904 0.1167 0.1870 0.0280  0.0201  0.0050  201 PRO B CB  
3747 C  CB  B PRO B  201 ? 0.1665 0.0956 0.2068 0.0233  0.0133  -0.0016 201 PRO B CB  
3748 C  CG  A PRO B  201 ? 0.1978 0.1927 0.2126 0.0534  -0.0403 -0.0311 201 PRO B CG  
3749 C  CG  B PRO B  201 ? 0.1222 0.1377 0.1773 0.0402  -0.0042 0.0010  201 PRO B CG  
3750 C  CD  A PRO B  201 ? 0.1283 0.1270 0.2012 0.0209  0.0367  0.0165  201 PRO B CD  
3751 C  CD  B PRO B  201 ? 0.1606 0.0951 0.1870 0.0309  0.0155  0.0147  201 PRO B CD  
3752 N  N   . CYS B  202 ? 0.1247 0.1019 0.1685 0.0044  0.0019  0.0088  202 CYS B N   
3753 C  CA  . CYS B  202 ? 0.1448 0.1147 0.1602 0.0059  -0.0126 -0.0004 202 CYS B CA  
3754 C  C   . CYS B  202 ? 0.1350 0.0960 0.1548 -0.0076 -0.0133 0.0081  202 CYS B C   
3755 O  O   . CYS B  202 ? 0.1724 0.1070 0.1489 -0.0076 -0.0141 -0.0068 202 CYS B O   
3756 C  CB  . CYS B  202 ? 0.1499 0.1277 0.1650 -0.0156 -0.0012 0.0011  202 CYS B CB  
3757 S  SG  . CYS B  202 ? 0.1355 0.1131 0.1662 0.0029  -0.0089 0.0000  202 CYS B SG  
3758 N  N   A ASN B  203 ? 0.1526 0.1122 0.1671 -0.0006 0.0048  -0.0134 203 ASN B N   
3759 N  N   B ASN B  203 ? 0.1563 0.1197 0.1703 0.0035  0.0041  -0.0073 203 ASN B N   
3760 C  CA  A ASN B  203 ? 0.1666 0.1300 0.1672 -0.0130 -0.0115 -0.0139 203 ASN B CA  
3761 C  CA  B ASN B  203 ? 0.1665 0.1198 0.1815 -0.0064 0.0013  -0.0017 203 ASN B CA  
3762 C  C   A ASN B  203 ? 0.1630 0.0985 0.1506 -0.0033 0.0159  -0.0345 203 ASN B C   
3763 C  C   B ASN B  203 ? 0.1557 0.0951 0.1450 0.0040  0.0141  -0.0261 203 ASN B C   
3764 O  O   A ASN B  203 ? 0.1400 0.0939 0.1473 -0.0030 0.0015  -0.0165 203 ASN B O   
3765 O  O   B ASN B  203 ? 0.1685 0.1076 0.1357 0.0017  -0.0003 -0.0302 203 ASN B O   
3766 C  CB  A ASN B  203 ? 0.2031 0.1190 0.1733 0.0692  0.0248  0.0096  203 ASN B CB  
3767 C  CB  B ASN B  203 ? 0.1789 0.1073 0.2330 0.0256  0.0231  0.0167  203 ASN B CB  
3768 C  CG  A ASN B  203 ? 0.1992 0.1170 0.2290 0.0917  0.0542  0.0063  203 ASN B CG  
3769 C  CG  B ASN B  203 ? 0.1903 0.1627 0.2672 0.0414  0.0257  0.0403  203 ASN B CG  
3770 O  OD1 A ASN B  203 ? 0.2522 0.1335 0.2238 0.0633  0.0201  0.0181  203 ASN B OD1 
3771 O  OD1 B ASN B  203 ? 0.2286 0.1747 0.2751 -0.0100 0.0380  0.0519  203 ASN B OD1 
3772 N  ND2 A ASN B  203 ? 0.3283 0.0983 0.3156 0.0763  0.0386  -0.0020 203 ASN B ND2 
3773 N  ND2 B ASN B  203 ? 0.2255 0.2606 0.2179 0.1243  0.0228  0.0431  203 ASN B ND2 
3774 N  N   . PRO B  204 ? 0.1861 0.1314 0.1472 -0.0059 -0.0136 -0.0287 204 PRO B N   
3775 C  CA  . PRO B  204 ? 0.1668 0.1797 0.1355 -0.0238 -0.0153 -0.0128 204 PRO B CA  
3776 C  C   . PRO B  204 ? 0.1818 0.1330 0.1618 -0.0232 -0.0115 -0.0255 204 PRO B C   
3777 O  O   . PRO B  204 ? 0.2399 0.2057 0.1633 -0.0370 -0.0018 -0.0248 204 PRO B O   
3778 C  CB  . PRO B  204 ? 0.1855 0.1913 0.1759 -0.0603 -0.0314 -0.0245 204 PRO B CB  
3779 C  CG  . PRO B  204 ? 0.2217 0.1872 0.2152 -0.0540 -0.0727 -0.0195 204 PRO B CG  
3780 C  CD  . PRO B  204 ? 0.2594 0.1518 0.1703 -0.0657 -0.0367 -0.0346 204 PRO B CD  
3781 N  N   . THR B  205 ? 0.1633 0.1297 0.1551 -0.0114 -0.0049 -0.0337 205 THR B N   
3782 C  CA  . THR B  205 ? 0.1744 0.1517 0.1879 -0.0018 0.0175  -0.0050 205 THR B CA  
3783 C  C   . THR B  205 ? 0.1455 0.1505 0.1675 0.0075  0.0063  -0.0280 205 THR B C   
3784 O  O   . THR B  205 ? 0.1710 0.1335 0.1970 0.0103  0.0138  -0.0330 205 THR B O   
3785 C  CB  . THR B  205 ? 0.2108 0.1388 0.1929 0.0150  -0.0174 -0.0130 205 THR B CB  
3786 O  OG1 . THR B  205 ? 0.2098 0.1564 0.1835 0.0095  -0.0182 -0.0072 205 THR B OG1 
3787 C  CG2 . THR B  205 ? 0.2312 0.1470 0.2243 -0.0054 0.0060  -0.0367 205 THR B CG2 
3788 N  N   . VAL B  206 ? 0.1503 0.1219 0.1367 0.0006  -0.0013 -0.0189 206 VAL B N   
3789 C  CA  . VAL B  206 ? 0.1400 0.1247 0.1383 -0.0070 -0.0022 -0.0066 206 VAL B CA  
3790 C  C   . VAL B  206 ? 0.1278 0.1306 0.1227 0.0082  -0.0179 -0.0175 206 VAL B C   
3791 O  O   . VAL B  206 ? 0.1371 0.1457 0.1710 -0.0031 -0.0179 0.0080  206 VAL B O   
3792 C  CB  . VAL B  206 ? 0.1315 0.1170 0.1323 0.0070  0.0089  0.0042  206 VAL B CB  
3793 C  CG1 . VAL B  206 ? 0.1301 0.1290 0.1568 -0.0110 0.0001  -0.0186 206 VAL B CG1 
3794 C  CG2 . VAL B  206 ? 0.1356 0.1297 0.1656 0.0164  0.0210  0.0199  206 VAL B CG2 
3795 N  N   . LEU B  207 ? 0.1313 0.1163 0.1111 0.0063  0.0119  -0.0111 207 LEU B N   
3796 C  CA  . LEU B  207 ? 0.1474 0.1200 0.1300 0.0063  0.0143  0.0006  207 LEU B CA  
3797 C  C   . LEU B  207 ? 0.1208 0.1312 0.0951 0.0022  0.0004  0.0039  207 LEU B C   
3798 O  O   . LEU B  207 ? 0.1300 0.1221 0.1271 0.0109  -0.0116 -0.0033 207 LEU B O   
3799 C  CB  . LEU B  207 ? 0.1694 0.1497 0.1406 0.0069  0.0236  -0.0244 207 LEU B CB  
3800 C  CG  . LEU B  207 ? 0.2825 0.2217 0.2045 -0.0399 0.0274  0.0431  207 LEU B CG  
3801 C  CD1 . LEU B  207 ? 0.3838 0.3736 0.2145 -0.0304 -0.0390 0.0334  207 LEU B CD1 
3802 C  CD2 . LEU B  207 ? 0.3403 0.4836 0.2951 0.0149  0.1229  0.0886  207 LEU B CD2 
3803 N  N   . TRP B  208 ? 0.1133 0.1206 0.1220 0.0024  -0.0013 0.0040  208 TRP B N   
3804 C  CA  . TRP B  208 ? 0.1193 0.1094 0.1179 -0.0035 -0.0091 0.0001  208 TRP B CA  
3805 C  C   . TRP B  208 ? 0.1252 0.1168 0.0947 0.0089  -0.0034 0.0111  208 TRP B C   
3806 O  O   . TRP B  208 ? 0.1404 0.1245 0.1185 0.0089  -0.0027 0.0139  208 TRP B O   
3807 C  CB  . TRP B  208 ? 0.1042 0.1228 0.1367 0.0068  -0.0091 0.0152  208 TRP B CB  
3808 C  CG  . TRP B  208 ? 0.1024 0.1051 0.1301 0.0023  -0.0091 0.0013  208 TRP B CG  
3809 C  CD1 . TRP B  208 ? 0.1170 0.1267 0.1128 -0.0037 -0.0065 0.0063  208 TRP B CD1 
3810 C  CD2 . TRP B  208 ? 0.1079 0.1058 0.1158 -0.0010 0.0091  -0.0047 208 TRP B CD2 
3811 N  NE1 . TRP B  208 ? 0.1062 0.1243 0.1258 -0.0009 0.0006  0.0060  208 TRP B NE1 
3812 C  CE2 . TRP B  208 ? 0.1114 0.0964 0.1122 -0.0021 0.0027  -0.0032 208 TRP B CE2 
3813 C  CE3 . TRP B  208 ? 0.0960 0.1159 0.1247 0.0195  -0.0048 -0.0025 208 TRP B CE3 
3814 C  CZ2 . TRP B  208 ? 0.1113 0.1221 0.1249 0.0046  0.0231  -0.0049 208 TRP B CZ2 
3815 C  CZ3 . TRP B  208 ? 0.1170 0.1313 0.1221 0.0006  -0.0025 0.0128  208 TRP B CZ3 
3816 C  CH2 . TRP B  208 ? 0.1272 0.1025 0.1254 0.0015  0.0094  -0.0085 208 TRP B CH2 
3817 N  N   . THR B  209 ? 0.1168 0.0945 0.1186 0.0071  -0.0049 0.0053  209 THR B N   
3818 C  CA  . THR B  209 ? 0.1170 0.0964 0.1179 0.0009  0.0049  0.0089  209 THR B CA  
3819 C  C   . THR B  209 ? 0.1031 0.1138 0.1058 0.0022  -0.0089 0.0215  209 THR B C   
3820 O  O   . THR B  209 ? 0.1412 0.1365 0.1017 0.0301  -0.0034 0.0137  209 THR B O   
3821 C  CB  . THR B  209 ? 0.1170 0.1125 0.1243 0.0098  0.0000  0.0089  209 THR B CB  
3822 O  OG1 . THR B  209 ? 0.1254 0.1476 0.1185 0.0093  0.0176  0.0151  209 THR B OG1 
3823 C  CG2 . THR B  209 ? 0.1290 0.1234 0.1447 -0.0087 -0.0060 0.0330  209 THR B CG2 
3824 N  N   . VAL B  210 ? 0.1023 0.1114 0.1149 0.0117  0.0071  0.0154  210 VAL B N   
3825 C  CA  . VAL B  210 ? 0.1026 0.1064 0.1287 0.0073  0.0204  0.0226  210 VAL B CA  
3826 C  C   . VAL B  210 ? 0.1039 0.1165 0.1087 0.0114  0.0078  0.0176  210 VAL B C   
3827 O  O   . VAL B  210 ? 0.1226 0.1195 0.1137 0.0098  0.0032  0.0270  210 VAL B O   
3828 C  CB  . VAL B  210 ? 0.0994 0.1049 0.1450 -0.0075 0.0040  0.0168  210 VAL B CB  
3829 C  CG1 . VAL B  210 ? 0.1236 0.1175 0.1306 0.0122  0.0150  0.0118  210 VAL B CG1 
3830 C  CG2 . VAL B  210 ? 0.1221 0.1069 0.1513 -0.0171 -0.0018 0.0218  210 VAL B CG2 
3831 N  N   . PHE B  211 ? 0.1106 0.1091 0.1168 -0.0046 0.0053  0.0150  211 PHE B N   
3832 C  CA  . PHE B  211 ? 0.1098 0.0958 0.1322 -0.0013 -0.0016 0.0209  211 PHE B CA  
3833 C  C   . PHE B  211 ? 0.1104 0.1154 0.1216 0.0031  0.0124  0.0189  211 PHE B C   
3834 O  O   . PHE B  211 ? 0.1140 0.1216 0.1316 0.0125  0.0119  0.0201  211 PHE B O   
3835 C  CB  . PHE B  211 ? 0.1086 0.1224 0.1263 0.0085  -0.0055 0.0159  211 PHE B CB  
3836 C  CG  . PHE B  211 ? 0.1042 0.1080 0.1247 -0.0086 -0.0086 0.0152  211 PHE B CG  
3837 C  CD1 . PHE B  211 ? 0.1073 0.1310 0.1507 -0.0149 0.0179  0.0182  211 PHE B CD1 
3838 C  CD2 . PHE B  211 ? 0.1294 0.1084 0.1468 -0.0044 -0.0225 0.0241  211 PHE B CD2 
3839 C  CE1 . PHE B  211 ? 0.1276 0.1399 0.1502 0.0050  0.0059  0.0139  211 PHE B CE1 
3840 C  CE2 . PHE B  211 ? 0.1435 0.1152 0.1757 -0.0029 -0.0054 0.0329  211 PHE B CE2 
3841 C  CZ  . PHE B  211 ? 0.1316 0.1707 0.1822 0.0037  0.0137  0.0060  211 PHE B CZ  
3842 N  N   . ARG B  212 ? 0.1216 0.1110 0.1419 0.0081  -0.0085 0.0350  212 ARG B N   
3843 C  CA  . ARG B  212 ? 0.1314 0.1188 0.1206 0.0148  -0.0015 0.0254  212 ARG B CA  
3844 C  C   . ARG B  212 ? 0.1348 0.1109 0.1377 0.0158  0.0142  0.0351  212 ARG B C   
3845 O  O   . ARG B  212 ? 0.1597 0.1430 0.1572 0.0205  0.0159  0.0239  212 ARG B O   
3846 C  CB  . ARG B  212 ? 0.1588 0.1049 0.1511 0.0263  0.0057  0.0458  212 ARG B CB  
3847 C  CG  . ARG B  212 ? 0.1728 0.1339 0.1488 0.0211  0.0018  0.0348  212 ARG B CG  
3848 C  CD  . ARG B  212 ? 0.1976 0.1394 0.1763 0.0332  -0.0004 0.0705  212 ARG B CD  
3849 N  NE  . ARG B  212 ? 0.2165 0.1637 0.1919 0.0785  -0.0215 0.0425  212 ARG B NE  
3850 C  CZ  . ARG B  212 ? 0.2457 0.2009 0.2329 0.0773  -0.0241 0.0547  212 ARG B CZ  
3851 N  NH1 . ARG B  212 ? 0.3125 0.1588 0.2456 0.0517  0.0220  0.0628  212 ARG B NH1 
3852 N  NH2 . ARG B  212 ? 0.2961 0.2342 0.2437 0.1251  -0.0179 0.0632  212 ARG B NH2 
3853 N  N   . ASN B  213 ? 0.1462 0.1012 0.1197 0.0066  -0.0185 0.0223  213 ASN B N   
3854 C  CA  . ASN B  213 ? 0.1819 0.1019 0.1345 -0.0008 -0.0212 0.0215  213 ASN B CA  
3855 C  C   . ASN B  213 ? 0.1459 0.1057 0.1305 0.0062  -0.0065 0.0200  213 ASN B C   
3856 O  O   . ASN B  213 ? 0.1624 0.1036 0.1469 0.0223  0.0041  0.0266  213 ASN B O   
3857 C  CB  . ASN B  213 ? 0.2308 0.1335 0.1827 -0.0547 -0.0074 0.0425  213 ASN B CB  
3858 C  CG  . ASN B  213 ? 0.2535 0.1509 0.2660 -0.0103 -0.0156 0.0745  213 ASN B CG  
3859 O  OD1 . ASN B  213 ? 0.3639 0.2109 0.3782 0.0044  0.0130  0.1667  213 ASN B OD1 
3860 N  ND2 . ASN B  213 ? 0.4238 0.2160 0.3140 0.0285  0.1034  0.1376  213 ASN B ND2 
3861 N  N   . PRO B  214 ? 0.1625 0.1133 0.1226 0.0262  -0.0058 0.0085  214 PRO B N   
3862 C  CA  . PRO B  214 ? 0.1317 0.1346 0.1285 -0.0017 -0.0044 0.0034  214 PRO B CA  
3863 C  C   . PRO B  214 ? 0.1213 0.1028 0.1274 -0.0106 -0.0032 0.0083  214 PRO B C   
3864 O  O   . PRO B  214 ? 0.1632 0.1235 0.1493 -0.0315 -0.0146 0.0240  214 PRO B O   
3865 C  CB  . PRO B  214 ? 0.1408 0.1455 0.1714 0.0083  0.0010  0.0053  214 PRO B CB  
3866 C  CG  . PRO B  214 ? 0.1852 0.1795 0.2084 0.0509  0.0266  0.0211  214 PRO B CG  
3867 C  CD  . PRO B  214 ? 0.1812 0.1724 0.1864 0.0626  0.0127  0.0221  214 PRO B CD  
3868 N  N   . VAL B  215 ? 0.1221 0.1152 0.1208 -0.0039 0.0032  0.0152  215 VAL B N   
3869 C  CA  . VAL B  215 ? 0.1303 0.1007 0.1161 0.0046  -0.0020 0.0062  215 VAL B CA  
3870 C  C   . VAL B  215 ? 0.1191 0.0886 0.1247 -0.0111 -0.0083 -0.0006 215 VAL B C   
3871 O  O   . VAL B  215 ? 0.1266 0.1217 0.1492 -0.0133 0.0100  -0.0152 215 VAL B O   
3872 C  CB  . VAL B  215 ? 0.1204 0.1062 0.1366 -0.0033 0.0103  0.0150  215 VAL B CB  
3873 C  CG1 . VAL B  215 ? 0.1549 0.1736 0.1780 -0.0001 0.0302  -0.0019 215 VAL B CG1 
3874 C  CG2 . VAL B  215 ? 0.1446 0.1155 0.1654 -0.0022 -0.0023 0.0100  215 VAL B CG2 
3875 N  N   . GLN B  216 ? 0.1283 0.0996 0.1134 -0.0024 0.0016  0.0106  216 GLN B N   
3876 C  CA  . GLN B  216 ? 0.1421 0.0983 0.1204 0.0040  0.0041  0.0145  216 GLN B CA  
3877 C  C   . GLN B  216 ? 0.1104 0.1055 0.1235 0.0034  -0.0023 -0.0107 216 GLN B C   
3878 O  O   . GLN B  216 ? 0.1259 0.1302 0.1381 0.0104  -0.0005 0.0044  216 GLN B O   
3879 C  CB  . GLN B  216 ? 0.1551 0.0942 0.1577 0.0136  -0.0102 0.0085  216 GLN B CB  
3880 C  CG  . GLN B  216 ? 0.1768 0.1107 0.1855 0.0254  -0.0223 0.0106  216 GLN B CG  
3881 C  CD  . GLN B  216 ? 0.1972 0.1261 0.1747 0.0274  -0.0088 0.0212  216 GLN B CD  
3882 O  OE1 . GLN B  216 ? 0.1632 0.1453 0.1822 -0.0003 -0.0184 0.0041  216 GLN B OE1 
3883 N  NE2 . GLN B  216 ? 0.3388 0.1818 0.2275 0.0751  -0.0864 -0.0165 216 GLN B NE2 
3884 N  N   . ILE B  217 ? 0.1350 0.0936 0.1103 0.0026  0.0065  -0.0023 217 ILE B N   
3885 C  CA  . ILE B  217 ? 0.1466 0.0902 0.1150 0.0022  -0.0059 -0.0070 217 ILE B CA  
3886 C  C   . ILE B  217 ? 0.1316 0.0829 0.1269 0.0033  0.0039  0.0025  217 ILE B C   
3887 O  O   . ILE B  217 ? 0.1322 0.0935 0.1351 0.0125  -0.0004 -0.0074 217 ILE B O   
3888 C  CB  . ILE B  217 ? 0.1332 0.0910 0.1464 0.0131  -0.0042 -0.0044 217 ILE B CB  
3889 C  CG1 . ILE B  217 ? 0.1509 0.0842 0.1482 -0.0160 0.0110  -0.0138 217 ILE B CG1 
3890 C  CG2 . ILE B  217 ? 0.1436 0.1001 0.1536 0.0024  0.0104  -0.0163 217 ILE B CG2 
3891 C  CD1 . ILE B  217 ? 0.1990 0.1091 0.1563 -0.0200 -0.0046 -0.0070 217 ILE B CD1 
3892 N  N   . SER B  218 ? 0.1470 0.0754 0.1222 0.0061  0.0013  -0.0024 218 SER B N   
3893 C  CA  . SER B  218 ? 0.1429 0.0971 0.1299 0.0021  0.0072  -0.0287 218 SER B CA  
3894 C  C   . SER B  218 ? 0.1482 0.1025 0.1326 0.0188  0.0043  0.0066  218 SER B C   
3895 O  O   . SER B  218 ? 0.1553 0.1001 0.1435 0.0069  0.0114  0.0030  218 SER B O   
3896 C  CB  . SER B  218 ? 0.1698 0.1012 0.1405 0.0055  -0.0216 -0.0102 218 SER B CB  
3897 O  OG  . SER B  218 ? 0.1894 0.1116 0.1414 0.0095  -0.0066 -0.0003 218 SER B OG  
3898 N  N   . GLN B  219 ? 0.1458 0.1366 0.1353 0.0110  0.0129  -0.0055 219 GLN B N   
3899 C  CA  . GLN B  219 ? 0.1716 0.1258 0.1841 0.0296  0.0239  0.0223  219 GLN B CA  
3900 C  C   . GLN B  219 ? 0.1576 0.1439 0.1521 0.0168  0.0263  -0.0073 219 GLN B C   
3901 O  O   . GLN B  219 ? 0.1817 0.1379 0.1495 -0.0003 0.0197  -0.0071 219 GLN B O   
3902 C  CB  . GLN B  219 ? 0.2305 0.1856 0.1884 0.0736  0.0805  0.0420  219 GLN B CB  
3903 C  CG  . GLN B  219 ? 0.2032 0.2949 0.3057 0.1060  0.0789  0.0615  219 GLN B CG  
3904 C  CD  . GLN B  219 ? 0.4160 0.4843 0.2849 -0.0127 -0.0635 0.0491  219 GLN B CD  
3905 O  OE1 . GLN B  219 ? 0.3389 0.3286 0.4305 0.0616  0.0040  0.0284  219 GLN B OE1 
3906 N  NE2 . GLN B  219 ? 0.2860 0.3701 0.2721 0.0729  -0.0023 -0.0225 219 GLN B NE2 
3907 N  N   . GLU B  220 ? 0.1813 0.1523 0.1263 0.0185  0.0218  -0.0133 220 GLU B N   
3908 C  CA  . GLU B  220 ? 0.2050 0.1590 0.1406 0.0245  0.0031  -0.0026 220 GLU B CA  
3909 C  C   . GLU B  220 ? 0.1692 0.1218 0.1537 0.0011  0.0138  0.0085  220 GLU B C   
3910 O  O   . GLU B  220 ? 0.2042 0.1324 0.1381 0.0047  0.0279  0.0075  220 GLU B O   
3911 C  CB  . GLU B  220 ? 0.2388 0.1726 0.1561 0.0040  -0.0136 -0.0341 220 GLU B CB  
3912 C  CG  . GLU B  220 ? 0.2721 0.1604 0.1870 0.0458  0.0138  -0.0093 220 GLU B CG  
3913 C  CD  . GLU B  220 ? 0.2913 0.1657 0.1775 0.0000  0.0252  -0.0398 220 GLU B CD  
3914 O  OE1 . GLU B  220 ? 0.2949 0.1691 0.1953 -0.0081 0.0340  -0.0225 220 GLU B OE1 
3915 O  OE2 . GLU B  220 ? 0.5383 0.2190 0.2819 0.0593  0.0871  -0.0473 220 GLU B OE2 
3916 N  N   . GLN B  221 ? 0.1591 0.1350 0.1219 -0.0013 0.0230  -0.0160 221 GLN B N   
3917 C  CA  . GLN B  221 ? 0.1507 0.1152 0.1238 0.0067  0.0198  -0.0041 221 GLN B CA  
3918 C  C   . GLN B  221 ? 0.1466 0.1150 0.1394 0.0032  0.0249  0.0033  221 GLN B C   
3919 O  O   . GLN B  221 ? 0.1678 0.1062 0.1580 0.0039  0.0273  0.0103  221 GLN B O   
3920 C  CB  . GLN B  221 ? 0.1532 0.1213 0.1326 -0.0100 0.0146  -0.0057 221 GLN B CB  
3921 C  CG  . GLN B  221 ? 0.1453 0.1351 0.1410 0.0067  0.0010  0.0011  221 GLN B CG  
3922 C  CD  . GLN B  221 ? 0.1313 0.0939 0.1249 -0.0013 -0.0089 -0.0037 221 GLN B CD  
3923 O  OE1 . GLN B  221 ? 0.1464 0.1016 0.1424 0.0076  -0.0116 -0.0017 221 GLN B OE1 
3924 N  NE2 . GLN B  221 ? 0.1489 0.1122 0.1553 0.0086  -0.0098 -0.0016 221 GLN B NE2 
3925 N  N   . LEU B  222 ? 0.1282 0.1146 0.1379 -0.0100 0.0124  -0.0009 222 LEU B N   
3926 C  CA  . LEU B  222 ? 0.1381 0.1219 0.1512 0.0033  0.0188  0.0054  222 LEU B CA  
3927 C  C   . LEU B  222 ? 0.1669 0.1131 0.1483 -0.0083 0.0342  -0.0091 222 LEU B C   
3928 O  O   . LEU B  222 ? 0.1632 0.1134 0.1600 0.0024  0.0300  -0.0036 222 LEU B O   
3929 C  CB  . LEU B  222 ? 0.1537 0.1300 0.1546 -0.0149 0.0096  -0.0032 222 LEU B CB  
3930 C  CG  . LEU B  222 ? 0.1557 0.1199 0.1491 -0.0106 0.0067  0.0111  222 LEU B CG  
3931 C  CD1 . LEU B  222 ? 0.1940 0.1347 0.1744 -0.0117 -0.0036 0.0144  222 LEU B CD1 
3932 C  CD2 . LEU B  222 ? 0.2012 0.1615 0.1654 -0.0124 0.0004  -0.0341 222 LEU B CD2 
3933 N  N   . LEU B  223 ? 0.1613 0.1341 0.1403 -0.0038 0.0283  0.0074  223 LEU B N   
3934 C  CA  . LEU B  223 ? 0.1985 0.1279 0.1503 0.0164  0.0500  0.0130  223 LEU B CA  
3935 C  C   . LEU B  223 ? 0.1748 0.1615 0.1511 0.0027  0.0374  -0.0064 223 LEU B C   
3936 O  O   . LEU B  223 ? 0.2046 0.1481 0.1870 -0.0066 0.0465  0.0226  223 LEU B O   
3937 C  CB  . LEU B  223 ? 0.2352 0.1383 0.1591 -0.0037 0.0418  0.0013  223 LEU B CB  
3938 C  CG  . LEU B  223 ? 0.2261 0.1844 0.2024 0.0157  0.0726  0.0323  223 LEU B CG  
3939 C  CD1 . LEU B  223 ? 0.2404 0.2091 0.2441 0.0351  0.0713  0.0307  223 LEU B CD1 
3940 C  CD2 . LEU B  223 ? 0.3276 0.2851 0.1621 0.0066  0.0719  -0.0526 223 LEU B CD2 
3941 N  N   . ALA B  224 ? 0.1993 0.1606 0.1508 0.0115  0.0314  0.0130  224 ALA B N   
3942 C  CA  . ALA B  224 ? 0.1936 0.1600 0.1822 0.0386  0.0348  0.0200  224 ALA B CA  
3943 C  C   . ALA B  224 ? 0.2254 0.1588 0.1908 0.0013  0.0666  0.0322  224 ALA B C   
3944 O  O   . ALA B  224 ? 0.2761 0.1425 0.2085 0.0306  0.0540  0.0478  224 ALA B O   
3945 C  CB  . ALA B  224 ? 0.1958 0.2196 0.2208 0.0302  0.0294  0.0281  224 ALA B CB  
3946 N  N   . LEU B  225 ? 0.1931 0.1307 0.1714 0.0138  0.0342  0.0020  225 LEU B N   
3947 C  CA  . LEU B  225 ? 0.1608 0.1276 0.1638 -0.0012 0.0417  0.0153  225 LEU B CA  
3948 C  C   . LEU B  225 ? 0.1650 0.1168 0.1885 0.0023  0.0294  -0.0193 225 LEU B C   
3949 O  O   . LEU B  225 ? 0.2275 0.1159 0.2441 -0.0089 0.0872  0.0103  225 LEU B O   
3950 C  CB  . LEU B  225 ? 0.1741 0.1411 0.1498 -0.0121 0.0441  -0.0021 225 LEU B CB  
3951 C  CG  . LEU B  225 ? 0.1591 0.1547 0.1753 0.0035  0.0363  -0.0012 225 LEU B CG  
3952 C  CD1 . LEU B  225 ? 0.2000 0.1661 0.1970 0.0226  0.0153  -0.0484 225 LEU B CD1 
3953 C  CD2 . LEU B  225 ? 0.1916 0.1745 0.1717 -0.0251 0.0379  -0.0030 225 LEU B CD2 
3954 N  N   . GLU B  226 ? 0.1710 0.1292 0.1573 0.0087  0.0527  0.0100  226 GLU B N   
3955 C  CA  . GLU B  226 ? 0.1894 0.1297 0.1735 -0.0062 0.0586  0.0181  226 GLU B CA  
3956 C  C   . GLU B  226 ? 0.1571 0.1441 0.1633 -0.0127 0.0425  -0.0006 226 GLU B C   
3957 O  O   . GLU B  226 ? 0.2329 0.1965 0.1931 -0.0578 0.0403  0.0173  226 GLU B O   
3958 C  CB  . GLU B  226 ? 0.1827 0.1459 0.1776 0.0043  0.0538  0.0346  226 GLU B CB  
3959 C  CG  . GLU B  226 ? 0.1935 0.1217 0.1691 -0.0220 0.0446  0.0039  226 GLU B CG  
3960 C  CD  . GLU B  226 ? 0.2077 0.1321 0.1644 0.0093  0.0166  -0.0109 226 GLU B CD  
3961 O  OE1 . GLU B  226 ? 0.1831 0.1654 0.1518 0.0239  0.0416  0.0008  226 GLU B OE1 
3962 O  OE2 . GLU B  226 ? 0.2208 0.1581 0.1700 0.0059  0.0046  0.0046  226 GLU B OE2 
3963 N  N   . THR B  227 ? 0.1869 0.1256 0.1649 0.0154  0.0438  0.0166  227 THR B N   
3964 C  CA  . THR B  227 ? 0.2270 0.1522 0.1645 0.0265  0.0554  0.0391  227 THR B CA  
3965 C  C   . THR B  227 ? 0.2671 0.1017 0.2213 0.0130  0.0560  0.0287  227 THR B C   
3966 O  O   . THR B  227 ? 0.3749 0.1801 0.2065 0.0576  0.0621  0.0514  227 THR B O   
3967 C  CB  . THR B  227 ? 0.2280 0.1932 0.1661 0.0204  0.0447  -0.0047 227 THR B CB  
3968 O  OG1 . THR B  227 ? 0.2254 0.1650 0.1903 0.0108  0.0367  0.0051  227 THR B OG1 
3969 C  CG2 . THR B  227 ? 0.2171 0.1818 0.2201 0.0354  0.0478  0.0190  227 THR B CG2 
3970 N  N   . ALA B  228 ? 0.2019 0.1320 0.1823 0.0301  0.0105  0.0104  228 ALA B N   
3971 C  CA  . ALA B  228 ? 0.2515 0.1504 0.2116 0.0475  -0.0236 0.0026  228 ALA B CA  
3972 C  C   . ALA B  228 ? 0.2740 0.1247 0.2135 0.0754  -0.0247 -0.0076 228 ALA B C   
3973 O  O   . ALA B  228 ? 0.3921 0.1475 0.1748 0.0490  -0.0300 0.0130  228 ALA B O   
3974 C  CB  . ALA B  228 ? 0.2248 0.2350 0.2913 0.0592  -0.0435 -0.0358 228 ALA B CB  
3975 N  N   . LEU B  229 ? 0.2432 0.1253 0.1743 -0.0229 0.0139  0.0335  229 LEU B N   
3976 C  CA  . LEU B  229 ? 0.1805 0.1412 0.1617 -0.0127 0.0283  0.0337  229 LEU B CA  
3977 C  C   . LEU B  229 ? 0.2082 0.1408 0.1583 -0.0140 0.0534  0.0148  229 LEU B C   
3978 O  O   . LEU B  229 ? 0.2090 0.1346 0.1661 -0.0057 0.0537  0.0279  229 LEU B O   
3979 C  CB  . LEU B  229 ? 0.2009 0.1844 0.1623 -0.0311 0.0331  0.0181  229 LEU B CB  
3980 C  CG  . LEU B  229 ? 0.2300 0.1642 0.1565 -0.0272 0.0369  0.0252  229 LEU B CG  
3981 C  CD1 . LEU B  229 ? 0.2393 0.2883 0.1633 -0.0528 0.0614  0.0458  229 LEU B CD1 
3982 C  CD2 . LEU B  229 ? 0.2569 0.2396 0.2565 -0.0456 -0.0118 0.0932  229 LEU B CD2 
3983 N  N   . TYR B  230 ? 0.2157 0.1251 0.1881 -0.0166 0.0583  0.0208  230 TYR B N   
3984 C  CA  . TYR B  230 ? 0.2298 0.1062 0.1952 -0.0314 0.0455  0.0243  230 TYR B CA  
3985 C  C   . TYR B  230 ? 0.2001 0.1469 0.1791 -0.0032 0.0439  0.0414  230 TYR B C   
3986 O  O   . TYR B  230 ? 0.1833 0.1484 0.2046 -0.0189 0.0447  0.0250  230 TYR B O   
3987 C  CB  . TYR B  230 ? 0.2550 0.1238 0.1995 -0.0217 0.0892  0.0206  230 TYR B CB  
3988 C  CG  . TYR B  230 ? 0.2253 0.1240 0.1890 -0.0151 0.0447  0.0289  230 TYR B CG  
3989 C  CD1 . TYR B  230 ? 0.2584 0.1627 0.2171 -0.0047 0.0159  0.0240  230 TYR B CD1 
3990 C  CD2 . TYR B  230 ? 0.2629 0.1940 0.1789 0.0061  0.0688  0.0340  230 TYR B CD2 
3991 C  CE1 . TYR B  230 ? 0.3225 0.1561 0.1990 -0.0065 0.0147  0.0263  230 TYR B CE1 
3992 C  CE2 . TYR B  230 ? 0.3055 0.2087 0.2079 0.0190  0.0311  0.0085  230 TYR B CE2 
3993 C  CZ  . TYR B  230 ? 0.3085 0.2124 0.1935 -0.0026 0.0248  -0.0165 230 TYR B CZ  
3994 O  OH  . TYR B  230 ? 0.4325 0.2323 0.2063 0.0456  0.0206  -0.0215 230 TYR B OH  
3995 N  N   . CYS B  231 ? 0.2196 0.1800 0.1778 -0.0260 0.0588  0.0387  231 CYS B N   
3996 C  CA  . CYS B  231 ? 0.2185 0.1689 0.1703 -0.0219 0.0423  0.0366  231 CYS B CA  
3997 C  C   . CYS B  231 ? 0.2267 0.1633 0.1825 -0.0107 0.0425  0.0184  231 CYS B C   
3998 O  O   . CYS B  231 ? 0.2626 0.1734 0.1825 -0.0167 0.0599  0.0205  231 CYS B O   
3999 C  CB  . CYS B  231 ? 0.3094 0.2078 0.2461 -0.0129 0.0111  0.0467  231 CYS B CB  
4000 S  SG  . CYS B  231 ? 0.3464 0.2492 0.3574 -0.0100 -0.0236 0.1106  231 CYS B SG  
4001 N  N   . THR B  232 ? 0.2304 0.1622 0.1762 -0.0026 0.0620  0.0568  232 THR B N   
4002 C  CA  . THR B  232 ? 0.1979 0.1336 0.1893 0.0003  0.0592  0.0286  232 THR B CA  
4003 C  C   . THR B  232 ? 0.2014 0.1757 0.1976 -0.0170 0.0752  0.0418  232 THR B C   
4004 O  O   . THR B  232 ? 0.1995 0.1515 0.2335 -0.0105 0.0763  0.0291  232 THR B O   
4005 C  CB  . THR B  232 ? 0.2064 0.1671 0.1735 -0.0207 0.0693  0.0154  232 THR B CB  
4006 O  OG1 . THR B  232 ? 0.1886 0.1470 0.1961 -0.0022 0.0528  0.0230  232 THR B OG1 
4007 C  CG2 . THR B  232 ? 0.2323 0.1694 0.2291 -0.0230 0.0451  -0.0018 232 THR B CG2 
4008 N  N   . HIS B  233 ? 0.2161 0.1573 0.2039 0.0068  0.0760  0.0519  233 HIS B N   
4009 C  CA  . HIS B  233 ? 0.2139 0.1375 0.2420 0.0081  0.0598  0.0268  233 HIS B CA  
4010 C  C   . HIS B  233 ? 0.2090 0.1414 0.2126 -0.0100 0.0709  0.0540  233 HIS B C   
4011 O  O   . HIS B  233 ? 0.2237 0.1844 0.2481 0.0055  0.0762  0.0877  233 HIS B O   
4012 C  CB  . HIS B  233 ? 0.2913 0.1500 0.3198 0.0088  0.0867  0.0278  233 HIS B CB  
4013 C  CG  . HIS B  233 ? 0.2833 0.1533 0.3414 0.0229  0.0367  0.0163  233 HIS B CG  
4014 N  ND1 . HIS B  233 ? 0.3398 0.4988 0.5043 0.0484  0.0053  -0.1699 233 HIS B ND1 
4015 C  CD2 . HIS B  233 ? 0.2980 0.1775 0.4408 0.0030  0.0921  -0.0436 233 HIS B CD2 
4016 C  CE1 . HIS B  233 ? 0.3359 0.4405 0.5355 0.0701  0.0555  -0.1373 233 HIS B CE1 
4017 N  NE2 . HIS B  233 ? 0.3873 0.2518 0.3799 0.0042  0.1272  -0.0195 233 HIS B NE2 
4018 N  N   . MET B  234 ? 0.2395 0.1402 0.2334 -0.0039 0.0534  0.0472  234 MET B N   
4019 C  CA  . MET B  234 ? 0.2287 0.1878 0.2162 -0.0283 0.0788  0.0356  234 MET B CA  
4020 C  C   . MET B  234 ? 0.2827 0.1612 0.2194 -0.0403 0.0712  0.0208  234 MET B C   
4021 O  O   . MET B  234 ? 0.2673 0.2035 0.2655 -0.0276 0.0878  0.0195  234 MET B O   
4022 C  CB  . MET B  234 ? 0.2383 0.2373 0.2228 -0.0172 0.0501  0.0376  234 MET B CB  
4023 C  CG  . MET B  234 ? 0.2182 0.3158 0.2939 0.0361  0.0390  0.0424  234 MET B CG  
4024 S  SD  . MET B  234 ? 0.2619 0.4723 0.3227 0.0467  0.0110  -0.0115 234 MET B SD  
4025 C  CE  . MET B  234 ? 0.3233 0.5744 0.2080 0.0560  0.0666  -0.0456 234 MET B CE  
4026 N  N   . ASP B  235 ? 0.2415 0.1791 0.2109 -0.0343 0.0343  0.0617  235 ASP B N   
4027 C  CA  . ASP B  235 ? 0.2345 0.2341 0.2327 -0.0350 0.0283  0.1026  235 ASP B CA  
4028 C  C   . ASP B  235 ? 0.2449 0.2192 0.1832 -0.0652 0.0174  0.0722  235 ASP B C   
4029 O  O   . ASP B  235 ? 0.2816 0.2652 0.2703 -0.0991 0.0102  0.1135  235 ASP B O   
4030 C  CB  . ASP B  235 ? 0.4383 0.1949 0.3163 -0.0049 0.0745  0.1146  235 ASP B CB  
4031 C  CG  . ASP B  235 ? 0.4392 0.1754 0.5502 -0.0053 -0.0402 0.0195  235 ASP B CG  
4032 O  OD1 . ASP B  235 ? 0.5824 0.2557 0.5324 0.0908  0.0099  0.0416  235 ASP B OD1 
4033 O  OD2 . ASP B  235 ? 0.8622 0.2082 0.7938 0.1039  -0.0001 0.0835  235 ASP B OD2 
4034 N  N   . ASP B  236 ? 0.2265 0.1852 0.1979 -0.0174 0.0385  0.0233  236 ASP B N   
4035 C  CA  . ASP B  236 ? 0.2194 0.1797 0.1752 -0.0201 0.0264  0.0391  236 ASP B CA  
4036 C  C   . ASP B  236 ? 0.2497 0.1414 0.1852 -0.0155 0.0300  0.0127  236 ASP B C   
4037 O  O   . ASP B  236 ? 0.2394 0.1565 0.2077 -0.0390 0.0313  0.0033  236 ASP B O   
4038 C  CB  . ASP B  236 ? 0.2692 0.2085 0.1739 -0.0299 0.0336  0.0385  236 ASP B CB  
4039 C  CG  . ASP B  236 ? 0.2611 0.1914 0.1976 -0.0311 0.0352  0.0099  236 ASP B CG  
4040 O  OD1 . ASP B  236 ? 0.2676 0.2104 0.2050 -0.0365 0.0340  -0.0023 236 ASP B OD1 
4041 O  OD2 . ASP B  236 ? 0.3473 0.2575 0.2100 -0.0565 0.0458  0.0067  236 ASP B OD2 
4042 N  N   . PRO B  237 ? 0.2438 0.1444 0.1909 -0.0282 0.0331  0.0093  237 PRO B N   
4043 C  CA  . PRO B  237 ? 0.2342 0.1643 0.2037 -0.0413 0.0390  0.0198  237 PRO B CA  
4044 C  C   . PRO B  237 ? 0.2327 0.1847 0.1728 -0.0252 0.0317  0.0217  237 PRO B C   
4045 O  O   . PRO B  237 ? 0.2485 0.2060 0.2024 -0.0182 0.0451  0.0351  237 PRO B O   
4046 C  CB  . PRO B  237 ? 0.2953 0.1593 0.2400 -0.0262 0.0528  0.0501  237 PRO B CB  
4047 C  CG  . PRO B  237 ? 0.3050 0.1806 0.2837 -0.0464 0.0993  0.0143  237 PRO B CG  
4048 C  CD  . PRO B  237 ? 0.2660 0.1395 0.2483 -0.0498 0.0339  0.0096  237 PRO B CD  
4049 N  N   A SER B  238 ? 0.2585 0.1414 0.1572 -0.0277 0.0500  0.0139  238 SER B N   
4050 N  N   B SER B  238 ? 0.2722 0.1202 0.1673 -0.0406 0.0435  0.0374  238 SER B N   
4051 C  CA  A SER B  238 ? 0.2508 0.1513 0.1883 -0.0469 0.0201  0.0490  238 SER B CA  
4052 C  CA  B SER B  238 ? 0.2135 0.1339 0.2258 -0.0325 0.0252  0.0257  238 SER B CA  
4053 C  C   A SER B  238 ? 0.2079 0.1111 0.1773 -0.0192 0.0297  0.0136  238 SER B C   
4054 C  C   B SER B  238 ? 0.1967 0.1355 0.1816 -0.0307 0.0135  0.0059  238 SER B C   
4055 O  O   A SER B  238 ? 0.1936 0.1700 0.1855 -0.0161 0.0032  0.0309  238 SER B O   
4056 O  O   B SER B  238 ? 0.1878 0.1556 0.1788 0.0006  0.0200  0.0055  238 SER B O   
4057 C  CB  A SER B  238 ? 0.2433 0.2036 0.2506 -0.1146 0.0122  0.0673  238 SER B CB  
4058 C  CB  B SER B  238 ? 0.2578 0.2658 0.2847 -0.1275 -0.0174 0.0319  238 SER B CB  
4059 O  OG  A SER B  238 ? 0.3323 0.2324 0.3096 -0.0867 -0.0666 0.0324  238 SER B OG  
4060 O  OG  B SER B  238 ? 0.3519 0.2662 0.2381 -0.1639 -0.0147 0.0346  238 SER B OG  
4061 N  N   . PRO B  239 ? 0.2328 0.1361 0.1645 -0.0244 0.0403  -0.0055 239 PRO B N   
4062 C  CA  . PRO B  239 ? 0.2080 0.1473 0.1929 -0.0552 0.0406  0.0273  239 PRO B CA  
4063 C  C   . PRO B  239 ? 0.1938 0.1444 0.2181 0.0044  0.0646  0.0001  239 PRO B C   
4064 O  O   . PRO B  239 ? 0.2296 0.1757 0.2204 0.0021  0.0589  0.0402  239 PRO B O   
4065 C  CB  . PRO B  239 ? 0.2320 0.2164 0.2021 -0.0877 0.0072  0.0238  239 PRO B CB  
4066 C  CG  . PRO B  239 ? 0.2992 0.2345 0.2189 -0.1172 0.0288  0.0187  239 PRO B CG  
4067 C  CD  . PRO B  239 ? 0.2389 0.1773 0.1599 -0.0477 0.0292  -0.0146 239 PRO B CD  
4068 N  N   . ARG B  240 ? 0.1788 0.1682 0.2071 -0.0163 0.0522  0.0434  240 ARG B N   
4069 C  CA  . ARG B  240 ? 0.2186 0.1676 0.2360 -0.0104 0.0163  0.0577  240 ARG B CA  
4070 C  C   . ARG B  240 ? 0.1806 0.1644 0.2193 0.0001  0.0618  0.0557  240 ARG B C   
4071 O  O   . ARG B  240 ? 0.2014 0.1609 0.2243 0.0033  0.0640  0.0604  240 ARG B O   
4072 C  CB  . ARG B  240 ? 0.2759 0.1878 0.2455 -0.0412 0.0245  0.0567  240 ARG B CB  
4073 C  CG  . ARG B  240 ? 0.3635 0.2855 0.2537 -0.1138 0.0064  0.0273  240 ARG B CG  
4074 C  CD  . ARG B  240 ? 0.3603 0.4474 0.2778 -0.1156 0.0385  -0.0386 240 ARG B CD  
4075 N  NE  . ARG B  240 ? 0.4087 0.6304 0.4730 -0.0231 0.1626  0.0020  240 ARG B NE  
4076 C  CZ  . ARG B  240 ? 0.2446 0.4818 0.4342 -0.0969 0.0621  -0.0452 240 ARG B CZ  
4077 N  NH1 . ARG B  240 ? 0.6115 0.4526 0.5407 -0.2727 0.1724  -0.0203 240 ARG B NH1 
4078 N  NH2 . ARG B  240 ? 0.3313 0.4785 0.6610 -0.0433 0.1967  -0.0967 240 ARG B NH2 
4079 N  N   . GLU B  241 ? 0.2097 0.1652 0.2455 0.0118  0.0715  0.0844  241 GLU B N   
4080 C  CA  . GLU B  241 ? 0.2775 0.1780 0.2016 -0.0044 0.0845  0.0351  241 GLU B CA  
4081 C  C   . GLU B  241 ? 0.2454 0.1645 0.2056 -0.0307 0.0336  0.0387  241 GLU B C   
4082 O  O   . GLU B  241 ? 0.2415 0.1846 0.2542 -0.0458 0.0299  0.0621  241 GLU B O   
4083 C  CB  . GLU B  241 ? 0.3075 0.1905 0.2418 0.0220  0.1088  0.0691  241 GLU B CB  
4084 C  CG  . GLU B  241 ? 0.3235 0.2410 0.2253 0.0122  0.0483  0.0710  241 GLU B CG  
4085 C  CD  . GLU B  241 ? 0.2498 0.4331 0.4353 0.1046  -0.0104 -0.0237 241 GLU B CD  
4086 O  OE1 . GLU B  241 ? 0.3741 0.5365 0.3639 0.1230  -0.0013 -0.0370 241 GLU B OE1 
4087 O  OE2 . GLU B  241 ? 0.4221 0.5404 0.4641 0.0906  -0.0585 -0.0513 241 GLU B OE2 
4088 N  N   . MET B  242 ? 0.2172 0.1463 0.1813 0.0051  0.0513  0.0713  242 MET B N   
4089 C  CA  . MET B  242 ? 0.2281 0.1221 0.1733 -0.0170 0.0337  0.0300  242 MET B CA  
4090 C  C   . MET B  242 ? 0.1773 0.1310 0.1427 -0.0018 0.0435  0.0250  242 MET B C   
4091 O  O   . MET B  242 ? 0.1993 0.1355 0.1525 -0.0264 0.0223  0.0447  242 MET B O   
4092 C  CB  . MET B  242 ? 0.2223 0.1606 0.1566 0.0233  0.0431  0.0340  242 MET B CB  
4093 C  CG  . MET B  242 ? 0.2342 0.1889 0.1676 -0.0024 0.0218  0.0096  242 MET B CG  
4094 S  SD  . MET B  242 ? 0.2191 0.1435 0.1659 -0.0030 0.0402  0.0245  242 MET B SD  
4095 C  CE  . MET B  242 ? 0.2775 0.1227 0.2027 -0.0051 0.0317  0.0267  242 MET B CE  
4096 N  N   . ILE B  243 ? 0.1724 0.1415 0.1485 -0.0088 0.0326  0.0266  243 ILE B N   
4097 C  CA  . ILE B  243 ? 0.1758 0.1396 0.1490 0.0010  0.0350  0.0207  243 ILE B CA  
4098 C  C   . ILE B  243 ? 0.1410 0.1212 0.1553 -0.0099 0.0379  0.0094  243 ILE B C   
4099 O  O   . ILE B  243 ? 0.1540 0.1428 0.1545 -0.0200 0.0455  0.0148  243 ILE B O   
4100 C  CB  . ILE B  243 ? 0.1893 0.1796 0.1625 -0.0075 0.0598  0.0252  243 ILE B CB  
4101 C  CG1 . ILE B  243 ? 0.2248 0.1976 0.1929 -0.0223 0.0846  0.0143  243 ILE B CG1 
4102 C  CG2 . ILE B  243 ? 0.2759 0.1920 0.1375 0.0203  0.0140  0.0044  243 ILE B CG2 
4103 C  CD1 . ILE B  243 ? 0.2773 0.2635 0.2440 -0.0265 0.1345  0.0094  243 ILE B CD1 
4104 N  N   . ASN B  244 ? 0.1286 0.1485 0.1396 0.0113  0.0447  0.0236  244 ASN B N   
4105 C  CA  . ASN B  244 ? 0.1231 0.1309 0.1633 0.0121  0.0425  0.0154  244 ASN B CA  
4106 C  C   . ASN B  244 ? 0.1319 0.1165 0.1360 -0.0083 0.0262  0.0114  244 ASN B C   
4107 O  O   . ASN B  244 ? 0.1142 0.1251 0.1760 -0.0082 0.0230  0.0044  244 ASN B O   
4108 C  CB  . ASN B  244 ? 0.1382 0.1500 0.2012 -0.0019 0.0534  -0.0018 244 ASN B CB  
4109 C  CG  . ASN B  244 ? 0.1461 0.1861 0.2452 -0.0035 0.0403  -0.0409 244 ASN B CG  
4110 O  OD1 . ASN B  244 ? 0.1640 0.1789 0.2667 0.0285  0.0637  -0.0148 244 ASN B OD1 
4111 N  ND2 . ASN B  244 ? 0.2266 0.2586 0.2874 0.0002  0.1373  -0.0460 244 ASN B ND2 
4112 N  N   . ASN B  245 ? 0.1136 0.1093 0.1332 -0.0046 0.0388  0.0083  245 ASN B N   
4113 C  CA  . ASN B  245 ? 0.1143 0.1064 0.1204 -0.0100 0.0130  0.0097  245 ASN B CA  
4114 C  C   . ASN B  245 ? 0.1114 0.0981 0.1230 -0.0131 0.0225  0.0174  245 ASN B C   
4115 O  O   . ASN B  245 ? 0.1175 0.1360 0.1296 0.0103  0.0200  0.0216  245 ASN B O   
4116 C  CB  . ASN B  245 ? 0.1230 0.0938 0.1436 -0.0131 0.0026  0.0174  245 ASN B CB  
4117 C  CG  . ASN B  245 ? 0.1240 0.0930 0.1369 -0.0064 0.0057  0.0249  245 ASN B CG  
4118 O  OD1 . ASN B  245 ? 0.1200 0.1028 0.1757 -0.0093 0.0087  0.0228  245 ASN B OD1 
4119 N  ND2 . ASN B  245 ? 0.1259 0.1198 0.1700 -0.0070 0.0011  -0.0027 245 ASN B ND2 
4120 N  N   . PHE B  246 ? 0.1119 0.1197 0.1330 -0.0140 -0.0006 0.0078  246 PHE B N   
4121 C  CA  . PHE B  246 ? 0.1143 0.0985 0.1211 -0.0152 -0.0069 -0.0018 246 PHE B CA  
4122 C  C   . PHE B  246 ? 0.1018 0.0974 0.1444 0.0008  0.0088  0.0137  246 PHE B C   
4123 O  O   . PHE B  246 ? 0.0858 0.1217 0.1393 -0.0031 -0.0011 0.0032  246 PHE B O   
4124 C  CB  . PHE B  246 ? 0.1231 0.1062 0.1478 -0.0029 0.0142  0.0061  246 PHE B CB  
4125 C  CG  . PHE B  246 ? 0.1131 0.1018 0.1407 -0.0210 -0.0066 0.0082  246 PHE B CG  
4126 C  CD1 . PHE B  246 ? 0.1351 0.0895 0.1489 -0.0145 0.0216  0.0107  246 PHE B CD1 
4127 C  CD2 . PHE B  246 ? 0.1578 0.1086 0.1731 -0.0040 -0.0102 0.0047  246 PHE B CD2 
4128 C  CE1 . PHE B  246 ? 0.1238 0.1307 0.1833 -0.0017 0.0144  0.0122  246 PHE B CE1 
4129 C  CE2 . PHE B  246 ? 0.1373 0.1424 0.1820 -0.0051 -0.0121 0.0077  246 PHE B CE2 
4130 C  CZ  . PHE B  246 ? 0.1451 0.1418 0.1776 -0.0031 0.0137  0.0157  246 PHE B CZ  
4131 N  N   . ARG B  247 ? 0.0930 0.1001 0.1292 -0.0070 -0.0015 0.0058  247 ARG B N   
4132 C  CA  . ARG B  247 ? 0.1003 0.0872 0.1404 -0.0093 -0.0005 0.0027  247 ARG B CA  
4133 C  C   . ARG B  247 ? 0.1012 0.0877 0.1301 -0.0066 0.0000  0.0115  247 ARG B C   
4134 O  O   . ARG B  247 ? 0.1044 0.0930 0.1504 -0.0027 -0.0044 0.0176  247 ARG B O   
4135 C  CB  . ARG B  247 ? 0.0987 0.1202 0.1412 -0.0154 -0.0043 -0.0040 247 ARG B CB  
4136 C  CG  . ARG B  247 ? 0.1089 0.1110 0.1441 -0.0115 0.0003  -0.0100 247 ARG B CG  
4137 C  CD  . ARG B  247 ? 0.1287 0.0828 0.1492 -0.0043 -0.0113 0.0029  247 ARG B CD  
4138 N  NE  . ARG B  247 ? 0.1112 0.1112 0.1400 -0.0063 0.0004  0.0008  247 ARG B NE  
4139 C  CZ  . ARG B  247 ? 0.1159 0.0933 0.1362 -0.0135 -0.0057 0.0133  247 ARG B CZ  
4140 N  NH1 . ARG B  247 ? 0.1281 0.1040 0.1606 0.0066  0.0094  0.0195  247 ARG B NH1 
4141 N  NH2 . ARG B  247 ? 0.1330 0.1009 0.1586 -0.0030 -0.0260 0.0140  247 ARG B NH2 
4142 N  N   . GLN B  248 ? 0.0906 0.1025 0.1391 -0.0026 -0.0008 0.0135  248 GLN B N   
4143 C  CA  . GLN B  248 ? 0.0826 0.1194 0.1346 -0.0036 -0.0121 0.0178  248 GLN B CA  
4144 C  C   . GLN B  248 ? 0.1001 0.0992 0.1235 -0.0038 -0.0132 0.0110  248 GLN B C   
4145 O  O   . GLN B  248 ? 0.1048 0.1124 0.1319 -0.0020 -0.0013 0.0135  248 GLN B O   
4146 C  CB  . GLN B  248 ? 0.0920 0.1026 0.1446 0.0036  -0.0020 0.0184  248 GLN B CB  
4147 C  CG  . GLN B  248 ? 0.1253 0.1168 0.1449 -0.0107 0.0105  0.0096  248 GLN B CG  
4148 C  CD  . GLN B  248 ? 0.1140 0.1195 0.1357 0.0168  0.0006  0.0248  248 GLN B CD  
4149 O  OE1 . GLN B  248 ? 0.1195 0.1127 0.1564 0.0099  -0.0017 0.0116  248 GLN B OE1 
4150 N  NE2 . GLN B  248 ? 0.1179 0.1400 0.1717 0.0192  -0.0156 0.0139  248 GLN B NE2 
4151 N  N   . VAL B  249 ? 0.0958 0.1176 0.1181 -0.0054 -0.0088 0.0243  249 VAL B N   
4152 C  CA  . VAL B  249 ? 0.1185 0.1027 0.1398 0.0052  -0.0161 0.0076  249 VAL B CA  
4153 C  C   . VAL B  249 ? 0.0972 0.1078 0.1462 -0.0114 -0.0117 0.0076  249 VAL B C   
4154 O  O   . VAL B  249 ? 0.1127 0.1188 0.1533 -0.0049 -0.0066 0.0140  249 VAL B O   
4155 C  CB  . VAL B  249 ? 0.1265 0.0951 0.1623 -0.0047 -0.0168 0.0209  249 VAL B CB  
4156 C  CG1 . VAL B  249 ? 0.1361 0.1200 0.1514 -0.0189 -0.0115 0.0162  249 VAL B CG1 
4157 C  CG2 . VAL B  249 ? 0.1337 0.1152 0.2224 0.0049  -0.0335 0.0342  249 VAL B CG2 
4158 N  N   . GLN B  250 ? 0.1227 0.1106 0.1278 -0.0136 -0.0124 0.0107  250 GLN B N   
4159 C  CA  . GLN B  250 ? 0.1082 0.1052 0.1272 0.0110  -0.0256 0.0029  250 GLN B CA  
4160 C  C   . GLN B  250 ? 0.1125 0.1299 0.1418 -0.0204 -0.0080 0.0225  250 GLN B C   
4161 O  O   . GLN B  250 ? 0.1479 0.1264 0.1565 -0.0103 -0.0072 0.0248  250 GLN B O   
4162 C  CB  . GLN B  250 ? 0.1203 0.1143 0.1442 0.0023  0.0029  0.0179  250 GLN B CB  
4163 C  CG  . GLN B  250 ? 0.1113 0.1220 0.1866 -0.0219 -0.0142 0.0400  250 GLN B CG  
4164 C  CD  . GLN B  250 ? 0.1183 0.0928 0.1549 -0.0039 -0.0179 0.0019  250 GLN B CD  
4165 O  OE1 . GLN B  250 ? 0.1335 0.1116 0.1586 -0.0050 -0.0145 0.0073  250 GLN B OE1 
4166 N  NE2 . GLN B  250 ? 0.1194 0.1106 0.1552 0.0021  -0.0064 0.0103  250 GLN B NE2 
4167 N  N   . LYS B  251 ? 0.1122 0.1527 0.1396 0.0131  -0.0189 -0.0038 251 LYS B N   
4168 C  CA  . LYS B  251 ? 0.1315 0.1822 0.1332 -0.0066 -0.0077 -0.0024 251 LYS B CA  
4169 C  C   . LYS B  251 ? 0.1211 0.1456 0.1443 0.0063  -0.0185 0.0073  251 LYS B C   
4170 O  O   . LYS B  251 ? 0.1445 0.1466 0.1746 0.0058  -0.0057 0.0155  251 LYS B O   
4171 C  CB  . LYS B  251 ? 0.1158 0.2438 0.1800 -0.0198 -0.0148 -0.0247 251 LYS B CB  
4172 C  CG  . LYS B  251 ? 0.1611 0.2721 0.1991 0.0297  0.0205  0.0260  251 LYS B CG  
4173 C  CD  . LYS B  251 ? 0.1855 0.3195 0.1655 0.0332  0.0219  0.0398  251 LYS B CD  
4174 C  CE  . LYS B  251 ? 0.1567 0.2541 0.1565 0.0046  0.0099  0.0170  251 LYS B CE  
4175 N  NZ  . LYS B  251 ? 0.1416 0.1685 0.1402 -0.0032 -0.0076 0.0227  251 LYS B NZ  
4176 N  N   . PHE B  252 ? 0.1355 0.1842 0.1516 0.0024  -0.0057 0.0319  252 PHE B N   
4177 C  CA  . PHE B  252 ? 0.1682 0.2043 0.1762 -0.0249 -0.0133 0.0671  252 PHE B CA  
4178 C  C   . PHE B  252 ? 0.3772 0.3482 0.2798 -0.0883 0.0462  0.0038  252 PHE B C   
4179 O  O   . PHE B  252 ? 0.2926 0.3176 0.3497 0.0077  0.0036  0.0626  252 PHE B O   
4180 C  CB  . PHE B  252 ? 0.1993 0.2179 0.2751 -0.0212 0.0270  -0.0273 252 PHE B CB  
4181 C  CG  . PHE B  252 ? 0.1861 0.2283 0.1905 -0.0387 -0.0373 0.0457  252 PHE B CG  
4182 C  CD1 . PHE B  252 ? 0.2278 0.2192 0.2552 -0.0710 -0.0662 0.0680  252 PHE B CD1 
4183 C  CD2 . PHE B  252 ? 0.2179 0.2582 0.1972 -0.0211 -0.0527 0.0321  252 PHE B CD2 
4184 C  CE1 . PHE B  252 ? 0.2319 0.3234 0.2843 -0.0550 -0.0475 0.0959  252 PHE B CE1 
4185 C  CE2 . PHE B  252 ? 0.2112 0.2847 0.3400 -0.0022 -0.0727 0.0809  252 PHE B CE2 
4186 C  CZ  . PHE B  252 ? 0.2824 0.3179 0.2602 -0.0417 -0.0780 0.0528  252 PHE B CZ  
4187 N  N   . ASP B  253 ? 0.2478 0.3615 0.2314 -0.0833 -0.0190 -0.0085 253 ASP B N   
4188 C  CA  . ASP B  253 ? 0.2579 0.2796 0.3204 -0.0160 0.0027  0.0148  253 ASP B CA  
4189 C  C   . ASP B  253 ? 0.3850 0.4254 0.2626 -0.0785 -0.0131 -0.0451 253 ASP B C   
4190 O  O   . ASP B  253 ? 0.5800 0.5077 0.3394 0.0000  0.0475  -0.0882 253 ASP B O   
4191 C  CB  . ASP B  253 ? 0.6269 0.3355 0.4291 -0.0039 0.0728  0.0674  253 ASP B CB  
4192 C  CG  . ASP B  253 ? 0.4997 0.6950 0.4225 0.1143  -0.0732 0.2813  253 ASP B CG  
4193 O  OD1 . ASP B  253 ? 0.4189 0.5698 0.4690 0.0989  0.0523  0.1077  253 ASP B OD1 
4194 O  OD2 . ASP B  253 ? 0.5303 0.6167 0.6390 0.1438  -0.2564 0.1074  253 ASP B OD2 
4195 N  N   . GLU B  254 ? 0.3043 0.3755 0.2755 -0.1430 -0.0228 -0.0375 254 GLU B N   
4196 C  CA  . GLU B  254 ? 0.3425 0.4399 0.3021 -0.1564 -0.0219 -0.0299 254 GLU B CA  
4197 C  C   . GLU B  254 ? 0.3031 0.3644 0.3708 -0.1115 -0.0914 0.1687  254 GLU B C   
4198 O  O   . GLU B  254 ? 0.3582 0.4420 0.3281 -0.0855 0.0170  0.1544  254 GLU B O   
4199 N  N   . ARG B  255 ? 0.2322 0.3480 0.4034 -0.0358 -0.0785 0.0584  255 ARG B N   
4200 C  CA  . ARG B  255 ? 0.2079 0.2685 0.2468 -0.0150 -0.0306 0.0035  255 ARG B CA  
4201 C  C   . ARG B  255 ? 0.2416 0.2803 0.3204 0.0104  -0.0453 -0.0624 255 ARG B C   
4202 O  O   . ARG B  255 ? 0.1946 0.3484 0.4468 -0.0131 -0.0078 -0.0575 255 ARG B O   
4203 C  CB  . ARG B  255 ? 0.3427 0.3195 0.2223 0.0418  0.0574  0.1034  255 ARG B CB  
4204 C  CG  . ARG B  255 ? 0.3356 0.3796 0.2540 0.0143  -0.0573 0.0957  255 ARG B CG  
4205 C  CD  . ARG B  255 ? 0.2138 0.4107 0.1908 0.0488  -0.0391 0.0400  255 ARG B CD  
4206 N  NE  . ARG B  255 ? 0.2532 0.3664 0.2484 -0.0728 -0.0184 0.0620  255 ARG B NE  
4207 C  CZ  . ARG B  255 ? 0.2029 0.4021 0.2391 0.0085  -0.0468 0.0663  255 ARG B CZ  
4208 N  NH1 . ARG B  255 ? 0.2039 0.1755 0.2441 -0.0099 -0.0746 0.0281  255 ARG B NH1 
4209 N  NH2 . ARG B  255 ? 0.2133 0.2603 0.1975 0.0958  -0.0168 0.0070  255 ARG B NH2 
4210 N  N   . LEU B  256 ? 0.2172 0.2907 0.3170 -0.0164 -0.0604 -0.0394 256 LEU B N   
4211 C  CA  . LEU B  256 ? 0.2807 0.2684 0.2516 0.0362  -0.1057 -0.0267 256 LEU B CA  
4212 C  C   . LEU B  256 ? 0.2473 0.1908 0.2300 0.0241  -0.0867 -0.0002 256 LEU B C   
4213 O  O   . LEU B  256 ? 0.2885 0.1982 0.3379 -0.0131 -0.1257 -0.0126 256 LEU B O   
4214 C  CB  . LEU B  256 ? 0.2385 0.3301 0.2434 0.0321  -0.0664 -0.0550 256 LEU B CB  
4215 C  CG  . LEU B  256 ? 0.2785 0.3139 0.2068 -0.0091 -0.0723 -0.0069 256 LEU B CG  
4216 C  CD1 . LEU B  256 ? 0.3401 0.5171 0.2781 -0.1073 -0.0167 0.0186  256 LEU B CD1 
4217 C  CD2 . LEU B  256 ? 0.2530 0.4557 0.3236 0.1137  -0.0959 -0.0008 256 LEU B CD2 
4218 N  N   . VAL B  257 ? 0.2215 0.2141 0.1980 -0.0432 -0.0686 0.0436  257 VAL B N   
4219 C  CA  . VAL B  257 ? 0.1592 0.1735 0.1934 -0.0231 -0.0506 0.0383  257 VAL B CA  
4220 C  C   . VAL B  257 ? 0.1509 0.1958 0.1973 0.0076  -0.0403 0.0809  257 VAL B C   
4221 O  O   . VAL B  257 ? 0.1571 0.1958 0.2478 -0.0018 -0.0423 0.0840  257 VAL B O   
4222 C  CB  . VAL B  257 ? 0.1361 0.1848 0.2414 -0.0184 -0.0168 0.0480  257 VAL B CB  
4223 C  CG1 . VAL B  257 ? 0.1419 0.2407 0.2115 -0.0037 -0.0477 0.0237  257 VAL B CG1 
4224 C  CG2 . VAL B  257 ? 0.1811 0.1917 0.2256 -0.0422 -0.0055 0.0400  257 VAL B CG2 
4225 N  N   . TYR B  258 ? 0.1555 0.1750 0.1610 -0.0231 -0.0353 0.0457  258 TYR B N   
4226 C  CA  . TYR B  258 ? 0.1433 0.1643 0.1601 0.0005  -0.0209 0.0294  258 TYR B CA  
4227 C  C   . TYR B  258 ? 0.1364 0.1526 0.1550 -0.0034 -0.0155 0.0455  258 TYR B C   
4228 O  O   . TYR B  258 ? 0.2043 0.1708 0.1693 -0.0170 -0.0536 0.0684  258 TYR B O   
4229 C  CB  . TYR B  258 ? 0.2065 0.2299 0.1596 0.0238  -0.0452 0.0096  258 TYR B CB  
4230 C  CG  . TYR B  258 ? 0.3211 0.2226 0.1485 -0.0103 -0.0391 0.0107  258 TYR B CG  
4231 C  CD1 . TYR B  258 ? 0.3261 0.2771 0.1796 0.0078  -0.1074 0.0062  258 TYR B CD1 
4232 C  CD2 . TYR B  258 ? 0.2638 0.2268 0.2351 0.0050  -0.0819 -0.0204 258 TYR B CD2 
4233 C  CE1 . TYR B  258 ? 0.4191 0.2755 0.3116 -0.0091 -0.1629 -0.0431 258 TYR B CE1 
4234 C  CE2 . TYR B  258 ? 0.3626 0.2642 0.2857 -0.0971 -0.0966 -0.0082 258 TYR B CE2 
4235 C  CZ  . TYR B  258 ? 0.3383 0.3420 0.3080 -0.0225 -0.1632 -0.0641 258 TYR B CZ  
4236 O  OH  . TYR B  258 ? 0.3888 0.3579 0.4023 -0.0854 -0.1587 -0.0460 258 TYR B OH  
4237 N  N   . THR B  259 ? 0.1417 0.1374 0.1540 -0.0211 -0.0098 0.0385  259 THR B N   
4238 C  CA  . THR B  259 ? 0.1554 0.1457 0.1453 0.0002  0.0022  0.0408  259 THR B CA  
4239 C  C   . THR B  259 ? 0.1436 0.1421 0.1252 -0.0091 0.0053  0.0315  259 THR B C   
4240 O  O   . THR B  259 ? 0.1631 0.1928 0.1283 -0.0002 -0.0012 0.0457  259 THR B O   
4241 C  CB  . THR B  259 ? 0.1337 0.1898 0.1406 0.0089  0.0188  0.0564  259 THR B CB  
4242 O  OG1 . THR B  259 ? 0.1634 0.1918 0.1676 0.0333  0.0082  0.0495  259 THR B OG1 
4243 C  CG2 . THR B  259 ? 0.1485 0.2039 0.1716 -0.0189 0.0210  0.0407  259 THR B CG2 
4244 N  N   . SER B  260 ? 0.1231 0.1487 0.1396 0.0064  -0.0038 0.0280  260 SER B N   
4245 C  CA  . SER B  260 ? 0.1231 0.1559 0.1484 0.0000  0.0163  0.0452  260 SER B CA  
4246 C  C   . SER B  260 ? 0.1471 0.1740 0.1276 -0.0187 0.0117  0.0525  260 SER B C   
4247 O  O   . SER B  260 ? 0.1782 0.1918 0.2276 -0.0273 0.0267  0.0710  260 SER B O   
4248 C  CB  . SER B  260 ? 0.1508 0.1978 0.1100 0.0055  -0.0034 0.0276  260 SER B CB  
4249 O  OG  . SER B  260 ? 0.1429 0.1643 0.1316 -0.0048 0.0144  0.0330  260 SER B OG  
4250 N  N   . PHE B  261 ? 0.1554 0.1370 0.1632 0.0067  0.0245  0.0370  261 PHE B N   
4251 C  CA  . PHE B  261 ? 0.1509 0.1480 0.1953 0.0141  -0.0232 0.0351  261 PHE B CA  
4252 C  C   . PHE B  261 ? 0.1649 0.1637 0.1739 0.0065  0.0017  0.0414  261 PHE B C   
4253 O  O   . PHE B  261 ? 0.1688 0.1807 0.1824 -0.0001 0.0026  0.0593  261 PHE B O   
4254 C  CB  . PHE B  261 ? 0.1791 0.1707 0.1715 -0.0170 -0.0042 0.0534  261 PHE B CB  
4255 C  CG  . PHE B  261 ? 0.1870 0.1688 0.1705 0.0226  -0.0059 0.0451  261 PHE B CG  
4256 C  CD1 . PHE B  261 ? 0.2116 0.1208 0.1451 0.0032  -0.0237 0.0271  261 PHE B CD1 
4257 C  CD2 . PHE B  261 ? 0.1995 0.1996 0.1785 0.0333  -0.0005 0.0579  261 PHE B CD2 
4258 C  CE1 . PHE B  261 ? 0.1974 0.2006 0.1408 0.0022  0.0023  0.0190  261 PHE B CE1 
4259 C  CE2 . PHE B  261 ? 0.2174 0.2290 0.1936 0.0231  -0.0037 0.0648  261 PHE B CE2 
4260 C  CZ  . PHE B  261 ? 0.2053 0.2035 0.1662 0.0126  0.0086  0.0356  261 PHE B CZ  
4261 N  N   . SER B  262 ? 0.2533 0.1810 0.2711 -0.0068 -0.0530 0.1040  262 SER B N   
4262 C  CA  . SER B  262 ? 0.3060 0.1502 0.3577 0.0392  -0.0741 0.0930  262 SER B CA  
4263 C  C   . SER B  262 ? 0.3705 0.3127 0.3567 0.2160  -0.1839 -0.0714 262 SER B C   
4264 O  O   . SER B  262 ? 0.3886 0.5802 0.2815 0.1499  -0.1185 -0.0542 262 SER B O   
4265 C  CB  . SER B  262 ? 0.2713 0.4518 0.4660 0.0105  -0.0643 0.2263  262 SER B CB  
4266 O  OG  . SER B  262 ? 0.5896 0.3938 0.4577 -0.0568 -0.1439 0.1137  262 SER B OG  
4267 N  N   . GLN B  263 ? 0.7955 0.7731 0.5881 0.4193  -0.2782 -0.4032 263 GLN B N   
4268 C  CA  . GLN B  263 ? 0.7734 0.2766 0.3756 0.1450  0.0209  -0.0199 263 GLN B CA  
4269 C  C   . GLN B  263 ? 0.5344 0.8229 0.7619 0.1854  -0.1848 0.0704  263 GLN B C   
4270 O  O   . GLN B  263 ? 0.4962 0.5118 0.6248 0.0688  -0.1392 0.3220  263 GLN B O   
4271 C  CB  . GLN B  263 ? 0.9821 0.4982 0.8668 0.3246  0.4738  0.3908  263 GLN B CB  
4272 C  CG  . GLN B  263 ? 0.8579 0.8912 1.0516 0.0431  0.1162  0.3705  263 GLN B CG  
4273 C  CD  . GLN B  263 ? 1.4112 0.4005 1.3501 0.1055  -0.2254 0.4021  263 GLN B CD  
4274 O  OE1 . GLN B  263 ? 0.6445 0.3883 0.6370 0.0044  -0.1590 0.0272  263 GLN B OE1 
4275 N  NE2 . GLN B  263 ? 1.2779 0.5052 2.1281 0.4940  -1.1715 0.0981  263 GLN B NE2 
4276 O  OXT . GLN B  263 ? 0.3640 0.2631 0.2849 0.0055  0.0019  0.0695  263 GLN B OXT 
4277 N  N   . LYS C  3   ? 1.1978 0.9584 1.0615 -0.3463 0.3535  -0.3691 3   LYS C N   
4278 C  CA  . LYS C  3   ? 0.6626 0.4101 0.8707 -0.1742 0.0838  -0.2559 3   LYS C CA  
4279 C  C   . LYS C  3   ? 0.6366 0.4069 0.4434 -0.0111 -0.0218 -0.2332 3   LYS C C   
4280 O  O   . LYS C  3   ? 0.8766 1.0556 0.9313 0.2052  0.2566  -0.0408 3   LYS C O   
4281 C  CB  . LYS C  3   ? 0.7650 0.4673 0.5920 -0.1772 0.2554  -0.3019 3   LYS C CB  
4282 N  N   . TRP C  4   ? 0.4113 0.3664 0.2302 -0.0656 -0.0447 -0.1347 4   TRP C N   
4283 C  CA  . TRP C  4   ? 0.2849 0.2577 0.2237 -0.0675 0.0061  -0.0406 4   TRP C CA  
4284 C  C   . TRP C  4   ? 0.3064 0.2790 0.1963 -0.0429 -0.0142 -0.0458 4   TRP C C   
4285 O  O   . TRP C  4   ? 0.2858 0.3087 0.2221 -0.0347 -0.0381 -0.0564 4   TRP C O   
4286 C  CB  . TRP C  4   ? 0.2669 0.2778 0.1872 -0.0622 0.0193  -0.0616 4   TRP C CB  
4287 C  CG  . TRP C  4   ? 0.2667 0.2145 0.1705 -0.0439 0.0057  -0.0023 4   TRP C CG  
4288 C  CD1 . TRP C  4   ? 0.2539 0.2544 0.2065 -0.0335 0.0254  -0.0065 4   TRP C CD1 
4289 C  CD2 . TRP C  4   ? 0.2284 0.2313 0.1549 -0.0172 -0.0493 -0.0106 4   TRP C CD2 
4290 N  NE1 . TRP C  4   ? 0.2503 0.2463 0.2186 -0.0532 -0.0379 -0.0611 4   TRP C NE1 
4291 C  CE2 . TRP C  4   ? 0.2719 0.2395 0.1506 -0.0126 -0.0284 -0.0208 4   TRP C CE2 
4292 C  CE3 . TRP C  4   ? 0.2788 0.1936 0.1584 -0.0299 -0.0215 -0.0352 4   TRP C CE3 
4293 C  CZ2 . TRP C  4   ? 0.2915 0.2731 0.1312 -0.0242 -0.0374 -0.0397 4   TRP C CZ2 
4294 C  CZ3 . TRP C  4   ? 0.2436 0.2344 0.1155 -0.0421 -0.0262 -0.0139 4   TRP C CZ3 
4295 C  CH2 . TRP C  4   ? 0.2537 0.2791 0.1597 -0.0189 -0.0317 -0.0359 4   TRP C CH2 
4296 N  N   . THR C  5   ? 0.2870 0.2373 0.1929 -0.0343 -0.0080 -0.0580 5   THR C N   
4297 C  CA  . THR C  5   ? 0.3177 0.2259 0.1672 0.0104  -0.0113 -0.0421 5   THR C CA  
4298 C  C   . THR C  5   ? 0.2839 0.2531 0.1463 -0.0128 0.0292  -0.0379 5   THR C C   
4299 O  O   . THR C  5   ? 0.2757 0.2520 0.1441 -0.0399 0.0023  -0.0141 5   THR C O   
4300 C  CB  . THR C  5   ? 0.3351 0.3276 0.2388 -0.0530 0.0370  -0.0928 5   THR C CB  
4301 O  OG1 . THR C  5   ? 0.3389 0.2964 0.2282 -0.0623 0.0289  -0.0593 5   THR C OG1 
4302 C  CG2 . THR C  5   ? 0.4186 0.3727 0.2334 -0.0536 -0.0086 -0.1393 5   THR C CG2 
4303 N  N   . TYR C  6   ? 0.3230 0.2789 0.1306 -0.0290 -0.0188 0.0079  6   TYR C N   
4304 C  CA  . TYR C  6   ? 0.2903 0.2491 0.1675 -0.0060 -0.0001 -0.0421 6   TYR C CA  
4305 C  C   . TYR C  6   ? 0.2927 0.2684 0.1861 0.0037  0.0004  -0.0092 6   TYR C C   
4306 O  O   . TYR C  6   ? 0.3690 0.3265 0.1938 -0.0713 -0.0420 -0.0275 6   TYR C O   
4307 C  CB  . TYR C  6   ? 0.3158 0.2701 0.1482 -0.0115 0.0322  -0.0140 6   TYR C CB  
4308 C  CG  . TYR C  6   ? 0.2306 0.2265 0.1910 -0.0240 0.0098  -0.0032 6   TYR C CG  
4309 C  CD1 . TYR C  6   ? 0.2323 0.2124 0.1785 -0.0306 0.0150  -0.0075 6   TYR C CD1 
4310 C  CD2 . TYR C  6   ? 0.2620 0.2365 0.1728 -0.0376 0.0236  -0.0081 6   TYR C CD2 
4311 C  CE1 . TYR C  6   ? 0.2019 0.1986 0.1847 -0.0313 -0.0033 0.0181  6   TYR C CE1 
4312 C  CE2 . TYR C  6   ? 0.2399 0.2676 0.1592 -0.0348 0.0060  -0.0197 6   TYR C CE2 
4313 C  CZ  . TYR C  6   ? 0.2283 0.2031 0.1495 -0.0534 -0.0307 0.0143  6   TYR C CZ  
4314 O  OH  . TYR C  6   ? 0.2344 0.3107 0.1433 -0.0740 -0.0037 -0.0132 6   TYR C OH  
4315 N  N   . PHE C  7   ? 0.3907 0.3252 0.3181 -0.0039 0.1132  -0.0974 7   PHE C N   
4316 C  CA  . PHE C  7   ? 0.3835 0.3835 0.3495 -0.1090 0.0835  -0.1782 7   PHE C CA  
4317 C  C   . PHE C  7   ? 0.8300 0.2734 0.5316 -0.0748 0.3598  -0.0877 7   PHE C C   
4318 O  O   . PHE C  7   ? 0.3873 0.3260 0.3806 -0.0234 0.0648  -0.0458 7   PHE C O   
4319 C  CB  . PHE C  7   ? 0.5710 0.3867 0.3471 -0.1588 0.0838  -0.1758 7   PHE C CB  
4320 C  CG  . PHE C  7   ? 0.4802 0.5716 0.1756 -0.1593 -0.0428 -0.0740 7   PHE C CG  
4321 C  CD1 . PHE C  7   ? 0.7012 0.5472 0.3671 -0.1315 0.0075  -0.2182 7   PHE C CD1 
4322 C  CD2 . PHE C  7   ? 0.4327 0.7717 0.5189 -0.1934 0.0122  -0.1851 7   PHE C CD2 
4323 C  CE1 . PHE C  7   ? 0.6185 0.4301 0.2857 0.0140  -0.0876 -0.1345 7   PHE C CE1 
4324 C  CE2 . PHE C  7   ? 0.5502 0.6631 0.2324 -0.2118 0.0150  -0.0309 7   PHE C CE2 
4325 C  CZ  . PHE C  7   ? 0.5967 0.7758 0.3975 -0.1745 -0.0189 -0.0811 7   PHE C CZ  
4326 N  N   . GLY C  8   ? 0.4787 0.6245 0.4348 -0.0149 0.0220  0.1344  8   GLY C N   
4327 C  CA  . GLY C  8   ? 0.4656 0.5314 0.3061 -0.1328 -0.0726 -0.0480 8   GLY C CA  
4328 C  C   . GLY C  8   ? 0.4801 0.3619 0.3556 0.0343  -0.0873 -0.0340 8   GLY C C   
4329 O  O   . GLY C  8   ? 0.4791 0.5072 0.4666 0.0289  -0.0409 -0.2298 8   GLY C O   
4330 N  N   . PRO C  9   ? 0.4919 0.3736 0.3272 0.0026  0.1300  -0.1502 9   PRO C N   
4331 C  CA  . PRO C  9   ? 0.3543 0.3538 0.3699 0.0596  0.0347  -0.1096 9   PRO C CA  
4332 C  C   . PRO C  9   ? 0.2818 0.1916 0.3437 -0.0103 0.0036  -0.0725 9   PRO C C   
4333 O  O   . PRO C  9   ? 0.3685 0.2896 0.3389 0.0489  0.0033  -0.0228 9   PRO C O   
4334 C  CB  . PRO C  9   ? 0.4093 0.2907 0.4320 0.0163  -0.0473 -0.1066 9   PRO C CB  
4335 C  CG  . PRO C  9   ? 0.4600 0.4864 0.4414 0.0017  -0.0878 -0.2903 9   PRO C CG  
4336 C  CD  . PRO C  9   ? 0.5496 0.5236 0.3553 -0.0128 0.0347  -0.2255 9   PRO C CD  
4337 N  N   . ASP C  10  ? 0.3086 0.3209 0.2807 -0.0035 0.0021  -0.1105 10  ASP C N   
4338 C  CA  . ASP C  10  ? 0.3297 0.2634 0.2803 -0.0027 -0.0138 -0.0999 10  ASP C CA  
4339 C  C   . ASP C  10  ? 0.3246 0.2004 0.2491 0.0234  -0.0381 -0.0212 10  ASP C C   
4340 O  O   . ASP C  10  ? 0.3353 0.2602 0.2211 -0.0111 -0.0480 -0.1052 10  ASP C O   
4341 C  CB  . ASP C  10  ? 0.4036 0.3219 0.2901 -0.0462 -0.0179 -0.1655 10  ASP C CB  
4342 C  CG  . ASP C  10  ? 0.6684 0.3336 0.3897 -0.0747 -0.0395 -0.1932 10  ASP C CG  
4343 O  OD1 . ASP C  10  ? 0.6980 0.3190 0.3867 -0.1277 0.0018  -0.1168 10  ASP C OD1 
4344 O  OD2 . ASP C  10  ? 0.5795 0.4803 0.4195 -0.0851 -0.0063 -0.2311 10  ASP C OD2 
4345 N  N   . GLY C  11  ? 0.3290 0.3017 0.2544 -0.0485 0.0179  -0.0810 11  GLY C N   
4346 C  CA  . GLY C  11  ? 0.2922 0.2725 0.1629 -0.0018 -0.0204 -0.0428 11  GLY C CA  
4347 C  C   . GLY C  11  ? 0.2025 0.1807 0.1532 -0.0194 -0.0381 -0.0223 11  GLY C C   
4348 O  O   . GLY C  11  ? 0.2256 0.1866 0.1808 -0.0253 -0.0350 -0.0374 11  GLY C O   
4349 N  N   . GLU C  12  ? 0.1936 0.1831 0.1602 -0.0256 -0.0106 -0.0245 12  GLU C N   
4350 C  CA  . GLU C  12  ? 0.1836 0.1364 0.1461 -0.0100 0.0058  -0.0163 12  GLU C CA  
4351 C  C   . GLU C  12  ? 0.1773 0.1544 0.1476 -0.0244 -0.0263 -0.0097 12  GLU C C   
4352 O  O   . GLU C  12  ? 0.1708 0.1571 0.1664 -0.0098 -0.0135 0.0062  12  GLU C O   
4353 C  CB  . GLU C  12  ? 0.1850 0.1676 0.1643 -0.0277 -0.0186 -0.0024 12  GLU C CB  
4354 C  CG  . GLU C  12  ? 0.1688 0.1455 0.1833 -0.0097 -0.0057 -0.0212 12  GLU C CG  
4355 C  CD  . GLU C  12  ? 0.1864 0.1532 0.1419 -0.0216 -0.0124 -0.0143 12  GLU C CD  
4356 O  OE1 . GLU C  12  ? 0.1685 0.1578 0.1451 -0.0088 -0.0084 -0.0029 12  GLU C OE1 
4357 O  OE2 . GLU C  12  ? 0.2527 0.1834 0.1548 -0.0462 -0.0174 -0.0126 12  GLU C OE2 
4358 N  N   . ASN C  13  ? 0.1762 0.1299 0.1606 -0.0217 -0.0159 -0.0042 13  ASN C N   
4359 C  CA  . ASN C  13  ? 0.1670 0.1278 0.1860 -0.0001 -0.0257 0.0182  13  ASN C CA  
4360 C  C   . ASN C  13  ? 0.1754 0.1328 0.1374 -0.0131 -0.0190 0.0011  13  ASN C C   
4361 O  O   . ASN C  13  ? 0.1846 0.1357 0.1782 -0.0177 -0.0266 0.0001  13  ASN C O   
4362 C  CB  . ASN C  13  ? 0.1795 0.1263 0.1938 -0.0215 0.0140  -0.0183 13  ASN C CB  
4363 C  CG  . ASN C  13  ? 0.1562 0.1272 0.1634 -0.0040 -0.0163 -0.0135 13  ASN C CG  
4364 O  OD1 . ASN C  13  ? 0.1706 0.1293 0.1859 -0.0189 -0.0094 -0.0139 13  ASN C OD1 
4365 N  ND2 . ASN C  13  ? 0.1573 0.1593 0.1535 -0.0260 -0.0160 0.0151  13  ASN C ND2 
4366 N  N   . SER C  14  ? 0.1719 0.1293 0.1764 -0.0182 0.0038  -0.0239 14  SER C N   
4367 C  CA  . SER C  14  ? 0.1865 0.1095 0.2104 -0.0233 0.0055  -0.0282 14  SER C CA  
4368 C  C   . SER C  14  ? 0.1872 0.1429 0.1495 -0.0294 -0.0029 -0.0173 14  SER C C   
4369 O  O   . SER C  14  ? 0.2148 0.1359 0.1889 -0.0519 0.0086  -0.0145 14  SER C O   
4370 C  CB  . SER C  14  ? 0.2180 0.1797 0.2808 -0.0369 0.0798  -0.0870 14  SER C CB  
4371 O  OG  . SER C  14  ? 0.2523 0.2777 0.2985 -0.0261 0.0328  -0.0629 14  SER C OG  
4372 N  N   . TRP C  15  ? 0.1673 0.1674 0.1507 -0.0111 -0.0099 -0.0234 15  TRP C N   
4373 C  CA  . TRP C  15  ? 0.1881 0.1500 0.1672 -0.0190 -0.0121 -0.0205 15  TRP C CA  
4374 C  C   . TRP C  15  ? 0.1938 0.1745 0.1591 -0.0188 0.0044  -0.0176 15  TRP C C   
4375 O  O   . TRP C  15  ? 0.1751 0.1732 0.1773 -0.0216 -0.0018 -0.0003 15  TRP C O   
4376 C  CB  . TRP C  15  ? 0.1976 0.1393 0.1593 -0.0190 0.0073  0.0066  15  TRP C CB  
4377 C  CG  . TRP C  15  ? 0.1804 0.1319 0.1561 -0.0160 -0.0119 -0.0247 15  TRP C CG  
4378 C  CD1 . TRP C  15  ? 0.2122 0.1476 0.1624 -0.0351 -0.0057 -0.0078 15  TRP C CD1 
4379 C  CD2 . TRP C  15  ? 0.1643 0.1373 0.1469 -0.0211 -0.0199 -0.0055 15  TRP C CD2 
4380 N  NE1 . TRP C  15  ? 0.1861 0.1438 0.1648 -0.0198 -0.0232 -0.0293 15  TRP C NE1 
4381 C  CE2 . TRP C  15  ? 0.1802 0.1418 0.1644 -0.0241 -0.0110 -0.0232 15  TRP C CE2 
4382 C  CE3 . TRP C  15  ? 0.1810 0.1300 0.1678 -0.0231 -0.0013 -0.0217 15  TRP C CE3 
4383 C  CZ2 . TRP C  15  ? 0.1583 0.1515 0.1665 -0.0139 -0.0244 -0.0279 15  TRP C CZ2 
4384 C  CZ3 . TRP C  15  ? 0.1560 0.1591 0.1277 -0.0261 -0.0151 -0.0219 15  TRP C CZ3 
4385 C  CH2 . TRP C  15  ? 0.1608 0.1724 0.1624 -0.0195 -0.0211 -0.0097 15  TRP C CH2 
4386 N  N   . SER C  16  ? 0.1716 0.1103 0.1725 0.0006  -0.0165 0.0006  16  SER C N   
4387 C  CA  . SER C  16  ? 0.1821 0.1298 0.1698 -0.0275 -0.0047 0.0001  16  SER C CA  
4388 C  C   . SER C  16  ? 0.2157 0.1298 0.1623 -0.0232 -0.0149 0.0046  16  SER C C   
4389 O  O   . SER C  16  ? 0.2163 0.1359 0.1756 -0.0280 -0.0032 0.0044  16  SER C O   
4390 C  CB  . SER C  16  ? 0.1752 0.1397 0.2090 -0.0245 -0.0147 -0.0304 16  SER C CB  
4391 O  OG  . SER C  16  ? 0.1970 0.1445 0.2188 -0.0159 -0.0158 0.0001  16  SER C OG  
4392 N  N   A LYS C  17  ? 0.1866 0.1253 0.1775 -0.0272 -0.0103 -0.0009 17  LYS C N   
4393 N  N   B LYS C  17  ? 0.1965 0.1275 0.1857 -0.0350 -0.0078 -0.0137 17  LYS C N   
4394 C  CA  A LYS C  17  ? 0.1797 0.1360 0.1916 -0.0188 -0.0175 -0.0119 17  LYS C CA  
4395 C  CA  B LYS C  17  ? 0.2004 0.1305 0.1970 -0.0314 -0.0164 -0.0031 17  LYS C CA  
4396 C  C   A LYS C  17  ? 0.1983 0.1251 0.1732 -0.0267 0.0005  -0.0428 17  LYS C C   
4397 C  C   B LYS C  17  ? 0.2262 0.1523 0.1773 -0.0545 -0.0038 -0.0073 17  LYS C C   
4398 O  O   A LYS C  17  ? 0.1852 0.1412 0.1982 0.0006  0.0301  -0.0129 17  LYS C O   
4399 O  O   B LYS C  17  ? 0.2208 0.1194 0.2502 -0.0531 -0.0035 -0.0132 17  LYS C O   
4400 C  CB  A LYS C  17  ? 0.1730 0.1746 0.2117 -0.0034 -0.0177 -0.0410 17  LYS C CB  
4401 C  CB  B LYS C  17  ? 0.1980 0.0623 0.2273 -0.0390 -0.0097 0.0185  17  LYS C CB  
4402 C  CG  A LYS C  17  ? 0.1778 0.2164 0.2036 -0.0044 0.0128  -0.0203 17  LYS C CG  
4403 C  CG  B LYS C  17  ? 0.2015 0.2172 0.2575 -0.0341 -0.0099 -0.0553 17  LYS C CG  
4404 C  CD  A LYS C  17  ? 0.2412 0.2535 0.2041 -0.0553 0.0175  -0.0436 17  LYS C CD  
4405 C  CD  B LYS C  17  ? 0.2746 0.2006 0.2541 0.0089  -0.0031 -0.0260 17  LYS C CD  
4406 C  CE  A LYS C  17  ? 0.2323 0.2293 0.2828 -0.0129 0.0190  0.0697  17  LYS C CE  
4407 C  CE  B LYS C  17  ? 0.3510 0.2611 0.2818 0.0475  0.0087  -0.2034 17  LYS C CE  
4408 N  NZ  A LYS C  17  ? 0.2091 0.2539 0.2868 -0.0223 0.0144  -0.0194 17  LYS C NZ  
4409 N  NZ  B LYS C  17  ? 0.2191 0.4041 0.4482 -0.0370 0.0603  -0.2118 17  LYS C NZ  
4410 N  N   A LYS C  18  ? 0.1949 0.1617 0.1903 -0.0477 -0.0212 -0.0102 18  LYS C N   
4411 N  N   B LYS C  18  ? 0.2128 0.1409 0.1719 -0.0295 -0.0031 -0.0259 18  LYS C N   
4412 C  CA  A LYS C  18  ? 0.2001 0.2033 0.2069 -0.0593 -0.0212 -0.0303 18  LYS C CA  
4413 C  CA  B LYS C  18  ? 0.2043 0.2140 0.1736 -0.0299 -0.0215 -0.0065 18  LYS C CA  
4414 C  C   A LYS C  18  ? 0.2407 0.1978 0.2299 -0.0782 0.0467  -0.0461 18  LYS C C   
4415 C  C   B LYS C  18  ? 0.2030 0.1729 0.1889 -0.0436 0.0087  -0.0207 18  LYS C C   
4416 O  O   A LYS C  18  ? 0.2404 0.1652 0.3028 -0.0690 0.0284  -0.0696 18  LYS C O   
4417 O  O   B LYS C  18  ? 0.2291 0.1694 0.2245 -0.0482 0.0352  -0.0342 18  LYS C O   
4418 C  CB  A LYS C  18  ? 0.3171 0.2499 0.2250 -0.0089 -0.0383 -0.0128 18  LYS C CB  
4419 C  CB  B LYS C  18  ? 0.2079 0.1895 0.1791 0.0019  -0.0231 -0.0568 18  LYS C CB  
4420 C  CG  A LYS C  18  ? 0.3189 0.2883 0.1996 0.0243  -0.0788 -0.0490 18  LYS C CG  
4421 C  CG  B LYS C  18  ? 0.2283 0.2236 0.2241 -0.0579 -0.0348 -0.0324 18  LYS C CG  
4422 C  CD  A LYS C  18  ? 0.3946 0.2746 0.3373 0.0587  -0.0023 -0.0133 18  LYS C CD  
4423 C  CD  B LYS C  18  ? 0.2816 0.2157 0.2540 -0.0462 -0.0505 -0.0192 18  LYS C CD  
4424 C  CE  A LYS C  18  ? 0.4607 0.2812 0.3319 0.1798  -0.0583 0.0412  18  LYS C CE  
4425 C  CE  B LYS C  18  ? 0.2985 0.3580 0.2849 -0.0417 -0.1073 0.0201  18  LYS C CE  
4426 N  NZ  A LYS C  18  ? 0.3278 0.4017 0.5149 0.1861  0.1115  0.2825  18  LYS C NZ  
4427 N  NZ  B LYS C  18  ? 0.4562 0.3118 0.4522 -0.0915 0.0038  -0.1539 18  LYS C NZ  
4428 N  N   . TYR C  19  ? 0.2082 0.1767 0.1970 -0.0330 0.0000  -0.0422 19  TYR C N   
4429 C  CA  . TYR C  19  ? 0.1902 0.1590 0.1958 -0.0307 -0.0132 -0.0179 19  TYR C CA  
4430 C  C   . TYR C  19  ? 0.1749 0.1407 0.1687 -0.0261 -0.0030 -0.0059 19  TYR C C   
4431 O  O   . TYR C  19  ? 0.2048 0.1567 0.1773 -0.0499 0.0175  -0.0296 19  TYR C O   
4432 C  CB  . TYR C  19  ? 0.2104 0.1685 0.2003 -0.0436 -0.0186 -0.0221 19  TYR C CB  
4433 C  CG  . TYR C  19  ? 0.2119 0.1634 0.1943 -0.0465 -0.0222 -0.0162 19  TYR C CG  
4434 C  CD1 . TYR C  19  ? 0.2131 0.1966 0.2415 -0.0710 -0.0026 -0.0105 19  TYR C CD1 
4435 C  CD2 . TYR C  19  ? 0.2193 0.2076 0.1942 -0.0263 0.0006  -0.0223 19  TYR C CD2 
4436 C  CE1 . TYR C  19  ? 0.2821 0.2059 0.2471 -0.0801 -0.0205 -0.0762 19  TYR C CE1 
4437 C  CE2 . TYR C  19  ? 0.2613 0.2107 0.2201 -0.0464 -0.0199 -0.0337 19  TYR C CE2 
4438 C  CZ  . TYR C  19  ? 0.2778 0.2244 0.2213 -0.0525 -0.0353 -0.0438 19  TYR C CZ  
4439 O  OH  . TYR C  19  ? 0.3904 0.2945 0.2109 -0.0409 -0.0664 -0.0672 19  TYR C OH  
4440 N  N   . PRO C  20  ? 0.2147 0.1557 0.1828 -0.0357 0.0050  0.0029  20  PRO C N   
4441 C  CA  . PRO C  20  ? 0.2029 0.1602 0.1797 -0.0077 -0.0060 -0.0121 20  PRO C CA  
4442 C  C   . PRO C  20  ? 0.1592 0.1534 0.2046 -0.0271 0.0092  0.0036  20  PRO C C   
4443 O  O   . PRO C  20  ? 0.1804 0.1492 0.1673 -0.0189 0.0083  0.0038  20  PRO C O   
4444 C  CB  . PRO C  20  ? 0.2538 0.1455 0.2273 -0.0392 0.0216  0.0110  20  PRO C CB  
4445 C  CG  . PRO C  20  ? 0.3578 0.2775 0.2759 -0.1298 -0.0588 0.0917  20  PRO C CG  
4446 C  CD  . PRO C  20  ? 0.2409 0.1611 0.2007 -0.0634 0.0091  0.0080  20  PRO C CD  
4447 N  N   . SER C  21  ? 0.1761 0.1348 0.1694 -0.0196 0.0055  0.0009  21  SER C N   
4448 C  CA  . SER C  21  ? 0.1675 0.1294 0.1818 -0.0174 0.0211  -0.0091 21  SER C CA  
4449 C  C   . SER C  21  ? 0.1627 0.1463 0.1497 -0.0218 -0.0168 0.0071  21  SER C C   
4450 O  O   . SER C  21  ? 0.1741 0.1523 0.1621 -0.0290 -0.0059 -0.0066 21  SER C O   
4451 C  CB  . SER C  21  ? 0.1834 0.1559 0.1622 -0.0115 0.0080  0.0004  21  SER C CB  
4452 O  OG  . SER C  21  ? 0.1962 0.1796 0.2282 -0.0436 0.0263  0.0075  21  SER C OG  
4453 N  N   . CYS C  22  ? 0.1679 0.1669 0.1474 -0.0372 -0.0010 0.0025  22  CYS C N   
4454 C  CA  . CYS C  22  ? 0.1671 0.1556 0.1373 -0.0463 -0.0036 -0.0095 22  CYS C CA  
4455 C  C   . CYS C  22  ? 0.1613 0.1351 0.1769 -0.0233 0.0072  0.0025  22  CYS C C   
4456 O  O   . CYS C  22  ? 0.1746 0.1533 0.1867 -0.0317 0.0034  0.0119  22  CYS C O   
4457 C  CB  . CYS C  22  ? 0.1775 0.1703 0.1500 -0.0329 0.0236  -0.0037 22  CYS C CB  
4458 S  SG  . CYS C  22  ? 0.1888 0.1729 0.1658 -0.0344 0.0057  -0.0218 22  CYS C SG  
4459 N  N   . GLY C  23  ? 0.1723 0.1443 0.1737 -0.0126 0.0000  0.0076  23  GLY C N   
4460 C  CA  . GLY C  23  ? 0.1822 0.1687 0.1594 -0.0161 -0.0041 0.0084  23  GLY C CA  
4461 C  C   . GLY C  23  ? 0.1747 0.1477 0.1804 -0.0326 0.0044  0.0141  23  GLY C C   
4462 O  O   . GLY C  23  ? 0.1869 0.1905 0.1798 -0.0022 -0.0178 0.0033  23  GLY C O   
4463 N  N   . GLY C  24  ? 0.1603 0.1849 0.1746 -0.0193 0.0022  0.0019  24  GLY C N   
4464 C  CA  . GLY C  24  ? 0.2270 0.1867 0.1681 -0.0108 0.0106  0.0073  24  GLY C CA  
4465 C  C   . GLY C  24  ? 0.2031 0.1602 0.1750 -0.0067 -0.0245 0.0300  24  GLY C C   
4466 O  O   . GLY C  24  ? 0.2294 0.1789 0.1909 -0.0308 -0.0166 0.0119  24  GLY C O   
4467 N  N   . LEU C  25  ? 0.2317 0.1621 0.1633 0.0018  -0.0103 0.0116  25  LEU C N   
4468 C  CA  . LEU C  25  ? 0.2601 0.1394 0.1687 0.0005  -0.0318 0.0282  25  LEU C CA  
4469 C  C   . LEU C  25  ? 0.1907 0.1523 0.1606 -0.0067 -0.0038 -0.0006 25  LEU C C   
4470 O  O   . LEU C  25  ? 0.2079 0.1756 0.1491 -0.0241 -0.0074 0.0062  25  LEU C O   
4471 C  CB  . LEU C  25  ? 0.3965 0.1987 0.1627 0.0628  -0.0348 0.0272  25  LEU C CB  
4472 C  CG  . LEU C  25  ? 0.4037 0.2414 0.2160 0.0810  -0.0557 0.0409  25  LEU C CG  
4473 C  CD1 . LEU C  25  ? 0.5999 0.3393 0.2020 0.1033  -0.0009 0.1005  25  LEU C CD1 
4474 C  CD2 . LEU C  25  ? 0.4808 0.4931 0.3699 0.0528  -0.1996 0.1208  25  LEU C CD2 
4475 N  N   . LEU C  26  ? 0.2576 0.1489 0.1312 0.0183  -0.0241 -0.0083 26  LEU C N   
4476 C  CA  . LEU C  26  ? 0.1907 0.1527 0.1415 -0.0099 -0.0077 0.0137  26  LEU C CA  
4477 C  C   . LEU C  26  ? 0.1813 0.1626 0.1405 -0.0089 -0.0283 -0.0115 26  LEU C C   
4478 O  O   . LEU C  26  ? 0.2005 0.2341 0.1369 0.0221  -0.0089 -0.0086 26  LEU C O   
4479 C  CB  . LEU C  26  ? 0.2254 0.2327 0.1611 -0.0034 0.0260  0.0408  26  LEU C CB  
4480 C  CG  . LEU C  26  ? 0.2534 0.3437 0.1892 -0.0370 0.0515  -0.0672 26  LEU C CG  
4481 C  CD1 . LEU C  26  ? 0.2582 0.4522 0.2706 -0.0447 0.1005  -0.0579 26  LEU C CD1 
4482 C  CD2 . LEU C  26  ? 0.3259 0.3726 0.1974 -0.1105 0.0399  -0.0834 26  LEU C CD2 
4483 N  N   . GLN C  27  ? 0.1669 0.1560 0.1361 -0.0141 -0.0153 0.0051  27  GLN C N   
4484 C  CA  . GLN C  27  ? 0.1580 0.1297 0.1128 0.0043  -0.0144 0.0095  27  GLN C CA  
4485 C  C   . GLN C  27  ? 0.1514 0.1384 0.1263 -0.0138 -0.0259 0.0019  27  GLN C C   
4486 O  O   . GLN C  27  ? 0.2224 0.1608 0.1366 -0.0341 -0.0601 0.0142  27  GLN C O   
4487 C  CB  . GLN C  27  ? 0.1433 0.1385 0.1505 0.0017  -0.0199 -0.0109 27  GLN C CB  
4488 C  CG  . GLN C  27  ? 0.1529 0.1345 0.1527 -0.0250 -0.0176 0.0142  27  GLN C CG  
4489 C  CD  . GLN C  27  ? 0.1408 0.1448 0.1281 -0.0091 -0.0170 -0.0006 27  GLN C CD  
4490 O  OE1 . GLN C  27  ? 0.1673 0.1513 0.1320 -0.0320 -0.0077 -0.0039 27  GLN C OE1 
4491 N  NE2 . GLN C  27  ? 0.1493 0.1527 0.1451 -0.0197 0.0001  -0.0010 27  GLN C NE2 
4492 N  N   . SER C  28  ? 0.1403 0.1414 0.1195 -0.0013 -0.0181 0.0105  28  SER C N   
4493 C  CA  . SER C  28  ? 0.1311 0.1269 0.1259 0.0139  0.0044  -0.0077 28  SER C CA  
4494 C  C   . SER C  28  ? 0.1076 0.1383 0.1351 0.0077  -0.0127 -0.0179 28  SER C C   
4495 O  O   . SER C  28  ? 0.1504 0.1392 0.1229 0.0008  -0.0113 -0.0041 28  SER C O   
4496 C  CB  . SER C  28  ? 0.1365 0.1823 0.1048 0.0077  -0.0102 -0.0152 28  SER C CB  
4497 O  OG  . SER C  28  ? 0.1412 0.1816 0.1041 -0.0003 -0.0044 -0.0012 28  SER C OG  
4498 N  N   . PRO C  29  ? 0.1322 0.1402 0.1112 -0.0097 -0.0133 -0.0073 29  PRO C N   
4499 C  CA  . PRO C  29  ? 0.1197 0.1284 0.1273 0.0018  -0.0190 0.0052  29  PRO C CA  
4500 C  C   . PRO C  29  ? 0.1335 0.1359 0.0951 0.0100  -0.0043 0.0074  29  PRO C C   
4501 O  O   . PRO C  29  ? 0.1330 0.1378 0.1091 0.0008  -0.0158 -0.0012 29  PRO C O   
4502 C  CB  . PRO C  29  ? 0.1382 0.1680 0.1055 0.0211  -0.0086 0.0127  29  PRO C CB  
4503 C  CG  . PRO C  29  ? 0.1457 0.1456 0.1262 0.0054  -0.0063 0.0027  29  PRO C CG  
4504 C  CD  . PRO C  29  ? 0.1565 0.1490 0.1133 -0.0258 0.0025  0.0091  29  PRO C CD  
4505 N  N   . ILE C  30  ? 0.1324 0.1513 0.1182 0.0154  -0.0139 0.0038  30  ILE C N   
4506 C  CA  . ILE C  30  ? 0.1576 0.1402 0.1100 -0.0171 -0.0183 0.0039  30  ILE C CA  
4507 C  C   . ILE C  30  ? 0.1253 0.1581 0.1278 -0.0093 0.0009  -0.0020 30  ILE C C   
4508 O  O   . ILE C  30  ? 0.1421 0.1534 0.1368 0.0079  -0.0136 0.0016  30  ILE C O   
4509 C  CB  . ILE C  30  ? 0.1438 0.1393 0.1091 -0.0003 0.0012  0.0001  30  ILE C CB  
4510 C  CG1 . ILE C  30  ? 0.1590 0.1482 0.1143 0.0173  -0.0031 -0.0111 30  ILE C CG1 
4511 C  CG2 . ILE C  30  ? 0.1965 0.1418 0.1186 -0.0010 -0.0027 0.0077  30  ILE C CG2 
4512 C  CD1 . ILE C  30  ? 0.1869 0.1937 0.1182 0.0135  -0.0089 -0.0084 30  ILE C CD1 
4513 N  N   . ASP C  31  ? 0.1240 0.1408 0.1408 -0.0041 -0.0118 0.0029  31  ASP C N   
4514 C  CA  . ASP C  31  ? 0.1345 0.1411 0.1604 -0.0201 -0.0140 -0.0021 31  ASP C CA  
4515 C  C   . ASP C  31  ? 0.1478 0.1518 0.1399 0.0013  -0.0117 0.0100  31  ASP C C   
4516 O  O   . ASP C  31  ? 0.2183 0.1569 0.1507 0.0062  -0.0144 0.0230  31  ASP C O   
4517 C  CB  . ASP C  31  ? 0.1469 0.1568 0.1891 -0.0188 -0.0223 0.0085  31  ASP C CB  
4518 C  CG  . ASP C  31  ? 0.1802 0.1897 0.1372 -0.0344 -0.0219 0.0209  31  ASP C CG  
4519 O  OD1 . ASP C  31  ? 0.1700 0.1730 0.1890 -0.0025 -0.0199 0.0086  31  ASP C OD1 
4520 O  OD2 . ASP C  31  ? 0.2533 0.2174 0.2188 -0.0886 -0.0732 0.0361  31  ASP C OD2 
4521 N  N   . LEU C  32  ? 0.1744 0.1628 0.1716 0.0185  -0.0029 0.0266  32  LEU C N   
4522 C  CA  . LEU C  32  ? 0.1791 0.1604 0.1742 0.0273  0.0131  0.0100  32  LEU C CA  
4523 C  C   . LEU C  32  ? 0.1878 0.2019 0.1712 0.0067  0.0263  0.0118  32  LEU C C   
4524 O  O   . LEU C  32  ? 0.2529 0.1716 0.1713 -0.0009 0.0034  0.0066  32  LEU C O   
4525 C  CB  . LEU C  32  ? 0.1831 0.1668 0.1675 0.0259  -0.0066 0.0059  32  LEU C CB  
4526 C  CG  . LEU C  32  ? 0.1597 0.1976 0.1516 0.0302  0.0186  0.0266  32  LEU C CG  
4527 C  CD1 . LEU C  32  ? 0.1676 0.2599 0.2169 0.0488  -0.0118 0.0261  32  LEU C CD1 
4528 C  CD2 . LEU C  32  ? 0.1980 0.1994 0.2021 -0.0100 0.0070  0.0491  32  LEU C CD2 
4529 N  N   . HIS C  33  ? 0.2358 0.2683 0.1830 -0.0717 -0.0103 0.0374  33  HIS C N   
4530 C  CA  . HIS C  33  ? 0.2451 0.2728 0.2847 -0.0709 0.0201  -0.0203 33  HIS C CA  
4531 C  C   . HIS C  33  ? 0.2193 0.2766 0.2621 -0.0784 0.0089  -0.0073 33  HIS C C   
4532 O  O   . HIS C  33  ? 0.1956 0.2348 0.2493 -0.0277 0.0075  -0.0029 33  HIS C O   
4533 C  CB  . HIS C  33  ? 0.3143 0.2369 0.3163 -0.0009 0.0582  -0.0178 33  HIS C CB  
4534 C  CG  . HIS C  33  ? 0.2478 0.3374 0.2390 0.0171  -0.0029 -0.0549 33  HIS C CG  
4535 N  ND1 . HIS C  33  ? 0.2675 0.5163 0.3145 0.0836  -0.0928 -0.1056 33  HIS C ND1 
4536 C  CD2 . HIS C  33  ? 0.3219 0.3288 0.3071 0.0372  -0.0751 -0.0675 33  HIS C CD2 
4537 C  CE1 . HIS C  33  ? 0.2942 0.5049 0.3105 -0.0845 -0.0682 -0.0060 33  HIS C CE1 
4538 N  NE2 . HIS C  33  ? 0.2868 0.3527 0.3249 0.0612  -0.0422 -0.0475 33  HIS C NE2 
4539 N  N   . SER C  34  ? 0.2957 0.2731 0.2657 -0.0914 0.0038  0.0194  34  SER C N   
4540 C  CA  . SER C  34  ? 0.3527 0.3114 0.3472 -0.0968 0.0582  0.0015  34  SER C CA  
4541 C  C   . SER C  34  ? 0.2585 0.2566 0.2676 -0.1016 0.0287  -0.0444 34  SER C C   
4542 O  O   . SER C  34  ? 0.3155 0.2401 0.3339 -0.0669 0.0318  -0.0738 34  SER C O   
4543 C  CB  . SER C  34  ? 0.3384 0.2841 0.5636 -0.0993 0.0784  -0.0942 34  SER C CB  
4544 O  OG  . SER C  34  ? 0.5030 0.4364 0.9203 0.0541  0.2394  0.1385  34  SER C OG  
4545 N  N   . ASP C  35  ? 0.2253 0.2556 0.4080 -0.0684 -0.0621 -0.0096 35  ASP C N   
4546 C  CA  . ASP C  35  ? 0.2259 0.2815 0.4253 -0.0374 -0.0450 -0.0791 35  ASP C CA  
4547 C  C   . ASP C  35  ? 0.2104 0.3259 0.2218 -0.0048 -0.0457 -0.0087 35  ASP C C   
4548 O  O   . ASP C  35  ? 0.2820 0.4243 0.2681 0.0030  -0.0949 -0.0066 35  ASP C O   
4549 C  CB  . ASP C  35  ? 0.1767 0.5119 0.5911 -0.0328 -0.0230 -0.0550 35  ASP C CB  
4550 C  CG  . ASP C  35  ? 0.5457 0.5848 0.8368 -0.1233 0.0669  -0.0055 35  ASP C CG  
4551 O  OD1 . ASP C  35  ? 0.3778 0.5685 1.0084 -0.2008 -0.1420 -0.0048 35  ASP C OD1 
4552 O  OD2 . ASP C  35  ? 0.5400 1.0737 0.8405 0.1379  -0.2348 -0.0158 35  ASP C OD2 
4553 N  N   . ILE C  36  ? 0.1659 0.2685 0.2415 -0.0201 -0.0161 -0.0205 36  ILE C N   
4554 C  CA  . ILE C  36  ? 0.1957 0.2386 0.1722 0.0219  -0.0350 0.0008  36  ILE C CA  
4555 C  C   . ILE C  36  ? 0.1973 0.2043 0.1572 0.0057  -0.0157 -0.0177 36  ILE C C   
4556 O  O   . ILE C  36  ? 0.1889 0.2139 0.2276 0.0170  -0.0122 -0.0052 36  ILE C O   
4557 C  CB  . ILE C  36  ? 0.2297 0.2326 0.2034 0.0276  0.0136  0.0006  36  ILE C CB  
4558 C  CG1 . ILE C  36  ? 0.3106 0.1852 0.2106 -0.0257 0.0194  0.0042  36  ILE C CG1 
4559 C  CG2 . ILE C  36  ? 0.2576 0.2488 0.3362 0.0780  -0.0052 0.0194  36  ILE C CG2 
4560 C  CD1 . ILE C  36  ? 0.2576 0.2098 0.3060 0.0106  0.0248  -0.0464 36  ILE C CD1 
4561 N  N   . LEU C  37  ? 0.1978 0.2317 0.1957 -0.0118 -0.0151 -0.0165 37  LEU C N   
4562 C  CA  . LEU C  37  ? 0.1668 0.2190 0.2283 0.0057  0.0092  -0.0085 37  LEU C CA  
4563 C  C   . LEU C  37  ? 0.2057 0.1856 0.2574 -0.0129 -0.0043 -0.0353 37  LEU C C   
4564 O  O   . LEU C  37  ? 0.2048 0.2296 0.2720 -0.0144 -0.0012 -0.0721 37  LEU C O   
4565 C  CB  . LEU C  37  ? 0.2486 0.2117 0.2325 -0.0343 0.0051  -0.0373 37  LEU C CB  
4566 C  CG  . LEU C  37  ? 0.2569 0.2250 0.2344 0.0193  -0.0012 -0.0093 37  LEU C CG  
4567 C  CD1 . LEU C  37  ? 0.2858 0.3076 0.2108 -0.0392 0.0006  0.0605  37  LEU C CD1 
4568 C  CD2 . LEU C  37  ? 0.1946 0.2217 0.2645 0.0188  -0.0185 -0.0200 37  LEU C CD2 
4569 N  N   . GLN C  38  ? 0.1810 0.2036 0.2101 -0.0057 -0.0114 -0.0250 38  GLN C N   
4570 C  CA  . GLN C  38  ? 0.2133 0.1878 0.2232 0.0117  -0.0158 -0.0229 38  GLN C CA  
4571 C  C   . GLN C  38  ? 0.2006 0.1666 0.2022 0.0037  -0.0060 -0.0063 38  GLN C C   
4572 O  O   . GLN C  38  ? 0.1922 0.1897 0.2011 -0.0025 -0.0164 -0.0062 38  GLN C O   
4573 C  CB  . GLN C  38  ? 0.2796 0.2165 0.1827 0.0234  -0.0381 -0.0460 38  GLN C CB  
4574 C  CG  . GLN C  38  ? 0.3061 0.2298 0.1908 0.0302  0.0080  -0.0251 38  GLN C CG  
4575 C  CD  . GLN C  38  ? 0.3416 0.2837 0.2264 0.0429  -0.0158 -0.0410 38  GLN C CD  
4576 O  OE1 . GLN C  38  ? 0.4339 0.5723 0.4801 -0.0223 -0.1095 -0.0223 38  GLN C OE1 
4577 N  NE2 . GLN C  38  ? 0.3453 0.3272 0.2201 0.0279  0.0031  -0.0486 38  GLN C NE2 
4578 N  N   . TYR C  39  ? 0.1983 0.1782 0.1897 0.0189  0.0047  -0.0093 39  TYR C N   
4579 C  CA  . TYR C  39  ? 0.2088 0.1603 0.2034 0.0347  -0.0013 0.0128  39  TYR C CA  
4580 C  C   . TYR C  39  ? 0.2205 0.1512 0.2005 0.0285  -0.0043 0.0039  39  TYR C C   
4581 O  O   . TYR C  39  ? 0.2322 0.1834 0.1961 0.0117  -0.0085 -0.0217 39  TYR C O   
4582 C  CB  . TYR C  39  ? 0.2427 0.1782 0.2435 0.0341  0.0038  -0.0142 39  TYR C CB  
4583 C  CG  . TYR C  39  ? 0.1997 0.1964 0.2388 0.0165  -0.0195 -0.0093 39  TYR C CG  
4584 C  CD1 . TYR C  39  ? 0.2924 0.2262 0.2654 0.0982  0.0192  -0.0096 39  TYR C CD1 
4585 C  CD2 . TYR C  39  ? 0.2215 0.2049 0.2852 0.0244  -0.0196 -0.0461 39  TYR C CD2 
4586 C  CE1 . TYR C  39  ? 0.2773 0.2685 0.2719 0.1198  -0.0315 -0.0339 39  TYR C CE1 
4587 C  CE2 . TYR C  39  ? 0.2634 0.2193 0.2713 0.0337  0.0157  -0.0491 39  TYR C CE2 
4588 C  CZ  . TYR C  39  ? 0.3083 0.2636 0.3114 0.1368  -0.0389 -0.0620 39  TYR C CZ  
4589 O  OH  . TYR C  39  ? 0.2761 0.2707 0.3994 0.1132  -0.0084 -0.0569 39  TYR C OH  
4590 N  N   . ASP C  40  ? 0.2003 0.2378 0.1700 0.0254  0.0039  -0.0165 40  ASP C N   
4591 C  CA  . ASP C  40  ? 0.1794 0.2342 0.2007 0.0121  0.0179  -0.0240 40  ASP C CA  
4592 C  C   . ASP C  40  ? 0.2273 0.2225 0.1531 0.0233  0.0055  -0.0129 40  ASP C C   
4593 O  O   . ASP C  40  ? 0.2020 0.2433 0.1745 0.0500  0.0148  0.0125  40  ASP C O   
4594 C  CB  . ASP C  40  ? 0.2079 0.2267 0.2105 0.0088  0.0436  0.0392  40  ASP C CB  
4595 C  CG  . ASP C  40  ? 0.2189 0.2245 0.3006 0.0381  0.0594  0.0480  40  ASP C CG  
4596 O  OD1 . ASP C  40  ? 0.2305 0.2520 0.2452 0.0347  0.0572  0.0611  40  ASP C OD1 
4597 O  OD2 . ASP C  40  ? 0.3452 0.2258 0.3814 0.0081  0.0857  0.0067  40  ASP C OD2 
4598 N  N   . ALA C  41  ? 0.2242 0.2584 0.1769 0.0377  0.0306  -0.0038 41  ALA C N   
4599 C  CA  . ALA C  41  ? 0.2127 0.2545 0.2404 0.0444  0.0341  -0.0613 41  ALA C CA  
4600 C  C   . ALA C  41  ? 0.1976 0.2354 0.2068 0.0603  0.0304  0.0166  41  ALA C C   
4601 O  O   . ALA C  41  ? 0.2026 0.3074 0.1958 0.0653  0.0298  0.0165  41  ALA C O   
4602 C  CB  . ALA C  41  ? 0.2612 0.3433 0.2382 0.0640  0.0557  -0.0579 41  ALA C CB  
4603 N  N   . SER C  42  ? 0.2252 0.2433 0.1587 0.0258  0.0335  0.0231  42  SER C N   
4604 C  CA  . SER C  42  ? 0.2439 0.2907 0.1758 -0.0049 0.0223  0.0138  42  SER C CA  
4605 C  C   . SER C  42  ? 0.1992 0.2811 0.1849 0.0468  0.0158  -0.0062 42  SER C C   
4606 O  O   . SER C  42  ? 0.2260 0.3054 0.2054 0.0194  0.0240  -0.0041 42  SER C O   
4607 C  CB  . SER C  42  ? 0.2247 0.2931 0.2518 0.0052  0.0414  0.0174  42  SER C CB  
4608 O  OG  . SER C  42  ? 0.2060 0.3130 0.2689 0.0430  0.0381  0.0276  42  SER C OG  
4609 N  N   . LEU C  43  ? 0.1830 0.2578 0.2005 0.0410  0.0310  0.0005  43  LEU C N   
4610 C  CA  . LEU C  43  ? 0.2037 0.3118 0.1490 0.0309  0.0087  0.0176  43  LEU C CA  
4611 C  C   . LEU C  43  ? 0.2058 0.3003 0.2212 0.0455  0.0274  0.0055  43  LEU C C   
4612 O  O   . LEU C  43  ? 0.2433 0.2931 0.2388 0.0873  0.0506  0.0279  43  LEU C O   
4613 C  CB  . LEU C  43  ? 0.2026 0.2623 0.1780 0.0620  0.0501  -0.0080 43  LEU C CB  
4614 C  CG  . LEU C  43  ? 0.1766 0.1952 0.1894 0.0089  0.0146  0.0088  43  LEU C CG  
4615 C  CD1 . LEU C  43  ? 0.1998 0.2124 0.1752 0.0219  0.0317  -0.0025 43  LEU C CD1 
4616 C  CD2 . LEU C  43  ? 0.2255 0.2421 0.2113 -0.0069 0.0134  -0.0079 43  LEU C CD2 
4617 N  N   . THR C  44  ? 0.2206 0.3176 0.1836 0.0560  0.0088  0.0218  44  THR C N   
4618 C  CA  . THR C  44  ? 0.2520 0.3255 0.2036 0.1053  0.0211  0.0143  44  THR C CA  
4619 C  C   . THR C  44  ? 0.2266 0.3298 0.2579 0.0949  -0.0483 0.0107  44  THR C C   
4620 O  O   . THR C  44  ? 0.2352 0.3129 0.2423 0.0826  -0.0044 -0.0274 44  THR C O   
4621 C  CB  . THR C  44  ? 0.2577 0.3755 0.2343 0.0760  0.0571  0.0324  44  THR C CB  
4622 O  OG1 . THR C  44  ? 0.2499 0.4547 0.2929 0.0181  0.0326  0.0399  44  THR C OG1 
4623 C  CG2 . THR C  44  ? 0.3406 0.4654 0.2382 0.1005  0.0761  0.0468  44  THR C CG2 
4624 N  N   . PRO C  45  ? 0.2515 0.3055 0.2285 0.1216  -0.0044 -0.0100 45  PRO C N   
4625 C  CA  . PRO C  45  ? 0.2606 0.3172 0.1951 0.0964  0.0094  -0.0048 45  PRO C CA  
4626 C  C   . PRO C  45  ? 0.3015 0.3444 0.2602 0.0703  -0.0325 -0.0653 45  PRO C C   
4627 O  O   . PRO C  45  ? 0.3030 0.5109 0.2947 0.0892  0.0294  -0.0488 45  PRO C O   
4628 C  CB  . PRO C  45  ? 0.3170 0.3348 0.2861 0.0792  0.0182  0.0653  45  PRO C CB  
4629 C  CG  . PRO C  45  ? 0.3508 0.2868 0.3802 0.1463  0.0126  0.0225  45  PRO C CG  
4630 C  CD  . PRO C  45  ? 0.3388 0.2807 0.3301 0.1102  -0.0039 0.0102  45  PRO C CD  
4631 N  N   . LEU C  46  ? 0.2561 0.2363 0.2622 0.0403  -0.0268 -0.0178 46  LEU C N   
4632 C  CA  . LEU C  46  ? 0.2579 0.2823 0.2547 0.0485  -0.0212 -0.0336 46  LEU C CA  
4633 C  C   . LEU C  46  ? 0.2739 0.3167 0.3762 0.0214  -0.0619 -0.0035 46  LEU C C   
4634 O  O   . LEU C  46  ? 0.2829 0.3523 0.3573 0.0662  -0.0271 -0.0160 46  LEU C O   
4635 C  CB  . LEU C  46  ? 0.2632 0.3607 0.2033 0.1050  -0.0260 -0.0048 46  LEU C CB  
4636 C  CG  . LEU C  46  ? 0.2179 0.3775 0.3227 0.0719  -0.0036 0.0787  46  LEU C CG  
4637 C  CD1 . LEU C  46  ? 0.2259 0.2626 0.3946 0.0798  -0.0059 -0.0029 46  LEU C CD1 
4638 C  CD2 . LEU C  46  ? 0.2893 0.4519 0.3013 0.0414  -0.0409 0.1187  46  LEU C CD2 
4639 N  N   . GLU C  47  ? 0.2721 0.3714 0.3028 0.0317  -0.0234 -0.0447 47  GLU C N   
4640 C  CA  . GLU C  47  ? 0.2579 0.3358 0.3066 0.1291  -0.0290 0.0207  47  GLU C CA  
4641 C  C   . GLU C  47  ? 0.2710 0.3368 0.3021 0.0536  -0.0085 0.0079  47  GLU C C   
4642 O  O   . GLU C  47  ? 0.3186 0.3464 0.2576 0.0690  -0.0167 0.0208  47  GLU C O   
4643 C  CB  . GLU C  47  ? 0.3898 0.4596 0.3822 0.1878  0.0332  0.0545  47  GLU C CB  
4644 C  CG  . GLU C  47  ? 0.3971 0.6574 0.4733 0.2899  0.0242  -0.0682 47  GLU C CG  
4645 N  N   . PHE C  48  ? 0.1746 0.2585 0.3172 0.0355  -0.0559 -0.0353 48  PHE C N   
4646 C  CA  . PHE C  48  ? 0.1877 0.3186 0.3384 -0.0044 -0.0248 -0.0253 48  PHE C CA  
4647 C  C   . PHE C  48  ? 0.1666 0.2948 0.3450 0.0168  -0.0600 0.0314  48  PHE C C   
4648 O  O   . PHE C  48  ? 0.3244 0.3741 0.4135 0.0754  -0.0780 0.0127  48  PHE C O   
4649 C  CB  . PHE C  48  ? 0.2459 0.3152 0.2687 0.0089  -0.0173 0.0216  48  PHE C CB  
4650 C  CG  . PHE C  48  ? 0.2860 0.2834 0.2386 -0.0131 0.0013  -0.0034 48  PHE C CG  
4651 C  CD1 . PHE C  48  ? 0.2251 0.3622 0.2794 0.0467  0.0005  -0.0854 48  PHE C CD1 
4652 C  CD2 . PHE C  48  ? 0.2315 0.2681 0.2588 -0.0394 -0.0181 0.0206  48  PHE C CD2 
4653 C  CE1 . PHE C  48  ? 0.2190 0.3236 0.2759 -0.0114 0.0229  -0.0508 48  PHE C CE1 
4654 C  CE2 . PHE C  48  ? 0.2876 0.3404 0.2405 -0.0507 -0.0205 0.0294  48  PHE C CE2 
4655 C  CZ  . PHE C  48  ? 0.2427 0.2967 0.2263 0.0396  0.0398  -0.0432 48  PHE C CZ  
4656 N  N   . GLN C  49  ? 0.2106 0.3155 0.2427 0.0600  -0.0495 -0.0052 49  GLN C N   
4657 C  CA  . GLN C  49  ? 0.1905 0.4436 0.3556 0.0236  -0.0435 0.0286  49  GLN C CA  
4658 C  C   . GLN C  49  ? 0.3231 0.3177 0.3725 0.0451  -0.0284 0.0523  49  GLN C C   
4659 O  O   . GLN C  49  ? 0.2128 0.3520 0.3244 0.0099  -0.0555 0.0008  49  GLN C O   
4660 C  CB  . GLN C  49  ? 0.2630 0.6364 0.2500 -0.0134 0.0082  -0.0635 49  GLN C CB  
4661 C  CG  . GLN C  49  ? 0.3042 0.5243 0.3595 -0.0055 0.0086  -0.0524 49  GLN C CG  
4662 C  CD  . GLN C  49  ? 0.6028 0.6485 0.7543 -0.1331 0.2791  -0.2486 49  GLN C CD  
4663 O  OE1 . GLN C  49  ? 0.9251 0.7751 1.1339 -0.3928 -0.3550 -0.2180 49  GLN C OE1 
4664 N  NE2 . GLN C  49  ? 0.7605 0.6125 0.7280 0.2929  0.2309  -0.1421 49  GLN C NE2 
4665 N  N   . GLY C  50  ? 0.2245 0.3592 0.3319 0.0105  -0.0329 -0.0190 50  GLY C N   
4666 C  CA  . GLY C  50  ? 0.2011 0.4150 0.2928 0.0333  -0.0201 -0.0282 50  GLY C CA  
4667 C  C   . GLY C  50  ? 0.1806 0.2903 0.2740 0.0252  -0.0417 -0.0077 50  GLY C C   
4668 O  O   . GLY C  50  ? 0.2203 0.4398 0.3683 -0.0254 -0.0257 -0.1045 50  GLY C O   
4669 N  N   . TYR C  51  ? 0.1967 0.3524 0.3190 0.0383  -0.0095 0.0136  51  TYR C N   
4670 C  CA  . TYR C  51  ? 0.1674 0.2990 0.3080 -0.0008 -0.0589 0.0225  51  TYR C CA  
4671 C  C   . TYR C  51  ? 0.2122 0.4921 0.2474 0.1240  -0.1178 -0.0594 51  TYR C C   
4672 O  O   . TYR C  51  ? 0.2351 0.2852 0.2900 0.0203  -0.0810 -0.0257 51  TYR C O   
4673 C  CB  . TYR C  51  ? 0.2339 0.2509 0.3201 -0.0117 -0.1014 -0.0016 51  TYR C CB  
4674 C  CG  . TYR C  51  ? 0.1670 0.3133 0.3004 0.0035  -0.0555 0.0357  51  TYR C CG  
4675 C  CD1 . TYR C  51  ? 0.1675 0.2365 0.2655 0.0050  -0.0484 -0.0121 51  TYR C CD1 
4676 C  CD2 . TYR C  51  ? 0.1986 0.2300 0.2206 0.0133  -0.0330 -0.0160 51  TYR C CD2 
4677 C  CE1 . TYR C  51  ? 0.1830 0.2599 0.3111 -0.0170 -0.0403 0.0059  51  TYR C CE1 
4678 C  CE2 . TYR C  51  ? 0.2015 0.2794 0.2832 0.0594  -0.0209 0.0722  51  TYR C CE2 
4679 C  CZ  . TYR C  51  ? 0.1942 0.2406 0.2468 -0.0142 -0.0752 0.0037  51  TYR C CZ  
4680 O  OH  . TYR C  51  ? 0.1839 0.2661 0.2824 0.0002  -0.0627 0.0441  51  TYR C OH  
4681 N  N   . ASN C  52  ? 0.1993 0.3749 0.3805 0.0539  -0.1321 -0.0401 52  ASN C N   
4682 C  CA  . ASN C  52  ? 0.2712 0.3502 0.4040 0.0674  -0.1150 -0.0814 52  ASN C CA  
4683 C  C   . ASN C  52  ? 0.2769 0.3199 0.4624 0.0403  -0.0722 -0.0864 52  ASN C C   
4684 O  O   . ASN C  52  ? 0.2528 0.4667 0.5585 0.0458  -0.1254 -0.0917 52  ASN C O   
4685 C  CB  . ASN C  52  ? 0.4611 0.3653 0.4817 0.2142  -0.0754 0.0166  52  ASN C CB  
4686 C  CG  . ASN C  52  ? 0.3294 0.7160 0.5085 0.2459  -0.1587 0.0840  52  ASN C CG  
4687 O  OD1 . ASN C  52  ? 0.4137 0.7860 0.6566 0.3037  -0.0326 0.0216  52  ASN C OD1 
4688 N  ND2 . ASN C  52  ? 0.5819 0.4424 0.5116 0.2558  0.0597  0.0692  52  ASN C ND2 
4689 N  N   . LEU C  53  ? 0.2931 0.3206 0.3903 0.0642  -0.1658 -0.0959 53  LEU C N   
4690 C  CA  . LEU C  53  ? 0.3027 0.3044 0.3786 0.0414  -0.0718 -0.0461 53  LEU C CA  
4691 C  C   . LEU C  53  ? 0.3827 0.4118 0.3947 -0.0375 -0.1275 -0.0514 53  LEU C C   
4692 O  O   . LEU C  53  ? 0.4412 0.5873 0.3843 0.0556  -0.1810 0.0820  53  LEU C O   
4693 C  CB  . LEU C  53  ? 0.2806 0.3021 0.3193 0.0618  -0.0795 -0.0588 53  LEU C CB  
4694 C  CG  . LEU C  53  ? 0.2685 0.3303 0.2339 0.0296  -0.0595 -0.0514 53  LEU C CG  
4695 C  CD1 . LEU C  53  ? 0.2999 0.3425 0.2445 0.0354  -0.0143 -0.0386 53  LEU C CD1 
4696 C  CD2 . LEU C  53  ? 0.3712 0.5023 0.3441 -0.0240 0.0584  -0.0121 53  LEU C CD2 
4697 N  N   . SER C  54  ? 0.2502 0.6375 0.7318 0.0534  -0.0980 -0.0556 54  SER C N   
4698 C  CA  . SER C  54  ? 0.3976 0.5632 0.3560 0.1148  0.0501  -0.0651 54  SER C CA  
4699 C  C   . SER C  54  ? 0.6140 0.8595 0.3527 0.2432  0.0556  0.0399  54  SER C C   
4700 O  O   . SER C  54  ? 0.4201 0.8276 0.7404 0.1938  -0.2987 -0.2080 54  SER C O   
4701 C  CB  . SER C  54  ? 0.4518 0.8313 0.7299 0.0322  0.1087  -0.0035 54  SER C CB  
4702 O  OG  . SER C  54  ? 0.9218 1.4232 0.5193 -0.1164 0.2586  -0.0432 54  SER C OG  
4703 N  N   . ALA C  55  ? 0.4632 0.6113 0.3057 0.1676  -0.1720 -0.0751 55  ALA C N   
4704 C  CA  . ALA C  55  ? 0.9714 0.8259 0.3290 -0.0461 -0.1072 -0.2056 55  ALA C CA  
4705 C  C   . ALA C  55  ? 0.8021 0.9566 0.5536 0.0304  -0.1897 -0.3048 55  ALA C C   
4706 O  O   . ALA C  55  ? 1.3753 1.0059 0.3926 0.2497  -0.2404 -0.2604 55  ALA C O   
4707 C  CB  . ALA C  55  ? 1.3310 0.8658 0.3546 -0.0352 -0.3414 -0.0038 55  ALA C CB  
4708 N  N   . ASN C  56  ? 0.6148 0.4866 0.4794 0.2029  -0.2644 -0.2292 56  ASN C N   
4709 C  CA  . ASN C  56  ? 0.3483 0.6581 0.9978 0.2838  -0.2138 -0.4349 56  ASN C CA  
4710 C  C   . ASN C  56  ? 0.7517 0.6113 0.7395 0.2435  -0.4168 -0.3854 56  ASN C C   
4711 O  O   . ASN C  56  ? 0.7646 0.5521 1.2444 0.2066  -0.6916 -0.5123 56  ASN C O   
4712 C  CB  . ASN C  56  ? 0.7736 0.8189 0.7763 0.3480  0.0282  -0.3289 56  ASN C CB  
4713 C  CG  . ASN C  56  ? 0.8846 1.0693 0.6305 0.3230  -0.0627 -0.2210 56  ASN C CG  
4714 O  OD1 . ASN C  56  ? 0.4567 0.6676 0.6253 0.2396  -0.1996 -0.0483 56  ASN C OD1 
4715 N  ND2 . ASN C  56  ? 0.4124 0.5633 1.0739 0.0649  0.0403  -0.3726 56  ASN C ND2 
4716 N  N   . LYS C  57  ? 0.6394 0.7043 0.8800 0.1729  -0.2708 -0.0949 57  LYS C N   
4717 C  CA  . LYS C  57  ? 0.4246 0.6485 0.6657 0.2374  0.0062  -0.2150 57  LYS C CA  
4718 C  C   . LYS C  57  ? 0.3074 0.3121 0.4023 0.0759  -0.1338 -0.1806 57  LYS C C   
4719 O  O   . LYS C  57  ? 0.3957 0.3599 0.5392 0.0113  -0.2912 -0.0484 57  LYS C O   
4720 C  CB  . LYS C  57  ? 0.4665 0.5272 0.6317 -0.0996 -0.0241 -0.1772 57  LYS C CB  
4721 C  CG  . LYS C  57  ? 0.5575 0.7743 0.6468 0.0746  0.2263  -0.2408 57  LYS C CG  
4722 N  N   . GLN C  58  ? 0.3462 0.3449 0.4169 0.0906  -0.1264 -0.1173 58  GLN C N   
4723 C  CA  . GLN C  58  ? 0.3526 0.4489 0.2852 0.0560  -0.1056 0.0106  58  GLN C CA  
4724 C  C   . GLN C  58  ? 0.2824 0.3554 0.2446 -0.0326 -0.0952 -0.0355 58  GLN C C   
4725 O  O   . GLN C  58  ? 0.2339 0.4078 0.3642 0.0178  -0.0858 0.0093  58  GLN C O   
4726 C  CB  . GLN C  58  ? 0.3689 0.3869 0.3019 0.0591  -0.1307 -0.0303 58  GLN C CB  
4727 C  CG  . GLN C  58  ? 0.4039 0.4831 0.3541 -0.0460 -0.1751 -0.1388 58  GLN C CG  
4728 C  CD  . GLN C  58  ? 0.4496 0.3781 0.2410 -0.0386 -0.0392 -0.0061 58  GLN C CD  
4729 O  OE1 . GLN C  58  ? 0.5457 0.4075 0.2600 -0.0542 -0.0798 0.0069  58  GLN C OE1 
4730 N  NE2 . GLN C  58  ? 0.3754 0.3374 0.3847 -0.0710 -0.0930 0.0159  58  GLN C NE2 
4731 N  N   . PHE C  59  ? 0.2888 0.3028 0.2736 -0.0199 -0.1147 -0.0641 59  PHE C N   
4732 C  CA  . PHE C  59  ? 0.3068 0.3737 0.2029 -0.0025 -0.1366 -0.0710 59  PHE C CA  
4733 C  C   . PHE C  59  ? 0.2814 0.3321 0.2375 -0.0145 -0.1157 0.0255  59  PHE C C   
4734 O  O   . PHE C  59  ? 0.2657 0.2994 0.2750 0.0055  -0.0917 -0.0364 59  PHE C O   
4735 C  CB  . PHE C  59  ? 0.2814 0.2801 0.2552 0.0513  -0.1103 -0.0482 59  PHE C CB  
4736 C  CG  . PHE C  59  ? 0.3055 0.3664 0.2462 0.0775  -0.1027 -0.0656 59  PHE C CG  
4737 C  CD1 . PHE C  59  ? 0.2762 0.3131 0.3036 -0.0027 -0.0772 -0.0478 59  PHE C CD1 
4738 C  CD2 . PHE C  59  ? 0.3046 0.2893 0.3600 0.0785  -0.0577 -0.0187 59  PHE C CD2 
4739 C  CE1 . PHE C  59  ? 0.2934 0.3515 0.3714 0.0133  -0.0921 -0.1121 59  PHE C CE1 
4740 C  CE2 . PHE C  59  ? 0.2361 0.4829 0.3396 0.0803  -0.1324 -0.0980 59  PHE C CE2 
4741 C  CZ  . PHE C  59  ? 0.2233 0.3768 0.5294 0.0374  -0.0420 -0.0540 59  PHE C CZ  
4742 N  N   . LEU C  60  ? 0.2579 0.2707 0.2931 0.0420  -0.1278 -0.0375 60  LEU C N   
4743 C  CA  . LEU C  60  ? 0.2618 0.2521 0.2550 0.0068  -0.0954 0.0027  60  LEU C CA  
4744 C  C   . LEU C  60  ? 0.2858 0.2210 0.2088 0.0097  -0.0949 -0.0414 60  LEU C C   
4745 O  O   . LEU C  60  ? 0.2915 0.2742 0.1948 0.0297  -0.1041 -0.0518 60  LEU C O   
4746 C  CB  . LEU C  60  ? 0.2400 0.2455 0.2473 -0.0079 -0.0562 -0.0346 60  LEU C CB  
4747 C  CG  . LEU C  60  ? 0.3770 0.2661 0.2937 -0.0165 -0.0380 -0.0620 60  LEU C CG  
4748 C  CD1 . LEU C  60  ? 0.3441 0.3874 0.3163 -0.0626 -0.0137 -0.1860 60  LEU C CD1 
4749 C  CD2 . LEU C  60  ? 0.3640 0.3675 0.3243 -0.0455 -0.0256 -0.0231 60  LEU C CD2 
4750 N  N   . LEU C  61  ? 0.2899 0.2926 0.2340 -0.0107 -0.0809 -0.0209 61  LEU C N   
4751 C  CA  . LEU C  61  ? 0.3192 0.2667 0.1702 0.0038  -0.1002 -0.0657 61  LEU C CA  
4752 C  C   . LEU C  61  ? 0.2541 0.2377 0.2131 -0.0348 -0.0695 -0.0373 61  LEU C C   
4753 O  O   . LEU C  61  ? 0.3244 0.3165 0.2069 -0.0103 -0.0991 -0.0566 61  LEU C O   
4754 C  CB  . LEU C  61  ? 0.2775 0.4206 0.2748 -0.0145 -0.1034 0.0938  61  LEU C CB  
4755 C  CG  . LEU C  61  ? 0.3374 0.3319 0.2191 -0.0333 -0.0954 0.0209  61  LEU C CG  
4756 C  CD1 . LEU C  61  ? 0.3949 0.2864 0.2525 -0.0508 -0.0743 -0.0033 61  LEU C CD1 
4757 C  CD2 . LEU C  61  ? 0.5351 0.2724 0.3229 0.0086  -0.0763 0.1052  61  LEU C CD2 
4758 N  N   . THR C  62  ? 0.2277 0.2615 0.2015 -0.0021 -0.0487 -0.0644 62  THR C N   
4759 C  CA  . THR C  62  ? 0.2728 0.2398 0.2197 0.0156  0.0000  -0.0298 62  THR C CA  
4760 C  C   . THR C  62  ? 0.2639 0.3083 0.3270 -0.0044 -0.0131 -0.1464 62  THR C C   
4761 O  O   . THR C  62  ? 0.3277 0.3116 0.2148 0.0005  -0.0625 -0.0631 62  THR C O   
4762 C  CB  . THR C  62  ? 0.3188 0.2416 0.2972 0.0065  -0.0209 -0.0456 62  THR C CB  
4763 O  OG1 . THR C  62  ? 0.3018 0.3577 0.3259 -0.0054 -0.0853 -0.0521 62  THR C OG1 
4764 C  CG2 . THR C  62  ? 0.4113 0.2879 0.4409 0.0626  0.0225  -0.0813 62  THR C CG2 
4765 N  N   . ASN C  63  ? 0.2675 0.3269 0.1845 0.0214  -0.0245 -0.0557 63  ASN C N   
4766 C  CA  . ASN C  63  ? 0.2208 0.2483 0.1956 0.0316  -0.0498 0.0232  63  ASN C CA  
4767 C  C   . ASN C  63  ? 0.3614 0.2147 0.1936 -0.0142 0.0017  -0.0289 63  ASN C C   
4768 O  O   . ASN C  63  ? 0.3046 0.2563 0.2508 0.0216  -0.0297 -0.0153 63  ASN C O   
4769 C  CB  . ASN C  63  ? 0.3145 0.3635 0.1333 0.0479  -0.0688 -0.0372 63  ASN C CB  
4770 C  CG  . ASN C  63  ? 0.2214 0.3080 0.2732 0.0017  -0.0502 0.0869  63  ASN C CG  
4771 O  OD1 . ASN C  63  ? 0.3270 0.3027 0.1685 0.0082  -0.0554 0.0083  63  ASN C OD1 
4772 N  ND2 . ASN C  63  ? 0.2678 0.2884 0.1830 -0.0134 -0.0369 -0.0160 63  ASN C ND2 
4773 N  N   . ASN C  64  ? 0.3465 0.1846 0.1825 -0.0273 -0.0411 0.0195  64  ASN C N   
4774 C  CA  . ASN C  64  ? 0.3876 0.2505 0.2449 -0.0201 -0.0451 0.0666  64  ASN C CA  
4775 C  C   . ASN C  64  ? 0.3079 0.1533 0.2815 0.0374  -0.0845 0.0032  64  ASN C C   
4776 O  O   . ASN C  64  ? 0.3709 0.2469 0.2438 -0.0155 -0.0496 0.0136  64  ASN C O   
4777 C  CB  . ASN C  64  ? 0.3632 0.3541 0.2132 -0.0826 -0.0318 0.0348  64  ASN C CB  
4778 C  CG  . ASN C  64  ? 0.2940 0.3865 0.1851 -0.0562 -0.0463 0.0064  64  ASN C CG  
4779 O  OD1 . ASN C  64  ? 0.3358 0.4092 0.1668 -0.0624 -0.0320 -0.0419 64  ASN C OD1 
4780 N  ND2 . ASN C  64  ? 0.3800 0.4342 0.2048 -0.0804 0.0215  0.0303  64  ASN C ND2 
4781 N  N   . GLY C  65  ? 0.3432 0.3549 0.1739 -0.0666 -0.0582 -0.0432 65  GLY C N   
4782 C  CA  . GLY C  65  ? 0.3771 0.3725 0.2142 -0.0326 -0.0614 -0.0280 65  GLY C CA  
4783 C  C   . GLY C  65  ? 0.2694 0.3540 0.1707 0.0066  -0.0458 -0.0187 65  GLY C C   
4784 O  O   . GLY C  65  ? 0.3433 0.4616 0.2446 -0.0059 -0.0245 -0.0759 65  GLY C O   
4785 N  N   . HIS C  66  ? 0.2998 0.3529 0.1893 -0.0709 -0.0390 -0.0424 66  HIS C N   
4786 C  CA  . HIS C  66  ? 0.3701 0.2523 0.2326 -0.0538 -0.1084 0.0200  66  HIS C CA  
4787 C  C   . HIS C  66  ? 0.2723 0.2176 0.1697 -0.0430 -0.0336 -0.0058 66  HIS C C   
4788 O  O   . HIS C  66  ? 0.2958 0.3186 0.2691 -0.0802 -0.0652 -0.0421 66  HIS C O   
4789 C  CB  . HIS C  66  ? 0.3743 0.2597 0.1592 -0.0452 -0.0812 -0.0117 66  HIS C CB  
4790 C  CG  . HIS C  66  ? 0.4110 0.3054 0.1595 -0.0472 -0.0732 -0.0211 66  HIS C CG  
4791 N  ND1 . HIS C  66  ? 0.3825 0.3192 0.2323 -0.0511 -0.1108 -0.0288 66  HIS C ND1 
4792 C  CD2 . HIS C  66  ? 0.3770 0.3401 0.1673 -0.0151 -0.0633 -0.0234 66  HIS C CD2 
4793 C  CE1 . HIS C  66  ? 0.3684 0.3319 0.2617 -0.0483 0.0204  -0.0381 66  HIS C CE1 
4794 N  NE2 . HIS C  66  ? 0.4149 0.3711 0.3224 0.0017  -0.0308 -0.0464 66  HIS C NE2 
4795 N  N   . SER C  67  ? 0.3394 0.2727 0.2369 0.0069  -0.0740 -0.0625 67  SER C N   
4796 C  CA  . SER C  67  ? 0.2719 0.2467 0.1265 -0.0438 -0.0497 -0.0206 67  SER C CA  
4797 C  C   . SER C  67  ? 0.3358 0.2675 0.2167 -0.0398 -0.0136 -0.0168 67  SER C C   
4798 O  O   . SER C  67  ? 0.3018 0.3098 0.1890 -0.0545 -0.0646 -0.0117 67  SER C O   
4799 C  CB  . SER C  67  ? 0.3721 0.2823 0.1885 0.0044  -0.0256 -0.0472 67  SER C CB  
4800 O  OG  . SER C  67  ? 0.2449 0.3582 0.1407 -0.0212 -0.0406 -0.0455 67  SER C OG  
4801 N  N   . VAL C  68  ? 0.2151 0.3197 0.1396 -0.0122 -0.0299 0.0076  68  VAL C N   
4802 C  CA  . VAL C  68  ? 0.2187 0.3082 0.1805 -0.0671 -0.0262 -0.0094 68  VAL C CA  
4803 C  C   . VAL C  68  ? 0.2960 0.3483 0.1450 -0.0374 -0.0283 -0.0333 68  VAL C C   
4804 O  O   . VAL C  68  ? 0.2614 0.3006 0.1551 -0.0186 -0.0297 -0.0219 68  VAL C O   
4805 C  CB  . VAL C  68  ? 0.2469 0.3118 0.2216 -0.0140 -0.0705 0.0438  68  VAL C CB  
4806 C  CG1 . VAL C  68  ? 0.3044 0.2588 0.2040 0.0040  -0.0117 0.0416  68  VAL C CG1 
4807 C  CG2 . VAL C  68  ? 0.2927 0.4241 0.2288 -0.0528 -0.1093 0.0055  68  VAL C CG2 
4808 N  N   . LYS C  69  ? 0.2649 0.3212 0.1599 0.0069  -0.0363 -0.0037 69  LYS C N   
4809 C  CA  . LYS C  69  ? 0.2196 0.2454 0.1575 0.0049  -0.0331 -0.0211 69  LYS C CA  
4810 C  C   . LYS C  69  ? 0.2558 0.2464 0.1947 0.0000  -0.0744 -0.0281 69  LYS C C   
4811 O  O   . LYS C  69  ? 0.3031 0.3105 0.2282 0.0198  -0.0928 -0.0825 69  LYS C O   
4812 C  CB  . LYS C  69  ? 0.4551 0.4395 0.2355 0.0992  0.0409  0.1711  69  LYS C CB  
4813 C  CG  . LYS C  69  ? 0.3224 0.4720 0.3716 0.0810  -0.0024 0.1717  69  LYS C CG  
4814 C  CD  . LYS C  69  ? 0.5662 0.3523 0.3154 0.0044  -0.0910 0.0889  69  LYS C CD  
4815 C  CE  . LYS C  69  ? 0.5299 0.4280 0.3211 0.0305  -0.0160 0.0450  69  LYS C CE  
4816 N  NZ  . LYS C  69  ? 0.5421 0.4426 0.3626 -0.0864 -0.0519 0.1196  69  LYS C NZ  
4817 N  N   . LEU C  70  ? 0.1784 0.3234 0.1592 -0.0036 -0.0807 -0.0573 70  LEU C N   
4818 C  CA  . LEU C  70  ? 0.1798 0.2250 0.2377 -0.0077 -0.0628 -0.0171 70  LEU C CA  
4819 C  C   . LEU C  70  ? 0.2286 0.2319 0.1576 -0.0308 -0.0502 -0.0326 70  LEU C C   
4820 O  O   . LEU C  70  ? 0.2271 0.2426 0.1777 -0.0091 -0.0681 -0.0160 70  LEU C O   
4821 C  CB  . LEU C  70  ? 0.1989 0.1861 0.2340 0.0124  -0.1036 -0.0308 70  LEU C CB  
4822 C  CG  . LEU C  70  ? 0.2498 0.2594 0.2281 0.0387  -0.0785 0.0111  70  LEU C CG  
4823 C  CD1 . LEU C  70  ? 0.2699 0.3647 0.2575 0.0102  -0.1445 0.0130  70  LEU C CD1 
4824 C  CD2 . LEU C  70  ? 0.2715 0.2594 0.2287 0.0854  -0.1226 -0.0759 70  LEU C CD2 
4825 N  N   . ASN C  71  ? 0.1951 0.2381 0.2267 -0.0140 -0.0527 -0.0310 71  ASN C N   
4826 C  CA  . ASN C  71  ? 0.2910 0.2315 0.2342 -0.0748 -0.0139 -0.0296 71  ASN C CA  
4827 C  C   . ASN C  71  ? 0.2606 0.2233 0.1998 -0.0126 -0.1249 -0.0472 71  ASN C C   
4828 O  O   . ASN C  71  ? 0.3468 0.3286 0.2194 0.0266  -0.0741 0.0263  71  ASN C O   
4829 C  CB  . ASN C  71  ? 0.2245 0.2810 0.2609 -0.0091 -0.0610 -0.0378 71  ASN C CB  
4830 C  CG  . ASN C  71  ? 0.3283 0.2852 0.4292 -0.0332 -0.0541 -0.0620 71  ASN C CG  
4831 O  OD1 . ASN C  71  ? 0.3829 0.2789 0.2958 -0.0348 -0.0319 -0.0216 71  ASN C OD1 
4832 N  ND2 . ASN C  71  ? 0.3861 0.3147 0.3592 -0.0807 -0.0468 -0.0289 71  ASN C ND2 
4833 N  N   . LEU C  72  ? 0.2316 0.2975 0.1746 -0.0124 -0.0612 -0.0423 72  LEU C N   
4834 C  CA  . LEU C  72  ? 0.2132 0.2615 0.2342 0.0241  -0.0728 -0.0274 72  LEU C CA  
4835 C  C   . LEU C  72  ? 0.2149 0.2380 0.2843 0.0142  -0.0549 0.0006  72  LEU C C   
4836 O  O   . LEU C  72  ? 0.2345 0.3110 0.2421 0.0339  -0.0122 0.0087  72  LEU C O   
4837 C  CB  . LEU C  72  ? 0.1974 0.2939 0.1852 0.0040  -0.0692 -0.0027 72  LEU C CB  
4838 C  CG  . LEU C  72  ? 0.2118 0.2782 0.1811 0.0073  -0.0702 0.0021  72  LEU C CG  
4839 C  CD1 . LEU C  72  ? 0.2396 0.2999 0.2095 -0.0275 -0.0996 0.0085  72  LEU C CD1 
4840 C  CD2 . LEU C  72  ? 0.2132 0.2724 0.2666 0.0307  -0.0363 0.0247  72  LEU C CD2 
4841 N  N   . PRO C  73  ? 0.3076 0.2888 0.2214 0.0192  -0.0152 -0.0392 73  PRO C N   
4842 C  CA  . PRO C  73  ? 0.2667 0.3604 0.2584 -0.0242 -0.0734 0.0251  73  PRO C CA  
4843 C  C   . PRO C  73  ? 0.1790 0.4827 0.2698 -0.0660 -0.0219 -0.0134 73  PRO C C   
4844 O  O   . PRO C  73  ? 0.2478 0.4374 0.2561 0.0446  -0.0653 -0.0263 73  PRO C O   
4845 C  CB  . PRO C  73  ? 0.2902 0.3508 0.2702 0.0108  -0.1024 0.0055  73  PRO C CB  
4846 C  CG  . PRO C  73  ? 0.2341 0.3051 0.2766 -0.0108 -0.0370 -0.0256 73  PRO C CG  
4847 C  CD  . PRO C  73  ? 0.2225 0.2398 0.3664 0.0335  -0.0436 -0.0214 73  PRO C CD  
4848 N  N   . SER C  74  ? 0.2888 0.3973 0.2896 0.0140  -0.0140 0.0361  74  SER C N   
4849 C  CA  . SER C  74  ? 0.2868 0.4862 0.3021 -0.0694 -0.0364 0.0580  74  SER C CA  
4850 C  C   . SER C  74  ? 0.3989 0.6032 0.3393 -0.0027 -0.1752 -0.0380 74  SER C C   
4851 O  O   . SER C  74  ? 0.2013 0.6190 0.3025 -0.0392 -0.0150 -0.0453 74  SER C O   
4852 C  CB  . SER C  74  ? 0.4847 0.5818 0.4472 -0.0829 -0.0377 0.1552  74  SER C CB  
4853 O  OG  . SER C  74  ? 0.4145 0.7694 0.3342 -0.0717 0.0391  -0.0054 74  SER C OG  
4854 N  N   . ASP C  75  ? 0.3107 0.4663 0.3835 -0.0386 -0.0500 -0.0291 75  ASP C N   
4855 C  CA  . ASP C  75  ? 0.2547 0.4110 0.4989 0.0480  -0.1270 -0.0468 75  ASP C CA  
4856 C  C   . ASP C  75  ? 0.2991 0.4110 0.4071 -0.0236 0.0379  0.0823  75  ASP C C   
4857 O  O   . ASP C  75  ? 0.1745 0.6066 0.4542 0.0602  -0.0527 -0.1188 75  ASP C O   
4858 C  CB  . ASP C  75  ? 0.3416 0.4562 0.3427 -0.0100 -0.1232 -0.0419 75  ASP C CB  
4859 C  CG  . ASP C  75  ? 0.2870 0.4611 0.3545 0.1087  -0.0935 -0.0719 75  ASP C CG  
4860 O  OD1 . ASP C  75  ? 0.2892 0.7050 0.3353 0.1247  -0.0062 -0.1070 75  ASP C OD1 
4861 O  OD2 . ASP C  75  ? 0.3671 0.4174 0.6782 -0.0436 0.1858  0.1017  75  ASP C OD2 
4862 N  N   . MET C  76  ? 0.2606 0.3513 0.2740 0.0450  -0.0816 -0.0262 76  MET C N   
4863 C  CA  . MET C  76  ? 0.2339 0.3101 0.2086 -0.0165 -0.0100 -0.0044 76  MET C CA  
4864 C  C   . MET C  76  ? 0.2640 0.3068 0.2186 0.0635  0.0164  0.0085  76  MET C C   
4865 O  O   . MET C  76  ? 0.1749 0.3481 0.2757 0.0179  -0.0277 0.0179  76  MET C O   
4866 C  CB  . MET C  76  ? 0.2234 0.3533 0.3328 0.0397  0.0223  0.0084  76  MET C CB  
4867 C  CG  . MET C  76  ? 0.1895 0.3726 0.2921 -0.0134 0.0334  -0.0073 76  MET C CG  
4868 S  SD  . MET C  76  ? 0.2287 0.2899 0.3703 -0.0103 0.0376  -0.0012 76  MET C SD  
4869 C  CE  . MET C  76  ? 0.2130 0.3222 0.3297 -0.0296 0.0403  0.0453  76  MET C CE  
4870 N  N   . HIS C  77  ? 0.1421 0.3583 0.2526 -0.0189 -0.0394 0.0207  77  HIS C N   
4871 C  CA  . HIS C  77  ? 0.1691 0.3634 0.2627 -0.0283 -0.0326 -0.0119 77  HIS C CA  
4872 C  C   . HIS C  77  ? 0.2434 0.2956 0.2057 0.0005  -0.0156 -0.0010 77  HIS C C   
4873 O  O   . HIS C  77  ? 0.1936 0.3545 0.2727 0.0288  -0.0100 0.0300  77  HIS C O   
4874 C  CB  . HIS C  77  ? 0.2423 0.4735 0.2803 -0.0510 0.0373  -0.0340 77  HIS C CB  
4875 C  CG  . HIS C  77  ? 0.2965 0.4292 0.2077 -0.0024 0.0292  0.0057  77  HIS C CG  
4876 N  ND1 . HIS C  77  ? 0.2856 0.4863 0.3139 -0.0955 -0.0155 -0.0681 77  HIS C ND1 
4877 C  CD2 . HIS C  77  ? 0.2223 0.3995 0.3303 -0.0128 -0.0011 -0.0441 77  HIS C CD2 
4878 C  CE1 . HIS C  77  ? 0.2948 0.4776 0.3832 -0.0669 -0.0072 -0.0252 77  HIS C CE1 
4879 N  NE2 . HIS C  77  ? 0.1872 0.5028 0.3865 -0.0129 0.0458  -0.0044 77  HIS C NE2 
4880 N  N   . ILE C  78  ? 0.2216 0.3188 0.2605 -0.0021 -0.0322 -0.0106 78  ILE C N   
4881 C  CA  . ILE C  78  ? 0.2444 0.2794 0.2493 -0.0043 0.0113  -0.0247 78  ILE C CA  
4882 C  C   . ILE C  78  ? 0.2129 0.3213 0.2842 -0.0279 -0.0285 0.0642  78  ILE C C   
4883 O  O   . ILE C  78  ? 0.2489 0.3717 0.2768 -0.0379 0.0119  0.0436  78  ILE C O   
4884 C  CB  . ILE C  78  ? 0.2113 0.3488 0.2126 -0.0040 -0.0144 0.0001  78  ILE C CB  
4885 C  CG1 . ILE C  78  ? 0.2067 0.3768 0.2608 -0.0392 0.0174  0.0157  78  ILE C CG1 
4886 C  CG2 . ILE C  78  ? 0.2353 0.3504 0.2742 0.0482  0.0146  -0.0497 78  ILE C CG2 
4887 C  CD1 . ILE C  78  ? 0.2221 0.3551 0.2176 -0.0128 -0.0125 -0.0111 78  ILE C CD1 
4888 N  N   . GLN C  79  ? 0.2672 0.3644 0.2559 -0.0141 0.0116  -0.0013 79  GLN C N   
4889 C  CA  . GLN C  79  ? 0.3116 0.4663 0.3403 0.0738  -0.0212 -0.1190 79  GLN C CA  
4890 C  C   . GLN C  79  ? 0.3061 0.3202 0.3129 0.0705  0.0159  -0.0064 79  GLN C C   
4891 O  O   . GLN C  79  ? 0.2861 0.3944 0.4045 0.0142  -0.0432 0.0500  79  GLN C O   
4892 C  CB  . GLN C  79  ? 0.3345 0.4801 0.4200 0.0589  -0.0502 -0.1279 79  GLN C CB  
4893 C  CG  . GLN C  79  ? 0.3983 0.9871 0.6637 0.3416  0.2162  -0.1430 79  GLN C CG  
4894 C  CD  . GLN C  79  ? 0.5127 0.9828 0.9277 0.1746  0.0923  -0.1525 79  GLN C CD  
4895 O  OE1 . GLN C  79  ? 0.8659 0.9697 0.8517 0.3846  0.0939  -0.0407 79  GLN C OE1 
4896 N  NE2 . GLN C  79  ? 0.4986 0.9078 0.4607 0.1372  0.1342  0.0536  79  GLN C NE2 
4897 N  N   . GLY C  80  ? 0.3507 0.4561 0.2537 0.0365  0.0546  -0.0012 80  GLY C N   
4898 C  CA  . GLY C  80  ? 0.2815 0.5123 0.3739 0.0413  0.0008  -0.0018 80  GLY C CA  
4899 C  C   . GLY C  80  ? 0.3240 0.3913 0.2808 0.0535  0.0572  -0.0811 80  GLY C C   
4900 O  O   . GLY C  80  ? 0.4126 0.4890 0.3336 -0.0363 0.0212  -0.1837 80  GLY C O   
4901 N  N   . LEU C  81  ? 0.2936 0.3467 0.2965 -0.0053 0.0082  -0.0252 81  LEU C N   
4902 C  CA  . LEU C  81  ? 0.3697 0.3365 0.2831 0.0030  0.0280  -0.0161 81  LEU C CA  
4903 C  C   . LEU C  81  ? 0.4040 0.4321 0.2312 -0.0125 0.0245  -0.0044 81  LEU C C   
4904 O  O   . LEU C  81  ? 0.3687 0.4667 0.2970 -0.0266 0.0601  -0.0546 81  LEU C O   
4905 C  CB  . LEU C  81  ? 0.3028 0.3158 0.2661 -0.0662 0.0080  -0.0447 81  LEU C CB  
4906 C  CG  . LEU C  81  ? 0.2521 0.3314 0.3078 -0.0857 -0.0280 0.0103  81  LEU C CG  
4907 C  CD1 . LEU C  81  ? 0.3632 0.4348 0.2629 -0.0719 0.0504  0.0103  81  LEU C CD1 
4908 C  CD2 . LEU C  81  ? 0.2335 0.3398 0.3168 -0.0236 -0.0257 -0.0003 81  LEU C CD2 
4909 N  N   . GLN C  82  ? 0.3565 0.4617 0.2157 -0.0814 -0.0517 0.0070  82  GLN C N   
4910 C  CA  . GLN C  82  ? 0.5516 0.5061 0.1737 -0.0889 0.0570  0.0084  82  GLN C CA  
4911 C  C   . GLN C  82  ? 0.4047 0.4731 0.2174 -0.0326 0.0582  0.0288  82  GLN C C   
4912 O  O   . GLN C  82  ? 0.4829 0.5077 0.2833 -0.0784 0.1231  0.0434  82  GLN C O   
4913 C  CB  . GLN C  82  ? 0.4945 0.5471 0.3085 -0.0181 0.0917  0.1523  82  GLN C CB  
4914 N  N   . SER C  83  ? 0.3091 0.4098 0.2315 -0.0741 0.0484  -0.0378 83  SER C N   
4915 C  CA  . SER C  83  ? 0.2643 0.3327 0.2052 -0.0361 -0.0110 0.0051  83  SER C CA  
4916 C  C   . SER C  83  ? 0.1804 0.3368 0.2386 -0.0212 0.0178  -0.0017 83  SER C C   
4917 O  O   . SER C  83  ? 0.1913 0.3031 0.2020 -0.0284 0.0076  0.0060  83  SER C O   
4918 C  CB  . SER C  83  ? 0.2922 0.2917 0.3299 0.0006  -0.0429 0.0531  83  SER C CB  
4919 O  OG  . SER C  83  ? 0.3511 0.4720 0.2497 0.0042  0.0019  0.0428  83  SER C OG  
4920 N  N   . ARG C  84  ? 0.2073 0.3089 0.1999 -0.0166 0.0174  0.0122  84  ARG C N   
4921 C  CA  . ARG C  84  ? 0.1814 0.2716 0.2286 -0.0027 -0.0323 -0.0409 84  ARG C CA  
4922 C  C   . ARG C  84  ? 0.1500 0.2502 0.1929 -0.0258 -0.0203 -0.0016 84  ARG C C   
4923 O  O   . ARG C  84  ? 0.1648 0.2850 0.2458 -0.0144 0.0179  0.0139  84  ARG C O   
4924 C  CB  . ARG C  84  ? 0.1712 0.4004 0.2664 -0.0344 -0.0138 -0.0278 84  ARG C CB  
4925 C  CG  . ARG C  84  ? 0.1736 0.3865 0.3273 -0.0383 -0.0617 0.0026  84  ARG C CG  
4926 C  CD  . ARG C  84  ? 0.1557 0.3572 0.3748 -0.0034 -0.0526 -0.0153 84  ARG C CD  
4927 N  NE  . ARG C  84  ? 0.1828 0.3305 0.3113 0.0212  -0.0266 0.0203  84  ARG C NE  
4928 C  CZ  . ARG C  84  ? 0.2079 0.3449 0.2592 0.0154  -0.0141 0.0038  84  ARG C CZ  
4929 N  NH1 . ARG C  84  ? 0.2058 0.4110 0.3224 0.0252  -0.0019 -0.0013 84  ARG C NH1 
4930 N  NH2 . ARG C  84  ? 0.2539 0.2794 0.3673 0.0117  0.0725  0.0401  84  ARG C NH2 
4931 N  N   . TYR C  85  ? 0.1593 0.3073 0.2036 -0.0082 -0.0148 0.0136  85  TYR C N   
4932 C  CA  . TYR C  85  ? 0.1349 0.3318 0.2115 -0.0079 -0.0260 -0.0250 85  TYR C CA  
4933 C  C   . TYR C  85  ? 0.1972 0.2795 0.2438 0.0057  0.0257  -0.0167 85  TYR C C   
4934 O  O   . TYR C  85  ? 0.1865 0.3158 0.2289 0.0012  -0.0518 0.0471  85  TYR C O   
4935 C  CB  . TYR C  85  ? 0.1253 0.3877 0.1823 -0.0286 -0.0039 0.0009  85  TYR C CB  
4936 C  CG  . TYR C  85  ? 0.1430 0.2891 0.1497 -0.0319 -0.0046 -0.0105 85  TYR C CG  
4937 C  CD1 . TYR C  85  ? 0.1512 0.2748 0.2030 -0.0167 -0.0193 -0.0109 85  TYR C CD1 
4938 C  CD2 . TYR C  85  ? 0.1629 0.3101 0.2204 -0.0358 0.0055  0.0032  85  TYR C CD2 
4939 C  CE1 . TYR C  85  ? 0.1976 0.2293 0.1706 -0.0166 -0.0134 0.0174  85  TYR C CE1 
4940 C  CE2 . TYR C  85  ? 0.1701 0.2971 0.1981 -0.0256 0.0245  -0.0091 85  TYR C CE2 
4941 C  CZ  . TYR C  85  ? 0.1536 0.2807 0.2303 -0.0153 0.0058  -0.0220 85  TYR C CZ  
4942 O  OH  . TYR C  85  ? 0.2062 0.3157 0.2197 -0.0270 -0.0283 0.0203  85  TYR C OH  
4943 N  N   . SER C  86  ? 0.1661 0.3098 0.1815 -0.0093 -0.0078 -0.0134 86  SER C N   
4944 C  CA  . SER C  86  ? 0.1832 0.3088 0.2007 -0.0175 -0.0314 -0.0071 86  SER C CA  
4945 C  C   . SER C  86  ? 0.2811 0.2445 0.1689 0.0450  0.0021  0.0118  86  SER C C   
4946 O  O   . SER C  86  ? 0.1924 0.2475 0.2408 -0.0237 -0.0250 0.0129  86  SER C O   
4947 C  CB  . SER C  86  ? 0.1562 0.4423 0.2294 -0.0757 -0.0042 -0.0082 86  SER C CB  
4948 O  OG  . SER C  86  ? 0.1497 0.4345 0.2442 -0.0268 -0.0141 -0.0174 86  SER C OG  
4949 N  N   . ALA C  87  ? 0.1544 0.3173 0.2312 -0.0069 -0.0179 0.0049  87  ALA C N   
4950 C  CA  . ALA C  87  ? 0.1606 0.2467 0.2133 -0.0060 0.0080  0.0035  87  ALA C CA  
4951 C  C   . ALA C  87  ? 0.1865 0.2508 0.1940 -0.0083 -0.0203 -0.0168 87  ALA C C   
4952 O  O   . ALA C  87  ? 0.1805 0.2784 0.2258 -0.0354 -0.0196 -0.0179 87  ALA C O   
4953 C  CB  . ALA C  87  ? 0.2097 0.3231 0.2147 0.0127  0.0037  0.0276  87  ALA C CB  
4954 N  N   . THR C  88  ? 0.1782 0.2215 0.2374 -0.0006 -0.0015 -0.0067 88  THR C N   
4955 C  CA  . THR C  88  ? 0.2026 0.2324 0.2027 -0.0219 -0.0187 -0.0065 88  THR C CA  
4956 C  C   . THR C  88  ? 0.1821 0.2299 0.1843 -0.0178 -0.0328 -0.0290 88  THR C C   
4957 O  O   . THR C  88  ? 0.2250 0.2366 0.1870 -0.0187 -0.0370 -0.0030 88  THR C O   
4958 C  CB  . THR C  88  ? 0.1753 0.2033 0.2456 -0.0094 -0.0273 -0.0170 88  THR C CB  
4959 O  OG1 . THR C  88  ? 0.2418 0.2901 0.2409 -0.0131 -0.0403 -0.0392 88  THR C OG1 
4960 C  CG2 . THR C  88  ? 0.1873 0.2476 0.2383 -0.0012 -0.0388 -0.0104 88  THR C CG2 
4961 N  N   . GLN C  89  ? 0.2271 0.2928 0.1471 -0.0544 -0.0284 0.0006  89  GLN C N   
4962 C  CA  . GLN C  89  ? 0.1559 0.2325 0.1900 -0.0060 -0.0726 -0.0252 89  GLN C CA  
4963 C  C   . GLN C  89  ? 0.2276 0.2193 0.1775 -0.0166 -0.0240 -0.0068 89  GLN C C   
4964 O  O   . GLN C  89  ? 0.1744 0.2828 0.1460 -0.0306 -0.0488 -0.0104 89  GLN C O   
4965 C  CB  . GLN C  89  ? 0.2655 0.2372 0.1967 0.0388  -0.0351 0.0000  89  GLN C CB  
4966 C  CG  . GLN C  89  ? 0.2142 0.3327 0.2158 0.0013  -0.0377 0.0050  89  GLN C CG  
4967 C  CD  . GLN C  89  ? 0.2167 0.2627 0.1781 0.0066  -0.0138 -0.0181 89  GLN C CD  
4968 O  OE1 . GLN C  89  ? 0.2320 0.3612 0.1916 -0.0713 -0.0504 -0.0024 89  GLN C OE1 
4969 N  NE2 . GLN C  89  ? 0.2930 0.3010 0.3265 0.0250  -0.0535 -0.0511 89  GLN C NE2 
4970 N  N   . LEU C  90  ? 0.1888 0.2614 0.1939 -0.0397 -0.0471 0.0245  90  LEU C N   
4971 C  CA  . LEU C  90  ? 0.1934 0.1916 0.1569 -0.0222 -0.0221 0.0008  90  LEU C CA  
4972 C  C   . LEU C  90  ? 0.1923 0.2226 0.1662 -0.0094 -0.0096 -0.0361 90  LEU C C   
4973 O  O   . LEU C  90  ? 0.2206 0.2389 0.1543 -0.0106 -0.0409 -0.0171 90  LEU C O   
4974 C  CB  . LEU C  90  ? 0.1956 0.2223 0.1445 0.0093  -0.0464 -0.0108 90  LEU C CB  
4975 C  CG  . LEU C  90  ? 0.2500 0.1969 0.1579 -0.0026 -0.0571 0.0273  90  LEU C CG  
4976 C  CD1 . LEU C  90  ? 0.2102 0.2870 0.1595 0.0072  -0.0535 0.0209  90  LEU C CD1 
4977 C  CD2 . LEU C  90  ? 0.2797 0.2001 0.1964 0.0189  -0.1264 0.0228  90  LEU C CD2 
4978 N  N   . HIS C  91  ? 0.1775 0.2857 0.1404 -0.0181 -0.0151 -0.0087 91  HIS C N   
4979 C  CA  . HIS C  91  ? 0.1882 0.2196 0.1028 -0.0210 -0.0294 -0.0118 91  HIS C CA  
4980 C  C   . HIS C  91  ? 0.2240 0.2479 0.0985 -0.0484 -0.0181 0.0067  91  HIS C C   
4981 O  O   . HIS C  91  ? 0.1675 0.2715 0.1637 -0.0120 -0.0374 -0.0221 91  HIS C O   
4982 C  CB  . HIS C  91  ? 0.2073 0.2271 0.1493 -0.0001 -0.0480 -0.0138 91  HIS C CB  
4983 C  CG  . HIS C  91  ? 0.1879 0.2597 0.1209 -0.0302 -0.0244 -0.0220 91  HIS C CG  
4984 N  ND1 . HIS C  91  ? 0.1790 0.2552 0.1230 -0.0197 -0.0219 -0.0021 91  HIS C ND1 
4985 C  CD2 . HIS C  91  ? 0.1858 0.2561 0.1091 0.0013  -0.0738 -0.0311 91  HIS C CD2 
4986 C  CE1 . HIS C  91  ? 0.1805 0.2560 0.1350 -0.0383 -0.0414 -0.0037 91  HIS C CE1 
4987 N  NE2 . HIS C  91  ? 0.1989 0.2684 0.1156 0.0013  -0.0284 -0.0033 91  HIS C NE2 
4988 N  N   . LEU C  92  ? 0.1811 0.2903 0.1316 -0.0276 -0.0295 0.0291  92  LEU C N   
4989 C  CA  . LEU C  92  ? 0.2725 0.2693 0.1388 -0.0223 -0.0044 0.0362  92  LEU C CA  
4990 C  C   . LEU C  92  ? 0.1775 0.1870 0.1168 0.0012  -0.0252 0.0120  92  LEU C C   
4991 O  O   . LEU C  92  ? 0.2112 0.2750 0.1400 -0.0201 -0.0218 0.0111  92  LEU C O   
4992 C  CB  . LEU C  92  ? 0.2142 0.3060 0.1825 0.0303  -0.0247 0.0597  92  LEU C CB  
4993 C  CG  . LEU C  92  ? 0.2663 0.2367 0.1883 0.0304  -0.0436 0.0601  92  LEU C CG  
4994 C  CD1 . LEU C  92  ? 0.2548 0.6019 0.4428 0.0230  -0.1676 -0.0876 92  LEU C CD1 
4995 C  CD2 . LEU C  92  ? 0.2230 0.2269 0.2992 0.0117  -0.0051 0.0427  92  LEU C CD2 
4996 N  N   . HIS C  93  ? 0.1907 0.2798 0.1195 -0.0110 -0.0197 0.0256  93  HIS C N   
4997 C  CA  . HIS C  93  ? 0.1845 0.2420 0.1359 -0.0023 -0.0324 0.0322  93  HIS C CA  
4998 C  C   . HIS C  93  ? 0.2042 0.2265 0.1338 -0.0005 -0.0467 0.0074  93  HIS C C   
4999 O  O   . HIS C  93  ? 0.1839 0.2463 0.1229 -0.0075 -0.0121 0.0292  93  HIS C O   
5000 C  CB  . HIS C  93  ? 0.1641 0.2662 0.1264 -0.0304 -0.0455 0.0339  93  HIS C CB  
5001 C  CG  . HIS C  93  ? 0.1610 0.2064 0.1003 -0.0100 -0.0234 0.0018  93  HIS C CG  
5002 N  ND1 . HIS C  93  ? 0.1737 0.2142 0.1466 -0.0043 -0.0156 0.0136  93  HIS C ND1 
5003 C  CD2 . HIS C  93  ? 0.1657 0.2448 0.1115 -0.0204 -0.0435 -0.0009 93  HIS C CD2 
5004 C  CE1 . HIS C  93  ? 0.1581 0.2148 0.1271 -0.0245 -0.0096 0.0013  93  HIS C CE1 
5005 N  NE2 . HIS C  93  ? 0.1891 0.2061 0.1254 -0.0118 -0.0478 -0.0114 93  HIS C NE2 
5006 N  N   . TRP C  94  ? 0.2103 0.2621 0.1058 -0.0337 -0.0264 0.0053  94  TRP C N   
5007 C  CA  . TRP C  94  ? 0.1836 0.2664 0.1230 -0.0078 -0.0256 0.0362  94  TRP C CA  
5008 C  C   . TRP C  94  ? 0.2110 0.2307 0.1079 -0.0065 -0.0141 0.0098  94  TRP C C   
5009 O  O   . TRP C  94  ? 0.1980 0.2467 0.1228 -0.0167 0.0009  0.0036  94  TRP C O   
5010 C  CB  . TRP C  94  ? 0.2229 0.2970 0.1143 -0.0259 -0.0313 0.0086  94  TRP C CB  
5011 C  CG  . TRP C  94  ? 0.2460 0.3265 0.0858 -0.0275 -0.0329 0.0041  94  TRP C CG  
5012 C  CD1 . TRP C  94  ? 0.2389 0.2960 0.1328 -0.0069 -0.0069 0.0259  94  TRP C CD1 
5013 C  CD2 . TRP C  94  ? 0.2213 0.2973 0.1439 -0.0167 -0.0533 -0.0194 94  TRP C CD2 
5014 N  NE1 . TRP C  94  ? 0.2301 0.3049 0.1345 -0.0252 -0.0258 -0.0047 94  TRP C NE1 
5015 C  CE2 . TRP C  94  ? 0.2550 0.3243 0.1163 -0.0497 -0.0232 0.0146  94  TRP C CE2 
5016 C  CE3 . TRP C  94  ? 0.2511 0.3565 0.1089 -0.0543 -0.0070 0.0495  94  TRP C CE3 
5017 C  CZ2 . TRP C  94  ? 0.2311 0.3133 0.1266 -0.0186 -0.0238 0.0027  94  TRP C CZ2 
5018 C  CZ3 . TRP C  94  ? 0.2001 0.3606 0.1565 -0.0293 -0.0344 -0.0087 94  TRP C CZ3 
5019 C  CH2 . TRP C  94  ? 0.2363 0.3587 0.1210 -0.0272 -0.0241 0.0261  94  TRP C CH2 
5020 N  N   . GLY C  95  ? 0.1897 0.3046 0.1287 -0.0181 -0.0083 0.0328  95  GLY C N   
5021 C  CA  . GLY C  95  ? 0.2021 0.3169 0.1233 -0.0352 0.0086  0.0160  95  GLY C CA  
5022 C  C   . GLY C  95  ? 0.2361 0.3076 0.1454 -0.0499 -0.0030 0.0054  95  GLY C C   
5023 O  O   . GLY C  95  ? 0.2298 0.3009 0.1295 -0.0088 0.0119  0.0108  95  GLY C O   
5024 N  N   . ASN C  96  ? 0.2655 0.3468 0.1353 -0.0418 0.0133  0.0134  96  ASN C N   
5025 C  CA  . ASN C  96  ? 0.2810 0.3463 0.1418 -0.0491 0.0128  0.0240  96  ASN C CA  
5026 C  C   . ASN C  96  ? 0.2366 0.3109 0.1543 -0.0099 -0.0046 0.0071  96  ASN C C   
5027 O  O   . ASN C  96  ? 0.2734 0.3261 0.1486 -0.0502 0.0179  0.0207  96  ASN C O   
5028 C  CB  . ASN C  96  ? 0.3608 0.3133 0.1897 -0.0408 0.0340  -0.0208 96  ASN C CB  
5029 C  CG  . ASN C  96  ? 0.2809 0.4344 0.2478 -0.0332 0.0753  0.0749  96  ASN C CG  
5030 O  OD1 . ASN C  96  ? 0.2931 0.5626 0.3937 -0.0502 0.1194  0.1356  96  ASN C OD1 
5031 N  ND2 . ASN C  96  ? 0.2719 0.4770 0.2717 -0.0017 0.0418  0.0419  96  ASN C ND2 
5032 N  N   . PRO C  97  ? 0.2815 0.3635 0.1495 -0.0445 0.0139  0.0027  97  PRO C N   
5033 C  CA  . PRO C  97  ? 0.2952 0.4245 0.1611 -0.0200 -0.0046 0.0802  97  PRO C CA  
5034 C  C   . PRO C  97  ? 0.3281 0.3259 0.1577 -0.0499 0.0351  0.0507  97  PRO C C   
5035 O  O   . PRO C  97  ? 0.3185 0.3621 0.2197 -0.0513 0.0266  0.0366  97  PRO C O   
5036 C  CB  . PRO C  97  ? 0.3709 0.4347 0.1621 -0.0068 -0.0099 0.0573  97  PRO C CB  
5037 C  CG  . PRO C  97  ? 0.3859 0.4616 0.1627 -0.0507 -0.0490 0.0431  97  PRO C CG  
5038 C  CD  . PRO C  97  ? 0.2810 0.4544 0.1290 -0.0996 -0.0292 -0.0151 97  PRO C CD  
5039 N  N   . ASN C  98  ? 0.2797 0.4181 0.1542 -0.0038 0.0409  0.0212  98  ASN C N   
5040 C  CA  . ASN C  98  ? 0.3367 0.4424 0.1986 -0.0680 0.0289  0.0073  98  ASN C CA  
5041 C  C   . ASN C  98  ? 0.2949 0.4240 0.1888 -0.0933 0.0257  0.0181  98  ASN C C   
5042 O  O   . ASN C  98  ? 0.2836 0.5116 0.2130 -0.1018 0.0409  -0.0105 98  ASN C O   
5043 C  CB  . ASN C  98  ? 0.3433 0.4095 0.2026 -0.0296 -0.0126 -0.0301 98  ASN C CB  
5044 C  CG  . ASN C  98  ? 0.5942 0.5071 0.2416 0.0050  -0.0036 -0.0333 98  ASN C CG  
5045 O  OD1 . ASN C  98  ? 0.5359 0.6888 0.2605 0.0135  0.1497  0.0445  98  ASN C OD1 
5046 N  ND2 . ASN C  98  ? 0.7463 0.5443 0.4028 -0.0161 -0.0812 -0.1506 98  ASN C ND2 
5047 N  N   . ASP C  99  ? 0.2882 0.3840 0.1507 -0.0446 0.0108  0.0209  99  ASP C N   
5048 C  CA  . ASP C  99  ? 0.2478 0.3703 0.1507 -0.0348 0.0190  -0.0275 99  ASP C CA  
5049 C  C   . ASP C  99  ? 0.2292 0.2805 0.1663 -0.0452 -0.0065 0.0080  99  ASP C C   
5050 O  O   . ASP C  99  ? 0.2866 0.2987 0.1656 -0.0361 0.0132  -0.0116 99  ASP C O   
5051 C  CB  . ASP C  99  ? 0.1967 0.4099 0.1990 0.0025  0.0368  -0.0130 99  ASP C CB  
5052 C  CG  . ASP C  99  ? 0.3651 0.3977 0.2220 -0.0215 0.0265  -0.0117 99  ASP C CG  
5053 O  OD1 . ASP C  99  ? 0.4717 0.4281 0.1693 -0.0945 -0.0334 0.0258  99  ASP C OD1 
5054 O  OD2 . ASP C  99  ? 0.3590 0.4231 0.3532 0.0811  -0.0832 -0.0776 99  ASP C OD2 
5055 N  N   . PRO C  100 ? 0.2517 0.2912 0.1370 -0.0055 0.0089  0.0395  100 PRO C N   
5056 C  CA  . PRO C  100 ? 0.2404 0.3510 0.1697 -0.0084 0.0184  0.0594  100 PRO C CA  
5057 C  C   . PRO C  100 ? 0.2710 0.2873 0.2039 -0.0411 0.0309  0.0365  100 PRO C C   
5058 O  O   . PRO C  100 ? 0.2746 0.2855 0.1784 0.0075  0.0289  0.0700  100 PRO C O   
5059 C  CB  . PRO C  100 ? 0.2566 0.3708 0.1729 -0.0562 0.0173  0.0897  100 PRO C CB  
5060 C  CG  . PRO C  100 ? 0.3299 0.3240 0.2036 -0.0508 -0.0094 0.1264  100 PRO C CG  
5061 C  CD  . PRO C  100 ? 0.3215 0.3529 0.1742 -0.0204 0.0179  0.0908  100 PRO C CD  
5062 N  N   . HIS C  101 ? 0.2092 0.2684 0.1623 -0.0376 -0.0043 0.0227  101 HIS C N   
5063 C  CA  . HIS C  101 ? 0.2265 0.2692 0.1430 -0.0111 0.0312  0.0168  101 HIS C CA  
5064 C  C   . HIS C  101 ? 0.2417 0.3143 0.1717 -0.0292 -0.0034 0.0666  101 HIS C C   
5065 O  O   . HIS C  101 ? 0.2471 0.2631 0.3024 -0.0114 -0.0375 0.0528  101 HIS C O   
5066 C  CB  . HIS C  101 ? 0.2954 0.3431 0.1567 -0.1242 0.0006  0.0189  101 HIS C CB  
5067 C  CG  . HIS C  101 ? 0.2947 0.2960 0.2181 -0.0242 0.0274  0.0177  101 HIS C CG  
5068 N  ND1 . HIS C  101 ? 0.2972 0.3261 0.2832 -0.0076 0.0427  0.0229  101 HIS C ND1 
5069 C  CD2 . HIS C  101 ? 0.3267 0.3156 0.1835 -0.0738 0.0367  -0.0151 101 HIS C CD2 
5070 C  CE1 . HIS C  101 ? 0.3186 0.4036 0.3461 -0.0469 0.0510  0.0679  101 HIS C CE1 
5071 N  NE2 . HIS C  101 ? 0.3445 0.3490 0.2678 -0.0996 0.0049  0.0288  101 HIS C NE2 
5072 N  N   . GLY C  102 ? 0.1890 0.2456 0.1849 -0.0060 0.0003  0.0308  102 GLY C N   
5073 C  CA  . GLY C  102 ? 0.2216 0.2453 0.1409 -0.0264 0.0256  0.0245  102 GLY C CA  
5074 C  C   . GLY C  102 ? 0.2033 0.2133 0.1209 0.0016  -0.0364 0.0206  102 GLY C C   
5075 O  O   . GLY C  102 ? 0.2178 0.2321 0.1346 -0.0107 -0.0091 0.0234  102 GLY C O   
5076 N  N   . SER C  103 ? 0.1794 0.2288 0.1231 0.0091  -0.0055 0.0284  103 SER C N   
5077 C  CA  . SER C  103 ? 0.1689 0.2091 0.1208 -0.0006 -0.0062 0.0222  103 SER C CA  
5078 C  C   . SER C  103 ? 0.1670 0.2217 0.1372 -0.0013 -0.0228 0.0288  103 SER C C   
5079 O  O   . SER C  103 ? 0.1764 0.2284 0.1507 0.0003  0.0070  0.0603  103 SER C O   
5080 C  CB  . SER C  103 ? 0.1744 0.1937 0.1539 -0.0006 -0.0281 0.0282  103 SER C CB  
5081 O  OG  . SER C  103 ? 0.1900 0.2042 0.1292 -0.0168 -0.0150 0.0297  103 SER C OG  
5082 N  N   . GLU C  104 ? 0.1546 0.2075 0.0994 -0.0050 -0.0132 0.0233  104 GLU C N   
5083 C  CA  . GLU C  104 ? 0.1526 0.1907 0.1175 0.0020  -0.0227 0.0199  104 GLU C CA  
5084 C  C   . GLU C  104 ? 0.1367 0.1657 0.1227 0.0001  -0.0088 0.0139  104 GLU C C   
5085 O  O   . GLU C  104 ? 0.1427 0.1682 0.1286 0.0055  -0.0088 0.0111  104 GLU C O   
5086 C  CB  . GLU C  104 ? 0.1652 0.1941 0.1079 -0.0208 -0.0138 0.0178  104 GLU C CB  
5087 C  CG  . GLU C  104 ? 0.1733 0.2165 0.1395 -0.0135 -0.0353 -0.0041 104 GLU C CG  
5088 C  CD  . GLU C  104 ? 0.1663 0.2024 0.1366 0.0012  -0.0160 -0.0229 104 GLU C CD  
5089 O  OE1 . GLU C  104 ? 0.1735 0.2175 0.1332 -0.0108 -0.0055 0.0111  104 GLU C OE1 
5090 O  OE2 . GLU C  104 ? 0.1641 0.2011 0.1582 -0.0122 -0.0086 -0.0088 104 GLU C OE2 
5091 N  N   . HIS C  105 ? 0.1324 0.1621 0.1321 0.0081  -0.0078 0.0108  105 HIS C N   
5092 C  CA  . HIS C  105 ? 0.1580 0.1399 0.1210 -0.0034 0.0011  0.0044  105 HIS C CA  
5093 C  C   . HIS C  105 ? 0.1450 0.1455 0.1217 0.0150  -0.0205 0.0174  105 HIS C C   
5094 O  O   . HIS C  105 ? 0.1810 0.1928 0.1336 0.0032  -0.0192 0.0325  105 HIS C O   
5095 C  CB  . HIS C  105 ? 0.1401 0.1631 0.1390 0.0135  0.0091  0.0124  105 HIS C CB  
5096 C  CG  . HIS C  105 ? 0.1429 0.1536 0.1369 0.0078  0.0004  0.0210  105 HIS C CG  
5097 N  ND1 . HIS C  105 ? 0.1498 0.1879 0.1397 -0.0154 -0.0021 0.0181  105 HIS C ND1 
5098 C  CD2 . HIS C  105 ? 0.1434 0.1485 0.1335 0.0111  0.0004  0.0183  105 HIS C CD2 
5099 C  CE1 . HIS C  105 ? 0.1522 0.2033 0.1176 0.0099  -0.0102 0.0113  105 HIS C CE1 
5100 N  NE2 . HIS C  105 ? 0.1550 0.1804 0.1154 0.0249  0.0013  0.0145  105 HIS C NE2 
5101 N  N   . THR C  106 ? 0.1490 0.1417 0.1371 -0.0020 -0.0199 0.0219  106 THR C N   
5102 C  CA  . THR C  106 ? 0.1416 0.1647 0.1496 -0.0055 -0.0061 0.0248  106 THR C CA  
5103 C  C   . THR C  106 ? 0.1381 0.1678 0.1430 0.0098  -0.0088 0.0177  106 THR C C   
5104 O  O   . THR C  106 ? 0.1656 0.1608 0.1545 0.0010  0.0004  0.0208  106 THR C O   
5105 C  CB  . THR C  106 ? 0.1547 0.1866 0.1360 0.0201  -0.0067 0.0164  106 THR C CB  
5106 O  OG1 . THR C  106 ? 0.1626 0.1590 0.1691 0.0113  -0.0080 0.0346  106 THR C OG1 
5107 C  CG2 . THR C  106 ? 0.1939 0.1967 0.1444 0.0346  0.0208  0.0000  106 THR C CG2 
5108 N  N   . VAL C  107 ? 0.1676 0.1435 0.1762 0.0215  -0.0001 0.0113  107 VAL C N   
5109 C  CA  . VAL C  107 ? 0.1716 0.1547 0.1855 0.0207  -0.0044 0.0132  107 VAL C CA  
5110 C  C   . VAL C  107 ? 0.1859 0.1517 0.1800 0.0172  0.0220  0.0017  107 VAL C C   
5111 O  O   . VAL C  107 ? 0.1754 0.1538 0.2132 0.0105  0.0041  0.0194  107 VAL C O   
5112 C  CB  . VAL C  107 ? 0.1731 0.1714 0.2380 0.0310  -0.0167 0.0198  107 VAL C CB  
5113 C  CG1 . VAL C  107 ? 0.2379 0.1730 0.2555 0.0582  0.0255  0.0128  107 VAL C CG1 
5114 C  CG2 . VAL C  107 ? 0.1630 0.2517 0.2480 0.0173  0.0057  0.0446  107 VAL C CG2 
5115 N  N   . SER C  108 ? 0.1791 0.1540 0.2072 -0.0052 0.0005  -0.0044 108 SER C N   
5116 C  CA  . SER C  108 ? 0.1875 0.1870 0.2307 -0.0088 0.0185  -0.0299 108 SER C CA  
5117 C  C   . SER C  108 ? 0.1848 0.1809 0.1864 0.0054  0.0099  0.0232  108 SER C C   
5118 O  O   . SER C  108 ? 0.1958 0.1934 0.2211 -0.0134 0.0119  0.0342  108 SER C O   
5119 C  CB  . SER C  108 ? 0.2475 0.1708 0.2901 0.0272  0.0339  -0.0351 108 SER C CB  
5120 O  OG  . SER C  108 ? 0.2739 0.2804 0.3360 -0.0013 0.0152  -0.0408 108 SER C OG  
5121 N  N   . GLY C  109 ? 0.1816 0.1401 0.1996 0.0130  -0.0027 0.0210  109 GLY C N   
5122 C  CA  . GLY C  109 ? 0.1873 0.2002 0.1747 0.0243  0.0060  0.0019  109 GLY C CA  
5123 C  C   . GLY C  109 ? 0.1727 0.1879 0.1834 0.0100  0.0050  -0.0058 109 GLY C C   
5124 O  O   . GLY C  109 ? 0.1914 0.2357 0.2191 0.0386  -0.0033 -0.0099 109 GLY C O   
5125 N  N   . GLN C  110 ? 0.1694 0.1724 0.1779 0.0107  0.0076  0.0288  110 GLN C N   
5126 C  CA  . GLN C  110 ? 0.2097 0.1806 0.2107 -0.0100 -0.0124 0.0105  110 GLN C CA  
5127 C  C   . GLN C  110 ? 0.1770 0.1747 0.1752 0.0261  -0.0078 0.0318  110 GLN C C   
5128 O  O   . GLN C  110 ? 0.1661 0.1720 0.1681 0.0087  0.0059  0.0228  110 GLN C O   
5129 C  CB  . GLN C  110 ? 0.2323 0.1723 0.2372 -0.0130 -0.0214 0.0341  110 GLN C CB  
5130 C  CG  . GLN C  110 ? 0.2006 0.1742 0.3015 0.0063  0.0070  -0.0026 110 GLN C CG  
5131 C  CD  . GLN C  110 ? 0.2104 0.2272 0.2561 0.0244  -0.0037 -0.0143 110 GLN C CD  
5132 O  OE1 . GLN C  110 ? 0.2297 0.2500 0.3089 -0.0069 0.0430  0.0413  110 GLN C OE1 
5133 N  NE2 . GLN C  110 ? 0.2606 0.2280 0.2700 0.0281  0.0190  0.0369  110 GLN C NE2 
5134 N  N   . HIS C  111 ? 0.1784 0.1849 0.1664 0.0187  0.0168  0.0241  111 HIS C N   
5135 C  CA  . HIS C  111 ? 0.1756 0.2088 0.1637 0.0093  -0.0220 0.0204  111 HIS C CA  
5136 C  C   . HIS C  111 ? 0.2259 0.2199 0.1742 -0.0205 0.0006  0.0747  111 HIS C C   
5137 O  O   . HIS C  111 ? 0.2313 0.2337 0.3036 -0.0310 -0.0292 0.0897  111 HIS C O   
5138 C  CB  . HIS C  111 ? 0.2427 0.2209 0.1891 -0.0275 0.0298  0.0443  111 HIS C CB  
5139 C  CG  . HIS C  111 ? 0.1859 0.2111 0.1630 -0.0168 0.0164  -0.0102 111 HIS C CG  
5140 N  ND1 . HIS C  111 ? 0.1979 0.2245 0.1772 -0.0025 0.0203  -0.0134 111 HIS C ND1 
5141 C  CD2 . HIS C  111 ? 0.1837 0.2252 0.2384 0.0065  0.0432  0.0207  111 HIS C CD2 
5142 C  CE1 . HIS C  111 ? 0.1777 0.1922 0.2212 -0.0077 0.0300  0.0000  111 HIS C CE1 
5143 N  NE2 . HIS C  111 ? 0.1914 0.2569 0.3165 0.0000  0.0264  0.0714  111 HIS C NE2 
5144 N  N   . PHE C  112 ? 0.2088 0.2118 0.1606 -0.0052 0.0020  0.0567  112 PHE C N   
5145 C  CA  . PHE C  112 ? 0.1978 0.2196 0.1524 0.0095  -0.0195 0.0364  112 PHE C CA  
5146 C  C   . PHE C  112 ? 0.2270 0.2075 0.1553 0.0161  -0.0109 0.0480  112 PHE C C   
5147 O  O   . PHE C  112 ? 0.2196 0.2226 0.1398 0.0147  -0.0072 0.0320  112 PHE C O   
5148 C  CB  . PHE C  112 ? 0.2122 0.2488 0.2004 0.0136  -0.0013 0.0429  112 PHE C CB  
5149 C  CG  . PHE C  112 ? 0.2940 0.2544 0.2013 0.0677  0.0310  0.0471  112 PHE C CG  
5150 C  CD1 . PHE C  112 ? 0.2742 0.3609 0.2078 -0.0347 0.0293  -0.0012 112 PHE C CD1 
5151 C  CD2 . PHE C  112 ? 0.2533 0.2599 0.3617 0.0519  0.0715  -0.0047 112 PHE C CD2 
5152 C  CE1 . PHE C  112 ? 0.3864 0.3725 0.2536 -0.0563 0.0749  0.0234  112 PHE C CE1 
5153 C  CE2 . PHE C  112 ? 0.2679 0.2537 0.3477 0.0178  0.0347  -0.0212 112 PHE C CE2 
5154 C  CZ  . PHE C  112 ? 0.3502 0.3920 0.4012 -0.0719 -0.0063 0.0114  112 PHE C CZ  
5155 N  N   . ALA C  113 ? 0.2117 0.2491 0.1569 -0.0048 -0.0181 0.0655  113 ALA C N   
5156 C  CA  . ALA C  113 ? 0.2453 0.2724 0.1166 -0.0012 -0.0271 0.0543  113 ALA C CA  
5157 C  C   . ALA C  113 ? 0.2274 0.2242 0.1398 0.0205  -0.0322 0.0533  113 ALA C C   
5158 O  O   . ALA C  113 ? 0.2293 0.2658 0.1600 -0.0015 -0.0071 0.0368  113 ALA C O   
5159 C  CB  . ALA C  113 ? 0.2272 0.3173 0.1659 -0.0081 -0.0431 0.0701  113 ALA C CB  
5160 N  N   . ALA C  114 ? 0.2126 0.2983 0.1333 -0.0018 -0.0149 0.0547  114 ALA C N   
5161 C  CA  . ALA C  114 ? 0.2133 0.2773 0.1106 -0.0222 -0.0148 0.0483  114 ALA C CA  
5162 C  C   . ALA C  114 ? 0.2011 0.2168 0.1439 -0.0130 -0.0292 0.0417  114 ALA C C   
5163 O  O   . ALA C  114 ? 0.1740 0.2234 0.1516 0.0139  -0.0128 0.0458  114 ALA C O   
5164 C  CB  . ALA C  114 ? 0.2146 0.2983 0.1549 -0.0305 -0.0454 0.0311  114 ALA C CB  
5165 N  N   . GLU C  115 ? 0.1858 0.2101 0.1335 -0.0024 -0.0097 0.0368  115 GLU C N   
5166 C  CA  . GLU C  115 ? 0.1585 0.2909 0.1260 -0.0185 -0.0082 0.0399  115 GLU C CA  
5167 C  C   . GLU C  115 ? 0.1625 0.1995 0.1504 0.0082  -0.0436 0.0334  115 GLU C C   
5168 O  O   . GLU C  115 ? 0.1741 0.2400 0.1872 -0.0089 -0.0151 0.0186  115 GLU C O   
5169 C  CB  . GLU C  115 ? 0.1681 0.2653 0.1044 -0.0094 -0.0115 0.0305  115 GLU C CB  
5170 C  CG  . GLU C  115 ? 0.1703 0.2822 0.1071 0.0037  -0.0192 0.0337  115 GLU C CG  
5171 C  CD  . GLU C  115 ? 0.1395 0.2445 0.1263 0.0151  0.0036  0.0251  115 GLU C CD  
5172 O  OE1 . GLU C  115 ? 0.1481 0.2342 0.1240 -0.0089 -0.0281 0.0154  115 GLU C OE1 
5173 O  OE2 . GLU C  115 ? 0.1538 0.2530 0.1351 0.0196  -0.0059 0.0303  115 GLU C OE2 
5174 N  N   . LEU C  116 ? 0.1918 0.2781 0.1262 0.0172  -0.0118 0.0498  116 LEU C N   
5175 C  CA  . LEU C  116 ? 0.1814 0.2651 0.1332 0.0034  -0.0308 0.0440  116 LEU C CA  
5176 C  C   . LEU C  116 ? 0.1627 0.1789 0.1195 0.0089  -0.0281 0.0306  116 LEU C C   
5177 O  O   . LEU C  116 ? 0.1573 0.2508 0.1523 0.0083  -0.0236 0.0111  116 LEU C O   
5178 C  CB  . LEU C  116 ? 0.1927 0.2893 0.1491 0.0184  -0.0201 0.0343  116 LEU C CB  
5179 C  CG  . LEU C  116 ? 0.1859 0.2694 0.2095 0.0117  -0.0814 0.0189  116 LEU C CG  
5180 C  CD1 . LEU C  116 ? 0.2565 0.3242 0.1962 -0.0289 -0.0661 -0.0097 116 LEU C CD1 
5181 C  CD2 . LEU C  116 ? 0.2573 0.2647 0.2123 0.0204  -0.0077 0.0721  116 LEU C CD2 
5182 N  N   . HIS C  117 ? 0.1665 0.2089 0.1545 -0.0021 -0.0208 0.0270  117 HIS C N   
5183 C  CA  . HIS C  117 ? 0.1627 0.2381 0.1297 -0.0049 -0.0080 0.0115  117 HIS C CA  
5184 C  C   . HIS C  117 ? 0.1659 0.2277 0.1635 -0.0153 -0.0190 -0.0311 117 HIS C C   
5185 O  O   . HIS C  117 ? 0.1633 0.2548 0.1418 -0.0190 -0.0321 -0.0046 117 HIS C O   
5186 C  CB  . HIS C  117 ? 0.1534 0.2521 0.1365 0.0018  -0.0302 0.0306  117 HIS C CB  
5187 C  CG  . HIS C  117 ? 0.1898 0.2063 0.1100 -0.0021 -0.0618 -0.0009 117 HIS C CG  
5188 N  ND1 . HIS C  117 ? 0.1416 0.2563 0.1789 0.0200  -0.0136 0.0688  117 HIS C ND1 
5189 C  CD2 . HIS C  117 ? 0.1425 0.2366 0.1152 0.0091  0.0052  0.0083  117 HIS C CD2 
5190 C  CE1 . HIS C  117 ? 0.1688 0.2093 0.1237 0.0083  -0.0072 0.0162  117 HIS C CE1 
5191 N  NE2 . HIS C  117 ? 0.1254 0.1982 0.1391 0.0201  -0.0182 0.0036  117 HIS C NE2 
5192 N  N   . ILE C  118 ? 0.1421 0.2736 0.1322 0.0098  -0.0283 0.0189  118 ILE C N   
5193 C  CA  . ILE C  118 ? 0.1471 0.2556 0.2077 0.0183  -0.0454 0.0579  118 ILE C CA  
5194 C  C   . ILE C  118 ? 0.1333 0.1900 0.1208 0.0038  -0.0230 0.0096  118 ILE C C   
5195 O  O   . ILE C  118 ? 0.1669 0.2662 0.1401 -0.0063 -0.0239 -0.0035 118 ILE C O   
5196 C  CB  . ILE C  118 ? 0.1797 0.2408 0.1734 0.0092  -0.0525 0.0434  118 ILE C CB  
5197 C  CG1 . ILE C  118 ? 0.1720 0.2363 0.2346 0.0291  -0.0449 0.0592  118 ILE C CG1 
5198 C  CG2 . ILE C  118 ? 0.1482 0.2800 0.2330 -0.0052 -0.0554 0.0513  118 ILE C CG2 
5199 C  CD1 . ILE C  118 ? 0.3333 0.1916 0.2152 0.0054  -0.0201 0.0429  118 ILE C CD1 
5200 N  N   . VAL C  119 ? 0.1640 0.2058 0.2199 -0.0438 -0.0216 0.0079  119 VAL C N   
5201 C  CA  . VAL C  119 ? 0.1585 0.2624 0.1655 -0.0388 -0.0325 0.0081  119 VAL C CA  
5202 C  C   . VAL C  119 ? 0.1449 0.2346 0.1549 -0.0121 -0.0440 -0.0041 119 VAL C C   
5203 O  O   . VAL C  119 ? 0.1684 0.2735 0.1553 -0.0212 -0.0256 -0.0072 119 VAL C O   
5204 C  CB  . VAL C  119 ? 0.1252 0.2245 0.2176 -0.0190 -0.0405 -0.0051 119 VAL C CB  
5205 C  CG1 . VAL C  119 ? 0.1663 0.2536 0.1867 -0.0133 -0.0249 0.0000  119 VAL C CG1 
5206 C  CG2 . VAL C  119 ? 0.1599 0.2895 0.1775 -0.0089 -0.0111 -0.0115 119 VAL C CG2 
5207 N  N   . HIS C  120 ? 0.1818 0.2757 0.1430 -0.0357 -0.0117 0.0151  120 HIS C N   
5208 C  CA  . HIS C  120 ? 0.1220 0.2685 0.2042 -0.0303 -0.0032 0.0111  120 HIS C CA  
5209 C  C   . HIS C  120 ? 0.1585 0.2734 0.1722 -0.0318 0.0052  -0.0141 120 HIS C C   
5210 O  O   . HIS C  120 ? 0.1636 0.2524 0.1689 -0.0245 -0.0144 -0.0189 120 HIS C O   
5211 C  CB  . HIS C  120 ? 0.1693 0.2603 0.1812 -0.0344 -0.0339 0.0008  120 HIS C CB  
5212 C  CG  . HIS C  120 ? 0.1526 0.2340 0.2256 -0.0312 0.0142  0.0145  120 HIS C CG  
5213 N  ND1 . HIS C  120 ? 0.1881 0.2305 0.1817 -0.0342 -0.0073 0.0149  120 HIS C ND1 
5214 C  CD2 . HIS C  120 ? 0.2441 0.2904 0.1982 0.0201  -0.0197 0.0324  120 HIS C CD2 
5215 C  CE1 . HIS C  120 ? 0.1890 0.2130 0.2393 0.0184  0.0365  0.0132  120 HIS C CE1 
5216 N  NE2 . HIS C  120 ? 0.1633 0.2742 0.2299 -0.0251 -0.0715 0.0367  120 HIS C NE2 
5217 N  N   . TYR C  121 ? 0.1351 0.2875 0.2133 -0.0216 -0.0086 0.0306  121 TYR C N   
5218 C  CA  . TYR C  121 ? 0.1721 0.2818 0.2170 -0.0297 0.0193  0.0302  121 TYR C CA  
5219 C  C   . TYR C  121 ? 0.2127 0.3110 0.2036 -0.0033 0.0168  0.0357  121 TYR C C   
5220 O  O   . TYR C  121 ? 0.2005 0.2918 0.1861 -0.0092 0.0111  0.0078  121 TYR C O   
5221 C  CB  . TYR C  121 ? 0.1569 0.3267 0.2197 -0.0531 0.0049  -0.0314 121 TYR C CB  
5222 C  CG  . TYR C  121 ? 0.1649 0.2505 0.2281 -0.0528 -0.0077 0.0089  121 TYR C CG  
5223 C  CD1 . TYR C  121 ? 0.1885 0.3461 0.2358 0.0212  -0.0080 -0.0004 121 TYR C CD1 
5224 C  CD2 . TYR C  121 ? 0.1815 0.2907 0.2272 -0.0697 -0.0134 0.0131  121 TYR C CD2 
5225 C  CE1 . TYR C  121 ? 0.2164 0.3647 0.2898 -0.0425 -0.0111 -0.0312 121 TYR C CE1 
5226 C  CE2 . TYR C  121 ? 0.1870 0.3763 0.2746 -0.0709 -0.0291 -0.0187 121 TYR C CE2 
5227 C  CZ  . TYR C  121 ? 0.1974 0.3165 0.3203 -0.0157 -0.0519 0.0158  121 TYR C CZ  
5228 O  OH  . TYR C  121 ? 0.2180 0.4551 0.3975 -0.0829 -0.0752 -0.0345 121 TYR C OH  
5229 N  N   . ASN C  122 ? 0.1836 0.2928 0.1709 -0.0614 -0.0013 0.0252  122 ASN C N   
5230 C  CA  . ASN C  122 ? 0.1634 0.3019 0.1822 -0.0431 0.0286  0.0206  122 ASN C CA  
5231 C  C   . ASN C  122 ? 0.1649 0.2705 0.1856 -0.0218 0.0176  0.0131  122 ASN C C   
5232 O  O   . ASN C  122 ? 0.1526 0.3080 0.2694 -0.0230 0.0082  0.0165  122 ASN C O   
5233 C  CB  . ASN C  122 ? 0.1809 0.3637 0.1678 -0.0438 -0.0144 0.0083  122 ASN C CB  
5234 C  CG  . ASN C  122 ? 0.1827 0.3426 0.2121 -0.0131 0.0431  0.0330  122 ASN C CG  
5235 O  OD1 . ASN C  122 ? 0.2015 0.3515 0.2050 -0.0062 0.0366  0.0425  122 ASN C OD1 
5236 N  ND2 . ASN C  122 ? 0.2313 0.3522 0.2056 -0.0111 -0.0269 0.0346  122 ASN C ND2 
5237 N  N   . SER C  123 ? 0.1763 0.2969 0.2196 -0.0240 0.0223  -0.0049 123 SER C N   
5238 C  CA  . SER C  123 ? 0.1698 0.3025 0.2228 -0.0491 0.0089  -0.0030 123 SER C CA  
5239 C  C   . SER C  123 ? 0.1958 0.2378 0.2203 -0.0386 0.0348  -0.0334 123 SER C C   
5240 O  O   . SER C  123 ? 0.1918 0.3444 0.2837 -0.0594 0.0255  -0.0044 123 SER C O   
5241 C  CB  . SER C  123 ? 0.2095 0.3690 0.2283 -0.0094 -0.0035 0.0076  123 SER C CB  
5242 O  OG  . SER C  123 ? 0.1564 0.3624 0.2474 -0.0234 -0.0009 -0.0135 123 SER C OG  
5243 N  N   . ASP C  124 ? 0.1550 0.3089 0.1917 -0.0334 0.0113  0.0070  124 ASP C N   
5244 C  CA  . ASP C  124 ? 0.2021 0.2681 0.1946 -0.0223 0.0260  0.0150  124 ASP C CA  
5245 C  C   . ASP C  124 ? 0.2274 0.2811 0.2251 -0.0336 0.0461  0.0209  124 ASP C C   
5246 O  O   . ASP C  124 ? 0.2232 0.3875 0.3578 -0.0178 0.0554  0.1140  124 ASP C O   
5247 C  CB  . ASP C  124 ? 0.1887 0.2824 0.2626 -0.0420 0.0210  -0.0087 124 ASP C CB  
5248 C  CG  . ASP C  124 ? 0.2786 0.2921 0.2102 -0.0258 0.0212  -0.0084 124 ASP C CG  
5249 O  OD1 . ASP C  124 ? 0.2060 0.3856 0.2394 -0.0032 -0.0052 -0.0041 124 ASP C OD1 
5250 O  OD2 . ASP C  124 ? 0.2572 0.3431 0.2308 -0.0687 0.0270  0.0094  124 ASP C OD2 
5251 N  N   . LEU C  125 ? 0.1779 0.2499 0.2046 -0.0364 0.0004  0.0062  125 LEU C N   
5252 C  CA  . LEU C  125 ? 0.2125 0.2962 0.2600 -0.0179 0.0094  0.0093  125 LEU C CA  
5253 C  C   . LEU C  125 ? 0.2949 0.2751 0.2619 -0.0254 -0.0065 0.0133  125 LEU C C   
5254 O  O   . LEU C  125 ? 0.2983 0.3060 0.2970 -0.0714 0.0083  0.0438  125 LEU C O   
5255 C  CB  . LEU C  125 ? 0.2158 0.2951 0.2150 -0.0264 -0.0285 0.0287  125 LEU C CB  
5256 C  CG  . LEU C  125 ? 0.2152 0.3174 0.2593 -0.0182 0.0354  -0.0189 125 LEU C CG  
5257 C  CD1 . LEU C  125 ? 0.2352 0.3258 0.2570 -0.0150 -0.0071 0.0269  125 LEU C CD1 
5258 C  CD2 . LEU C  125 ? 0.3535 0.2999 0.2869 -0.0864 0.0812  -0.0508 125 LEU C CD2 
5259 N  N   . TYR C  126 ? 0.1990 0.3407 0.2489 -0.0446 0.0392  -0.0166 126 TYR C N   
5260 C  CA  . TYR C  126 ? 0.2005 0.2801 0.2917 -0.0410 0.0261  -0.0011 126 TYR C CA  
5261 C  C   . TYR C  126 ? 0.2237 0.2922 0.2646 -0.0392 0.0190  0.0341  126 TYR C C   
5262 O  O   . TYR C  126 ? 0.2479 0.2619 0.2744 -0.0326 -0.0293 -0.0037 126 TYR C O   
5263 C  CB  . TYR C  126 ? 0.2075 0.2583 0.2882 -0.0055 0.0467  0.0417  126 TYR C CB  
5264 C  CG  . TYR C  126 ? 0.1878 0.2632 0.3231 -0.0089 -0.0086 0.0461  126 TYR C CG  
5265 C  CD1 . TYR C  126 ? 0.2377 0.3323 0.3467 -0.0054 0.0102  0.0660  126 TYR C CD1 
5266 C  CD2 . TYR C  126 ? 0.2000 0.3080 0.2732 -0.0355 0.0549  0.0219  126 TYR C CD2 
5267 C  CE1 . TYR C  126 ? 0.1879 0.2922 0.3274 -0.0391 -0.0037 0.0187  126 TYR C CE1 
5268 C  CE2 . TYR C  126 ? 0.2049 0.2649 0.3191 -0.0234 0.0036  0.0544  126 TYR C CE2 
5269 C  CZ  . TYR C  126 ? 0.1874 0.2967 0.2906 -0.0257 0.0547  0.0539  126 TYR C CZ  
5270 O  OH  . TYR C  126 ? 0.2217 0.2958 0.2712 -0.0299 0.0030  0.0264  126 TYR C OH  
5271 N  N   . PRO C  127 ? 0.2348 0.3439 0.2733 -0.0537 -0.0258 -0.0197 127 PRO C N   
5272 C  CA  . PRO C  127 ? 0.2098 0.3555 0.2858 -0.0709 -0.0274 -0.0298 127 PRO C CA  
5273 C  C   . PRO C  127 ? 0.2776 0.4205 0.2946 -0.0354 -0.0253 -0.0274 127 PRO C C   
5274 O  O   . PRO C  127 ? 0.2893 0.5056 0.3568 -0.0545 -0.0815 -0.0254 127 PRO C O   
5275 C  CB  . PRO C  127 ? 0.3649 0.3795 0.3801 -0.0823 -0.1045 -0.0586 127 PRO C CB  
5276 C  CG  . PRO C  127 ? 0.3816 0.2876 0.4073 -0.0976 -0.0270 0.0016  127 PRO C CG  
5277 C  CD  . PRO C  127 ? 0.3116 0.3344 0.3523 -0.1026 0.0185  -0.0139 127 PRO C CD  
5278 N  N   . ASP C  128 ? 0.2664 0.3128 0.2962 -0.0413 -0.0154 -0.0308 128 ASP C N   
5279 C  CA  . ASP C  128 ? 0.2759 0.3984 0.2490 -0.0522 -0.0259 -0.0421 128 ASP C CA  
5280 C  C   . ASP C  128 ? 0.2587 0.3634 0.2403 0.0263  0.0300  0.0031  128 ASP C C   
5281 O  O   . ASP C  128 ? 0.2640 0.3412 0.2669 -0.0431 -0.0085 -0.0067 128 ASP C O   
5282 C  CB  . ASP C  128 ? 0.4141 0.3970 0.3066 -0.0719 -0.0282 -0.0923 128 ASP C CB  
5283 C  CG  . ASP C  128 ? 0.4122 0.5073 0.3583 -0.1738 -0.0745 -0.0133 128 ASP C CG  
5284 O  OD1 . ASP C  128 ? 0.3607 0.3946 0.4851 -0.0458 -0.0412 -0.1401 128 ASP C OD1 
5285 O  OD2 . ASP C  128 ? 0.3504 0.4348 0.6959 -0.1175 -0.0862 0.0578  128 ASP C OD2 
5286 N  N   . ALA C  129 ? 0.3033 0.3263 0.2239 -0.0255 0.0440  -0.0419 129 ALA C N   
5287 C  CA  . ALA C  129 ? 0.2793 0.2667 0.2631 0.0038  0.0472  -0.0030 129 ALA C CA  
5288 C  C   . ALA C  129 ? 0.2755 0.4139 0.2267 0.0403  0.0340  0.0030  129 ALA C C   
5289 O  O   . ALA C  129 ? 0.2809 0.3194 0.3160 -0.0031 -0.0140 0.0602  129 ALA C O   
5290 C  CB  . ALA C  129 ? 0.4357 0.3321 0.2477 -0.0168 -0.0069 0.0109  129 ALA C CB  
5291 N  N   . SER C  130 ? 0.3641 0.3088 0.3209 0.0110  0.0527  -0.0065 130 SER C N   
5292 C  CA  . SER C  130 ? 0.3457 0.4156 0.3613 0.0456  0.1025  -0.0699 130 SER C CA  
5293 C  C   . SER C  130 ? 0.3802 0.4311 0.3158 -0.0523 0.0207  -0.0862 130 SER C C   
5294 O  O   . SER C  130 ? 0.3326 0.4366 0.3882 0.0170  0.0861  0.0251  130 SER C O   
5295 C  CB  . SER C  130 ? 0.6081 0.7208 0.3494 -0.0496 0.0135  -0.2100 130 SER C CB  
5296 O  OG  . SER C  130 ? 0.6684 0.8301 0.6023 -0.2417 -0.1394 -0.2981 130 SER C OG  
5297 N  N   . THR C  131 ? 0.3219 0.3052 0.3259 -0.0156 -0.0185 -0.0660 131 THR C N   
5298 C  CA  . THR C  131 ? 0.2940 0.2921 0.3227 -0.0211 0.0402  -0.0712 131 THR C CA  
5299 C  C   . THR C  131 ? 0.2040 0.2758 0.2768 0.0196  0.0216  -0.0200 131 THR C C   
5300 O  O   . THR C  131 ? 0.2526 0.2535 0.3389 -0.0194 0.0087  0.0263  131 THR C O   
5301 C  CB  . THR C  131 ? 0.2600 0.3234 0.3605 -0.0705 -0.0462 -0.0109 131 THR C CB  
5302 O  OG1 . THR C  131 ? 0.3892 0.3455 0.4053 -0.1134 -0.0706 -0.0297 131 THR C OG1 
5303 C  CG2 . THR C  131 ? 0.3440 0.3104 0.3239 0.0164  0.0439  0.0010  131 THR C CG2 
5304 N  N   . ALA C  132 ? 0.1999 0.2730 0.2680 -0.0368 0.0201  -0.0088 132 ALA C N   
5305 C  CA  . ALA C  132 ? 0.1954 0.2799 0.3330 -0.0261 -0.0502 -0.0095 132 ALA C CA  
5306 C  C   . ALA C  132 ? 0.2106 0.2405 0.2764 -0.0673 0.0512  0.0078  132 ALA C C   
5307 O  O   . ALA C  132 ? 0.1988 0.2674 0.2664 -0.0485 0.0348  -0.0054 132 ALA C O   
5308 C  CB  . ALA C  132 ? 0.1536 0.2462 0.3018 -0.0300 0.0253  -0.0286 132 ALA C CB  
5309 N  N   . SER C  133 ? 0.2390 0.2918 0.2751 -0.0532 0.0677  -0.0144 133 SER C N   
5310 C  CA  . SER C  133 ? 0.1901 0.3809 0.2676 -0.0523 0.0333  -0.0049 133 SER C CA  
5311 C  C   . SER C  133 ? 0.2303 0.1876 0.2277 -0.0441 0.0392  -0.0194 133 SER C C   
5312 O  O   . SER C  133 ? 0.2114 0.2266 0.2788 -0.0594 0.0245  -0.0154 133 SER C O   
5313 C  CB  . SER C  133 ? 0.2375 0.2840 0.2949 0.0325  0.0827  0.0227  133 SER C CB  
5314 O  OG  . SER C  133 ? 0.2742 0.2694 0.2649 -0.0300 0.0017  -0.0358 133 SER C OG  
5315 N  N   . ASN C  134 ? 0.1926 0.2172 0.2787 -0.0626 0.0179  0.0199  134 ASN C N   
5316 C  CA  . ASN C  134 ? 0.2025 0.2456 0.2698 0.0089  -0.0041 -0.0070 134 ASN C CA  
5317 C  C   . ASN C  134 ? 0.2107 0.2235 0.2679 -0.0269 0.0452  -0.0010 134 ASN C C   
5318 O  O   . ASN C  134 ? 0.2952 0.2764 0.3357 -0.0398 -0.0062 0.0209  134 ASN C O   
5319 C  CB  . ASN C  134 ? 0.2731 0.2209 0.3326 -0.0620 0.1100  0.0099  134 ASN C CB  
5320 C  CG  . ASN C  134 ? 0.2795 0.2398 0.4440 -0.0627 0.0840  0.0342  134 ASN C CG  
5321 O  OD1 . ASN C  134 ? 0.2994 0.2995 0.5209 -0.1041 0.1147  -0.0829 134 ASN C OD1 
5322 N  ND2 . ASN C  134 ? 0.3282 0.2698 0.5128 -0.0643 0.1161  0.0039  134 ASN C ND2 
5323 N  N   . LYS C  135 ? 0.1832 0.2791 0.2860 -0.0706 0.0350  0.0040  135 LYS C N   
5324 C  CA  . LYS C  135 ? 0.2322 0.2442 0.2645 -0.0606 0.0388  0.0214  135 LYS C CA  
5325 C  C   . LYS C  135 ? 0.2157 0.2852 0.2523 -0.0550 0.0487  0.0122  135 LYS C C   
5326 O  O   . LYS C  135 ? 0.2146 0.2843 0.2051 -0.0281 0.0274  0.0274  135 LYS C O   
5327 C  CB  . LYS C  135 ? 0.2241 0.2973 0.3526 -0.0833 0.0765  0.0334  135 LYS C CB  
5328 C  CG  . LYS C  135 ? 0.2619 0.3768 0.3786 -0.1110 -0.0052 -0.0702 135 LYS C CG  
5329 C  CD  . LYS C  135 ? 0.2847 0.3461 0.4267 -0.1261 0.0228  -0.0158 135 LYS C CD  
5330 C  CE  . LYS C  135 ? 0.3517 0.2710 0.3504 0.0107  0.0144  0.0457  135 LYS C CE  
5331 N  NZ  . LYS C  135 ? 0.3437 0.3594 0.3565 -0.0735 0.0627  -0.0606 135 LYS C NZ  
5332 N  N   . SER C  136 ? 0.2821 0.3209 0.2540 0.0059  0.0814  0.0148  136 SER C N   
5333 C  CA  . SER C  136 ? 0.2949 0.3240 0.2305 0.0671  0.0034  0.0218  136 SER C CA  
5334 C  C   . SER C  136 ? 0.2329 0.2512 0.2137 -0.0173 0.0106  0.0355  136 SER C C   
5335 O  O   . SER C  136 ? 0.2530 0.2916 0.2106 -0.0458 0.0219  0.0326  136 SER C O   
5336 C  CB  . SER C  136 ? 0.4215 0.4329 0.2215 0.0271  0.0196  0.0658  136 SER C CB  
5337 O  OG  . SER C  136 ? 0.4865 0.3965 0.3386 0.0719  0.0510  0.0740  136 SER C OG  
5338 N  N   . GLU C  137 ? 0.2640 0.2423 0.2287 -0.0011 0.0315  0.0170  137 GLU C N   
5339 C  CA  . GLU C  137 ? 0.2099 0.2559 0.2020 -0.0250 0.0072  0.0054  137 GLU C CA  
5340 C  C   . GLU C  137 ? 0.2051 0.2556 0.1770 -0.0321 0.0276  -0.0016 137 GLU C C   
5341 O  O   . GLU C  137 ? 0.1832 0.2825 0.2174 -0.0119 -0.0048 -0.0242 137 GLU C O   
5342 C  CB  . GLU C  137 ? 0.2096 0.3475 0.1845 0.0267  0.0146  0.0172  137 GLU C CB  
5343 C  CG  . GLU C  137 ? 0.3573 0.3814 0.1900 -0.0195 -0.0025 -0.0233 137 GLU C CG  
5344 C  CD  . GLU C  137 ? 0.3840 0.4574 0.2126 -0.0702 0.0079  -0.0337 137 GLU C CD  
5345 O  OE1 . GLU C  137 ? 0.3933 0.7753 0.5197 -0.0324 -0.0715 -0.1270 137 GLU C OE1 
5346 O  OE2 . GLU C  137 ? 0.5000 0.5158 0.3104 -0.0284 -0.0228 -0.1279 137 GLU C OE2 
5347 N  N   . GLY C  138 ? 0.1719 0.2216 0.1964 -0.0270 0.0031  0.0219  138 GLY C N   
5348 C  CA  . GLY C  138 ? 0.1811 0.2544 0.2046 -0.0388 -0.0046 0.0078  138 GLY C CA  
5349 C  C   . GLY C  138 ? 0.1461 0.2676 0.2056 -0.0406 -0.0178 0.0162  138 GLY C C   
5350 O  O   . GLY C  138 ? 0.1477 0.2822 0.2057 -0.0196 0.0009  0.0115  138 GLY C O   
5351 N  N   . LEU C  139 ? 0.1682 0.2411 0.1572 -0.0411 0.0113  0.0097  139 LEU C N   
5352 C  CA  . LEU C  139 ? 0.1507 0.1993 0.1899 -0.0359 -0.0199 0.0136  139 LEU C CA  
5353 C  C   . LEU C  139 ? 0.1509 0.2192 0.1797 -0.0286 0.0233  -0.0215 139 LEU C C   
5354 O  O   . LEU C  139 ? 0.1502 0.2592 0.1506 -0.0311 -0.0093 -0.0144 139 LEU C O   
5355 C  CB  . LEU C  139 ? 0.1451 0.2658 0.2128 -0.0581 0.0223  -0.0234 139 LEU C CB  
5356 C  CG  . LEU C  139 ? 0.1666 0.2681 0.1859 -0.0348 0.0031  -0.0223 139 LEU C CG  
5357 C  CD1 . LEU C  139 ? 0.1911 0.2588 0.2638 -0.0135 0.0464  -0.0249 139 LEU C CD1 
5358 C  CD2 . LEU C  139 ? 0.1372 0.2926 0.2779 -0.0374 -0.0190 -0.0673 139 LEU C CD2 
5359 N  N   . ALA C  140 ? 0.1585 0.2399 0.2015 -0.0173 0.0245  0.0184  140 ALA C N   
5360 C  CA  . ALA C  140 ? 0.1671 0.2261 0.1401 0.0044  0.0024  0.0184  140 ALA C CA  
5361 C  C   . ALA C  140 ? 0.1451 0.2572 0.1477 -0.0153 -0.0241 0.0022  140 ALA C C   
5362 O  O   . ALA C  140 ? 0.1575 0.3073 0.1485 -0.0265 -0.0212 -0.0030 140 ALA C O   
5363 C  CB  . ALA C  140 ? 0.1412 0.2652 0.1743 0.0055  -0.0193 -0.0055 140 ALA C CB  
5364 N  N   . VAL C  141 ? 0.1542 0.2442 0.1310 -0.0170 -0.0086 0.0066  141 VAL C N   
5365 C  CA  . VAL C  141 ? 0.1626 0.2227 0.1390 -0.0094 -0.0013 0.0319  141 VAL C CA  
5366 C  C   . VAL C  141 ? 0.1318 0.2273 0.1158 0.0013  -0.0057 0.0215  141 VAL C C   
5367 O  O   . VAL C  141 ? 0.1685 0.2500 0.1435 -0.0052 -0.0254 0.0013  141 VAL C O   
5368 C  CB  . VAL C  141 ? 0.1414 0.2169 0.1336 0.0066  -0.0229 0.0268  141 VAL C CB  
5369 C  CG1 . VAL C  141 ? 0.1736 0.3115 0.1150 0.0078  -0.0091 0.0324  141 VAL C CG1 
5370 C  CG2 . VAL C  141 ? 0.1795 0.2385 0.1520 -0.0251 -0.0281 0.0052  141 VAL C CG2 
5371 N  N   . LEU C  142 ? 0.1504 0.2130 0.1647 0.0050  -0.0082 0.0419  142 LEU C N   
5372 C  CA  . LEU C  142 ? 0.1308 0.2057 0.1345 0.0126  -0.0337 0.0128  142 LEU C CA  
5373 C  C   . LEU C  142 ? 0.1479 0.2392 0.1638 0.0055  -0.0070 -0.0269 142 LEU C C   
5374 O  O   . LEU C  142 ? 0.1764 0.2459 0.1532 -0.0095 -0.0155 0.0069  142 LEU C O   
5375 C  CB  . LEU C  142 ? 0.1548 0.2459 0.1821 0.0385  -0.0239 0.0082  142 LEU C CB  
5376 C  CG  . LEU C  142 ? 0.1406 0.2825 0.1623 0.0189  -0.0175 0.0181  142 LEU C CG  
5377 C  CD1 . LEU C  142 ? 0.1808 0.3096 0.2180 0.0250  -0.0359 0.0397  142 LEU C CD1 
5378 C  CD2 . LEU C  142 ? 0.2043 0.2913 0.1749 0.0271  0.0013  -0.0036 142 LEU C CD2 
5379 N  N   . ALA C  143 ? 0.1637 0.2421 0.1296 -0.0004 -0.0050 0.0240  143 ALA C N   
5380 C  CA  . ALA C  143 ? 0.1397 0.2115 0.1541 0.0087  -0.0118 0.0403  143 ALA C CA  
5381 C  C   . ALA C  143 ? 0.1411 0.2165 0.1439 0.0111  0.0009  0.0290  143 ALA C C   
5382 O  O   . ALA C  143 ? 0.1875 0.2084 0.1723 0.0253  0.0025  0.0468  143 ALA C O   
5383 C  CB  . ALA C  143 ? 0.1354 0.2011 0.1605 0.0153  -0.0211 0.0018  143 ALA C CB  
5384 N  N   . VAL C  144 ? 0.1646 0.2061 0.1485 0.0228  -0.0098 0.0287  144 VAL C N   
5385 C  CA  . VAL C  144 ? 0.1277 0.2195 0.2035 0.0257  -0.0177 0.0535  144 VAL C CA  
5386 C  C   . VAL C  144 ? 0.1887 0.1958 0.1817 0.0530  -0.0596 0.0366  144 VAL C C   
5387 O  O   . VAL C  144 ? 0.2064 0.2308 0.1714 0.0151  0.0013  0.0283  144 VAL C O   
5388 C  CB  . VAL C  144 ? 0.1753 0.2471 0.1776 0.0204  -0.0336 0.0697  144 VAL C CB  
5389 C  CG1 . VAL C  144 ? 0.2327 0.2685 0.2126 0.0217  -0.0152 0.0763  144 VAL C CG1 
5390 C  CG2 . VAL C  144 ? 0.1694 0.3174 0.2041 0.0513  -0.0115 0.0595  144 VAL C CG2 
5391 N  N   . LEU C  145 ? 0.1974 0.1996 0.1689 0.0240  -0.0100 0.0717  145 LEU C N   
5392 C  CA  . LEU C  145 ? 0.1888 0.2491 0.1490 -0.0035 -0.0013 0.0625  145 LEU C CA  
5393 C  C   . LEU C  145 ? 0.1990 0.2645 0.1831 0.0321  -0.0290 0.0669  145 LEU C C   
5394 O  O   . LEU C  145 ? 0.2457 0.2856 0.1960 0.0589  0.0076  0.0809  145 LEU C O   
5395 C  CB  . LEU C  145 ? 0.2308 0.2198 0.1751 -0.0067 -0.0159 0.0659  145 LEU C CB  
5396 C  CG  . LEU C  145 ? 0.2446 0.2166 0.1997 0.0159  -0.0316 0.0601  145 LEU C CG  
5397 C  CD1 . LEU C  145 ? 0.2130 0.2249 0.2457 0.0287  0.0001  0.0188  145 LEU C CD1 
5398 C  CD2 . LEU C  145 ? 0.2433 0.2386 0.2182 0.0384  -0.0603 0.0688  145 LEU C CD2 
5399 N  N   . ILE C  146 ? 0.2167 0.2346 0.1684 0.0182  0.0060  0.0785  146 ILE C N   
5400 C  CA  . ILE C  146 ? 0.2028 0.2178 0.1967 0.0095  -0.0102 0.0660  146 ILE C CA  
5401 C  C   . ILE C  146 ? 0.2586 0.2560 0.1782 0.0285  -0.0110 0.1017  146 ILE C C   
5402 O  O   . ILE C  146 ? 0.2285 0.2673 0.1983 0.0201  -0.0078 0.0938  146 ILE C O   
5403 C  CB  . ILE C  146 ? 0.2262 0.2725 0.1500 -0.0085 -0.0138 0.0616  146 ILE C CB  
5404 C  CG1 . ILE C  146 ? 0.2279 0.2689 0.1904 0.0287  0.0054  0.0687  146 ILE C CG1 
5405 C  CG2 . ILE C  146 ? 0.2446 0.2793 0.1417 0.0423  -0.0394 0.0464  146 ILE C CG2 
5406 C  CD1 . ILE C  146 ? 0.2595 0.3022 0.2011 0.0030  -0.0502 0.0648  146 ILE C CD1 
5407 N  N   . GLU C  147 ? 0.2755 0.2564 0.2383 0.0179  0.0370  0.1099  147 GLU C N   
5408 C  CA  . GLU C  147 ? 0.2824 0.2834 0.2468 -0.0245 -0.0265 0.1402  147 GLU C CA  
5409 C  C   . GLU C  147 ? 0.2660 0.3031 0.2444 0.0442  0.0097  0.0996  147 GLU C C   
5410 O  O   . GLU C  147 ? 0.2773 0.3121 0.2461 0.0312  0.0091  0.1261  147 GLU C O   
5411 C  CB  . GLU C  147 ? 0.2881 0.2694 0.2898 0.0113  -0.0122 0.0908  147 GLU C CB  
5412 C  CG  . GLU C  147 ? 0.3558 0.2425 0.2889 -0.0174 0.0105  0.0963  147 GLU C CG  
5413 C  CD  . GLU C  147 ? 0.3739 0.2192 0.3884 -0.0539 -0.0131 0.1081  147 GLU C CD  
5414 O  OE1 . GLU C  147 ? 0.3477 0.4479 0.3649 0.0264  -0.0011 0.0939  147 GLU C OE1 
5415 O  OE2 . GLU C  147 ? 0.4759 0.2667 0.5118 0.0424  0.0340  0.0487  147 GLU C OE2 
5416 N  N   . MET C  148 ? 0.2722 0.3858 0.2838 0.0020  0.0284  0.1808  148 MET C N   
5417 C  CA  . MET C  148 ? 0.3701 0.3682 0.2524 0.0480  0.0227  0.1580  148 MET C CA  
5418 C  C   . MET C  148 ? 0.3820 0.3519 0.3416 -0.0714 0.0309  0.1350  148 MET C C   
5419 O  O   . MET C  148 ? 0.3679 0.3168 0.3353 0.0015  -0.0462 0.1575  148 MET C O   
5420 C  CB  . MET C  148 ? 0.4613 0.5159 0.1725 0.1082  0.0384  0.1386  148 MET C CB  
5421 C  CG  . MET C  148 ? 0.5666 0.5338 0.3777 -0.0233 0.1074  -0.1165 148 MET C CG  
5422 S  SD  . MET C  148 ? 0.5470 0.9458 0.6830 0.1284  0.2543  0.1448  148 MET C SD  
5423 C  CE  . MET C  148 ? 1.3025 1.0756 0.4320 0.3991  0.2496  0.2558  148 MET C CE  
5424 N  N   . GLY C  149 ? 0.4497 0.4387 0.3759 0.1747  0.0405  0.2604  149 GLY C N   
5425 C  CA  . GLY C  149 ? 0.4047 0.3412 0.3219 0.0216  -0.0146 0.1029  149 GLY C CA  
5426 C  C   . GLY C  149 ? 0.3823 0.3802 0.4248 0.1013  -0.1088 0.0034  149 GLY C C   
5427 O  O   . GLY C  149 ? 0.4123 0.2463 0.3977 -0.0076 -0.0136 0.1430  149 GLY C O   
5428 N  N   . SER C  150 ? 0.5289 0.4156 0.3319 0.1565  -0.0342 0.1439  150 SER C N   
5429 C  CA  . SER C  150 ? 0.4286 0.3012 0.3290 -0.0125 -0.0447 0.0257  150 SER C CA  
5430 C  C   . SER C  150 ? 0.3741 0.3879 0.4290 -0.0465 -0.1402 0.1314  150 SER C C   
5431 O  O   . SER C  150 ? 0.4165 0.4451 0.3200 0.0727  -0.0315 0.1443  150 SER C O   
5432 C  CB  . SER C  150 ? 0.6371 0.1734 0.4938 0.0801  -0.1002 -0.0086 150 SER C CB  
5433 O  OG  . SER C  150 ? 0.6391 0.3685 0.8162 -0.1562 -0.0546 0.0932  150 SER C OG  
5434 N  N   . PHE C  151 ? 0.4196 0.4208 0.3212 0.0282  -0.0856 0.1671  151 PHE C N   
5435 C  CA  . PHE C  151 ? 0.4111 0.5321 0.2888 -0.0308 -0.0681 0.1964  151 PHE C CA  
5436 C  C   . PHE C  151 ? 0.4729 0.3147 0.4017 -0.1010 0.0451  0.1232  151 PHE C C   
5437 O  O   . PHE C  151 ? 0.4827 0.5056 0.2946 0.0602  -0.0510 0.0842  151 PHE C O   
5438 C  CB  . PHE C  151 ? 0.4072 0.5305 0.2894 -0.0113 -0.0897 0.2064  151 PHE C CB  
5439 C  CG  . PHE C  151 ? 0.4321 0.3668 0.2805 0.0747  -0.0427 0.1359  151 PHE C CG  
5440 C  CD1 . PHE C  151 ? 0.5496 0.3590 0.2062 -0.0069 -0.0904 0.0450  151 PHE C CD1 
5441 C  CD2 . PHE C  151 ? 0.4376 0.5287 0.3531 0.0307  -0.0976 0.2347  151 PHE C CD2 
5442 C  CE1 . PHE C  151 ? 0.4304 0.3912 0.2640 0.0392  -0.1066 0.1130  151 PHE C CE1 
5443 C  CE2 . PHE C  151 ? 0.4398 0.4032 0.2823 0.1346  -0.0227 0.1146  151 PHE C CE2 
5444 C  CZ  . PHE C  151 ? 0.4266 0.4213 0.2593 0.1087  -0.0688 0.1009  151 PHE C CZ  
5445 N  N   . ASN C  152 ? 0.3089 0.2997 0.3346 0.0265  -0.0505 0.1176  152 ASN C N   
5446 C  CA  . ASN C  152 ? 0.3380 0.2777 0.2617 0.0483  -0.0325 0.0726  152 ASN C CA  
5447 C  C   . ASN C  152 ? 0.3671 0.2611 0.2319 0.0945  -0.0958 0.0805  152 ASN C C   
5448 O  O   . ASN C  152 ? 0.3698 0.3004 0.2888 0.0675  -0.0763 0.0740  152 ASN C O   
5449 C  CB  . ASN C  152 ? 0.2878 0.2723 0.2870 0.0427  -0.0389 0.0881  152 ASN C CB  
5450 C  CG  . ASN C  152 ? 0.3209 0.4183 0.2495 -0.0453 -0.0760 0.1360  152 ASN C CG  
5451 O  OD1 . ASN C  152 ? 0.3464 0.3177 0.3309 0.0074  -0.0629 0.1046  152 ASN C OD1 
5452 N  ND2 . ASN C  152 ? 0.3104 0.3536 0.2746 0.0248  -0.0541 0.0983  152 ASN C ND2 
5453 N  N   . PRO C  153 ? 0.3348 0.3001 0.2733 0.0696  -0.0610 0.0173  153 PRO C N   
5454 C  CA  . PRO C  153 ? 0.3470 0.2325 0.3987 0.0473  -0.1077 0.0767  153 PRO C CA  
5455 C  C   . PRO C  153 ? 0.3170 0.2412 0.2395 -0.0006 -0.1110 0.0214  153 PRO C C   
5456 O  O   . PRO C  153 ? 0.3964 0.3510 0.2248 -0.0337 -0.0981 0.0067  153 PRO C O   
5457 C  CB  . PRO C  153 ? 0.3307 0.3316 0.3083 0.0531  -0.1116 0.0701  153 PRO C CB  
5458 C  CG  . PRO C  153 ? 0.4064 0.3782 0.3878 0.0040  -0.1439 0.0302  153 PRO C CG  
5459 C  CD  . PRO C  153 ? 0.3443 0.2688 0.3069 0.1541  0.0010  0.0796  153 PRO C CD  
5460 N  N   . SER C  154 ? 0.3207 0.3166 0.2645 0.0773  -0.1013 0.0873  154 SER C N   
5461 C  CA  . SER C  154 ? 0.4138 0.3447 0.1904 0.0605  -0.0540 0.0727  154 SER C CA  
5462 C  C   . SER C  154 ? 0.2864 0.2605 0.1869 -0.0008 -0.0854 0.0189  154 SER C C   
5463 O  O   . SER C  154 ? 0.3173 0.3177 0.2449 0.0013  -0.0817 0.0614  154 SER C O   
5464 C  CB  . SER C  154 ? 0.3471 0.4484 0.3204 0.1628  -0.0429 -0.0453 154 SER C CB  
5465 O  OG  . SER C  154 ? 0.5302 0.3003 0.4041 0.0659  -0.0436 0.0581  154 SER C OG  
5466 N  N   . TYR C  155 ? 0.3015 0.2487 0.2433 0.0398  -0.0456 0.0050  155 TYR C N   
5467 C  CA  . TYR C  155 ? 0.2755 0.3267 0.3026 0.0164  -0.0372 -0.0208 155 TYR C CA  
5468 C  C   . TYR C  155 ? 0.2655 0.2516 0.1750 0.0688  -0.0673 0.0231  155 TYR C C   
5469 O  O   . TYR C  155 ? 0.3073 0.2417 0.2345 0.0407  -0.0585 -0.0020 155 TYR C O   
5470 C  CB  . TYR C  155 ? 0.2896 0.3497 0.2056 -0.0089 -0.0858 0.0754  155 TYR C CB  
5471 C  CG  . TYR C  155 ? 0.2919 0.2049 0.2254 0.0230  0.0131  0.0444  155 TYR C CG  
5472 C  CD1 . TYR C  155 ? 0.3028 0.2254 0.2153 0.0651  -0.0779 0.0147  155 TYR C CD1 
5473 C  CD2 . TYR C  155 ? 0.2500 0.2748 0.1864 0.0388  -0.0275 0.0337  155 TYR C CD2 
5474 C  CE1 . TYR C  155 ? 0.2262 0.2505 0.2640 0.0086  -0.0149 0.0794  155 TYR C CE1 
5475 C  CE2 . TYR C  155 ? 0.2566 0.3134 0.2261 -0.0059 -0.0210 0.0408  155 TYR C CE2 
5476 C  CZ  . TYR C  155 ? 0.2467 0.2759 0.1908 0.0373  -0.0826 0.0394  155 TYR C CZ  
5477 O  OH  . TYR C  155 ? 0.2310 0.3034 0.2114 0.0231  -0.0534 0.0692  155 TYR C OH  
5478 N  N   . ASP C  156 ? 0.3096 0.3195 0.2430 0.0506  -0.0936 0.0359  156 ASP C N   
5479 C  CA  . ASP C  156 ? 0.4242 0.3364 0.2018 -0.0269 -0.1126 0.0599  156 ASP C CA  
5480 C  C   . ASP C  156 ? 0.2981 0.3064 0.2906 0.0285  -0.0774 0.0008  156 ASP C C   
5481 O  O   . ASP C  156 ? 0.3811 0.2577 0.2816 0.0255  -0.0701 0.0261  156 ASP C O   
5482 C  CB  . ASP C  156 ? 0.4887 0.3633 0.2436 0.1223  -0.0534 0.0754  156 ASP C CB  
5483 C  CG  . ASP C  156 ? 0.5285 0.6105 0.2716 0.1601  -0.0311 0.1675  156 ASP C CG  
5484 O  OD1 . ASP C  156 ? 0.4589 0.4219 0.2568 0.0092  -0.0706 0.0715  156 ASP C OD1 
5485 O  OD2 . ASP C  156 ? 0.5723 0.7228 0.2719 0.1841  -0.1228 0.1000  156 ASP C OD2 
5486 N  N   . LYS C  157 ? 0.3379 0.2132 0.2453 0.0197  -0.0697 0.0049  157 LYS C N   
5487 C  CA  . LYS C  157 ? 0.2768 0.2927 0.3159 0.0458  -0.0694 0.0678  157 LYS C CA  
5488 C  C   . LYS C  157 ? 0.4259 0.2193 0.3200 -0.0500 -0.1127 0.0489  157 LYS C C   
5489 O  O   . LYS C  157 ? 0.4469 0.2942 0.4892 -0.0629 -0.2028 0.0655  157 LYS C O   
5490 C  CB  . LYS C  157 ? 0.3774 0.4417 0.3037 0.0924  -0.1121 0.0464  157 LYS C CB  
5491 C  CG  . LYS C  157 ? 0.2781 0.3683 0.6240 0.1221  0.0306  -0.0148 157 LYS C CG  
5492 C  CD  . LYS C  157 ? 0.4869 0.3169 0.3371 0.0728  -0.0895 -0.0594 157 LYS C CD  
5493 C  CE  . LYS C  157 ? 0.4581 0.4099 0.6933 0.1804  -0.0093 0.0758  157 LYS C CE  
5494 N  NZ  . LYS C  157 ? 0.7033 0.6459 0.5085 0.3521  -0.2777 -0.0682 157 LYS C NZ  
5495 N  N   . ILE C  158 ? 0.4342 0.2907 0.2267 0.0890  -0.0833 0.0589  158 ILE C N   
5496 C  CA  . ILE C  158 ? 0.2744 0.3273 0.2532 0.0593  -0.0483 0.0379  158 ILE C CA  
5497 C  C   . ILE C  158 ? 0.3412 0.2223 0.2419 0.0348  -0.0212 -0.0418 158 ILE C C   
5498 O  O   . ILE C  158 ? 0.3714 0.2705 0.2259 0.0272  -0.0758 0.0089  158 ILE C O   
5499 C  CB  . ILE C  158 ? 0.3538 0.2538 0.2147 0.0734  -0.0436 0.0339  158 ILE C CB  
5500 C  CG1 . ILE C  158 ? 0.3165 0.3854 0.3186 0.0566  0.0145  0.0210  158 ILE C CG1 
5501 C  CG2 . ILE C  158 ? 0.4697 0.2117 0.2664 0.0879  -0.0969 0.0109  158 ILE C CG2 
5502 C  CD1 . ILE C  158 ? 0.5344 0.3661 0.2680 0.0820  -0.0108 0.0761  158 ILE C CD1 
5503 N  N   . PHE C  159 ? 0.3412 0.3651 0.2146 -0.0029 -0.0491 0.1189  159 PHE C N   
5504 C  CA  . PHE C  159 ? 0.3005 0.2174 0.2423 0.0153  -0.0670 0.0352  159 PHE C CA  
5505 C  C   . PHE C  159 ? 0.3190 0.3700 0.2324 0.0864  -0.1307 -0.0335 159 PHE C C   
5506 O  O   . PHE C  159 ? 0.3485 0.3222 0.2192 0.0352  -0.0751 0.0542  159 PHE C O   
5507 C  CB  . PHE C  159 ? 0.4160 0.3240 0.1858 -0.0718 -0.1236 0.0819  159 PHE C CB  
5508 C  CG  . PHE C  159 ? 0.2919 0.2814 0.2032 0.0358  -0.0583 0.0278  159 PHE C CG  
5509 C  CD1 . PHE C  159 ? 0.3736 0.2805 0.2240 0.0354  -0.1116 0.0215  159 PHE C CD1 
5510 C  CD2 . PHE C  159 ? 0.3441 0.3246 0.2331 -0.0188 -0.1258 0.0351  159 PHE C CD2 
5511 C  CE1 . PHE C  159 ? 0.3269 0.3328 0.2248 0.0486  -0.0873 0.0057  159 PHE C CE1 
5512 C  CE2 . PHE C  159 ? 0.3855 0.4861 0.1730 0.0386  -0.0333 0.0438  159 PHE C CE2 
5513 C  CZ  . PHE C  159 ? 0.3325 0.3386 0.1993 0.0403  -0.0954 0.0108  159 PHE C CZ  
5514 N  N   . SER C  160 ? 0.3466 0.3076 0.1972 0.0314  -0.0901 0.0589  160 SER C N   
5515 C  CA  . SER C  160 ? 0.3468 0.3523 0.2249 0.0275  -0.1620 -0.0276 160 SER C CA  
5516 C  C   . SER C  160 ? 0.3662 0.4009 0.2143 0.0124  -0.0959 0.0110  160 SER C C   
5517 O  O   . SER C  160 ? 0.5176 0.4870 0.2683 0.0436  -0.2213 -0.0201 160 SER C O   
5518 C  CB  . SER C  160 ? 0.4362 0.4845 0.2672 0.0905  -0.0947 0.1278  160 SER C CB  
5519 O  OG  . SER C  160 ? 0.3748 0.4235 0.3497 0.1346  -0.0902 0.0361  160 SER C OG  
5520 N  N   . HIS C  161 ? 0.3908 0.2728 0.1926 -0.0093 -0.1482 -0.0203 161 HIS C N   
5521 C  CA  . HIS C  161 ? 0.3699 0.3184 0.2458 -0.0171 -0.0585 0.0009  161 HIS C CA  
5522 C  C   . HIS C  161 ? 0.3521 0.3102 0.1725 -0.0109 -0.0990 -0.0179 161 HIS C C   
5523 O  O   . HIS C  161 ? 0.3472 0.2854 0.2242 0.0323  -0.0757 -0.0412 161 HIS C O   
5524 C  CB  . HIS C  161 ? 0.3199 0.3357 0.2702 0.0188  -0.0710 0.0161  161 HIS C CB  
5525 C  CG  . HIS C  161 ? 0.3094 0.3606 0.4192 -0.0039 -0.1274 0.0388  161 HIS C CG  
5526 N  ND1 . HIS C  161 ? 0.3527 0.3806 0.4263 -0.0026 -0.1439 -0.0287 161 HIS C ND1 
5527 C  CD2 . HIS C  161 ? 0.3622 0.4066 0.4252 0.0074  -0.0721 -0.0457 161 HIS C CD2 
5528 C  CE1 . HIS C  161 ? 0.3110 0.3878 0.6262 0.0263  -0.1439 0.0080  161 HIS C CE1 
5529 N  NE2 . HIS C  161 ? 0.4791 0.6100 0.3319 0.1117  -0.1329 -0.0184 161 HIS C NE2 
5530 N  N   . LEU C  162 ? 0.3468 0.3322 0.1906 0.0588  -0.0752 -0.0197 162 LEU C N   
5531 C  CA  . LEU C  162 ? 0.3125 0.2730 0.2632 0.0677  -0.0926 -0.0427 162 LEU C CA  
5532 C  C   . LEU C  162 ? 0.2913 0.2590 0.1661 0.0194  -0.0736 -0.0094 162 LEU C C   
5533 O  O   . LEU C  162 ? 0.2847 0.2723 0.2029 -0.0002 -0.0839 -0.0139 162 LEU C O   
5534 C  CB  . LEU C  162 ? 0.3495 0.4180 0.2171 0.0113  -0.1026 -0.0871 162 LEU C CB  
5535 C  CG  . LEU C  162 ? 0.3565 0.2788 0.2337 0.0421  -0.1324 -0.0451 162 LEU C CG  
5536 C  CD1 . LEU C  162 ? 0.4288 0.2896 0.4676 0.0475  -0.2837 -0.1038 162 LEU C CD1 
5537 C  CD2 . LEU C  162 ? 0.4858 0.4525 0.1870 0.0278  -0.0394 0.0305  162 LEU C CD2 
5538 N  N   . GLN C  163 ? 0.2989 0.3391 0.1858 -0.0304 -0.0967 -0.0068 163 GLN C N   
5539 C  CA  . GLN C  163 ? 0.3657 0.3091 0.1842 -0.0392 -0.0575 -0.0008 163 GLN C CA  
5540 C  C   . GLN C  163 ? 0.3393 0.2559 0.2599 -0.0134 -0.0354 -0.0344 163 GLN C C   
5541 O  O   . GLN C  163 ? 0.3707 0.3021 0.3045 -0.0223 -0.0513 -0.0508 163 GLN C O   
5542 C  CB  . GLN C  163 ? 0.3134 0.4317 0.1723 -0.0670 0.0147  -0.0021 163 GLN C CB  
5543 C  CG  . GLN C  163 ? 0.3625 0.4398 0.2408 -0.0637 0.0128  0.0671  163 GLN C CG  
5544 C  CD  . GLN C  163 ? 0.3971 0.4182 0.2381 -0.0403 -0.0621 -0.0537 163 GLN C CD  
5545 O  OE1 . GLN C  163 ? 0.4189 0.4232 0.2193 -0.0826 -0.0507 0.0102  163 GLN C OE1 
5546 N  NE2 . GLN C  163 ? 0.5459 0.5850 0.3731 -0.1424 -0.2549 0.0064  163 GLN C NE2 
5547 N  N   . HIS C  164 ? 0.3080 0.2736 0.2005 -0.0130 -0.1232 0.0170  164 HIS C N   
5548 C  CA  . HIS C  164 ? 0.2547 0.2663 0.2754 0.0100  -0.0919 0.0414  164 HIS C CA  
5549 C  C   . HIS C  164 ? 0.3353 0.2805 0.2133 -0.0420 -0.1005 0.0304  164 HIS C C   
5550 O  O   . HIS C  164 ? 0.3873 0.2746 0.3454 -0.0296 -0.1341 0.0047  164 HIS C O   
5551 C  CB  . HIS C  164 ? 0.3052 0.3280 0.2854 -0.0114 -0.0991 0.0602  164 HIS C CB  
5552 C  CG  . HIS C  164 ? 0.2603 0.2813 0.2184 -0.0303 -0.0507 0.0639  164 HIS C CG  
5553 N  ND1 . HIS C  164 ? 0.3089 0.3765 0.2107 0.0491  -0.0375 0.0584  164 HIS C ND1 
5554 C  CD2 . HIS C  164 ? 0.2515 0.3276 0.3163 -0.0298 -0.1174 -0.0043 164 HIS C CD2 
5555 C  CE1 . HIS C  164 ? 0.2298 0.4251 0.2995 0.0754  0.0301  0.1401  164 HIS C CE1 
5556 N  NE2 . HIS C  164 ? 0.3304 0.4452 0.3953 0.0648  -0.2075 0.0627  164 HIS C NE2 
5557 N  N   . VAL C  165 ? 0.3101 0.3222 0.2755 -0.0132 -0.1470 0.0219  165 VAL C N   
5558 C  CA  . VAL C  165 ? 0.3215 0.3106 0.2651 0.0686  -0.0728 0.0019  165 VAL C CA  
5559 C  C   . VAL C  165 ? 0.3121 0.1917 0.2466 0.0153  -0.0122 0.0239  165 VAL C C   
5560 O  O   . VAL C  165 ? 0.3204 0.2604 0.2031 0.0229  -0.0657 0.0009  165 VAL C O   
5561 C  CB  . VAL C  165 ? 0.3001 0.2771 0.2465 -0.0508 -0.0535 0.0050  165 VAL C CB  
5562 C  CG1 . VAL C  165 ? 0.3183 0.2992 0.3156 -0.0251 -0.0670 0.0657  165 VAL C CG1 
5563 C  CG2 . VAL C  165 ? 0.4574 0.2714 0.1553 -0.0335 -0.0083 0.0339  165 VAL C CG2 
5564 N  N   . LYS C  166 ? 0.3242 0.3052 0.2198 -0.0442 -0.0154 -0.0173 166 LYS C N   
5565 C  CA  . LYS C  166 ? 0.2992 0.3780 0.1994 0.0243  -0.0114 0.0316  166 LYS C CA  
5566 C  C   . LYS C  166 ? 0.3753 0.3431 0.1660 -0.0273 -0.0794 -0.0201 166 LYS C C   
5567 O  O   . LYS C  166 ? 0.3040 0.3658 0.2364 -0.0277 -0.0806 -0.0072 166 LYS C O   
5568 C  CB  . LYS C  166 ? 0.5400 0.2859 0.1645 0.0682  -0.0023 -0.0025 166 LYS C CB  
5569 C  CG  . LYS C  166 ? 0.5766 0.3956 0.2592 -0.0031 -0.0441 0.1376  166 LYS C CG  
5570 C  CD  . LYS C  166 ? 0.4051 0.6372 0.3060 -0.1750 0.0190  0.0862  166 LYS C CD  
5571 C  CE  . LYS C  166 ? 0.4344 0.5719 0.1815 -0.1395 -0.0103 -0.0370 166 LYS C CE  
5572 N  NZ  . LYS C  166 ? 0.4903 0.4950 0.1580 -0.0506 -0.0204 0.0025  166 LYS C NZ  
5573 N  N   . TYR C  167 ? 0.2896 0.3237 0.2021 -0.0030 -0.0157 0.0204  167 TYR C N   
5574 C  CA  . TYR C  167 ? 0.3077 0.3173 0.1932 -0.0067 0.0201  0.0059  167 TYR C CA  
5575 C  C   . TYR C  167 ? 0.3180 0.2403 0.2385 -0.0022 0.0272  0.0441  167 TYR C C   
5576 O  O   . TYR C  167 ? 0.3538 0.3310 0.1457 0.0179  -0.0183 -0.0005 167 TYR C O   
5577 C  CB  . TYR C  167 ? 0.3452 0.2915 0.2321 -0.0051 0.0776  -0.0142 167 TYR C CB  
5578 C  CG  . TYR C  167 ? 0.3948 0.3854 0.1556 0.0051  0.0185  0.0273  167 TYR C CG  
5579 C  CD1 . TYR C  167 ? 0.4137 0.3786 0.2559 0.0620  0.0326  0.0983  167 TYR C CD1 
5580 C  CD2 . TYR C  167 ? 0.3191 0.3609 0.2048 0.0193  -0.0339 -0.0407 167 TYR C CD2 
5581 C  CE1 . TYR C  167 ? 0.3926 0.7032 0.3533 0.0058  0.0420  0.2307  167 TYR C CE1 
5582 C  CE2 . TYR C  167 ? 0.4596 0.5102 0.2602 0.1259  0.0768  0.0270  167 TYR C CE2 
5583 C  CZ  . TYR C  167 ? 0.4656 0.4952 0.2433 0.1026  0.0792  0.1471  167 TYR C CZ  
5584 O  OH  . TYR C  167 ? 0.3794 0.4772 0.3255 0.0598  0.0815  0.1430  167 TYR C OH  
5585 N  N   . LYS C  168 ? 0.3283 0.2393 0.2159 -0.0419 -0.0259 0.0094  168 LYS C N   
5586 C  CA  . LYS C  168 ? 0.2947 0.2931 0.1928 0.0037  0.0083  0.0215  168 LYS C CA  
5587 C  C   . LYS C  168 ? 0.3765 0.3078 0.2353 -0.0636 0.0446  -0.0209 168 LYS C C   
5588 O  O   . LYS C  168 ? 0.4275 0.2924 0.2332 -0.0359 0.0031  -0.0302 168 LYS C O   
5589 C  CB  . LYS C  168 ? 0.3644 0.2599 0.2696 0.0115  -0.0166 0.0409  168 LYS C CB  
5590 C  CG  . LYS C  168 ? 0.3328 0.3287 0.2414 0.0131  -0.0200 0.0444  168 LYS C CG  
5591 C  CD  . LYS C  168 ? 0.3449 0.2601 0.3992 0.0033  -0.0723 0.0150  168 LYS C CD  
5592 C  CE  . LYS C  168 ? 0.3611 0.4332 0.3799 0.0646  -0.0443 0.0082  168 LYS C CE  
5593 N  NZ  . LYS C  168 ? 0.5978 0.9341 0.3163 0.1114  -0.1191 -0.0428 168 LYS C NZ  
5594 N  N   . GLY C  169 ? 0.2978 0.2685 0.2478 -0.0110 0.0043  -0.0050 169 GLY C N   
5595 C  CA  . GLY C  169 ? 0.2913 0.3450 0.3317 -0.0078 0.0245  0.0238  169 GLY C CA  
5596 C  C   . GLY C  169 ? 0.3592 0.3552 0.2382 0.0030  0.0164  0.0644  169 GLY C C   
5597 O  O   . GLY C  169 ? 0.4789 0.4102 0.3159 -0.1500 -0.0126 0.0189  169 GLY C O   
5598 N  N   . GLN C  170 ? 0.3569 0.2389 0.2243 -0.0057 0.0032  -0.0278 170 GLN C N   
5599 C  CA  . GLN C  170 ? 0.3158 0.2615 0.2604 0.0237  0.0572  0.0490  170 GLN C CA  
5600 C  C   . GLN C  170 ? 0.3513 0.2621 0.2644 -0.0223 -0.0305 -0.0935 170 GLN C C   
5601 O  O   . GLN C  170 ? 0.3080 0.3339 0.2024 -0.0076 -0.0218 -0.0642 170 GLN C O   
5602 C  CB  . GLN C  170 ? 0.3316 0.2426 0.2702 -0.0564 -0.0020 -0.0402 170 GLN C CB  
5603 C  CG  . GLN C  170 ? 0.3480 0.2530 0.2064 -0.0293 0.0331  -0.0265 170 GLN C CG  
5604 C  CD  . GLN C  170 ? 0.3784 0.3947 0.2211 -0.1486 -0.0032 -0.0250 170 GLN C CD  
5605 O  OE1 . GLN C  170 ? 0.3762 0.3142 0.1815 -0.0612 -0.0817 -0.0188 170 GLN C OE1 
5606 N  NE2 . GLN C  170 ? 0.4179 0.5024 0.1908 -0.0859 -0.0194 -0.0573 170 GLN C NE2 
5607 N  N   . GLU C  171 ? 0.3304 0.3168 0.2188 -0.0120 0.0208  -0.0206 171 GLU C N   
5608 C  CA  . GLU C  171 ? 0.3025 0.2688 0.2517 0.0122  -0.0565 -0.0574 171 GLU C CA  
5609 C  C   . GLU C  171 ? 0.4199 0.2846 0.1905 -0.0149 -0.0785 -0.0273 171 GLU C C   
5610 O  O   . GLU C  171 ? 0.2794 0.4403 0.2118 -0.0504 -0.0447 -0.0647 171 GLU C O   
5611 C  CB  . GLU C  171 ? 0.4286 0.3583 0.3436 -0.0047 0.0666  0.0873  171 GLU C CB  
5612 C  CG  . GLU C  171 ? 0.4317 0.3776 0.3957 -0.0419 -0.0442 0.0605  171 GLU C CG  
5613 C  CD  . GLU C  171 ? 0.3833 0.4988 0.5517 0.0500  0.0350  0.2463  171 GLU C CD  
5614 O  OE1 . GLU C  171 ? 0.3996 0.3437 0.5398 -0.0348 0.1062  0.0326  171 GLU C OE1 
5615 O  OE2 . GLU C  171 ? 0.8185 0.5431 0.4197 0.1356  0.0851  0.2171  171 GLU C OE2 
5616 N  N   . ALA C  172 ? 0.2879 0.3288 0.1962 0.0050  -0.0754 -0.0724 172 ALA C N   
5617 C  CA  . ALA C  172 ? 0.2648 0.3226 0.3010 -0.0103 -0.0655 0.0294  172 ALA C CA  
5618 C  C   . ALA C  172 ? 0.3718 0.2895 0.2847 0.0040  -0.1500 -0.0282 172 ALA C C   
5619 O  O   . ALA C  172 ? 0.6306 0.6377 0.2737 -0.0223 -0.2436 -0.0491 172 ALA C O   
5620 C  CB  . ALA C  172 ? 0.2798 0.5858 0.4481 -0.1580 -0.1327 0.1942  172 ALA C CB  
5621 N  N   . PHE C  173 ? 0.4866 0.4601 0.2266 0.1411  -0.1478 -0.0161 173 PHE C N   
5622 C  CA  . PHE C  173 ? 0.5813 0.3235 0.3896 0.0579  -0.0012 -0.1467 173 PHE C CA  
5623 C  C   . PHE C  173 ? 0.7204 0.3406 0.2742 -0.0396 -0.0507 -0.0040 173 PHE C C   
5624 O  O   . PHE C  173 ? 0.4438 0.4459 0.2930 -0.0283 -0.1398 0.0088  173 PHE C O   
5625 C  CB  . PHE C  173 ? 0.4696 0.4377 0.3001 0.0745  -0.0225 0.0436  173 PHE C CB  
5626 C  CG  . PHE C  173 ? 0.4718 0.4895 0.3141 0.0152  -0.0637 0.0201  173 PHE C CG  
5627 C  CD1 . PHE C  173 ? 0.4579 0.5019 0.2597 -0.0988 -0.1337 0.0294  173 PHE C CD1 
5628 C  CD2 . PHE C  173 ? 0.6555 0.5411 0.3516 -0.0182 -0.2187 0.0291  173 PHE C CD2 
5629 C  CE1 . PHE C  173 ? 0.3911 0.5062 0.3252 -0.0555 -0.0754 0.0092  173 PHE C CE1 
5630 C  CE2 . PHE C  173 ? 0.5502 0.6218 0.3890 -0.1447 -0.1289 -0.0428 173 PHE C CE2 
5631 C  CZ  . PHE C  173 ? 0.4429 0.3820 0.4064 -0.1171 -0.0892 0.0067  173 PHE C CZ  
5632 N  N   . VAL C  174 ? 0.5589 0.2436 0.3064 0.0560  -0.1306 -0.0211 174 VAL C N   
5633 C  CA  . VAL C  174 ? 0.5182 0.2404 0.3652 -0.0196 -0.1815 0.0542  174 VAL C CA  
5634 C  C   . VAL C  174 ? 0.5183 0.4675 0.3629 0.0438  -0.2082 0.1298  174 VAL C C   
5635 O  O   . VAL C  174 ? 0.4011 0.2829 0.4075 0.0722  -0.2411 0.0003  174 VAL C O   
5636 C  CB  . VAL C  174 ? 0.5340 0.3838 0.3336 0.1127  -0.2336 -0.0381 174 VAL C CB  
5637 C  CG1 . VAL C  174 ? 0.4075 0.3164 0.2861 -0.0188 -0.1722 0.0460  174 VAL C CG1 
5638 C  CG2 . VAL C  174 ? 0.4523 0.3655 0.5096 -0.0238 -0.1641 0.1826  174 VAL C CG2 
5639 N  N   . PRO C  175 ? 0.4277 0.3157 0.3776 0.0135  -0.0939 -0.0298 175 PRO C N   
5640 C  CA  . PRO C  175 ? 0.3545 0.4893 0.2255 0.1096  -0.1336 0.0450  175 PRO C CA  
5641 C  C   . PRO C  175 ? 0.4219 0.3475 0.2293 -0.0410 -0.1532 0.0992  175 PRO C C   
5642 O  O   . PRO C  175 ? 0.3507 0.5207 0.4050 0.0243  -0.1902 0.0600  175 PRO C O   
5643 C  CB  . PRO C  175 ? 0.5953 0.4010 0.4384 0.1007  -0.0375 0.1256  175 PRO C CB  
5644 C  CG  . PRO C  175 ? 0.4462 0.4064 0.4129 0.0463  -0.1781 0.1088  175 PRO C CG  
5645 C  CD  . PRO C  175 ? 0.4506 0.3269 0.3289 0.0179  -0.1777 0.0376  175 PRO C CD  
5646 N  N   . GLY C  176 ? 0.3962 0.2698 0.3092 0.0309  -0.1349 -0.0035 176 GLY C N   
5647 C  CA  . GLY C  176 ? 0.3601 0.3268 0.4314 0.0104  -0.1731 -0.1148 176 GLY C CA  
5648 C  C   . GLY C  176 ? 0.4809 0.2895 0.5205 0.0787  -0.2804 -0.0379 176 GLY C C   
5649 O  O   . GLY C  176 ? 0.5345 0.3749 0.4034 0.0443  -0.3067 -0.0303 176 GLY C O   
5650 N  N   . PHE C  177 ? 0.3938 0.2913 0.3661 0.0342  -0.1698 -0.0237 177 PHE C N   
5651 C  CA  . PHE C  177 ? 0.2917 0.3368 0.3944 0.0193  -0.2174 -0.0737 177 PHE C CA  
5652 C  C   . PHE C  177 ? 0.3310 0.3069 0.3324 -0.0218 -0.0913 -0.0100 177 PHE C C   
5653 O  O   . PHE C  177 ? 0.3327 0.3206 0.2916 0.0610  -0.0632 -0.0289 177 PHE C O   
5654 C  CB  . PHE C  177 ? 0.3403 0.4283 0.3786 -0.0162 -0.2573 0.0395  177 PHE C CB  
5655 C  CG  . PHE C  177 ? 0.2830 0.3985 0.2499 0.0496  -0.0772 0.0292  177 PHE C CG  
5656 C  CD1 . PHE C  177 ? 0.2821 0.4781 0.3392 0.0986  -0.0325 -0.0414 177 PHE C CD1 
5657 C  CD2 . PHE C  177 ? 0.3890 0.4948 0.2491 -0.0181 -0.1170 0.0674  177 PHE C CD2 
5658 C  CE1 . PHE C  177 ? 0.2947 0.4714 0.3350 0.0397  -0.1322 -0.0068 177 PHE C CE1 
5659 C  CE2 . PHE C  177 ? 0.3741 0.3884 0.1606 0.0389  -0.0739 0.0011  177 PHE C CE2 
5660 C  CZ  . PHE C  177 ? 0.3770 0.4449 0.2629 -0.0542 -0.0352 -0.0803 177 PHE C CZ  
5661 N  N   . ASN C  178 ? 0.2672 0.3039 0.2974 0.0482  -0.1047 0.0065  178 ASN C N   
5662 C  CA  . ASN C  178 ? 0.2458 0.3379 0.3250 0.1129  -0.0762 0.0176  178 ASN C CA  
5663 C  C   . ASN C  178 ? 0.2426 0.2782 0.4176 0.0637  -0.0571 0.0113  178 ASN C C   
5664 O  O   . ASN C  178 ? 0.3131 0.3303 0.2816 0.0374  -0.0960 0.0502  178 ASN C O   
5665 C  CB  . ASN C  178 ? 0.3170 0.2744 0.4069 0.1314  -0.0692 0.0548  178 ASN C CB  
5666 C  CG  . ASN C  178 ? 0.3244 0.3801 0.4379 0.1032  -0.1684 0.0142  178 ASN C CG  
5667 O  OD1 . ASN C  178 ? 0.2930 0.3236 0.3276 0.0601  -0.1046 -0.0118 178 ASN C OD1 
5668 N  ND2 . ASN C  178 ? 0.3717 0.3328 0.5031 0.1848  -0.0912 -0.0350 178 ASN C ND2 
5669 N  N   . ILE C  179 ? 0.2858 0.2410 0.2971 0.0974  -0.0892 -0.0149 179 ILE C N   
5670 C  CA  . ILE C  179 ? 0.1980 0.2614 0.2920 0.0345  -0.0610 0.0369  179 ILE C CA  
5671 C  C   . ILE C  179 ? 0.2237 0.2550 0.2375 0.0418  -0.0098 0.0353  179 ILE C C   
5672 O  O   . ILE C  179 ? 0.2039 0.2861 0.2716 0.0070  -0.0394 0.0507  179 ILE C O   
5673 C  CB  . ILE C  179 ? 0.2259 0.2430 0.2626 0.0094  -0.0697 0.0288  179 ILE C CB  
5674 C  CG1 . ILE C  179 ? 0.2595 0.3536 0.2698 -0.0018 -0.0265 -0.0359 179 ILE C CG1 
5675 C  CG2 . ILE C  179 ? 0.2244 0.3317 0.2739 -0.0089 -0.0630 0.0847  179 ILE C CG2 
5676 C  CD1 . ILE C  179 ? 0.2708 0.3356 0.2788 -0.0080 -0.0377 -0.0098 179 ILE C CD1 
5677 N  N   . GLU C  180 ? 0.2712 0.2293 0.2526 0.0301  -0.0705 0.0311  180 GLU C N   
5678 C  CA  . GLU C  180 ? 0.1976 0.2969 0.2610 0.0352  -0.0381 0.0107  180 GLU C CA  
5679 C  C   . GLU C  180 ? 0.3019 0.2737 0.2700 0.0646  -0.0509 0.0453  180 GLU C C   
5680 O  O   . GLU C  180 ? 0.3300 0.2836 0.2713 -0.0039 -0.0666 0.0000  180 GLU C O   
5681 C  CB  . GLU C  180 ? 0.3159 0.3732 0.3220 0.0653  -0.0073 -0.0249 180 GLU C CB  
5682 C  CG  . GLU C  180 ? 0.3162 0.3977 0.3972 0.0485  -0.0646 -0.1005 180 GLU C CG  
5683 C  CD  . GLU C  180 ? 0.4005 0.4799 0.3255 0.0067  -0.0478 -0.0278 180 GLU C CD  
5684 O  OE1 . GLU C  180 ? 0.4136 0.3950 0.3602 0.0160  -0.0328 -0.1435 180 GLU C OE1 
5685 O  OE2 . GLU C  180 ? 0.5213 0.4143 0.3731 0.1210  -0.1004 -0.1229 180 GLU C OE2 
5686 N  N   . GLU C  181 ? 0.2734 0.2556 0.2721 0.0432  -0.0499 0.0634  181 GLU C N   
5687 C  CA  . GLU C  181 ? 0.2658 0.2910 0.3044 0.0494  -0.0474 0.1157  181 GLU C CA  
5688 C  C   . GLU C  181 ? 0.2931 0.2026 0.3574 0.0478  0.0586  -0.0089 181 GLU C C   
5689 O  O   . GLU C  181 ? 0.2383 0.2979 0.3259 0.0255  -0.0127 0.0863  181 GLU C O   
5690 C  CB  . GLU C  181 ? 0.2521 0.4916 0.3186 0.0809  -0.0388 0.1696  181 GLU C CB  
5691 C  CG  . GLU C  181 ? 0.3098 0.6431 0.5236 0.1559  -0.0280 0.1235  181 GLU C CG  
5692 C  CD  . GLU C  181 ? 0.4055 0.8179 0.4521 0.1656  -0.0901 0.2585  181 GLU C CD  
5693 O  OE1 . GLU C  181 ? 0.2597 1.1920 0.6560 0.1307  -0.0681 0.0093  181 GLU C OE1 
5694 O  OE2 . GLU C  181 ? 0.4178 1.0038 0.7052 0.2495  -0.1113 0.2176  181 GLU C OE2 
5695 N  N   . LEU C  182 ? 0.2558 0.2185 0.2215 0.0578  -0.0337 0.0032  182 LEU C N   
5696 C  CA  . LEU C  182 ? 0.2143 0.2317 0.2441 0.0292  -0.0391 0.0003  182 LEU C CA  
5697 C  C   . LEU C  182 ? 0.2474 0.2456 0.2814 -0.0248 -0.0269 -0.0073 182 LEU C C   
5698 O  O   . LEU C  182 ? 0.2311 0.3439 0.2061 0.0255  -0.0164 0.0790  182 LEU C O   
5699 C  CB  . LEU C  182 ? 0.2323 0.2272 0.2489 0.0092  -0.0611 0.0212  182 LEU C CB  
5700 C  CG  . LEU C  182 ? 0.2588 0.2319 0.1773 0.0147  -0.0250 0.0248  182 LEU C CG  
5701 C  CD1 . LEU C  182 ? 0.3195 0.2250 0.2652 0.0489  -0.0330 -0.0009 182 LEU C CD1 
5702 C  CD2 . LEU C  182 ? 0.3040 0.2972 0.1956 0.0039  -0.0150 0.0148  182 LEU C CD2 
5703 N  N   . LEU C  183 ? 0.2528 0.2359 0.2126 0.0335  -0.0536 0.0378  183 LEU C N   
5704 C  CA  . LEU C  183 ? 0.2438 0.2540 0.2280 -0.0119 -0.0321 0.0365  183 LEU C CA  
5705 C  C   . LEU C  183 ? 0.2076 0.2369 0.2709 0.0610  -0.0099 0.0242  183 LEU C C   
5706 O  O   . LEU C  183 ? 0.2942 0.2973 0.2639 0.0809  -0.0762 0.0465  183 LEU C O   
5707 C  CB  . LEU C  183 ? 0.2297 0.2550 0.2728 0.0243  -0.0066 0.0397  183 LEU C CB  
5708 C  CG  . LEU C  183 ? 0.3353 0.2273 0.2354 0.0248  0.0035  -0.0049 183 LEU C CG  
5709 C  CD1 . LEU C  183 ? 0.3788 0.4180 0.3122 0.0073  0.1250  0.0281  183 LEU C CD1 
5710 C  CD2 . LEU C  183 ? 0.2807 0.3149 0.2885 0.0429  -0.0102 0.0982  183 LEU C CD2 
5711 N  N   . PRO C  184 ? 0.2192 0.2567 0.2470 -0.0021 -0.0103 0.0723  184 PRO C N   
5712 C  CA  . PRO C  184 ? 0.2500 0.1825 0.2405 0.0294  -0.0229 0.0288  184 PRO C CA  
5713 C  C   . PRO C  184 ? 0.3841 0.2635 0.1837 -0.0136 0.0094  -0.0604 184 PRO C C   
5714 O  O   . PRO C  184 ? 0.3252 0.2922 0.2920 0.0201  0.0234  0.0446  184 PRO C O   
5715 C  CB  . PRO C  184 ? 0.3161 0.3494 0.2866 -0.0004 -0.0605 0.0846  184 PRO C CB  
5716 C  CG  . PRO C  184 ? 0.2876 0.2251 0.2579 -0.0263 -0.0245 0.0435  184 PRO C CG  
5717 C  CD  . PRO C  184 ? 0.2463 0.2416 0.2111 0.0280  -0.0419 0.0480  184 PRO C CD  
5718 N  N   . GLU C  185 ? 0.3631 0.2754 0.3041 -0.0438 -0.0717 -0.0577 185 GLU C N   
5719 C  CA  . GLU C  185 ? 0.4412 0.2523 0.3010 -0.0297 -0.0568 0.0024  185 GLU C CA  
5720 C  C   . GLU C  185 ? 0.3191 0.3183 0.2966 0.0489  -0.0514 0.0156  185 GLU C C   
5721 O  O   . GLU C  185 ? 0.3007 0.3353 0.3820 0.0878  -0.0234 0.0571  185 GLU C O   
5722 C  CB  . GLU C  185 ? 0.5149 0.3793 0.2979 -0.0888 -0.0414 0.1044  185 GLU C CB  
5723 C  CG  . GLU C  185 ? 0.7458 0.6183 0.3048 0.0878  -0.0615 0.1455  185 GLU C CG  
5724 C  CD  . GLU C  185 ? 0.6916 0.6086 0.7355 0.2478  0.0160  0.2271  185 GLU C CD  
5725 O  OE1 . GLU C  185 ? 0.9947 1.0197 0.7164 -0.0363 0.0436  0.4624  185 GLU C OE1 
5726 O  OE2 . GLU C  185 ? 1.3543 1.0631 0.7628 0.1270  -0.2017 0.3365  185 GLU C OE2 
5727 N  N   . ARG C  186 ? 0.4075 0.2192 0.3626 0.0958  -0.0072 0.0057  186 ARG C N   
5728 C  CA  . ARG C  186 ? 0.4750 0.3741 0.3283 0.0100  -0.1461 -0.0303 186 ARG C CA  
5729 C  C   . ARG C  186 ? 0.2544 0.3434 0.2626 0.0414  -0.0604 -0.0406 186 ARG C C   
5730 O  O   . ARG C  186 ? 0.2823 0.3630 0.2800 0.0763  0.0155  0.0515  186 ARG C O   
5731 C  CB  . ARG C  186 ? 0.3358 0.2626 0.4895 0.0122  0.0401  -0.0326 186 ARG C CB  
5732 C  CG  . ARG C  186 ? 0.5359 0.2186 0.5732 -0.0596 -0.0294 -0.0801 186 ARG C CG  
5733 C  CD  . ARG C  186 ? 0.7184 0.3470 0.4619 -0.2463 -0.0873 0.0127  186 ARG C CD  
5734 N  NE  . ARG C  186 ? 0.9286 0.4009 0.7983 0.0239  0.2474  0.0047  186 ARG C NE  
5735 C  CZ  . ARG C  186 ? 0.8031 0.8675 0.7695 -0.1400 0.1937  0.1104  186 ARG C CZ  
5736 N  NH1 . ARG C  186 ? 1.1015 0.4536 0.9351 -0.3682 -0.1544 0.1018  186 ARG C NH1 
5737 N  NH2 . ARG C  186 ? 0.7729 0.3240 1.1973 0.0961  0.3132  -0.0690 186 ARG C NH2 
5738 N  N   . THR C  187 ? 0.2949 0.2417 0.2757 0.0495  0.0177  -0.0152 187 THR C N   
5739 C  CA  . THR C  187 ? 0.2875 0.2409 0.2310 0.0435  0.0241  0.0321  187 THR C CA  
5740 C  C   . THR C  187 ? 0.3080 0.3045 0.2771 0.1429  0.0651  0.0147  187 THR C C   
5741 O  O   . THR C  187 ? 0.2763 0.2935 0.2514 0.0728  0.0063  0.0122  187 THR C O   
5742 C  CB  . THR C  187 ? 0.2334 0.2965 0.3046 0.0575  0.0278  -0.0250 187 THR C CB  
5743 O  OG1 . THR C  187 ? 0.2834 0.3271 0.3947 0.0945  -0.0089 0.0009  187 THR C OG1 
5744 C  CG2 . THR C  187 ? 0.2953 0.3430 0.2555 0.0086  -0.0003 -0.0048 187 THR C CG2 
5745 N  N   . ALA C  188 ? 0.2855 0.2948 0.2246 0.1207  -0.0133 0.0394  188 ALA C N   
5746 C  CA  . ALA C  188 ? 0.2538 0.2713 0.2213 0.1112  -0.0089 -0.0160 188 ALA C CA  
5747 C  C   . ALA C  188 ? 0.2120 0.2397 0.2213 0.0649  0.0215  0.0307  188 ALA C C   
5748 O  O   . ALA C  188 ? 0.2494 0.2591 0.2179 0.0952  0.0052  0.0531  188 ALA C O   
5749 C  CB  . ALA C  188 ? 0.4194 0.2852 0.2917 0.1474  -0.0108 -0.0129 188 ALA C CB  
5750 N  N   . GLU C  189 ? 0.2610 0.2303 0.2309 0.0920  0.0414  0.0196  189 GLU C N   
5751 C  CA  . GLU C  189 ? 0.2424 0.2140 0.2752 0.0730  0.0440  0.0253  189 GLU C CA  
5752 C  C   . GLU C  189 ? 0.2586 0.2284 0.1992 0.1095  -0.0052 0.0021  189 GLU C C   
5753 O  O   . GLU C  189 ? 0.2215 0.2400 0.2138 0.0623  0.0253  0.0269  189 GLU C O   
5754 C  CB  . GLU C  189 ? 0.3209 0.1563 0.3737 0.0602  0.0690  0.0000  189 GLU C CB  
5755 C  CG  . GLU C  189 ? 0.4623 0.1696 0.4611 0.0124  0.0913  -0.0370 189 GLU C CG  
5756 C  CD  . GLU C  189 ? 0.5260 0.2500 0.5704 0.0212  0.1835  0.0329  189 GLU C CD  
5757 O  OE1 . GLU C  189 ? 0.4136 0.2837 0.5480 -0.0003 0.1153  0.0296  189 GLU C OE1 
5758 O  OE2 . GLU C  189 ? 0.5779 0.3773 0.8407 0.1758  0.0886  -0.0209 189 GLU C OE2 
5759 N  N   . TYR C  190 ? 0.2169 0.1960 0.2144 0.0702  0.0247  0.0363  190 TYR C N   
5760 C  CA  . TYR C  190 ? 0.2375 0.1591 0.1933 0.0652  0.0116  0.0263  190 TYR C CA  
5761 C  C   . TYR C  190 ? 0.2016 0.1866 0.1515 0.0387  0.0379  0.0392  190 TYR C C   
5762 O  O   . TYR C  190 ? 0.2222 0.1790 0.1875 0.0564  0.0212  0.0261  190 TYR C O   
5763 C  CB  . TYR C  190 ? 0.2115 0.2425 0.1505 0.0243  0.0058  0.0201  190 TYR C CB  
5764 C  CG  . TYR C  190 ? 0.1825 0.2053 0.1508 0.0536  0.0100  0.0115  190 TYR C CG  
5765 C  CD1 . TYR C  190 ? 0.1928 0.2301 0.1683 0.0479  0.0212  0.0251  190 TYR C CD1 
5766 C  CD2 . TYR C  190 ? 0.2066 0.2351 0.2046 0.0517  0.0103  0.0114  190 TYR C CD2 
5767 C  CE1 . TYR C  190 ? 0.1775 0.2391 0.1852 0.0296  0.0047  0.0220  190 TYR C CE1 
5768 C  CE2 . TYR C  190 ? 0.2120 0.2627 0.1769 0.0439  0.0183  0.0253  190 TYR C CE2 
5769 C  CZ  . TYR C  190 ? 0.2184 0.2670 0.1720 0.0408  0.0247  0.0115  190 TYR C CZ  
5770 O  OH  . TYR C  190 ? 0.2011 0.2922 0.1788 0.0550  0.0253  0.0050  190 TYR C OH  
5771 N  N   . TYR C  191 ? 0.1747 0.1700 0.1732 0.0339  -0.0072 0.0067  191 TYR C N   
5772 C  CA  . TYR C  191 ? 0.1651 0.1564 0.1736 0.0303  0.0013  0.0342  191 TYR C CA  
5773 C  C   . TYR C  191 ? 0.1472 0.1576 0.1362 0.0110  0.0063  -0.0027 191 TYR C C   
5774 O  O   . TYR C  191 ? 0.1841 0.2146 0.1363 0.0029  -0.0052 0.0064  191 TYR C O   
5775 C  CB  . TYR C  191 ? 0.1526 0.1863 0.1812 0.0198  0.0082  0.0080  191 TYR C CB  
5776 C  CG  . TYR C  191 ? 0.1761 0.1673 0.1703 0.0239  -0.0127 0.0074  191 TYR C CG  
5777 C  CD1 . TYR C  191 ? 0.1983 0.1671 0.1555 -0.0031 0.0132  -0.0153 191 TYR C CD1 
5778 C  CD2 . TYR C  191 ? 0.2004 0.1529 0.1722 0.0501  0.0154  0.0172  191 TYR C CD2 
5779 C  CE1 . TYR C  191 ? 0.1987 0.1860 0.2235 0.0300  0.0322  0.0061  191 TYR C CE1 
5780 C  CE2 . TYR C  191 ? 0.2042 0.1582 0.2528 0.0565  0.0188  0.0325  191 TYR C CE2 
5781 C  CZ  . TYR C  191 ? 0.2045 0.1981 0.2217 0.0044  0.0562  0.0120  191 TYR C CZ  
5782 O  OH  . TYR C  191 ? 0.2305 0.1933 0.2867 -0.0055 0.0435  0.0267  191 TYR C OH  
5783 N  N   . ARG C  192 ? 0.1752 0.1790 0.1398 0.0176  -0.0137 0.0300  192 ARG C N   
5784 C  CA  . ARG C  192 ? 0.1496 0.1842 0.1569 0.0131  -0.0017 0.0110  192 ARG C CA  
5785 C  C   . ARG C  192 ? 0.1211 0.1641 0.1467 -0.0011 -0.0060 -0.0016 192 ARG C C   
5786 O  O   . ARG C  192 ? 0.1689 0.1581 0.1404 0.0015  -0.0216 -0.0155 192 ARG C O   
5787 C  CB  . ARG C  192 ? 0.1585 0.1838 0.1703 0.0278  0.0030  -0.0043 192 ARG C CB  
5788 C  CG  . ARG C  192 ? 0.1873 0.2007 0.1605 -0.0055 0.0142  -0.0220 192 ARG C CG  
5789 C  CD  . ARG C  192 ? 0.1548 0.2504 0.1591 0.0172  -0.0100 -0.0103 192 ARG C CD  
5790 N  NE  . ARG C  192 ? 0.1634 0.2385 0.1663 0.0072  -0.0047 -0.0219 192 ARG C NE  
5791 C  CZ  . ARG C  192 ? 0.1661 0.2574 0.1907 0.0170  -0.0144 -0.0086 192 ARG C CZ  
5792 N  NH1 . ARG C  192 ? 0.1816 0.3113 0.1694 0.0046  0.0176  -0.0212 192 ARG C NH1 
5793 N  NH2 . ARG C  192 ? 0.1869 0.2795 0.2149 0.0116  -0.0023 0.0044  192 ARG C NH2 
5794 N  N   . TYR C  193 ? 0.1479 0.1380 0.1204 0.0000  0.0017  -0.0032 193 TYR C N   
5795 C  CA  . TYR C  193 ? 0.1455 0.1493 0.1475 0.0013  -0.0111 0.0108  193 TYR C CA  
5796 C  C   . TYR C  193 ? 0.1381 0.1577 0.1125 -0.0006 -0.0027 0.0111  193 TYR C C   
5797 O  O   . TYR C  193 ? 0.1565 0.1732 0.1282 0.0004  -0.0272 0.0022  193 TYR C O   
5798 C  CB  . TYR C  193 ? 0.1486 0.1734 0.1295 -0.0057 -0.0096 -0.0179 193 TYR C CB  
5799 C  CG  . TYR C  193 ? 0.1244 0.1498 0.1202 -0.0137 -0.0122 0.0019  193 TYR C CG  
5800 C  CD1 . TYR C  193 ? 0.1346 0.1564 0.1288 0.0038  0.0054  0.0075  193 TYR C CD1 
5801 C  CD2 . TYR C  193 ? 0.1356 0.1620 0.1288 0.0106  -0.0059 -0.0036 193 TYR C CD2 
5802 C  CE1 . TYR C  193 ? 0.1240 0.1688 0.1272 -0.0069 -0.0139 -0.0020 193 TYR C CE1 
5803 C  CE2 . TYR C  193 ? 0.1303 0.1819 0.1168 -0.0008 -0.0231 0.0006  193 TYR C CE2 
5804 C  CZ  . TYR C  193 ? 0.1197 0.1562 0.1230 -0.0005 0.0010  -0.0026 193 TYR C CZ  
5805 O  OH  . TYR C  193 ? 0.1349 0.1636 0.1311 0.0000  -0.0044 -0.0042 193 TYR C OH  
5806 N  N   . ARG C  194 ? 0.1534 0.1619 0.1272 0.0043  -0.0053 0.0148  194 ARG C N   
5807 C  CA  . ARG C  194 ? 0.1515 0.1642 0.1329 -0.0063 0.0071  0.0004  194 ARG C CA  
5808 C  C   . ARG C  194 ? 0.1423 0.1731 0.1403 -0.0099 -0.0156 0.0022  194 ARG C C   
5809 O  O   . ARG C  194 ? 0.1520 0.1810 0.1503 -0.0033 -0.0289 -0.0111 194 ARG C O   
5810 C  CB  . ARG C  194 ? 0.2476 0.1913 0.1354 -0.0006 0.0380  0.0294  194 ARG C CB  
5811 C  CG  . ARG C  194 ? 0.2627 0.2570 0.1733 0.0054  0.0374  0.0083  194 ARG C CG  
5812 C  CD  . ARG C  194 ? 0.5109 0.5831 0.3258 0.0021  0.1926  0.0856  194 ARG C CD  
5813 N  NE  . ARG C  194 ? 0.5636 0.7619 0.5327 0.1217  0.1671  0.0618  194 ARG C NE  
5814 C  CZ  . ARG C  194 ? 0.5809 0.7525 0.8719 0.0554  0.0558  -0.3588 194 ARG C CZ  
5815 N  NH1 . ARG C  194 ? 0.3443 0.6880 0.4058 -0.1428 0.0712  -0.0849 194 ARG C NH1 
5816 N  NH2 . ARG C  194 ? 0.5483 0.7171 0.6000 0.1333  0.1416  -0.0569 194 ARG C NH2 
5817 N  N   . GLY C  195 ? 0.1580 0.1485 0.1245 -0.0073 -0.0059 -0.0042 195 GLY C N   
5818 C  CA  . GLY C  195 ? 0.1327 0.1668 0.1308 -0.0079 -0.0184 -0.0102 195 GLY C CA  
5819 C  C   . GLY C  195 ? 0.1361 0.1809 0.1404 -0.0151 0.0047  0.0207  195 GLY C C   
5820 O  O   . GLY C  195 ? 0.1529 0.1639 0.1474 -0.0192 0.0093  -0.0019 195 GLY C O   
5821 N  N   . SER C  196 ? 0.1494 0.1611 0.1262 -0.0057 -0.0060 -0.0013 196 SER C N   
5822 C  CA  . SER C  196 ? 0.1672 0.1503 0.1347 -0.0216 -0.0208 0.0078  196 SER C CA  
5823 C  C   . SER C  196 ? 0.1485 0.1685 0.1404 -0.0270 0.0104  -0.0120 196 SER C C   
5824 O  O   . SER C  196 ? 0.1507 0.1781 0.1237 -0.0211 -0.0129 -0.0029 196 SER C O   
5825 C  CB  . SER C  196 ? 0.1317 0.1678 0.1427 -0.0106 0.0192  0.0103  196 SER C CB  
5826 O  OG  . SER C  196 ? 0.1376 0.1504 0.1414 -0.0058 0.0041  -0.0108 196 SER C OG  
5827 N  N   . LEU C  197 ? 0.1478 0.1642 0.1282 -0.0147 -0.0172 -0.0093 197 LEU C N   
5828 C  CA  . LEU C  197 ? 0.1617 0.1934 0.1263 -0.0378 -0.0017 -0.0209 197 LEU C CA  
5829 C  C   . LEU C  197 ? 0.1653 0.1476 0.1366 0.0084  -0.0081 0.0060  197 LEU C C   
5830 O  O   . LEU C  197 ? 0.1551 0.1826 0.1323 -0.0022 0.0035  -0.0103 197 LEU C O   
5831 C  CB  . LEU C  197 ? 0.1609 0.1986 0.1600 -0.0234 -0.0151 -0.0259 197 LEU C CB  
5832 C  CG  . LEU C  197 ? 0.1915 0.2216 0.1989 -0.0721 -0.0348 -0.0062 197 LEU C CG  
5833 C  CD1 . LEU C  197 ? 0.2091 0.2863 0.2076 -0.0547 0.0035  -0.0048 197 LEU C CD1 
5834 C  CD2 . LEU C  197 ? 0.2098 0.2558 0.2233 -0.0776 -0.0429 -0.0309 197 LEU C CD2 
5835 N  N   . THR C  198 ? 0.1511 0.1624 0.1428 -0.0208 -0.0240 -0.0068 198 THR C N   
5836 C  CA  . THR C  198 ? 0.1512 0.1703 0.1368 -0.0083 0.0085  -0.0114 198 THR C CA  
5837 C  C   . THR C  198 ? 0.1388 0.1925 0.1304 -0.0359 -0.0097 -0.0009 198 THR C C   
5838 O  O   . THR C  198 ? 0.1555 0.1766 0.1455 -0.0337 0.0091  -0.0196 198 THR C O   
5839 C  CB  . THR C  198 ? 0.1786 0.1730 0.1100 -0.0158 -0.0390 -0.0273 198 THR C CB  
5840 O  OG1 . THR C  198 ? 0.1488 0.1958 0.1258 -0.0257 -0.0346 -0.0027 198 THR C OG1 
5841 C  CG2 . THR C  198 ? 0.1631 0.1859 0.1373 -0.0196 -0.0298 -0.0164 198 THR C CG2 
5842 N  N   . THR C  199 ? 0.1580 0.1743 0.1448 -0.0409 -0.0108 -0.0189 199 THR C N   
5843 C  CA  . THR C  199 ? 0.1778 0.1525 0.1474 -0.0012 -0.0353 -0.0247 199 THR C CA  
5844 C  C   . THR C  199 ? 0.1408 0.1671 0.1637 -0.0299 -0.0102 -0.0185 199 THR C C   
5845 O  O   . THR C  199 ? 0.1726 0.2098 0.1505 -0.0336 -0.0098 -0.0220 199 THR C O   
5846 C  CB  . THR C  199 ? 0.1588 0.1909 0.1736 -0.0075 -0.0352 -0.0042 199 THR C CB  
5847 O  OG1 . THR C  199 ? 0.1727 0.2518 0.1701 -0.0171 -0.0416 0.0000  199 THR C OG1 
5848 C  CG2 . THR C  199 ? 0.1988 0.2078 0.1709 0.0000  -0.0421 -0.0183 199 THR C CG2 
5849 N  N   . PRO C  200 ? 0.1602 0.1829 0.1267 -0.0237 -0.0201 -0.0143 200 PRO C N   
5850 C  CA  . PRO C  200 ? 0.1894 0.1886 0.1657 -0.0484 -0.0095 -0.0073 200 PRO C CA  
5851 C  C   . PRO C  200 ? 0.1953 0.2150 0.1479 -0.0726 -0.0311 -0.0399 200 PRO C C   
5852 O  O   . PRO C  200 ? 0.1790 0.2366 0.1984 -0.0502 -0.0212 -0.0163 200 PRO C O   
5853 C  CB  . PRO C  200 ? 0.1861 0.2135 0.1620 -0.0407 -0.0069 -0.0304 200 PRO C CB  
5854 C  CG  . PRO C  200 ? 0.1984 0.1707 0.1926 -0.0352 0.0076  -0.0375 200 PRO C CG  
5855 C  CD  . PRO C  200 ? 0.1886 0.2210 0.1260 -0.0248 0.0031  -0.0272 200 PRO C CD  
5856 N  N   . PRO C  201 ? 0.1766 0.2092 0.1561 -0.0409 -0.0021 -0.0118 201 PRO C N   
5857 C  CA  . PRO C  201 ? 0.2067 0.1655 0.1933 -0.0493 -0.0264 -0.0273 201 PRO C CA  
5858 C  C   . PRO C  201 ? 0.1514 0.1584 0.1669 -0.0039 -0.0104 -0.0100 201 PRO C C   
5859 O  O   . PRO C  201 ? 0.2071 0.1627 0.1810 -0.0368 -0.0052 0.0051  201 PRO C O   
5860 C  CB  . PRO C  201 ? 0.2003 0.2084 0.1764 -0.0748 0.0008  -0.0380 201 PRO C CB  
5861 C  CG  . PRO C  201 ? 0.2250 0.2561 0.2199 -0.0666 -0.0035 -0.0131 201 PRO C CG  
5862 C  CD  . PRO C  201 ? 0.1859 0.2291 0.2426 -0.0690 -0.0258 -0.0279 201 PRO C CD  
5863 N  N   . CYS C  202 ? 0.1614 0.1588 0.1562 -0.0194 -0.0117 -0.0138 202 CYS C N   
5864 C  CA  . CYS C  202 ? 0.1513 0.1639 0.1472 -0.0219 -0.0114 -0.0249 202 CYS C CA  
5865 C  C   . CYS C  202 ? 0.1471 0.1543 0.1566 -0.0020 -0.0035 -0.0044 202 CYS C C   
5866 O  O   . CYS C  202 ? 0.1641 0.1812 0.1487 -0.0182 -0.0009 0.0030  202 CYS C O   
5867 C  CB  . CYS C  202 ? 0.1776 0.1788 0.1444 -0.0080 0.0145  -0.0041 202 CYS C CB  
5868 S  SG  . CYS C  202 ? 0.1654 0.1923 0.1472 -0.0306 -0.0044 -0.0134 202 CYS C SG  
5869 N  N   . ASN C  203 ? 0.1461 0.1773 0.1672 -0.0364 0.0000  -0.0044 203 ASN C N   
5870 C  CA  . ASN C  203 ? 0.1620 0.1905 0.1858 -0.0510 0.0188  -0.0084 203 ASN C CA  
5871 C  C   . ASN C  203 ? 0.1445 0.1962 0.1958 -0.0504 0.0187  0.0080  203 ASN C C   
5872 O  O   . ASN C  203 ? 0.1619 0.1823 0.1497 -0.0289 0.0082  -0.0057 203 ASN C O   
5873 C  CB  . ASN C  203 ? 0.1600 0.2408 0.1785 -0.0779 0.0116  -0.0259 203 ASN C CB  
5874 C  CG  . ASN C  203 ? 0.2048 0.2132 0.1865 -0.0293 0.0037  -0.0102 203 ASN C CG  
5875 O  OD1 . ASN C  203 ? 0.2509 0.2233 0.2440 -0.0839 0.0009  -0.0487 203 ASN C OD1 
5876 N  ND2 . ASN C  203 ? 0.2516 0.2003 0.2917 -0.0259 0.0378  -0.0288 203 ASN C ND2 
5877 N  N   . PRO C  204 ? 0.1713 0.1736 0.1700 -0.0300 0.0091  0.0106  204 PRO C N   
5878 C  CA  . PRO C  204 ? 0.1504 0.2069 0.1769 -0.0289 -0.0091 -0.0158 204 PRO C CA  
5879 C  C   . PRO C  204 ? 0.1627 0.1958 0.1261 -0.0303 -0.0025 -0.0044 204 PRO C C   
5880 O  O   . PRO C  204 ? 0.2112 0.2320 0.1492 -0.0175 -0.0059 0.0108  204 PRO C O   
5881 C  CB  . PRO C  204 ? 0.1909 0.1976 0.1649 -0.0109 -0.0080 0.0071  204 PRO C CB  
5882 C  CG  . PRO C  204 ? 0.2182 0.2310 0.1822 -0.0230 -0.0066 0.0106  204 PRO C CG  
5883 C  CD  . PRO C  204 ? 0.2271 0.1614 0.1964 0.0106  0.0055  0.0008  204 PRO C CD  
5884 N  N   . THR C  205 ? 0.1427 0.2053 0.1608 -0.0234 -0.0003 0.0075  205 THR C N   
5885 C  CA  . THR C  205 ? 0.1345 0.2157 0.1708 -0.0194 0.0079  0.0015  205 THR C CA  
5886 C  C   . THR C  205 ? 0.1513 0.2221 0.1516 -0.0249 0.0194  -0.0005 205 THR C C   
5887 O  O   . THR C  205 ? 0.1468 0.2451 0.2000 -0.0175 0.0042  0.0032  205 THR C O   
5888 C  CB  . THR C  205 ? 0.1673 0.2304 0.1687 -0.0310 0.0089  -0.0265 205 THR C CB  
5889 O  OG1 . THR C  205 ? 0.1782 0.2552 0.1917 -0.0436 0.0004  -0.0037 205 THR C OG1 
5890 C  CG2 . THR C  205 ? 0.1994 0.2304 0.2825 -0.0533 -0.0212 0.0506  205 THR C CG2 
5891 N  N   . VAL C  206 ? 0.1682 0.1917 0.1671 -0.0104 0.0238  0.0201  206 VAL C N   
5892 C  CA  . VAL C  206 ? 0.1615 0.1727 0.1509 -0.0353 0.0138  -0.0002 206 VAL C CA  
5893 C  C   . VAL C  206 ? 0.1402 0.1759 0.1430 -0.0187 0.0096  0.0085  206 VAL C C   
5894 O  O   . VAL C  206 ? 0.1378 0.2202 0.1830 -0.0116 -0.0171 0.0096  206 VAL C O   
5895 C  CB  . VAL C  206 ? 0.1466 0.2023 0.1468 -0.0020 0.0027  -0.0036 206 VAL C CB  
5896 C  CG1 . VAL C  206 ? 0.1395 0.2137 0.1530 -0.0055 -0.0053 -0.0111 206 VAL C CG1 
5897 C  CG2 . VAL C  206 ? 0.1561 0.2266 0.1454 -0.0189 -0.0087 -0.0296 206 VAL C CG2 
5898 N  N   . LEU C  207 ? 0.1679 0.1953 0.1261 0.0135  -0.0044 0.0047  207 LEU C N   
5899 C  CA  . LEU C  207 ? 0.1629 0.2091 0.1507 0.0178  0.0153  -0.0024 207 LEU C CA  
5900 C  C   . LEU C  207 ? 0.1364 0.1782 0.1293 0.0037  -0.0175 -0.0138 207 LEU C C   
5901 O  O   . LEU C  207 ? 0.1476 0.2223 0.1351 -0.0081 -0.0203 0.0030  207 LEU C O   
5902 C  CB  . LEU C  207 ? 0.1611 0.2289 0.1838 0.0223  0.0244  -0.0082 207 LEU C CB  
5903 C  CG  . LEU C  207 ? 0.2419 0.2649 0.1951 0.0584  0.0201  -0.0106 207 LEU C CG  
5904 C  CD1 . LEU C  207 ? 0.4323 0.3560 0.1738 0.0324  -0.0412 -0.0449 207 LEU C CD1 
5905 C  CD2 . LEU C  207 ? 0.3305 0.5831 0.3324 0.0679  0.1069  -0.1171 207 LEU C CD2 
5906 N  N   . TRP C  208 ? 0.1336 0.1993 0.1391 0.0081  -0.0054 0.0117  208 TRP C N   
5907 C  CA  . TRP C  208 ? 0.1299 0.1719 0.1586 -0.0047 -0.0005 0.0100  208 TRP C CA  
5908 C  C   . TRP C  208 ? 0.1491 0.1623 0.1254 -0.0060 -0.0118 0.0263  208 TRP C C   
5909 O  O   . TRP C  208 ? 0.1675 0.2031 0.1328 0.0098  -0.0081 -0.0008 208 TRP C O   
5910 C  CB  . TRP C  208 ? 0.1235 0.1817 0.1471 0.0148  -0.0258 -0.0037 208 TRP C CB  
5911 C  CG  . TRP C  208 ? 0.1439 0.1693 0.1076 0.0050  -0.0117 0.0041  208 TRP C CG  
5912 C  CD1 . TRP C  208 ? 0.1364 0.1797 0.1270 0.0026  -0.0108 -0.0012 208 TRP C CD1 
5913 C  CD2 . TRP C  208 ? 0.1271 0.1911 0.1105 -0.0043 -0.0196 0.0062  208 TRP C CD2 
5914 N  NE1 . TRP C  208 ? 0.1463 0.1805 0.1231 0.0041  -0.0069 0.0127  208 TRP C NE1 
5915 C  CE2 . TRP C  208 ? 0.1338 0.1892 0.1479 0.0015  0.0003  0.0044  208 TRP C CE2 
5916 C  CE3 . TRP C  208 ? 0.1359 0.2098 0.1332 0.0115  -0.0190 0.0088  208 TRP C CE3 
5917 C  CZ2 . TRP C  208 ? 0.1475 0.2226 0.1265 -0.0092 -0.0020 0.0134  208 TRP C CZ2 
5918 C  CZ3 . TRP C  208 ? 0.1621 0.2125 0.1075 0.0015  -0.0195 0.0111  208 TRP C CZ3 
5919 C  CH2 . TRP C  208 ? 0.1609 0.1841 0.1636 0.0038  0.0054  0.0162  208 TRP C CH2 
5920 N  N   . THR C  209 ? 0.1596 0.1786 0.1423 0.0290  -0.0027 0.0261  209 THR C N   
5921 C  CA  . THR C  209 ? 0.1469 0.1852 0.1342 0.0013  -0.0114 0.0111  209 THR C CA  
5922 C  C   . THR C  209 ? 0.1714 0.1903 0.1164 0.0188  -0.0071 -0.0044 209 THR C C   
5923 O  O   . THR C  209 ? 0.1969 0.2423 0.1163 0.0135  -0.0092 0.0088  209 THR C O   
5924 C  CB  . THR C  209 ? 0.1418 0.2232 0.1663 0.0108  -0.0098 0.0008  209 THR C CB  
5925 O  OG1 . THR C  209 ? 0.1494 0.2345 0.1430 0.0215  0.0010  0.0035  209 THR C OG1 
5926 C  CG2 . THR C  209 ? 0.1791 0.2154 0.1967 -0.0076 0.0081  0.0059  209 THR C CG2 
5927 N  N   . VAL C  210 ? 0.1586 0.1990 0.1320 0.0222  -0.0097 0.0320  210 VAL C N   
5928 C  CA  . VAL C  210 ? 0.1586 0.1649 0.1667 0.0405  0.0050  0.0300  210 VAL C CA  
5929 C  C   . VAL C  210 ? 0.1805 0.2003 0.1166 0.0215  0.0179  0.0226  210 VAL C C   
5930 O  O   . VAL C  210 ? 0.1860 0.1789 0.1562 0.0313  0.0170  0.0040  210 VAL C O   
5931 C  CB  . VAL C  210 ? 0.1628 0.1720 0.1574 0.0210  -0.0073 0.0125  210 VAL C CB  
5932 C  CG1 . VAL C  210 ? 0.1843 0.1927 0.1481 0.0120  0.0122  0.0128  210 VAL C CG1 
5933 C  CG2 . VAL C  210 ? 0.1912 0.1736 0.1615 0.0152  -0.0068 0.0198  210 VAL C CG2 
5934 N  N   . PHE C  211 ? 0.1700 0.2023 0.1758 0.0642  0.0055  0.0322  211 PHE C N   
5935 C  CA  . PHE C  211 ? 0.1923 0.1814 0.1760 0.0297  0.0107  0.0293  211 PHE C CA  
5936 C  C   . PHE C  211 ? 0.2158 0.1918 0.1965 0.0339  0.0200  0.0675  211 PHE C C   
5937 O  O   . PHE C  211 ? 0.2000 0.2281 0.1858 0.0463  0.0164  0.0385  211 PHE C O   
5938 C  CB  . PHE C  211 ? 0.1822 0.2341 0.1839 0.0155  -0.0067 0.0616  211 PHE C CB  
5939 C  CG  . PHE C  211 ? 0.1727 0.1971 0.1832 0.0420  0.0004  0.0502  211 PHE C CG  
5940 C  CD1 . PHE C  211 ? 0.1766 0.2367 0.1973 0.0491  -0.0052 0.0376  211 PHE C CD1 
5941 C  CD2 . PHE C  211 ? 0.2189 0.2540 0.2344 0.0151  -0.0584 0.0455  211 PHE C CD2 
5942 C  CE1 . PHE C  211 ? 0.1530 0.2640 0.2597 0.0725  -0.0103 0.0118  211 PHE C CE1 
5943 C  CE2 . PHE C  211 ? 0.1960 0.2428 0.2636 0.0376  -0.0578 0.0370  211 PHE C CE2 
5944 C  CZ  . PHE C  211 ? 0.2107 0.2473 0.2788 0.0216  -0.0441 0.0414  211 PHE C CZ  
5945 N  N   . ARG C  212 ? 0.2093 0.1830 0.2085 0.0410  0.0136  0.0427  212 ARG C N   
5946 C  CA  . ARG C  212 ? 0.2424 0.1791 0.2005 0.0321  -0.0054 0.0275  212 ARG C CA  
5947 C  C   . ARG C  212 ? 0.2106 0.2133 0.2267 0.0465  0.0203  0.0580  212 ARG C C   
5948 O  O   . ARG C  212 ? 0.2101 0.2440 0.2253 0.0227  0.0207  0.0300  212 ARG C O   
5949 C  CB  . ARG C  212 ? 0.1930 0.1905 0.2253 0.0012  -0.0050 0.0114  212 ARG C CB  
5950 C  CG  . ARG C  212 ? 0.3044 0.1755 0.3109 -0.0176 -0.0205 -0.0422 212 ARG C CG  
5951 C  CD  . ARG C  212 ? 0.4125 0.2345 0.3088 -0.0424 0.0359  -0.0486 212 ARG C CD  
5952 N  NE  . ARG C  212 ? 0.5012 0.3066 0.3815 -0.1354 0.0201  -0.0898 212 ARG C NE  
5953 C  CZ  . ARG C  212 ? 0.5527 0.3841 0.3896 -0.0502 -0.0208 -0.0583 212 ARG C CZ  
5954 N  NH1 . ARG C  212 ? 0.8117 0.2824 0.7792 0.0785  0.1035  -0.0547 212 ARG C NH1 
5955 N  NH2 . ARG C  212 ? 0.5945 0.3394 0.3227 -0.1533 -0.0113 0.0064  212 ARG C NH2 
5956 N  N   . ASN C  213 ? 0.2399 0.2129 0.2135 0.0157  0.0145  0.0673  213 ASN C N   
5957 C  CA  . ASN C  213 ? 0.2576 0.2435 0.2455 0.0595  -0.0013 0.0671  213 ASN C CA  
5958 C  C   . ASN C  213 ? 0.2487 0.2027 0.2084 0.0099  -0.0053 0.0440  213 ASN C C   
5959 O  O   . ASN C  213 ? 0.2513 0.2675 0.2215 0.0446  0.0021  0.0658  213 ASN C O   
5960 C  CB  . ASN C  213 ? 0.2827 0.2033 0.3291 0.0539  0.0635  0.0533  213 ASN C CB  
5961 C  CG  . ASN C  213 ? 0.3825 0.1213 0.4315 0.0476  0.0523  0.0054  213 ASN C CG  
5962 O  OD1 . ASN C  213 ? 0.4077 0.3612 0.3371 -0.0313 0.0465  0.0184  213 ASN C OD1 
5963 N  ND2 . ASN C  213 ? 0.3788 0.3441 0.3782 0.0367  0.0493  0.0263  213 ASN C ND2 
5964 N  N   . PRO C  214 ? 0.2613 0.2155 0.2472 0.0168  0.0009  0.0488  214 PRO C N   
5965 C  CA  . PRO C  214 ? 0.2515 0.2660 0.1910 0.0394  0.0115  0.0696  214 PRO C CA  
5966 C  C   . PRO C  214 ? 0.2597 0.2190 0.2326 0.0318  -0.0199 0.0730  214 PRO C C   
5967 O  O   . PRO C  214 ? 0.3468 0.2913 0.2666 0.0853  0.0099  0.1118  214 PRO C O   
5968 C  CB  . PRO C  214 ? 0.2802 0.2395 0.2386 0.0380  0.0423  0.0834  214 PRO C CB  
5969 C  CG  . PRO C  214 ? 0.2576 0.2701 0.2515 -0.0234 -0.0010 0.0717  214 PRO C CG  
5970 C  CD  . PRO C  214 ? 0.2615 0.2565 0.2709 0.0086  -0.0201 0.0085  214 PRO C CD  
5971 N  N   . VAL C  215 ? 0.2727 0.2493 0.2203 0.0286  -0.0092 0.0702  215 VAL C N   
5972 C  CA  . VAL C  215 ? 0.3028 0.3072 0.1909 0.0271  -0.0077 0.0924  215 VAL C CA  
5973 C  C   . VAL C  215 ? 0.2818 0.2153 0.2800 0.0509  -0.0236 0.1127  215 VAL C C   
5974 O  O   . VAL C  215 ? 0.2693 0.2750 0.2388 0.0535  0.0044  0.0879  215 VAL C O   
5975 C  CB  . VAL C  215 ? 0.3234 0.2521 0.2050 0.0150  -0.0088 0.0700  215 VAL C CB  
5976 C  CG1 . VAL C  215 ? 0.3222 0.3154 0.1882 0.0107  -0.0046 0.0505  215 VAL C CG1 
5977 C  CG2 . VAL C  215 ? 0.2498 0.2523 0.2691 0.0534  -0.0164 0.0941  215 VAL C CG2 
5978 N  N   . GLN C  216 ? 0.2974 0.2964 0.2239 0.0445  0.0034  0.0978  216 GLN C N   
5979 C  CA  . GLN C  216 ? 0.3343 0.2177 0.2606 -0.0340 0.0477  0.0187  216 GLN C CA  
5980 C  C   . GLN C  216 ? 0.3973 0.3516 0.1836 0.0919  -0.0133 0.0647  216 GLN C C   
5981 O  O   . GLN C  216 ? 0.3454 0.3625 0.2890 0.0866  0.0332  0.1028  216 GLN C O   
5982 C  CB  . GLN C  216 ? 0.3098 0.2167 0.3877 -0.0249 -0.0010 0.0413  216 GLN C CB  
5983 C  CG  . GLN C  216 ? 0.4412 0.2354 0.3443 -0.0058 -0.0080 0.0687  216 GLN C CG  
5984 C  CD  . GLN C  216 ? 0.7233 0.2518 0.9275 -0.2759 -0.0548 0.0150  216 GLN C CD  
5985 O  OE1 . GLN C  216 ? 0.6335 0.7867 0.4606 -0.0335 -0.0217 -0.1957 216 GLN C OE1 
5986 N  NE2 . GLN C  216 ? 0.8494 0.3613 0.5230 -0.0141 -0.2459 -0.0307 216 GLN C NE2 
5987 N  N   . ILE C  217 ? 0.3234 0.2819 0.2611 0.0309  -0.0037 0.0917  217 ILE C N   
5988 C  CA  . ILE C  217 ? 0.3098 0.2988 0.1843 0.0106  -0.0348 0.1042  217 ILE C CA  
5989 C  C   . ILE C  217 ? 0.3818 0.2283 0.1870 0.0771  0.0093  0.0677  217 ILE C C   
5990 O  O   . ILE C  217 ? 0.3344 0.3934 0.2443 -0.0178 -0.0519 0.1296  217 ILE C O   
5991 C  CB  . ILE C  217 ? 0.2770 0.2653 0.2657 0.0451  0.0145  0.0979  217 ILE C CB  
5992 C  CG1 . ILE C  217 ? 0.2407 0.2291 0.2163 0.0357  -0.0130 0.0261  217 ILE C CG1 
5993 C  CG2 . ILE C  217 ? 0.2692 0.2885 0.2678 0.0034  -0.0054 0.1028  217 ILE C CG2 
5994 C  CD1 . ILE C  217 ? 0.3050 0.2111 0.2416 -0.0166 -0.0362 0.0347  217 ILE C CD1 
5995 N  N   . SER C  218 ? 0.3359 0.3847 0.1739 0.0413  -0.0035 0.1072  218 SER C N   
5996 C  CA  . SER C  218 ? 0.4530 0.3650 0.1803 0.0628  0.0303  0.1460  218 SER C CA  
5997 C  C   . SER C  218 ? 0.3700 0.2780 0.3457 -0.0161 0.0317  0.0894  218 SER C C   
5998 O  O   . SER C  218 ? 0.3462 0.3461 0.2563 -0.0312 -0.0308 0.0880  218 SER C O   
5999 C  CB  . SER C  218 ? 0.4307 0.3328 0.1898 0.0254  -0.0317 0.0908  218 SER C CB  
6000 O  OG  . SER C  218 ? 0.4452 0.4348 0.2454 0.0239  -0.1002 0.1277  218 SER C OG  
6001 N  N   . GLN C  219 ? 0.4005 0.5116 0.3071 0.0245  0.0135  0.2152  219 GLN C N   
6002 C  CA  . GLN C  219 ? 0.3679 0.5466 0.3845 -0.0186 0.0064  0.1687  219 GLN C CA  
6003 C  C   . GLN C  219 ? 0.4205 0.3770 0.3027 0.0055  0.0670  0.1812  219 GLN C C   
6004 O  O   . GLN C  219 ? 0.3361 0.4278 0.2425 -0.0013 -0.0002 0.1344  219 GLN C O   
6005 C  CB  . GLN C  219 ? 0.5879 0.4268 0.5414 -0.0064 0.2506  0.0982  219 GLN C CB  
6006 N  N   . GLU C  220 ? 0.4567 0.5028 0.2218 0.0710  0.0190  0.1052  220 GLU C N   
6007 C  CA  . GLU C  220 ? 0.4313 0.4497 0.3129 0.0467  -0.0386 0.1727  220 GLU C CA  
6008 C  C   . GLU C  220 ? 0.3033 0.2545 0.1929 0.0761  -0.0499 0.0455  220 GLU C C   
6009 O  O   . GLU C  220 ? 0.3570 0.3560 0.1787 0.0569  -0.0145 0.0724  220 GLU C O   
6010 C  CB  . GLU C  220 ? 0.4366 0.4617 0.3033 0.1291  -0.0117 0.1848  220 GLU C CB  
6011 C  CG  . GLU C  220 ? 0.5322 0.5051 0.4337 0.0420  0.0493  0.2015  220 GLU C CG  
6012 C  CD  . GLU C  220 ? 0.7419 0.6409 0.4295 0.0535  -0.0628 0.1001  220 GLU C CD  
6013 O  OE1 . GLU C  220 ? 0.8817 0.7577 0.2455 -0.0788 0.0451  0.1540  220 GLU C OE1 
6014 O  OE2 . GLU C  220 ? 0.9163 0.5363 0.6761 -0.0094 -0.0227 0.2132  220 GLU C OE2 
6015 N  N   . GLN C  221 ? 0.3109 0.5200 0.2557 0.0529  -0.0527 0.1351  221 GLN C N   
6016 C  CA  . GLN C  221 ? 0.3732 0.3942 0.2059 0.0421  -0.0298 0.0970  221 GLN C CA  
6017 C  C   . GLN C  221 ? 0.2674 0.2992 0.1590 0.0083  -0.0410 0.0622  221 GLN C C   
6018 O  O   . GLN C  221 ? 0.3193 0.3308 0.1981 0.0128  -0.0580 0.0296  221 GLN C O   
6019 C  CB  . GLN C  221 ? 0.3837 0.3446 0.1882 0.1082  -0.0651 0.0467  221 GLN C CB  
6020 C  CG  . GLN C  221 ? 0.2960 0.4258 0.2023 0.0401  -0.0211 0.0586  221 GLN C CG  
6021 C  CD  . GLN C  221 ? 0.3378 0.3274 0.1703 0.0493  -0.0586 0.0516  221 GLN C CD  
6022 O  OE1 . GLN C  221 ? 0.3485 0.3169 0.2086 0.0139  -0.0400 0.0653  221 GLN C OE1 
6023 N  NE2 . GLN C  221 ? 0.3124 0.3684 0.2646 0.0278  -0.0333 0.0934  221 GLN C NE2 
6024 N  N   . LEU C  222 ? 0.3121 0.4310 0.1672 0.0288  0.0053  0.1050  222 LEU C N   
6025 C  CA  . LEU C  222 ? 0.2768 0.3462 0.1895 -0.0013 -0.0789 0.0657  222 LEU C CA  
6026 C  C   . LEU C  222 ? 0.3053 0.2867 0.1819 0.0036  -0.0255 0.0726  222 LEU C C   
6027 O  O   . LEU C  222 ? 0.2976 0.3379 0.1451 0.0036  -0.0132 0.0554  222 LEU C O   
6028 C  CB  . LEU C  222 ? 0.3791 0.3258 0.1793 -0.0370 -0.0095 0.0660  222 LEU C CB  
6029 C  CG  . LEU C  222 ? 0.2684 0.3994 0.2115 -0.0018 0.0019  0.0855  222 LEU C CG  
6030 C  CD1 . LEU C  222 ? 0.2419 0.4385 0.1755 0.0151  -0.0273 0.1269  222 LEU C CD1 
6031 C  CD2 . LEU C  222 ? 0.3184 0.3886 0.2287 -0.0670 0.0650  0.1046  222 LEU C CD2 
6032 N  N   . LEU C  223 ? 0.2863 0.3269 0.1624 0.0225  -0.0462 0.0618  223 LEU C N   
6033 C  CA  . LEU C  223 ? 0.3911 0.4149 0.1558 -0.0487 0.0418  0.0543  223 LEU C CA  
6034 C  C   . LEU C  223 ? 0.3220 0.2870 0.1116 0.0394  -0.0124 0.0596  223 LEU C C   
6035 O  O   . LEU C  223 ? 0.3199 0.3582 0.1908 0.0100  -0.0395 0.0370  223 LEU C O   
6036 C  CB  . LEU C  223 ? 0.4827 0.5899 0.1964 0.0898  0.0721  0.1557  223 LEU C CB  
6037 C  CG  . LEU C  223 ? 0.5438 0.6777 0.1876 0.1824  0.0591  0.1481  223 LEU C CG  
6038 C  CD1 . LEU C  223 ? 0.4549 0.7161 0.2354 0.0866  0.1067  0.0873  223 LEU C CD1 
6039 C  CD2 . LEU C  223 ? 0.7081 0.6585 0.2037 -0.0939 -0.0049 0.1324  223 LEU C CD2 
6040 N  N   . ALA C  224 ? 0.3172 0.4014 0.1865 -0.0083 0.0293  0.1272  224 ALA C N   
6041 C  CA  . ALA C  224 ? 0.2879 0.5477 0.2909 -0.0522 0.0190  0.0920  224 ALA C CA  
6042 C  C   . ALA C  224 ? 0.2974 0.3838 0.1428 0.0247  -0.0472 0.0192  224 ALA C C   
6043 O  O   . ALA C  224 ? 0.3406 0.4763 0.2259 -0.0149 -0.0133 -0.0545 224 ALA C O   
6044 C  CB  . ALA C  224 ? 0.3634 0.5593 0.1803 0.0589  -0.0207 0.0245  224 ALA C CB  
6045 N  N   . LEU C  225 ? 0.3048 0.4579 0.1715 -0.0071 -0.0651 0.0097  225 LEU C N   
6046 C  CA  . LEU C  225 ? 0.3770 0.3974 0.1682 0.0208  -0.0573 0.0200  225 LEU C CA  
6047 C  C   . LEU C  225 ? 0.3077 0.3191 0.1393 -0.0060 -0.0479 -0.0383 225 LEU C C   
6048 O  O   . LEU C  225 ? 0.2821 0.3895 0.2394 -0.0385 -0.0144 -0.0416 225 LEU C O   
6049 C  CB  . LEU C  225 ? 0.3107 0.5198 0.1541 0.0252  -0.0278 0.0664  225 LEU C CB  
6050 C  CG  . LEU C  225 ? 0.2938 0.4100 0.1600 -0.0474 -0.0383 0.0236  225 LEU C CG  
6051 C  CD1 . LEU C  225 ? 0.2834 0.3971 0.2164 -0.0044 -0.0406 0.0819  225 LEU C CD1 
6052 C  CD2 . LEU C  225 ? 0.3018 0.3689 0.1692 0.0502  -0.0303 0.0375  225 LEU C CD2 
6053 N  N   . GLU C  226 ? 0.2849 0.4580 0.1235 -0.0127 -0.0294 0.0487  226 GLU C N   
6054 C  CA  . GLU C  226 ? 0.2506 0.3911 0.1584 -0.0119 -0.0344 0.0220  226 GLU C CA  
6055 C  C   . GLU C  226 ? 0.3768 0.3424 0.1538 0.0220  -0.0207 0.0535  226 GLU C C   
6056 O  O   . GLU C  226 ? 0.3868 0.4230 0.1839 0.0057  -0.0616 -0.0149 226 GLU C O   
6057 C  CB  . GLU C  226 ? 0.2427 0.4992 0.1537 -0.0563 -0.0229 0.0074  226 GLU C CB  
6058 C  CG  . GLU C  226 ? 0.2528 0.3851 0.1143 -0.0210 -0.0179 0.0538  226 GLU C CG  
6059 C  CD  . GLU C  226 ? 0.2999 0.2865 0.1433 -0.0030 -0.0270 0.0632  226 GLU C CD  
6060 O  OE1 . GLU C  226 ? 0.3305 0.4091 0.1450 -0.0450 0.0110  0.0685  226 GLU C OE1 
6061 O  OE2 . GLU C  226 ? 0.2825 0.4256 0.1444 -0.0330 -0.0125 0.0583  226 GLU C OE2 
6062 N  N   . THR C  227 ? 0.2762 0.5829 0.1331 -0.0787 -0.0418 -0.0425 227 THR C N   
6063 C  CA  . THR C  227 ? 0.3468 0.4870 0.1238 -0.1042 -0.0148 -0.0102 227 THR C CA  
6064 C  C   . THR C  227 ? 0.2752 0.4106 0.1936 0.0057  -0.0624 -0.0602 227 THR C C   
6065 O  O   . THR C  227 ? 0.3894 0.5723 0.1812 -0.0559 -0.0546 -0.0586 227 THR C O   
6066 C  CB  . THR C  227 ? 0.4200 0.4404 0.2606 -0.1250 -0.0063 -0.0293 227 THR C CB  
6067 O  OG1 . THR C  227 ? 0.4552 0.4663 0.1796 -0.1208 0.0128  0.0419  227 THR C OG1 
6068 C  CG2 . THR C  227 ? 0.3750 0.4170 0.2201 -0.1008 0.0574  -0.0514 227 THR C CG2 
6069 N  N   . ALA C  228 ? 0.3114 0.5256 0.1716 -0.0441 -0.0579 0.0063  228 ALA C N   
6070 C  CA  . ALA C  228 ? 0.3504 0.4054 0.1895 -0.0236 -0.1009 0.0063  228 ALA C CA  
6071 C  C   . ALA C  228 ? 0.4124 0.4120 0.1967 0.0546  -0.1355 -0.0691 228 ALA C C   
6072 O  O   . ALA C  228 ? 0.3385 0.4858 0.1723 -0.0173 -0.0798 -0.0100 228 ALA C O   
6073 C  CB  . ALA C  228 ? 0.2757 0.5110 0.4564 -0.0208 -0.1463 0.0032  228 ALA C CB  
6074 N  N   . LEU C  229 ? 0.2768 0.3871 0.1805 -0.0030 -0.0888 0.0107  229 LEU C N   
6075 C  CA  . LEU C  229 ? 0.2813 0.3823 0.1690 -0.0143 -0.0186 0.0088  229 LEU C CA  
6076 C  C   . LEU C  229 ? 0.3053 0.2762 0.2278 -0.0489 -0.0339 -0.0196 229 LEU C C   
6077 O  O   . LEU C  229 ? 0.2829 0.3159 0.2262 -0.0409 -0.0587 -0.0313 229 LEU C O   
6078 C  CB  . LEU C  229 ? 0.2752 0.4038 0.2049 0.0632  -0.0134 -0.0110 229 LEU C CB  
6079 C  CG  . LEU C  229 ? 0.3186 0.3255 0.1512 0.0148  -0.0446 -0.0255 229 LEU C CG  
6080 C  CD1 . LEU C  229 ? 0.2902 0.7530 0.1809 0.0364  -0.0458 0.0761  229 LEU C CD1 
6081 C  CD2 . LEU C  229 ? 0.2243 0.3971 0.2487 -0.0069 -0.0463 -0.0712 229 LEU C CD2 
6082 N  N   . TYR C  230 ? 0.2453 0.2803 0.4056 -0.0575 -0.0609 -0.0140 230 TYR C N   
6083 C  CA  . TYR C  230 ? 0.3045 0.4004 0.3092 0.0370  -0.0673 -0.0151 230 TYR C CA  
6084 C  C   . TYR C  230 ? 0.3379 0.2773 0.3385 0.0190  -0.0334 -0.0052 230 TYR C C   
6085 O  O   . TYR C  230 ? 0.3661 0.6183 0.2216 -0.0744 -0.0727 -0.0916 230 TYR C O   
6086 C  CB  . TYR C  230 ? 0.3626 0.4092 0.2484 -0.0571 -0.0670 -0.0126 230 TYR C CB  
6087 C  CG  . TYR C  230 ? 0.5238 0.6050 0.4210 -0.0688 -0.1035 0.2081  230 TYR C CG  
6088 C  CD1 . TYR C  230 ? 0.7869 0.4041 0.6071 0.0033  0.1109  0.2421  230 TYR C CD1 
6089 C  CD2 . TYR C  230 ? 0.6700 0.2513 0.3536 -0.0778 0.0872  -0.0092 230 TYR C CD2 
6090 C  CE1 . TYR C  230 ? 0.8979 1.1250 0.6633 0.0911  0.1672  0.5903  230 TYR C CE1 
6091 C  CE2 . TYR C  230 ? 0.7555 0.4564 0.6445 -0.2829 -0.0184 0.2359  230 TYR C CE2 
6092 C  CZ  . TYR C  230 ? 0.6286 0.7259 0.8702 -0.1888 0.0588  0.3805  230 TYR C CZ  
6093 O  OH  . TYR C  230 ? 1.2243 1.1910 0.8440 -0.1509 0.0478  0.6779  230 TYR C OH  
6094 N  N   . CYS C  231 ? 0.3273 0.2566 0.2960 -0.0282 -0.0318 -0.0561 231 CYS C N   
6095 C  CA  . CYS C  231 ? 0.3682 0.4199 0.2543 -0.0822 -0.0653 -0.0693 231 CYS C CA  
6096 C  C   . CYS C  231 ? 0.6010 0.3962 0.1947 -0.1958 -0.1295 -0.0333 231 CYS C C   
6097 O  O   . CYS C  231 ? 0.4742 0.4030 0.2222 -0.0532 -0.0391 -0.0312 231 CYS C O   
6098 C  CB  . CYS C  231 ? 0.3895 0.5715 0.2101 -0.1819 -0.0549 -0.1001 231 CYS C CB  
6099 S  SG  . CYS C  231 ? 0.4080 0.6520 0.4103 -0.0611 -0.1439 -0.0199 231 CYS C SG  
6100 N  N   . THR C  232 ? 0.3709 0.3359 0.2267 -0.0346 -0.0243 -0.0553 232 THR C N   
6101 C  CA  . THR C  232 ? 0.4166 0.3721 0.2077 -0.1157 0.0352  -0.0758 232 THR C CA  
6102 C  C   . THR C  232 ? 0.3652 0.3564 0.3204 -0.0622 0.0079  -0.0012 232 THR C C   
6103 O  O   . THR C  232 ? 0.3163 0.3477 0.1892 -0.0424 -0.0094 -0.0089 232 THR C O   
6104 C  CB  . THR C  232 ? 0.3274 0.3880 0.3128 -0.0499 0.0675  0.0397  232 THR C CB  
6105 O  OG1 . THR C  232 ? 0.4222 0.2981 0.2799 -0.1081 0.0098  -0.0794 232 THR C OG1 
6106 C  CG2 . THR C  232 ? 0.3269 0.4016 0.3856 -0.0086 -0.0715 -0.0721 232 THR C CG2 
6107 N  N   . HIS C  233 ? 0.4495 0.4068 0.2927 -0.1408 0.0378  -0.1057 233 HIS C N   
6108 C  CA  . HIS C  233 ? 0.4395 0.3017 0.2879 -0.1533 0.0276  -0.0672 233 HIS C CA  
6109 C  C   . HIS C  233 ? 0.4204 0.3098 0.3001 0.0048  0.0181  -0.0770 233 HIS C C   
6110 O  O   . HIS C  233 ? 0.4118 0.4111 0.3082 -0.0330 0.0117  -0.1516 233 HIS C O   
6111 C  CB  . HIS C  233 ? 0.4714 0.3443 0.3010 -0.1550 -0.0461 -0.0122 233 HIS C CB  
6112 C  CG  . HIS C  233 ? 0.7608 0.3782 0.4862 -0.1111 0.0907  0.1543  233 HIS C CG  
6113 N  ND1 . HIS C  233 ? 1.0272 0.7839 0.4468 -0.1036 0.0037  0.2505  233 HIS C ND1 
6114 C  CD2 . HIS C  233 ? 0.6932 0.4310 0.5380 -0.1729 -0.0680 -0.1586 233 HIS C CD2 
6115 C  CE1 . HIS C  233 ? 0.8851 0.4234 0.4279 -0.3298 -0.0255 -0.0377 233 HIS C CE1 
6116 N  NE2 . HIS C  233 ? 0.8307 0.9448 0.6973 -0.3761 0.0359  0.0079  233 HIS C NE2 
6117 N  N   . MET C  234 ? 0.3806 0.5776 0.2550 -0.1311 -0.0089 -0.0239 234 MET C N   
6118 C  CA  . MET C  234 ? 0.5088 0.6005 0.2551 -0.0866 0.0663  -0.0217 234 MET C CA  
6119 C  C   . MET C  234 ? 0.5520 0.6957 0.3019 -0.1050 0.0936  -0.0147 234 MET C C   
6120 O  O   . MET C  234 ? 0.6027 1.1949 0.3069 -0.3804 0.1234  -0.0368 234 MET C O   
6121 C  CB  . MET C  234 ? 0.5141 0.7417 0.2468 -0.2682 -0.0064 -0.0795 234 MET C CB  
6122 C  CG  . MET C  234 ? 0.7138 0.9649 0.4652 -0.1692 0.0116  0.1709  234 MET C CG  
6123 S  SD  . MET C  234 ? 0.7512 1.0946 0.4087 -0.0122 0.1151  -0.1414 234 MET C SD  
6124 C  CE  . MET C  234 ? 0.4380 0.7559 0.3026 -0.0680 -0.1580 -0.0075 234 MET C CE  
6125 N  N   . ASP C  235 ? 0.7118 0.6704 0.2734 -0.1555 -0.0127 -0.2714 235 ASP C N   
6126 C  CA  . ASP C  235 ? 0.7262 0.7498 0.4794 0.0430  0.0937  -0.1386 235 ASP C CA  
6127 C  C   . ASP C  235 ? 0.7241 0.6642 0.6700 -0.1294 -0.0719 -0.3197 235 ASP C C   
6128 O  O   . ASP C  235 ? 2.4176 1.0556 1.4723 -0.8574 1.1387  -1.1174 235 ASP C O   
6129 N  N   . ASP C  236 ? 0.4555 0.4687 0.4098 -0.1222 0.0546  -0.0883 236 ASP C N   
6130 C  CA  . ASP C  236 ? 0.4529 0.4495 0.4595 -0.1143 0.0351  -0.2211 236 ASP C CA  
6131 C  C   . ASP C  236 ? 0.5996 0.5795 0.5768 0.0477  0.1629  0.0138  236 ASP C C   
6132 O  O   . ASP C  236 ? 0.6775 0.5974 0.3149 -0.1226 -0.0143 0.0438  236 ASP C O   
6133 C  CB  . ASP C  236 ? 0.5666 0.5252 0.3267 -0.0904 0.0418  -0.1111 236 ASP C CB  
6134 C  CG  . ASP C  236 ? 0.6036 0.5958 0.4580 -0.0047 -0.0687 -0.1998 236 ASP C CG  
6135 O  OD1 . ASP C  236 ? 0.7988 0.6488 0.6510 -0.0168 0.0284  -0.2497 236 ASP C OD1 
6136 O  OD2 . ASP C  236 ? 0.6038 0.5950 0.4256 -0.0050 0.0203  -0.0657 236 ASP C OD2 
6137 N  N   . PRO C  237 ? 0.4756 0.5991 0.5758 -0.0190 0.0592  -0.1198 237 PRO C N   
6138 C  CA  . PRO C  237 ? 0.5090 0.5025 0.5008 -0.0885 0.0624  -0.1256 237 PRO C CA  
6139 C  C   . PRO C  237 ? 0.6244 0.3865 0.4363 -0.1133 0.1287  -0.0950 237 PRO C C   
6140 O  O   . PRO C  237 ? 0.5888 0.3554 0.4334 0.0126  0.1377  0.0173  237 PRO C O   
6141 C  CB  . PRO C  237 ? 0.7572 0.5051 0.3494 -0.0164 0.0337  -0.1030 237 PRO C CB  
6142 C  CG  . PRO C  237 ? 0.5951 0.3155 0.5484 0.0584  0.1315  -0.0722 237 PRO C CG  
6143 C  CD  . PRO C  237 ? 0.5600 0.5756 0.5271 0.2585  0.0419  0.0554  237 PRO C CD  
6144 N  N   . SER C  238 ? 0.5339 0.4064 0.4066 -0.1234 0.0691  -0.0888 238 SER C N   
6145 C  CA  . SER C  238 ? 0.4594 0.5200 0.3813 -0.0766 -0.0240 -0.0743 238 SER C CA  
6146 C  C   . SER C  238 ? 0.4665 0.5917 0.4411 -0.0143 0.1393  0.0511  238 SER C C   
6147 O  O   . SER C  238 ? 0.5766 0.4449 0.4117 -0.1923 0.0339  0.0430  238 SER C O   
6148 C  CB  . SER C  238 ? 0.5710 0.7121 0.3537 0.0158  -0.0710 -0.0930 238 SER C CB  
6149 O  OG  . SER C  238 ? 0.8893 0.6632 0.5996 -0.0321 0.0017  -0.2658 238 SER C OG  
6150 N  N   . PRO C  239 ? 0.4460 0.4459 0.2763 -0.1522 0.0588  -0.0463 239 PRO C N   
6151 C  CA  . PRO C  239 ? 0.3607 0.4726 0.2251 -0.0958 0.0780  -0.0084 239 PRO C CA  
6152 C  C   . PRO C  239 ? 0.4314 0.4589 0.3856 -0.2037 0.1088  -0.0908 239 PRO C C   
6153 O  O   . PRO C  239 ? 0.4026 0.6796 0.3559 -0.2068 0.0587  -0.0956 239 PRO C O   
6154 C  CB  . PRO C  239 ? 0.5926 0.4646 0.2273 -0.0916 0.0750  0.0996  239 PRO C CB  
6155 C  CG  . PRO C  239 ? 0.4530 0.3974 0.3520 -0.0038 0.1282  0.0058  239 PRO C CG  
6156 C  CD  . PRO C  239 ? 0.4719 0.4055 0.2840 0.0070  0.0624  -0.0033 239 PRO C CD  
6157 N  N   . ARG C  240 ? 0.3806 0.4268 0.3367 -0.1181 0.0201  -0.1072 240 ARG C N   
6158 C  CA  . ARG C  240 ? 0.3635 0.4010 0.2996 -0.0948 -0.0792 -0.0520 240 ARG C CA  
6159 C  C   . ARG C  240 ? 0.3646 0.4574 0.2284 -0.0952 -0.0662 -0.0392 240 ARG C C   
6160 O  O   . ARG C  240 ? 0.3430 0.5553 0.3943 -0.1305 0.0019  -0.1116 240 ARG C O   
6161 C  CB  . ARG C  240 ? 0.3122 0.4602 0.3231 0.0109  -0.0908 -0.0403 240 ARG C CB  
6162 C  CG  . ARG C  240 ? 0.4543 0.4584 0.2556 -0.0519 -0.0559 0.0346  240 ARG C CG  
6163 C  CD  . ARG C  240 ? 0.7424 0.5998 0.4649 -0.1570 -0.3690 0.1108  240 ARG C CD  
6164 N  N   . GLU C  241 ? 0.4166 0.3963 0.1964 -0.1101 0.0325  -0.0420 241 GLU C N   
6165 C  CA  . GLU C  241 ? 0.3458 0.3937 0.2182 -0.0469 0.0643  -0.0383 241 GLU C CA  
6166 C  C   . GLU C  241 ? 0.2772 0.4289 0.2104 -0.0851 -0.0089 -0.0408 241 GLU C C   
6167 O  O   . GLU C  241 ? 0.2833 0.4902 0.2882 -0.0225 -0.0595 -0.0901 241 GLU C O   
6168 C  CB  . GLU C  241 ? 0.4446 0.4581 0.2689 -0.1659 0.1307  -0.0994 241 GLU C CB  
6169 C  CG  . GLU C  241 ? 0.5734 0.4405 0.3296 -0.0027 0.1241  0.0406  241 GLU C CG  
6170 C  CD  . GLU C  241 ? 0.7705 0.8857 0.7088 -0.3000 0.1362  0.0649  241 GLU C CD  
6171 O  OE1 . GLU C  241 ? 0.7923 1.0746 0.4406 -0.2117 0.3376  -0.0162 241 GLU C OE1 
6172 O  OE2 . GLU C  241 ? 0.9215 1.0233 0.9224 -0.3527 0.4262  0.0678  241 GLU C OE2 
6173 N  N   . MET C  242 ? 0.2967 0.4175 0.1861 -0.0472 -0.0239 -0.0631 242 MET C N   
6174 C  CA  . MET C  242 ? 0.2455 0.3630 0.1749 -0.0721 -0.0211 -0.0299 242 MET C CA  
6175 C  C   . MET C  242 ? 0.2683 0.3115 0.1574 -0.0313 -0.0353 -0.0105 242 MET C C   
6176 O  O   . MET C  242 ? 0.2630 0.3440 0.1620 -0.0324 -0.0204 -0.0116 242 MET C O   
6177 C  CB  . MET C  242 ? 0.2264 0.3388 0.1722 -0.0451 -0.0354 -0.0187 242 MET C CB  
6178 C  CG  . MET C  242 ? 0.2740 0.3476 0.1543 -0.0662 -0.0465 -0.0201 242 MET C CG  
6179 S  SD  . MET C  242 ? 0.3129 0.3906 0.1687 -0.0407 -0.0331 -0.0341 242 MET C SD  
6180 C  CE  . MET C  242 ? 0.3677 0.4007 0.1814 -0.0735 -0.0665 -0.0547 242 MET C CE  
6181 N  N   . ILE C  243 ? 0.2356 0.3287 0.1338 0.0019  -0.0221 -0.0303 243 ILE C N   
6182 C  CA  . ILE C  243 ? 0.2235 0.3511 0.1181 -0.0510 -0.0272 -0.0167 243 ILE C CA  
6183 C  C   . ILE C  243 ? 0.1995 0.2557 0.1298 -0.0060 0.0030  -0.0044 243 ILE C C   
6184 O  O   . ILE C  243 ? 0.2159 0.2812 0.1411 -0.0105 -0.0167 -0.0156 243 ILE C O   
6185 C  CB  . ILE C  243 ? 0.2350 0.3822 0.1243 -0.0312 -0.0142 0.0008  243 ILE C CB  
6186 C  CG1 . ILE C  243 ? 0.3064 0.3938 0.1547 -0.0190 0.0236  -0.0126 243 ILE C CG1 
6187 C  CG2 . ILE C  243 ? 0.3364 0.4252 0.1453 -0.0886 -0.0504 0.0128  243 ILE C CG2 
6188 C  CD1 . ILE C  243 ? 0.3644 0.3653 0.2030 -0.0091 0.1016  0.0048  243 ILE C CD1 
6189 N  N   . ASN C  244 ? 0.1876 0.2722 0.1459 -0.0339 0.0000  -0.0145 244 ASN C N   
6190 C  CA  . ASN C  244 ? 0.1855 0.2822 0.1398 -0.0293 -0.0412 0.0179  244 ASN C CA  
6191 C  C   . ASN C  244 ? 0.1793 0.2441 0.1318 0.0121  -0.0214 -0.0038 244 ASN C C   
6192 O  O   . ASN C  244 ? 0.2040 0.2486 0.1515 -0.0097 -0.0135 -0.0033 244 ASN C O   
6193 C  CB  . ASN C  244 ? 0.1879 0.2715 0.1697 -0.0358 -0.0050 0.0049  244 ASN C CB  
6194 C  CG  . ASN C  244 ? 0.2142 0.2978 0.1835 -0.0179 -0.0296 -0.0047 244 ASN C CG  
6195 O  OD1 . ASN C  244 ? 0.2383 0.3026 0.2170 -0.0307 0.0186  0.0324  244 ASN C OD1 
6196 N  ND2 . ASN C  244 ? 0.2375 0.5098 0.2025 -0.0238 0.0556  -0.0075 244 ASN C ND2 
6197 N  N   . ASN C  245 ? 0.1822 0.2893 0.1230 -0.0212 -0.0163 -0.0245 245 ASN C N   
6198 C  CA  . ASN C  245 ? 0.1663 0.2664 0.1276 -0.0334 -0.0079 -0.0210 245 ASN C CA  
6199 C  C   . ASN C  245 ? 0.1683 0.2358 0.1267 -0.0162 -0.0062 -0.0193 245 ASN C C   
6200 O  O   . ASN C  245 ? 0.1635 0.2969 0.1561 -0.0370 -0.0059 -0.0221 245 ASN C O   
6201 C  CB  . ASN C  245 ? 0.1655 0.2568 0.1712 -0.0250 -0.0387 0.0066  245 ASN C CB  
6202 C  CG  . ASN C  245 ? 0.2280 0.2749 0.1193 -0.0206 -0.0160 -0.0046 245 ASN C CG  
6203 O  OD1 . ASN C  245 ? 0.2168 0.2523 0.1592 -0.0212 -0.0390 -0.0054 245 ASN C OD1 
6204 N  ND2 . ASN C  245 ? 0.2085 0.3353 0.2039 -0.0447 -0.0732 0.0059  245 ASN C ND2 
6205 N  N   . PHE C  246 ? 0.1729 0.2324 0.1041 -0.0175 -0.0250 0.0033  246 PHE C N   
6206 C  CA  . PHE C  246 ? 0.1952 0.2276 0.1064 0.0083  -0.0107 0.0035  246 PHE C CA  
6207 C  C   . PHE C  246 ? 0.1732 0.1971 0.1278 0.0031  -0.0247 -0.0276 246 PHE C C   
6208 O  O   . PHE C  246 ? 0.1782 0.1990 0.1111 0.0040  -0.0133 -0.0050 246 PHE C O   
6209 C  CB  . PHE C  246 ? 0.1731 0.2036 0.1278 0.0308  -0.0148 0.0044  246 PHE C CB  
6210 C  CG  . PHE C  246 ? 0.1725 0.1851 0.1401 0.0022  -0.0219 0.0119  246 PHE C CG  
6211 C  CD1 . PHE C  246 ? 0.2075 0.2066 0.1552 -0.0211 -0.0197 0.0487  246 PHE C CD1 
6212 C  CD2 . PHE C  246 ? 0.1725 0.1958 0.1796 -0.0027 -0.0367 0.0151  246 PHE C CD2 
6213 C  CE1 . PHE C  246 ? 0.2249 0.2137 0.1266 -0.0205 -0.0178 0.0165  246 PHE C CE1 
6214 C  CE2 . PHE C  246 ? 0.1855 0.2165 0.1590 -0.0339 -0.0356 0.0155  246 PHE C CE2 
6215 C  CZ  . PHE C  246 ? 0.1902 0.2427 0.1654 -0.0434 -0.0301 0.0127  246 PHE C CZ  
6216 N  N   . ARG C  247 ? 0.1583 0.1751 0.1040 -0.0171 -0.0308 0.0010  247 ARG C N   
6217 C  CA  . ARG C  247 ? 0.1449 0.1767 0.1093 -0.0113 -0.0146 0.0122  247 ARG C CA  
6218 C  C   . ARG C  247 ? 0.1641 0.1641 0.1003 -0.0010 -0.0035 -0.0027 247 ARG C C   
6219 O  O   . ARG C  247 ? 0.1534 0.1634 0.1263 -0.0041 -0.0131 0.0100  247 ARG C O   
6220 C  CB  . ARG C  247 ? 0.1423 0.1748 0.1179 -0.0176 -0.0099 0.0000  247 ARG C CB  
6221 C  CG  . ARG C  247 ? 0.1556 0.1742 0.1116 -0.0115 -0.0252 0.0041  247 ARG C CG  
6222 C  CD  . ARG C  247 ? 0.1654 0.1408 0.1130 -0.0043 0.0005  -0.0009 247 ARG C CD  
6223 N  NE  . ARG C  247 ? 0.1557 0.1452 0.1269 -0.0168 -0.0225 -0.0060 247 ARG C NE  
6224 C  CZ  . ARG C  247 ? 0.1485 0.1311 0.1218 -0.0148 -0.0116 -0.0114 247 ARG C CZ  
6225 N  NH1 . ARG C  247 ? 0.1518 0.1622 0.1382 -0.0155 -0.0070 -0.0299 247 ARG C NH1 
6226 N  NH2 . ARG C  247 ? 0.1824 0.1225 0.1450 -0.0120 -0.0144 -0.0017 247 ARG C NH2 
6227 N  N   . GLN C  248 ? 0.1512 0.1685 0.1041 -0.0097 -0.0192 -0.0061 248 GLN C N   
6228 C  CA  . GLN C  248 ? 0.1226 0.1795 0.1195 -0.0108 -0.0078 -0.0070 248 GLN C CA  
6229 C  C   . GLN C  248 ? 0.1430 0.1470 0.1102 -0.0049 -0.0208 0.0031  248 GLN C C   
6230 O  O   . GLN C  248 ? 0.1535 0.1500 0.1134 -0.0131 -0.0141 0.0054  248 GLN C O   
6231 C  CB  . GLN C  248 ? 0.1534 0.1522 0.1129 0.0102  0.0035  -0.0012 248 GLN C CB  
6232 C  CG  . GLN C  248 ? 0.1797 0.1464 0.1102 0.0006  -0.0009 0.0083  248 GLN C CG  
6233 C  CD  . GLN C  248 ? 0.1429 0.1670 0.1359 -0.0002 -0.0205 -0.0026 248 GLN C CD  
6234 O  OE1 . GLN C  248 ? 0.2096 0.2172 0.1698 -0.0320 -0.0530 0.0379  248 GLN C OE1 
6235 N  NE2 . GLN C  248 ? 0.1857 0.2156 0.1445 -0.0253 -0.0306 0.0158  248 GLN C NE2 
6236 N  N   . VAL C  249 ? 0.1488 0.1274 0.1202 0.0053  -0.0108 0.0013  249 VAL C N   
6237 C  CA  . VAL C  249 ? 0.1599 0.1380 0.1085 0.0065  -0.0297 -0.0069 249 VAL C CA  
6238 C  C   . VAL C  249 ? 0.1421 0.1344 0.1271 0.0060  -0.0199 -0.0244 249 VAL C C   
6239 O  O   . VAL C  249 ? 0.1393 0.1517 0.1321 0.0124  -0.0113 -0.0041 249 VAL C O   
6240 C  CB  . VAL C  249 ? 0.1887 0.1315 0.1496 0.0029  -0.0276 0.0114  249 VAL C CB  
6241 C  CG1 . VAL C  249 ? 0.2143 0.1378 0.1509 0.0207  -0.0425 0.0145  249 VAL C CG1 
6242 C  CG2 . VAL C  249 ? 0.1976 0.1365 0.2028 -0.0115 -0.0245 0.0093  249 VAL C CG2 
6243 N  N   . GLN C  250 ? 0.1404 0.1233 0.1197 -0.0024 -0.0179 -0.0027 250 GLN C N   
6244 C  CA  . GLN C  250 ? 0.1472 0.1249 0.1143 0.0091  -0.0173 0.0072  250 GLN C CA  
6245 C  C   . GLN C  250 ? 0.1495 0.1458 0.1235 0.0177  -0.0111 -0.0061 250 GLN C C   
6246 O  O   . GLN C  250 ? 0.1877 0.1441 0.1480 0.0074  -0.0274 -0.0110 250 GLN C O   
6247 C  CB  . GLN C  250 ? 0.1222 0.1651 0.1324 -0.0062 -0.0212 -0.0041 250 GLN C CB  
6248 C  CG  . GLN C  250 ? 0.1515 0.1292 0.1324 -0.0017 -0.0193 -0.0114 250 GLN C CG  
6249 C  CD  . GLN C  250 ? 0.1329 0.1246 0.1339 -0.0083 -0.0113 -0.0044 250 GLN C CD  
6250 O  OE1 . GLN C  250 ? 0.1656 0.1363 0.1453 0.0055  -0.0023 0.0084  250 GLN C OE1 
6251 N  NE2 . GLN C  250 ? 0.1527 0.1580 0.1219 -0.0161 -0.0122 -0.0081 250 GLN C NE2 
6252 N  N   . LYS C  251 ? 0.1482 0.1618 0.1129 0.0044  -0.0144 0.0054  251 LYS C N   
6253 C  CA  . LYS C  251 ? 0.1309 0.1778 0.1107 0.0000  -0.0168 -0.0111 251 LYS C CA  
6254 C  C   . LYS C  251 ? 0.1204 0.1672 0.1380 0.0008  -0.0226 -0.0085 251 LYS C C   
6255 O  O   . LYS C  251 ? 0.1346 0.1715 0.1484 0.0004  -0.0066 -0.0124 251 LYS C O   
6256 C  CB  . LYS C  251 ? 0.1358 0.2284 0.1328 0.0370  -0.0126 -0.0009 251 LYS C CB  
6257 C  CG  . LYS C  251 ? 0.1613 0.2396 0.1292 0.0444  0.0138  -0.0189 251 LYS C CG  
6258 C  CD  . LYS C  251 ? 0.1643 0.2382 0.1459 0.0242  0.0071  0.0148  251 LYS C CD  
6259 C  CE  . LYS C  251 ? 0.1378 0.2141 0.1175 0.0166  0.0059  0.0044  251 LYS C CE  
6260 N  NZ  . LYS C  251 ? 0.1496 0.1403 0.1263 -0.0003 -0.0055 -0.0068 251 LYS C NZ  
6261 N  N   A PHE C  252 ? 0.1424 0.1696 0.1660 0.0003  -0.0155 -0.0290 252 PHE C N   
6262 N  N   B PHE C  252 ? 0.1579 0.1772 0.1532 0.0057  -0.0140 -0.0282 252 PHE C N   
6263 C  CA  A PHE C  252 ? 0.1690 0.2222 0.1234 0.0344  -0.0077 -0.0165 252 PHE C CA  
6264 C  CA  B PHE C  252 ? 0.1572 0.2171 0.1134 0.0190  -0.0098 -0.0025 252 PHE C CA  
6265 C  C   A PHE C  252 ? 0.1437 0.1626 0.1555 0.0293  0.0001  -0.0150 252 PHE C C   
6266 C  C   B PHE C  252 ? 0.2086 0.1993 0.1849 0.0120  -0.0439 -0.0109 252 PHE C C   
6267 O  O   A PHE C  252 ? 0.2391 0.1745 0.1759 0.0088  -0.0168 -0.0012 252 PHE C O   
6268 O  O   B PHE C  252 ? 0.2082 0.2139 0.2154 -0.0080 -0.0373 -0.0454 252 PHE C O   
6269 C  CB  A PHE C  252 ? 0.1614 0.1860 0.1330 0.0135  -0.0282 -0.0364 252 PHE C CB  
6270 C  CB  B PHE C  252 ? 0.1625 0.1857 0.1504 0.0077  0.0111  0.0333  252 PHE C CB  
6271 C  CG  A PHE C  252 ? 0.1618 0.1469 0.1238 0.0170  -0.0210 -0.0024 252 PHE C CG  
6272 C  CG  B PHE C  252 ? 0.1646 0.1668 0.1175 0.0063  -0.0083 0.0006  252 PHE C CG  
6273 C  CD1 A PHE C  252 ? 0.1728 0.1949 0.1336 -0.0244 0.0154  -0.0055 252 PHE C CD1 
6274 C  CD1 B PHE C  252 ? 0.1655 0.1707 0.1098 0.0054  -0.0373 0.0542  252 PHE C CD1 
6275 C  CD2 A PHE C  252 ? 0.1730 0.1696 0.1432 0.0212  -0.0263 -0.0010 252 PHE C CD2 
6276 C  CD2 B PHE C  252 ? 0.1648 0.1852 0.1896 -0.0029 0.0126  0.0002  252 PHE C CD2 
6277 C  CE1 A PHE C  252 ? 0.1629 0.1406 0.1577 -0.0030 -0.0210 -0.0209 252 PHE C CE1 
6278 C  CE1 B PHE C  252 ? 0.1841 0.1671 0.1217 0.0126  -0.0147 0.0435  252 PHE C CE1 
6279 C  CE2 A PHE C  252 ? 0.1615 0.2067 0.1630 0.0189  -0.0343 -0.0254 252 PHE C CE2 
6280 C  CE2 B PHE C  252 ? 0.1776 0.1738 0.1729 0.0131  0.0162  0.0084  252 PHE C CE2 
6281 C  CZ  A PHE C  252 ? 0.1658 0.1421 0.1465 -0.0038 -0.0157 0.0075  252 PHE C CZ  
6282 C  CZ  B PHE C  252 ? 0.1773 0.1715 0.1549 -0.0043 0.0023  0.0443  252 PHE C CZ  
6283 N  N   A ASP C  253 ? 0.1718 0.2268 0.1386 0.0001  0.0013  -0.0121 253 ASP C N   
6284 N  N   B ASP C  253 ? 0.2550 0.2627 0.1584 0.0140  -0.0639 -0.0166 253 ASP C N   
6285 C  CA  A ASP C  253 ? 0.2063 0.2256 0.1470 0.0137  -0.0182 -0.0086 253 ASP C CA  
6286 C  CA  B ASP C  253 ? 0.2303 0.2888 0.1741 0.0175  -0.0613 0.0084  253 ASP C CA  
6287 C  C   A ASP C  253 ? 0.1566 0.2134 0.1897 0.0148  0.0129  -0.0018 253 ASP C C   
6288 C  C   B ASP C  253 ? 0.2193 0.2428 0.1812 0.0323  -0.0550 -0.0076 253 ASP C C   
6289 O  O   A ASP C  253 ? 0.1839 0.2288 0.1606 0.0100  -0.0111 0.0033  253 ASP C O   
6290 O  O   B ASP C  253 ? 0.2920 0.2689 0.1965 -0.0002 -0.0096 -0.0080 253 ASP C O   
6291 C  CB  A ASP C  253 ? 0.2086 0.3092 0.2175 0.0600  0.0253  0.0111  253 ASP C CB  
6292 C  CB  B ASP C  253 ? 0.3077 0.3008 0.1948 0.0974  -0.0337 -0.0333 253 ASP C CB  
6293 C  CG  A ASP C  253 ? 0.2107 0.2956 0.2367 0.0705  0.0538  0.0227  253 ASP C CG  
6294 C  CG  B ASP C  253 ? 0.3634 0.4257 0.3928 0.0134  -0.0510 -0.0600 253 ASP C CG  
6295 O  OD1 A ASP C  253 ? 0.3082 0.3646 0.3324 -0.0255 0.0428  0.0242  253 ASP C OD1 
6296 O  OD1 B ASP C  253 ? 0.2799 0.3968 0.3517 0.0383  -0.1372 -0.0606 253 ASP C OD1 
6297 O  OD2 A ASP C  253 ? 0.3581 0.4813 0.2413 0.1997  0.0308  -0.0766 253 ASP C OD2 
6298 O  OD2 B ASP C  253 ? 0.5797 0.4641 0.4012 0.2734  0.1582  0.0183  253 ASP C OD2 
6299 N  N   . GLU C  254 ? 0.1770 0.2599 0.1857 0.0290  -0.0436 -0.0229 254 GLU C N   
6300 C  CA  . GLU C  254 ? 0.1878 0.2890 0.1952 0.0378  -0.0190 -0.0266 254 GLU C CA  
6301 C  C   . GLU C  254 ? 0.1913 0.2693 0.1654 0.0187  -0.0355 -0.0131 254 GLU C C   
6302 O  O   . GLU C  254 ? 0.2349 0.2937 0.1850 0.0342  -0.0156 0.0309  254 GLU C O   
6303 C  CB  . GLU C  254 ? 0.2314 0.2947 0.2309 0.0467  -0.0517 0.0084  254 GLU C CB  
6304 C  CG  . GLU C  254 ? 0.2454 0.4557 0.2276 -0.0275 -0.0707 -0.0012 254 GLU C CG  
6305 C  CD  . GLU C  254 ? 0.3000 0.4139 0.4621 -0.1271 -0.2259 0.1599  254 GLU C CD  
6306 O  OE1 . GLU C  254 ? 0.8403 0.8139 0.4008 -0.1934 -0.1265 -0.2060 254 GLU C OE1 
6307 O  OE2 . GLU C  254 ? 0.5096 0.6391 0.3761 -0.2825 0.0401  -0.1330 254 GLU C OE2 
6308 N  N   . ARG C  255 ? 0.1992 0.2056 0.1836 0.0234  -0.0229 -0.0034 255 ARG C N   
6309 C  CA  . ARG C  255 ? 0.1833 0.1979 0.1884 0.0281  -0.0423 -0.0185 255 ARG C CA  
6310 C  C   . ARG C  255 ? 0.2071 0.1927 0.1400 0.0252  -0.0204 -0.0253 255 ARG C C   
6311 O  O   . ARG C  255 ? 0.1820 0.2310 0.2200 0.0265  -0.0054 0.0016  255 ARG C O   
6312 C  CB  . ARG C  255 ? 0.2191 0.1710 0.1657 -0.0070 -0.0098 -0.0127 255 ARG C CB  
6313 C  CG  . ARG C  255 ? 0.2535 0.1852 0.1750 -0.0129 -0.0458 -0.0027 255 ARG C CG  
6314 C  CD  . ARG C  255 ? 0.2119 0.1993 0.1986 -0.0095 -0.0454 -0.0129 255 ARG C CD  
6315 N  NE  . ARG C  255 ? 0.2068 0.2493 0.1855 -0.0242 -0.0496 -0.0041 255 ARG C NE  
6316 C  CZ  . ARG C  255 ? 0.2045 0.1753 0.1729 -0.0054 -0.0015 -0.0013 255 ARG C CZ  
6317 N  NH1 . ARG C  255 ? 0.2368 0.1857 0.2101 -0.0071 -0.0117 -0.0336 255 ARG C NH1 
6318 N  NH2 . ARG C  255 ? 0.1881 0.2214 0.1568 -0.0201 -0.0231 0.0000  255 ARG C NH2 
6319 N  N   . LEU C  256 ? 0.1934 0.1946 0.1821 0.0237  -0.0244 -0.0269 256 LEU C N   
6320 C  CA  . LEU C  256 ? 0.1949 0.1821 0.1755 0.0533  -0.0337 -0.0214 256 LEU C CA  
6321 C  C   . LEU C  256 ? 0.1848 0.1967 0.1736 0.0127  -0.0081 -0.0290 256 LEU C C   
6322 O  O   . LEU C  256 ? 0.1879 0.1938 0.1830 0.0221  -0.0436 -0.0099 256 LEU C O   
6323 C  CB  . LEU C  256 ? 0.2594 0.2435 0.1822 0.0679  -0.0595 -0.0456 256 LEU C CB  
6324 C  CG  . LEU C  256 ? 0.2606 0.2344 0.2011 0.0543  -0.0520 -0.0387 256 LEU C CG  
6325 C  CD1 . LEU C  256 ? 0.4162 0.3504 0.1970 0.1319  -0.0312 -0.1007 256 LEU C CD1 
6326 C  CD2 . LEU C  256 ? 0.3334 0.3066 0.2535 -0.0586 -0.1067 -0.0215 256 LEU C CD2 
6327 N  N   . VAL C  257 ? 0.1922 0.1824 0.1647 0.0507  -0.0215 -0.0265 257 VAL C N   
6328 C  CA  . VAL C  257 ? 0.1736 0.1688 0.1619 0.0227  -0.0162 -0.0473 257 VAL C CA  
6329 C  C   . VAL C  257 ? 0.1633 0.1368 0.2126 0.0190  -0.0217 -0.0331 257 VAL C C   
6330 O  O   . VAL C  257 ? 0.1841 0.1768 0.2182 0.0100  -0.0107 -0.0547 257 VAL C O   
6331 C  CB  . VAL C  257 ? 0.1986 0.2004 0.1558 0.0524  -0.0039 -0.0196 257 VAL C CB  
6332 C  CG1 . VAL C  257 ? 0.2055 0.2539 0.1983 0.0585  -0.0234 -0.0057 257 VAL C CG1 
6333 C  CG2 . VAL C  257 ? 0.2515 0.2022 0.1691 0.0796  0.0097  -0.0171 257 VAL C CG2 
6334 N  N   . TYR C  258 ? 0.1540 0.1733 0.1785 0.0258  -0.0146 -0.0110 258 TYR C N   
6335 C  CA  . TYR C  258 ? 0.1707 0.1613 0.1641 0.0093  -0.0111 -0.0190 258 TYR C CA  
6336 C  C   . TYR C  258 ? 0.1811 0.1718 0.1791 -0.0055 -0.0103 -0.0050 258 TYR C C   
6337 O  O   . TYR C  258 ? 0.2120 0.1849 0.1949 0.0225  -0.0428 -0.0280 258 TYR C O   
6338 C  CB  . TYR C  258 ? 0.1684 0.1892 0.1738 0.0144  -0.0033 0.0089  258 TYR C CB  
6339 C  CG  . TYR C  258 ? 0.1837 0.2410 0.1777 0.0227  -0.0171 0.0060  258 TYR C CG  
6340 C  CD1 . TYR C  258 ? 0.2423 0.2911 0.1604 0.0429  -0.0137 -0.0262 258 TYR C CD1 
6341 C  CD2 . TYR C  258 ? 0.2443 0.2166 0.1933 -0.0125 -0.0336 0.0227  258 TYR C CD2 
6342 C  CE1 . TYR C  258 ? 0.2640 0.2672 0.2453 0.0219  -0.0339 0.0207  258 TYR C CE1 
6343 C  CE2 . TYR C  258 ? 0.3356 0.2431 0.2164 -0.0388 -0.0679 0.0250  258 TYR C CE2 
6344 C  CZ  . TYR C  258 ? 0.2548 0.2531 0.2210 0.0291  -0.0431 0.0275  258 TYR C CZ  
6345 O  OH  . TYR C  258 ? 0.3644 0.3231 0.2392 0.0384  -0.0462 0.0634  258 TYR C OH  
6346 N  N   . THR C  259 ? 0.1825 0.1669 0.1964 0.0111  -0.0157 0.0000  259 THR C N   
6347 C  CA  . THR C  259 ? 0.1794 0.1814 0.1500 0.0330  0.0026  -0.0114 259 THR C CA  
6348 C  C   . THR C  259 ? 0.1687 0.2407 0.1811 0.0313  0.0205  0.0093  259 THR C C   
6349 O  O   . THR C  259 ? 0.2187 0.2162 0.1939 0.0574  0.0254  0.0006  259 THR C O   
6350 C  CB  . THR C  259 ? 0.1996 0.2062 0.1969 0.0165  0.0203  -0.0228 259 THR C CB  
6351 O  OG1 . THR C  259 ? 0.2444 0.2200 0.2343 -0.0322 0.0108  -0.0362 259 THR C OG1 
6352 C  CG2 . THR C  259 ? 0.1929 0.2002 0.2262 0.0286  0.0132  0.0127  259 THR C CG2 
6353 N  N   . SER C  260 ? 0.2075 0.2138 0.1906 0.0690  0.0103  0.0284  260 SER C N   
6354 C  CA  . SER C  260 ? 0.2190 0.2552 0.2543 0.0753  0.0197  0.0159  260 SER C CA  
6355 C  C   . SER C  260 ? 0.2649 0.2619 0.2258 0.0917  0.0138  -0.0106 260 SER C C   
6356 O  O   . SER C  260 ? 0.3600 0.3642 0.3655 0.1847  0.0166  -0.0489 260 SER C O   
6357 C  CB  . SER C  260 ? 0.2031 0.3410 0.2191 0.0679  0.0228  0.0719  260 SER C CB  
6358 O  OG  . SER C  260 ? 0.2150 0.2544 0.2075 0.0564  0.0310  0.0313  260 SER C OG  
6359 N  N   . PHE C  261 ? 0.3159 0.1681 0.2929 0.0539  0.0287  0.0270  261 PHE C N   
6360 C  CA  . PHE C  261 ? 0.3039 0.2218 0.2897 0.0058  -0.0006 0.0151  261 PHE C CA  
6361 C  C   . PHE C  261 ? 0.3964 0.2033 0.2617 -0.0421 -0.0528 -0.0094 261 PHE C C   
6362 O  O   . PHE C  261 ? 0.4519 0.2903 0.2717 0.0420  0.0317  -0.0523 261 PHE C O   
6363 C  CB  . PHE C  261 ? 0.3252 0.1990 0.2858 0.0054  0.0330  -0.0334 261 PHE C CB  
6364 C  CG  . PHE C  261 ? 0.2742 0.2045 0.2346 0.0012  0.0172  0.0070  261 PHE C CG  
6365 C  CD1 . PHE C  261 ? 0.3234 0.2182 0.2353 -0.0387 0.0109  0.0117  261 PHE C CD1 
6366 C  CD2 . PHE C  261 ? 0.3191 0.1860 0.2135 0.0142  0.0508  0.0258  261 PHE C CD2 
6367 C  CE1 . PHE C  261 ? 0.3325 0.2542 0.3096 -0.0444 0.0450  -0.0111 261 PHE C CE1 
6368 C  CE2 . PHE C  261 ? 0.2908 0.2205 0.2342 0.0311  0.0500  0.0167  261 PHE C CE2 
6369 C  CZ  . PHE C  261 ? 0.3109 0.2211 0.2708 -0.0247 0.0562  -0.0069 261 PHE C CZ  
6370 N  N   . SER C  262 ? 0.6253 0.2270 0.3762 -0.0469 -0.0992 -0.0452 262 SER C N   
6371 C  CA  . SER C  262 ? 0.8533 0.2431 0.3911 -0.2005 -0.2421 0.1018  262 SER C CA  
6372 C  C   . SER C  262 ? 0.6980 0.6524 0.8730 -0.0183 -0.0571 0.2960  262 SER C C   
6373 O  O   . SER C  262 ? 0.4673 0.6275 1.6109 -0.0542 0.3765  -0.4133 262 SER C O   
6374 C  CB  . SER C  262 ? 1.5668 0.7128 0.3323 -0.0565 -0.2397 -0.0508 262 SER C CB  
6375 O  OG  . SER C  262 ? 1.7058 0.6943 0.5204 -0.4137 0.3389  -0.3080 262 SER C OG  
6376 N  N   . GLN C  263 ? 0.9495 0.4686 0.3950 -0.2692 -0.2176 0.1869  263 GLN C N   
6377 C  CA  . GLN C  263 ? 0.6244 0.2920 0.4322 0.0255  0.0295  -0.0119 263 GLN C CA  
6378 C  C   . GLN C  263 ? 1.0355 0.6006 0.4465 0.1184  0.0653  -0.0885 263 GLN C C   
6379 O  O   . GLN C  263 ? 1.1446 0.6304 0.3944 0.2606  -0.0263 -0.2085 263 GLN C O   
6380 C  CB  . GLN C  263 ? 0.4713 0.2495 0.6684 -0.0434 -0.0308 -0.1367 263 GLN C CB  
6381 C  CG  . GLN C  263 ? 0.5073 0.4052 0.6656 0.0031  0.0063  -0.0057 263 GLN C CG  
6382 C  CD  . GLN C  263 ? 0.2828 0.4567 0.3515 -0.0966 0.0113  -0.0067 263 GLN C CD  
6383 O  OE1 . GLN C  263 ? 0.3875 0.3453 0.5374 -0.0919 -0.1643 0.0938  263 GLN C OE1 
6384 N  NE2 . GLN C  263 ? 0.2897 0.2224 0.3048 -0.0340 -0.0011 0.0135  263 GLN C NE2 
6385 N  N   . LYS D  3   ? 0.6386 0.2924 0.6756 0.1263  0.1268  0.1412  3   LYS D N   
6386 C  CA  . LYS D  3   ? 0.6258 0.2283 0.5427 0.0619  0.0527  0.1351  3   LYS D CA  
6387 C  C   . LYS D  3   ? 0.5633 0.2278 0.3101 0.0284  0.1542  0.0391  3   LYS D C   
6388 O  O   . LYS D  3   ? 0.4780 0.4045 0.2473 0.0131  0.0916  0.0761  3   LYS D O   
6389 C  CB  . LYS D  3   ? 0.8628 0.3054 0.5375 0.0357  0.1800  0.1903  3   LYS D CB  
6390 C  CG  . LYS D  3   ? 0.8379 0.5655 0.6035 -0.1057 0.3303  -0.0948 3   LYS D CG  
6391 N  N   . TRP D  4   ? 0.3142 0.1557 0.1839 -0.0088 -0.0061 0.0264  4   TRP D N   
6392 C  CA  . TRP D  4   ? 0.2713 0.1298 0.1960 -0.0288 0.0144  0.0223  4   TRP D CA  
6393 C  C   . TRP D  4   ? 0.1891 0.1578 0.1848 -0.0295 0.0247  0.0152  4   TRP D C   
6394 O  O   . TRP D  4   ? 0.2258 0.2017 0.1861 -0.0190 -0.0114 0.0220  4   TRP D O   
6395 C  CB  . TRP D  4   ? 0.2202 0.1622 0.1623 -0.0187 -0.0094 0.0008  4   TRP D CB  
6396 C  CG  . TRP D  4   ? 0.1967 0.1356 0.1699 -0.0052 -0.0110 0.0068  4   TRP D CG  
6397 C  CD1 . TRP D  4   ? 0.2265 0.1595 0.1989 0.0126  -0.0193 -0.0070 4   TRP D CD1 
6398 C  CD2 . TRP D  4   ? 0.2049 0.1662 0.1517 -0.0096 -0.0166 -0.0193 4   TRP D CD2 
6399 N  NE1 . TRP D  4   ? 0.2262 0.1868 0.2010 0.0392  -0.0197 0.0073  4   TRP D NE1 
6400 C  CE2 . TRP D  4   ? 0.2061 0.1764 0.1294 0.0248  -0.0147 0.0000  4   TRP D CE2 
6401 C  CE3 . TRP D  4   ? 0.2058 0.1527 0.1445 -0.0039 -0.0156 -0.0250 4   TRP D CE3 
6402 C  CZ2 . TRP D  4   ? 0.1716 0.2371 0.1464 -0.0079 -0.0125 0.0132  4   TRP D CZ2 
6403 C  CZ3 . TRP D  4   ? 0.2065 0.1810 0.1326 -0.0366 -0.0324 -0.0109 4   TRP D CZ3 
6404 C  CH2 . TRP D  4   ? 0.1990 0.1997 0.1399 -0.0102 -0.0323 -0.0053 4   TRP D CH2 
6405 N  N   . THR D  5   ? 0.2160 0.1495 0.1684 -0.0201 0.0022  0.0071  5   THR D N   
6406 C  CA  . THR D  5   ? 0.2107 0.1372 0.1714 -0.0260 0.0050  0.0010  5   THR D CA  
6407 C  C   . THR D  5   ? 0.1913 0.1796 0.1507 -0.0253 -0.0062 0.0080  5   THR D C   
6408 O  O   . THR D  5   ? 0.2144 0.1527 0.1410 -0.0271 -0.0049 -0.0018 5   THR D O   
6409 C  CB  . THR D  5   ? 0.2698 0.1667 0.1606 -0.0220 -0.0046 0.0102  5   THR D CB  
6410 O  OG1 . THR D  5   ? 0.2648 0.2336 0.1984 -0.0173 0.0387  0.0325  5   THR D OG1 
6411 C  CG2 . THR D  5   ? 0.3206 0.1651 0.1825 -0.0342 0.0458  0.0256  5   THR D CG2 
6412 N  N   . TYR D  6   ? 0.2013 0.1555 0.1512 -0.0406 0.0021  -0.0048 6   TYR D N   
6413 C  CA  . TYR D  6   ? 0.1905 0.1619 0.1632 -0.0188 0.0153  -0.0212 6   TYR D CA  
6414 C  C   . TYR D  6   ? 0.2081 0.1523 0.1557 -0.0350 0.0077  -0.0120 6   TYR D C   
6415 O  O   . TYR D  6   ? 0.1894 0.1864 0.1902 -0.0313 -0.0137 -0.0071 6   TYR D O   
6416 C  CB  . TYR D  6   ? 0.1687 0.1587 0.1836 -0.0352 0.0132  -0.0040 6   TYR D CB  
6417 C  CG  . TYR D  6   ? 0.1586 0.1355 0.1437 -0.0119 0.0000  -0.0132 6   TYR D CG  
6418 C  CD1 . TYR D  6   ? 0.1688 0.1199 0.1554 -0.0144 0.0051  -0.0103 6   TYR D CD1 
6419 C  CD2 . TYR D  6   ? 0.1649 0.1312 0.1485 -0.0134 -0.0003 -0.0096 6   TYR D CD2 
6420 C  CE1 . TYR D  6   ? 0.1575 0.1042 0.1565 -0.0185 0.0095  -0.0068 6   TYR D CE1 
6421 C  CE2 . TYR D  6   ? 0.1904 0.1195 0.1271 0.0089  0.0083  -0.0029 6   TYR D CE2 
6422 C  CZ  . TYR D  6   ? 0.1666 0.1339 0.1252 -0.0043 0.0004  -0.0145 6   TYR D CZ  
6423 O  OH  . TYR D  6   ? 0.1750 0.1467 0.1330 0.0154  0.0139  -0.0145 6   TYR D OH  
6424 N  N   . PHE D  7   ? 0.2197 0.1953 0.1705 -0.0375 0.0369  0.0012  7   PHE D N   
6425 C  CA  . PHE D  7   ? 0.2156 0.2450 0.2468 -0.0366 0.0411  -0.0299 7   PHE D CA  
6426 C  C   . PHE D  7   ? 0.2420 0.2511 0.2796 0.0026  0.0710  0.0702  7   PHE D C   
6427 O  O   . PHE D  7   ? 0.2357 0.3028 0.4799 -0.0487 0.0579  0.1141  7   PHE D O   
6428 C  CB  . PHE D  7   ? 0.3658 0.3940 0.2676 -0.0339 0.0775  -0.1066 7   PHE D CB  
6429 C  CG  . PHE D  7   ? 0.3980 0.4308 0.3198 -0.0631 0.1147  -0.0313 7   PHE D CG  
6430 C  CD1 . PHE D  7   ? 0.3934 0.4774 0.3987 -0.0170 0.1197  -0.0328 7   PHE D CD1 
6431 C  CD2 . PHE D  7   ? 0.5924 0.3620 0.3890 0.1418  0.1614  0.0546  7   PHE D CD2 
6432 C  CE1 . PHE D  7   ? 0.4686 0.5024 0.3635 0.0775  0.1608  -0.0269 7   PHE D CE1 
6433 C  CE2 . PHE D  7   ? 0.5758 0.8384 0.3574 0.1172  0.2139  0.0184  7   PHE D CE2 
6434 C  CZ  . PHE D  7   ? 0.6678 0.7480 0.6813 0.0431  0.3454  0.2039  7   PHE D CZ  
6435 N  N   . GLY D  8   ? 0.2569 0.2378 0.2158 -0.0339 0.0442  -0.0020 8   GLY D N   
6436 C  CA  . GLY D  8   ? 0.2577 0.2805 0.2533 -0.0925 -0.0005 0.0084  8   GLY D CA  
6437 C  C   . GLY D  8   ? 0.2147 0.2754 0.2859 -0.0913 0.0452  0.0267  8   GLY D C   
6438 O  O   . GLY D  8   ? 0.2448 0.2791 0.2561 -0.0754 0.0220  0.0483  8   GLY D O   
6439 N  N   . PRO D  9   ? 0.2801 0.2624 0.2670 -0.1058 0.0177  0.0483  9   PRO D N   
6440 C  CA  . PRO D  9   ? 0.2955 0.2587 0.3010 -0.0916 0.0479  0.0240  9   PRO D CA  
6441 C  C   . PRO D  9   ? 0.2810 0.2703 0.2366 -0.1155 0.0198  -0.0041 9   PRO D C   
6442 O  O   . PRO D  9   ? 0.3172 0.2573 0.2367 -0.1067 -0.0178 0.0040  9   PRO D O   
6443 C  CB  . PRO D  9   ? 0.3792 0.3134 0.2998 -0.1884 0.0315  0.0693  9   PRO D CB  
6444 C  CG  . PRO D  9   ? 0.5757 0.3008 0.3055 -0.0976 -0.0130 0.0379  9   PRO D CG  
6445 C  CD  . PRO D  9   ? 0.3723 0.3424 0.2565 -0.1231 0.0904  0.0433  9   PRO D CD  
6446 N  N   . ASP D  10  ? 0.2772 0.2190 0.2543 -0.0853 -0.0084 0.0515  10  ASP D N   
6447 C  CA  . ASP D  10  ? 0.2839 0.1661 0.2350 -0.0636 -0.0186 0.0333  10  ASP D CA  
6448 C  C   . ASP D  10  ? 0.2500 0.1721 0.1522 -0.0389 -0.0260 0.0152  10  ASP D C   
6449 O  O   . ASP D  10  ? 0.2152 0.1725 0.1781 -0.0286 -0.0245 0.0124  10  ASP D O   
6450 C  CB  . ASP D  10  ? 0.2843 0.1795 0.2462 -0.0363 -0.0475 0.0305  10  ASP D CB  
6451 C  CG  . ASP D  10  ? 0.5037 0.2591 0.2828 -0.1324 -0.0432 0.0782  10  ASP D CG  
6452 O  OD1 . ASP D  10  ? 0.4851 0.2143 0.3614 -0.0998 -0.0394 0.0479  10  ASP D OD1 
6453 O  OD2 . ASP D  10  ? 0.4688 0.3467 0.2674 -0.0679 -0.0126 0.0835  10  ASP D OD2 
6454 N  N   . GLY D  11  ? 0.2384 0.1728 0.1876 -0.0446 -0.0396 0.0236  11  GLY D N   
6455 C  CA  . GLY D  11  ? 0.1986 0.1745 0.1439 -0.0471 -0.0018 0.0521  11  GLY D CA  
6456 C  C   . GLY D  11  ? 0.1766 0.1371 0.1520 -0.0118 -0.0117 0.0182  11  GLY D C   
6457 O  O   . GLY D  11  ? 0.1810 0.1258 0.1635 -0.0148 -0.0177 0.0085  11  GLY D O   
6458 N  N   . GLU D  12  ? 0.1567 0.1387 0.1483 -0.0161 -0.0093 0.0176  12  GLU D N   
6459 C  CA  . GLU D  12  ? 0.1500 0.1306 0.1366 -0.0244 -0.0074 -0.0051 12  GLU D CA  
6460 C  C   . GLU D  12  ? 0.1489 0.1084 0.1490 -0.0171 0.0114  0.0015  12  GLU D C   
6461 O  O   . GLU D  12  ? 0.1645 0.1256 0.1393 -0.0170 0.0094  -0.0092 12  GLU D O   
6462 C  CB  . GLU D  12  ? 0.1555 0.1000 0.1627 -0.0008 -0.0075 0.0080  12  GLU D CB  
6463 C  CG  . GLU D  12  ? 0.1597 0.1203 0.1612 0.0033  0.0016  -0.0006 12  GLU D CG  
6464 C  CD  . GLU D  12  ? 0.1503 0.1400 0.1587 -0.0026 -0.0124 -0.0043 12  GLU D CD  
6465 O  OE1 . GLU D  12  ? 0.1468 0.1369 0.1477 -0.0020 -0.0004 -0.0043 12  GLU D OE1 
6466 O  OE2 . GLU D  12  ? 0.1967 0.1209 0.1606 -0.0220 -0.0219 0.0116  12  GLU D OE2 
6467 N  N   . ASN D  13  ? 0.1454 0.1133 0.1692 -0.0209 -0.0004 -0.0015 13  ASN D N   
6468 C  CA  . ASN D  13  ? 0.1505 0.1159 0.1561 -0.0102 -0.0106 0.0010  13  ASN D CA  
6469 C  C   . ASN D  13  ? 0.1759 0.1062 0.1554 -0.0203 -0.0095 0.0025  13  ASN D C   
6470 O  O   . ASN D  13  ? 0.1844 0.1361 0.1707 -0.0234 -0.0184 -0.0058 13  ASN D O   
6471 C  CB  . ASN D  13  ? 0.1472 0.1177 0.1953 -0.0135 -0.0006 -0.0122 13  ASN D CB  
6472 C  CG  . ASN D  13  ? 0.1509 0.1360 0.1429 -0.0225 -0.0109 -0.0071 13  ASN D CG  
6473 O  OD1 . ASN D  13  ? 0.1476 0.1361 0.1599 -0.0100 -0.0026 0.0060  13  ASN D OD1 
6474 N  ND2 . ASN D  13  ? 0.1471 0.1664 0.1476 0.0000  -0.0057 -0.0143 13  ASN D ND2 
6475 N  N   . SER D  14  ? 0.1457 0.1089 0.1653 -0.0036 0.0048  0.0031  14  SER D N   
6476 C  CA  . SER D  14  ? 0.1456 0.0942 0.1700 -0.0155 -0.0020 0.0089  14  SER D CA  
6477 C  C   . SER D  14  ? 0.1568 0.1139 0.1420 0.0062  -0.0018 -0.0022 14  SER D C   
6478 O  O   . SER D  14  ? 0.1713 0.1120 0.1755 -0.0189 0.0100  -0.0002 14  SER D O   
6479 C  CB  . SER D  14  ? 0.1555 0.1351 0.1791 -0.0052 0.0330  0.0170  14  SER D CB  
6480 O  OG  . SER D  14  ? 0.1788 0.1734 0.2235 -0.0158 0.0383  0.0132  14  SER D OG  
6481 N  N   . TRP D  15  ? 0.1523 0.1228 0.1332 -0.0236 0.0168  -0.0036 15  TRP D N   
6482 C  CA  . TRP D  15  ? 0.1612 0.1321 0.1461 -0.0358 0.0190  -0.0152 15  TRP D CA  
6483 C  C   . TRP D  15  ? 0.1416 0.1272 0.1382 -0.0171 -0.0048 -0.0060 15  TRP D C   
6484 O  O   . TRP D  15  ? 0.1619 0.1143 0.1734 -0.0025 0.0039  0.0010  15  TRP D O   
6485 C  CB  . TRP D  15  ? 0.1518 0.1265 0.1486 -0.0318 0.0099  -0.0152 15  TRP D CB  
6486 C  CG  . TRP D  15  ? 0.1425 0.1068 0.1437 -0.0085 -0.0116 -0.0066 15  TRP D CG  
6487 C  CD1 . TRP D  15  ? 0.1594 0.1222 0.1448 -0.0013 -0.0212 -0.0041 15  TRP D CD1 
6488 C  CD2 . TRP D  15  ? 0.1696 0.1091 0.1279 -0.0186 -0.0100 0.0009  15  TRP D CD2 
6489 N  NE1 . TRP D  15  ? 0.1618 0.1219 0.1342 -0.0124 -0.0129 -0.0016 15  TRP D NE1 
6490 C  CE2 . TRP D  15  ? 0.1425 0.1115 0.1309 -0.0172 -0.0157 -0.0010 15  TRP D CE2 
6491 C  CE3 . TRP D  15  ? 0.1430 0.1125 0.1517 0.0001  -0.0111 0.0063  15  TRP D CE3 
6492 C  CZ2 . TRP D  15  ? 0.1497 0.1040 0.1652 -0.0064 -0.0149 -0.0077 15  TRP D CZ2 
6493 C  CZ3 . TRP D  15  ? 0.1539 0.1207 0.1609 -0.0106 -0.0168 0.0021  15  TRP D CZ3 
6494 C  CH2 . TRP D  15  ? 0.1630 0.1212 0.1408 -0.0003 -0.0166 -0.0022 15  TRP D CH2 
6495 N  N   . SER D  16  ? 0.1720 0.1228 0.1444 -0.0369 -0.0050 -0.0099 16  SER D N   
6496 C  CA  . SER D  16  ? 0.1786 0.1299 0.1564 -0.0159 -0.0054 -0.0081 16  SER D CA  
6497 C  C   . SER D  16  ? 0.1739 0.1426 0.1540 -0.0326 0.0226  -0.0326 16  SER D C   
6498 O  O   . SER D  16  ? 0.2139 0.1326 0.1682 -0.0182 0.0161  -0.0176 16  SER D O   
6499 C  CB  . SER D  16  ? 0.1985 0.1428 0.1803 -0.0211 -0.0082 -0.0165 16  SER D CB  
6500 O  OG  . SER D  16  ? 0.2524 0.1886 0.2684 -0.0501 -0.0305 -0.0332 16  SER D OG  
6501 N  N   . LYS D  17  ? 0.1604 0.1114 0.1647 -0.0194 0.0010  -0.0021 17  LYS D N   
6502 C  CA  . LYS D  17  ? 0.1782 0.1137 0.1895 -0.0285 0.0229  -0.0212 17  LYS D CA  
6503 C  C   . LYS D  17  ? 0.1564 0.1402 0.1969 -0.0064 0.0272  -0.0211 17  LYS D C   
6504 O  O   . LYS D  17  ? 0.2012 0.1333 0.2279 -0.0341 0.0298  -0.0113 17  LYS D O   
6505 C  CB  . LYS D  17  ? 0.1855 0.1220 0.1913 -0.0092 0.0467  -0.0340 17  LYS D CB  
6506 C  CG  . LYS D  17  ? 0.1739 0.1658 0.1847 -0.0356 0.0168  -0.0263 17  LYS D CG  
6507 C  CD  . LYS D  17  ? 0.2041 0.1491 0.2103 -0.0119 0.0542  -0.0092 17  LYS D CD  
6508 C  CE  . LYS D  17  ? 0.1682 0.1487 0.2167 -0.0326 0.0178  -0.0261 17  LYS D CE  
6509 N  NZ  . LYS D  17  ? 0.2171 0.1667 0.2206 -0.0366 0.0374  -0.0334 17  LYS D NZ  
6510 N  N   . LYS D  18  ? 0.1796 0.1317 0.1729 -0.0175 -0.0026 0.0059  18  LYS D N   
6511 C  CA  . LYS D  18  ? 0.1586 0.1373 0.2103 -0.0022 0.0248  0.0012  18  LYS D CA  
6512 C  C   . LYS D  18  ? 0.1958 0.1016 0.2384 -0.0039 0.0363  0.0231  18  LYS D C   
6513 O  O   . LYS D  18  ? 0.2056 0.1511 0.2886 -0.0010 0.0438  0.0273  18  LYS D O   
6514 C  CB  . LYS D  18  ? 0.1912 0.1948 0.2211 -0.0227 0.0179  0.0384  18  LYS D CB  
6515 C  CG  . LYS D  18  ? 0.2892 0.3172 0.2073 -0.0979 0.0124  0.0421  18  LYS D CG  
6516 C  CD  . LYS D  18  ? 0.2776 0.4096 0.2033 -0.0840 -0.0301 0.0611  18  LYS D CD  
6517 C  CE  . LYS D  18  ? 0.4359 0.5901 0.1984 -0.2229 -0.0313 0.0694  18  LYS D CE  
6518 N  NZ  . LYS D  18  ? 0.4531 0.8043 0.2353 -0.3069 -0.0629 0.0421  18  LYS D NZ  
6519 N  N   . TYR D  19  ? 0.1923 0.1140 0.1625 -0.0279 0.0188  -0.0118 19  TYR D N   
6520 C  CA  . TYR D  19  ? 0.1947 0.1123 0.1672 -0.0186 0.0274  0.0067  19  TYR D CA  
6521 C  C   . TYR D  19  ? 0.2107 0.1468 0.1446 -0.0023 0.0269  -0.0127 19  TYR D C   
6522 O  O   . TYR D  19  ? 0.1946 0.1306 0.1671 -0.0120 0.0142  -0.0219 19  TYR D O   
6523 C  CB  . TYR D  19  ? 0.2270 0.1190 0.1685 -0.0214 -0.0038 -0.0128 19  TYR D CB  
6524 C  CG  . TYR D  19  ? 0.1911 0.1079 0.1761 0.0047  0.0163  0.0015  19  TYR D CG  
6525 C  CD1 . TYR D  19  ? 0.2150 0.1310 0.2057 -0.0095 -0.0091 0.0088  19  TYR D CD1 
6526 C  CD2 . TYR D  19  ? 0.2086 0.1327 0.1666 -0.0229 0.0100  -0.0063 19  TYR D CD2 
6527 C  CE1 . TYR D  19  ? 0.2773 0.1938 0.2011 0.0279  -0.0337 -0.0013 19  TYR D CE1 
6528 C  CE2 . TYR D  19  ? 0.2049 0.1822 0.2096 -0.0631 -0.0271 0.0092  19  TYR D CE2 
6529 C  CZ  . TYR D  19  ? 0.2579 0.1864 0.2205 -0.0031 -0.0207 0.0075  19  TYR D CZ  
6530 O  OH  . TYR D  19  ? 0.3450 0.2314 0.2278 0.0100  -0.0562 0.0414  19  TYR D OH  
6531 N  N   . PRO D  20  ? 0.2158 0.1376 0.1584 -0.0267 0.0080  -0.0065 20  PRO D N   
6532 C  CA  . PRO D  20  ? 0.2327 0.1192 0.2015 -0.0325 -0.0254 -0.0232 20  PRO D CA  
6533 C  C   . PRO D  20  ? 0.2110 0.1127 0.1772 0.0015  -0.0126 -0.0282 20  PRO D C   
6534 O  O   . PRO D  20  ? 0.2064 0.1503 0.1651 -0.0264 -0.0079 -0.0337 20  PRO D O   
6535 C  CB  . PRO D  20  ? 0.2794 0.1444 0.2258 -0.0190 -0.0143 -0.0339 20  PRO D CB  
6536 C  CG  . PRO D  20  ? 0.3292 0.2183 0.2335 0.0291  -0.0389 -0.0629 20  PRO D CG  
6537 C  CD  . PRO D  20  ? 0.2530 0.1142 0.1654 -0.0160 0.0187  -0.0350 20  PRO D CD  
6538 N  N   . SER D  21  ? 0.2125 0.1273 0.1636 -0.0114 0.0154  -0.0162 21  SER D N   
6539 C  CA  . SER D  21  ? 0.2147 0.1398 0.1439 -0.0167 0.0048  -0.0085 21  SER D CA  
6540 C  C   . SER D  21  ? 0.2036 0.1292 0.1474 -0.0223 -0.0004 -0.0154 21  SER D C   
6541 O  O   . SER D  21  ? 0.2375 0.1512 0.1442 -0.0277 -0.0122 -0.0126 21  SER D O   
6542 C  CB  . SER D  21  ? 0.2329 0.1537 0.1479 -0.0130 0.0279  -0.0361 21  SER D CB  
6543 O  OG  . SER D  21  ? 0.2567 0.1717 0.1922 0.0168  0.0277  -0.0515 21  SER D OG  
6544 N  N   . CYS D  22  ? 0.1777 0.1328 0.1376 -0.0162 0.0051  -0.0253 22  CYS D N   
6545 C  CA  . CYS D  22  ? 0.1865 0.1333 0.1384 0.0010  -0.0042 -0.0255 22  CYS D CA  
6546 C  C   . CYS D  22  ? 0.2096 0.1465 0.1825 -0.0126 -0.0029 -0.0209 22  CYS D C   
6547 O  O   . CYS D  22  ? 0.2139 0.1599 0.1872 0.0110  -0.0298 -0.0263 22  CYS D O   
6548 C  CB  . CYS D  22  ? 0.1942 0.1446 0.1491 -0.0193 0.0075  0.0039  22  CYS D CB  
6549 S  SG  . CYS D  22  ? 0.1948 0.1307 0.1448 -0.0046 0.0029  -0.0066 22  CYS D SG  
6550 N  N   . GLY D  23  ? 0.2099 0.1452 0.1824 -0.0152 -0.0297 -0.0256 23  GLY D N   
6551 C  CA  . GLY D  23  ? 0.2429 0.1754 0.1755 -0.0061 -0.0256 -0.0276 23  GLY D CA  
6552 C  C   . GLY D  23  ? 0.2472 0.1966 0.1945 -0.0029 -0.0319 -0.0236 23  GLY D C   
6553 O  O   . GLY D  23  ? 0.2561 0.2490 0.2081 0.0011  -0.0520 -0.0390 23  GLY D O   
6554 N  N   . GLY D  24  ? 0.2514 0.1760 0.1615 -0.0089 -0.0295 -0.0403 24  GLY D N   
6555 C  CA  . GLY D  24  ? 0.2987 0.2157 0.1635 -0.0486 0.0142  -0.0146 24  GLY D CA  
6556 C  C   . GLY D  24  ? 0.2942 0.2310 0.1631 -0.0219 -0.0331 -0.0155 24  GLY D C   
6557 O  O   . GLY D  24  ? 0.3622 0.2350 0.2105 0.0110  -0.0622 -0.0227 24  GLY D O   
6558 N  N   A LEU D  25  ? 0.4092 0.1894 0.2357 -0.0749 0.0106  -0.0193 25  LEU D N   
6559 N  N   B LEU D  25  ? 0.4048 0.1759 0.2134 -0.0818 0.0070  -0.0173 25  LEU D N   
6560 C  CA  A LEU D  25  ? 0.4759 0.2696 0.1703 -0.1152 -0.0453 0.0092  25  LEU D CA  
6561 C  CA  B LEU D  25  ? 0.4410 0.2188 0.1314 -0.1131 -0.0108 0.0137  25  LEU D CA  
6562 C  C   A LEU D  25  ? 0.3748 0.2507 0.1518 -0.0401 -0.0494 -0.0051 25  LEU D C   
6563 C  C   B LEU D  25  ? 0.3393 0.2272 0.1042 -0.0560 0.0027  -0.0179 25  LEU D C   
6564 O  O   A LEU D  25  ? 0.3474 0.2328 0.2155 -0.0552 -0.0204 -0.0210 25  LEU D O   
6565 O  O   B LEU D  25  ? 0.2888 0.1416 0.1459 -0.0990 0.0296  -0.0153 25  LEU D O   
6566 C  CB  A LEU D  25  ? 0.5412 0.3748 0.1666 -0.1332 -0.0219 -0.0295 25  LEU D CB  
6567 C  CB  B LEU D  25  ? 0.4675 0.3336 0.1435 -0.1487 -0.0159 -0.0880 25  LEU D CB  
6568 C  CG  A LEU D  25  ? 0.4381 0.3684 0.2552 -0.0564 -0.0632 -0.0322 25  LEU D CG  
6569 C  CG  B LEU D  25  ? 0.3937 0.2511 0.1537 -0.0647 -0.0519 -0.0259 25  LEU D CG  
6570 C  CD1 A LEU D  25  ? 0.4197 0.5617 0.2764 -0.0330 0.0283  -0.1174 25  LEU D CD1 
6571 C  CD1 B LEU D  25  ? 0.4466 0.5526 0.1916 -0.1015 -0.0230 -0.1338 25  LEU D CD1 
6572 C  CD2 A LEU D  25  ? 0.6243 0.4653 0.2498 0.0257  -0.0364 -0.0072 25  LEU D CD2 
6573 C  CD2 B LEU D  25  ? 0.5407 0.3080 0.1168 0.0210  -0.0573 -0.0223 25  LEU D CD2 
6574 N  N   . LEU D  26  ? 0.3770 0.2212 0.1412 -0.0710 -0.0361 0.0022  26  LEU D N   
6575 C  CA  . LEU D  26  ? 0.3189 0.1976 0.1394 -0.0061 -0.0359 -0.0122 26  LEU D CA  
6576 C  C   . LEU D  26  ? 0.2247 0.1525 0.1438 0.0065  -0.0031 0.0048  26  LEU D C   
6577 O  O   . LEU D  26  ? 0.2259 0.2087 0.1492 0.0079  0.0228  0.0102  26  LEU D O   
6578 C  CB  . LEU D  26  ? 0.4073 0.2685 0.1629 -0.0616 0.0611  -0.0494 26  LEU D CB  
6579 C  CG  . LEU D  26  ? 0.6789 0.4693 0.1736 0.0286  -0.0092 -0.0255 26  LEU D CG  
6580 C  CD1 . LEU D  26  ? 0.7519 0.5448 0.1608 -0.0004 0.0668  -0.0694 26  LEU D CD1 
6581 C  CD2 . LEU D  26  ? 0.9542 0.3956 0.1386 -0.0791 0.0103  0.0376  26  LEU D CD2 
6582 N  N   . GLN D  27  ? 0.2228 0.1601 0.1335 -0.0219 -0.0033 -0.0125 27  GLN D N   
6583 C  CA  . GLN D  27  ? 0.1870 0.1118 0.1161 -0.0087 -0.0091 0.0082  27  GLN D CA  
6584 C  C   . GLN D  27  ? 0.1740 0.1161 0.1328 -0.0013 -0.0073 0.0165  27  GLN D C   
6585 O  O   . GLN D  27  ? 0.1985 0.1398 0.1302 0.0018  -0.0135 0.0035  27  GLN D O   
6586 C  CB  . GLN D  27  ? 0.1744 0.1293 0.1746 0.0046  -0.0083 -0.0012 27  GLN D CB  
6587 C  CG  . GLN D  27  ? 0.2046 0.1482 0.1664 -0.0159 -0.0135 -0.0337 27  GLN D CG  
6588 C  CD  . GLN D  27  ? 0.2006 0.1388 0.1165 -0.0175 -0.0091 -0.0148 27  GLN D CD  
6589 O  OE1 . GLN D  27  ? 0.2116 0.1412 0.1188 -0.0136 -0.0004 -0.0100 27  GLN D OE1 
6590 N  NE2 . GLN D  27  ? 0.2031 0.1419 0.1405 -0.0076 -0.0018 -0.0334 27  GLN D NE2 
6591 N  N   . SER D  28  ? 0.1729 0.1273 0.1170 0.0008  -0.0174 0.0004  28  SER D N   
6592 C  CA  . SER D  28  ? 0.1530 0.1429 0.1195 -0.0059 -0.0084 -0.0167 28  SER D CA  
6593 C  C   . SER D  28  ? 0.1320 0.1467 0.1329 0.0055  -0.0109 0.0074  28  SER D C   
6594 O  O   . SER D  28  ? 0.1507 0.1204 0.1450 -0.0031 0.0008  0.0070  28  SER D O   
6595 C  CB  . SER D  28  ? 0.1552 0.1228 0.1136 -0.0010 0.0136  -0.0092 28  SER D CB  
6596 O  OG  . SER D  28  ? 0.1915 0.1259 0.1089 0.0118  0.0037  -0.0022 28  SER D OG  
6597 N  N   . PRO D  29  ? 0.1392 0.1134 0.1209 -0.0016 0.0006  0.0102  29  PRO D N   
6598 C  CA  . PRO D  29  ? 0.1342 0.1186 0.1235 -0.0039 -0.0116 -0.0017 29  PRO D CA  
6599 C  C   . PRO D  29  ? 0.1316 0.1177 0.1118 -0.0068 0.0156  0.0055  29  PRO D C   
6600 O  O   . PRO D  29  ? 0.1406 0.1330 0.1238 -0.0073 -0.0016 0.0122  29  PRO D O   
6601 C  CB  . PRO D  29  ? 0.1664 0.1332 0.1050 -0.0208 -0.0001 -0.0002 29  PRO D CB  
6602 C  CG  . PRO D  29  ? 0.1353 0.1098 0.1365 -0.0046 -0.0049 0.0089  29  PRO D CG  
6603 C  CD  . PRO D  29  ? 0.1439 0.1079 0.1165 -0.0055 0.0029  -0.0060 29  PRO D CD  
6604 N  N   . ILE D  30  ? 0.1480 0.1095 0.1231 0.0032  0.0071  0.0218  30  ILE D N   
6605 C  CA  . ILE D  30  ? 0.1694 0.1295 0.1039 0.0084  -0.0075 0.0251  30  ILE D CA  
6606 C  C   . ILE D  30  ? 0.1408 0.1266 0.1394 0.0058  0.0033  0.0214  30  ILE D C   
6607 O  O   . ILE D  30  ? 0.1465 0.1310 0.1405 0.0150  0.0025  0.0183  30  ILE D O   
6608 C  CB  . ILE D  30  ? 0.1866 0.1311 0.1168 0.0156  0.0125  0.0217  30  ILE D CB  
6609 C  CG1 . ILE D  30  ? 0.1836 0.1925 0.1283 0.0105  0.0273  0.0183  30  ILE D CG1 
6610 C  CG2 . ILE D  30  ? 0.2755 0.1340 0.1443 0.0109  -0.0026 -0.0130 30  ILE D CG2 
6611 C  CD1 . ILE D  30  ? 0.2480 0.2423 0.1145 0.0310  0.0179  0.0314  30  ILE D CD1 
6612 N  N   . ASP D  31  ? 0.1509 0.1332 0.1308 0.0099  0.0136  0.0265  31  ASP D N   
6613 C  CA  . ASP D  31  ? 0.1608 0.1326 0.1305 0.0160  0.0158  0.0237  31  ASP D CA  
6614 C  C   . ASP D  31  ? 0.1638 0.1417 0.1247 0.0262  -0.0089 0.0108  31  ASP D C   
6615 O  O   . ASP D  31  ? 0.2423 0.2231 0.1378 -0.0567 -0.0190 0.0187  31  ASP D O   
6616 C  CB  . ASP D  31  ? 0.1679 0.1429 0.1478 0.0154  0.0113  0.0168  31  ASP D CB  
6617 C  CG  . ASP D  31  ? 0.1906 0.1533 0.1693 0.0384  -0.0057 0.0048  31  ASP D CG  
6618 O  OD1 . ASP D  31  ? 0.1894 0.1545 0.1798 0.0227  -0.0161 -0.0008 31  ASP D OD1 
6619 O  OD2 . ASP D  31  ? 0.3010 0.2117 0.1733 0.0439  -0.0520 0.0165  31  ASP D OD2 
6620 N  N   . LEU D  32  ? 0.1748 0.1463 0.1254 -0.0003 -0.0030 -0.0006 32  LEU D N   
6621 C  CA  . LEU D  32  ? 0.1945 0.1463 0.1575 -0.0069 0.0216  0.0447  32  LEU D CA  
6622 C  C   . LEU D  32  ? 0.1989 0.1593 0.1538 -0.0098 0.0245  0.0107  32  LEU D C   
6623 O  O   . LEU D  32  ? 0.2344 0.1581 0.1751 0.0353  -0.0148 0.0263  32  LEU D O   
6624 C  CB  . LEU D  32  ? 0.1878 0.1860 0.1955 0.0018  0.0215  0.0195  32  LEU D CB  
6625 C  CG  . LEU D  32  ? 0.1655 0.2039 0.1615 0.0133  0.0276  0.0034  32  LEU D CG  
6626 C  CD1 . LEU D  32  ? 0.1805 0.1832 0.1829 0.0021  0.0335  -0.0057 32  LEU D CD1 
6627 C  CD2 . LEU D  32  ? 0.2624 0.2155 0.1972 0.0301  0.0099  -0.0108 32  LEU D CD2 
6628 N  N   . HIS D  33  ? 0.2244 0.1706 0.1402 0.0025  0.0143  0.0278  33  HIS D N   
6629 C  CA  . HIS D  33  ? 0.1884 0.1741 0.1525 0.0280  0.0221  0.0207  33  HIS D CA  
6630 C  C   . HIS D  33  ? 0.1652 0.1944 0.1527 0.0257  0.0003  0.0127  33  HIS D C   
6631 O  O   . HIS D  33  ? 0.2092 0.1785 0.1666 0.0227  0.0319  0.0406  33  HIS D O   
6632 C  CB  . HIS D  33  ? 0.1978 0.2160 0.1889 -0.0018 0.0283  0.0357  33  HIS D CB  
6633 C  CG  . HIS D  33  ? 0.2496 0.2297 0.1386 -0.0211 0.0097  0.0489  33  HIS D CG  
6634 N  ND1 . HIS D  33  ? 0.3397 0.2245 0.1986 -0.0653 -0.0690 0.0775  33  HIS D ND1 
6635 C  CD2 . HIS D  33  ? 0.2115 0.3256 0.1891 0.0666  0.0003  0.0245  33  HIS D CD2 
6636 C  CE1 . HIS D  33  ? 0.2998 0.2666 0.2536 -0.0732 -0.0817 0.0579  33  HIS D CE1 
6637 N  NE2 . HIS D  33  ? 0.2216 0.3628 0.1733 0.0042  -0.0040 0.0521  33  HIS D NE2 
6638 N  N   . SER D  34  ? 0.2237 0.2237 0.1732 0.0468  0.0187  0.0494  34  SER D N   
6639 C  CA  . SER D  34  ? 0.2252 0.1873 0.1891 0.0271  0.0312  0.0488  34  SER D CA  
6640 C  C   . SER D  34  ? 0.2341 0.2217 0.1676 0.0291  0.0000  0.0525  34  SER D C   
6641 O  O   . SER D  34  ? 0.2489 0.2381 0.1661 0.0359  0.0156  0.0501  34  SER D O   
6642 C  CB  . SER D  34  ? 0.2936 0.2346 0.2680 0.0544  0.0117  0.1149  34  SER D CB  
6643 O  OG  . SER D  34  ? 0.3240 0.2760 0.3443 0.0579  -0.0414 0.0306  34  SER D OG  
6644 N  N   . ASP D  35  ? 0.2149 0.2032 0.1600 0.0097  -0.0044 0.0237  35  ASP D N   
6645 C  CA  . ASP D  35  ? 0.2097 0.2475 0.1844 0.0364  0.0130  0.0087  35  ASP D CA  
6646 C  C   . ASP D  35  ? 0.2100 0.2497 0.1415 0.0258  0.0092  -0.0006 35  ASP D C   
6647 O  O   . ASP D  35  ? 0.2688 0.3097 0.1522 0.0351  -0.0157 0.0036  35  ASP D O   
6648 C  CB  . ASP D  35  ? 0.1910 0.3693 0.2836 0.0184  0.0055  0.0022  35  ASP D CB  
6649 C  CG  . ASP D  35  ? 0.2723 0.3644 0.2866 0.0730  0.0020  0.0414  35  ASP D CG  
6650 O  OD1 . ASP D  35  ? 0.2723 0.3790 0.3120 0.0480  0.0418  0.0970  35  ASP D OD1 
6651 O  OD2 . ASP D  35  ? 0.2509 0.4084 0.2406 0.0049  0.0086  0.0671  35  ASP D OD2 
6652 N  N   . ILE D  36  ? 0.2128 0.2152 0.1777 0.0319  0.0152  0.0379  36  ILE D N   
6653 C  CA  . ILE D  36  ? 0.1845 0.2210 0.1894 0.0267  0.0027  0.0130  36  ILE D CA  
6654 C  C   . ILE D  36  ? 0.1997 0.1773 0.1683 0.0287  0.0021  0.0319  36  ILE D C   
6655 O  O   . ILE D  36  ? 0.2321 0.2105 0.2332 0.0381  0.0089  0.0118  36  ILE D O   
6656 C  CB  . ILE D  36  ? 0.2828 0.2582 0.1657 -0.0185 0.0055  0.0407  36  ILE D CB  
6657 C  CG1 . ILE D  36  ? 0.3265 0.2764 0.2023 0.0324  -0.0225 0.0469  36  ILE D CG1 
6658 C  CG2 . ILE D  36  ? 0.2902 0.3547 0.2901 -0.0320 -0.0009 0.1075  36  ILE D CG2 
6659 C  CD1 . ILE D  36  ? 0.2798 0.2834 0.1924 0.0037  -0.0008 0.0062  36  ILE D CD1 
6660 N  N   . LEU D  37  ? 0.1823 0.2126 0.1621 -0.0035 0.0026  0.0361  37  LEU D N   
6661 C  CA  . LEU D  37  ? 0.1974 0.2004 0.1523 0.0154  0.0142  0.0403  37  LEU D CA  
6662 C  C   . LEU D  37  ? 0.2195 0.2336 0.1828 0.0647  0.0211  0.0572  37  LEU D C   
6663 O  O   . LEU D  37  ? 0.2283 0.2848 0.2139 0.0730  0.0284  0.0986  37  LEU D O   
6664 C  CB  . LEU D  37  ? 0.2146 0.1969 0.1694 0.0127  0.0122  0.0055  37  LEU D CB  
6665 C  CG  . LEU D  37  ? 0.2035 0.2508 0.1762 0.0288  0.0414  -0.0027 37  LEU D CG  
6666 C  CD1 . LEU D  37  ? 0.2731 0.2771 0.3015 0.1018  -0.0438 -0.0356 37  LEU D CD1 
6667 C  CD2 . LEU D  37  ? 0.2335 0.2192 0.1855 0.0080  0.0212  0.0343  37  LEU D CD2 
6668 N  N   . GLN D  38  ? 0.2013 0.2148 0.1523 0.0365  0.0377  0.0405  38  GLN D N   
6669 C  CA  . GLN D  38  ? 0.2149 0.2316 0.1625 0.0211  0.0388  0.0342  38  GLN D CA  
6670 C  C   . GLN D  38  ? 0.2068 0.1897 0.1442 0.0282  0.0402  0.0357  38  GLN D C   
6671 O  O   . GLN D  38  ? 0.2162 0.2124 0.1423 0.0424  0.0245  0.0460  38  GLN D O   
6672 C  CB  . GLN D  38  ? 0.2705 0.3322 0.1560 -0.0088 0.0055  0.0184  38  GLN D CB  
6673 C  CG  . GLN D  38  ? 0.3054 0.4659 0.1803 0.0006  0.0518  0.0071  38  GLN D CG  
6674 C  CD  . GLN D  38  ? 0.4555 0.6056 0.2451 0.0147  -0.1513 -0.0055 38  GLN D CD  
6675 O  OE1 . GLN D  38  ? 0.4323 0.8917 0.2178 0.0510  -0.0352 -0.0668 38  GLN D OE1 
6676 N  NE2 . GLN D  38  ? 0.5115 0.4609 0.2464 -0.0820 -0.0701 -0.0333 38  GLN D NE2 
6677 N  N   . TYR D  39  ? 0.2033 0.2004 0.1782 0.0379  0.0410  0.0606  39  TYR D N   
6678 C  CA  . TYR D  39  ? 0.1903 0.1701 0.1366 0.0412  0.0329  0.0330  39  TYR D CA  
6679 C  C   . TYR D  39  ? 0.2089 0.1671 0.1476 0.0108  0.0127  0.0357  39  TYR D C   
6680 O  O   . TYR D  39  ? 0.2335 0.2346 0.1452 0.0484  0.0173  0.0291  39  TYR D O   
6681 C  CB  . TYR D  39  ? 0.2325 0.1957 0.2087 0.0532  0.0314  0.0743  39  TYR D CB  
6682 C  CG  . TYR D  39  ? 0.2309 0.1781 0.1815 0.0430  0.0479  0.0403  39  TYR D CG  
6683 C  CD1 . TYR D  39  ? 0.2371 0.2202 0.1870 0.0247  0.0485  0.0454  39  TYR D CD1 
6684 C  CD2 . TYR D  39  ? 0.2712 0.1920 0.1807 0.0298  0.0392  0.0317  39  TYR D CD2 
6685 C  CE1 . TYR D  39  ? 0.2449 0.2081 0.2033 0.0217  0.0611  0.0408  39  TYR D CE1 
6686 C  CE2 . TYR D  39  ? 0.2825 0.1927 0.2128 0.0337  0.0560  0.0287  39  TYR D CE2 
6687 C  CZ  . TYR D  39  ? 0.2470 0.2123 0.2414 0.0088  0.0497  0.0472  39  TYR D CZ  
6688 O  OH  . TYR D  39  ? 0.2916 0.2494 0.2865 -0.0029 0.1089  0.0247  39  TYR D OH  
6689 N  N   . ASP D  40  ? 0.1790 0.1929 0.1491 0.0391  0.0488  0.0239  40  ASP D N   
6690 C  CA  . ASP D  40  ? 0.2073 0.1601 0.1721 0.0399  0.0509  0.0108  40  ASP D CA  
6691 C  C   . ASP D  40  ? 0.2000 0.1969 0.1560 0.0407  0.0298  0.0052  40  ASP D C   
6692 O  O   . ASP D  40  ? 0.2158 0.2170 0.1584 0.0535  0.0502  0.0089  40  ASP D O   
6693 C  CB  . ASP D  40  ? 0.2321 0.1560 0.1997 0.0199  0.0491  0.0286  40  ASP D CB  
6694 C  CG  . ASP D  40  ? 0.2971 0.1886 0.2254 0.0413  0.0408  0.0285  40  ASP D CG  
6695 O  OD1 . ASP D  40  ? 0.2143 0.2331 0.2371 0.0273  0.0394  -0.0114 40  ASP D OD1 
6696 O  OD2 . ASP D  40  ? 0.4025 0.2184 0.3116 0.0738  0.0505  0.0537  40  ASP D OD2 
6697 N  N   . ALA D  41  ? 0.2181 0.1720 0.1388 0.0248  0.0537  0.0053  41  ALA D N   
6698 C  CA  . ALA D  41  ? 0.2271 0.1666 0.1847 0.0168  0.0590  0.0263  41  ALA D CA  
6699 C  C   . ALA D  41  ? 0.2093 0.1983 0.1683 0.0015  0.0598  -0.0204 41  ALA D C   
6700 O  O   . ALA D  41  ? 0.2090 0.2049 0.2102 -0.0044 0.0509  -0.0059 41  ALA D O   
6701 C  CB  . ALA D  41  ? 0.2770 0.1961 0.1861 0.0211  0.0524  0.0328  41  ALA D CB  
6702 N  N   . SER D  42  ? 0.2353 0.1669 0.1656 0.0326  0.0671  0.0039  42  SER D N   
6703 C  CA  . SER D  42  ? 0.2420 0.2133 0.1872 0.0455  0.0819  -0.0075 42  SER D CA  
6704 C  C   . SER D  42  ? 0.2101 0.2329 0.2045 0.0409  0.0446  0.0088  42  SER D C   
6705 O  O   . SER D  42  ? 0.2172 0.2845 0.2786 0.0675  0.0557  0.0422  42  SER D O   
6706 C  CB  . SER D  42  ? 0.2852 0.1949 0.3387 0.0162  0.1132  -0.0172 42  SER D CB  
6707 O  OG  . SER D  42  ? 0.3276 0.2155 0.3414 0.0476  0.1205  0.0177  42  SER D OG  
6708 N  N   . LEU D  43  ? 0.2277 0.2128 0.1780 0.0347  0.0690  0.0320  43  LEU D N   
6709 C  CA  . LEU D  43  ? 0.2338 0.2529 0.1814 0.0276  0.0480  0.0469  43  LEU D CA  
6710 C  C   . LEU D  43  ? 0.1907 0.2441 0.2424 0.0348  0.0392  0.0217  43  LEU D C   
6711 O  O   . LEU D  43  ? 0.2316 0.2606 0.2242 0.0299  0.0608  0.0723  43  LEU D O   
6712 C  CB  . LEU D  43  ? 0.1901 0.2180 0.1641 0.0309  0.0497  0.0151  43  LEU D CB  
6713 C  CG  . LEU D  43  ? 0.1999 0.2626 0.2311 0.0315  0.0308  0.0651  43  LEU D CG  
6714 C  CD1 . LEU D  43  ? 0.2569 0.2297 0.1900 0.0545  0.0582  0.0370  43  LEU D CD1 
6715 C  CD2 . LEU D  43  ? 0.2512 0.2280 0.2434 0.0521  0.0212  0.0386  43  LEU D CD2 
6716 N  N   . THR D  44  ? 0.1969 0.2930 0.1993 0.0265  0.0425  0.0291  44  THR D N   
6717 C  CA  . THR D  44  ? 0.2026 0.2651 0.1984 0.0114  0.0134  0.0469  44  THR D CA  
6718 C  C   . THR D  44  ? 0.2277 0.2889 0.1685 -0.0030 0.0535  0.0254  44  THR D C   
6719 O  O   . THR D  44  ? 0.1841 0.2526 0.2096 0.0380  0.0428  0.0512  44  THR D O   
6720 C  CB  . THR D  44  ? 0.2366 0.3270 0.2072 0.0015  0.0637  0.0436  44  THR D CB  
6721 O  OG1 . THR D  44  ? 0.2630 0.3766 0.3257 0.0760  0.1066  0.0306  44  THR D OG1 
6722 C  CG2 . THR D  44  ? 0.2407 0.5374 0.1955 -0.0170 0.0603  0.0588  44  THR D CG2 
6723 N  N   . PRO D  45  ? 0.2065 0.2256 0.2085 0.0013  0.0115  0.0543  45  PRO D N   
6724 C  CA  . PRO D  45  ? 0.2420 0.2949 0.2250 0.0060  0.0245  0.0057  45  PRO D CA  
6725 C  C   . PRO D  45  ? 0.1678 0.2938 0.2361 0.0336  0.0322  0.0461  45  PRO D C   
6726 O  O   . PRO D  45  ? 0.2107 0.3620 0.2735 0.0552  0.0413  0.0456  45  PRO D O   
6727 C  CB  . PRO D  45  ? 0.2784 0.2454 0.3814 -0.0072 0.0301  0.0996  45  PRO D CB  
6728 C  CG  . PRO D  45  ? 0.2710 0.3384 0.2244 0.0370  0.0171  0.0336  45  PRO D CG  
6729 C  CD  . PRO D  45  ? 0.2688 0.2971 0.2257 -0.0424 0.0469  0.0760  45  PRO D CD  
6730 N  N   . LEU D  46  ? 0.2191 0.2788 0.2378 0.0270  0.0251  0.0913  46  LEU D N   
6731 C  CA  . LEU D  46  ? 0.2389 0.2362 0.2127 0.0644  0.0566  0.0451  46  LEU D CA  
6732 C  C   . LEU D  46  ? 0.2539 0.2838 0.2238 0.0578  0.0672  0.0806  46  LEU D C   
6733 O  O   . LEU D  46  ? 0.1830 0.2828 0.2843 0.0209  0.0284  0.0691  46  LEU D O   
6734 C  CB  . LEU D  46  ? 0.2359 0.2644 0.2521 0.0403  0.0526  0.0862  46  LEU D CB  
6735 C  CG  . LEU D  46  ? 0.2628 0.2431 0.2718 0.0548  0.0431  0.0179  46  LEU D CG  
6736 C  CD1 . LEU D  46  ? 0.3053 0.2674 0.3391 0.0131  0.0173  0.0817  46  LEU D CD1 
6737 C  CD2 . LEU D  46  ? 0.3838 0.3173 0.4099 0.1295  0.0553  -0.0693 46  LEU D CD2 
6738 N  N   . GLU D  47  ? 0.2365 0.3796 0.2732 0.1033  0.0820  0.1815  47  GLU D N   
6739 C  CA  . GLU D  47  ? 0.2378 0.4527 0.2475 0.0550  0.0893  0.1566  47  GLU D CA  
6740 C  C   . GLU D  47  ? 0.2280 0.3327 0.2710 0.0305  0.0763  0.1031  47  GLU D C   
6741 O  O   . GLU D  47  ? 0.2979 0.3564 0.2327 0.0643  0.0776  0.0920  47  GLU D O   
6742 C  CB  . GLU D  47  ? 0.1992 0.4459 0.3565 0.0687  0.1014  0.2019  47  GLU D CB  
6743 C  CG  . GLU D  47  ? 0.1992 0.5582 0.4529 0.0684  0.0805  0.2849  47  GLU D CG  
6744 C  CD  . GLU D  47  ? 0.2712 0.7893 0.6172 0.0220  0.1333  0.2387  47  GLU D CD  
6745 O  OE1 . GLU D  47  ? 0.2827 1.0784 0.6036 0.1220  0.0732  0.0814  47  GLU D OE1 
6746 O  OE2 . GLU D  47  ? 0.5546 1.1135 0.6634 -0.0601 -0.0199 0.3407  47  GLU D OE2 
6747 N  N   . PHE D  48  ? 0.2217 0.2782 0.2877 0.0472  0.0855  0.1030  48  PHE D N   
6748 C  CA  . PHE D  48  ? 0.2285 0.2120 0.2474 0.0462  0.0604  0.0744  48  PHE D CA  
6749 C  C   . PHE D  48  ? 0.2159 0.3215 0.3920 0.0342  0.1089  0.0722  48  PHE D C   
6750 O  O   . PHE D  48  ? 0.2893 0.2796 0.4762 0.0737  0.0034  0.1080  48  PHE D O   
6751 C  CB  . PHE D  48  ? 0.2334 0.2332 0.2676 0.0062  0.0250  0.0411  48  PHE D CB  
6752 C  CG  . PHE D  48  ? 0.2482 0.2211 0.2020 0.0124  0.0429  0.0517  48  PHE D CG  
6753 C  CD1 . PHE D  48  ? 0.2050 0.2504 0.2109 0.0142  0.0668  0.0195  48  PHE D CD1 
6754 C  CD2 . PHE D  48  ? 0.2506 0.2025 0.2929 0.0226  0.0353  0.0377  48  PHE D CD2 
6755 C  CE1 . PHE D  48  ? 0.2354 0.2662 0.2131 0.0212  0.0640  0.0585  48  PHE D CE1 
6756 C  CE2 . PHE D  48  ? 0.2759 0.2615 0.2635 0.0122  0.0621  0.0699  48  PHE D CE2 
6757 C  CZ  . PHE D  48  ? 0.2257 0.2275 0.3001 0.0065  0.1126  0.0179  48  PHE D CZ  
6758 N  N   . GLN D  49  ? 0.1755 0.2435 0.3024 0.0549  0.0952  0.0907  49  GLN D N   
6759 C  CA  . GLN D  49  ? 0.1948 0.3257 0.3110 0.0420  0.0819  0.1103  49  GLN D CA  
6760 C  C   . GLN D  49  ? 0.1835 0.2358 0.2815 0.0454  0.0675  0.0683  49  GLN D C   
6761 O  O   . GLN D  49  ? 0.2001 0.2197 0.2781 0.0352  0.0666  0.0632  49  GLN D O   
6762 C  CB  . GLN D  49  ? 0.2342 0.3491 0.3107 0.0626  0.1336  0.0943  49  GLN D CB  
6763 C  CG  . GLN D  49  ? 0.2878 0.3131 0.2693 0.0283  0.0519  0.0769  49  GLN D CG  
6764 C  CD  . GLN D  49  ? 0.2633 0.4283 0.2866 -0.0092 0.0475  0.1436  49  GLN D CD  
6765 O  OE1 . GLN D  49  ? 0.2370 0.7808 0.5906 0.0666  0.0692  0.1975  49  GLN D OE1 
6766 N  NE2 . GLN D  49  ? 0.3642 0.4380 0.4279 0.1143  0.0932  0.0728  49  GLN D NE2 
6767 N  N   . GLY D  50  ? 0.1656 0.2815 0.2693 0.0364  0.0845  0.0675  50  GLY D N   
6768 C  CA  . GLY D  50  ? 0.1555 0.3334 0.3121 0.0425  0.1087  0.0948  50  GLY D CA  
6769 C  C   . GLY D  50  ? 0.1418 0.2482 0.2737 0.0361  0.0623  0.0694  50  GLY D C   
6770 O  O   . GLY D  50  ? 0.1646 0.2447 0.2791 0.0339  0.0575  0.0582  50  GLY D O   
6771 N  N   . TYR D  51  ? 0.1443 0.2400 0.2940 0.0187  0.0702  0.0507  51  TYR D N   
6772 C  CA  . TYR D  51  ? 0.1311 0.1930 0.2584 0.0187  0.0543  0.0091  51  TYR D CA  
6773 C  C   . TYR D  51  ? 0.1642 0.1903 0.2597 -0.0263 0.0174  0.0440  51  TYR D C   
6774 O  O   . TYR D  51  ? 0.1358 0.2157 0.2557 -0.0064 0.0241  0.0234  51  TYR D O   
6775 C  CB  . TYR D  51  ? 0.1669 0.1780 0.2758 -0.0031 0.0511  0.0228  51  TYR D CB  
6776 C  CG  . TYR D  51  ? 0.1578 0.1667 0.2183 -0.0248 0.0510  0.0286  51  TYR D CG  
6777 C  CD1 . TYR D  51  ? 0.1697 0.1929 0.2446 0.0138  0.0550  0.0175  51  TYR D CD1 
6778 C  CD2 . TYR D  51  ? 0.1399 0.1606 0.2196 -0.0117 0.0381  0.0174  51  TYR D CD2 
6779 C  CE1 . TYR D  51  ? 0.1592 0.2066 0.2040 0.0365  0.0373  0.0383  51  TYR D CE1 
6780 C  CE2 . TYR D  51  ? 0.1513 0.1643 0.1963 -0.0050 0.0294  -0.0071 51  TYR D CE2 
6781 C  CZ  . TYR D  51  ? 0.1606 0.1719 0.2231 0.0287  -0.0042 0.0047  51  TYR D CZ  
6782 O  OH  . TYR D  51  ? 0.1939 0.2190 0.2294 0.0356  -0.0017 -0.0203 51  TYR D OH  
6783 N  N   . ASN D  52  ? 0.1592 0.2223 0.3066 -0.0134 0.0155  0.0185  52  ASN D N   
6784 C  CA  . ASN D  52  ? 0.1858 0.2010 0.3153 -0.0443 0.0325  0.0554  52  ASN D CA  
6785 C  C   . ASN D  52  ? 0.1846 0.2437 0.2799 0.0178  0.0586  0.0596  52  ASN D C   
6786 O  O   . ASN D  52  ? 0.1726 0.2839 0.3664 0.0070  0.0656  0.0855  52  ASN D O   
6787 C  CB  . ASN D  52  ? 0.1832 0.2551 0.3289 -0.0639 0.0313  0.0377  52  ASN D CB  
6788 C  CG  . ASN D  52  ? 0.2330 0.2290 0.3554 -0.0584 -0.0320 0.0359  52  ASN D CG  
6789 O  OD1 . ASN D  52  ? 0.4355 0.3919 0.3843 -0.1769 0.0193  -0.0141 52  ASN D OD1 
6790 N  ND2 . ASN D  52  ? 0.3931 0.3073 0.5728 -0.1506 0.0013  0.0484  52  ASN D ND2 
6791 N  N   . LEU D  53  ? 0.1893 0.2001 0.2901 -0.0297 0.0394  0.0319  53  LEU D N   
6792 C  CA  . LEU D  53  ? 0.1763 0.1781 0.2577 -0.0157 0.0084  0.0012  53  LEU D CA  
6793 C  C   . LEU D  53  ? 0.1707 0.2036 0.2412 -0.0034 0.0266  -0.0170 53  LEU D C   
6794 O  O   . LEU D  53  ? 0.2268 0.2203 0.3069 -0.0031 0.0484  -0.0331 53  LEU D O   
6795 C  CB  . LEU D  53  ? 0.1556 0.1861 0.2759 -0.0022 0.0150  0.0017  53  LEU D CB  
6796 C  CG  . LEU D  53  ? 0.1690 0.1835 0.2918 -0.0143 -0.0011 0.0276  53  LEU D CG  
6797 C  CD1 . LEU D  53  ? 0.1895 0.2498 0.3046 -0.0467 -0.0104 0.0573  53  LEU D CD1 
6798 C  CD2 . LEU D  53  ? 0.2718 0.2456 0.2730 -0.0074 0.0258  0.0150  53  LEU D CD2 
6799 N  N   . SER D  54  ? 0.1736 0.2780 0.2338 -0.0106 0.0266  0.0041  54  SER D N   
6800 C  CA  . SER D  54  ? 0.1930 0.2517 0.2811 -0.0098 0.0114  -0.0365 54  SER D CA  
6801 C  C   . SER D  54  ? 0.1928 0.2355 0.2539 -0.0351 0.0580  -0.0140 54  SER D C   
6802 O  O   . SER D  54  ? 0.1967 0.2420 0.2484 -0.0373 0.0509  -0.0288 54  SER D O   
6803 C  CB  . SER D  54  ? 0.1673 0.2892 0.2856 0.0184  -0.0183 -0.0475 54  SER D CB  
6804 O  OG  . SER D  54  ? 0.1900 0.3948 0.2694 -0.0330 0.0340  -0.0530 54  SER D OG  
6805 N  N   . ALA D  55  ? 0.2473 0.3281 0.2496 -0.1026 0.0401  -0.0337 55  ALA D N   
6806 C  CA  . ALA D  55  ? 0.3089 0.2248 0.2554 -0.0478 0.0783  -0.0568 55  ALA D CA  
6807 C  C   . ALA D  55  ? 0.2438 0.3197 0.2415 -0.0201 0.0432  -0.0344 55  ALA D C   
6808 O  O   . ALA D  55  ? 0.2493 0.3267 0.2487 -0.0380 0.0440  -0.0587 55  ALA D O   
6809 C  CB  . ALA D  55  ? 0.6381 0.2426 0.2369 -0.0599 0.0395  -0.0428 55  ALA D CB  
6810 N  N   . ASN D  56  ? 0.1967 0.3660 0.3001 -0.0284 0.0306  -0.0486 56  ASN D N   
6811 C  CA  . ASN D  56  ? 0.2506 0.3938 0.2505 -0.0377 0.0694  -0.0392 56  ASN D CA  
6812 C  C   . ASN D  56  ? 0.1682 0.3387 0.3537 -0.0265 0.0358  0.0558  56  ASN D C   
6813 O  O   . ASN D  56  ? 0.2654 0.3177 0.5600 -0.0374 -0.0753 0.0587  56  ASN D O   
6814 C  CB  . ASN D  56  ? 0.1870 0.4394 0.2694 -0.0500 -0.0234 -0.0370 56  ASN D CB  
6815 C  CG  . ASN D  56  ? 0.4794 0.5631 0.5535 -0.1254 0.0296  -0.2218 56  ASN D CG  
6816 O  OD1 . ASN D  56  ? 0.3637 0.7434 0.5287 -0.0427 -0.0775 -0.3028 56  ASN D OD1 
6817 N  ND2 . ASN D  56  ? 0.8201 0.8585 0.4543 -0.4765 0.1744  -0.2032 56  ASN D ND2 
6818 N  N   A LYS D  57  ? 0.1628 0.3556 0.2782 0.0063  0.0073  -0.0210 57  LYS D N   
6819 N  N   B LYS D  57  ? 0.1439 0.3313 0.2375 -0.0316 0.0498  -0.0326 57  LYS D N   
6820 C  CA  A LYS D  57  ? 0.1711 0.2936 0.3234 0.0533  0.0289  0.0264  57  LYS D CA  
6821 C  CA  B LYS D  57  ? 0.1463 0.2799 0.2915 0.0231  0.0357  0.0210  57  LYS D CA  
6822 C  C   A LYS D  57  ? 0.1640 0.2604 0.3075 0.0186  0.0044  0.0111  57  LYS D C   
6823 C  C   B LYS D  57  ? 0.1581 0.2531 0.2459 0.0230  0.0228  0.0162  57  LYS D C   
6824 O  O   A LYS D  57  ? 0.2287 0.2347 0.2629 0.0482  0.0032  0.0373  57  LYS D O   
6825 O  O   B LYS D  57  ? 0.1574 0.2469 0.2206 0.0147  0.0290  0.0324  57  LYS D O   
6826 C  CB  A LYS D  57  ? 0.2063 0.2790 0.3055 -0.0013 0.0515  -0.0407 57  LYS D CB  
6827 C  CB  B LYS D  57  ? 0.1967 0.2157 0.2755 0.0254  0.0413  0.0212  57  LYS D CB  
6828 C  CG  A LYS D  57  ? 0.2015 0.3084 0.3705 0.1056  0.0122  -0.0015 57  LYS D CG  
6829 C  CG  B LYS D  57  ? 0.2502 0.2698 0.2888 0.0141  0.0732  0.0267  57  LYS D CG  
6830 C  CD  A LYS D  57  ? 0.3971 0.3415 0.3016 0.0046  0.1070  0.0335  57  LYS D CD  
6831 C  CD  B LYS D  57  ? 0.2316 0.3615 0.3397 0.0019  0.0581  -0.0245 57  LYS D CD  
6832 C  CE  A LYS D  57  ? 0.4162 0.4184 0.5779 0.0211  0.1247  0.0310  57  LYS D CE  
6833 C  CE  B LYS D  57  ? 0.2041 0.3847 0.3551 -0.0735 0.0186  0.0362  57  LYS D CE  
6834 N  NZ  A LYS D  57  ? 0.2370 0.3177 0.4665 -0.0287 0.1195  -0.0655 57  LYS D NZ  
6835 N  NZ  B LYS D  57  ? 0.3970 0.4915 0.3507 0.0703  -0.1072 0.0074  57  LYS D NZ  
6836 N  N   . GLN D  58  ? 0.1624 0.2879 0.2705 0.0114  -0.0023 0.0188  58  GLN D N   
6837 C  CA  . GLN D  58  ? 0.1369 0.3446 0.2320 -0.0172 0.0050  0.0177  58  GLN D CA  
6838 C  C   . GLN D  58  ? 0.1928 0.2133 0.2412 0.0124  0.0165  -0.0137 58  GLN D C   
6839 O  O   . GLN D  58  ? 0.1814 0.2518 0.2471 0.0161  -0.0027 -0.0035 58  GLN D O   
6840 C  CB  . GLN D  58  ? 0.1753 0.6276 0.2366 -0.0363 -0.0145 0.0424  58  GLN D CB  
6841 C  CG  . GLN D  58  ? 0.3518 0.5238 0.4646 0.0970  0.0498  0.2350  58  GLN D CG  
6842 C  CD  . GLN D  58  ? 0.4062 0.4753 0.3598 0.0307  -0.0125 0.0886  58  GLN D CD  
6843 O  OE1 . GLN D  58  ? 0.3226 0.4260 0.3766 -0.0706 -0.0606 -0.0290 58  GLN D OE1 
6844 N  NE2 . GLN D  58  ? 0.3167 0.4491 0.7373 -0.0753 -0.1518 0.0128  58  GLN D NE2 
6845 N  N   . PHE D  59  ? 0.1595 0.2023 0.2245 0.0039  -0.0065 0.0094  59  PHE D N   
6846 C  CA  . PHE D  59  ? 0.1627 0.2185 0.1818 -0.0066 0.0043  0.0103  59  PHE D CA  
6847 C  C   . PHE D  59  ? 0.1707 0.1798 0.1722 0.0079  -0.0039 0.0043  59  PHE D C   
6848 O  O   . PHE D  59  ? 0.1632 0.2117 0.1921 -0.0128 -0.0027 -0.0089 59  PHE D O   
6849 C  CB  . PHE D  59  ? 0.1536 0.1898 0.2181 0.0061  0.0058  -0.0024 59  PHE D CB  
6850 C  CG  . PHE D  59  ? 0.1539 0.1680 0.2155 0.0044  0.0208  0.0147  59  PHE D CG  
6851 C  CD1 . PHE D  59  ? 0.1585 0.2125 0.1984 0.0003  0.0053  0.0299  59  PHE D CD1 
6852 C  CD2 . PHE D  59  ? 0.1904 0.2249 0.1926 0.0055  0.0183  0.0082  59  PHE D CD2 
6853 C  CE1 . PHE D  59  ? 0.1564 0.2141 0.2035 0.0030  0.0259  0.0221  59  PHE D CE1 
6854 C  CE2 . PHE D  59  ? 0.1893 0.2262 0.2169 0.0031  0.0076  -0.0005 59  PHE D CE2 
6855 C  CZ  . PHE D  59  ? 0.1860 0.2241 0.2339 0.0004  0.0318  0.0055  59  PHE D CZ  
6856 N  N   . LEU D  60  ? 0.1599 0.1773 0.1956 0.0082  -0.0051 0.0313  60  LEU D N   
6857 C  CA  . LEU D  60  ? 0.1539 0.1806 0.2312 -0.0024 -0.0044 0.0418  60  LEU D CA  
6858 C  C   . LEU D  60  ? 0.1552 0.1779 0.1782 0.0050  -0.0374 0.0194  60  LEU D C   
6859 O  O   . LEU D  60  ? 0.1533 0.2134 0.1782 0.0089  -0.0298 0.0128  60  LEU D O   
6860 C  CB  . LEU D  60  ? 0.1782 0.1759 0.3101 -0.0168 0.0065  0.0317  60  LEU D CB  
6861 C  CG  . LEU D  60  ? 0.2558 0.2460 0.3572 -0.0288 0.0214  0.0793  60  LEU D CG  
6862 C  CD1 . LEU D  60  ? 0.3269 0.2763 0.3068 0.0136  0.0173  0.0954  60  LEU D CD1 
6863 C  CD2 . LEU D  60  ? 0.3827 0.2342 0.5273 -0.1051 0.0030  0.0784  60  LEU D CD2 
6864 N  N   . LEU D  61  ? 0.1470 0.2114 0.1676 -0.0084 -0.0139 0.0129  61  LEU D N   
6865 C  CA  . LEU D  61  ? 0.1454 0.1643 0.1779 -0.0143 -0.0061 0.0300  61  LEU D CA  
6866 C  C   . LEU D  61  ? 0.1412 0.1854 0.1586 -0.0097 -0.0216 0.0256  61  LEU D C   
6867 O  O   . LEU D  61  ? 0.1752 0.2638 0.1825 -0.0299 -0.0473 0.0582  61  LEU D O   
6868 C  CB  . LEU D  61  ? 0.1740 0.1973 0.1861 -0.0282 -0.0137 0.0031  61  LEU D CB  
6869 C  CG  . LEU D  61  ? 0.1927 0.2011 0.1632 -0.0258 0.0070  -0.0162 61  LEU D CG  
6870 C  CD1 . LEU D  61  ? 0.2430 0.1758 0.1928 -0.0277 -0.0044 -0.0102 61  LEU D CD1 
6871 C  CD2 . LEU D  61  ? 0.2459 0.2439 0.2088 -0.0350 -0.0227 -0.0446 61  LEU D CD2 
6872 N  N   . THR D  62  ? 0.1264 0.2103 0.1766 -0.0225 -0.0150 0.0321  62  THR D N   
6873 C  CA  . THR D  62  ? 0.1348 0.1940 0.2110 -0.0160 -0.0181 0.0565  62  THR D CA  
6874 C  C   . THR D  62  ? 0.1659 0.1619 0.2301 -0.0263 -0.0094 0.0619  62  THR D C   
6875 O  O   . THR D  62  ? 0.1571 0.2249 0.2056 0.0078  0.0046  0.0626  62  THR D O   
6876 C  CB  . THR D  62  ? 0.2205 0.1384 0.3852 0.0067  0.0904  0.0104  62  THR D CB  
6877 O  OG1 . THR D  62  ? 0.2592 0.2557 0.3702 0.0004  0.0041  0.0315  62  THR D OG1 
6878 C  CG2 . THR D  62  ? 0.2740 0.2017 0.5195 -0.0176 0.1086  0.0537  62  THR D CG2 
6879 N  N   . ASN D  63  ? 0.1651 0.2020 0.1863 -0.0311 0.0003  0.0546  63  ASN D N   
6880 C  CA  . ASN D  63  ? 0.1733 0.1719 0.2060 -0.0407 0.0097  0.0301  63  ASN D CA  
6881 C  C   . ASN D  63  ? 0.1921 0.1691 0.2009 -0.0164 0.0285  0.0301  63  ASN D C   
6882 O  O   . ASN D  63  ? 0.1946 0.1753 0.2432 -0.0203 -0.0067 0.0352  63  ASN D O   
6883 C  CB  . ASN D  63  ? 0.1762 0.2315 0.1981 -0.0131 0.0176  0.0587  63  ASN D CB  
6884 C  CG  . ASN D  63  ? 0.1912 0.1807 0.1786 -0.0318 0.0139  0.0127  63  ASN D CG  
6885 O  OD1 . ASN D  63  ? 0.1806 0.1929 0.2055 -0.0160 -0.0015 0.0305  63  ASN D OD1 
6886 N  ND2 . ASN D  63  ? 0.2295 0.1643 0.2160 0.0105  0.0155  0.0460  63  ASN D ND2 
6887 N  N   . ASN D  64  ? 0.1766 0.1885 0.2007 -0.0036 -0.0074 0.0130  64  ASN D N   
6888 C  CA  . ASN D  64  ? 0.2130 0.2162 0.2287 -0.0336 0.0068  -0.0104 64  ASN D CA  
6889 C  C   . ASN D  64  ? 0.2169 0.2063 0.2229 -0.0111 -0.0385 0.0184  64  ASN D C   
6890 O  O   . ASN D  64  ? 0.2475 0.2049 0.2243 -0.0139 -0.0265 0.0189  64  ASN D O   
6891 C  CB  . ASN D  64  ? 0.2386 0.1800 0.2250 0.0456  -0.0241 -0.0153 64  ASN D CB  
6892 C  CG  . ASN D  64  ? 0.1706 0.1976 0.2073 -0.0242 -0.0031 0.0009  64  ASN D CG  
6893 O  OD1 . ASN D  64  ? 0.2218 0.1724 0.2122 0.0042  0.0250  0.0034  64  ASN D OD1 
6894 N  ND2 . ASN D  64  ? 0.2532 0.2986 0.1992 -0.0407 0.0301  -0.0153 64  ASN D ND2 
6895 N  N   . GLY D  65  ? 0.1718 0.2110 0.1828 -0.0126 -0.0078 0.0465  65  GLY D N   
6896 C  CA  . GLY D  65  ? 0.1769 0.2622 0.1994 -0.0335 -0.0264 0.0558  65  GLY D CA  
6897 C  C   . GLY D  65  ? 0.2120 0.2266 0.1775 -0.0018 -0.0073 0.0398  65  GLY D C   
6898 O  O   . GLY D  65  ? 0.1893 0.3595 0.2432 -0.0226 -0.0092 0.0970  65  GLY D O   
6899 N  N   . HIS D  66  ? 0.1998 0.1582 0.1627 -0.0183 -0.0184 0.0160  66  HIS D N   
6900 C  CA  . HIS D  66  ? 0.1943 0.1681 0.1791 -0.0174 -0.0315 0.0310  66  HIS D CA  
6901 C  C   . HIS D  66  ? 0.1663 0.1679 0.1906 -0.0080 -0.0145 0.0146  66  HIS D C   
6902 O  O   . HIS D  66  ? 0.1938 0.1572 0.2057 0.0027  -0.0278 -0.0055 66  HIS D O   
6903 C  CB  . HIS D  66  ? 0.3326 0.1938 0.1734 -0.0064 -0.0345 0.0274  66  HIS D CB  
6904 C  CG  . HIS D  66  ? 0.2944 0.2528 0.1786 -0.0049 -0.0100 -0.0086 66  HIS D CG  
6905 N  ND1 . HIS D  66  ? 0.3655 0.2186 0.1676 -0.0405 -0.0348 0.0205  66  HIS D ND1 
6906 C  CD2 . HIS D  66  ? 0.2878 0.3227 0.1654 0.0037  -0.0455 0.0283  66  HIS D CD2 
6907 C  CE1 . HIS D  66  ? 0.2907 0.1939 0.2169 -0.0537 -0.0372 0.0243  66  HIS D CE1 
6908 N  NE2 . HIS D  66  ? 0.3013 0.2463 0.2279 -0.0454 -0.0115 0.0403  66  HIS D NE2 
6909 N  N   . SER D  67  ? 0.1651 0.1515 0.2013 -0.0166 -0.0044 -0.0003 67  SER D N   
6910 C  CA  . SER D  67  ? 0.1514 0.1514 0.1584 -0.0150 -0.0186 0.0145  67  SER D CA  
6911 C  C   . SER D  67  ? 0.1653 0.1408 0.1538 -0.0006 0.0002  0.0234  67  SER D C   
6912 O  O   . SER D  67  ? 0.1748 0.1623 0.1861 -0.0068 -0.0165 0.0229  67  SER D O   
6913 C  CB  . SER D  67  ? 0.1965 0.1380 0.1815 -0.0013 0.0155  0.0279  67  SER D CB  
6914 O  OG  . SER D  67  ? 0.1718 0.1764 0.1822 -0.0128 -0.0048 0.0266  67  SER D OG  
6915 N  N   . VAL D  68  ? 0.1527 0.1721 0.1701 -0.0184 -0.0111 0.0156  68  VAL D N   
6916 C  CA  . VAL D  68  ? 0.1398 0.2331 0.1789 0.0043  0.0075  -0.0109 68  VAL D CA  
6917 C  C   . VAL D  68  ? 0.1469 0.1606 0.1808 0.0076  0.0067  0.0434  68  VAL D C   
6918 O  O   . VAL D  68  ? 0.1654 0.1717 0.1627 0.0082  0.0016  0.0113  68  VAL D O   
6919 C  CB  . VAL D  68  ? 0.2059 0.2221 0.1650 -0.0030 0.0193  0.0116  68  VAL D CB  
6920 C  CG1 . VAL D  68  ? 0.1953 0.1984 0.2169 -0.0042 0.0133  -0.0463 68  VAL D CG1 
6921 C  CG2 . VAL D  68  ? 0.2099 0.3448 0.2346 0.0473  -0.0267 0.0185  68  VAL D CG2 
6922 N  N   . LYS D  69  ? 0.1537 0.1824 0.1703 0.0109  -0.0026 0.0228  69  LYS D N   
6923 C  CA  . LYS D  69  ? 0.1429 0.1605 0.1571 -0.0234 -0.0093 0.0042  69  LYS D CA  
6924 C  C   . LYS D  69  ? 0.1415 0.1381 0.1423 -0.0027 -0.0058 0.0330  69  LYS D C   
6925 O  O   . LYS D  69  ? 0.1435 0.2332 0.1666 -0.0131 -0.0177 0.0515  69  LYS D O   
6926 C  CB  . LYS D  69  ? 0.2031 0.2076 0.2922 -0.0227 -0.0458 -0.0462 69  LYS D CB  
6927 C  CG  . LYS D  69  ? 0.3402 0.2764 0.4280 -0.0280 -0.0721 -0.0966 69  LYS D CG  
6928 C  CD  . LYS D  69  ? 0.3104 0.2494 0.3989 -0.0340 0.0478  -0.1086 69  LYS D CD  
6929 C  CE  . LYS D  69  ? 0.3516 0.3091 0.3943 -0.0369 -0.0198 -0.0161 69  LYS D CE  
6930 N  NZ  . LYS D  69  ? 0.4381 0.2328 0.3592 -0.0039 0.0049  -0.0661 69  LYS D NZ  
6931 N  N   . LEU D  70  ? 0.1280 0.1436 0.1455 0.0002  0.0034  0.0080  70  LEU D N   
6932 C  CA  . LEU D  70  ? 0.1259 0.1298 0.1612 0.0099  0.0050  0.0073  70  LEU D CA  
6933 C  C   . LEU D  70  ? 0.1332 0.1485 0.1351 0.0044  -0.0139 0.0120  70  LEU D C   
6934 O  O   . LEU D  70  ? 0.1500 0.1539 0.1433 0.0107  -0.0118 0.0093  70  LEU D O   
6935 C  CB  . LEU D  70  ? 0.1522 0.1209 0.1799 -0.0071 -0.0086 0.0079  70  LEU D CB  
6936 C  CG  . LEU D  70  ? 0.1396 0.1662 0.1633 0.0088  0.0000  -0.0088 70  LEU D CG  
6937 C  CD1 . LEU D  70  ? 0.1525 0.2020 0.1852 -0.0097 -0.0253 -0.0159 70  LEU D CD1 
6938 C  CD2 . LEU D  70  ? 0.1843 0.1571 0.2150 -0.0186 -0.0174 -0.0010 70  LEU D CD2 
6939 N  N   . ASN D  71  ? 0.1429 0.1412 0.1591 0.0171  -0.0036 0.0129  71  ASN D N   
6940 C  CA  . ASN D  71  ? 0.1517 0.1480 0.1883 0.0215  0.0255  0.0190  71  ASN D CA  
6941 C  C   . ASN D  71  ? 0.1715 0.1477 0.1926 0.0131  0.0291  0.0081  71  ASN D C   
6942 O  O   . ASN D  71  ? 0.1908 0.2213 0.1890 -0.0125 0.0183  -0.0111 71  ASN D O   
6943 C  CB  . ASN D  71  ? 0.2623 0.1789 0.2224 0.0521  0.0113  -0.0074 71  ASN D CB  
6944 C  CG  . ASN D  71  ? 0.3028 0.1995 0.2582 0.0695  0.0436  -0.0080 71  ASN D CG  
6945 O  OD1 . ASN D  71  ? 0.3067 0.2303 0.3280 -0.0195 0.0494  -0.0011 71  ASN D OD1 
6946 N  ND2 . ASN D  71  ? 0.3807 0.2350 0.3741 0.1047  0.0730  0.0499  71  ASN D ND2 
6947 N  N   . LEU D  72  ? 0.1729 0.1339 0.1786 0.0122  0.0102  0.0133  72  LEU D N   
6948 C  CA  . LEU D  72  ? 0.1629 0.1638 0.1887 0.0310  0.0278  0.0113  72  LEU D CA  
6949 C  C   . LEU D  72  ? 0.1806 0.1689 0.1546 0.0269  0.0099  -0.0080 72  LEU D C   
6950 O  O   . LEU D  72  ? 0.1976 0.1707 0.2183 0.0277  0.0366  -0.0069 72  LEU D O   
6951 C  CB  . LEU D  72  ? 0.1521 0.1514 0.1960 0.0346  0.0223  0.0077  72  LEU D CB  
6952 C  CG  . LEU D  72  ? 0.1903 0.1427 0.1867 0.0236  0.0077  0.0010  72  LEU D CG  
6953 C  CD1 . LEU D  72  ? 0.1293 0.1536 0.1928 0.0044  0.0182  0.0200  72  LEU D CD1 
6954 C  CD2 . LEU D  72  ? 0.1794 0.1516 0.1976 0.0040  0.0219  -0.0271 72  LEU D CD2 
6955 N  N   . PRO D  73  ? 0.1691 0.1653 0.2028 0.0343  0.0394  0.0109  73  PRO D N   
6956 C  CA  . PRO D  73  ? 0.1894 0.1752 0.2182 0.0491  0.0484  0.0243  73  PRO D CA  
6957 C  C   . PRO D  73  ? 0.2321 0.2046 0.2104 0.0108  0.0608  0.0151  73  PRO D C   
6958 O  O   . PRO D  73  ? 0.2503 0.2236 0.2366 0.0355  0.0744  0.0320  73  PRO D O   
6959 C  CB  . PRO D  73  ? 0.1993 0.2153 0.2798 0.0340  0.0556  0.0135  73  PRO D CB  
6960 C  CG  . PRO D  73  ? 0.1670 0.2112 0.2749 0.0183  0.0354  -0.0001 73  PRO D CG  
6961 C  CD  . PRO D  73  ? 0.1650 0.1879 0.2347 0.0241  0.0063  0.0069  73  PRO D CD  
6962 N  N   . SER D  74  ? 0.2643 0.2436 0.2136 0.0534  0.0763  -0.0161 74  SER D N   
6963 C  CA  . SER D  74  ? 0.2779 0.2341 0.2214 0.0618  0.0822  0.0113  74  SER D CA  
6964 C  C   . SER D  74  ? 0.2824 0.2253 0.2426 0.0668  0.0688  0.0251  74  SER D C   
6965 O  O   . SER D  74  ? 0.2627 0.3278 0.2408 0.0636  0.0540  0.0019  74  SER D O   
6966 C  CB  . SER D  74  ? 0.3553 0.2764 0.3246 0.1054  0.0646  -0.0436 74  SER D CB  
6967 O  OG  . SER D  74  ? 0.3773 0.3129 0.3078 0.1201  0.0484  -0.0168 74  SER D OG  
6968 N  N   . ASP D  75  ? 0.2259 0.2621 0.2741 0.0551  0.0690  0.0463  75  ASP D N   
6969 C  CA  . ASP D  75  ? 0.2341 0.2642 0.2599 0.0749  0.0971  0.0615  75  ASP D CA  
6970 C  C   . ASP D  75  ? 0.2443 0.2718 0.2903 0.0773  0.0796  0.0878  75  ASP D C   
6971 O  O   . ASP D  75  ? 0.2368 0.3280 0.2876 0.0807  0.0767  0.1152  75  ASP D O   
6972 C  CB  . ASP D  75  ? 0.2086 0.3825 0.4131 0.0428  0.0315  0.1145  75  ASP D CB  
6973 C  CG  . ASP D  75  ? 0.4018 0.5492 0.4904 -0.1272 0.1011  0.0976  75  ASP D CG  
6974 O  OD1 . ASP D  75  ? 0.5137 0.5881 0.6596 -0.1160 0.2543  0.1043  75  ASP D OD1 
6975 O  OD2 . ASP D  75  ? 0.5851 0.7019 1.1179 -0.2780 0.0769  -0.2352 75  ASP D OD2 
6976 N  N   . MET D  76  ? 0.2249 0.2590 0.2449 0.0593  0.0624  0.0605  76  MET D N   
6977 C  CA  . MET D  76  ? 0.1998 0.2516 0.2415 0.0240  0.0807  0.0552  76  MET D CA  
6978 C  C   . MET D  76  ? 0.1802 0.2144 0.2697 0.0681  0.0767  0.0646  76  MET D C   
6979 O  O   . MET D  76  ? 0.1999 0.2302 0.2421 0.0410  0.0812  0.0307  76  MET D O   
6980 C  CB  . MET D  76  ? 0.2209 0.2164 0.2559 0.0369  0.0556  0.0375  76  MET D CB  
6981 C  CG  . MET D  76  ? 0.2146 0.2569 0.2874 0.0354  0.1074  0.0442  76  MET D CG  
6982 S  SD  . MET D  76  ? 0.2010 0.2269 0.2680 -0.0038 0.0646  -0.0030 76  MET D SD  
6983 C  CE  . MET D  76  ? 0.2128 0.2000 0.2474 0.0013  0.0717  0.0192  76  MET D CE  
6984 N  N   . HIS D  77  ? 0.1817 0.2666 0.2327 0.0797  0.0718  0.0695  77  HIS D N   
6985 C  CA  . HIS D  77  ? 0.2334 0.2022 0.2561 0.0731  0.0798  0.0575  77  HIS D CA  
6986 C  C   . HIS D  77  ? 0.2075 0.2391 0.2145 0.0516  0.0807  0.0562  77  HIS D C   
6987 O  O   . HIS D  77  ? 0.2210 0.2349 0.2346 0.0684  0.0474  0.0255  77  HIS D O   
6988 C  CB  . HIS D  77  ? 0.2341 0.1867 0.3046 0.0793  0.0824  0.0147  77  HIS D CB  
6989 C  CG  . HIS D  77  ? 0.2548 0.2701 0.2699 0.0737  0.0989  0.0397  77  HIS D CG  
6990 N  ND1 . HIS D  77  ? 0.2272 0.3137 0.3809 0.0687  0.1258  0.0690  77  HIS D ND1 
6991 C  CD2 . HIS D  77  ? 0.3039 0.3517 0.3142 0.0623  0.1189  0.1040  77  HIS D CD2 
6992 C  CE1 . HIS D  77  ? 0.3035 0.4139 0.3282 -0.0122 0.1547  0.0405  77  HIS D CE1 
6993 N  NE2 . HIS D  77  ? 0.2734 0.4293 0.3524 0.0255  0.1548  0.0094  77  HIS D NE2 
6994 N  N   . ILE D  78  ? 0.1981 0.2308 0.2273 0.0431  0.0665  0.0554  78  ILE D N   
6995 C  CA  . ILE D  78  ? 0.2280 0.2369 0.2268 0.0820  0.0876  0.0886  78  ILE D CA  
6996 C  C   . ILE D  78  ? 0.3511 0.2430 0.2876 0.1357  0.1586  0.0784  78  ILE D C   
6997 O  O   . ILE D  78  ? 0.4724 0.2757 0.2508 0.1925  0.1522  0.0653  78  ILE D O   
6998 C  CB  . ILE D  78  ? 0.2326 0.1931 0.1780 0.0528  0.0384  0.0430  78  ILE D CB  
6999 C  CG1 . ILE D  78  ? 0.2261 0.3485 0.2117 0.0872  0.0642  0.0359  78  ILE D CG1 
7000 C  CG2 . ILE D  78  ? 0.3033 0.2696 0.2130 0.0822  0.0267  0.0785  78  ILE D CG2 
7001 C  CD1 . ILE D  78  ? 0.2482 0.3207 0.2037 0.0750  0.0434  0.0383  78  ILE D CD1 
7002 N  N   . GLN D  79  ? 0.3514 0.3112 0.3362 0.1450  0.2067  0.1577  79  GLN D N   
7003 C  CA  . GLN D  79  ? 0.4885 0.3955 0.2997 0.2172  0.1946  0.1251  79  GLN D CA  
7004 C  C   . GLN D  79  ? 0.5574 0.3729 0.3098 0.2606  0.1866  0.1366  79  GLN D C   
7005 O  O   . GLN D  79  ? 0.5417 0.3861 0.2856 0.2452  0.2067  0.1583  79  GLN D O   
7006 C  CB  . GLN D  79  ? 0.4298 0.6480 0.5856 0.1495  0.3493  0.2869  79  GLN D CB  
7007 C  CG  . GLN D  79  ? 0.7364 0.9056 0.2840 0.2419  0.0692  0.0668  79  GLN D CG  
7008 C  CD  . GLN D  79  ? 0.8553 0.9029 0.4971 0.4333  -0.0477 0.0271  79  GLN D CD  
7009 O  OE1 . GLN D  79  ? 0.4312 0.6578 0.4212 0.1228  0.1100  0.0017  79  GLN D OE1 
7010 N  NE2 . GLN D  79  ? 0.6885 0.7537 0.4089 0.3281  0.1697  0.1863  79  GLN D NE2 
7011 N  N   . GLY D  80  ? 0.6096 0.4111 0.3901 0.2715  0.1430  0.1509  80  GLY D N   
7012 C  CA  . GLY D  80  ? 0.4759 0.3704 0.1645 0.1778  0.0972  -0.0273 80  GLY D CA  
7013 C  C   . GLY D  80  ? 0.5054 0.3685 0.1714 0.1014  0.0987  0.0754  80  GLY D C   
7014 O  O   . GLY D  80  ? 0.5362 0.4425 0.3194 0.2196  0.1918  0.1949  80  GLY D O   
7015 N  N   . LEU D  81  ? 0.3592 0.2179 0.2112 0.0815  0.0873  0.0440  81  LEU D N   
7016 C  CA  . LEU D  81  ? 0.3757 0.2825 0.2184 0.0866  0.0939  0.0323  81  LEU D CA  
7017 C  C   . LEU D  81  ? 0.3716 0.1664 0.2042 -0.0381 0.0183  -0.0168 81  LEU D C   
7018 O  O   . LEU D  81  ? 0.4551 0.3994 0.4734 0.1092  0.1096  0.1090  81  LEU D O   
7019 C  CB  . LEU D  81  ? 0.5470 0.2245 0.2741 0.1585  0.1949  0.0380  81  LEU D CB  
7020 C  CG  . LEU D  81  ? 0.3690 0.2172 0.2268 0.0879  0.1119  0.0267  81  LEU D CG  
7021 C  CD1 . LEU D  81  ? 0.4327 0.2728 0.1996 0.0539  0.0839  0.0536  81  LEU D CD1 
7022 C  CD2 . LEU D  81  ? 0.3897 0.2071 0.2222 0.0604  0.0234  0.0047  81  LEU D CD2 
7023 N  N   . GLN D  82  ? 0.3577 0.2365 0.2213 0.0039  0.1021  -0.0245 82  GLN D N   
7024 C  CA  . GLN D  82  ? 0.2676 0.2810 0.1949 0.0763  -0.0521 -0.0877 82  GLN D CA  
7025 C  C   . GLN D  82  ? 0.4000 0.3025 0.1958 0.0914  0.0763  -0.0098 82  GLN D C   
7026 O  O   . GLN D  82  ? 0.3586 0.2852 0.2125 0.0029  0.0319  -0.0725 82  GLN D O   
7027 C  CB  . GLN D  82  ? 0.3759 0.3137 0.2859 -0.1189 0.0136  -0.0446 82  GLN D CB  
7028 C  CG  . GLN D  82  ? 0.4764 0.3565 0.3616 -0.0959 0.0885  -0.0498 82  GLN D CG  
7029 C  CD  . GLN D  82  ? 0.5778 0.2662 0.3225 -0.0925 0.0612  -0.1176 82  GLN D CD  
7030 O  OE1 . GLN D  82  ? 0.3998 0.3574 0.3889 -0.0054 0.0242  -0.1217 82  GLN D OE1 
7031 N  NE2 . GLN D  82  ? 0.3396 0.3567 0.2680 0.0153  -0.0089 0.0348  82  GLN D NE2 
7032 N  N   . SER D  83  ? 0.4800 0.2850 0.1938 0.1473  0.0778  0.0376  83  SER D N   
7033 C  CA  . SER D  83  ? 0.4250 0.2843 0.1942 0.1151  0.0867  0.0079  83  SER D CA  
7034 C  C   . SER D  83  ? 0.3831 0.2216 0.2014 0.0963  0.1054  0.0444  83  SER D C   
7035 O  O   . SER D  83  ? 0.4694 0.2185 0.2142 0.1399  0.1795  0.0583  83  SER D O   
7036 C  CB  . SER D  83  ? 0.4408 0.2482 0.2148 0.1127  0.0178  0.0002  83  SER D CB  
7037 O  OG  . SER D  83  ? 0.6470 0.3484 0.1731 0.1420  -0.0124 -0.0374 83  SER D OG  
7038 N  N   . ARG D  84  ? 0.3617 0.2746 0.1813 0.1044  0.1389  0.0369  84  ARG D N   
7039 C  CA  . ARG D  84  ? 0.3158 0.2316 0.1990 0.0666  0.1140  0.0650  84  ARG D CA  
7040 C  C   . ARG D  84  ? 0.3091 0.1827 0.2253 0.0838  0.1245  0.0359  84  ARG D C   
7041 O  O   . ARG D  84  ? 0.3203 0.1953 0.2347 0.0662  0.1285  0.0238  84  ARG D O   
7042 C  CB  . ARG D  84  ? 0.3030 0.2674 0.2569 0.0359  0.1137  0.0639  84  ARG D CB  
7043 C  CG  . ARG D  84  ? 0.3444 0.2242 0.3371 0.1024  0.0754  0.0370  84  ARG D CG  
7044 C  CD  . ARG D  84  ? 0.3421 0.2838 0.2967 0.0209  0.0640  0.0524  84  ARG D CD  
7045 N  NE  . ARG D  84  ? 0.3629 0.4221 0.3513 0.1322  0.1066  0.0751  84  ARG D NE  
7046 C  CZ  . ARG D  84  ? 0.3649 0.5273 0.3400 0.2222  0.1234  0.1265  84  ARG D CZ  
7047 N  NH1 . ARG D  84  ? 0.2992 0.5599 0.7657 0.1817  0.2204  0.1434  84  ARG D NH1 
7048 N  NH2 . ARG D  84  ? 0.4963 0.4043 0.2537 0.1820  0.0401  0.0485  84  ARG D NH2 
7049 N  N   . TYR D  85  ? 0.2618 0.2107 0.1717 0.0657  0.0752  0.0267  85  TYR D N   
7050 C  CA  . TYR D  85  ? 0.2001 0.1771 0.1626 0.0442  0.0684  0.0160  85  TYR D CA  
7051 C  C   . TYR D  85  ? 0.2176 0.2060 0.2008 0.0653  0.0745  0.0218  85  TYR D C   
7052 O  O   . TYR D  85  ? 0.2018 0.2211 0.2098 0.0368  0.0303  0.0565  85  TYR D O   
7053 C  CB  . TYR D  85  ? 0.1800 0.2535 0.1766 0.0584  0.0493  -0.0163 85  TYR D CB  
7054 C  CG  . TYR D  85  ? 0.2175 0.1529 0.1727 0.0613  0.0282  -0.0008 85  TYR D CG  
7055 C  CD1 . TYR D  85  ? 0.3001 0.1539 0.1687 0.0653  0.0277  -0.0015 85  TYR D CD1 
7056 C  CD2 . TYR D  85  ? 0.2316 0.1517 0.1619 0.0639  0.0253  -0.0064 85  TYR D CD2 
7057 C  CE1 . TYR D  85  ? 0.2901 0.2085 0.1659 0.0435  0.0418  -0.0041 85  TYR D CE1 
7058 C  CE2 . TYR D  85  ? 0.2044 0.1949 0.1597 0.0767  0.0245  0.0002  85  TYR D CE2 
7059 C  CZ  . TYR D  85  ? 0.2709 0.1650 0.1992 0.0727  0.0348  -0.0073 85  TYR D CZ  
7060 O  OH  . TYR D  85  ? 0.2978 0.2371 0.1723 0.0495  0.0151  0.0340  85  TYR D OH  
7061 N  N   . SER D  86  ? 0.2021 0.1995 0.1732 0.0650  0.0626  0.0310  86  SER D N   
7062 C  CA  . SER D  86  ? 0.1823 0.2286 0.1883 0.0756  0.0763  0.0057  86  SER D CA  
7063 C  C   . SER D  86  ? 0.1818 0.1418 0.1539 0.0367  0.0347  0.0018  86  SER D C   
7064 O  O   . SER D  86  ? 0.1865 0.1682 0.1714 0.0438  0.0402  -0.0021 86  SER D O   
7065 C  CB  . SER D  86  ? 0.2169 0.2585 0.1642 0.0985  0.0794  0.0332  86  SER D CB  
7066 O  OG  . SER D  86  ? 0.2169 0.2323 0.2283 0.0822  0.0926  0.0010  86  SER D OG  
7067 N  N   . ALA D  87  ? 0.1938 0.1461 0.1549 0.0394  0.0469  0.0165  87  ALA D N   
7068 C  CA  . ALA D  87  ? 0.1986 0.1540 0.1613 0.0183  0.0665  0.0032  87  ALA D CA  
7069 C  C   . ALA D  87  ? 0.1784 0.1482 0.1755 0.0445  0.0316  -0.0070 87  ALA D C   
7070 O  O   . ALA D  87  ? 0.1724 0.1937 0.1859 0.0423  0.0316  0.0217  87  ALA D O   
7071 C  CB  . ALA D  87  ? 0.2017 0.2037 0.1790 0.0322  0.0488  -0.0256 87  ALA D CB  
7072 N  N   . THR D  88  ? 0.1690 0.1669 0.1442 0.0355  0.0446  0.0069  88  THR D N   
7073 C  CA  . THR D  88  ? 0.2067 0.1463 0.1481 0.0208  0.0436  -0.0089 88  THR D CA  
7074 C  C   . THR D  88  ? 0.1679 0.1403 0.1336 0.0285  0.0122  -0.0133 88  THR D C   
7075 O  O   . THR D  88  ? 0.1662 0.1438 0.1502 0.0162  0.0137  -0.0196 88  THR D O   
7076 C  CB  . THR D  88  ? 0.2208 0.1465 0.1763 0.0322  0.0325  0.0015  88  THR D CB  
7077 O  OG1 . THR D  88  ? 0.3037 0.1694 0.1818 -0.0068 0.0390  -0.0144 88  THR D OG1 
7078 C  CG2 . THR D  88  ? 0.1963 0.1884 0.1995 0.0190  0.0125  -0.0542 88  THR D CG2 
7079 N  N   . GLN D  89  ? 0.1512 0.1300 0.1392 0.0206  0.0299  -0.0086 89  GLN D N   
7080 C  CA  . GLN D  89  ? 0.1554 0.1322 0.1240 0.0311  0.0271  0.0071  89  GLN D CA  
7081 C  C   . GLN D  89  ? 0.1217 0.1132 0.1388 0.0052  0.0111  -0.0003 89  GLN D C   
7082 O  O   . GLN D  89  ? 0.1582 0.1335 0.1324 0.0317  0.0079  0.0021  89  GLN D O   
7083 C  CB  . GLN D  89  ? 0.1534 0.1140 0.1493 0.0024  0.0146  0.0016  89  GLN D CB  
7084 C  CG  . GLN D  89  ? 0.1500 0.1865 0.2013 -0.0057 0.0156  -0.0301 89  GLN D CG  
7085 C  CD  . GLN D  89  ? 0.1741 0.1452 0.1791 0.0183  -0.0206 -0.0058 89  GLN D CD  
7086 O  OE1 . GLN D  89  ? 0.1651 0.1738 0.1954 0.0335  0.0097  -0.0048 89  GLN D OE1 
7087 N  NE2 . GLN D  89  ? 0.2338 0.2280 0.2745 -0.0110 0.0283  0.0329  89  GLN D NE2 
7088 N  N   . LEU D  90  ? 0.1184 0.1261 0.1353 0.0162  0.0136  -0.0111 90  LEU D N   
7089 C  CA  . LEU D  90  ? 0.1143 0.1224 0.1417 0.0188  0.0243  -0.0031 90  LEU D CA  
7090 C  C   . LEU D  90  ? 0.1115 0.1147 0.1190 0.0085  0.0062  0.0017  90  LEU D C   
7091 O  O   . LEU D  90  ? 0.1333 0.1257 0.1340 0.0161  0.0097  0.0079  90  LEU D O   
7092 C  CB  . LEU D  90  ? 0.1231 0.1290 0.1460 0.0097  0.0098  0.0156  90  LEU D CB  
7093 C  CG  . LEU D  90  ? 0.1237 0.1244 0.1608 -0.0008 -0.0013 0.0021  90  LEU D CG  
7094 C  CD1 . LEU D  90  ? 0.1553 0.1313 0.1515 -0.0013 0.0000  -0.0041 90  LEU D CD1 
7095 C  CD2 . LEU D  90  ? 0.1484 0.1394 0.2095 -0.0256 0.0069  0.0079  90  LEU D CD2 
7096 N  N   . HIS D  91  ? 0.1098 0.1112 0.1315 0.0124  0.0158  -0.0035 91  HIS D N   
7097 C  CA  . HIS D  91  ? 0.1127 0.1095 0.1243 0.0064  0.0206  0.0043  91  HIS D CA  
7098 C  C   . HIS D  91  ? 0.1046 0.1129 0.1227 0.0018  0.0023  0.0033  91  HIS D C   
7099 O  O   . HIS D  91  ? 0.1328 0.1070 0.1225 0.0111  0.0139  0.0000  91  HIS D O   
7100 C  CB  . HIS D  91  ? 0.1186 0.1247 0.1105 -0.0013 0.0057  -0.0037 91  HIS D CB  
7101 C  CG  . HIS D  91  ? 0.1116 0.0960 0.1217 -0.0058 0.0074  -0.0002 91  HIS D CG  
7102 N  ND1 . HIS D  91  ? 0.1217 0.1149 0.1416 -0.0055 0.0074  -0.0032 91  HIS D ND1 
7103 C  CD2 . HIS D  91  ? 0.1286 0.1177 0.1116 -0.0135 -0.0016 0.0054  91  HIS D CD2 
7104 C  CE1 . HIS D  91  ? 0.1136 0.1273 0.1209 0.0081  0.0064  0.0077  91  HIS D CE1 
7105 N  NE2 . HIS D  91  ? 0.1209 0.1261 0.1005 0.0053  -0.0013 0.0053  91  HIS D NE2 
7106 N  N   . LEU D  92  ? 0.1073 0.1173 0.1307 0.0094  0.0163  0.0041  92  LEU D N   
7107 C  CA  . LEU D  92  ? 0.1122 0.1209 0.1339 0.0049  0.0063  -0.0083 92  LEU D CA  
7108 C  C   . LEU D  92  ? 0.1156 0.1077 0.1042 -0.0097 -0.0025 0.0004  92  LEU D C   
7109 O  O   . LEU D  92  ? 0.1318 0.1157 0.1420 0.0051  0.0017  -0.0013 92  LEU D O   
7110 C  CB  . LEU D  92  ? 0.1333 0.1556 0.1852 -0.0249 0.0237  -0.0599 92  LEU D CB  
7111 C  CG  . LEU D  92  ? 0.1327 0.1797 0.1795 -0.0234 -0.0005 -0.0402 92  LEU D CG  
7112 C  CD1 . LEU D  92  ? 0.1970 0.2289 0.2581 -0.0140 -0.0502 -0.0234 92  LEU D CD1 
7113 C  CD2 . LEU D  92  ? 0.1430 0.1851 0.3170 -0.0208 0.0301  0.0308  92  LEU D CD2 
7114 N  N   . HIS D  93  ? 0.1210 0.1177 0.1152 0.0127  0.0118  -0.0065 93  HIS D N   
7115 C  CA  . HIS D  93  ? 0.1157 0.1195 0.1133 0.0027  0.0083  -0.0133 93  HIS D CA  
7116 C  C   . HIS D  93  ? 0.1026 0.1118 0.1296 0.0000  0.0084  0.0016  93  HIS D C   
7117 O  O   . HIS D  93  ? 0.1377 0.1258 0.1218 -0.0031 0.0226  -0.0055 93  HIS D O   
7118 C  CB  . HIS D  93  ? 0.1155 0.1168 0.1235 0.0095  0.0067  -0.0086 93  HIS D CB  
7119 C  CG  . HIS D  93  ? 0.1259 0.1087 0.1104 0.0055  0.0040  -0.0019 93  HIS D CG  
7120 N  ND1 . HIS D  93  ? 0.1191 0.1263 0.1210 -0.0066 0.0006  0.0030  93  HIS D ND1 
7121 C  CD2 . HIS D  93  ? 0.1204 0.1198 0.1073 0.0038  0.0044  -0.0054 93  HIS D CD2 
7122 C  CE1 . HIS D  93  ? 0.1282 0.1425 0.1079 0.0048  0.0190  0.0135  93  HIS D CE1 
7123 N  NE2 . HIS D  93  ? 0.1290 0.1091 0.0951 -0.0006 0.0121  0.0083  93  HIS D NE2 
7124 N  N   . TRP D  94  ? 0.1221 0.1084 0.1177 0.0055  0.0156  -0.0093 94  TRP D N   
7125 C  CA  . TRP D  94  ? 0.1242 0.1168 0.1212 -0.0052 0.0179  -0.0170 94  TRP D CA  
7126 C  C   . TRP D  94  ? 0.1423 0.1103 0.1221 -0.0052 0.0214  -0.0091 94  TRP D C   
7127 O  O   . TRP D  94  ? 0.1238 0.1330 0.1240 0.0025  0.0179  -0.0064 94  TRP D O   
7128 C  CB  . TRP D  94  ? 0.1493 0.1122 0.1351 0.0048  0.0107  -0.0139 94  TRP D CB  
7129 C  CG  . TRP D  94  ? 0.1338 0.1186 0.1341 -0.0067 0.0135  0.0025  94  TRP D CG  
7130 C  CD1 . TRP D  94  ? 0.1473 0.1170 0.1430 -0.0065 0.0129  0.0008  94  TRP D CD1 
7131 C  CD2 . TRP D  94  ? 0.1382 0.1358 0.1252 0.0015  0.0010  -0.0177 94  TRP D CD2 
7132 N  NE1 . TRP D  94  ? 0.1342 0.1373 0.1412 0.0003  0.0013  0.0066  94  TRP D NE1 
7133 C  CE2 . TRP D  94  ? 0.1295 0.1360 0.1373 0.0011  0.0125  -0.0096 94  TRP D CE2 
7134 C  CE3 . TRP D  94  ? 0.1438 0.1295 0.1238 0.0013  0.0017  -0.0037 94  TRP D CE3 
7135 C  CZ2 . TRP D  94  ? 0.1468 0.1579 0.1441 0.0133  0.0218  -0.0120 94  TRP D CZ2 
7136 C  CZ3 . TRP D  94  ? 0.1198 0.1557 0.1481 -0.0062 -0.0055 -0.0066 94  TRP D CZ3 
7137 C  CH2 . TRP D  94  ? 0.1517 0.1563 0.1375 0.0136  0.0012  -0.0097 94  TRP D CH2 
7138 N  N   . GLY D  95  ? 0.1319 0.1335 0.1308 0.0122  0.0281  -0.0111 95  GLY D N   
7139 C  CA  . GLY D  95  ? 0.1424 0.1568 0.1374 0.0111  0.0214  0.0109  95  GLY D CA  
7140 C  C   . GLY D  95  ? 0.1359 0.1563 0.1543 -0.0068 0.0381  -0.0055 95  GLY D C   
7141 O  O   . GLY D  95  ? 0.1493 0.1551 0.1365 -0.0023 0.0350  -0.0126 95  GLY D O   
7142 N  N   . ASN D  96  ? 0.1457 0.1796 0.1481 -0.0095 0.0447  -0.0153 96  ASN D N   
7143 C  CA  . ASN D  96  ? 0.2029 0.1676 0.1475 -0.0140 0.0362  -0.0145 96  ASN D CA  
7144 C  C   . ASN D  96  ? 0.1602 0.2127 0.1561 -0.0065 0.0231  -0.0334 96  ASN D C   
7145 O  O   . ASN D  96  ? 0.2043 0.1987 0.1801 0.0057  0.0582  -0.0494 96  ASN D O   
7146 C  CB  . ASN D  96  ? 0.1712 0.2282 0.2111 -0.0100 0.0432  0.0121  96  ASN D CB  
7147 C  CG  . ASN D  96  ? 0.1990 0.2247 0.2114 -0.0168 0.0524  -0.0485 96  ASN D CG  
7148 O  OD1 . ASN D  96  ? 0.2046 0.2579 0.3080 -0.0039 0.0775  -0.1023 96  ASN D OD1 
7149 N  ND2 . ASN D  96  ? 0.2062 0.2376 0.2234 0.0150  0.0430  -0.0143 96  ASN D ND2 
7150 N  N   . PRO D  97  ? 0.1712 0.2440 0.1784 -0.0055 0.0384  -0.0422 97  PRO D N   
7151 C  CA  . PRO D  97  ? 0.2599 0.2895 0.2329 0.0046  0.0535  -0.1100 97  PRO D CA  
7152 C  C   . PRO D  97  ? 0.2679 0.2397 0.2095 -0.0150 0.0348  -0.0696 97  PRO D C   
7153 O  O   . PRO D  97  ? 0.3916 0.2788 0.3132 -0.0234 0.1188  -0.1192 97  PRO D O   
7154 C  CB  . PRO D  97  ? 0.2745 0.4538 0.1890 0.0452  0.0286  -0.1637 97  PRO D CB  
7155 C  CG  . PRO D  97  ? 0.2469 0.4385 0.1738 0.0565  0.0000  -0.1055 97  PRO D CG  
7156 C  CD  . PRO D  97  ? 0.2009 0.2755 0.1822 0.0264  0.0297  -0.0203 97  PRO D CD  
7157 N  N   . ASN D  98  ? 0.2115 0.2225 0.1830 0.0259  0.0479  -0.0294 98  ASN D N   
7158 C  CA  . ASN D  98  ? 0.2640 0.2613 0.2429 0.0419  0.0331  -0.0006 98  ASN D CA  
7159 C  C   . ASN D  98  ? 0.2922 0.3298 0.2389 0.0851  0.1220  0.0277  98  ASN D C   
7160 O  O   . ASN D  98  ? 0.3260 0.4216 0.2916 0.1669  0.0929  0.0109  98  ASN D O   
7161 C  CB  . ASN D  98  ? 0.2112 0.2963 0.2386 0.0286  0.0372  0.0130  98  ASN D CB  
7162 C  CG  . ASN D  98  ? 0.3873 0.4244 0.1855 -0.0734 0.0083  -0.0776 98  ASN D CG  
7163 O  OD1 . ASN D  98  ? 0.4179 0.6501 0.2353 -0.1114 0.0701  -0.1502 98  ASN D OD1 
7164 N  ND2 . ASN D  98  ? 0.3774 0.4692 0.3514 -0.0604 0.0253  0.0022  98  ASN D ND2 
7165 N  N   . ASP D  99  ? 0.2126 0.2741 0.1920 0.0356  0.0657  -0.0174 99  ASP D N   
7166 C  CA  . ASP D  99  ? 0.1826 0.2877 0.1833 -0.0053 0.0559  -0.0166 99  ASP D CA  
7167 C  C   . ASP D  99  ? 0.2064 0.1639 0.1773 0.0006  0.0401  -0.0140 99  ASP D C   
7168 O  O   . ASP D  99  ? 0.1940 0.1855 0.1823 0.0046  0.0361  -0.0110 99  ASP D O   
7169 C  CB  . ASP D  99  ? 0.2226 0.2991 0.2488 -0.0392 0.0233  0.0061  99  ASP D CB  
7170 C  CG  . ASP D  99  ? 0.2713 0.3410 0.2517 -0.0203 -0.0826 0.0030  99  ASP D CG  
7171 O  OD1 . ASP D  99  ? 0.3925 0.3416 0.2550 0.0363  0.0175  0.0467  99  ASP D OD1 
7172 O  OD2 . ASP D  99  ? 0.4205 0.4079 0.4387 -0.0429 -0.2090 -0.0264 99  ASP D OD2 
7173 N  N   . PRO D  100 ? 0.2061 0.1812 0.1773 -0.0037 0.0505  -0.0405 100 PRO D N   
7174 C  CA  . PRO D  100 ? 0.2048 0.1831 0.1808 -0.0243 0.0473  -0.0420 100 PRO D CA  
7175 C  C   . PRO D  100 ? 0.1866 0.1496 0.1789 -0.0039 0.0611  -0.0274 100 PRO D C   
7176 O  O   . PRO D  100 ? 0.2113 0.1784 0.2083 -0.0141 0.0637  -0.0343 100 PRO D O   
7177 C  CB  . PRO D  100 ? 0.2696 0.1967 0.2513 -0.0264 -0.0039 -0.0670 100 PRO D CB  
7178 C  CG  . PRO D  100 ? 0.3161 0.1924 0.2563 -0.0241 0.0463  -0.0588 100 PRO D CG  
7179 C  CD  . PRO D  100 ? 0.3104 0.1588 0.2153 -0.0160 0.0685  -0.0595 100 PRO D CD  
7180 N  N   . HIS D  101 ? 0.1778 0.1747 0.1662 0.0182  0.0189  -0.0286 101 HIS D N   
7181 C  CA  . HIS D  101 ? 0.1773 0.1870 0.1530 0.0105  0.0201  -0.0046 101 HIS D CA  
7182 C  C   . HIS D  101 ? 0.1710 0.1571 0.1625 -0.0092 0.0175  -0.0204 101 HIS D C   
7183 O  O   . HIS D  101 ? 0.1937 0.2087 0.2129 -0.0009 -0.0080 -0.0188 101 HIS D O   
7184 C  CB  . HIS D  101 ? 0.2186 0.2398 0.1946 0.0592  0.0312  0.0258  101 HIS D CB  
7185 C  CG  . HIS D  101 ? 0.2561 0.2489 0.2773 0.0870  0.0416  0.0170  101 HIS D CG  
7186 N  ND1 . HIS D  101 ? 0.3353 0.3200 0.3464 0.0965  0.0609  0.0267  101 HIS D ND1 
7187 C  CD2 . HIS D  101 ? 0.2875 0.2371 0.2868 0.0876  0.0665  0.0242  101 HIS D CD2 
7188 C  CE1 . HIS D  101 ? 0.3617 0.2585 0.4663 0.1077  0.1051  0.0215  101 HIS D CE1 
7189 N  NE2 . HIS D  101 ? 0.3710 0.2263 0.3862 0.1161  0.0344  -0.0067 101 HIS D NE2 
7190 N  N   . GLY D  102 ? 0.1532 0.1439 0.1406 -0.0040 0.0152  -0.0010 102 GLY D N   
7191 C  CA  . GLY D  102 ? 0.1491 0.1527 0.1525 -0.0148 0.0261  -0.0068 102 GLY D CA  
7192 C  C   . GLY D  102 ? 0.1278 0.1240 0.1366 -0.0006 -0.0023 -0.0126 102 GLY D C   
7193 O  O   . GLY D  102 ? 0.1629 0.1365 0.1449 -0.0067 0.0038  0.0122  102 GLY D O   
7194 N  N   . SER D  103 ? 0.1324 0.1409 0.1193 0.0091  0.0125  -0.0008 103 SER D N   
7195 C  CA  . SER D  103 ? 0.1247 0.1396 0.1174 -0.0024 0.0134  -0.0111 103 SER D CA  
7196 C  C   . SER D  103 ? 0.1208 0.1156 0.1176 0.0005  0.0135  -0.0055 103 SER D C   
7197 O  O   . SER D  103 ? 0.1391 0.1483 0.1518 0.0054  0.0097  -0.0260 103 SER D O   
7198 C  CB  . SER D  103 ? 0.1231 0.1227 0.1481 0.0176  0.0059  0.0193  103 SER D CB  
7199 O  OG  . SER D  103 ? 0.1285 0.1204 0.1399 0.0121  0.0042  -0.0002 103 SER D OG  
7200 N  N   . GLU D  104 ? 0.1369 0.1304 0.1055 0.0104  -0.0048 -0.0051 104 GLU D N   
7201 C  CA  . GLU D  104 ? 0.1421 0.1103 0.1238 0.0081  -0.0203 0.0069  104 GLU D CA  
7202 C  C   . GLU D  104 ? 0.1220 0.1107 0.1140 0.0065  -0.0049 -0.0061 104 GLU D C   
7203 O  O   . GLU D  104 ? 0.1282 0.1195 0.1284 -0.0042 -0.0030 0.0016  104 GLU D O   
7204 C  CB  . GLU D  104 ? 0.1744 0.1179 0.1200 0.0172  -0.0005 0.0077  104 GLU D CB  
7205 C  CG  . GLU D  104 ? 0.1590 0.1106 0.1242 0.0047  -0.0050 0.0044  104 GLU D CG  
7206 C  CD  . GLU D  104 ? 0.1347 0.1209 0.1096 0.0076  0.0081  -0.0110 104 GLU D CD  
7207 O  OE1 . GLU D  104 ? 0.1339 0.1318 0.1416 0.0089  0.0143  -0.0192 104 GLU D OE1 
7208 O  OE2 . GLU D  104 ? 0.1384 0.1378 0.1442 0.0016  0.0115  0.0133  104 GLU D OE2 
7209 N  N   . HIS D  105 ? 0.1373 0.1251 0.1152 0.0050  0.0055  0.0088  105 HIS D N   
7210 C  CA  . HIS D  105 ? 0.1263 0.1154 0.1195 0.0100  0.0038  0.0182  105 HIS D CA  
7211 C  C   . HIS D  105 ? 0.1296 0.1185 0.1216 0.0065  -0.0044 0.0054  105 HIS D C   
7212 O  O   . HIS D  105 ? 0.1555 0.1318 0.1333 0.0231  -0.0104 -0.0125 105 HIS D O   
7213 C  CB  . HIS D  105 ? 0.1294 0.1279 0.1287 -0.0027 0.0113  0.0026  105 HIS D CB  
7214 C  CG  . HIS D  105 ? 0.1319 0.1238 0.1247 0.0057  0.0181  0.0086  105 HIS D CG  
7215 N  ND1 . HIS D  105 ? 0.1439 0.1262 0.1367 0.0142  0.0134  0.0004  105 HIS D ND1 
7216 C  CD2 . HIS D  105 ? 0.1507 0.1492 0.1141 0.0116  0.0182  -0.0044 105 HIS D CD2 
7217 C  CE1 . HIS D  105 ? 0.1449 0.1698 0.1204 0.0231  0.0040  -0.0081 105 HIS D CE1 
7218 N  NE2 . HIS D  105 ? 0.1534 0.1421 0.1234 0.0061  0.0166  -0.0118 105 HIS D NE2 
7219 N  N   . THR D  106 ? 0.1435 0.1292 0.1351 0.0207  -0.0022 0.0050  106 THR D N   
7220 C  CA  . THR D  106 ? 0.1492 0.1251 0.1367 0.0118  0.0029  0.0126  106 THR D CA  
7221 C  C   . THR D  106 ? 0.1476 0.1287 0.1389 0.0132  -0.0201 0.0074  106 THR D C   
7222 O  O   . THR D  106 ? 0.1620 0.1556 0.1323 0.0223  -0.0001 0.0092  106 THR D O   
7223 C  CB  . THR D  106 ? 0.1516 0.1339 0.1495 0.0212  -0.0012 -0.0135 106 THR D CB  
7224 O  OG1 . THR D  106 ? 0.1628 0.1586 0.1605 0.0175  -0.0117 -0.0179 106 THR D OG1 
7225 C  CG2 . THR D  106 ? 0.1764 0.1527 0.1747 0.0041  0.0336  0.0286  106 THR D CG2 
7226 N  N   . VAL D  107 ? 0.1625 0.1286 0.1574 0.0165  -0.0073 0.0058  107 VAL D N   
7227 C  CA  . VAL D  107 ? 0.1656 0.1331 0.1811 0.0287  -0.0145 0.0310  107 VAL D CA  
7228 C  C   . VAL D  107 ? 0.1685 0.1575 0.1904 0.0127  -0.0089 0.0103  107 VAL D C   
7229 O  O   . VAL D  107 ? 0.2078 0.1527 0.1900 0.0425  -0.0259 -0.0024 107 VAL D O   
7230 C  CB  . VAL D  107 ? 0.1788 0.1636 0.1858 0.0022  -0.0070 0.0210  107 VAL D CB  
7231 C  CG1 . VAL D  107 ? 0.2379 0.1570 0.2889 0.0031  0.0029  0.0547  107 VAL D CG1 
7232 C  CG2 . VAL D  107 ? 0.1893 0.1637 0.2327 0.0154  -0.0069 0.0201  107 VAL D CG2 
7233 N  N   . SER D  108 ? 0.2049 0.1468 0.1694 0.0387  -0.0276 0.0442  108 SER D N   
7234 C  CA  . SER D  108 ? 0.2298 0.1515 0.2058 0.0628  -0.0111 0.0197  108 SER D CA  
7235 C  C   . SER D  108 ? 0.1847 0.1549 0.1773 0.0374  -0.0249 0.0000  108 SER D C   
7236 O  O   . SER D  108 ? 0.2179 0.2026 0.2113 0.0675  -0.0174 0.0009  108 SER D O   
7237 C  CB  . SER D  108 ? 0.2483 0.1557 0.2920 0.0807  0.0347  0.0611  108 SER D CB  
7238 O  OG  . SER D  108 ? 0.2708 0.2255 0.2648 0.0449  0.0190  0.0795  108 SER D OG  
7239 N  N   . GLY D  109 ? 0.1857 0.1750 0.1642 0.0177  -0.0069 0.0137  109 GLY D N   
7240 C  CA  . GLY D  109 ? 0.1559 0.2031 0.1807 0.0284  -0.0156 0.0088  109 GLY D CA  
7241 C  C   . GLY D  109 ? 0.1813 0.2243 0.1881 0.0511  0.0121  -0.0059 109 GLY D C   
7242 O  O   . GLY D  109 ? 0.2113 0.3827 0.2001 0.0109  -0.0013 -0.0001 109 GLY D O   
7243 N  N   . GLN D  110 ? 0.1795 0.2011 0.1797 0.0399  -0.0140 -0.0095 110 GLN D N   
7244 C  CA  . GLN D  110 ? 0.1934 0.1854 0.1773 0.0500  -0.0362 -0.0139 110 GLN D CA  
7245 C  C   . GLN D  110 ? 0.1454 0.1641 0.1730 0.0297  -0.0070 0.0023  110 GLN D C   
7246 O  O   . GLN D  110 ? 0.1649 0.1513 0.1524 0.0337  -0.0004 -0.0092 110 GLN D O   
7247 C  CB  . GLN D  110 ? 0.2315 0.1913 0.2663 0.0529  -0.0358 0.0388  110 GLN D CB  
7248 C  CG  . GLN D  110 ? 0.3142 0.2221 0.3328 0.1197  -0.0268 -0.0185 110 GLN D CG  
7249 C  CD  . GLN D  110 ? 0.3076 0.3274 0.3646 0.1450  -0.0444 -0.0036 110 GLN D CD  
7250 O  OE1 . GLN D  110 ? 0.4267 0.3729 0.3614 0.0643  0.0635  -0.0599 110 GLN D OE1 
7251 N  NE2 . GLN D  110 ? 0.3951 0.2500 0.4301 0.0207  -0.0358 0.0930  110 GLN D NE2 
7252 N  N   . HIS D  111 ? 0.1644 0.1782 0.1626 0.0312  0.0031  0.0001  111 HIS D N   
7253 C  CA  . HIS D  111 ? 0.1583 0.1735 0.1403 0.0216  -0.0046 0.0078  111 HIS D CA  
7254 C  C   . HIS D  111 ? 0.1680 0.1602 0.1773 0.0342  -0.0132 -0.0286 111 HIS D C   
7255 O  O   . HIS D  111 ? 0.1991 0.1642 0.3024 0.0501  -0.0282 -0.0509 111 HIS D O   
7256 C  CB  . HIS D  111 ? 0.1850 0.1708 0.1741 0.0003  0.0277  -0.0204 111 HIS D CB  
7257 C  CG  . HIS D  111 ? 0.1780 0.1531 0.1496 0.0150  0.0239  0.0000  111 HIS D CG  
7258 N  ND1 . HIS D  111 ? 0.2027 0.1661 0.1482 0.0242  0.0206  -0.0093 111 HIS D ND1 
7259 C  CD2 . HIS D  111 ? 0.1732 0.1816 0.2098 -0.0013 0.0002  -0.0261 111 HIS D CD2 
7260 C  CE1 . HIS D  111 ? 0.1753 0.1812 0.2101 0.0122  0.0431  -0.0165 111 HIS D CE1 
7261 N  NE2 . HIS D  111 ? 0.1817 0.2071 0.2579 -0.0036 0.0201  -0.0264 111 HIS D NE2 
7262 N  N   . PHE D  112 ? 0.1385 0.1254 0.1556 0.0225  -0.0022 -0.0060 112 PHE D N   
7263 C  CA  . PHE D  112 ? 0.1525 0.1198 0.1588 0.0083  0.0165  0.0025  112 PHE D CA  
7264 C  C   . PHE D  112 ? 0.1167 0.1120 0.1480 0.0174  0.0106  -0.0121 112 PHE D C   
7265 O  O   . PHE D  112 ? 0.1511 0.1229 0.1407 -0.0020 0.0077  -0.0062 112 PHE D O   
7266 C  CB  . PHE D  112 ? 0.1535 0.1676 0.1810 0.0018  0.0351  0.0390  112 PHE D CB  
7267 C  CG  . PHE D  112 ? 0.1660 0.1619 0.1921 0.0335  0.0100  0.0059  112 PHE D CG  
7268 C  CD1 . PHE D  112 ? 0.2319 0.2863 0.1863 0.0958  0.0148  0.0597  112 PHE D CD1 
7269 C  CD2 . PHE D  112 ? 0.2379 0.1834 0.2840 -0.0214 0.0245  0.0614  112 PHE D CD2 
7270 C  CE1 . PHE D  112 ? 0.2552 0.2910 0.2016 0.0673  0.0163  0.0693  112 PHE D CE1 
7271 C  CE2 . PHE D  112 ? 0.2424 0.2997 0.3869 0.0158  0.0111  0.1600  112 PHE D CE2 
7272 C  CZ  . PHE D  112 ? 0.2637 0.2708 0.2653 0.0440  0.0588  0.0722  112 PHE D CZ  
7273 N  N   . ALA D  113 ? 0.1368 0.1204 0.1344 0.0158  0.0091  -0.0071 113 ALA D N   
7274 C  CA  . ALA D  113 ? 0.1432 0.1172 0.1408 0.0071  0.0097  -0.0058 113 ALA D CA  
7275 C  C   . ALA D  113 ? 0.1277 0.1246 0.1353 -0.0066 0.0229  -0.0136 113 ALA D C   
7276 O  O   . ALA D  113 ? 0.1424 0.1273 0.1291 -0.0088 0.0254  -0.0096 113 ALA D O   
7277 C  CB  . ALA D  113 ? 0.1715 0.1540 0.1534 0.0044  0.0044  -0.0431 113 ALA D CB  
7278 N  N   . ALA D  114 ? 0.1345 0.1134 0.1280 0.0027  0.0211  -0.0152 114 ALA D N   
7279 C  CA  . ALA D  114 ? 0.1251 0.1100 0.1170 0.0127  0.0168  -0.0025 114 ALA D CA  
7280 C  C   . ALA D  114 ? 0.1186 0.1127 0.1177 -0.0009 0.0159  -0.0085 114 ALA D C   
7281 O  O   . ALA D  114 ? 0.1211 0.1093 0.1302 0.0038  0.0121  -0.0020 114 ALA D O   
7282 C  CB  . ALA D  114 ? 0.1408 0.1220 0.1338 0.0059  -0.0037 0.0043  114 ALA D CB  
7283 N  N   . GLU D  115 ? 0.1188 0.1109 0.1161 0.0089  0.0113  -0.0083 115 GLU D N   
7284 C  CA  . GLU D  115 ? 0.1216 0.1355 0.1245 0.0151  0.0288  -0.0135 115 GLU D CA  
7285 C  C   . GLU D  115 ? 0.1208 0.1070 0.1130 0.0089  0.0095  -0.0089 115 GLU D C   
7286 O  O   . GLU D  115 ? 0.1365 0.1289 0.1466 -0.0047 0.0117  0.0037  115 GLU D O   
7287 C  CB  . GLU D  115 ? 0.1339 0.1346 0.1210 0.0036  0.0146  -0.0136 115 GLU D CB  
7288 C  CG  . GLU D  115 ? 0.1432 0.1696 0.1075 0.0022  0.0142  -0.0054 115 GLU D CG  
7289 C  CD  . GLU D  115 ? 0.1228 0.1184 0.1361 0.0022  0.0086  -0.0001 115 GLU D CD  
7290 O  OE1 . GLU D  115 ? 0.1370 0.1364 0.1303 0.0085  0.0063  0.0077  115 GLU D OE1 
7291 O  OE2 . GLU D  115 ? 0.1441 0.1265 0.1274 0.0114  -0.0020 0.0031  115 GLU D OE2 
7292 N  N   . LEU D  116 ? 0.1201 0.0981 0.1267 0.0122  0.0227  -0.0060 116 LEU D N   
7293 C  CA  . LEU D  116 ? 0.1060 0.1014 0.1330 0.0089  0.0286  -0.0114 116 LEU D CA  
7294 C  C   . LEU D  116 ? 0.1134 0.1195 0.1136 0.0172  0.0281  0.0004  116 LEU D C   
7295 O  O   . LEU D  116 ? 0.1333 0.1136 0.1275 0.0078  0.0237  0.0105  116 LEU D O   
7296 C  CB  . LEU D  116 ? 0.1165 0.1445 0.1567 -0.0030 0.0100  -0.0085 116 LEU D CB  
7297 C  CG  . LEU D  116 ? 0.1116 0.1260 0.1654 -0.0036 0.0032  0.0111  116 LEU D CG  
7298 C  CD1 . LEU D  116 ? 0.1315 0.1488 0.1597 -0.0017 0.0019  0.0039  116 LEU D CD1 
7299 C  CD2 . LEU D  116 ? 0.1428 0.1394 0.2082 -0.0074 0.0182  0.0102  116 LEU D CD2 
7300 N  N   . HIS D  117 ? 0.1091 0.0996 0.1305 0.0132  0.0198  -0.0135 117 HIS D N   
7301 C  CA  . HIS D  117 ? 0.1058 0.1082 0.1267 0.0021  0.0160  -0.0146 117 HIS D CA  
7302 C  C   . HIS D  117 ? 0.1134 0.0985 0.1131 0.0023  0.0181  0.0015  117 HIS D C   
7303 O  O   . HIS D  117 ? 0.1249 0.1305 0.1228 0.0174  0.0186  0.0120  117 HIS D O   
7304 C  CB  . HIS D  117 ? 0.1104 0.1157 0.1256 -0.0018 0.0066  -0.0054 117 HIS D CB  
7305 C  CG  . HIS D  117 ? 0.1116 0.1211 0.1236 0.0173  0.0162  0.0020  117 HIS D CG  
7306 N  ND1 . HIS D  117 ? 0.1188 0.1039 0.1045 0.0052  0.0103  -0.0144 117 HIS D ND1 
7307 C  CD2 . HIS D  117 ? 0.1472 0.1240 0.1199 0.0072  -0.0070 0.0038  117 HIS D CD2 
7308 C  CE1 . HIS D  117 ? 0.1225 0.1247 0.1001 0.0137  0.0131  -0.0004 117 HIS D CE1 
7309 N  NE2 . HIS D  117 ? 0.1314 0.1231 0.1035 0.0034  0.0082  0.0048  117 HIS D NE2 
7310 N  N   . ILE D  118 ? 0.1112 0.1138 0.1208 0.0052  0.0243  0.0083  118 ILE D N   
7311 C  CA  . ILE D  118 ? 0.1116 0.1259 0.1363 0.0135  0.0223  0.0052  118 ILE D CA  
7312 C  C   . ILE D  118 ? 0.1213 0.1394 0.1227 0.0097  0.0194  0.0005  118 ILE D C   
7313 O  O   . ILE D  118 ? 0.1539 0.1316 0.1365 0.0285  0.0269  0.0018  118 ILE D O   
7314 C  CB  . ILE D  118 ? 0.1301 0.1364 0.1427 -0.0003 0.0267  -0.0006 118 ILE D CB  
7315 C  CG1 . ILE D  118 ? 0.1523 0.1192 0.1614 -0.0114 0.0260  -0.0005 118 ILE D CG1 
7316 C  CG2 . ILE D  118 ? 0.1335 0.1645 0.1703 0.0219  0.0258  0.0093  118 ILE D CG2 
7317 C  CD1 . ILE D  118 ? 0.1866 0.1468 0.1899 -0.0403 0.0484  -0.0048 118 ILE D CD1 
7318 N  N   . VAL D  119 ? 0.1401 0.1123 0.1360 0.0120  0.0267  -0.0036 119 VAL D N   
7319 C  CA  . VAL D  119 ? 0.1409 0.1134 0.1382 0.0175  0.0313  0.0011  119 VAL D CA  
7320 C  C   . VAL D  119 ? 0.1472 0.1290 0.1299 0.0282  0.0305  -0.0094 119 VAL D C   
7321 O  O   . VAL D  119 ? 0.1465 0.1463 0.1439 0.0391  0.0221  0.0044  119 VAL D O   
7322 C  CB  . VAL D  119 ? 0.1521 0.1322 0.1402 0.0060  0.0276  -0.0084 119 VAL D CB  
7323 C  CG1 . VAL D  119 ? 0.1812 0.1285 0.1495 0.0082  0.0165  -0.0174 119 VAL D CG1 
7324 C  CG2 . VAL D  119 ? 0.1451 0.1390 0.1473 0.0225  0.0136  0.0068  119 VAL D CG2 
7325 N  N   . HIS D  120 ? 0.1709 0.1252 0.1360 0.0283  0.0337  -0.0069 120 HIS D N   
7326 C  CA  . HIS D  120 ? 0.1708 0.1291 0.1437 0.0370  0.0403  0.0005  120 HIS D CA  
7327 C  C   . HIS D  120 ? 0.1914 0.1536 0.1430 0.0475  0.0272  0.0141  120 HIS D C   
7328 O  O   . HIS D  120 ? 0.2010 0.1477 0.1427 0.0484  0.0198  -0.0129 120 HIS D O   
7329 C  CB  . HIS D  120 ? 0.1879 0.1366 0.1575 0.0295  0.0515  0.0010  120 HIS D CB  
7330 C  CG  . HIS D  120 ? 0.1848 0.1262 0.1614 0.0408  0.0375  0.0054  120 HIS D CG  
7331 N  ND1 . HIS D  120 ? 0.1833 0.1460 0.1649 0.0392  0.0551  -0.0061 120 HIS D ND1 
7332 C  CD2 . HIS D  120 ? 0.1844 0.1449 0.1603 0.0047  0.0091  0.0019  120 HIS D CD2 
7333 C  CE1 . HIS D  120 ? 0.1688 0.1861 0.1653 -0.0053 0.0309  0.0168  120 HIS D CE1 
7334 N  NE2 . HIS D  120 ? 0.1673 0.1608 0.1737 0.0063  0.0281  0.0176  120 HIS D NE2 
7335 N  N   . TYR D  121 ? 0.2049 0.1421 0.1605 0.0513  0.0375  -0.0069 121 TYR D N   
7336 C  CA  . TYR D  121 ? 0.2584 0.1313 0.1284 0.0264  0.0560  -0.0095 121 TYR D CA  
7337 C  C   . TYR D  121 ? 0.2079 0.1454 0.1725 0.0535  0.0263  0.0218  121 TYR D C   
7338 O  O   . TYR D  121 ? 0.2159 0.1582 0.1699 0.0598  0.0611  0.0031  121 TYR D O   
7339 C  CB  . TYR D  121 ? 0.2005 0.1565 0.1530 0.0475  0.0313  0.0035  121 TYR D CB  
7340 C  CG  . TYR D  121 ? 0.1974 0.1661 0.1492 0.0484  0.0416  -0.0001 121 TYR D CG  
7341 C  CD1 . TYR D  121 ? 0.2439 0.1674 0.1654 0.0377  0.0117  0.0348  121 TYR D CD1 
7342 C  CD2 . TYR D  121 ? 0.2326 0.1453 0.1722 0.0414  0.0540  0.0089  121 TYR D CD2 
7343 C  CE1 . TYR D  121 ? 0.2349 0.1884 0.2455 0.0063  0.0089  0.0655  121 TYR D CE1 
7344 C  CE2 . TYR D  121 ? 0.2372 0.2071 0.2508 0.0735  0.0743  0.0569  121 TYR D CE2 
7345 C  CZ  . TYR D  121 ? 0.2664 0.2761 0.2661 0.0646  0.0427  0.0958  121 TYR D CZ  
7346 O  OH  . TYR D  121 ? 0.2436 0.3614 0.4139 0.1108  0.0454  0.1699  121 TYR D OH  
7347 N  N   . ASN D  122 ? 0.2226 0.1578 0.1475 0.0592  0.0442  0.0036  122 ASN D N   
7348 C  CA  . ASN D  122 ? 0.2439 0.1804 0.1985 0.0781  0.0908  0.0209  122 ASN D CA  
7349 C  C   . ASN D  122 ? 0.2431 0.1996 0.1319 0.0540  0.0607  0.0024  122 ASN D C   
7350 O  O   . ASN D  122 ? 0.2667 0.1703 0.1722 0.0665  0.0517  -0.0077 122 ASN D O   
7351 C  CB  . ASN D  122 ? 0.3147 0.1990 0.1582 0.0829  0.0590  0.0001  122 ASN D CB  
7352 C  CG  . ASN D  122 ? 0.2798 0.2116 0.1681 0.0886  0.0456  -0.0027 122 ASN D CG  
7353 O  OD1 . ASN D  122 ? 0.3158 0.2314 0.1651 0.1040  0.0683  0.0111  122 ASN D OD1 
7354 N  ND2 . ASN D  122 ? 0.3107 0.2286 0.2023 0.0992  0.0228  0.0084  122 ASN D ND2 
7355 N  N   . SER D  123 ? 0.2321 0.1879 0.1829 0.0578  0.0672  0.0209  123 SER D N   
7356 C  CA  . SER D  123 ? 0.2405 0.2344 0.2398 0.0756  0.1007  0.0024  123 SER D CA  
7357 C  C   . SER D  123 ? 0.2592 0.2144 0.2190 0.0741  0.0756  0.0111  123 SER D C   
7358 O  O   . SER D  123 ? 0.3166 0.2212 0.2705 0.1072  0.1106  0.0247  123 SER D O   
7359 C  CB  . SER D  123 ? 0.2509 0.1524 0.2679 0.0593  0.0807  0.0701  123 SER D CB  
7360 O  OG  . SER D  123 ? 0.3123 0.1800 0.2222 0.0374  0.0960  0.0289  123 SER D OG  
7361 N  N   . ASP D  124 ? 0.3725 0.2190 0.1752 0.0936  0.1303  0.0303  124 ASP D N   
7362 C  CA  . ASP D  124 ? 0.3687 0.2402 0.2087 0.1195  0.0978  0.0291  124 ASP D CA  
7363 C  C   . ASP D  124 ? 0.3552 0.2282 0.2436 0.0967  0.1198  0.0461  124 ASP D C   
7364 O  O   . ASP D  124 ? 0.4273 0.2697 0.3820 0.1049  0.1954  -0.0316 124 ASP D O   
7365 C  CB  . ASP D  124 ? 0.4035 0.2290 0.2369 0.0914  0.1044  0.0245  124 ASP D CB  
7366 C  CG  . ASP D  124 ? 0.2988 0.3251 0.3225 0.0289  0.1015  -0.0511 124 ASP D CG  
7367 O  OD1 . ASP D  124 ? 0.3088 0.3622 0.2134 0.0077  0.1103  -0.0559 124 ASP D OD1 
7368 O  OD2 . ASP D  124 ? 0.3711 0.3233 0.2874 0.1093  0.0801  0.0024  124 ASP D OD2 
7369 N  N   . LEU D  125 ? 0.2876 0.2277 0.2001 0.0793  0.0653  0.0318  125 LEU D N   
7370 C  CA  . LEU D  125 ? 0.3092 0.2663 0.1734 0.0603  0.0563  -0.0194 125 LEU D CA  
7371 C  C   . LEU D  125 ? 0.3106 0.2215 0.1574 0.0158  0.0336  -0.0312 125 LEU D C   
7372 O  O   . LEU D  125 ? 0.3846 0.2128 0.1845 0.1023  0.0158  -0.0353 125 LEU D O   
7373 C  CB  . LEU D  125 ? 0.3523 0.3200 0.1430 0.1316  0.0210  -0.0100 125 LEU D CB  
7374 C  CG  . LEU D  125 ? 0.4097 0.3679 0.1857 0.0785  -0.0070 0.0175  125 LEU D CG  
7375 C  CD1 . LEU D  125 ? 0.3905 0.3987 0.2439 0.0696  0.0230  0.0071  125 LEU D CD1 
7376 C  CD2 . LEU D  125 ? 0.4520 0.3845 0.2247 0.1103  -0.0465 0.1218  125 LEU D CD2 
7377 N  N   . TYR D  126 ? 0.2692 0.1801 0.1662 0.0739  0.0171  -0.0070 126 TYR D N   
7378 C  CA  . TYR D  126 ? 0.2505 0.1924 0.1712 0.0599  0.0100  -0.0223 126 TYR D CA  
7379 C  C   . TYR D  126 ? 0.2477 0.2203 0.1801 0.0623  0.0089  -0.0212 126 TYR D C   
7380 O  O   . TYR D  126 ? 0.2540 0.2295 0.1932 0.0520  0.0198  0.0030  126 TYR D O   
7381 C  CB  . TYR D  126 ? 0.2348 0.1932 0.1726 0.0675  0.0027  0.0043  126 TYR D CB  
7382 C  CG  . TYR D  126 ? 0.2586 0.1894 0.1685 0.0595  0.0103  -0.0242 126 TYR D CG  
7383 C  CD1 . TYR D  126 ? 0.2991 0.1925 0.2170 0.0883  -0.0042 -0.0443 126 TYR D CD1 
7384 C  CD2 . TYR D  126 ? 0.2586 0.1751 0.1605 0.0468  0.0038  0.0072  126 TYR D CD2 
7385 C  CE1 . TYR D  126 ? 0.2588 0.1886 0.2136 0.0578  0.0000  -0.0433 126 TYR D CE1 
7386 C  CE2 . TYR D  126 ? 0.2813 0.2183 0.1460 0.0565  -0.0078 -0.0296 126 TYR D CE2 
7387 C  CZ  . TYR D  126 ? 0.3013 0.2000 0.1517 0.0776  -0.0196 -0.0388 126 TYR D CZ  
7388 O  OH  . TYR D  126 ? 0.3004 0.1967 0.1939 0.0633  -0.0298 -0.0267 126 TYR D OH  
7389 N  N   . PRO D  127 ? 0.2459 0.1846 0.2029 0.0487  -0.0008 -0.0282 127 PRO D N   
7390 C  CA  . PRO D  127 ? 0.2392 0.2017 0.2459 0.0700  0.0033  0.0138  127 PRO D CA  
7391 C  C   . PRO D  127 ? 0.2270 0.2243 0.2235 0.0473  0.0074  0.0199  127 PRO D C   
7392 O  O   . PRO D  127 ? 0.2451 0.2635 0.2274 0.0300  0.0127  -0.0075 127 PRO D O   
7393 C  CB  . PRO D  127 ? 0.3148 0.1914 0.2142 0.0902  -0.0032 0.0095  127 PRO D CB  
7394 C  CG  . PRO D  127 ? 0.3348 0.2021 0.2100 0.0757  -0.0166 -0.0005 127 PRO D CG  
7395 C  CD  . PRO D  127 ? 0.3306 0.1597 0.2011 0.0498  -0.0057 -0.0122 127 PRO D CD  
7396 N  N   . ASP D  128 ? 0.2485 0.1674 0.1764 0.0396  0.0122  0.0148  128 ASP D N   
7397 C  CA  . ASP D  128 ? 0.2271 0.2019 0.1415 0.0146  0.0183  0.0128  128 ASP D CA  
7398 C  C   . ASP D  128 ? 0.2304 0.1903 0.1585 0.0197  0.0058  0.0072  128 ASP D C   
7399 O  O   . ASP D  128 ? 0.2397 0.1770 0.1691 0.0308  0.0097  -0.0063 128 ASP D O   
7400 C  CB  . ASP D  128 ? 0.2671 0.1477 0.2250 0.0253  -0.0560 0.0411  128 ASP D CB  
7401 C  CG  . ASP D  128 ? 0.2846 0.1654 0.1879 0.0182  0.0282  0.0113  128 ASP D CG  
7402 O  OD1 . ASP D  128 ? 0.2863 0.1925 0.2289 0.0342  -0.0088 -0.0240 128 ASP D OD1 
7403 O  OD2 . ASP D  128 ? 0.2890 0.2154 0.2343 -0.0038 0.0092  0.0125  128 ASP D OD2 
7404 N  N   . ALA D  129 ? 0.2359 0.1725 0.1651 0.0285  0.0355  0.0133  129 ALA D N   
7405 C  CA  . ALA D  129 ? 0.2168 0.1588 0.1488 0.0027  0.0279  -0.0273 129 ALA D CA  
7406 C  C   . ALA D  129 ? 0.2168 0.1824 0.1463 -0.0099 0.0106  -0.0131 129 ALA D C   
7407 O  O   . ALA D  129 ? 0.2555 0.1560 0.1849 0.0075  0.0057  -0.0228 129 ALA D O   
7408 C  CB  . ALA D  129 ? 0.3015 0.2122 0.1861 0.0137  0.0211  -0.0606 129 ALA D CB  
7409 N  N   A SER D  130 ? 0.2694 0.1572 0.1679 0.0082  0.0110  -0.0052 130 SER D N   
7410 N  N   B SER D  130 ? 0.2398 0.1660 0.1439 0.0087  0.0178  -0.0011 130 SER D N   
7411 C  CA  A SER D  130 ? 0.2409 0.1887 0.1801 0.0135  -0.0095 -0.0009 130 SER D CA  
7412 C  CA  B SER D  130 ? 0.2545 0.1875 0.1446 -0.0044 0.0077  -0.0004 130 SER D CA  
7413 C  C   A SER D  130 ? 0.2207 0.1733 0.1879 0.0135  0.0065  -0.0043 130 SER D C   
7414 C  C   B SER D  130 ? 0.2345 0.1548 0.1744 0.0134  0.0087  -0.0125 130 SER D C   
7415 O  O   A SER D  130 ? 0.2482 0.1851 0.1643 0.0030  0.0030  -0.0304 130 SER D O   
7416 O  O   B SER D  130 ? 0.2682 0.1978 0.1759 0.0210  0.0036  -0.0060 130 SER D O   
7417 C  CB  A SER D  130 ? 0.3180 0.1920 0.1818 -0.0592 -0.0082 0.0398  130 SER D CB  
7418 C  CB  B SER D  130 ? 0.2218 0.1477 0.1701 0.0205  0.0039  -0.0055 130 SER D CB  
7419 O  OG  A SER D  130 ? 0.3459 0.1863 0.2574 -0.0204 -0.0197 0.0146  130 SER D OG  
7420 O  OG  B SER D  130 ? 0.2460 0.1793 0.2170 -0.0189 -0.0038 0.0400  130 SER D OG  
7421 N  N   . THR D  131 ? 0.2681 0.1732 0.1748 0.0215  0.0144  -0.0067 131 THR D N   
7422 C  CA  . THR D  131 ? 0.2445 0.1610 0.1579 0.0266  -0.0263 -0.0268 131 THR D CA  
7423 C  C   . THR D  131 ? 0.2487 0.1890 0.1934 0.0190  -0.0179 0.0027  131 THR D C   
7424 O  O   . THR D  131 ? 0.2443 0.1787 0.1985 0.0294  -0.0176 -0.0336 131 THR D O   
7425 C  CB  . THR D  131 ? 0.2907 0.1663 0.1857 0.0436  -0.0048 -0.0003 131 THR D CB  
7426 O  OG1 . THR D  131 ? 0.2740 0.1573 0.2556 0.0343  -0.0193 -0.0110 131 THR D OG1 
7427 C  CG2 . THR D  131 ? 0.3276 0.2546 0.2144 0.0599  0.0359  -0.0563 131 THR D CG2 
7428 N  N   . ALA D  132 ? 0.2385 0.1764 0.1508 0.0292  0.0223  0.0069  132 ALA D N   
7429 C  CA  . ALA D  132 ? 0.2588 0.1655 0.1527 0.0348  0.0050  0.0186  132 ALA D CA  
7430 C  C   . ALA D  132 ? 0.2420 0.1599 0.1491 0.0357  0.0000  -0.0015 132 ALA D C   
7431 O  O   . ALA D  132 ? 0.2666 0.1781 0.1557 0.0525  0.0116  -0.0085 132 ALA D O   
7432 C  CB  . ALA D  132 ? 0.2448 0.1449 0.1791 0.0314  0.0270  -0.0142 132 ALA D CB  
7433 N  N   . SER D  133 ? 0.2374 0.1761 0.1404 0.0377  0.0074  -0.0187 133 SER D N   
7434 C  CA  . SER D  133 ? 0.2196 0.1669 0.1614 0.0241  0.0168  -0.0026 133 SER D CA  
7435 C  C   . SER D  133 ? 0.2503 0.1559 0.1910 0.0422  0.0087  0.0107  133 SER D C   
7436 O  O   . SER D  133 ? 0.2597 0.1692 0.1550 0.0247  0.0174  0.0164  133 SER D O   
7437 C  CB  . SER D  133 ? 0.2949 0.1820 0.1582 0.0070  0.0132  0.0190  133 SER D CB  
7438 O  OG  . SER D  133 ? 0.3181 0.2113 0.1733 0.0500  0.0237  0.0417  133 SER D OG  
7439 N  N   . ASN D  134 ? 0.2658 0.1678 0.1725 0.0229  0.0110  -0.0040 134 ASN D N   
7440 C  CA  . ASN D  134 ? 0.2891 0.1773 0.1693 0.0241  0.0167  0.0032  134 ASN D CA  
7441 C  C   . ASN D  134 ? 0.2338 0.1985 0.1780 0.0329  -0.0092 -0.0174 134 ASN D C   
7442 O  O   . ASN D  134 ? 0.2957 0.2185 0.1888 -0.0230 0.0044  -0.0019 134 ASN D O   
7443 C  CB  . ASN D  134 ? 0.3797 0.1852 0.2633 -0.0225 0.0554  0.0513  134 ASN D CB  
7444 C  CG  . ASN D  134 ? 0.3197 0.2168 0.3625 -0.0065 -0.0331 0.0848  134 ASN D CG  
7445 O  OD1 . ASN D  134 ? 0.2851 0.1730 0.3181 0.0222  -0.0043 0.0231  134 ASN D OD1 
7446 N  ND2 . ASN D  134 ? 0.3815 0.2226 0.3330 -0.0457 -0.0250 0.0480  134 ASN D ND2 
7447 N  N   . LYS D  135 ? 0.2477 0.1877 0.1581 0.0294  -0.0029 -0.0140 135 LYS D N   
7448 C  CA  . LYS D  135 ? 0.2928 0.2307 0.1454 0.0816  0.0407  0.0252  135 LYS D CA  
7449 C  C   . LYS D  135 ? 0.2718 0.1831 0.1551 0.0270  0.0352  -0.0043 135 LYS D C   
7450 O  O   . LYS D  135 ? 0.2518 0.2131 0.1669 0.0370  0.0027  -0.0138 135 LYS D O   
7451 C  CB  . LYS D  135 ? 0.2555 0.2234 0.1858 0.0593  0.0550  -0.0096 135 LYS D CB  
7452 C  CG  . LYS D  135 ? 0.3181 0.1956 0.2860 0.0595  -0.0199 0.0040  135 LYS D CG  
7453 C  CD  . LYS D  135 ? 0.3191 0.2499 0.2176 0.0381  -0.0065 -0.0208 135 LYS D CD  
7454 C  CE  . LYS D  135 ? 0.3690 0.2388 0.2614 0.0461  -0.0258 0.0000  135 LYS D CE  
7455 N  NZ  . LYS D  135 ? 0.3289 0.1938 0.2832 0.0306  -0.0394 -0.0241 135 LYS D NZ  
7456 N  N   A SER D  136 ? 0.2424 0.2576 0.1550 0.0621  0.0121  0.0139  136 SER D N   
7457 N  N   B SER D  136 ? 0.2577 0.2447 0.1593 0.0302  0.0024  0.0141  136 SER D N   
7458 C  CA  A SER D  136 ? 0.2907 0.2371 0.1527 -0.0173 -0.0214 0.0240  136 SER D CA  
7459 C  CA  B SER D  136 ? 0.2708 0.2358 0.1358 -0.0032 -0.0263 0.0158  136 SER D CA  
7460 C  C   A SER D  136 ? 0.2529 0.2064 0.1354 0.0502  0.0074  -0.0438 136 SER D C   
7461 C  C   B SER D  136 ? 0.2522 0.2035 0.1359 0.0450  0.0155  -0.0441 136 SER D C   
7462 O  O   A SER D  136 ? 0.2455 0.2006 0.1245 0.0221  0.0233  -0.0363 136 SER D O   
7463 O  O   B SER D  136 ? 0.2529 0.1917 0.1732 0.0230  0.0077  -0.0139 136 SER D O   
7464 C  CB  A SER D  136 ? 0.3325 0.3380 0.1715 -0.0807 -0.0305 -0.0150 136 SER D CB  
7465 C  CB  B SER D  136 ? 0.2426 0.3449 0.1840 -0.0103 -0.0109 -0.0615 136 SER D CB  
7466 O  OG  A SER D  136 ? 0.2736 0.3396 0.2513 -0.0365 0.0108  0.0402  136 SER D OG  
7467 O  OG  B SER D  136 ? 0.3561 0.3362 0.1861 -0.1215 -0.0108 0.0502  136 SER D OG  
7468 N  N   . GLU D  137 ? 0.3204 0.2040 0.1464 0.0665  0.0134  -0.0373 137 GLU D N   
7469 C  CA  . GLU D  137 ? 0.3222 0.1861 0.1365 0.0659  -0.0046 0.0013  137 GLU D CA  
7470 C  C   . GLU D  137 ? 0.2696 0.1587 0.1570 0.0471  0.0118  -0.0100 137 GLU D C   
7471 O  O   . GLU D  137 ? 0.2889 0.1952 0.1480 0.0405  0.0340  0.0044  137 GLU D O   
7472 C  CB  . GLU D  137 ? 0.3777 0.2207 0.1287 0.0000  0.0092  0.0132  137 GLU D CB  
7473 C  CG  . GLU D  137 ? 0.4404 0.2895 0.1597 0.0705  0.0152  -0.0106 137 GLU D CG  
7474 C  CD  . GLU D  137 ? 0.5375 0.3139 0.1703 0.1395  -0.0094 -0.0089 137 GLU D CD  
7475 O  OE1 . GLU D  137 ? 0.8430 0.2855 0.4970 0.1673  -0.2138 -0.0226 137 GLU D OE1 
7476 O  OE2 . GLU D  137 ? 0.3555 0.7068 0.4397 0.0871  -0.0936 -0.0776 137 GLU D OE2 
7477 N  N   . GLY D  138 ? 0.2746 0.1933 0.1439 0.0761  0.0279  0.0077  138 GLY D N   
7478 C  CA  . GLY D  138 ? 0.2672 0.1746 0.1268 0.0569  -0.0268 -0.0172 138 GLY D CA  
7479 C  C   . GLY D  138 ? 0.1902 0.1701 0.1441 0.0397  0.0075  -0.0148 138 GLY D C   
7480 O  O   . GLY D  138 ? 0.2117 0.1766 0.1484 0.0443  0.0264  -0.0152 138 GLY D O   
7481 N  N   . LEU D  139 ? 0.2421 0.1376 0.1301 0.0519  0.0211  -0.0125 139 LEU D N   
7482 C  CA  . LEU D  139 ? 0.2090 0.1436 0.1200 0.0336  0.0085  0.0015  139 LEU D CA  
7483 C  C   . LEU D  139 ? 0.1807 0.1573 0.1273 0.0172  0.0293  0.0039  139 LEU D C   
7484 O  O   . LEU D  139 ? 0.2305 0.1632 0.1324 0.0534  0.0318  -0.0006 139 LEU D O   
7485 C  CB  . LEU D  139 ? 0.2299 0.1512 0.1183 0.0341  0.0325  0.0027  139 LEU D CB  
7486 C  CG  . LEU D  139 ? 0.2153 0.1483 0.1402 0.0311  0.0311  0.0000  139 LEU D CG  
7487 C  CD1 . LEU D  139 ? 0.2229 0.1517 0.1709 0.0322  0.0548  0.0218  139 LEU D CD1 
7488 C  CD2 . LEU D  139 ? 0.2311 0.1896 0.1670 0.0326  -0.0077 0.0147  139 LEU D CD2 
7489 N  N   . ALA D  140 ? 0.2053 0.1326 0.1442 0.0388  0.0216  -0.0087 140 ALA D N   
7490 C  CA  . ALA D  140 ? 0.2095 0.1154 0.1302 0.0211  0.0317  -0.0122 140 ALA D CA  
7491 C  C   . ALA D  140 ? 0.1542 0.1308 0.1296 0.0247  0.0072  0.0015  140 ALA D C   
7492 O  O   . ALA D  140 ? 0.1787 0.1508 0.1529 0.0430  0.0098  -0.0077 140 ALA D O   
7493 C  CB  . ALA D  140 ? 0.2125 0.1746 0.1621 0.0539  0.0630  0.0252  140 ALA D CB  
7494 N  N   . VAL D  141 ? 0.1685 0.1382 0.1141 0.0307  0.0344  0.0048  141 VAL D N   
7495 C  CA  . VAL D  141 ? 0.1605 0.1379 0.1210 0.0186  0.0229  0.0055  141 VAL D CA  
7496 C  C   . VAL D  141 ? 0.1292 0.1500 0.1287 0.0279  0.0323  0.0119  141 VAL D C   
7497 O  O   . VAL D  141 ? 0.1881 0.1412 0.1306 0.0392  0.0250  0.0061  141 VAL D O   
7498 C  CB  . VAL D  141 ? 0.1430 0.1367 0.1177 0.0163  0.0177  -0.0008 141 VAL D CB  
7499 C  CG1 . VAL D  141 ? 0.1718 0.1685 0.1216 0.0113  0.0280  -0.0078 141 VAL D CG1 
7500 C  CG2 . VAL D  141 ? 0.1847 0.1436 0.1588 0.0003  -0.0011 0.0124  141 VAL D CG2 
7501 N  N   . LEU D  142 ? 0.1425 0.1150 0.1289 0.0173  0.0363  0.0041  142 LEU D N   
7502 C  CA  . LEU D  142 ? 0.1428 0.1208 0.1474 0.0233  0.0353  0.0126  142 LEU D CA  
7503 C  C   . LEU D  142 ? 0.1689 0.1128 0.1183 0.0265  0.0217  0.0181  142 LEU D C   
7504 O  O   . LEU D  142 ? 0.1744 0.1348 0.1333 0.0326  0.0200  0.0111  142 LEU D O   
7505 C  CB  . LEU D  142 ? 0.1445 0.1706 0.1794 0.0158  0.0369  0.0159  142 LEU D CB  
7506 C  CG  . LEU D  142 ? 0.1635 0.1636 0.1594 0.0380  0.0364  -0.0001 142 LEU D CG  
7507 C  CD1 . LEU D  142 ? 0.1946 0.1509 0.2258 0.0020  0.0397  -0.0037 142 LEU D CD1 
7508 C  CD2 . LEU D  142 ? 0.1896 0.2041 0.1581 0.0418  0.0463  0.0275  142 LEU D CD2 
7509 N  N   . ALA D  143 ? 0.1464 0.1183 0.1426 0.0074  0.0301  0.0001  143 ALA D N   
7510 C  CA  . ALA D  143 ? 0.1411 0.1247 0.1197 0.0075  0.0266  -0.0029 143 ALA D CA  
7511 C  C   . ALA D  143 ? 0.1165 0.1181 0.1249 -0.0012 0.0236  0.0201  143 ALA D C   
7512 O  O   . ALA D  143 ? 0.1603 0.1220 0.1269 0.0089  0.0319  0.0157  143 ALA D O   
7513 C  CB  . ALA D  143 ? 0.1560 0.1382 0.1336 -0.0085 0.0109  0.0080  143 ALA D CB  
7514 N  N   . VAL D  144 ? 0.1366 0.1091 0.1279 0.0157  0.0265  -0.0039 144 VAL D N   
7515 C  CA  . VAL D  144 ? 0.1281 0.1259 0.1302 0.0085  0.0245  -0.0201 144 VAL D CA  
7516 C  C   . VAL D  144 ? 0.1272 0.1229 0.1202 0.0055  0.0207  0.0058  144 VAL D C   
7517 O  O   . VAL D  144 ? 0.1505 0.1192 0.1445 0.0082  0.0348  0.0120  144 VAL D O   
7518 C  CB  . VAL D  144 ? 0.1326 0.1351 0.1693 -0.0189 0.0343  -0.0054 144 VAL D CB  
7519 C  CG1 . VAL D  144 ? 0.1627 0.1480 0.1681 -0.0184 0.0119  -0.0239 144 VAL D CG1 
7520 C  CG2 . VAL D  144 ? 0.1573 0.1500 0.1647 0.0138  0.0388  -0.0087 144 VAL D CG2 
7521 N  N   . LEU D  145 ? 0.1292 0.1249 0.1346 0.0108  0.0227  0.0046  145 LEU D N   
7522 C  CA  . LEU D  145 ? 0.1231 0.1438 0.1328 0.0148  0.0143  -0.0154 145 LEU D CA  
7523 C  C   . LEU D  145 ? 0.1366 0.0960 0.1459 -0.0033 0.0234  -0.0115 145 LEU D C   
7524 O  O   . LEU D  145 ? 0.1505 0.1347 0.1491 -0.0233 0.0225  -0.0054 145 LEU D O   
7525 C  CB  . LEU D  145 ? 0.1499 0.1297 0.1577 0.0149  -0.0013 -0.0155 145 LEU D CB  
7526 C  CG  . LEU D  145 ? 0.1996 0.1514 0.1769 0.0168  -0.0044 -0.0192 145 LEU D CG  
7527 C  CD1 . LEU D  145 ? 0.2083 0.2406 0.1659 0.0331  -0.0223 0.0027  145 LEU D CD1 
7528 C  CD2 . LEU D  145 ? 0.2020 0.2202 0.2049 0.0197  -0.0441 -0.0193 145 LEU D CD2 
7529 N  N   . ILE D  146 ? 0.1378 0.1271 0.1287 0.0098  0.0186  -0.0240 146 ILE D N   
7530 C  CA  . ILE D  146 ? 0.1292 0.1293 0.1367 -0.0052 0.0155  -0.0214 146 ILE D CA  
7531 C  C   . ILE D  146 ? 0.1342 0.1224 0.1299 -0.0033 0.0269  -0.0170 146 ILE D C   
7532 O  O   . ILE D  146 ? 0.1436 0.1262 0.1621 -0.0096 0.0310  -0.0187 146 ILE D O   
7533 C  CB  . ILE D  146 ? 0.1405 0.1304 0.1397 0.0076  0.0009  -0.0162 146 ILE D CB  
7534 C  CG1 . ILE D  146 ? 0.1474 0.1377 0.1701 0.0124  0.0367  0.0026  146 ILE D CG1 
7535 C  CG2 . ILE D  146 ? 0.1521 0.1491 0.1580 -0.0019 -0.0048 -0.0376 146 ILE D CG2 
7536 C  CD1 . ILE D  146 ? 0.1660 0.1082 0.1781 0.0060  0.0091  -0.0016 146 ILE D CD1 
7537 N  N   A GLU D  147 ? 0.1344 0.1037 0.1238 -0.0037 0.0251  -0.0097 147 GLU D N   
7538 N  N   B GLU D  147 ? 0.1399 0.1166 0.1447 0.0059  -0.0190 -0.0300 147 GLU D N   
7539 C  CA  A GLU D  147 ? 0.1673 0.1110 0.1664 0.0348  -0.0038 -0.0147 147 GLU D CA  
7540 C  CA  B GLU D  147 ? 0.1495 0.1130 0.1375 -0.0018 0.0220  -0.0081 147 GLU D CA  
7541 C  C   A GLU D  147 ? 0.1290 0.1249 0.1479 0.0038  0.0254  -0.0023 147 GLU D C   
7542 C  C   B GLU D  147 ? 0.1313 0.1127 0.1351 0.0001  0.0139  -0.0115 147 GLU D C   
7543 O  O   A GLU D  147 ? 0.1308 0.1240 0.1167 0.0138  0.0075  -0.0006 147 GLU D O   
7544 O  O   B GLU D  147 ? 0.1310 0.1694 0.1483 -0.0089 0.0023  0.0147  147 GLU D O   
7545 C  CB  A GLU D  147 ? 0.2064 0.1075 0.2875 0.0530  -0.0323 0.0086  147 GLU D CB  
7546 C  CB  B GLU D  147 ? 0.1366 0.1308 0.1480 0.0092  -0.0057 0.0111  147 GLU D CB  
7547 C  CG  A GLU D  147 ? 0.3552 0.2009 0.2446 -0.0269 -0.0621 0.0341  147 GLU D CG  
7548 C  CG  B GLU D  147 ? 0.1748 0.1251 0.1542 0.0240  0.0336  0.0205  147 GLU D CG  
7549 C  CD  A GLU D  147 ? 0.2909 0.2697 0.2493 0.0146  -0.0128 0.0833  147 GLU D CD  
7550 C  CD  B GLU D  147 ? 0.2984 0.1839 0.2216 -0.0053 0.0699  0.0851  147 GLU D CD  
7551 O  OE1 A GLU D  147 ? 0.3346 0.2632 0.2623 0.0411  0.0207  0.0819  147 GLU D OE1 
7552 O  OE1 B GLU D  147 ? 0.4026 0.3101 0.2825 0.0245  0.0556  0.0190  147 GLU D OE1 
7553 O  OE2 A GLU D  147 ? 0.4512 0.2198 0.3710 0.0529  -0.1119 0.0124  147 GLU D OE2 
7554 O  OE2 B GLU D  147 ? 0.4047 0.2757 0.3682 0.1134  0.0395  0.0541  147 GLU D OE2 
7555 N  N   . MET D  148 ? 0.1659 0.1161 0.1525 -0.0006 0.0346  0.0027  148 MET D N   
7556 C  CA  . MET D  148 ? 0.1463 0.1328 0.1429 0.0092  0.0272  -0.0010 148 MET D CA  
7557 C  C   . MET D  148 ? 0.1615 0.1170 0.1514 0.0279  -0.0024 0.0013  148 MET D C   
7558 O  O   . MET D  148 ? 0.1881 0.1112 0.1986 0.0151  -0.0116 0.0006  148 MET D O   
7559 C  CB  . MET D  148 ? 0.1572 0.1958 0.1487 0.0377  0.0133  -0.0004 148 MET D CB  
7560 C  CG  . MET D  148 ? 0.2082 0.1787 0.1698 0.0094  0.0564  -0.0044 148 MET D CG  
7561 S  SD  . MET D  148 ? 0.2243 0.1878 0.2093 0.0020  0.0628  -0.0063 148 MET D SD  
7562 C  CE  . MET D  148 ? 0.2676 0.1664 0.2565 -0.0006 0.0584  -0.0271 148 MET D CE  
7563 N  N   . GLY D  149 ? 0.1558 0.1280 0.1674 0.0083  0.0074  -0.0150 149 GLY D N   
7564 C  CA  . GLY D  149 ? 0.1614 0.1249 0.1668 0.0150  -0.0060 -0.0238 149 GLY D CA  
7565 C  C   . GLY D  149 ? 0.1582 0.1140 0.1615 0.0189  0.0046  -0.0132 149 GLY D C   
7566 O  O   . GLY D  149 ? 0.1674 0.1317 0.1665 0.0288  0.0092  -0.0063 149 GLY D O   
7567 N  N   . SER D  150 ? 0.1426 0.1259 0.1828 0.0174  0.0023  -0.0048 150 SER D N   
7568 C  CA  . SER D  150 ? 0.1487 0.1259 0.1670 0.0173  0.0054  -0.0016 150 SER D CA  
7569 C  C   . SER D  150 ? 0.1563 0.1221 0.1654 -0.0118 0.0044  0.0009  150 SER D C   
7570 O  O   . SER D  150 ? 0.1756 0.1383 0.1914 0.0165  -0.0027 0.0025  150 SER D O   
7571 C  CB  . SER D  150 ? 0.1709 0.1257 0.2184 0.0031  0.0099  0.0034  150 SER D CB  
7572 O  OG  . SER D  150 ? 0.1895 0.1227 0.2005 0.0242  0.0122  0.0146  150 SER D OG  
7573 N  N   . PHE D  151 ? 0.1781 0.1369 0.1818 0.0194  -0.0021 -0.0031 151 PHE D N   
7574 C  CA  . PHE D  151 ? 0.1611 0.1409 0.1766 0.0104  -0.0006 -0.0083 151 PHE D CA  
7575 C  C   . PHE D  151 ? 0.1600 0.1234 0.1718 0.0150  0.0070  0.0105  151 PHE D C   
7576 O  O   . PHE D  151 ? 0.1855 0.1336 0.2221 -0.0182 0.0194  -0.0083 151 PHE D O   
7577 C  CB  . PHE D  151 ? 0.1958 0.1296 0.1782 0.0369  -0.0264 -0.0122 151 PHE D CB  
7578 C  CG  . PHE D  151 ? 0.1727 0.1569 0.1741 -0.0020 -0.0168 0.0089  151 PHE D CG  
7579 C  CD1 . PHE D  151 ? 0.2183 0.1404 0.1939 0.0097  -0.0291 -0.0048 151 PHE D CD1 
7580 C  CD2 . PHE D  151 ? 0.1896 0.1735 0.2273 0.0137  -0.0425 -0.0072 151 PHE D CD2 
7581 C  CE1 . PHE D  151 ? 0.2288 0.1751 0.2323 0.0094  -0.0573 -0.0032 151 PHE D CE1 
7582 C  CE2 . PHE D  151 ? 0.2208 0.1933 0.2133 0.0447  -0.0228 -0.0048 151 PHE D CE2 
7583 C  CZ  . PHE D  151 ? 0.2509 0.1882 0.1839 0.0405  -0.0378 -0.0189 151 PHE D CZ  
7584 N  N   . ASN D  152 ? 0.1660 0.1229 0.1797 0.0157  0.0021  -0.0036 152 ASN D N   
7585 C  CA  . ASN D  152 ? 0.1508 0.1436 0.1787 0.0204  0.0012  -0.0223 152 ASN D CA  
7586 C  C   . ASN D  152 ? 0.1383 0.1438 0.1893 -0.0059 0.0210  0.0044  152 ASN D C   
7587 O  O   . ASN D  152 ? 0.1421 0.1342 0.1985 0.0039  0.0131  -0.0043 152 ASN D O   
7588 C  CB  . ASN D  152 ? 0.1500 0.1566 0.1593 -0.0124 -0.0072 -0.0124 152 ASN D CB  
7589 C  CG  . ASN D  152 ? 0.1342 0.1587 0.2022 -0.0078 0.0233  -0.0089 152 ASN D CG  
7590 O  OD1 . ASN D  152 ? 0.1523 0.1573 0.2113 -0.0072 0.0161  -0.0015 152 ASN D OD1 
7591 N  ND2 . ASN D  152 ? 0.1586 0.1434 0.1953 -0.0009 0.0164  -0.0124 152 ASN D ND2 
7592 N  N   . PRO D  153 ? 0.1386 0.1495 0.2238 -0.0097 0.0037  -0.0044 153 PRO D N   
7593 C  CA  . PRO D  153 ? 0.1491 0.1864 0.2464 0.0044  -0.0223 -0.0380 153 PRO D CA  
7594 C  C   . PRO D  153 ? 0.1423 0.1582 0.2262 -0.0117 0.0144  -0.0143 153 PRO D C   
7595 O  O   . PRO D  153 ? 0.2001 0.1934 0.2511 0.0190  -0.0233 0.0041  153 PRO D O   
7596 C  CB  . PRO D  153 ? 0.1718 0.1650 0.2850 -0.0162 -0.0167 -0.0146 153 PRO D CB  
7597 C  CG  . PRO D  153 ? 0.1722 0.2020 0.4953 -0.0256 -0.0763 0.0447  153 PRO D CG  
7598 C  CD  . PRO D  153 ? 0.1592 0.1597 0.3318 -0.0154 -0.0058 -0.0064 153 PRO D CD  
7599 N  N   . SER D  154 ? 0.1373 0.1919 0.2082 0.0095  0.0168  -0.0088 154 SER D N   
7600 C  CA  . SER D  154 ? 0.1553 0.1933 0.2395 -0.0050 0.0288  -0.0288 154 SER D CA  
7601 C  C   . SER D  154 ? 0.1442 0.1646 0.2367 0.0436  0.0139  -0.0161 154 SER D C   
7602 O  O   . SER D  154 ? 0.1605 0.1749 0.2406 0.0320  0.0218  -0.0256 154 SER D O   
7603 C  CB  . SER D  154 ? 0.1631 0.2129 0.2710 -0.0252 0.0496  -0.0182 154 SER D CB  
7604 O  OG  . SER D  154 ? 0.2251 0.2537 0.2926 -0.0743 0.0588  -0.0330 154 SER D OG  
7605 N  N   . TYR D  155 ? 0.1399 0.1703 0.1991 0.0043  0.0046  -0.0108 155 TYR D N   
7606 C  CA  . TYR D  155 ? 0.1517 0.1586 0.2032 0.0096  0.0110  -0.0098 155 TYR D CA  
7607 C  C   . TYR D  155 ? 0.1511 0.1452 0.1956 0.0065  -0.0099 -0.0059 155 TYR D C   
7608 O  O   . TYR D  155 ? 0.1614 0.1455 0.2140 0.0059  0.0134  -0.0187 155 TYR D O   
7609 C  CB  . TYR D  155 ? 0.1218 0.1503 0.2406 0.0051  0.0149  -0.0258 155 TYR D CB  
7610 C  CG  . TYR D  155 ? 0.1324 0.1310 0.2012 0.0136  0.0195  -0.0120 155 TYR D CG  
7611 C  CD1 . TYR D  155 ? 0.1453 0.1195 0.2098 0.0134  0.0083  -0.0188 155 TYR D CD1 
7612 C  CD2 . TYR D  155 ? 0.1292 0.1464 0.2159 -0.0067 0.0167  -0.0073 155 TYR D CD2 
7613 C  CE1 . TYR D  155 ? 0.1581 0.1351 0.2034 0.0016  0.0043  -0.0232 155 TYR D CE1 
7614 C  CE2 . TYR D  155 ? 0.1769 0.1503 0.1901 0.0097  0.0219  -0.0067 155 TYR D CE2 
7615 C  CZ  . TYR D  155 ? 0.1409 0.1215 0.1898 0.0254  0.0162  -0.0080 155 TYR D CZ  
7616 O  OH  . TYR D  155 ? 0.1520 0.1516 0.1982 0.0164  0.0086  -0.0201 155 TYR D OH  
7617 N  N   . ASP D  156 ? 0.1391 0.1658 0.2012 0.0205  0.0091  -0.0391 156 ASP D N   
7618 C  CA  . ASP D  156 ? 0.1978 0.1487 0.2156 0.0178  0.0052  -0.0330 156 ASP D CA  
7619 C  C   . ASP D  156 ? 0.1886 0.1515 0.2201 0.0066  0.0039  0.0035  156 ASP D C   
7620 O  O   . ASP D  156 ? 0.2159 0.1620 0.2065 0.0078  0.0025  -0.0190 156 ASP D O   
7621 C  CB  . ASP D  156 ? 0.2446 0.1541 0.2066 -0.0037 -0.0038 -0.0331 156 ASP D CB  
7622 C  CG  . ASP D  156 ? 0.2344 0.1925 0.2621 0.0539  -0.0193 -0.0233 156 ASP D CG  
7623 O  OD1 . ASP D  156 ? 0.2476 0.1748 0.2082 0.0595  -0.0092 0.0006  156 ASP D OD1 
7624 O  OD2 . ASP D  156 ? 0.2713 0.2744 0.2113 0.0144  -0.0608 0.0058  156 ASP D OD2 
7625 N  N   . LYS D  157 ? 0.1699 0.1472 0.2371 0.0184  -0.0050 -0.0038 157 LYS D N   
7626 C  CA  . LYS D  157 ? 0.1886 0.1441 0.2778 0.0425  0.0195  0.0127  157 LYS D CA  
7627 C  C   . LYS D  157 ? 0.2026 0.1557 0.3203 0.0436  0.0133  0.0218  157 LYS D C   
7628 O  O   . LYS D  157 ? 0.2462 0.1781 0.3491 0.0467  -0.0308 0.0348  157 LYS D O   
7629 C  CB  . LYS D  157 ? 0.1418 0.2206 0.3312 0.0516  0.0197  -0.0184 157 LYS D CB  
7630 C  CG  . LYS D  157 ? 0.1575 0.2040 0.3855 0.0262  0.0732  0.0046  157 LYS D CG  
7631 C  CD  . LYS D  157 ? 0.2718 0.2843 0.3416 0.0115  0.0439  -0.0526 157 LYS D CD  
7632 C  CE  . LYS D  157 ? 0.2054 0.2939 0.4895 -0.0286 0.0858  -0.0414 157 LYS D CE  
7633 N  NZ  . LYS D  157 ? 0.3107 0.4065 0.5217 -0.0741 0.1551  -0.0475 157 LYS D NZ  
7634 N  N   . ILE D  158 ? 0.2067 0.1445 0.2277 0.0083  0.0010  -0.0232 158 ILE D N   
7635 C  CA  . ILE D  158 ? 0.2447 0.1533 0.2017 0.0030  0.0228  -0.0125 158 ILE D CA  
7636 C  C   . ILE D  158 ? 0.1953 0.1551 0.1870 0.0084  -0.0114 -0.0129 158 ILE D C   
7637 O  O   . ILE D  158 ? 0.2242 0.1692 0.1814 0.0135  -0.0218 -0.0125 158 ILE D O   
7638 C  CB  . ILE D  158 ? 0.2645 0.1694 0.1731 -0.0328 0.0229  -0.0125 158 ILE D CB  
7639 C  CG1 . ILE D  158 ? 0.3537 0.1991 0.2360 -0.0488 0.0669  -0.0500 158 ILE D CG1 
7640 C  CG2 . ILE D  158 ? 0.2427 0.1579 0.2157 -0.0184 0.0069  0.0120  158 ILE D CG2 
7641 C  CD1 . ILE D  158 ? 0.5050 0.2296 0.1973 -0.1030 0.0063  -0.0430 158 ILE D CD1 
7642 N  N   . PHE D  159 ? 0.1842 0.1680 0.1955 0.0168  0.0121  -0.0297 159 PHE D N   
7643 C  CA  . PHE D  159 ? 0.1835 0.1498 0.2012 0.0113  0.0023  -0.0203 159 PHE D CA  
7644 C  C   . PHE D  159 ? 0.1691 0.1876 0.1801 -0.0184 0.0044  -0.0514 159 PHE D C   
7645 O  O   . PHE D  159 ? 0.1949 0.2116 0.1946 -0.0034 0.0029  -0.0285 159 PHE D O   
7646 C  CB  . PHE D  159 ? 0.1644 0.1703 0.2043 -0.0109 -0.0206 -0.0145 159 PHE D CB  
7647 C  CG  . PHE D  159 ? 0.1604 0.1635 0.1889 0.0118  0.0039  -0.0247 159 PHE D CG  
7648 C  CD1 . PHE D  159 ? 0.2347 0.1864 0.2099 -0.0350 -0.0318 -0.0303 159 PHE D CD1 
7649 C  CD2 . PHE D  159 ? 0.1720 0.1622 0.2181 0.0096  0.0189  0.0027  159 PHE D CD2 
7650 C  CE1 . PHE D  159 ? 0.1826 0.2228 0.2273 -0.0276 -0.0414 -0.0066 159 PHE D CE1 
7651 C  CE2 . PHE D  159 ? 0.1456 0.1982 0.2430 0.0034  0.0186  0.0033  159 PHE D CE2 
7652 C  CZ  . PHE D  159 ? 0.1882 0.2153 0.2687 -0.0108 -0.0089 0.0044  159 PHE D CZ  
7653 N  N   . SER D  160 ? 0.2013 0.1995 0.1910 -0.0225 -0.0104 -0.0525 160 SER D N   
7654 C  CA  . SER D  160 ? 0.2049 0.2023 0.1584 -0.0398 -0.0146 -0.0326 160 SER D CA  
7655 C  C   . SER D  160 ? 0.1773 0.2486 0.2130 -0.0022 -0.0199 0.0003  160 SER D C   
7656 O  O   . SER D  160 ? 0.2520 0.2537 0.2120 -0.0044 -0.0375 -0.0269 160 SER D O   
7657 C  CB  . SER D  160 ? 0.1919 0.2915 0.2352 -0.0142 -0.0141 -0.0831 160 SER D CB  
7658 O  OG  . SER D  160 ? 0.2320 0.2849 0.2322 -0.0108 -0.0049 -0.0864 160 SER D OG  
7659 N  N   . HIS D  161 ? 0.1564 0.1958 0.2328 -0.0003 -0.0171 -0.0312 161 HIS D N   
7660 C  CA  . HIS D  161 ? 0.2030 0.1924 0.1978 -0.0021 -0.0132 -0.0255 161 HIS D CA  
7661 C  C   . HIS D  161 ? 0.2051 0.1873 0.1824 -0.0306 -0.0433 0.0129  161 HIS D C   
7662 O  O   . HIS D  161 ? 0.2249 0.1971 0.2126 -0.0205 -0.0432 0.0113  161 HIS D O   
7663 C  CB  . HIS D  161 ? 0.1896 0.2199 0.1878 -0.0011 -0.0024 -0.0204 161 HIS D CB  
7664 C  CG  . HIS D  161 ? 0.2155 0.2630 0.1995 0.0037  -0.0188 -0.0296 161 HIS D CG  
7665 N  ND1 . HIS D  161 ? 0.2432 0.2542 0.2383 0.0255  -0.0261 -0.0129 161 HIS D ND1 
7666 C  CD2 . HIS D  161 ? 0.1962 0.2451 0.2766 0.0402  0.0336  0.0050  161 HIS D CD2 
7667 C  CE1 . HIS D  161 ? 0.2952 0.2525 0.2973 -0.0035 0.0050  -0.0192 161 HIS D CE1 
7668 N  NE2 . HIS D  161 ? 0.2018 0.2773 0.2893 0.0286  0.0330  -0.0157 161 HIS D NE2 
7669 N  N   . LEU D  162 ? 0.1944 0.2460 0.1958 -0.0207 -0.0198 0.0053  162 LEU D N   
7670 C  CA  . LEU D  162 ? 0.2058 0.2579 0.2069 -0.0387 -0.0302 0.0185  162 LEU D CA  
7671 C  C   . LEU D  162 ? 0.2068 0.2230 0.2144 -0.0297 -0.0203 -0.0005 162 LEU D C   
7672 O  O   . LEU D  162 ? 0.2600 0.2716 0.2155 -0.0488 -0.0452 0.0414  162 LEU D O   
7673 C  CB  . LEU D  162 ? 0.2321 0.2843 0.2419 -0.0089 -0.0068 0.0298  162 LEU D CB  
7674 C  CG  . LEU D  162 ? 0.2483 0.2618 0.2200 -0.0405 -0.0179 0.0156  162 LEU D CG  
7675 C  CD1 . LEU D  162 ? 0.1750 0.3940 0.3935 0.0172  -0.0488 0.0391  162 LEU D CD1 
7676 C  CD2 . LEU D  162 ? 0.3795 0.3458 0.2298 -0.1307 -0.0900 0.0010  162 LEU D CD2 
7677 N  N   . GLN D  163 ? 0.2216 0.3700 0.2046 0.0070  -0.0270 -0.0137 163 GLN D N   
7678 C  CA  . GLN D  163 ? 0.3005 0.4141 0.2265 -0.0111 0.0278  0.0261  163 GLN D CA  
7679 C  C   . GLN D  163 ? 0.2615 0.4182 0.2415 0.0148  0.0032  0.1077  163 GLN D C   
7680 O  O   . GLN D  163 ? 0.3995 0.5473 0.3785 0.0401  0.0471  0.2487  163 GLN D O   
7681 C  CB  . GLN D  163 ? 0.3952 0.5994 0.3076 -0.0270 0.0016  -0.0754 163 GLN D CB  
7682 C  CG  . GLN D  163 ? 0.7665 0.4177 0.5739 0.0364  -0.0198 -0.2927 163 GLN D CG  
7683 C  CD  . GLN D  163 ? 0.6372 0.8804 0.4352 0.3447  0.0561  0.3077  163 GLN D CD  
7684 O  OE1 . GLN D  163 ? 0.2682 1.5601 1.8298 0.2917  0.4674  0.8293  163 GLN D OE1 
7685 N  NE2 . GLN D  163 ? 0.4953 0.4381 0.6151 0.1291  -0.2221 0.0368  163 GLN D NE2 
7686 N  N   . HIS D  164 ? 0.1961 0.3678 0.1876 -0.0195 -0.0425 0.0086  164 HIS D N   
7687 C  CA  . HIS D  164 ? 0.2456 0.3644 0.2459 -0.0304 -0.0374 0.0782  164 HIS D CA  
7688 C  C   . HIS D  164 ? 0.2397 0.3026 0.2410 -0.0099 -0.0603 0.0836  164 HIS D C   
7689 O  O   . HIS D  164 ? 0.2687 0.3240 0.3512 -0.0008 -0.0773 0.0908  164 HIS D O   
7690 C  CB  . HIS D  164 ? 0.2191 0.3563 0.2972 -0.0009 -0.0555 0.0372  164 HIS D CB  
7691 C  CG  . HIS D  164 ? 0.2643 0.4692 0.3261 -0.0030 -0.0403 -0.0021 164 HIS D CG  
7692 N  ND1 . HIS D  164 ? 0.4040 0.7092 0.4016 -0.0988 -0.0923 0.0154  164 HIS D ND1 
7693 C  CD2 . HIS D  164 ? 0.3353 0.5552 0.4868 -0.0787 -0.2353 -0.0156 164 HIS D CD2 
7694 C  CE1 . HIS D  164 ? 0.4985 0.6707 0.6809 -0.1102 -0.2301 0.0424  164 HIS D CE1 
7695 N  NE2 . HIS D  164 ? 0.4586 0.7937 0.5725 -0.2111 -0.2298 -0.0259 164 HIS D NE2 
7696 N  N   . VAL D  165 ? 0.1870 0.2681 0.2316 -0.0256 -0.0480 0.0730  165 VAL D N   
7697 C  CA  . VAL D  165 ? 0.1743 0.2645 0.2443 -0.0291 -0.0190 0.0392  165 VAL D CA  
7698 C  C   . VAL D  165 ? 0.1886 0.2254 0.2225 -0.0285 0.0109  0.0321  165 VAL D C   
7699 O  O   . VAL D  165 ? 0.1814 0.2309 0.2214 -0.0313 0.0006  0.0548  165 VAL D O   
7700 C  CB  . VAL D  165 ? 0.1906 0.2567 0.2450 -0.0032 0.0355  0.0515  165 VAL D CB  
7701 C  CG1 . VAL D  165 ? 0.1789 0.2621 0.3044 -0.0037 -0.0072 0.0100  165 VAL D CG1 
7702 C  CG2 . VAL D  165 ? 0.1972 0.2296 0.2125 -0.0314 -0.0317 0.0515  165 VAL D CG2 
7703 N  N   . LYS D  166 ? 0.1925 0.2131 0.2056 -0.0298 -0.0199 0.0380  166 LYS D N   
7704 C  CA  . LYS D  166 ? 0.2234 0.1922 0.2168 -0.0277 -0.0073 0.0522  166 LYS D CA  
7705 C  C   . LYS D  166 ? 0.1844 0.2105 0.2400 0.0061  0.0103  0.0291  166 LYS D C   
7706 O  O   . LYS D  166 ? 0.2049 0.1954 0.2516 -0.0205 -0.0171 0.0414  166 LYS D O   
7707 C  CB  . LYS D  166 ? 0.3210 0.2495 0.2242 -0.0021 0.0126  -0.0073 166 LYS D CB  
7708 C  CG  . LYS D  166 ? 0.3698 0.3532 0.2302 0.0490  0.0116  0.0526  166 LYS D CG  
7709 C  CD  . LYS D  166 ? 0.6271 0.6777 0.1605 0.0237  0.0467  0.0700  166 LYS D CD  
7710 N  N   . TYR D  167 ? 0.1922 0.1940 0.2518 -0.0263 -0.0005 0.0478  167 TYR D N   
7711 C  CA  . TYR D  167 ? 0.2008 0.1771 0.2096 -0.0295 0.0190  0.0201  167 TYR D CA  
7712 C  C   . TYR D  167 ? 0.2076 0.1782 0.1896 -0.0171 0.0074  0.0343  167 TYR D C   
7713 O  O   . TYR D  167 ? 0.1847 0.1852 0.2250 -0.0113 0.0133  0.0231  167 TYR D O   
7714 C  CB  . TYR D  167 ? 0.2350 0.1527 0.2342 0.0094  0.0467  0.0357  167 TYR D CB  
7715 C  CG  . TYR D  167 ? 0.3026 0.1839 0.2615 0.0042  0.0270  0.0328  167 TYR D CG  
7716 C  CD1 . TYR D  167 ? 0.2703 0.2205 0.2606 -0.0097 0.0555  0.0512  167 TYR D CD1 
7717 C  CD2 . TYR D  167 ? 0.3155 0.2428 0.2104 -0.0206 0.0443  0.0474  167 TYR D CD2 
7718 C  CE1 . TYR D  167 ? 0.3278 0.2066 0.3082 0.0475  0.0309  0.0392  167 TYR D CE1 
7719 C  CE2 . TYR D  167 ? 0.3577 0.2744 0.3291 0.0508  0.0949  0.0197  167 TYR D CE2 
7720 C  CZ  . TYR D  167 ? 0.2981 0.2006 0.2663 0.0092  0.0681  0.0003  167 TYR D CZ  
7721 O  OH  . TYR D  167 ? 0.4707 0.3032 0.3045 0.1140  0.0700  0.0086  167 TYR D OH  
7722 N  N   . LYS D  168 ? 0.1938 0.1993 0.1734 -0.0268 0.0021  0.0311  168 LYS D N   
7723 C  CA  . LYS D  168 ? 0.1988 0.2351 0.2028 -0.0069 0.0003  0.0126  168 LYS D CA  
7724 C  C   . LYS D  168 ? 0.2102 0.2114 0.2010 -0.0098 -0.0179 0.0373  168 LYS D C   
7725 O  O   . LYS D  168 ? 0.2432 0.2125 0.2541 0.0145  0.0012  0.0712  168 LYS D O   
7726 C  CB  . LYS D  168 ? 0.2451 0.2463 0.1894 -0.0354 -0.0042 0.0227  168 LYS D CB  
7727 C  CG  . LYS D  168 ? 0.2703 0.2224 0.2393 -0.0617 0.0066  0.0136  168 LYS D CG  
7728 C  CD  . LYS D  168 ? 0.2720 0.2460 0.2620 -0.0666 -0.0091 0.0234  168 LYS D CD  
7729 C  CE  . LYS D  168 ? 0.4036 0.3137 0.3999 -0.0974 -0.0089 -0.1103 168 LYS D CE  
7730 N  NZ  . LYS D  168 ? 0.3953 0.4118 0.4462 -0.1254 -0.0685 0.0031  168 LYS D NZ  
7731 N  N   . GLY D  169 ? 0.2289 0.2128 0.2329 -0.0187 0.0282  0.0300  169 GLY D N   
7732 C  CA  . GLY D  169 ? 0.2818 0.2017 0.3062 0.0067  0.0009  -0.0278 169 GLY D CA  
7733 C  C   . GLY D  169 ? 0.2399 0.2485 0.3094 -0.0222 0.0292  0.0071  169 GLY D C   
7734 O  O   . GLY D  169 ? 0.2398 0.2647 0.4277 0.0321  0.0139  0.0072  169 GLY D O   
7735 N  N   . GLN D  170 ? 0.2225 0.2059 0.2713 -0.0256 0.0337  0.0359  170 GLN D N   
7736 C  CA  . GLN D  170 ? 0.2069 0.1807 0.2949 -0.0285 0.0218  0.0640  170 GLN D CA  
7737 C  C   . GLN D  170 ? 0.1480 0.2080 0.2618 -0.0212 -0.0186 0.0762  170 GLN D C   
7738 O  O   . GLN D  170 ? 0.2003 0.2158 0.2254 -0.0164 -0.0336 0.0490  170 GLN D O   
7739 C  CB  . GLN D  170 ? 0.2297 0.2502 0.2329 -0.0148 -0.0161 0.1005  170 GLN D CB  
7740 C  CG  . GLN D  170 ? 0.2520 0.2315 0.2565 0.0310  0.0203  0.0751  170 GLN D CG  
7741 C  CD  . GLN D  170 ? 0.2861 0.2708 0.2168 0.0359  -0.0254 0.0632  170 GLN D CD  
7742 O  OE1 . GLN D  170 ? 0.2796 0.2600 0.2258 0.0117  -0.0089 0.0608  170 GLN D OE1 
7743 N  NE2 . GLN D  170 ? 0.3795 0.3961 0.2536 0.0988  0.0672  0.1472  170 GLN D NE2 
7744 N  N   . GLU D  171 ? 0.1573 0.3017 0.2309 -0.0208 -0.0150 0.0915  171 GLU D N   
7745 C  CA  . GLU D  171 ? 0.2295 0.2758 0.2474 -0.0838 0.0020  0.0716  171 GLU D CA  
7746 C  C   . GLU D  171 ? 0.1831 0.3392 0.2405 -0.0559 -0.0433 0.0658  171 GLU D C   
7747 O  O   . GLU D  171 ? 0.2611 0.4341 0.2302 -0.0102 -0.0378 0.1077  171 GLU D O   
7748 C  CB  . GLU D  171 ? 0.2667 0.4049 0.3638 -0.0573 0.1015  0.0102  171 GLU D CB  
7749 C  CG  . GLU D  171 ? 0.3114 0.3698 0.3897 0.0187  0.0762  0.0697  171 GLU D CG  
7750 C  CD  . GLU D  171 ? 0.6567 0.3884 0.5956 0.1072  0.0957  0.0660  171 GLU D CD  
7751 O  OE1 . GLU D  171 ? 0.6921 0.5079 0.5649 0.0692  0.0795  0.2491  171 GLU D OE1 
7752 O  OE2 . GLU D  171 ? 0.6042 0.2636 0.6434 0.0723  0.2545  0.0649  171 GLU D OE2 
7753 N  N   . ALA D  172 ? 0.2124 0.3209 0.1833 -0.0621 -0.0231 0.0425  172 ALA D N   
7754 C  CA  . ALA D  172 ? 0.2253 0.3482 0.1676 -0.0922 -0.0443 0.0445  172 ALA D CA  
7755 C  C   . ALA D  172 ? 0.1652 0.3191 0.1807 -0.0262 -0.0449 0.0754  172 ALA D C   
7756 O  O   . ALA D  172 ? 0.1753 0.3714 0.1645 -0.0493 -0.0337 0.0451  172 ALA D O   
7757 C  CB  . ALA D  172 ? 0.2530 0.3912 0.2495 -0.0917 -0.0055 -0.0414 172 ALA D CB  
7758 N  N   . PHE D  173 ? 0.1781 0.3612 0.2138 -0.0599 -0.0330 0.0553  173 PHE D N   
7759 C  CA  . PHE D  173 ? 0.1916 0.2717 0.1927 -0.0535 -0.0077 0.0518  173 PHE D CA  
7760 C  C   . PHE D  173 ? 0.2112 0.2887 0.2190 -0.0498 -0.0344 -0.0298 173 PHE D C   
7761 O  O   . PHE D  173 ? 0.2974 0.3471 0.2280 -0.0782 -0.0312 -0.0518 173 PHE D O   
7762 C  CB  . PHE D  173 ? 0.1397 0.3343 0.3542 -0.0359 -0.0502 0.0183  173 PHE D CB  
7763 C  CG  . PHE D  173 ? 0.2065 0.2793 0.3860 0.0245  -0.0497 0.0471  173 PHE D CG  
7764 C  CD1 . PHE D  173 ? 0.2321 0.4147 0.4781 -0.0092 -0.0322 0.0546  173 PHE D CD1 
7765 C  CD2 . PHE D  173 ? 0.2715 0.4348 0.6642 -0.0080 0.0048  0.2256  173 PHE D CD2 
7766 C  CE1 . PHE D  173 ? 0.2944 0.4791 0.5006 0.1068  -0.0908 0.0334  173 PHE D CE1 
7767 C  CE2 . PHE D  173 ? 0.5387 0.4279 0.5614 0.0815  -0.0027 0.2353  173 PHE D CE2 
7768 C  CZ  . PHE D  173 ? 0.5980 0.5008 0.6237 0.2453  -0.1323 0.1066  173 PHE D CZ  
7769 N  N   . VAL D  174 ? 0.1751 0.2293 0.2037 -0.0370 0.0092  0.0141  174 VAL D N   
7770 C  CA  . VAL D  174 ? 0.1892 0.2459 0.2359 -0.0487 0.0196  -0.0083 174 VAL D CA  
7771 C  C   . VAL D  174 ? 0.1468 0.1997 0.2536 -0.0372 0.0120  -0.0359 174 VAL D C   
7772 O  O   . VAL D  174 ? 0.1722 0.2264 0.2222 -0.0182 0.0130  -0.0472 174 VAL D O   
7773 C  CB  . VAL D  174 ? 0.1148 0.2604 0.2728 0.0174  0.0111  -0.0267 174 VAL D CB  
7774 C  CG1 . VAL D  174 ? 0.1969 0.2489 0.2827 -0.0100 0.0086  -0.0234 174 VAL D CG1 
7775 C  CG2 . VAL D  174 ? 0.1449 0.3307 0.2882 -0.0069 0.0226  -0.0266 174 VAL D CG2 
7776 N  N   . PRO D  175 ? 0.1596 0.2161 0.2299 -0.0225 0.0008  -0.0212 175 PRO D N   
7777 C  CA  . PRO D  175 ? 0.1451 0.2444 0.2112 -0.0406 0.0171  -0.0075 175 PRO D CA  
7778 C  C   . PRO D  175 ? 0.1729 0.1967 0.2277 -0.0086 0.0166  -0.0077 175 PRO D C   
7779 O  O   . PRO D  175 ? 0.1907 0.2087 0.2368 0.0062  0.0237  -0.0054 175 PRO D O   
7780 C  CB  . PRO D  175 ? 0.2208 0.2550 0.2300 -0.0602 0.0136  -0.0251 175 PRO D CB  
7781 C  CG  . PRO D  175 ? 0.2215 0.3928 0.2795 -0.1209 0.0259  -0.0396 175 PRO D CG  
7782 C  CD  . PRO D  175 ? 0.1835 0.2299 0.2139 -0.0369 0.0038  -0.0414 175 PRO D CD  
7783 N  N   . GLY D  176 ? 0.1821 0.2294 0.1978 -0.0077 0.0211  0.0109  176 GLY D N   
7784 C  CA  . GLY D  176 ? 0.2064 0.1725 0.2089 -0.0026 0.0085  0.0023  176 GLY D CA  
7785 C  C   . GLY D  176 ? 0.1694 0.1888 0.2428 -0.0044 0.0206  -0.0096 176 GLY D C   
7786 O  O   . GLY D  176 ? 0.2346 0.2317 0.2499 -0.0431 0.0124  -0.0339 176 GLY D O   
7787 N  N   . PHE D  177 ? 0.1678 0.1922 0.2697 0.0078  0.0115  0.0156  177 PHE D N   
7788 C  CA  . PHE D  177 ? 0.1888 0.1716 0.2785 -0.0037 0.0295  -0.0245 177 PHE D CA  
7789 C  C   . PHE D  177 ? 0.1663 0.1631 0.2613 -0.0080 0.0245  0.0198  177 PHE D C   
7790 O  O   . PHE D  177 ? 0.1943 0.1893 0.2597 -0.0141 0.0115  0.0006  177 PHE D O   
7791 C  CB  . PHE D  177 ? 0.2024 0.1983 0.2560 -0.0103 -0.0010 -0.0212 177 PHE D CB  
7792 C  CG  . PHE D  177 ? 0.1891 0.2280 0.2409 0.0214  -0.0031 -0.0272 177 PHE D CG  
7793 C  CD1 . PHE D  177 ? 0.1730 0.2385 0.2468 0.0159  0.0379  -0.0455 177 PHE D CD1 
7794 C  CD2 . PHE D  177 ? 0.2640 0.2155 0.2676 0.0423  -0.0135 -0.0535 177 PHE D CD2 
7795 C  CE1 . PHE D  177 ? 0.1644 0.2782 0.2294 0.0418  0.0141  -0.0325 177 PHE D CE1 
7796 C  CE2 . PHE D  177 ? 0.2431 0.2994 0.2892 0.0413  0.0461  -0.0340 177 PHE D CE2 
7797 C  CZ  . PHE D  177 ? 0.1745 0.3033 0.2520 0.0564  0.0285  -0.0184 177 PHE D CZ  
7798 N  N   . ASN D  178 ? 0.2129 0.1766 0.3041 -0.0296 -0.0077 0.0313  178 ASN D N   
7799 C  CA  . ASN D  178 ? 0.1706 0.1953 0.3310 -0.0314 0.0068  0.0532  178 ASN D CA  
7800 C  C   . ASN D  178 ? 0.1518 0.1821 0.2888 -0.0105 0.0121  -0.0074 178 ASN D C   
7801 O  O   . ASN D  178 ? 0.1975 0.1620 0.2876 -0.0052 0.0366  -0.0027 178 ASN D O   
7802 C  CB  . ASN D  178 ? 0.2079 0.2164 0.3608 -0.0446 -0.0089 0.0825  178 ASN D CB  
7803 C  CG  . ASN D  178 ? 0.1906 0.2337 0.3360 -0.0214 0.0474  0.0583  178 ASN D CG  
7804 O  OD1 . ASN D  178 ? 0.2086 0.2506 0.2863 -0.0086 0.0516  0.0509  178 ASN D OD1 
7805 N  ND2 . ASN D  178 ? 0.3125 0.2574 0.4307 -0.1111 0.0132  0.0961  178 ASN D ND2 
7806 N  N   . ILE D  179 ? 0.1625 0.1788 0.2395 -0.0311 0.0341  0.0065  179 ILE D N   
7807 C  CA  . ILE D  179 ? 0.1397 0.1876 0.2405 -0.0072 0.0156  0.0124  179 ILE D CA  
7808 C  C   . ILE D  179 ? 0.1481 0.1885 0.2431 0.0005  0.0370  0.0135  179 ILE D C   
7809 O  O   . ILE D  179 ? 0.1474 0.1942 0.2368 0.0068  0.0332  -0.0096 179 ILE D O   
7810 C  CB  . ILE D  179 ? 0.1706 0.1701 0.2193 -0.0146 0.0442  0.0019  179 ILE D CB  
7811 C  CG1 . ILE D  179 ? 0.1628 0.2323 0.2274 -0.0008 0.0359  0.0283  179 ILE D CG1 
7812 C  CG2 . ILE D  179 ? 0.1458 0.2127 0.2469 0.0081  0.0302  -0.0361 179 ILE D CG2 
7813 C  CD1 . ILE D  179 ? 0.1837 0.1953 0.2581 -0.0054 0.0407  0.0011  179 ILE D CD1 
7814 N  N   . GLU D  180 ? 0.1594 0.1612 0.2649 -0.0023 0.0550  0.0136  180 GLU D N   
7815 C  CA  . GLU D  180 ? 0.1780 0.1946 0.2491 -0.0006 0.0571  0.0027  180 GLU D CA  
7816 C  C   . GLU D  180 ? 0.1714 0.1817 0.2141 -0.0019 0.0693  0.0129  180 GLU D C   
7817 O  O   . GLU D  180 ? 0.1716 0.1796 0.2660 -0.0076 0.0414  0.0361  180 GLU D O   
7818 C  CB  . GLU D  180 ? 0.1728 0.2398 0.3454 0.0162  0.0900  0.0740  180 GLU D CB  
7819 C  CG  . GLU D  180 ? 0.3031 0.2710 0.3480 -0.0254 0.0614  0.0700  180 GLU D CG  
7820 C  CD  . GLU D  180 ? 0.3520 0.3666 0.3921 -0.0767 0.1094  0.1509  180 GLU D CD  
7821 O  OE1 . GLU D  180 ? 0.4300 0.4244 0.4173 -0.0013 0.1738  0.1454  180 GLU D OE1 
7822 O  OE2 . GLU D  180 ? 0.3838 0.4943 0.3515 -0.0358 0.1229  0.1257  180 GLU D OE2 
7823 N  N   . GLU D  181 ? 0.1455 0.1748 0.2615 -0.0176 0.0612  -0.0032 181 GLU D N   
7824 C  CA  . GLU D  181 ? 0.1658 0.1718 0.2415 -0.0126 0.0438  -0.0164 181 GLU D CA  
7825 C  C   . GLU D  181 ? 0.1538 0.1471 0.2538 -0.0105 0.0230  0.0006  181 GLU D C   
7826 O  O   . GLU D  181 ? 0.1767 0.1527 0.2878 0.0013  0.0353  -0.0234 181 GLU D O   
7827 C  CB  . GLU D  181 ? 0.1706 0.2488 0.2522 0.0029  0.0405  -0.0126 181 GLU D CB  
7828 C  CG  . GLU D  181 ? 0.1727 0.2878 0.3350 -0.0155 0.0037  -0.0266 181 GLU D CG  
7829 C  CD  . GLU D  181 ? 0.2536 0.3525 0.3656 -0.0921 -0.0121 -0.0431 181 GLU D CD  
7830 O  OE1 . GLU D  181 ? 0.3235 0.3579 0.3516 0.0016  0.0200  -0.0288 181 GLU D OE1 
7831 O  OE2 . GLU D  181 ? 0.2558 0.3356 0.4131 -0.0590 -0.0379 -0.0361 181 GLU D OE2 
7832 N  N   . LEU D  182 ? 0.1412 0.1449 0.2092 -0.0132 0.0120  -0.0058 182 LEU D N   
7833 C  CA  . LEU D  182 ? 0.1335 0.1520 0.2137 -0.0136 0.0264  -0.0073 182 LEU D CA  
7834 C  C   . LEU D  182 ? 0.1427 0.1280 0.1828 0.0024  0.0316  -0.0089 182 LEU D C   
7835 O  O   . LEU D  182 ? 0.1476 0.1586 0.2137 -0.0072 0.0317  0.0011  182 LEU D O   
7836 C  CB  . LEU D  182 ? 0.1538 0.1427 0.2170 0.0030  0.0249  0.0110  182 LEU D CB  
7837 C  CG  . LEU D  182 ? 0.1432 0.1606 0.1954 0.0082  0.0335  -0.0011 182 LEU D CG  
7838 C  CD1 . LEU D  182 ? 0.1699 0.1520 0.2136 0.0055  0.0339  -0.0072 182 LEU D CD1 
7839 C  CD2 . LEU D  182 ? 0.1711 0.1504 0.2171 -0.0013 0.0376  -0.0072 182 LEU D CD2 
7840 N  N   . LEU D  183 ? 0.1758 0.1591 0.2145 -0.0198 0.0445  0.0085  183 LEU D N   
7841 C  CA  . LEU D  183 ? 0.2146 0.1584 0.1933 -0.0039 0.0380  0.0223  183 LEU D CA  
7842 C  C   . LEU D  183 ? 0.1782 0.1564 0.1851 -0.0262 0.0108  -0.0021 183 LEU D C   
7843 O  O   . LEU D  183 ? 0.1767 0.1620 0.2483 -0.0146 0.0095  -0.0096 183 LEU D O   
7844 C  CB  . LEU D  183 ? 0.2169 0.1769 0.2095 -0.0074 0.0686  0.0083  183 LEU D CB  
7845 C  CG  . LEU D  183 ? 0.2393 0.1502 0.2230 -0.0004 0.0457  -0.0050 183 LEU D CG  
7846 C  CD1 . LEU D  183 ? 0.3433 0.2545 0.2374 0.0635  0.1134  0.0243  183 LEU D CD1 
7847 C  CD2 . LEU D  183 ? 0.2371 0.2050 0.2922 0.0013  0.0274  0.0036  183 LEU D CD2 
7848 N  N   . PRO D  184 ? 0.1746 0.1456 0.1741 -0.0138 0.0392  -0.0036 184 PRO D N   
7849 C  CA  . PRO D  184 ? 0.1945 0.1674 0.2646 -0.0174 0.0494  0.0001  184 PRO D CA  
7850 C  C   . PRO D  184 ? 0.2552 0.1478 0.2408 -0.0380 0.0545  -0.0218 184 PRO D C   
7851 O  O   . PRO D  184 ? 0.2963 0.2025 0.2708 -0.0464 0.1078  0.0173  184 PRO D O   
7852 C  CB  . PRO D  184 ? 0.2136 0.1791 0.1946 -0.0128 0.0005  -0.0094 184 PRO D CB  
7853 C  CG  . PRO D  184 ? 0.1742 0.1976 0.1803 0.0228  0.0048  -0.0158 184 PRO D CG  
7854 C  CD  . PRO D  184 ? 0.1564 0.1980 0.1962 -0.0201 0.0306  0.0188  184 PRO D CD  
7855 N  N   . GLU D  185 ? 0.2474 0.1580 0.2609 -0.0190 0.0329  0.0274  185 GLU D N   
7856 C  CA  . GLU D  185 ? 0.2530 0.1802 0.2723 -0.0268 0.0479  0.0283  185 GLU D CA  
7857 C  C   . GLU D  185 ? 0.2432 0.2404 0.2742 -0.0582 0.0251  0.0245  185 GLU D C   
7858 O  O   . GLU D  185 ? 0.2305 0.2320 0.2744 -0.0400 0.0266  0.0702  185 GLU D O   
7859 C  CB  . GLU D  185 ? 0.3671 0.1615 0.2870 0.0070  -0.0197 0.0024  185 GLU D CB  
7860 C  CG  . GLU D  185 ? 0.5319 0.1780 0.3064 -0.0346 0.0257  -0.0354 185 GLU D CG  
7861 N  N   . ARG D  186 ? 0.2602 0.1651 0.2444 -0.0388 0.0550  0.0021  186 ARG D N   
7862 C  CA  . ARG D  186 ? 0.2622 0.2019 0.2467 -0.0427 0.0067  0.0365  186 ARG D CA  
7863 C  C   . ARG D  186 ? 0.2183 0.2072 0.2307 -0.0023 0.0673  0.0337  186 ARG D C   
7864 O  O   . ARG D  186 ? 0.2258 0.2021 0.2386 0.0065  0.0472  0.0173  186 ARG D O   
7865 C  CB  . ARG D  186 ? 0.3503 0.1698 0.3125 -0.0059 0.0584  0.0417  186 ARG D CB  
7866 C  CG  . ARG D  186 ? 0.4535 0.1514 0.4029 0.0162  0.0438  0.0365  186 ARG D CG  
7867 C  CD  . ARG D  186 ? 0.5335 0.3230 0.5102 0.0866  -0.0041 0.1309  186 ARG D CD  
7868 N  NE  . ARG D  186 ? 0.6583 0.2276 0.5086 -0.0796 0.0234  -0.0189 186 ARG D NE  
7869 C  CZ  . ARG D  186 ? 0.8301 0.2566 0.7161 0.0081  0.0759  -0.1895 186 ARG D CZ  
7870 N  NH1 . ARG D  186 ? 0.9581 0.4379 0.3865 -0.1302 -0.0774 0.0416  186 ARG D NH1 
7871 N  NH2 . ARG D  186 ? 1.0238 0.6059 0.6594 -0.0502 0.2312  -0.2062 186 ARG D NH2 
7872 N  N   . THR D  187 ? 0.2302 0.1734 0.2292 0.0100  0.0472  0.0345  187 THR D N   
7873 C  CA  . THR D  187 ? 0.1910 0.1769 0.2680 -0.0095 0.0369  0.0373  187 THR D CA  
7874 C  C   . THR D  187 ? 0.2216 0.1646 0.2184 0.0043  0.0458  0.0249  187 THR D C   
7875 O  O   . THR D  187 ? 0.2313 0.2167 0.1978 0.0034  0.0615  0.0424  187 THR D O   
7876 C  CB  . THR D  187 ? 0.1929 0.2040 0.1924 0.0008  0.0364  0.0590  187 THR D CB  
7877 O  OG1 . THR D  187 ? 0.2092 0.2392 0.2770 0.0150  0.0408  0.0532  187 THR D OG1 
7878 C  CG2 . THR D  187 ? 0.2550 0.2292 0.2278 0.0146  -0.0036 0.0254  187 THR D CG2 
7879 N  N   . ALA D  188 ? 0.1834 0.2067 0.2057 -0.0044 0.0436  0.0222  188 ALA D N   
7880 C  CA  . ALA D  188 ? 0.2129 0.2330 0.2015 -0.0215 0.0309  0.0675  188 ALA D CA  
7881 C  C   . ALA D  188 ? 0.1870 0.1908 0.1805 -0.0142 0.0392  0.0345  188 ALA D C   
7882 O  O   . ALA D  188 ? 0.1981 0.2149 0.2065 0.0082  0.0434  0.0391  188 ALA D O   
7883 C  CB  . ALA D  188 ? 0.2398 0.2560 0.2197 -0.0309 0.0525  0.0834  188 ALA D CB  
7884 N  N   . GLU D  189 ? 0.2019 0.1811 0.2229 0.0036  0.0620  0.0596  189 GLU D N   
7885 C  CA  . GLU D  189 ? 0.2019 0.1526 0.2161 0.0055  0.0345  0.0577  189 GLU D CA  
7886 C  C   . GLU D  189 ? 0.1527 0.1324 0.1671 0.0177  0.0381  0.0342  189 GLU D C   
7887 O  O   . GLU D  189 ? 0.1648 0.1544 0.1782 -0.0049 0.0398  0.0010  189 GLU D O   
7888 C  CB  . GLU D  189 ? 0.2462 0.1540 0.2406 -0.0229 0.0410  0.0423  189 GLU D CB  
7889 C  CG  . GLU D  189 ? 0.2874 0.1851 0.2928 -0.0288 0.0655  0.0272  189 GLU D CG  
7890 C  CD  . GLU D  189 ? 0.2843 0.2583 0.4486 -0.0788 0.0600  -0.0318 189 GLU D CD  
7891 O  OE1 . GLU D  189 ? 0.3294 0.1931 0.4400 -0.0078 0.1063  0.0402  189 GLU D OE1 
7892 O  OE2 . GLU D  189 ? 0.5681 0.2904 0.7751 -0.1464 0.2089  0.0100  189 GLU D OE2 
7893 N  N   . TYR D  190 ? 0.1703 0.1584 0.1694 0.0041  0.0350  0.0226  190 TYR D N   
7894 C  CA  . TYR D  190 ? 0.1652 0.1342 0.1400 0.0016  0.0398  0.0179  190 TYR D CA  
7895 C  C   . TYR D  190 ? 0.1676 0.1567 0.1449 0.0186  0.0267  0.0087  190 TYR D C   
7896 O  O   . TYR D  190 ? 0.1949 0.1499 0.1484 0.0131  0.0392  0.0290  190 TYR D O   
7897 C  CB  . TYR D  190 ? 0.1840 0.1785 0.1603 0.0348  0.0655  0.0414  190 TYR D CB  
7898 C  CG  . TYR D  190 ? 0.1626 0.1495 0.1575 0.0294  0.0406  0.0274  190 TYR D CG  
7899 C  CD1 . TYR D  190 ? 0.1801 0.1474 0.1540 0.0158  0.0398  0.0194  190 TYR D CD1 
7900 C  CD2 . TYR D  190 ? 0.1730 0.1849 0.1989 0.0244  0.0530  0.0328  190 TYR D CD2 
7901 C  CE1 . TYR D  190 ? 0.1785 0.1881 0.1703 0.0334  0.0669  0.0498  190 TYR D CE1 
7902 C  CE2 . TYR D  190 ? 0.1601 0.1856 0.1706 0.0148  0.0446  0.0234  190 TYR D CE2 
7903 C  CZ  . TYR D  190 ? 0.1870 0.1990 0.1696 0.0225  0.0248  0.0302  190 TYR D CZ  
7904 O  OH  . TYR D  190 ? 0.2035 0.1984 0.1625 0.0432  0.0594  0.0268  190 TYR D OH  
7905 N  N   . TYR D  191 ? 0.1560 0.1417 0.1313 0.0078  0.0374  0.0332  191 TYR D N   
7906 C  CA  . TYR D  191 ? 0.1712 0.1520 0.1353 0.0166  0.0315  0.0247  191 TYR D CA  
7907 C  C   . TYR D  191 ? 0.1535 0.1497 0.1396 0.0184  0.0255  0.0287  191 TYR D C   
7908 O  O   . TYR D  191 ? 0.2080 0.1610 0.1265 0.0320  0.0153  0.0204  191 TYR D O   
7909 C  CB  . TYR D  191 ? 0.1807 0.1357 0.1425 0.0198  0.0454  0.0190  191 TYR D CB  
7910 C  CG  . TYR D  191 ? 0.1779 0.1472 0.1263 0.0095  0.0260  0.0245  191 TYR D CG  
7911 C  CD1 . TYR D  191 ? 0.1848 0.1493 0.1472 0.0325  0.0496  0.0203  191 TYR D CD1 
7912 C  CD2 . TYR D  191 ? 0.1678 0.1518 0.1591 0.0077  0.0322  0.0197  191 TYR D CD2 
7913 C  CE1 . TYR D  191 ? 0.1731 0.1640 0.1834 0.0343  0.0313  -0.0016 191 TYR D CE1 
7914 C  CE2 . TYR D  191 ? 0.1581 0.1795 0.1932 0.0043  0.0572  0.0207  191 TYR D CE2 
7915 C  CZ  . TYR D  191 ? 0.1717 0.1515 0.1823 0.0141  0.0408  0.0010  191 TYR D CZ  
7916 O  OH  . TYR D  191 ? 0.2393 0.1711 0.2315 0.0574  0.0529  -0.0160 191 TYR D OH  
7917 N  N   . ARG D  192 ? 0.1857 0.1396 0.1463 0.0079  0.0340  0.0141  192 ARG D N   
7918 C  CA  . ARG D  192 ? 0.1973 0.1319 0.1382 0.0214  0.0193  0.0212  192 ARG D CA  
7919 C  C   . ARG D  192 ? 0.1736 0.1443 0.1375 0.0243  0.0122  0.0060  192 ARG D C   
7920 O  O   . ARG D  192 ? 0.2026 0.1495 0.1443 0.0200  0.0078  0.0219  192 ARG D O   
7921 C  CB  . ARG D  192 ? 0.2028 0.1643 0.1661 0.0410  0.0341  0.0195  192 ARG D CB  
7922 C  CG  . ARG D  192 ? 0.2315 0.2133 0.2209 0.0804  0.0540  0.0151  192 ARG D CG  
7923 C  CD  . ARG D  192 ? 0.2722 0.2016 0.1635 0.0317  0.0120  0.0011  192 ARG D CD  
7924 N  NE  . ARG D  192 ? 0.2303 0.1752 0.2119 0.0578  0.0333  0.0218  192 ARG D NE  
7925 C  CZ  . ARG D  192 ? 0.2363 0.1886 0.1649 0.0392  0.0289  0.0172  192 ARG D CZ  
7926 N  NH1 . ARG D  192 ? 0.3251 0.2974 0.1669 0.1449  0.0648  0.0414  192 ARG D NH1 
7927 N  NH2 . ARG D  192 ? 0.2351 0.1818 0.2226 0.0526  0.0403  0.0468  192 ARG D NH2 
7928 N  N   . TYR D  193 ? 0.1907 0.1518 0.1217 0.0280  0.0277  0.0132  193 TYR D N   
7929 C  CA  . TYR D  193 ? 0.1914 0.1611 0.1194 0.0083  0.0048  0.0247  193 TYR D CA  
7930 C  C   . TYR D  193 ? 0.1955 0.1489 0.1150 0.0040  -0.0073 -0.0009 193 TYR D C   
7931 O  O   . TYR D  193 ? 0.2187 0.1542 0.1242 0.0419  0.0057  -0.0048 193 TYR D O   
7932 C  CB  . TYR D  193 ? 0.1786 0.1623 0.1168 0.0216  -0.0065 0.0270  193 TYR D CB  
7933 C  CG  . TYR D  193 ? 0.1845 0.1341 0.1372 0.0248  0.0013  0.0097  193 TYR D CG  
7934 C  CD1 . TYR D  193 ? 0.1787 0.1508 0.1424 0.0282  0.0004  0.0069  193 TYR D CD1 
7935 C  CD2 . TYR D  193 ? 0.2028 0.1559 0.1363 0.0182  0.0078  0.0100  193 TYR D CD2 
7936 C  CE1 . TYR D  193 ? 0.1670 0.1301 0.1329 0.0107  0.0082  0.0147  193 TYR D CE1 
7937 C  CE2 . TYR D  193 ? 0.2149 0.1646 0.1249 0.0323  0.0069  -0.0049 193 TYR D CE2 
7938 C  CZ  . TYR D  193 ? 0.1733 0.1439 0.1267 0.0129  0.0109  0.0059  193 TYR D CZ  
7939 O  OH  . TYR D  193 ? 0.1787 0.1344 0.1278 0.0154  0.0151  0.0064  193 TYR D OH  
7940 N  N   . ARG D  194 ? 0.2426 0.1692 0.1212 -0.0164 -0.0059 0.0257  194 ARG D N   
7941 C  CA  . ARG D  194 ? 0.2945 0.1642 0.1451 0.0087  0.0425  -0.0187 194 ARG D CA  
7942 C  C   . ARG D  194 ? 0.2235 0.1730 0.1242 0.0081  0.0122  -0.0117 194 ARG D C   
7943 O  O   . ARG D  194 ? 0.2615 0.1689 0.1356 0.0114  -0.0247 0.0165  194 ARG D O   
7944 C  CB  . ARG D  194 ? 0.3882 0.2206 0.1376 -0.0035 0.0474  -0.0284 194 ARG D CB  
7945 C  CG  . ARG D  194 ? 0.5596 0.3362 0.1781 -0.0985 0.0991  -0.0062 194 ARG D CG  
7946 C  CD  . ARG D  194 ? 0.5279 0.4287 0.3674 0.0109  0.1600  0.0251  194 ARG D CD  
7947 N  NE  . ARG D  194 ? 0.8808 0.7634 0.5052 -0.0348 0.3565  0.1574  194 ARG D NE  
7948 C  CZ  . ARG D  194 ? 0.8742 0.9642 0.9218 0.0743  0.3729  0.0538  194 ARG D CZ  
7949 N  NH1 . ARG D  194 ? 1.8485 0.9875 0.7160 0.2328  0.8965  0.2133  194 ARG D NH1 
7950 N  NH2 . ARG D  194 ? 0.9370 0.6612 0.6304 0.0783  0.2559  0.1244  194 ARG D NH2 
7951 N  N   . GLY D  195 ? 0.2415 0.1463 0.1049 0.0136  -0.0043 -0.0034 195 GLY D N   
7952 C  CA  . GLY D  195 ? 0.2282 0.1471 0.1273 0.0036  -0.0046 0.0179  195 GLY D CA  
7953 C  C   . GLY D  195 ? 0.1970 0.1575 0.1249 0.0295  0.0017  0.0005  195 GLY D C   
7954 O  O   . GLY D  195 ? 0.2196 0.1471 0.1190 0.0185  0.0149  -0.0124 195 GLY D O   
7955 N  N   . SER D  196 ? 0.1944 0.1149 0.1140 0.0074  0.0068  -0.0006 196 SER D N   
7956 C  CA  . SER D  196 ? 0.1935 0.1021 0.1231 0.0254  -0.0088 0.0064  196 SER D CA  
7957 C  C   . SER D  196 ? 0.1733 0.1207 0.1231 0.0198  0.0025  0.0013  196 SER D C   
7958 O  O   . SER D  196 ? 0.1689 0.1191 0.1263 0.0091  -0.0005 -0.0042 196 SER D O   
7959 C  CB  . SER D  196 ? 0.1923 0.1592 0.1212 0.0353  -0.0069 -0.0179 196 SER D CB  
7960 O  OG  . SER D  196 ? 0.1883 0.1244 0.1310 0.0067  -0.0026 -0.0129 196 SER D OG  
7961 N  N   . LEU D  197 ? 0.1791 0.1204 0.1161 0.0134  0.0005  -0.0033 197 LEU D N   
7962 C  CA  . LEU D  197 ? 0.1711 0.1193 0.1067 0.0082  0.0006  0.0122  197 LEU D CA  
7963 C  C   . LEU D  197 ? 0.1479 0.1052 0.1329 0.0024  -0.0129 0.0083  197 LEU D C   
7964 O  O   . LEU D  197 ? 0.1645 0.1303 0.1173 0.0030  0.0039  -0.0005 197 LEU D O   
7965 C  CB  . LEU D  197 ? 0.1545 0.1115 0.1446 0.0103  0.0135  -0.0013 197 LEU D CB  
7966 C  CG  . LEU D  197 ? 0.1829 0.1198 0.1730 0.0195  -0.0184 0.0073  197 LEU D CG  
7967 C  CD1 . LEU D  197 ? 0.2694 0.1764 0.1778 0.0736  0.0602  0.0402  197 LEU D CD1 
7968 C  CD2 . LEU D  197 ? 0.2196 0.1573 0.1477 0.0498  -0.0039 0.0122  197 LEU D CD2 
7969 N  N   . THR D  198 ? 0.1516 0.1089 0.1124 0.0053  0.0110  0.0022  198 THR D N   
7970 C  CA  . THR D  198 ? 0.1397 0.1210 0.1231 -0.0029 0.0061  -0.0038 198 THR D CA  
7971 C  C   . THR D  198 ? 0.1345 0.1044 0.1147 0.0000  0.0126  -0.0080 198 THR D C   
7972 O  O   . THR D  198 ? 0.1434 0.1141 0.1258 -0.0005 0.0081  0.0015  198 THR D O   
7973 C  CB  . THR D  198 ? 0.1372 0.0992 0.1222 0.0017  -0.0069 -0.0006 198 THR D CB  
7974 O  OG1 . THR D  198 ? 0.1329 0.1235 0.1112 -0.0039 -0.0012 -0.0004 198 THR D OG1 
7975 C  CG2 . THR D  198 ? 0.1685 0.1167 0.1235 0.0084  0.0150  0.0089  198 THR D CG2 
7976 N  N   . THR D  199 ? 0.1512 0.1121 0.1222 0.0052  -0.0003 0.0030  199 THR D N   
7977 C  CA  . THR D  199 ? 0.1507 0.1023 0.1285 -0.0057 -0.0060 0.0079  199 THR D CA  
7978 C  C   . THR D  199 ? 0.1641 0.1282 0.1236 -0.0009 -0.0046 -0.0049 199 THR D C   
7979 O  O   . THR D  199 ? 0.1800 0.1316 0.1330 -0.0170 -0.0027 -0.0141 199 THR D O   
7980 C  CB  . THR D  199 ? 0.1359 0.1246 0.1518 -0.0006 -0.0065 -0.0120 199 THR D CB  
7981 O  OG1 . THR D  199 ? 0.1673 0.1490 0.1520 0.0113  -0.0083 -0.0116 199 THR D OG1 
7982 C  CG2 . THR D  199 ? 0.1800 0.1279 0.1500 -0.0087 -0.0144 -0.0162 199 THR D CG2 
7983 N  N   . PRO D  200 ? 0.1565 0.1156 0.1210 -0.0075 -0.0001 -0.0036 200 PRO D N   
7984 C  CA  . PRO D  200 ? 0.1723 0.1093 0.1391 -0.0027 0.0041  -0.0121 200 PRO D CA  
7985 C  C   . PRO D  200 ? 0.1681 0.1310 0.1572 -0.0178 0.0000  0.0018  200 PRO D C   
7986 O  O   . PRO D  200 ? 0.1712 0.1561 0.1573 0.0119  -0.0120 -0.0138 200 PRO D O   
7987 C  CB  . PRO D  200 ? 0.1725 0.1426 0.1423 -0.0050 0.0240  0.0001  200 PRO D CB  
7988 C  CG  . PRO D  200 ? 0.1759 0.1168 0.1660 -0.0201 0.0077  -0.0144 200 PRO D CG  
7989 C  CD  . PRO D  200 ? 0.1586 0.1287 0.1320 -0.0079 0.0020  -0.0133 200 PRO D CD  
7990 N  N   . PRO D  201 ? 0.1839 0.1238 0.1479 0.0156  0.0125  0.0120  201 PRO D N   
7991 C  CA  . PRO D  201 ? 0.2030 0.1109 0.1469 -0.0098 -0.0044 -0.0058 201 PRO D CA  
7992 C  C   . PRO D  201 ? 0.1943 0.1257 0.1229 -0.0122 0.0011  -0.0039 201 PRO D C   
7993 O  O   . PRO D  201 ? 0.2119 0.1311 0.1515 -0.0181 -0.0008 -0.0194 201 PRO D O   
7994 C  CB  . PRO D  201 ? 0.2184 0.1530 0.1867 0.0234  0.0201  -0.0152 201 PRO D CB  
7995 C  CG  . PRO D  201 ? 0.2469 0.2432 0.3406 0.0719  -0.0394 -0.1439 201 PRO D CG  
7996 C  CD  . PRO D  201 ? 0.1879 0.1389 0.2167 0.0281  0.0003  0.0031  201 PRO D CD  
7997 N  N   . CYS D  202 ? 0.1877 0.1073 0.1556 0.0008  0.0184  0.0036  202 CYS D N   
7998 C  CA  . CYS D  202 ? 0.1867 0.1342 0.1237 -0.0010 0.0029  -0.0176 202 CYS D CA  
7999 C  C   . CYS D  202 ? 0.1900 0.1204 0.1507 -0.0141 -0.0019 -0.0114 202 CYS D C   
8000 O  O   . CYS D  202 ? 0.2256 0.1536 0.1357 0.0070  -0.0021 -0.0037 202 CYS D O   
8001 C  CB  . CYS D  202 ? 0.1870 0.1646 0.1555 0.0022  0.0102  -0.0003 202 CYS D CB  
8002 S  SG  . CYS D  202 ? 0.1922 0.1322 0.1356 -0.0012 -0.0019 -0.0107 202 CYS D SG  
8003 N  N   . ASN D  203 ? 0.1976 0.1291 0.1467 0.0076  0.0150  -0.0225 203 ASN D N   
8004 C  CA  . ASN D  203 ? 0.2605 0.1429 0.1246 0.0110  0.0337  -0.0067 203 ASN D CA  
8005 C  C   . ASN D  203 ? 0.2117 0.1509 0.1104 -0.0093 0.0094  -0.0027 203 ASN D C   
8006 O  O   . ASN D  203 ? 0.2126 0.1406 0.1204 0.0093  0.0053  -0.0147 203 ASN D O   
8007 C  CB  . ASN D  203 ? 0.2662 0.1387 0.1890 0.0387  0.0580  -0.0018 203 ASN D CB  
8008 C  CG  . ASN D  203 ? 0.2992 0.1458 0.2194 0.0684  0.0230  -0.0115 203 ASN D CG  
8009 O  OD1 . ASN D  203 ? 0.3952 0.2202 0.2478 0.0196  0.0447  0.0021  203 ASN D OD1 
8010 N  ND2 . ASN D  203 ? 0.3741 0.1489 0.3055 0.0055  0.0212  0.0238  203 ASN D ND2 
8011 N  N   . PRO D  204 ? 0.2409 0.1357 0.1201 -0.0001 0.0038  -0.0159 204 PRO D N   
8012 C  CA  . PRO D  204 ? 0.1869 0.1522 0.1344 -0.0004 -0.0081 0.0050  204 PRO D CA  
8013 C  C   . PRO D  204 ? 0.1961 0.1599 0.1336 0.0089  0.0362  -0.0079 204 PRO D C   
8014 O  O   . PRO D  204 ? 0.2437 0.2068 0.1497 0.0283  0.0218  0.0000  204 PRO D O   
8015 C  CB  . PRO D  204 ? 0.2345 0.1624 0.1700 0.0027  -0.0190 -0.0218 204 PRO D CB  
8016 C  CG  . PRO D  204 ? 0.2976 0.1521 0.1588 -0.0257 -0.0201 -0.0085 204 PRO D CG  
8017 C  CD  . PRO D  204 ? 0.2913 0.1727 0.1497 -0.0383 -0.0078 -0.0222 204 PRO D CD  
8018 N  N   . THR D  205 ? 0.1773 0.1218 0.1614 0.0230  0.0118  -0.0094 205 THR D N   
8019 C  CA  . THR D  205 ? 0.1895 0.1640 0.1498 0.0168  -0.0027 -0.0044 205 THR D CA  
8020 C  C   . THR D  205 ? 0.2094 0.1433 0.1262 0.0204  0.0198  0.0001  205 THR D C   
8021 O  O   . THR D  205 ? 0.2119 0.1498 0.1518 0.0189  0.0201  -0.0200 205 THR D O   
8022 C  CB  . THR D  205 ? 0.2451 0.1585 0.1379 0.0375  0.0232  0.0203  205 THR D CB  
8023 O  OG1 . THR D  205 ? 0.2467 0.1578 0.1445 0.0318  0.0234  0.0088  205 THR D OG1 
8024 C  CG2 . THR D  205 ? 0.2742 0.1301 0.1830 0.0145  0.0083  -0.0094 205 THR D CG2 
8025 N  N   . VAL D  206 ? 0.2083 0.1322 0.1357 0.0194  0.0139  -0.0065 206 VAL D N   
8026 C  CA  . VAL D  206 ? 0.2095 0.1430 0.1149 0.0062  0.0102  0.0019  206 VAL D CA  
8027 C  C   . VAL D  206 ? 0.1927 0.1640 0.1184 0.0247  -0.0015 -0.0221 206 VAL D C   
8028 O  O   . VAL D  206 ? 0.2131 0.1418 0.1715 0.0149  -0.0120 0.0064  206 VAL D O   
8029 C  CB  . VAL D  206 ? 0.1996 0.1421 0.1276 0.0271  0.0159  -0.0063 206 VAL D CB  
8030 C  CG1 . VAL D  206 ? 0.1882 0.1714 0.1228 0.0115  0.0337  -0.0221 206 VAL D CG1 
8031 C  CG2 . VAL D  206 ? 0.2036 0.1530 0.1107 0.0485  0.0167  0.0102  206 VAL D CG2 
8032 N  N   . LEU D  207 ? 0.1926 0.1273 0.1233 0.0166  0.0194  0.0102  207 LEU D N   
8033 C  CA  . LEU D  207 ? 0.2398 0.1228 0.1244 0.0174  0.0491  0.0048  207 LEU D CA  
8034 C  C   . LEU D  207 ? 0.1876 0.1549 0.1191 0.0179  0.0273  0.0172  207 LEU D C   
8035 O  O   . LEU D  207 ? 0.1972 0.1483 0.1345 0.0322  0.0181  0.0036  207 LEU D O   
8036 C  CB  . LEU D  207 ? 0.2775 0.1854 0.1809 -0.0017 0.0820  0.0284  207 LEU D CB  
8037 C  CG  . LEU D  207 ? 0.3882 0.2115 0.1788 -0.0835 0.0317  0.0173  207 LEU D CG  
8038 C  CD1 . LEU D  207 ? 0.4257 0.2895 0.1939 -0.0036 0.0298  0.0278  207 LEU D CD1 
8039 C  CD2 . LEU D  207 ? 0.4810 0.4437 0.4022 -0.1857 0.0835  0.1778  207 LEU D CD2 
8040 N  N   . TRP D  208 ? 0.1939 0.1386 0.1259 0.0057  0.0104  0.0133  208 TRP D N   
8041 C  CA  . TRP D  208 ? 0.1904 0.1281 0.1391 0.0167  0.0156  -0.0070 208 TRP D CA  
8042 C  C   . TRP D  208 ? 0.1630 0.1415 0.1277 0.0146  0.0082  0.0288  208 TRP D C   
8043 O  O   . TRP D  208 ? 0.2473 0.1362 0.1202 0.0304  0.0245  0.0256  208 TRP D O   
8044 C  CB  . TRP D  208 ? 0.1694 0.1505 0.1306 0.0199  0.0053  0.0124  208 TRP D CB  
8045 C  CG  . TRP D  208 ? 0.1756 0.1382 0.1096 0.0185  0.0040  0.0126  208 TRP D CG  
8046 C  CD1 . TRP D  208 ? 0.1619 0.1500 0.1224 0.0271  -0.0010 -0.0003 208 TRP D CD1 
8047 C  CD2 . TRP D  208 ? 0.1725 0.1192 0.1224 0.0097  0.0145  -0.0096 208 TRP D CD2 
8048 N  NE1 . TRP D  208 ? 0.1699 0.1300 0.1260 0.0098  0.0000  -0.0155 208 TRP D NE1 
8049 C  CE2 . TRP D  208 ? 0.1618 0.1132 0.1268 0.0139  0.0220  -0.0124 208 TRP D CE2 
8050 C  CE3 . TRP D  208 ? 0.1458 0.1257 0.1283 0.0060  0.0075  -0.0080 208 TRP D CE3 
8051 C  CZ2 . TRP D  208 ? 0.1478 0.1561 0.1206 0.0238  0.0212  -0.0088 208 TRP D CZ2 
8052 C  CZ3 . TRP D  208 ? 0.1557 0.1209 0.1142 0.0136  0.0212  -0.0026 208 TRP D CZ3 
8053 C  CH2 . TRP D  208 ? 0.1583 0.1168 0.1240 0.0132  0.0160  -0.0043 208 TRP D CH2 
8054 N  N   . THR D  209 ? 0.1547 0.1188 0.1331 0.0210  0.0234  0.0120  209 THR D N   
8055 C  CA  . THR D  209 ? 0.1590 0.1157 0.1377 0.0272  0.0320  0.0061  209 THR D CA  
8056 C  C   . THR D  209 ? 0.1617 0.1215 0.1146 0.0168  0.0308  0.0245  209 THR D C   
8057 O  O   . THR D  209 ? 0.2023 0.1349 0.1233 0.0344  0.0170  0.0093  209 THR D O   
8058 C  CB  . THR D  209 ? 0.1650 0.1159 0.1580 0.0107  0.0343  0.0251  209 THR D CB  
8059 O  OG1 . THR D  209 ? 0.1958 0.1532 0.1438 0.0311  0.0695  0.0114  209 THR D OG1 
8060 C  CG2 . THR D  209 ? 0.2026 0.1283 0.1946 0.0091  0.0508  0.0294  209 THR D CG2 
8061 N  N   . VAL D  210 ? 0.1442 0.1282 0.1354 0.0236  0.0285  0.0054  210 VAL D N   
8062 C  CA  . VAL D  210 ? 0.1735 0.1191 0.1150 0.0204  0.0284  0.0125  210 VAL D CA  
8063 C  C   . VAL D  210 ? 0.1317 0.1434 0.1292 0.0164  0.0233  0.0234  210 VAL D C   
8064 O  O   . VAL D  210 ? 0.1733 0.1369 0.1284 0.0187  0.0315  0.0223  210 VAL D O   
8065 C  CB  . VAL D  210 ? 0.1435 0.1298 0.1435 0.0087  0.0228  0.0054  210 VAL D CB  
8066 C  CG1 . VAL D  210 ? 0.1806 0.1548 0.1284 0.0143  0.0193  -0.0061 210 VAL D CG1 
8067 C  CG2 . VAL D  210 ? 0.1817 0.1318 0.1337 -0.0054 0.0184  0.0230  210 VAL D CG2 
8068 N  N   . PHE D  211 ? 0.1355 0.1164 0.1415 -0.0013 0.0292  0.0143  211 PHE D N   
8069 C  CA  . PHE D  211 ? 0.1595 0.1121 0.1527 -0.0037 0.0133  0.0110  211 PHE D CA  
8070 C  C   . PHE D  211 ? 0.1527 0.1295 0.1674 -0.0110 0.0361  0.0189  211 PHE D C   
8071 O  O   . PHE D  211 ? 0.1736 0.1346 0.1685 0.0008  0.0456  0.0082  211 PHE D O   
8072 C  CB  . PHE D  211 ? 0.1605 0.1329 0.1665 -0.0166 0.0396  0.0036  211 PHE D CB  
8073 C  CG  . PHE D  211 ? 0.1643 0.1318 0.1618 0.0027  0.0300  0.0334  211 PHE D CG  
8074 C  CD1 . PHE D  211 ? 0.1549 0.1646 0.1963 -0.0175 0.0611  0.0121  211 PHE D CD1 
8075 C  CD2 . PHE D  211 ? 0.1582 0.1468 0.2064 -0.0089 0.0089  0.0454  211 PHE D CD2 
8076 C  CE1 . PHE D  211 ? 0.1803 0.2110 0.1818 0.0088  0.0631  0.0332  211 PHE D CE1 
8077 C  CE2 . PHE D  211 ? 0.1727 0.1719 0.2215 0.0105  0.0115  0.0312  211 PHE D CE2 
8078 C  CZ  . PHE D  211 ? 0.1956 0.1767 0.2611 -0.0234 0.0634  0.0585  211 PHE D CZ  
8079 N  N   . ARG D  212 ? 0.1682 0.1143 0.1685 0.0037  0.0350  0.0192  212 ARG D N   
8080 C  CA  . ARG D  212 ? 0.1923 0.1253 0.1723 0.0228  0.0282  0.0128  212 ARG D CA  
8081 C  C   . ARG D  212 ? 0.1675 0.1238 0.1826 0.0177  0.0231  0.0232  212 ARG D C   
8082 O  O   . ARG D  212 ? 0.1933 0.1436 0.1970 0.0221  0.0494  0.0195  212 ARG D O   
8083 C  CB  . ARG D  212 ? 0.2218 0.1517 0.1683 0.0165  0.0152  0.0319  212 ARG D CB  
8084 C  CG  . ARG D  212 ? 0.2119 0.1676 0.2024 0.0484  0.0280  0.0737  212 ARG D CG  
8085 C  CD  . ARG D  212 ? 0.2464 0.1377 0.2275 0.0429  0.0391  0.0400  212 ARG D CD  
8086 N  NE  . ARG D  212 ? 0.2982 0.1666 0.2398 0.0759  0.0166  0.0548  212 ARG D NE  
8087 C  CZ  . ARG D  212 ? 0.3244 0.2452 0.2764 0.1010  0.0521  0.0894  212 ARG D CZ  
8088 N  NH1 . ARG D  212 ? 0.3289 0.2032 0.3585 0.0047  0.0164  0.0781  212 ARG D NH1 
8089 N  NH2 . ARG D  212 ? 0.3256 0.2470 0.4107 0.1106  0.0292  0.1216  212 ARG D NH2 
8090 N  N   . ASN D  213 ? 0.1839 0.1340 0.1456 0.0022  0.0205  0.0035  213 ASN D N   
8091 C  CA  . ASN D  213 ? 0.1878 0.1307 0.1614 -0.0117 0.0111  0.0160  213 ASN D CA  
8092 C  C   . ASN D  213 ? 0.1782 0.1396 0.1668 0.0055  0.0197  0.0277  213 ASN D C   
8093 O  O   . ASN D  213 ? 0.1943 0.1192 0.1805 0.0144  0.0369  0.0220  213 ASN D O   
8094 C  CB  . ASN D  213 ? 0.2336 0.1297 0.1935 -0.0419 0.0164  0.0189  213 ASN D CB  
8095 C  CG  . ASN D  213 ? 0.2457 0.1885 0.2684 -0.0276 0.0314  0.0907  213 ASN D CG  
8096 O  OD1 . ASN D  213 ? 0.3471 0.2290 0.3673 0.0256  0.0231  0.1448  213 ASN D OD1 
8097 N  ND2 . ASN D  213 ? 0.3759 0.1885 0.3382 -0.0073 0.1047  0.1066  213 ASN D ND2 
8098 N  N   . PRO D  214 ? 0.2077 0.1367 0.1573 0.0290  0.0226  0.0172  214 PRO D N   
8099 C  CA  . PRO D  214 ? 0.1670 0.1439 0.1620 0.0015  0.0212  0.0044  214 PRO D CA  
8100 C  C   . PRO D  214 ? 0.1638 0.1411 0.1508 -0.0079 0.0270  -0.0092 214 PRO D C   
8101 O  O   . PRO D  214 ? 0.2061 0.1428 0.1882 -0.0210 0.0243  0.0312  214 PRO D O   
8102 C  CB  . PRO D  214 ? 0.1781 0.1367 0.1971 0.0324  0.0385  -0.0032 214 PRO D CB  
8103 C  CG  . PRO D  214 ? 0.2316 0.1970 0.2026 0.0359  0.0409  -0.0044 214 PRO D CG  
8104 C  CD  . PRO D  214 ? 0.2087 0.1854 0.2002 0.0590  0.0462  0.0069  214 PRO D CD  
8105 N  N   . VAL D  215 ? 0.1634 0.1439 0.1421 -0.0145 0.0068  0.0074  215 VAL D N   
8106 C  CA  . VAL D  215 ? 0.1482 0.1453 0.1474 0.0030  0.0409  0.0136  215 VAL D CA  
8107 C  C   . VAL D  215 ? 0.1541 0.1156 0.1620 -0.0166 0.0240  0.0179  215 VAL D C   
8108 O  O   . VAL D  215 ? 0.1488 0.1706 0.1729 -0.0145 0.0302  -0.0269 215 VAL D O   
8109 C  CB  . VAL D  215 ? 0.1361 0.1216 0.1795 -0.0065 0.0374  -0.0057 215 VAL D CB  
8110 C  CG1 . VAL D  215 ? 0.1557 0.2218 0.1804 0.0059  0.0436  -0.0140 215 VAL D CG1 
8111 C  CG2 . VAL D  215 ? 0.1715 0.1257 0.1813 -0.0096 0.0115  0.0156  215 VAL D CG2 
8112 N  N   . GLN D  216 ? 0.1569 0.1256 0.1479 -0.0004 0.0171  -0.0012 216 GLN D N   
8113 C  CA  . GLN D  216 ? 0.1531 0.1240 0.1384 0.0210  0.0105  -0.0006 216 GLN D CA  
8114 C  C   . GLN D  216 ? 0.1332 0.1449 0.1547 0.0083  0.0109  -0.0206 216 GLN D C   
8115 O  O   . GLN D  216 ? 0.1388 0.1723 0.1651 0.0121  0.0135  0.0046  216 GLN D O   
8116 C  CB  . GLN D  216 ? 0.1679 0.1451 0.1669 0.0162  0.0105  0.0071  216 GLN D CB  
8117 C  CG  . GLN D  216 ? 0.1955 0.1444 0.1829 0.0290  -0.0153 0.0103  216 GLN D CG  
8118 C  CD  . GLN D  216 ? 0.2238 0.1742 0.1893 0.0234  -0.0111 0.0172  216 GLN D CD  
8119 O  OE1 . GLN D  216 ? 0.2180 0.1475 0.1812 0.0005  0.0005  0.0140  216 GLN D OE1 
8120 N  NE2 . GLN D  216 ? 0.3497 0.2026 0.2226 0.0471  -0.0539 0.0065  216 GLN D NE2 
8121 N  N   . ILE D  217 ? 0.1492 0.1201 0.1354 0.0091  0.0078  -0.0124 217 ILE D N   
8122 C  CA  . ILE D  217 ? 0.1610 0.1170 0.1462 0.0083  0.0178  -0.0060 217 ILE D CA  
8123 C  C   . ILE D  217 ? 0.1303 0.1312 0.1350 0.0054  0.0086  0.0125  217 ILE D C   
8124 O  O   . ILE D  217 ? 0.1482 0.1289 0.1595 0.0156  0.0089  0.0005  217 ILE D O   
8125 C  CB  . ILE D  217 ? 0.1430 0.1296 0.1614 -0.0017 0.0057  -0.0157 217 ILE D CB  
8126 C  CG1 . ILE D  217 ? 0.1578 0.1267 0.1771 -0.0095 -0.0077 0.0019  217 ILE D CG1 
8127 C  CG2 . ILE D  217 ? 0.1803 0.1279 0.1934 0.0141  0.0223  -0.0203 217 ILE D CG2 
8128 C  CD1 . ILE D  217 ? 0.2177 0.1156 0.2120 -0.0042 0.0003  0.0117  217 ILE D CD1 
8129 N  N   . SER D  218 ? 0.1537 0.1080 0.1513 0.0168  0.0179  0.0025  218 SER D N   
8130 C  CA  . SER D  218 ? 0.1608 0.1274 0.1290 0.0159  0.0125  -0.0002 218 SER D CA  
8131 C  C   . SER D  218 ? 0.1682 0.1279 0.1350 0.0012  0.0072  -0.0041 218 SER D C   
8132 O  O   . SER D  218 ? 0.1694 0.1282 0.1467 -0.0037 0.0036  0.0064  218 SER D O   
8133 C  CB  . SER D  218 ? 0.1984 0.1237 0.1420 0.0263  -0.0035 -0.0075 218 SER D CB  
8134 O  OG  . SER D  218 ? 0.1731 0.1532 0.1544 0.0152  -0.0083 0.0035  218 SER D OG  
8135 N  N   . GLN D  219 ? 0.1445 0.1690 0.1609 0.0197  0.0136  0.0102  219 GLN D N   
8136 C  CA  . GLN D  219 ? 0.1500 0.1980 0.1723 0.0363  0.0385  0.0413  219 GLN D CA  
8137 C  C   . GLN D  219 ? 0.1787 0.1479 0.1280 0.0161  0.0094  -0.0125 219 GLN D C   
8138 O  O   . GLN D  219 ? 0.1848 0.1586 0.1647 0.0018  0.0276  0.0064  219 GLN D O   
8139 C  CB  . GLN D  219 ? 0.2225 0.2325 0.2082 0.0570  0.0872  0.0527  219 GLN D CB  
8140 C  CG  . GLN D  219 ? 0.2228 0.2782 0.2577 0.0792  0.0506  0.0528  219 GLN D CG  
8141 C  CD  . GLN D  219 ? 0.2638 0.2972 0.3267 0.0400  0.0598  0.0622  219 GLN D CD  
8142 O  OE1 . GLN D  219 ? 0.3762 0.4563 0.3230 0.0374  -0.0321 0.0274  219 GLN D OE1 
8143 N  NE2 . GLN D  219 ? 0.3177 0.4141 0.3298 0.0064  -0.0348 0.0819  219 GLN D NE2 
8144 N  N   . GLU D  220 ? 0.1821 0.1659 0.1491 0.0065  0.0036  -0.0152 220 GLU D N   
8145 C  CA  . GLU D  220 ? 0.1700 0.1629 0.1522 0.0130  -0.0223 -0.0070 220 GLU D CA  
8146 C  C   . GLU D  220 ? 0.1766 0.1448 0.1371 0.0087  -0.0085 0.0132  220 GLU D C   
8147 O  O   . GLU D  220 ? 0.1965 0.1466 0.1435 -0.0010 -0.0074 0.0061  220 GLU D O   
8148 C  CB  . GLU D  220 ? 0.2014 0.2094 0.1804 -0.0102 -0.0130 -0.0347 220 GLU D CB  
8149 C  CG  . GLU D  220 ? 0.2382 0.2012 0.1875 0.0194  0.0034  -0.0373 220 GLU D CG  
8150 C  CD  . GLU D  220 ? 0.3617 0.2471 0.2455 0.0301  0.0472  -0.0324 220 GLU D CD  
8151 O  OE1 . GLU D  220 ? 0.3383 0.1979 0.2856 0.0042  0.0471  -0.0504 220 GLU D OE1 
8152 O  OE2 . GLU D  220 ? 0.6504 0.2831 0.3467 0.1153  0.1432  -0.0330 220 GLU D OE2 
8153 N  N   . GLN D  221 ? 0.1509 0.1550 0.1498 0.0105  0.0062  -0.0097 221 GLN D N   
8154 C  CA  . GLN D  221 ? 0.1601 0.1377 0.1603 -0.0047 0.0077  0.0049  221 GLN D CA  
8155 C  C   . GLN D  221 ? 0.1521 0.1137 0.1557 0.0061  0.0009  0.0057  221 GLN D C   
8156 O  O   . GLN D  221 ? 0.1732 0.1216 0.1711 0.0097  0.0058  0.0094  221 GLN D O   
8157 C  CB  . GLN D  221 ? 0.1512 0.1618 0.1468 -0.0018 -0.0053 0.0054  221 GLN D CB  
8158 C  CG  . GLN D  221 ? 0.1447 0.1459 0.1623 -0.0124 -0.0094 0.0035  221 GLN D CG  
8159 C  CD  . GLN D  221 ? 0.1586 0.1265 0.1619 0.0091  -0.0189 -0.0150 221 GLN D CD  
8160 O  OE1 . GLN D  221 ? 0.1472 0.1353 0.1646 0.0035  0.0009  0.0134  221 GLN D OE1 
8161 N  NE2 . GLN D  221 ? 0.1428 0.1222 0.1763 0.0122  -0.0048 -0.0163 221 GLN D NE2 
8162 N  N   . LEU D  222 ? 0.1574 0.1545 0.1322 0.0087  0.0024  0.0006  222 LEU D N   
8163 C  CA  . LEU D  222 ? 0.1537 0.1415 0.1364 0.0091  -0.0133 -0.0086 222 LEU D CA  
8164 C  C   . LEU D  222 ? 0.1646 0.1312 0.1397 0.0184  -0.0057 -0.0127 222 LEU D C   
8165 O  O   . LEU D  222 ? 0.1640 0.1420 0.1652 -0.0021 0.0055  -0.0176 222 LEU D O   
8166 C  CB  . LEU D  222 ? 0.1793 0.1618 0.1499 0.0199  0.0073  0.0072  222 LEU D CB  
8167 C  CG  . LEU D  222 ? 0.2107 0.1621 0.1851 -0.0023 0.0309  -0.0122 222 LEU D CG  
8168 C  CD1 . LEU D  222 ? 0.2422 0.1648 0.2083 -0.0030 0.0015  0.0119  222 LEU D CD1 
8169 C  CD2 . LEU D  222 ? 0.2556 0.1971 0.1651 0.0179  -0.0168 -0.0675 222 LEU D CD2 
8170 N  N   . LEU D  223 ? 0.1488 0.1601 0.1279 -0.0026 -0.0041 -0.0097 223 LEU D N   
8171 C  CA  . LEU D  223 ? 0.1941 0.1459 0.1408 0.0062  0.0146  0.0068  223 LEU D CA  
8172 C  C   . LEU D  223 ? 0.1721 0.1554 0.1419 -0.0089 -0.0054 0.0133  223 LEU D C   
8173 O  O   . LEU D  223 ? 0.2034 0.1582 0.1524 -0.0256 0.0044  0.0089  223 LEU D O   
8174 C  CB  . LEU D  223 ? 0.2089 0.1832 0.1339 -0.0118 0.0091  -0.0019 223 LEU D CB  
8175 C  CG  . LEU D  223 ? 0.2279 0.1939 0.1865 0.0192  0.0279  0.0108  223 LEU D CG  
8176 C  CD1 . LEU D  223 ? 0.2225 0.2408 0.2395 -0.0066 0.0425  -0.0260 223 LEU D CD1 
8177 C  CD2 . LEU D  223 ? 0.2733 0.2219 0.1705 -0.0077 0.0407  -0.0367 223 LEU D CD2 
8178 N  N   . ALA D  224 ? 0.1557 0.1804 0.1582 0.0006  -0.0167 0.0097  224 ALA D N   
8179 C  CA  . ALA D  224 ? 0.1882 0.1504 0.1935 -0.0026 -0.0228 0.0218  224 ALA D CA  
8180 C  C   . ALA D  224 ? 0.1652 0.1397 0.2066 0.0013  0.0027  0.0206  224 ALA D C   
8181 O  O   . ALA D  224 ? 0.2212 0.1451 0.2523 0.0092  0.0096  0.0256  224 ALA D O   
8182 C  CB  . ALA D  224 ? 0.1801 0.2209 0.2591 0.0016  -0.0658 0.0458  224 ALA D CB  
8183 N  N   . LEU D  225 ? 0.1830 0.1542 0.1869 0.0153  0.0049  -0.0053 225 LEU D N   
8184 C  CA  . LEU D  225 ? 0.1676 0.1669 0.1955 -0.0017 0.0128  -0.0033 225 LEU D CA  
8185 C  C   . LEU D  225 ? 0.1717 0.1332 0.2000 0.0063  0.0044  -0.0294 225 LEU D C   
8186 O  O   . LEU D  225 ? 0.2063 0.1373 0.2461 0.0127  0.0390  0.0081  225 LEU D O   
8187 C  CB  . LEU D  225 ? 0.1810 0.1416 0.1930 0.0012  0.0228  -0.0128 225 LEU D CB  
8188 C  CG  . LEU D  225 ? 0.1933 0.1647 0.1861 0.0151  -0.0299 -0.0205 225 LEU D CG  
8189 C  CD1 . LEU D  225 ? 0.2033 0.1663 0.2127 0.0299  -0.0070 -0.0462 225 LEU D CD1 
8190 C  CD2 . LEU D  225 ? 0.2059 0.1975 0.1730 0.0170  0.0018  -0.0295 225 LEU D CD2 
8191 N  N   . GLU D  226 ? 0.1583 0.1506 0.1832 -0.0001 0.0234  -0.0052 226 GLU D N   
8192 C  CA  . GLU D  226 ? 0.1640 0.1656 0.1746 0.0057  0.0075  0.0328  226 GLU D CA  
8193 C  C   . GLU D  226 ? 0.2153 0.1516 0.1796 -0.0351 -0.0041 0.0266  226 GLU D C   
8194 O  O   . GLU D  226 ? 0.2357 0.2254 0.2296 -0.0594 -0.0383 0.0449  226 GLU D O   
8195 C  CB  . GLU D  226 ? 0.1575 0.1614 0.1684 -0.0176 -0.0010 0.0157  226 GLU D CB  
8196 C  CG  . GLU D  226 ? 0.1743 0.1530 0.1638 -0.0164 0.0024  0.0058  226 GLU D CG  
8197 C  CD  . GLU D  226 ? 0.1812 0.1953 0.1393 -0.0097 0.0156  -0.0037 226 GLU D CD  
8198 O  OE1 . GLU D  226 ? 0.1980 0.1884 0.1566 0.0219  0.0267  -0.0091 226 GLU D OE1 
8199 O  OE2 . GLU D  226 ? 0.3345 0.1680 0.1917 -0.0005 0.0017  0.0053  226 GLU D OE2 
8200 N  N   . THR D  227 ? 0.1790 0.1635 0.1604 -0.0044 0.0019  0.0004  227 THR D N   
8201 C  CA  . THR D  227 ? 0.2137 0.1849 0.1857 0.0204  0.0229  0.0248  227 THR D CA  
8202 C  C   . THR D  227 ? 0.2246 0.2100 0.1785 0.0062  -0.0032 0.0290  227 THR D C   
8203 O  O   . THR D  227 ? 0.2927 0.2333 0.2092 0.0275  -0.0013 0.0493  227 THR D O   
8204 C  CB  . THR D  227 ? 0.2136 0.2140 0.2027 0.0052  0.0322  -0.0052 227 THR D CB  
8205 O  OG1 . THR D  227 ? 0.2472 0.2288 0.1786 -0.0126 0.0199  0.0162  227 THR D OG1 
8206 C  CG2 . THR D  227 ? 0.2461 0.2322 0.1997 0.0342  0.0188  0.0075  227 THR D CG2 
8207 N  N   . ALA D  228 ? 0.2036 0.1532 0.2003 0.0106  -0.0110 0.0082  228 ALA D N   
8208 C  CA  . ALA D  228 ? 0.2034 0.1753 0.2840 0.0219  -0.0337 0.0322  228 ALA D CA  
8209 C  C   . ALA D  228 ? 0.2183 0.1843 0.2625 -0.0006 -0.0296 0.0486  228 ALA D C   
8210 O  O   . ALA D  228 ? 0.3787 0.2095 0.3139 0.0302  -0.1303 0.0656  228 ALA D O   
8211 C  CB  . ALA D  228 ? 0.1776 0.2508 0.3716 0.0075  -0.0280 0.0098  228 ALA D CB  
8212 N  N   . LEU D  229 ? 0.1918 0.1634 0.1925 -0.0040 0.0152  0.0356  229 LEU D N   
8213 C  CA  . LEU D  229 ? 0.2127 0.1554 0.2246 -0.0118 0.0168  0.0359  229 LEU D CA  
8214 C  C   . LEU D  229 ? 0.1965 0.1743 0.2343 -0.0063 -0.0100 0.0423  229 LEU D C   
8215 O  O   . LEU D  229 ? 0.1864 0.1632 0.2185 -0.0025 0.0050  0.0528  229 LEU D O   
8216 C  CB  . LEU D  229 ? 0.2017 0.2036 0.2046 -0.0205 0.0013  0.0065  229 LEU D CB  
8217 C  CG  . LEU D  229 ? 0.2262 0.1824 0.1938 -0.0163 0.0008  0.0324  229 LEU D CG  
8218 C  CD1 . LEU D  229 ? 0.2375 0.3274 0.2157 -0.0532 0.0427  -0.0631 229 LEU D CD1 
8219 C  CD2 . LEU D  229 ? 0.2177 0.1689 0.3107 -0.0135 -0.0183 0.0756  229 LEU D CD2 
8220 N  N   . TYR D  230 ? 0.2110 0.1636 0.3088 -0.0068 0.0350  0.0735  230 TYR D N   
8221 C  CA  . TYR D  230 ? 0.2076 0.1513 0.3063 -0.0244 0.0005  0.0486  230 TYR D CA  
8222 C  C   . TYR D  230 ? 0.2043 0.2085 0.2352 -0.0021 0.0121  0.0763  230 TYR D C   
8223 O  O   . TYR D  230 ? 0.2016 0.1940 0.3068 0.0012  0.0578  0.0554  230 TYR D O   
8224 C  CB  . TYR D  230 ? 0.2620 0.1913 0.2685 -0.0057 0.0538  0.0610  230 TYR D CB  
8225 C  CG  . TYR D  230 ? 0.2629 0.2242 0.2815 -0.0231 0.0557  0.0378  230 TYR D CG  
8226 C  CD1 . TYR D  230 ? 0.2243 0.2955 0.3660 0.0493  -0.0048 -0.0414 230 TYR D CD1 
8227 C  CD2 . TYR D  230 ? 0.2642 0.2244 0.3274 -0.0066 0.0640  0.0593  230 TYR D CD2 
8228 C  CE1 . TYR D  230 ? 0.3124 0.3141 0.4294 -0.0337 -0.0601 -0.1234 230 TYR D CE1 
8229 C  CE2 . TYR D  230 ? 0.2743 0.3175 0.3605 0.0092  0.0305  -0.0270 230 TYR D CE2 
8230 C  CZ  . TYR D  230 ? 0.2879 0.4544 0.3764 0.0288  0.0147  -0.1197 230 TYR D CZ  
8231 O  OH  . TYR D  230 ? 0.3416 0.6276 0.4542 0.0554  0.0743  -0.1708 230 TYR D OH  
8232 N  N   . CYS D  231 ? 0.2333 0.1932 0.2606 -0.0250 0.0236  0.0597  231 CYS D N   
8233 C  CA  . CYS D  231 ? 0.2763 0.2087 0.2420 -0.0410 0.0320  0.0282  231 CYS D CA  
8234 C  C   . CYS D  231 ? 0.2042 0.2109 0.2467 -0.0433 0.0089  0.0352  231 CYS D C   
8235 O  O   . CYS D  231 ? 0.3186 0.2435 0.2601 -0.0239 -0.0245 0.0488  231 CYS D O   
8236 C  CB  . CYS D  231 ? 0.5681 0.3549 0.2354 -0.1832 -0.1625 0.1700  231 CYS D CB  
8237 S  SG  . CYS D  231 ? 0.4035 0.3285 0.4196 -0.0184 -0.1129 0.0807  231 CYS D SG  
8238 N  N   . THR D  232 ? 0.2394 0.2133 0.2379 -0.0272 0.0366  0.0498  232 THR D N   
8239 C  CA  . THR D  232 ? 0.2432 0.2000 0.2431 -0.0223 0.0188  0.0684  232 THR D CA  
8240 C  C   . THR D  232 ? 0.2423 0.1788 0.2108 -0.0315 0.0445  0.0491  232 THR D C   
8241 O  O   . THR D  232 ? 0.2237 0.2016 0.2395 -0.0237 0.0203  0.0610  232 THR D O   
8242 C  CB  . THR D  232 ? 0.2361 0.2064 0.2383 -0.0189 -0.0050 0.0561  232 THR D CB  
8243 O  OG1 . THR D  232 ? 0.2273 0.2237 0.2838 -0.0128 0.0543  0.0783  232 THR D OG1 
8244 C  CG2 . THR D  232 ? 0.2560 0.3050 0.3288 -0.0895 -0.0140 0.1114  232 THR D CG2 
8245 N  N   . HIS D  233 ? 0.2230 0.1805 0.1991 -0.0175 0.0068  0.0429  233 HIS D N   
8246 C  CA  . HIS D  233 ? 0.2424 0.1751 0.2124 0.0150  0.0132  0.0181  233 HIS D CA  
8247 C  C   . HIS D  233 ? 0.2485 0.1656 0.2060 -0.0336 0.0115  0.0176  233 HIS D C   
8248 O  O   . HIS D  233 ? 0.2631 0.1865 0.2046 -0.0053 0.0252  0.0446  233 HIS D O   
8249 C  CB  . HIS D  233 ? 0.2919 0.1518 0.3051 0.0456  -0.0083 -0.0066 233 HIS D CB  
8250 C  CG  . HIS D  233 ? 0.2894 0.1963 0.3482 -0.0319 0.0000  -0.0121 233 HIS D CG  
8251 N  ND1 . HIS D  233 ? 0.4165 0.4599 0.3996 0.0146  0.0121  -0.1733 233 HIS D ND1 
8252 C  CD2 . HIS D  233 ? 0.3588 0.3006 0.3576 -0.0613 0.0643  -0.0303 233 HIS D CD2 
8253 C  CE1 . HIS D  233 ? 0.3828 0.4360 0.5154 0.0469  0.1108  -0.1341 233 HIS D CE1 
8254 N  NE2 . HIS D  233 ? 0.4605 0.3280 0.3610 -0.0036 0.0999  0.0238  233 HIS D NE2 
8255 N  N   . MET D  234 ? 0.2587 0.2150 0.1801 -0.0058 0.0085  0.0505  234 MET D N   
8256 C  CA  . MET D  234 ? 0.2781 0.2286 0.1812 -0.0353 0.0085  0.0361  234 MET D CA  
8257 C  C   . MET D  234 ? 0.3525 0.2318 0.1584 -0.0006 0.0396  0.0237  234 MET D C   
8258 O  O   . MET D  234 ? 0.3201 0.3121 0.2159 -0.0514 0.0544  -0.0313 234 MET D O   
8259 C  CB  . MET D  234 ? 0.3096 0.2713 0.2022 -0.0543 -0.0365 0.0241  234 MET D CB  
8260 C  CG  . MET D  234 ? 0.3297 0.3569 0.2713 -0.0630 -0.0397 -0.0854 234 MET D CG  
8261 S  SD  . MET D  234 ? 0.3712 0.6075 0.2943 -0.0332 -0.0548 -0.0721 234 MET D SD  
8262 C  CE  . MET D  234 ? 0.3555 0.7547 0.3158 0.0529  -0.0992 -0.1588 234 MET D CE  
8263 N  N   . ASP D  235 ? 0.3309 0.2104 0.2306 -0.0381 -0.0280 0.0844  235 ASP D N   
8264 C  CA  . ASP D  235 ? 0.3343 0.2564 0.3272 -0.0813 0.0414  0.0564  235 ASP D CA  
8265 C  C   . ASP D  235 ? 0.3459 0.3015 0.2420 -0.0626 0.0055  0.0951  235 ASP D C   
8266 O  O   . ASP D  235 ? 0.3844 0.3052 0.2873 -0.0800 0.0094  0.1096  235 ASP D O   
8267 C  CB  . ASP D  235 ? 0.4520 0.3300 0.4532 -0.0584 -0.0190 0.2112  235 ASP D CB  
8268 C  CG  . ASP D  235 ? 0.6655 0.3610 0.4906 0.1241  -0.0944 0.1861  235 ASP D CG  
8269 O  OD1 . ASP D  235 ? 0.5708 0.3315 0.4499 0.0240  -0.1069 0.0822  235 ASP D OD1 
8270 O  OD2 . ASP D  235 ? 0.6470 0.3062 0.6696 0.1351  0.0108  0.1197  235 ASP D OD2 
8271 N  N   . ASP D  236 ? 0.2761 0.2242 0.2760 -0.0557 0.0133  0.0546  236 ASP D N   
8272 C  CA  . ASP D  236 ? 0.2746 0.2531 0.2798 -0.0637 0.0275  0.0892  236 ASP D CA  
8273 C  C   . ASP D  236 ? 0.3200 0.2849 0.3512 -0.0884 0.0616  0.0403  236 ASP D C   
8274 O  O   . ASP D  236 ? 0.3391 0.3121 0.2955 -0.0724 0.0716  -0.0006 236 ASP D O   
8275 C  CB  . ASP D  236 ? 0.2637 0.2697 0.2485 -0.0487 0.0025  0.0407  236 ASP D CB  
8276 C  CG  . ASP D  236 ? 0.2928 0.3071 0.2392 -0.0893 0.0110  0.0259  236 ASP D CG  
8277 O  OD1 . ASP D  236 ? 0.2892 0.3400 0.3213 -0.0895 0.0228  -0.0064 236 ASP D OD1 
8278 O  OD2 . ASP D  236 ? 0.2917 0.3309 0.3004 -0.0478 0.0063  0.0095  236 ASP D OD2 
8279 N  N   . PRO D  237 ? 0.3009 0.2816 0.3662 -0.0536 0.0650  0.1047  237 PRO D N   
8280 C  CA  . PRO D  237 ? 0.3882 0.3299 0.3327 -0.0861 0.0900  0.0828  237 PRO D CA  
8281 C  C   . PRO D  237 ? 0.4748 0.3107 0.4041 -0.0164 0.0934  0.1248  237 PRO D C   
8282 O  O   . PRO D  237 ? 0.5103 0.3619 0.5162 -0.0547 0.2434  0.1145  237 PRO D O   
8283 C  CB  . PRO D  237 ? 0.4455 0.3708 0.3978 -0.1370 0.1119  0.0738  237 PRO D CB  
8284 C  CG  . PRO D  237 ? 0.3869 0.3383 0.4781 -0.0551 0.0873  0.1538  237 PRO D CG  
8285 C  CD  . PRO D  237 ? 0.3756 0.2865 0.4201 -0.1155 0.0516  0.1390  237 PRO D CD  
8286 N  N   . SER D  238 ? 0.3122 0.3416 0.3991 -0.0771 0.0648  0.1671  238 SER D N   
8287 C  CA  . SER D  238 ? 0.4367 0.2929 0.3967 -0.0833 0.0359  0.1975  238 SER D CA  
8288 C  C   . SER D  238 ? 0.3386 0.3458 0.3504 -0.0469 0.0488  0.1382  238 SER D C   
8289 O  O   . SER D  238 ? 0.2852 0.3125 0.4258 -0.0551 0.0265  0.1262  238 SER D O   
8290 C  CB  . SER D  238 ? 0.3671 0.3669 0.4885 -0.1324 0.0175  0.1231  238 SER D CB  
8291 O  OG  . SER D  238 ? 0.3926 0.7710 0.7196 -0.0215 0.0156  0.0768  238 SER D OG  
8292 N  N   . PRO D  239 ? 0.2991 0.2545 0.4545 -0.0312 0.1412  0.0685  239 PRO D N   
8293 C  CA  . PRO D  239 ? 0.3083 0.3634 0.3258 -0.0264 0.1380  0.1534  239 PRO D CA  
8294 C  C   . PRO D  239 ? 0.3360 0.2785 0.5332 0.0656  0.2091  0.1860  239 PRO D C   
8295 O  O   . PRO D  239 ? 0.3353 0.3886 0.7088 0.0794  0.2663  0.2165  239 PRO D O   
8296 C  CB  . PRO D  239 ? 0.3304 0.2381 0.4533 -0.0095 0.1152  0.0875  239 PRO D CB  
8297 C  CG  . PRO D  239 ? 0.5019 0.3996 0.4853 -0.1197 0.1869  0.1623  239 PRO D CG  
8298 C  CD  . PRO D  239 ? 0.4045 0.3652 0.4091 -0.0082 0.0858  0.1467  239 PRO D CD  
8299 N  N   . ARG D  240 ? 0.2493 0.3598 0.4051 -0.0207 0.1107  0.1420  240 ARG D N   
8300 C  CA  . ARG D  240 ? 0.2312 0.2410 0.3881 0.0221  0.0476  0.1125  240 ARG D CA  
8301 C  C   . ARG D  240 ? 0.2320 0.2673 0.4177 0.0026  0.1493  0.0884  240 ARG D C   
8302 O  O   . ARG D  240 ? 0.2240 0.2244 0.3674 -0.0138 0.0640  0.1075  240 ARG D O   
8303 C  CB  . ARG D  240 ? 0.4231 0.2992 0.4063 -0.1622 0.0776  0.0694  240 ARG D CB  
8304 N  N   . GLU D  241 ? 0.2117 0.2345 0.3140 -0.0089 0.0782  0.0679  241 GLU D N   
8305 C  CA  . GLU D  241 ? 0.2365 0.1917 0.2583 0.0031  0.0522  0.0675  241 GLU D CA  
8306 C  C   . GLU D  241 ? 0.2311 0.2236 0.2646 -0.0221 0.0048  0.1160  241 GLU D C   
8307 O  O   . GLU D  241 ? 0.2210 0.2288 0.3277 -0.0268 -0.0060 0.0875  241 GLU D O   
8308 C  CB  . GLU D  241 ? 0.2852 0.2333 0.3254 0.0294  0.0944  0.0930  241 GLU D CB  
8309 C  CG  . GLU D  241 ? 0.3254 0.3905 0.3063 -0.0047 0.0610  0.0420  241 GLU D CG  
8310 C  CD  . GLU D  241 ? 0.2504 0.3453 0.6357 -0.0133 0.0011  0.0515  241 GLU D CD  
8311 O  OE1 . GLU D  241 ? 0.2588 0.8333 0.5985 0.0343  0.0194  -0.1996 241 GLU D OE1 
8312 O  OE2 . GLU D  241 ? 0.3602 0.4332 0.6906 0.0633  0.0217  -0.0449 241 GLU D OE2 
8313 N  N   . MET D  242 ? 0.2042 0.1791 0.2371 -0.0184 0.0359  0.0549  242 MET D N   
8314 C  CA  . MET D  242 ? 0.1945 0.1819 0.2272 0.0017  0.0029  0.0332  242 MET D CA  
8315 C  C   . MET D  242 ? 0.1267 0.1789 0.1873 -0.0153 -0.0036 0.0170  242 MET D C   
8316 O  O   . MET D  242 ? 0.1823 0.1818 0.1798 -0.0243 -0.0092 0.0252  242 MET D O   
8317 C  CB  . MET D  242 ? 0.1700 0.1951 0.1854 -0.0017 -0.0060 0.0379  242 MET D CB  
8318 C  CG  . MET D  242 ? 0.1870 0.1836 0.2102 0.0126  -0.0189 0.0167  242 MET D CG  
8319 S  SD  . MET D  242 ? 0.2074 0.1722 0.1822 -0.0063 0.0051  0.0269  242 MET D SD  
8320 C  CE  . MET D  242 ? 0.2529 0.1573 0.2046 -0.0068 0.0301  0.0302  242 MET D CE  
8321 N  N   . ILE D  243 ? 0.1618 0.1719 0.1324 -0.0193 -0.0103 0.0244  243 ILE D N   
8322 C  CA  . ILE D  243 ? 0.2014 0.1586 0.1260 0.0102  -0.0018 0.0147  243 ILE D CA  
8323 C  C   . ILE D  243 ? 0.1393 0.1350 0.1249 0.0038  0.0104  0.0032  243 ILE D C   
8324 O  O   . ILE D  243 ? 0.1615 0.1509 0.1324 -0.0168 0.0146  -0.0059 243 ILE D O   
8325 C  CB  . ILE D  243 ? 0.2046 0.1770 0.1435 -0.0181 0.0211  -0.0136 243 ILE D CB  
8326 C  CG1 . ILE D  243 ? 0.2001 0.2487 0.1855 -0.0205 0.0560  -0.0149 243 ILE D CG1 
8327 C  CG2 . ILE D  243 ? 0.2727 0.2328 0.1476 -0.0023 -0.0074 -0.0232 243 ILE D CG2 
8328 C  CD1 . ILE D  243 ? 0.2727 0.2987 0.2208 -0.0356 0.0938  -0.0411 243 ILE D CD1 
8329 N  N   . ASN D  244 ? 0.1289 0.1526 0.1204 -0.0019 0.0070  0.0237  244 ASN D N   
8330 C  CA  . ASN D  244 ? 0.1143 0.1287 0.1468 -0.0016 0.0040  -0.0135 244 ASN D CA  
8331 C  C   . ASN D  244 ? 0.1375 0.1270 0.1246 -0.0050 -0.0058 -0.0016 244 ASN D C   
8332 O  O   . ASN D  244 ? 0.1240 0.1434 0.1444 -0.0009 -0.0054 0.0017  244 ASN D O   
8333 C  CB  . ASN D  244 ? 0.1254 0.1526 0.1580 0.0089  0.0108  -0.0172 244 ASN D CB  
8334 C  CG  . ASN D  244 ? 0.1073 0.2074 0.2349 -0.0016 0.0237  -0.0417 244 ASN D CG  
8335 O  OD1 . ASN D  244 ? 0.1615 0.1863 0.2186 0.0055  0.0184  -0.0366 244 ASN D OD1 
8336 N  ND2 . ASN D  244 ? 0.2424 0.2855 0.3230 -0.0650 0.1081  -0.1003 244 ASN D ND2 
8337 N  N   . ASN D  245 ? 0.1105 0.1377 0.1219 -0.0145 0.0107  -0.0016 245 ASN D N   
8338 C  CA  . ASN D  245 ? 0.1211 0.1206 0.1210 0.0088  0.0182  0.0120  245 ASN D CA  
8339 C  C   . ASN D  245 ? 0.1141 0.1150 0.1294 -0.0039 0.0122  0.0030  245 ASN D C   
8340 O  O   . ASN D  245 ? 0.1337 0.1479 0.1466 0.0132  0.0221  0.0159  245 ASN D O   
8341 C  CB  . ASN D  245 ? 0.1322 0.1185 0.1376 -0.0064 -0.0023 0.0066  245 ASN D CB  
8342 C  CG  . ASN D  245 ? 0.1421 0.0974 0.1364 -0.0074 0.0034  0.0067  245 ASN D CG  
8343 O  OD1 . ASN D  245 ? 0.1245 0.1103 0.1755 -0.0155 0.0010  0.0062  245 ASN D OD1 
8344 N  ND2 . ASN D  245 ? 0.1306 0.1458 0.1874 0.0120  -0.0100 0.0126  245 ASN D ND2 
8345 N  N   . PHE D  246 ? 0.1296 0.1341 0.1119 -0.0012 -0.0098 -0.0004 246 PHE D N   
8346 C  CA  . PHE D  246 ? 0.1193 0.1257 0.1161 -0.0128 -0.0080 -0.0010 246 PHE D CA  
8347 C  C   . PHE D  246 ? 0.1105 0.1163 0.1188 0.0064  0.0057  -0.0074 246 PHE D C   
8348 O  O   . PHE D  246 ? 0.1191 0.1397 0.1259 -0.0065 -0.0031 -0.0019 246 PHE D O   
8349 C  CB  . PHE D  246 ? 0.1353 0.1274 0.1292 -0.0120 0.0183  -0.0003 246 PHE D CB  
8350 C  CG  . PHE D  246 ? 0.1449 0.1344 0.1184 -0.0192 0.0017  -0.0013 246 PHE D CG  
8351 C  CD1 . PHE D  246 ? 0.1449 0.1342 0.1283 -0.0238 0.0194  -0.0027 246 PHE D CD1 
8352 C  CD2 . PHE D  246 ? 0.1634 0.1360 0.1584 -0.0129 -0.0168 0.0009  246 PHE D CD2 
8353 C  CE1 . PHE D  246 ? 0.1512 0.1315 0.1597 0.0054  0.0025  0.0049  246 PHE D CE1 
8354 C  CE2 . PHE D  246 ? 0.1603 0.1627 0.1681 0.0144  -0.0239 -0.0017 246 PHE D CE2 
8355 C  CZ  . PHE D  246 ? 0.1569 0.1661 0.1673 -0.0049 -0.0111 0.0006  246 PHE D CZ  
8356 N  N   . ARG D  247 ? 0.1186 0.1103 0.1164 0.0001  -0.0100 -0.0058 247 ARG D N   
8357 C  CA  . ARG D  247 ? 0.1247 0.1037 0.1141 0.0041  -0.0183 0.0013  247 ARG D CA  
8358 C  C   . ARG D  247 ? 0.1271 0.1173 0.1051 -0.0057 0.0039  -0.0015 247 ARG D C   
8359 O  O   . ARG D  247 ? 0.1364 0.1107 0.1266 -0.0020 -0.0040 0.0065  247 ARG D O   
8360 C  CB  . ARG D  247 ? 0.1254 0.1309 0.1191 -0.0086 0.0024  -0.0181 247 ARG D CB  
8361 C  CG  . ARG D  247 ? 0.1254 0.1133 0.1370 0.0073  0.0000  -0.0201 247 ARG D CG  
8362 C  CD  . ARG D  247 ? 0.1628 0.0999 0.1215 -0.0110 0.0170  -0.0104 247 ARG D CD  
8363 N  NE  . ARG D  247 ? 0.1485 0.1116 0.1224 0.0026  -0.0109 -0.0074 247 ARG D NE  
8364 C  CZ  . ARG D  247 ? 0.1480 0.1194 0.1156 -0.0008 -0.0038 0.0026  247 ARG D CZ  
8365 N  NH1 . ARG D  247 ? 0.1597 0.1370 0.1333 0.0052  0.0038  -0.0048 247 ARG D NH1 
8366 N  NH2 . ARG D  247 ? 0.1659 0.1252 0.1231 -0.0044 -0.0153 -0.0059 247 ARG D NH2 
8367 N  N   . GLN D  248 ? 0.1254 0.1231 0.1116 -0.0010 -0.0061 -0.0013 248 GLN D N   
8368 C  CA  . GLN D  248 ? 0.1140 0.1277 0.1010 0.0022  0.0075  0.0212  248 GLN D CA  
8369 C  C   . GLN D  248 ? 0.1261 0.1079 0.1208 -0.0055 -0.0003 0.0000  248 GLN D C   
8370 O  O   . GLN D  248 ? 0.1350 0.1188 0.1166 -0.0010 0.0035  -0.0029 248 GLN D O   
8371 C  CB  . GLN D  248 ? 0.1356 0.1414 0.1155 -0.0025 0.0000  0.0006  248 GLN D CB  
8372 C  CG  . GLN D  248 ? 0.1449 0.1323 0.1213 -0.0043 0.0085  -0.0186 248 GLN D CG  
8373 C  CD  . GLN D  248 ? 0.1354 0.1318 0.1204 0.0031  -0.0062 0.0141  248 GLN D CD  
8374 O  OE1 . GLN D  248 ? 0.1523 0.1380 0.1468 -0.0015 -0.0288 -0.0083 248 GLN D OE1 
8375 N  NE2 . GLN D  248 ? 0.1698 0.1355 0.1679 0.0299  -0.0275 -0.0117 248 GLN D NE2 
8376 N  N   . VAL D  249 ? 0.1430 0.1264 0.1188 -0.0081 -0.0036 0.0175  249 VAL D N   
8377 C  CA  . VAL D  249 ? 0.1466 0.1324 0.1067 -0.0062 -0.0074 0.0122  249 VAL D CA  
8378 C  C   . VAL D  249 ? 0.1436 0.1414 0.1222 -0.0168 0.0000  0.0170  249 VAL D C   
8379 O  O   . VAL D  249 ? 0.1445 0.1520 0.1159 -0.0049 -0.0218 0.0060  249 VAL D O   
8380 C  CB  . VAL D  249 ? 0.1546 0.1177 0.1390 -0.0024 0.0110  0.0135  249 VAL D CB  
8381 C  CG1 . VAL D  249 ? 0.1723 0.1412 0.1485 -0.0190 -0.0047 0.0210  249 VAL D CG1 
8382 C  CG2 . VAL D  249 ? 0.1739 0.1579 0.1976 0.0232  -0.0276 0.0155  249 VAL D CG2 
8383 N  N   . GLN D  250 ? 0.1697 0.1235 0.1206 -0.0065 0.0030  0.0034  250 GLN D N   
8384 C  CA  . GLN D  250 ? 0.1626 0.1314 0.1272 0.0003  -0.0220 -0.0027 250 GLN D CA  
8385 C  C   . GLN D  250 ? 0.1612 0.1405 0.1313 -0.0146 0.0075  -0.0053 250 GLN D C   
8386 O  O   . GLN D  250 ? 0.1954 0.1500 0.1386 -0.0153 -0.0079 0.0188  250 GLN D O   
8387 C  CB  . GLN D  250 ? 0.1500 0.1393 0.1292 0.0010  -0.0078 -0.0055 250 GLN D CB  
8388 C  CG  . GLN D  250 ? 0.1611 0.1395 0.1405 -0.0162 -0.0136 0.0094  250 GLN D CG  
8389 C  CD  . GLN D  250 ? 0.1494 0.1059 0.1242 -0.0037 -0.0009 0.0044  250 GLN D CD  
8390 O  OE1 . GLN D  250 ? 0.1668 0.1395 0.1290 -0.0174 -0.0103 -0.0047 250 GLN D OE1 
8391 N  NE2 . GLN D  250 ? 0.1597 0.1377 0.1197 0.0038  -0.0033 0.0013  250 GLN D NE2 
8392 N  N   . LYS D  251 ? 0.1594 0.1749 0.1204 -0.0071 -0.0177 0.0008  251 LYS D N   
8393 C  CA  . LYS D  251 ? 0.1629 0.2282 0.1292 -0.0005 -0.0073 0.0176  251 LYS D CA  
8394 C  C   . LYS D  251 ? 0.1910 0.2127 0.1102 -0.0100 -0.0106 -0.0055 251 LYS D C   
8395 O  O   . LYS D  251 ? 0.1883 0.1769 0.1449 -0.0116 0.0035  -0.0006 251 LYS D O   
8396 C  CB  . LYS D  251 ? 0.1642 0.3094 0.1378 -0.0572 -0.0015 -0.0002 251 LYS D CB  
8397 C  CG  . LYS D  251 ? 0.1958 0.2797 0.1606 -0.0115 0.0157  0.0165  251 LYS D CG  
8398 C  CD  . LYS D  251 ? 0.2015 0.2802 0.1703 0.0387  0.0270  0.0253  251 LYS D CD  
8399 C  CE  . LYS D  251 ? 0.1817 0.3247 0.1268 -0.0128 0.0023  0.0006  251 LYS D CE  
8400 N  NZ  . LYS D  251 ? 0.2070 0.2364 0.1120 -0.0240 -0.0030 0.0110  251 LYS D NZ  
8401 N  N   . PHE D  252 ? 0.2082 0.2302 0.1482 0.0024  -0.0054 0.0219  252 PHE D N   
8402 C  CA  . PHE D  252 ? 0.2142 0.2115 0.1360 -0.0119 0.0117  0.0363  252 PHE D CA  
8403 C  C   . PHE D  252 ? 0.2597 0.2549 0.2389 -0.0560 0.0483  0.0072  252 PHE D C   
8404 O  O   . PHE D  252 ? 0.2789 0.2922 0.2108 -0.0055 0.0181  0.0474  252 PHE D O   
8405 C  CB  . PHE D  252 ? 0.2597 0.2329 0.2595 -0.0236 0.0334  0.0109  252 PHE D CB  
8406 C  CG  . PHE D  252 ? 0.3569 0.2879 0.2678 -0.0702 0.0291  -0.0153 252 PHE D CG  
8407 C  CD1 . PHE D  252 ? 0.4879 0.2775 0.4623 -0.1236 0.1636  0.0070  252 PHE D CD1 
8408 C  CD2 . PHE D  252 ? 0.3033 0.3294 0.5290 -0.0636 -0.1861 0.0308  252 PHE D CD2 
8409 C  CE1 . PHE D  252 ? 0.4517 0.2987 0.3827 -0.1296 -0.0414 0.1804  252 PHE D CE1 
8410 C  CE2 . PHE D  252 ? 0.4772 0.3197 0.4899 -0.0664 -0.0184 -0.0080 252 PHE D CE2 
8411 C  CZ  . PHE D  252 ? 0.4612 0.3158 0.2617 0.0484  -0.0867 0.0955  252 PHE D CZ  
8412 N  N   . ASP D  253 ? 0.3087 0.2981 0.1851 -0.0690 -0.0012 0.0209  253 ASP D N   
8413 C  CA  . ASP D  253 ? 0.3282 0.2801 0.2254 -0.0341 0.0116  0.0084  253 ASP D CA  
8414 C  C   . ASP D  253 ? 0.3036 0.3662 0.1899 -0.0412 -0.0209 -0.0678 253 ASP D C   
8415 O  O   . ASP D  253 ? 0.5059 0.2875 0.2762 0.0381  0.0627  0.0332  253 ASP D O   
8416 C  CB  . ASP D  253 ? 0.4693 0.2811 0.3065 0.0139  0.0320  0.0410  253 ASP D CB  
8417 C  CG  . ASP D  253 ? 0.3858 0.3256 0.2760 0.0403  0.0280  0.0608  253 ASP D CG  
8418 O  OD1 . ASP D  253 ? 0.3798 0.4101 0.3834 -0.0587 0.0332  0.0927  253 ASP D OD1 
8419 O  OD2 . ASP D  253 ? 0.4108 0.3658 0.2601 0.0983  -0.0132 -0.0111 253 ASP D OD2 
8420 N  N   . GLU D  254 ? 0.3400 0.4098 0.2118 -0.1216 -0.0639 0.0073  254 GLU D N   
8421 C  CA  . GLU D  254 ? 0.4241 0.3722 0.2545 -0.1084 -0.0933 0.0432  254 GLU D CA  
8422 C  C   . GLU D  254 ? 0.3273 0.3365 0.2836 -0.0295 -0.0719 0.1319  254 GLU D C   
8423 O  O   . GLU D  254 ? 0.4095 0.4749 0.2832 -0.1077 -0.0434 0.1534  254 GLU D O   
8424 C  CB  . GLU D  254 ? 0.4604 0.4102 0.1899 -0.0557 -0.0100 0.0174  254 GLU D CB  
8425 C  CG  . GLU D  254 ? 0.4943 0.8686 0.3041 -0.0880 -0.0789 -0.2207 254 GLU D CG  
8426 C  CD  . GLU D  254 ? 0.6633 1.0812 0.7418 -0.0571 -0.1852 0.0174  254 GLU D CD  
8427 O  OE1 . GLU D  254 ? 0.6831 1.5599 1.1672 -0.2694 0.0659  0.0649  254 GLU D OE1 
8428 O  OE2 . GLU D  254 ? 1.1341 1.0805 0.3788 0.1235  0.0949  0.1456  254 GLU D OE2 
8429 N  N   . ARG D  255 ? 0.2627 0.3525 0.2360 -0.0339 -0.0022 0.0658  255 ARG D N   
8430 C  CA  . ARG D  255 ? 0.2689 0.2407 0.1659 -0.0111 -0.0144 0.0275  255 ARG D CA  
8431 C  C   . ARG D  255 ? 0.2769 0.2759 0.2055 -0.0257 -0.0286 -0.0001 255 ARG D C   
8432 O  O   . ARG D  255 ? 0.2726 0.3902 0.2996 -0.0265 0.0258  -0.0412 255 ARG D O   
8433 C  CB  . ARG D  255 ? 0.2815 0.2978 0.1839 -0.0069 0.0054  0.0337  255 ARG D CB  
8434 C  CG  . ARG D  255 ? 0.3650 0.2833 0.2004 -0.0185 0.0320  0.0634  255 ARG D CG  
8435 C  CD  . ARG D  255 ? 0.2605 0.3798 0.1735 0.0487  0.0013  0.0309  255 ARG D CD  
8436 N  NE  . ARG D  255 ? 0.2796 0.2825 0.1913 -0.0243 0.0102  0.0152  255 ARG D NE  
8437 C  CZ  . ARG D  255 ? 0.2372 0.2586 0.1811 0.0086  -0.0179 0.0479  255 ARG D CZ  
8438 N  NH1 . ARG D  255 ? 0.2245 0.1775 0.2075 -0.0029 -0.0480 0.0198  255 ARG D NH1 
8439 N  NH2 . ARG D  255 ? 0.2241 0.2338 0.1865 0.0489  -0.0048 0.0030  255 ARG D NH2 
8440 N  N   . LEU D  256 ? 0.2599 0.2565 0.2500 -0.0122 0.0162  -0.0454 256 LEU D N   
8441 C  CA  . LEU D  256 ? 0.2743 0.2409 0.1967 -0.0239 -0.0341 0.0041  256 LEU D CA  
8442 C  C   . LEU D  256 ? 0.2610 0.2252 0.2077 0.0065  -0.0378 0.0241  256 LEU D C   
8443 O  O   . LEU D  256 ? 0.3213 0.2023 0.2788 0.0058  -0.0350 0.0233  256 LEU D O   
8444 C  CB  . LEU D  256 ? 0.3199 0.2632 0.2112 0.0166  -0.0539 0.0029  256 LEU D CB  
8445 C  CG  . LEU D  256 ? 0.3583 0.3418 0.2046 0.0147  -0.0812 0.0051  256 LEU D CG  
8446 C  CD1 . LEU D  256 ? 0.6900 0.4764 0.2088 -0.0023 -0.1257 0.0912  256 LEU D CD1 
8447 C  CD2 . LEU D  256 ? 0.4892 0.4005 0.2599 0.1500  -0.0691 0.0009  256 LEU D CD2 
8448 N  N   . VAL D  257 ? 0.2552 0.2034 0.1710 0.0106  0.0044  0.0163  257 VAL D N   
8449 C  CA  . VAL D  257 ? 0.2103 0.2050 0.1617 0.0005  0.0106  0.0331  257 VAL D CA  
8450 C  C   . VAL D  257 ? 0.2022 0.1936 0.1545 0.0227  -0.0008 0.0452  257 VAL D C   
8451 O  O   . VAL D  257 ? 0.2260 0.2134 0.1955 0.0540  0.0182  0.0688  257 VAL D O   
8452 C  CB  . VAL D  257 ? 0.2243 0.2165 0.1814 0.0220  0.0167  0.0153  257 VAL D CB  
8453 C  CG1 . VAL D  257 ? 0.1988 0.2173 0.1920 0.0118  0.0072  0.0190  257 VAL D CG1 
8454 C  CG2 . VAL D  257 ? 0.2306 0.2072 0.1796 -0.0072 0.0175  0.0111  257 VAL D CG2 
8455 N  N   . TYR D  258 ? 0.1902 0.1826 0.1560 0.0120  0.0236  0.0375  258 TYR D N   
8456 C  CA  . TYR D  258 ? 0.1927 0.1727 0.1705 0.0037  0.0190  0.0134  258 TYR D CA  
8457 C  C   . TYR D  258 ? 0.1872 0.1280 0.1625 0.0079  0.0061  0.0423  258 TYR D C   
8458 O  O   . TYR D  258 ? 0.2697 0.1773 0.1827 0.0020  -0.0183 0.0709  258 TYR D O   
8459 C  CB  . TYR D  258 ? 0.2367 0.1838 0.1841 0.0259  0.0261  0.0100  258 TYR D CB  
8460 C  CG  . TYR D  258 ? 0.2811 0.1826 0.1869 0.0194  0.0412  -0.0099 258 TYR D CG  
8461 C  CD1 . TYR D  258 ? 0.2777 0.2771 0.1587 -0.0013 0.0267  0.0115  258 TYR D CD1 
8462 C  CD2 . TYR D  258 ? 0.3567 0.1995 0.2302 -0.0299 0.0324  -0.0096 258 TYR D CD2 
8463 C  CE1 . TYR D  258 ? 0.2890 0.2619 0.2860 -0.0386 0.0164  -0.0476 258 TYR D CE1 
8464 C  CE2 . TYR D  258 ? 0.3758 0.2401 0.2463 0.0348  -0.0228 -0.0282 258 TYR D CE2 
8465 C  CZ  . TYR D  258 ? 0.2382 0.3012 0.2429 -0.0071 0.0139  -0.0188 258 TYR D CZ  
8466 O  OH  . TYR D  258 ? 0.3829 0.3057 0.3640 -0.0023 -0.0483 -0.0838 258 TYR D OH  
8467 N  N   . THR D  259 ? 0.1881 0.1505 0.1689 0.0106  0.0275  0.0353  259 THR D N   
8468 C  CA  . THR D  259 ? 0.1860 0.1602 0.1584 0.0081  0.0268  0.0523  259 THR D CA  
8469 C  C   . THR D  259 ? 0.1728 0.1561 0.1511 0.0381  0.0300  0.0362  259 THR D C   
8470 O  O   . THR D  259 ? 0.2240 0.2086 0.1410 0.0401  0.0397  0.0537  259 THR D O   
8471 C  CB  . THR D  259 ? 0.1939 0.2020 0.1632 0.0592  0.0417  0.0467  259 THR D CB  
8472 O  OG1 . THR D  259 ? 0.1955 0.2034 0.1818 0.0653  0.0359  0.0458  259 THR D OG1 
8473 C  CG2 . THR D  259 ? 0.1916 0.2258 0.1652 0.0134  0.0466  0.0257  259 THR D CG2 
8474 N  N   . SER D  260 ? 0.1733 0.1734 0.1515 0.0187  0.0452  0.0331  260 SER D N   
8475 C  CA  . SER D  260 ? 0.1852 0.2049 0.1802 0.0306  0.0740  0.0275  260 SER D CA  
8476 C  C   . SER D  260 ? 0.2132 0.2324 0.2115 -0.0114 0.0596  0.0606  260 SER D C   
8477 O  O   . SER D  260 ? 0.2640 0.3125 0.3484 -0.0453 0.0589  0.1414  260 SER D O   
8478 C  CB  . SER D  260 ? 0.1946 0.3379 0.1489 0.0289  0.0588  0.0140  260 SER D CB  
8479 O  OG  . SER D  260 ? 0.1984 0.2380 0.1716 0.0057  0.0621  0.0433  260 SER D OG  
8480 N  N   . PHE D  261 ? 0.2321 0.1726 0.2218 0.0107  0.0546  0.0604  261 PHE D N   
8481 C  CA  . PHE D  261 ? 0.2768 0.1709 0.2572 -0.0337 0.0455  0.0201  261 PHE D CA  
8482 C  C   . PHE D  261 ? 0.2966 0.1937 0.3131 -0.0440 0.0407  0.0668  261 PHE D C   
8483 O  O   . PHE D  261 ? 0.2546 0.1974 0.2162 0.0331  0.0357  0.0576  261 PHE D O   
8484 C  CB  . PHE D  261 ? 0.3032 0.1949 0.2515 -0.0203 0.0568  0.0518  261 PHE D CB  
8485 C  CG  . PHE D  261 ? 0.2848 0.1636 0.2263 0.0100  0.0560  0.0214  261 PHE D CG  
8486 C  CD1 . PHE D  261 ? 0.2813 0.1843 0.1690 -0.0013 0.0242  0.0173  261 PHE D CD1 
8487 C  CD2 . PHE D  261 ? 0.3076 0.1817 0.2417 0.0600  0.0549  0.0629  261 PHE D CD2 
8488 C  CE1 . PHE D  261 ? 0.2560 0.1591 0.1963 0.0042  0.0156  0.0276  261 PHE D CE1 
8489 C  CE2 . PHE D  261 ? 0.2554 0.2477 0.2636 0.0365  0.0268  0.0564  261 PHE D CE2 
8490 C  CZ  . PHE D  261 ? 0.2481 0.2054 0.1872 0.0042  0.0222  0.0260  261 PHE D CZ  
8491 N  N   . SER D  262 ? 0.4546 0.2470 0.5418 -0.1133 -0.1291 0.2002  262 SER D N   
8492 C  CA  . SER D  262 ? 0.4468 0.5137 0.5594 -0.0982 -0.1012 0.2118  262 SER D CA  
8493 C  C   . SER D  262 ? 0.6161 0.5309 1.0312 0.0518  -0.0438 -0.0277 262 SER D C   
8494 O  O   . SER D  262 ? 0.5954 0.4043 1.4131 0.1128  -0.1095 0.1040  262 SER D O   
8495 C  CB  . SER D  262 ? 0.7350 0.6437 0.5596 -0.0303 -0.2615 0.3572  262 SER D CB  
8496 O  OG  . SER D  262 ? 0.7725 0.5498 0.5802 -0.0468 -0.0257 0.3107  262 SER D OG  
8497 N  N   . GLN D  263 ? 0.5680 0.5371 0.6278 -0.0406 -0.0256 0.3069  263 GLN D N   
8498 C  CA  . GLN D  263 ? 0.6829 1.0691 0.7649 0.0469  0.0917  -0.1107 263 GLN D CA  
8499 C  C   . GLN D  263 ? 0.9323 1.1006 0.7957 -0.0008 0.0751  0.1392  263 GLN D C   
8500 O  O   . GLN D  263 ? 1.2444 0.5845 0.8201 0.4776  0.2527  0.4316  263 GLN D O   
8501 O  OXT . GLN D  263 ? 1.0967 0.9009 0.7821 0.2640  -0.0431 0.2388  263 GLN D OXT 
8502 ZN ZN  . ZN  E  .   ? 0.0992 0.1208 0.1283 -0.0011 -0.0072 0.0162  301 ZN  A ZN  
8503 C  C6  A EM5 F  .   ? 0.0936 0.1269 0.1687 -0.0137 -0.0124 0.0362  302 EM5 A C6  
8504 C  C6  B EM5 F  .   ? 0.1222 0.1602 0.1660 -0.0258 -0.0041 0.0434  302 EM5 A C6  
8505 C  C7  A EM5 F  .   ? 0.1216 0.1179 0.1588 -0.0053 -0.0278 0.0035  302 EM5 A C7  
8506 C  C7  B EM5 F  .   ? 0.1252 0.1357 0.1615 -0.0064 -0.0154 0.0248  302 EM5 A C7  
8507 C  C8  A EM5 F  .   ? 0.1285 0.1603 0.1615 -0.0139 -0.0266 0.0000  302 EM5 A C8  
8508 C  C8  B EM5 F  .   ? 0.1397 0.1611 0.1852 -0.0108 -0.0264 0.0117  302 EM5 A C8  
8509 C  C9  A EM5 F  .   ? 0.1177 0.1590 0.1689 -0.0150 -0.0303 0.0013  302 EM5 A C9  
8510 C  C9  B EM5 F  .   ? 0.1380 0.1639 0.1715 0.0001  -0.0196 -0.0055 302 EM5 A C9  
8511 C  C10 A EM5 F  .   ? 0.0933 0.1369 0.1456 -0.0103 -0.0049 0.0157  302 EM5 A C10 
8512 C  C10 B EM5 F  .   ? 0.1361 0.1328 0.1703 0.0163  -0.0424 0.0022  302 EM5 A C10 
8513 C  C12 A EM5 F  .   ? 0.1147 0.1947 0.1775 -0.0271 -0.0289 -0.0139 302 EM5 A C12 
8514 C  C12 B EM5 F  .   ? 0.1509 0.2199 0.1993 -0.0422 -0.0237 -0.0483 302 EM5 A C12 
8515 C  C2  A EM5 F  .   ? 0.1036 0.1257 0.1436 -0.0143 -0.0121 0.0175  302 EM5 A C2  
8516 C  C2  B EM5 F  .   ? 0.0994 0.1311 0.1522 -0.0126 -0.0083 0.0209  302 EM5 A C2  
8517 N  N5  A EM5 F  .   ? 0.1213 0.1080 0.1152 0.0274  -0.0170 0.0291  302 EM5 A N5  
8518 N  N5  B EM5 F  .   ? 0.1234 0.1356 0.1782 -0.0205 -0.0059 0.0067  302 EM5 A N5  
8519 C  C15 A EM5 F  .   ? 0.2233 0.2737 0.1954 0.0467  0.0001  -0.0282 302 EM5 A C15 
8520 C  C15 B EM5 F  .   ? 0.1799 0.2671 0.1939 0.0245  -0.0015 -0.0416 302 EM5 A C15 
8521 C  C16 A EM5 F  .   ? 0.3860 0.1756 0.2134 -0.0126 0.0439  -0.0305 302 EM5 A C16 
8522 C  C16 B EM5 F  .   ? 0.4549 0.2467 0.3231 0.0311  -0.0012 -0.1176 302 EM5 A C16 
8523 O  O13 A EM5 F  .   ? 0.1496 0.2436 0.2100 0.0226  -0.0298 -0.0313 302 EM5 A O13 
8524 O  O13 B EM5 F  .   ? 0.1980 0.3107 0.2595 -0.0149 -0.0441 -0.0856 302 EM5 A O13 
8525 N  N14 A EM5 F  .   ? 0.1393 0.1889 0.1633 -0.0004 0.0013  -0.0097 302 EM5 A N14 
8526 N  N14 B EM5 F  .   ? 0.1757 0.1930 0.2035 -0.0181 0.0104  -0.0507 302 EM5 A N14 
8527 O  O17 A EM5 F  .   ? 0.3953 0.3360 0.3734 0.0741  0.0541  0.0690  302 EM5 A O17 
8528 O  O17 B EM5 F  .   ? 0.5471 0.2381 0.3905 -0.0432 -0.2180 0.0835  302 EM5 A O17 
8529 S  S1  A EM5 F  .   ? 0.1024 0.1203 0.1452 -0.0029 -0.0103 0.0214  302 EM5 A S1  
8530 S  S1  B EM5 F  .   ? 0.1058 0.1235 0.1508 -0.0027 -0.0120 0.0215  302 EM5 A S1  
8531 O  O4  A EM5 F  .   ? 0.0987 0.1131 0.1466 -0.0087 -0.0218 0.0198  302 EM5 A O4  
8532 O  O4  B EM5 F  .   ? 0.1000 0.1201 0.1526 -0.0080 -0.0234 0.0206  302 EM5 A O4  
8533 O  O3  A EM5 F  .   ? 0.1103 0.1229 0.1435 0.0158  0.0025  0.0251  302 EM5 A O3  
8534 O  O3  B EM5 F  .   ? 0.1145 0.1302 0.1482 0.0160  -0.0035 0.0288  302 EM5 A O3  
8535 CL CL1 A EM5 F  .   ? 0.1302 0.1338 0.1565 -0.0035 -0.0016 0.0128  302 EM5 A CL1 
8536 CL CL1 B EM5 F  .   ? 0.1246 0.1511 0.1683 -0.0120 0.0017  0.0183  302 EM5 A CL1 
8537 N  N18 A EM5 F  .   ? 0.1747 0.1761 0.2238 -0.0502 -0.0334 0.0103  302 EM5 A N18 
8538 N  N18 B EM5 F  .   ? 0.1923 0.1569 0.2388 -0.0298 -0.0216 0.0069  302 EM5 A N18 
8539 C  C19 A EM5 F  .   ? 0.1984 0.1979 0.2244 -0.0214 0.0159  -0.0115 302 EM5 A C19 
8540 C  C19 B EM5 F  .   ? 0.1915 0.1788 0.2813 -0.0525 0.0010  -0.0125 302 EM5 A C19 
8541 C  C23 A EM5 F  .   ? 0.2181 0.1840 0.2831 -0.0153 0.0189  0.0317  302 EM5 A C23 
8542 C  C23 B EM5 F  .   ? 0.2755 0.1850 0.3400 -0.0216 0.0513  -0.0311 302 EM5 A C23 
8543 C  C24 A EM5 F  .   ? 0.2500 0.2702 0.2788 -0.0401 0.0480  0.0139  302 EM5 A C24 
8544 C  C24 B EM5 F  .   ? 0.2309 0.1941 0.3644 0.0041  0.0025  0.0273  302 EM5 A C24 
8545 C  C22 A EM5 F  .   ? 0.2532 0.2101 0.2755 -0.0439 0.0381  0.0048  302 EM5 A C22 
8546 C  C22 B EM5 F  .   ? 0.2396 0.1843 0.4211 0.0089  0.0469  -0.0116 302 EM5 A C22 
8547 C  C21 A EM5 F  .   ? 0.2113 0.2051 0.2997 -0.0108 0.0570  -0.0173 302 EM5 A C21 
8548 C  C21 B EM5 F  .   ? 0.2902 0.2006 0.4296 -0.1039 0.0279  0.0170  302 EM5 A C21 
8549 C  C20 A EM5 F  .   ? 0.1588 0.2489 0.2716 -0.0186 0.0168  0.0276  302 EM5 A C20 
8550 C  C20 B EM5 F  .   ? 0.2021 0.2304 0.3547 -0.0089 0.0152  0.0549  302 EM5 A C20 
8551 C  C1  . EDO G  .   ? 0.7850 0.6646 0.9410 -0.2820 -0.0792 0.0886  303 EDO A C1  
8552 O  O1  . EDO G  .   ? 0.5666 0.8118 0.8075 -0.1286 0.2228  0.1257  303 EDO A O1  
8553 C  C2  . EDO G  .   ? 0.5798 0.6144 0.5504 0.1407  -0.2094 -0.2122 303 EDO A C2  
8554 O  O2  . EDO G  .   ? 0.8200 0.4608 0.5827 0.1189  -0.0841 -0.0488 303 EDO A O2  
8555 C  C1  . PEG H  .   ? 0.3281 0.6510 0.5954 -0.0406 0.0081  -0.1473 304 PEG A C1  
8556 O  O1  . PEG H  .   ? 0.2398 0.3482 0.4726 -0.0138 0.0159  -0.1003 304 PEG A O1  
8557 C  C2  . PEG H  .   ? 0.1960 0.4041 0.5346 -0.0719 -0.0111 -0.0392 304 PEG A C2  
8558 O  O2  . PEG H  .   ? 0.2718 0.9717 0.7232 -0.2728 -0.1848 0.1508  304 PEG A O2  
8559 C  C3  . PEG H  .   ? 0.9395 1.5325 0.4410 0.0205  -0.4464 0.0453  304 PEG A C3  
8560 C  C4  . PEG H  .   ? 0.7919 1.3522 0.7187 0.2224  -0.3217 0.1656  304 PEG A C4  
8561 O  O4  . PEG H  .   ? 0.5368 0.8613 1.0184 0.0095  -0.3626 -0.3842 304 PEG A O4  
8562 C  C1  . EDO I  .   ? 0.2213 0.3771 0.3634 0.0434  0.0192  0.0707  305 EDO A C1  
8563 O  O1  . EDO I  .   ? 0.3671 0.5122 0.7332 0.0765  -0.0881 0.0952  305 EDO A O1  
8564 C  C2  . EDO I  .   ? 0.3430 0.3613 0.4340 -0.0129 -0.0637 0.0551  305 EDO A C2  
8565 O  O2  . EDO I  .   ? 0.1996 0.3127 0.3263 -0.0305 0.0076  0.0318  305 EDO A O2  
8566 ZN ZN  . ZN  J  .   ? 0.0924 0.0919 0.1133 0.0009  0.0038  0.0040  301 ZN  B ZN  
8567 C  C6  A EM5 K  .   ? 0.1114 0.1008 0.1152 0.0042  -0.0033 -0.0061 302 EM5 B C6  
8568 C  C6  B EM5 K  .   ? 0.1295 0.1253 0.1368 0.0147  0.0019  -0.0049 302 EM5 B C6  
8569 C  C7  A EM5 K  .   ? 0.1167 0.0951 0.1421 0.0059  0.0000  -0.0167 302 EM5 B C7  
8570 C  C7  B EM5 K  .   ? 0.1504 0.1107 0.1633 0.0053  -0.0125 -0.0110 302 EM5 B C7  
8571 C  C8  A EM5 K  .   ? 0.1293 0.0899 0.1430 0.0071  -0.0160 0.0053  302 EM5 B C8  
8572 C  C8  B EM5 K  .   ? 0.1673 0.1193 0.1654 0.0320  -0.0095 0.0127  302 EM5 B C8  
8573 C  C9  A EM5 K  .   ? 0.1293 0.1039 0.1358 -0.0022 -0.0078 0.0142  302 EM5 B C9  
8574 C  C9  B EM5 K  .   ? 0.1566 0.1407 0.1581 0.0288  0.0016  0.0320  302 EM5 B C9  
8575 C  C10 A EM5 K  .   ? 0.1295 0.1148 0.1353 0.0018  -0.0006 0.0172  302 EM5 B C10 
8576 C  C10 B EM5 K  .   ? 0.1204 0.1274 0.1570 -0.0044 -0.0176 0.0319  302 EM5 B C10 
8577 C  C12 A EM5 K  .   ? 0.1503 0.1534 0.1615 0.0088  -0.0289 0.0386  302 EM5 B C12 
8578 C  C12 B EM5 K  .   ? 0.1701 0.1483 0.2058 0.0488  -0.0157 0.0795  302 EM5 B C12 
8579 C  C2  A EM5 K  .   ? 0.1224 0.0937 0.1133 0.0029  0.0031  -0.0043 302 EM5 B C2  
8580 C  C2  B EM5 K  .   ? 0.1349 0.0971 0.1164 -0.0069 0.0006  -0.0102 302 EM5 B C2  
8581 N  N5  A EM5 K  .   ? 0.1267 0.1344 0.1622 0.0187  0.0335  0.0082  302 EM5 B N5  
8582 N  N5  B EM5 K  .   ? 0.0792 0.0774 0.1128 -0.0047 -0.0221 -0.0044 302 EM5 B N5  
8583 C  C15 A EM5 K  .   ? 0.1963 0.2588 0.2353 -0.0148 0.0268  0.0732  302 EM5 B C15 
8584 C  C15 B EM5 K  .   ? 0.1240 0.2123 0.2579 0.0110  -0.0049 0.1114  302 EM5 B C15 
8585 C  C16 A EM5 K  .   ? 0.1734 0.2795 0.1773 -0.0734 0.0420  0.0493  302 EM5 B C16 
8586 C  C16 B EM5 K  .   ? 0.1854 0.2040 0.2812 -0.0113 0.0210  0.0655  302 EM5 B C16 
8587 O  O13 A EM5 K  .   ? 0.1500 0.2122 0.1601 0.0013  -0.0058 0.0441  302 EM5 B O13 
8588 O  O13 B EM5 K  .   ? 0.1901 0.3004 0.2758 0.0088  -0.0485 0.1222  302 EM5 B O13 
8589 N  N14 A EM5 K  .   ? 0.1262 0.1798 0.1572 0.0039  -0.0050 0.0267  302 EM5 B N14 
8590 N  N14 B EM5 K  .   ? 0.1407 0.1759 0.1861 -0.0081 -0.0076 0.0469  302 EM5 B N14 
8591 O  O17 A EM5 K  .   ? 0.3628 0.2634 0.2649 -0.1670 0.0383  0.0405  302 EM5 B O17 
8592 O  O17 B EM5 K  .   ? 0.2892 0.3880 0.3502 0.0539  -0.0052 0.0509  302 EM5 B O17 
8593 S  S1  A EM5 K  .   ? 0.0992 0.0915 0.1207 -0.0003 -0.0037 0.0011  302 EM5 B S1  
8594 S  S1  B EM5 K  .   ? 0.1036 0.1040 0.1288 -0.0005 -0.0010 -0.0012 302 EM5 B S1  
8595 O  O4  A EM5 K  .   ? 0.1040 0.0973 0.1229 0.0062  -0.0006 0.0032  302 EM5 B O4  
8596 O  O4  B EM5 K  .   ? 0.1046 0.1080 0.1297 0.0040  -0.0026 -0.0015 302 EM5 B O4  
8597 O  O3  A EM5 K  .   ? 0.1028 0.1091 0.1587 -0.0089 0.0039  0.0002  302 EM5 B O3  
8598 O  O3  B EM5 K  .   ? 0.0899 0.1070 0.1340 -0.0009 0.0025  -0.0042 302 EM5 B O3  
8599 CL CL1 A EM5 K  .   ? 0.1247 0.1042 0.1365 0.0057  0.0109  0.0001  302 EM5 B CL1 
8600 CL CL1 B EM5 K  .   ? 0.1511 0.1345 0.1560 0.0181  0.0113  -0.0021 302 EM5 B CL1 
8601 N  N18 A EM5 K  .   ? 0.1798 0.1054 0.2155 0.0447  0.0186  0.0110  302 EM5 B N18 
8602 N  N18 B EM5 K  .   ? 0.1987 0.1471 0.2340 0.0590  -0.0247 0.0257  302 EM5 B N18 
8603 C  C19 A EM5 K  .   ? 0.1932 0.1410 0.1997 0.0173  0.0087  -0.0016 302 EM5 B C19 
8604 C  C19 B EM5 K  .   ? 0.2505 0.1095 0.3356 0.0436  0.0333  0.0389  302 EM5 B C19 
8605 C  C23 A EM5 K  .   ? 0.2697 0.1412 0.2224 -0.0002 0.0334  -0.0107 302 EM5 B C23 
8606 C  C23 B EM5 K  .   ? 0.3224 0.0989 0.3809 0.0687  0.0613  0.0121  302 EM5 B C23 
8607 C  C24 A EM5 K  .   ? 0.2243 0.0966 0.2517 0.0317  -0.0144 -0.0089 302 EM5 B C24 
8608 C  C24 B EM5 K  .   ? 0.2940 0.1660 0.3784 0.0185  0.0598  -0.0381 302 EM5 B C24 
8609 C  C22 A EM5 K  .   ? 0.1773 0.1209 0.2929 0.0514  0.0182  -0.0041 302 EM5 B C22 
8610 C  C22 B EM5 K  .   ? 0.2691 0.2151 0.3280 -0.0038 0.0185  0.0148  302 EM5 B C22 
8611 C  C21 A EM5 K  .   ? 0.2389 0.1231 0.3521 0.0405  0.0298  -0.0074 302 EM5 B C21 
8612 C  C21 B EM5 K  .   ? 0.2277 0.2195 0.3885 0.0493  0.0694  0.0059  302 EM5 B C21 
8613 C  C20 A EM5 K  .   ? 0.2294 0.1280 0.2176 -0.0173 0.0175  -0.0241 302 EM5 B C20 
8614 C  C20 B EM5 K  .   ? 0.2377 0.1593 0.3028 0.0413  0.0683  0.0261  302 EM5 B C20 
8615 C  C1  . EDO L  .   ? 0.2264 0.2798 0.3856 0.0053  0.0801  0.0284  303 EDO B C1  
8616 O  O1  . EDO L  .   ? 0.3261 0.2703 0.2548 0.0122  -0.0017 -0.0266 303 EDO B O1  
8617 C  C2  . EDO L  .   ? 0.4479 0.2226 0.5366 0.0732  0.1256  -0.0262 303 EDO B C2  
8618 O  O2  . EDO L  .   ? 0.7300 0.6636 0.5587 -0.3700 0.0233  -0.0807 303 EDO B O2  
8619 C  C1  . EDO M  .   ? 0.6676 0.9212 1.0009 0.1558  0.2757  -0.0633 304 EDO B C1  
8620 O  O1  . EDO M  .   ? 0.3238 0.2433 0.2876 0.0919  -0.0146 0.0339  304 EDO B O1  
8621 C  C2  . EDO M  .   ? 0.8368 0.4418 0.6276 0.1039  0.3306  0.1550  304 EDO B C2  
8622 O  O2  . EDO M  .   ? 0.8294 0.7373 0.3295 -0.1665 0.1687  -0.1430 304 EDO B O2  
8623 C  C1  . EDO N  .   ? 0.6000 0.3500 0.2108 0.0570  -0.1280 -0.0314 305 EDO B C1  
8624 O  O1  . EDO N  .   ? 1.1542 0.6098 0.6158 0.1183  0.0089  -0.1861 305 EDO B O1  
8625 C  C2  . EDO N  .   ? 0.2660 0.3532 0.1857 -0.0212 -0.0625 -0.0573 305 EDO B C2  
8626 O  O2  . EDO N  .   ? 0.4090 0.3024 0.3680 -0.0008 -0.0184 -0.0228 305 EDO B O2  
8627 C  C1  . EDO O  .   ? 0.6743 0.4845 0.3736 -0.0346 0.1614  -0.0008 306 EDO B C1  
8628 O  O1  . EDO O  .   ? 0.4459 0.1503 0.3596 -0.0370 -0.0528 -0.0022 306 EDO B O1  
8629 C  C2  . EDO O  .   ? 0.2976 0.3458 0.2737 0.0991  -0.0288 0.0331  306 EDO B C2  
8630 O  O2  . EDO O  .   ? 0.3960 0.2751 0.3206 0.0772  0.0381  -0.0029 306 EDO B O2  
8631 ZN ZN  . ZN  P  .   ? 0.1603 0.2333 0.1159 -0.0200 -0.0204 -0.0052 301 ZN  C ZN  
8632 C  C6  . EM5 Q  .   ? 0.1555 0.2745 0.1574 -0.0326 -0.0131 -0.0122 302 EM5 C C6  
8633 C  C7  . EM5 Q  .   ? 0.1818 0.2946 0.1905 -0.0608 -0.0089 -0.0402 302 EM5 C C7  
8634 C  C8  . EM5 Q  .   ? 0.2034 0.2558 0.1838 -0.0647 -0.0099 -0.0052 302 EM5 C C8  
8635 C  C9  . EM5 Q  .   ? 0.2166 0.2629 0.1335 -0.0508 -0.0319 -0.0083 302 EM5 C C9  
8636 C  C10 . EM5 Q  .   ? 0.1786 0.2180 0.1577 -0.0315 -0.0451 -0.0153 302 EM5 C C10 
8637 C  C12 . EM5 Q  .   ? 0.2421 0.2597 0.1814 -0.0498 -0.0642 -0.0627 302 EM5 C C12 
8638 C  C2  . EM5 Q  .   ? 0.1634 0.2473 0.1509 -0.0284 -0.0262 -0.0311 302 EM5 C C2  
8639 N  N5  . EM5 Q  .   ? 0.1617 0.2045 0.1179 0.0054  -0.0221 0.0225  302 EM5 C N5  
8640 C  C15 . EM5 Q  .   ? 0.3590 0.5442 0.1993 0.0753  -0.1065 -0.1560 302 EM5 C C15 
8641 C  C16 . EM5 Q  .   ? 0.5485 0.5668 0.5616 -0.0050 -0.2355 0.1028  302 EM5 C C16 
8642 O  O13 . EM5 Q  .   ? 0.2309 0.3937 0.2754 -0.0446 -0.0584 -0.0972 302 EM5 C O13 
8643 N  N14 . EM5 Q  .   ? 0.2555 0.3671 0.1945 -0.0115 -0.0223 -0.0663 302 EM5 C N14 
8644 O  O17 . EM5 Q  .   ? 0.9362 0.5041 0.3778 0.0556  -0.2975 0.0157  302 EM5 C O17 
8645 S  S1  . EM5 Q  .   ? 0.1580 0.2075 0.1376 -0.0055 -0.0161 0.0036  302 EM5 C S1  
8646 O  O4  . EM5 Q  .   ? 0.1512 0.2219 0.1103 -0.0120 -0.0283 -0.0066 302 EM5 C O4  
8647 O  O3  . EM5 Q  .   ? 0.2242 0.1918 0.0991 -0.0370 -0.0460 0.0058  302 EM5 C O3  
8648 CL CL1 . EM5 Q  .   ? 0.1699 0.2676 0.1651 -0.0292 -0.0080 -0.0059 302 EM5 C CL1 
8649 N  N18 . EM5 Q  .   ? 0.2253 0.2708 0.2646 -0.0572 -0.0200 -0.0132 302 EM5 C N18 
8650 C  C19 . EM5 Q  .   ? 0.2532 0.2897 0.2690 -0.0243 0.0105  -0.0068 302 EM5 C C19 
8651 C  C23 . EM5 Q  .   ? 0.4615 0.3389 0.2584 -0.1495 -0.0019 -0.0787 302 EM5 C C23 
8652 C  C24 . EM5 Q  .   ? 0.3345 0.2473 0.3345 -0.0514 -0.0143 0.0107  302 EM5 C C24 
8653 C  C22 . EM5 Q  .   ? 0.3603 0.3403 0.3347 -0.0535 -0.0239 -0.0781 302 EM5 C C22 
8654 C  C21 . EM5 Q  .   ? 0.2297 0.3899 0.3659 -0.0340 0.0780  -0.1161 302 EM5 C C21 
8655 C  C20 . EM5 Q  .   ? 0.2666 0.2926 0.3376 -0.0165 -0.0243 0.0099  302 EM5 C C20 
8656 C  C1  . EDO R  .   ? 0.5614 0.4677 0.4023 -0.0775 0.0039  0.0241  303 EDO C C1  
8657 O  O1  . EDO R  .   ? 0.3676 0.3981 0.4792 -0.1307 0.0713  -0.0794 303 EDO C O1  
8658 C  C2  . EDO R  .   ? 0.2768 0.2057 0.3095 -0.0609 0.0589  -0.0436 303 EDO C C2  
8659 O  O2  . EDO R  .   ? 0.3076 0.2007 0.4587 -0.0500 0.0217  -0.0665 303 EDO C O2  
8660 ZN ZN  . ZN  S  .   ? 0.1249 0.1082 0.1134 0.0011  0.0086  -0.0006 301 ZN  D ZN  
8661 C  C6  . EM5 T  .   ? 0.1503 0.1350 0.1270 -0.0068 0.0122  0.0091  302 EM5 D C6  
8662 C  C7  . EM5 T  .   ? 0.1491 0.1324 0.1637 0.0152  -0.0024 0.0091  302 EM5 D C7  
8663 C  C8  . EM5 T  .   ? 0.1809 0.1394 0.1502 0.0110  0.0201  0.0158  302 EM5 D C8  
8664 C  C9  . EM5 T  .   ? 0.1437 0.1387 0.1563 -0.0039 0.0042  0.0120  302 EM5 D C9  
8665 C  C10 . EM5 T  .   ? 0.1539 0.1492 0.1336 0.0063  -0.0065 0.0120  302 EM5 D C10 
8666 C  C12 . EM5 T  .   ? 0.1851 0.1643 0.1688 0.0143  -0.0157 0.0400  302 EM5 D C12 
8667 C  C2  . EM5 T  .   ? 0.1540 0.1261 0.1274 0.0189  0.0044  -0.0064 302 EM5 D C2  
8668 N  N5  . EM5 T  .   ? 0.1517 0.1193 0.1204 -0.0027 0.0010  -0.0240 302 EM5 D N5  
8669 C  C15 . EM5 T  .   ? 0.2541 0.2478 0.1911 -0.0465 -0.0005 0.0922  302 EM5 D C15 
8670 C  C16 . EM5 T  .   ? 0.5233 0.3533 0.3228 -0.0533 0.0658  0.0354  302 EM5 D C16 
8671 O  O13 . EM5 T  .   ? 0.1994 0.3004 0.2023 0.0156  -0.0062 0.0499  302 EM5 D O13 
8672 N  N14 . EM5 T  .   ? 0.1732 0.2092 0.1676 -0.0200 -0.0124 0.0411  302 EM5 D N14 
8673 O  O17 . EM5 T  .   ? 0.6009 0.3394 0.3607 -0.1175 -0.1252 0.0680  302 EM5 D O17 
8674 S  S1  . EM5 T  .   ? 0.1434 0.1164 0.1179 0.0018  0.0044  -0.0049 302 EM5 D S1  
8675 O  O4  . EM5 T  .   ? 0.1402 0.1253 0.1168 0.0128  0.0004  -0.0106 302 EM5 D O4  
8676 O  O3  . EM5 T  .   ? 0.1461 0.1226 0.1339 -0.0020 0.0144  -0.0076 302 EM5 D O3  
8677 CL CL1 . EM5 T  .   ? 0.1761 0.1337 0.1441 0.0185  0.0190  -0.0079 302 EM5 D CL1 
8678 N  N18 . EM5 T  .   ? 0.2423 0.1311 0.2061 0.0460  0.0226  0.0073  302 EM5 D N18 
8679 C  C19 . EM5 T  .   ? 0.2380 0.1429 0.2233 0.0289  0.0446  0.0126  302 EM5 D C19 
8680 C  C23 . EM5 T  .   ? 0.2474 0.1697 0.2237 0.0305  0.0217  0.0359  302 EM5 D C23 
8681 C  C24 . EM5 T  .   ? 0.2698 0.1685 0.2679 0.0288  0.0425  -0.0070 302 EM5 D C24 
8682 C  C22 . EM5 T  .   ? 0.2471 0.1751 0.2610 0.0547  0.0407  0.0019  302 EM5 D C22 
8683 C  C21 . EM5 T  .   ? 0.3096 0.1870 0.3707 0.0363  0.1209  -0.0173 302 EM5 D C21 
8684 C  C20 . EM5 T  .   ? 0.2328 0.1771 0.2527 0.0276  0.0339  -0.0339 302 EM5 D C20 
8685 C  C1  . EDO U  .   ? 0.2911 0.2020 0.1973 0.0620  -0.0113 -0.0201 303 EDO D C1  
8686 O  O1  . EDO U  .   ? 0.7868 0.8373 0.5863 -0.2954 -0.0403 0.1246  303 EDO D O1  
8687 C  C2  . EDO U  .   ? 0.3435 0.2865 0.2158 0.0692  0.0478  0.0357  303 EDO D C2  
8688 O  O2  . EDO U  .   ? 0.5473 0.4470 0.4360 0.0198  0.1649  0.2128  303 EDO D O2  
8689 C  C1  . EDO V  .   ? 0.5840 0.5312 0.3057 -0.0132 0.2000  -0.0138 304 EDO D C1  
8690 O  O1  . EDO V  .   ? 0.5525 0.5840 0.2806 0.0226  0.0322  0.0845  304 EDO D O1  
8691 C  C2  . EDO V  .   ? 0.2825 0.3489 0.3811 -0.0036 0.1588  0.0554  304 EDO D C2  
8692 O  O2  . EDO V  .   ? 0.2906 0.2511 0.2812 0.0496  0.1158  0.0649  304 EDO D O2  
8693 C  C1  . EDO W  .   ? 0.6853 0.4361 0.5019 0.0721  -0.2702 -0.0146 305 EDO D C1  
8694 O  O1  . EDO W  .   ? 0.4905 0.1877 0.2881 0.0390  0.0521  -0.0072 305 EDO D O1  
8695 C  C2  . EDO W  .   ? 0.5037 0.5812 0.3243 0.2081  -0.0988 -0.1181 305 EDO D C2  
8696 O  O2  . EDO W  .   ? 0.7497 0.9768 0.5031 -0.0104 0.0185  -0.1100 305 EDO D O2  
8697 C  C1  . EDO X  .   ? 0.5827 0.6900 0.4281 -0.2911 -0.0168 -0.2274 306 EDO D C1  
8698 O  O1  . EDO X  .   ? 0.3307 0.6069 0.2474 -0.0965 -0.0890 0.0907  306 EDO D O1  
8699 C  C2  . EDO X  .   ? 0.4397 1.3645 0.6342 -0.1087 0.1754  -0.0463 306 EDO D C2  
8700 O  O2  . EDO X  .   ? 0.5532 0.8464 0.2857 -0.1524 -0.0447 -0.0925 306 EDO D O2  
8701 C  C1  . PEG Y  .   ? 0.9018 0.3795 0.6111 0.1657  -0.0110 -0.1298 307 PEG D C1  
8702 O  O1  . PEG Y  .   ? 0.3898 0.3395 0.3025 -0.0131 0.0643  -0.0551 307 PEG D O1  
8703 C  C2  . PEG Y  .   ? 0.8438 0.6513 0.3619 0.0322  -0.2020 -0.0108 307 PEG D C2  
8704 O  O2  . PEG Y  .   ? 0.8033 0.3880 0.2524 0.0130  -0.0775 -0.0776 307 PEG D O2  
8705 C  C3  . PEG Y  .   ? 1.3011 0.3787 0.7429 0.0374  -0.0478 -0.2581 307 PEG D C3  
8706 C  C4  . PEG Y  .   ? 0.7533 0.2310 1.2885 -0.0440 0.0876  0.0840  307 PEG D C4  
8707 O  O4  . PEG Y  .   ? 1.0147 0.6057 0.6294 0.1899  0.4271  0.1622  307 PEG D O4  
8708 C  C1  . EDO Z  .   ? 0.5098 0.4458 0.3723 0.0248  -0.0571 -0.0699 308 EDO D C1  
8709 O  O1  . EDO Z  .   ? 0.3773 0.4844 0.2081 -0.0715 -0.0457 0.0055  308 EDO D O1  
8710 C  C2  . EDO Z  .   ? 0.3086 0.4007 0.3083 0.1330  -0.0713 0.0411  308 EDO D C2  
8711 O  O2  . EDO Z  .   ? 0.4054 0.4013 0.3961 0.0436  0.0606  0.1170  308 EDO D O2  
8712 O  O   . HOH AA .   ? 0.2972 0.2576 0.2609 0.0258  -0.0383 0.0055  401 HOH A O   
8713 O  O   . HOH AA .   ? 0.5657 0.4883 0.4861 0.0347  0.1374  -0.0121 402 HOH A O   
8714 O  O   . HOH AA .   ? 0.3542 0.4247 0.4540 -0.0961 0.1509  -0.0741 403 HOH A O   
8715 O  O   . HOH AA .   ? 0.5225 0.6318 0.3547 0.1150  -0.0569 0.1411  404 HOH A O   
8716 O  O   . HOH AA .   ? 0.3725 0.3137 0.2888 -0.0435 -0.0531 0.0476  405 HOH A O   
8717 O  O   . HOH AA .   ? 0.4890 0.4982 0.4726 -0.0016 0.1095  0.1021  406 HOH A O   
8718 O  O   . HOH AA .   ? 0.5631 0.3470 0.4546 -0.0029 0.1089  0.0673  407 HOH A O   
8719 O  O   . HOH AA .   ? 0.2632 0.7246 0.4001 -0.0670 -0.0436 -0.0586 408 HOH A O   
8720 O  O   . HOH AA .   ? 0.8136 0.4581 0.6327 -0.1159 -0.2881 -0.0039 409 HOH A O   
8721 O  O   . HOH AA .   ? 0.3228 0.4664 0.3118 0.0081  0.0319  0.0559  410 HOH A O   
8722 O  O   . HOH AA .   ? 0.2156 0.4861 0.4199 -0.0158 -0.0298 -0.0103 411 HOH A O   
8723 O  O   . HOH AA .   ? 0.3768 0.3119 0.5231 0.0182  0.1398  -0.0383 412 HOH A O   
8724 O  O   . HOH AA .   ? 0.2011 0.2062 0.2290 -0.0019 0.0005  0.0813  413 HOH A O   
8725 O  O   . HOH AA .   ? 0.2938 0.4652 0.5551 0.0888  -0.1023 -0.0100 414 HOH A O   
8726 O  O   . HOH AA .   ? 0.3932 0.3816 0.2573 0.0205  -0.0110 -0.0068 415 HOH A O   
8727 O  O   . HOH AA .   ? 0.1424 0.1524 0.1515 -0.0201 0.0089  0.0072  416 HOH A O   
8728 O  O   . HOH AA .   ? 0.3847 0.2820 0.4311 0.0586  -0.0267 -0.0143 417 HOH A O   
8729 O  O   . HOH AA .   ? 0.5993 1.3368 0.7807 -0.4514 -0.0763 0.1948  418 HOH A O   
8730 O  O   . HOH AA .   ? 0.4119 0.3810 0.5073 0.1272  0.0679  0.0499  419 HOH A O   
8731 O  O   . HOH AA .   ? 0.3049 0.2778 0.5341 -0.0348 -0.0943 0.0041  420 HOH A O   
8732 O  O   . HOH AA .   ? 0.2648 0.5220 0.3831 0.1093  -0.0406 0.0424  421 HOH A O   
8733 O  O   . HOH AA .   ? 0.2849 0.3234 0.3212 -0.0813 0.0562  -0.0635 422 HOH A O   
8734 O  O   . HOH AA .   ? 0.4892 0.3933 0.3141 -0.2350 -0.1074 0.0927  423 HOH A O   
8735 O  O   . HOH AA .   ? 0.4373 0.4190 0.3353 -0.0502 -0.0507 -0.0959 424 HOH A O   
8736 O  O   . HOH AA .   ? 0.5120 0.2454 0.5546 0.0135  0.0884  0.0247  425 HOH A O   
8737 O  O   . HOH AA .   ? 0.2129 0.2303 0.3561 0.0508  0.0684  0.0512  426 HOH A O   
8738 O  O   . HOH AA .   ? 0.3527 0.3189 0.2793 -0.0519 0.0211  0.0266  427 HOH A O   
8739 O  O   . HOH AA .   ? 0.3318 0.3581 0.2535 0.0337  -0.0015 0.0159  428 HOH A O   
8740 O  O   . HOH AA .   ? 0.3186 0.6233 0.7153 -0.0088 0.0584  0.2249  429 HOH A O   
8741 O  O   . HOH AA .   ? 0.3828 0.5110 0.2182 0.1238  0.0219  0.1042  430 HOH A O   
8742 O  O   . HOH AA .   ? 0.3480 0.3338 0.3078 0.0249  -0.0530 0.1195  431 HOH A O   
8743 O  O   . HOH AA .   ? 0.2621 0.3350 0.2667 0.0065  0.0127  0.0082  432 HOH A O   
8744 O  O   . HOH AA .   ? 0.2048 0.2451 0.3797 -0.0475 -0.0121 -0.0242 433 HOH A O   
8745 O  O   . HOH AA .   ? 0.3682 0.3332 0.2790 0.0242  -0.0227 0.0605  434 HOH A O   
8746 O  O   . HOH AA .   ? 0.2064 0.2854 0.2947 0.0137  0.0000  0.0456  435 HOH A O   
8747 O  O   . HOH AA .   ? 0.2713 0.3572 0.3808 -0.0486 -0.0025 0.0295  436 HOH A O   
8748 O  O   . HOH AA .   ? 0.2045 0.3773 0.4790 0.0440  -0.0310 0.0086  437 HOH A O   
8749 O  O   . HOH AA .   ? 0.2840 0.2671 0.2333 -0.0158 0.0135  -0.0074 438 HOH A O   
8750 O  O   . HOH AA .   ? 0.1401 0.1845 0.1673 0.0087  -0.0044 0.0184  439 HOH A O   
8751 O  O   . HOH AA .   ? 0.1929 0.2958 0.1858 0.0416  0.0009  0.0603  440 HOH A O   
8752 O  O   . HOH AA .   ? 0.3680 0.4278 0.3553 0.1604  0.0190  0.1138  441 HOH A O   
8753 O  O   . HOH AA .   ? 0.1823 0.1336 0.1967 -0.0121 -0.0185 0.0048  442 HOH A O   
8754 O  O   . HOH AA .   ? 0.5860 0.3160 0.3274 -0.0807 0.0153  -0.0102 443 HOH A O   
8755 O  O   . HOH AA .   ? 0.3563 0.4153 0.2466 -0.0141 0.0025  0.0411  444 HOH A O   
8756 O  O   . HOH AA .   ? 0.4133 0.5466 0.3642 0.2384  -0.1591 -0.1280 445 HOH A O   
8757 O  O   . HOH AA .   ? 0.3215 0.2278 0.4127 0.1084  0.1253  0.1205  446 HOH A O   
8758 O  O   . HOH AA .   ? 0.4008 0.5631 0.6793 -0.0359 -0.0520 0.0095  447 HOH A O   
8759 O  O   . HOH AA .   ? 0.2833 0.3996 0.3553 -0.0359 -0.0893 -0.0046 448 HOH A O   
8760 O  O   . HOH AA .   ? 0.1861 0.3801 0.2820 0.0039  0.0337  0.0651  449 HOH A O   
8761 O  O   . HOH AA .   ? 0.1606 0.1566 0.2272 0.0074  -0.0267 0.0270  450 HOH A O   
8762 O  O   . HOH AA .   ? 0.3514 0.3210 0.3028 -0.0034 -0.0083 -0.0209 451 HOH A O   
8763 O  O   . HOH AA .   ? 0.1869 0.1439 0.1636 -0.0063 0.0293  0.0226  452 HOH A O   
8764 O  O   . HOH AA .   ? 0.1389 0.1405 0.1877 0.0075  -0.0150 0.0256  453 HOH A O   
8765 O  O   . HOH AA .   ? 0.2565 0.3017 0.4593 -0.0423 -0.1421 0.0518  454 HOH A O   
8766 O  O   . HOH AA .   ? 0.3958 0.4072 0.5932 0.1377  -0.0044 0.1452  455 HOH A O   
8767 O  O   . HOH AA .   ? 0.2270 0.3175 0.2984 -0.0155 0.0251  0.0311  456 HOH A O   
8768 O  O   . HOH AA .   ? 0.2804 0.4509 0.2759 -0.0281 -0.0617 0.0842  457 HOH A O   
8769 O  O   . HOH AA .   ? 0.3403 0.6703 0.3609 -0.0587 0.0467  0.1553  458 HOH A O   
8770 O  O   . HOH AA .   ? 0.5253 0.3941 0.4375 -0.0451 0.0924  0.0151  459 HOH A O   
8771 O  O   . HOH AA .   ? 0.5977 0.4104 0.3591 -0.2115 -0.1397 0.0143  460 HOH A O   
8772 O  O   . HOH AA .   ? 0.3371 0.2832 0.3970 -0.0574 -0.0823 -0.0377 461 HOH A O   
8773 O  O   . HOH AA .   ? 0.1684 0.2455 0.2403 0.0271  -0.0089 0.0006  462 HOH A O   
8774 O  O   . HOH AA .   ? 0.1331 0.1482 0.1863 -0.0132 0.0109  0.0096  463 HOH A O   
8775 O  O   . HOH AA .   ? 0.5304 0.3153 0.5862 -0.0133 -0.1127 -0.1608 464 HOH A O   
8776 O  O   . HOH AA .   ? 0.1903 0.2673 0.1739 -0.0405 -0.0425 0.0248  465 HOH A O   
8777 O  O   . HOH AA .   ? 0.1743 0.1899 0.2487 0.0153  -0.0563 -0.0019 466 HOH A O   
8778 O  O   . HOH AA .   ? 0.3180 0.2664 0.2450 -0.0595 -0.0926 0.0341  467 HOH A O   
8779 O  O   . HOH AA .   ? 0.7424 0.5475 0.3264 -0.0071 0.0792  0.0451  468 HOH A O   
8780 O  O   . HOH AA .   ? 0.1179 0.1253 0.1650 0.0012  -0.0005 0.0322  469 HOH A O   
8781 O  O   . HOH AA .   ? 0.2066 0.4987 0.2996 0.0283  0.0315  -0.0789 470 HOH A O   
8782 O  O   . HOH AA .   ? 0.2205 0.2310 0.1966 0.0340  -0.0428 -0.0077 471 HOH A O   
8783 O  O   . HOH AA .   ? 0.2175 0.2352 0.2754 0.0037  0.0302  0.0770  472 HOH A O   
8784 O  O   . HOH AA .   ? 0.3965 0.2240 0.2361 -0.0890 0.0186  0.0675  473 HOH A O   
8785 O  O   . HOH AA .   ? 0.4178 0.2003 0.4961 0.0117  0.2149  0.0377  474 HOH A O   
8786 O  O   . HOH AA .   ? 0.2631 0.3219 0.2780 0.0881  0.0389  0.0566  475 HOH A O   
8787 O  O   . HOH AA .   ? 0.2251 0.2931 0.3134 0.0534  -0.0478 0.0079  476 HOH A O   
8788 O  O   . HOH AA .   ? 0.3944 0.2721 0.4373 -0.0072 0.1887  0.0218  477 HOH A O   
8789 O  O   . HOH AA .   ? 0.3768 0.1975 0.3384 0.0556  0.0075  0.0141  478 HOH A O   
8790 O  O   . HOH AA .   ? 0.3045 0.3048 0.3019 -0.0049 -0.0087 -0.0584 479 HOH A O   
8791 O  O   . HOH AA .   ? 0.1955 0.2374 0.2545 -0.0154 0.0201  0.0767  480 HOH A O   
8792 O  O   . HOH AA .   ? 0.2455 0.2760 0.2470 -0.0139 0.0650  0.0048  481 HOH A O   
8793 O  O   . HOH AA .   ? 0.2860 0.4178 0.2534 0.0003  0.0052  0.0911  482 HOH A O   
8794 O  O   . HOH AA .   ? 0.2214 0.2000 0.1697 0.0073  -0.0289 -0.0273 483 HOH A O   
8795 O  O   . HOH AA .   ? 0.2563 0.3124 0.6452 -0.0194 0.0516  0.0838  484 HOH A O   
8796 O  O   . HOH AA .   ? 0.1657 0.1451 0.2441 0.0188  -0.0164 0.0027  485 HOH A O   
8797 O  O   . HOH AA .   ? 0.1884 0.2829 0.2752 0.0409  0.0201  0.0307  486 HOH A O   
8798 O  O   . HOH AA .   ? 0.1570 0.3192 0.3132 -0.0413 -0.0165 0.0282  487 HOH A O   
8799 O  O   . HOH AA .   ? 0.2732 0.3418 0.5879 0.0508  -0.0428 -0.0037 488 HOH A O   
8800 O  O   . HOH AA .   ? 0.4707 0.3059 0.5316 0.1411  0.0311  0.1511  489 HOH A O   
8801 O  O   . HOH AA .   ? 0.1067 0.1091 0.1738 0.0047  -0.0053 0.0205  490 HOH A O   
8802 O  O   . HOH AA .   ? 0.5126 0.5912 0.4402 0.0124  -0.1288 -0.0414 491 HOH A O   
8803 O  O   . HOH AA .   ? 0.2811 0.7867 0.8410 0.1717  -0.1728 -0.2732 492 HOH A O   
8804 O  O   . HOH AA .   ? 0.4794 0.4157 0.5804 0.1065  0.1298  0.0381  493 HOH A O   
8805 O  O   . HOH AA .   ? 0.1827 0.1924 0.3343 0.0017  -0.0140 -0.0132 494 HOH A O   
8806 O  O   . HOH AA .   ? 0.1395 0.1190 0.1896 -0.0029 -0.0145 0.0103  495 HOH A O   
8807 O  O   . HOH AA .   ? 0.2900 0.3688 0.1527 0.0077  0.0330  0.0071  496 HOH A O   
8808 O  O   . HOH AA .   ? 0.2254 0.1371 0.2566 -0.0456 -0.0525 -0.0048 497 HOH A O   
8809 O  O   . HOH AA .   ? 0.4138 0.2759 0.5924 0.0173  0.0109  0.0985  498 HOH A O   
8810 O  O   . HOH AA .   ? 0.3658 0.2904 0.2653 -0.0862 0.0027  -0.0468 499 HOH A O   
8811 O  O   . HOH AA .   ? 0.3014 0.5697 0.5367 0.0249  -0.1195 0.2497  500 HOH A O   
8812 O  O   . HOH AA .   ? 0.2123 0.2197 0.2764 0.0179  0.0517  0.0428  501 HOH A O   
8813 O  O   . HOH AA .   ? 0.3077 0.4873 0.3375 -0.0927 0.0312  0.1004  502 HOH A O   
8814 O  O   . HOH AA .   ? 0.2804 0.7546 0.4143 -0.1203 -0.1286 0.1204  503 HOH A O   
8815 O  O   . HOH AA .   ? 0.1649 0.1303 0.1642 0.0032  0.0183  -0.0037 504 HOH A O   
8816 O  O   . HOH AA .   ? 0.3006 0.4239 0.2640 -0.0772 -0.0828 0.1148  505 HOH A O   
8817 O  O   . HOH AA .   ? 0.1539 0.1279 0.2194 -0.0248 -0.0263 0.0305  506 HOH A O   
8818 O  O   . HOH AA .   ? 0.1697 0.4181 0.4714 -0.0413 -0.0602 0.0712  507 HOH A O   
8819 O  O   . HOH AA .   ? 0.5179 0.3175 0.4078 0.1379  0.0234  0.0209  508 HOH A O   
8820 O  O   . HOH AA .   ? 0.1464 0.1097 0.2162 -0.0174 -0.0348 0.0233  509 HOH A O   
8821 O  O   . HOH AA .   ? 0.3143 0.2420 0.2575 0.0403  -0.0253 0.0343  510 HOH A O   
8822 O  O   . HOH AA .   ? 0.3147 0.5052 0.2596 0.0608  0.0226  0.0263  511 HOH A O   
8823 O  O   . HOH AA .   ? 0.3062 0.2134 0.2538 -0.0257 0.0080  0.0532  512 HOH A O   
8824 O  O   . HOH AA .   ? 0.3186 0.2100 0.3736 0.0274  0.0509  0.0935  513 HOH A O   
8825 O  O   . HOH AA .   ? 0.2099 0.2703 0.2743 0.0119  0.0558  0.0480  514 HOH A O   
8826 O  O   . HOH AA .   ? 0.2679 0.2966 0.2579 0.0227  0.0282  -0.0402 515 HOH A O   
8827 O  O   . HOH AA .   ? 0.2185 0.2746 0.3277 -0.0099 0.0414  0.0283  516 HOH A O   
8828 O  O   . HOH AA .   ? 0.2843 0.4674 0.3843 -0.1813 -0.0356 -0.0620 517 HOH A O   
8829 O  O   . HOH AA .   ? 0.2857 0.3441 0.3949 -0.0974 -0.1297 0.0907  518 HOH A O   
8830 O  O   . HOH AA .   ? 0.3516 0.2900 0.2515 -0.0489 0.0000  0.0383  519 HOH A O   
8831 O  O   . HOH AA .   ? 0.3308 0.3200 0.2542 -0.0530 0.0792  0.0013  520 HOH A O   
8832 O  O   . HOH AA .   ? 0.3048 0.3089 0.4298 -0.0851 -0.0363 0.1029  521 HOH A O   
8833 O  O   . HOH AA .   ? 0.2911 0.3865 0.3877 0.1021  -0.0549 -0.0674 522 HOH A O   
8834 O  O   . HOH AA .   ? 0.3481 0.4241 0.5256 0.1785  -0.1094 -0.1500 523 HOH A O   
8835 O  O   . HOH AA .   ? 0.3547 0.3660 0.3312 -0.0252 -0.0991 0.0035  524 HOH A O   
8836 O  O   . HOH AA .   ? 0.4650 0.3564 0.2830 -0.0789 0.0442  0.0498  525 HOH A O   
8837 O  O   . HOH AA .   ? 0.2838 0.4568 0.5554 -0.0480 -0.0729 0.0619  526 HOH A O   
8838 O  O   . HOH AA .   ? 0.1312 0.1483 0.1846 0.0009  0.0080  0.0200  527 HOH A O   
8839 O  O   . HOH AA .   ? 0.4430 0.4283 0.4521 -0.0181 0.0013  -0.0086 528 HOH A O   
8840 O  O   . HOH AA .   ? 0.2732 0.3176 0.3059 -0.0129 0.0108  0.1333  529 HOH A O   
8841 O  O   . HOH AA .   ? 0.3883 0.3920 0.3749 0.0317  0.1215  0.0525  530 HOH A O   
8842 O  O   . HOH AA .   ? 0.1591 0.1599 0.1923 -0.0103 -0.0124 0.0309  531 HOH A O   
8843 O  O   . HOH AA .   ? 0.9393 0.3013 0.5696 0.0554  0.2320  -0.0744 532 HOH A O   
8844 O  O   . HOH AA .   ? 0.3968 0.3182 0.1748 -0.1187 -0.0921 0.0257  533 HOH A O   
8845 O  O   . HOH AA .   ? 0.5377 0.4904 0.5401 -0.0292 0.0156  -0.0016 534 HOH A O   
8846 O  O   . HOH AA .   ? 0.2907 0.3259 0.2967 -0.0354 -0.0081 -0.0539 535 HOH A O   
8847 O  O   . HOH AA .   ? 0.4659 0.3049 0.3185 -0.1046 0.0109  0.0397  536 HOH A O   
8848 O  O   . HOH AA .   ? 0.4502 0.3741 0.3666 0.0724  0.1157  0.1720  537 HOH A O   
8849 O  O   . HOH AA .   ? 0.3265 0.5498 0.4084 -0.1137 -0.0517 0.0238  538 HOH A O   
8850 O  O   . HOH AA .   ? 0.3141 0.2797 0.2383 -0.0277 -0.0980 0.0431  539 HOH A O   
8851 O  O   . HOH AA .   ? 0.2469 0.1821 0.2366 -0.0490 0.0300  0.0368  540 HOH A O   
8852 O  O   . HOH AA .   ? 0.3017 0.5677 0.3262 -0.0600 0.1477  -0.0542 541 HOH A O   
8853 O  O   . HOH AA .   ? 0.2284 0.2498 0.2821 -0.0050 0.0356  -0.0363 542 HOH A O   
8854 O  O   . HOH AA .   ? 0.2539 0.2730 0.3301 0.1259  -0.0013 0.0362  543 HOH A O   
8855 O  O   . HOH AA .   ? 0.2596 0.2080 0.1854 -0.0240 0.0244  0.0209  544 HOH A O   
8856 O  O   . HOH AA .   ? 0.2100 0.4447 0.3089 -0.0289 0.0062  0.0626  545 HOH A O   
8857 O  O   . HOH AA .   ? 0.3179 0.5360 0.6245 -0.1047 0.1687  -0.2115 546 HOH A O   
8858 O  O   . HOH AA .   ? 0.5481 0.3922 0.5274 0.1276  -0.1235 -0.0102 547 HOH A O   
8859 O  O   . HOH AA .   ? 0.1896 0.4733 0.4941 -0.0692 -0.0340 0.0051  548 HOH A O   
8860 O  O   . HOH AA .   ? 0.7569 0.3506 0.4746 -0.0862 0.0082  0.1609  549 HOH A O   
8861 O  O   . HOH AA .   ? 0.2893 0.3212 0.2606 0.0071  -0.0313 0.0325  550 HOH A O   
8862 O  O   . HOH AA .   ? 0.1629 0.2119 0.2600 -0.0253 -0.0168 0.0557  551 HOH A O   
8863 O  O   . HOH AA .   ? 0.6241 0.3547 0.5131 0.0739  -0.1101 -0.1101 552 HOH A O   
8864 O  O   . HOH AA .   ? 0.1786 0.2116 0.2351 0.0143  0.0178  0.0408  553 HOH A O   
8865 O  O   . HOH AA .   ? 0.5107 0.5014 0.4718 -0.2237 0.0229  -0.1062 554 HOH A O   
8866 O  O   . HOH AA .   ? 0.3543 0.5371 0.3326 -0.1244 0.1562  -0.0868 555 HOH A O   
8867 O  O   . HOH AA .   ? 0.3352 0.3574 0.3834 -0.0517 -0.0539 0.0615  556 HOH A O   
8868 O  O   . HOH AA .   ? 0.4049 0.6610 0.4580 0.0570  -0.1967 -0.0087 557 HOH A O   
8869 O  O   . HOH AA .   ? 0.1791 0.1502 0.2472 0.0187  0.0296  0.0299  558 HOH A O   
8870 O  O   . HOH AA .   ? 0.8327 0.3617 0.5113 0.2355  -0.0460 -0.1291 559 HOH A O   
8871 O  O   . HOH AA .   ? 0.4388 0.3928 0.6145 -0.1540 -0.1802 -0.0778 560 HOH A O   
8872 O  O   . HOH AA .   ? 0.4629 0.4054 0.3607 -0.0442 0.0416  0.1955  561 HOH A O   
8873 O  O   . HOH AA .   ? 0.3174 0.4436 0.2166 -0.0538 0.0343  0.0563  562 HOH A O   
8874 O  O   . HOH AA .   ? 0.5086 0.2825 0.2432 0.0388  -0.0178 0.0175  563 HOH A O   
8875 O  O   . HOH AA .   ? 0.4556 0.6053 0.3308 -0.1128 0.0423  -0.0668 564 HOH A O   
8876 O  O   . HOH AA .   ? 0.4277 0.4009 0.4163 -0.1758 0.0042  0.1073  565 HOH A O   
8877 O  O   . HOH AA .   ? 0.3814 0.4041 0.6786 -0.0946 -0.1840 0.1681  566 HOH A O   
8878 O  O   . HOH AA .   ? 0.2952 0.1943 0.3585 0.0377  -0.1655 -0.0147 567 HOH A O   
8879 O  O   . HOH AA .   ? 0.2376 0.4322 0.3199 0.1264  0.0465  0.1034  568 HOH A O   
8880 O  O   . HOH AA .   ? 0.1925 0.2860 0.2703 0.0276  0.0296  0.0713  569 HOH A O   
8881 O  O   . HOH AA .   ? 0.1401 0.1981 0.1961 0.0261  -0.0204 -0.0077 570 HOH A O   
8882 O  O   . HOH AA .   ? 0.3825 0.6417 0.3953 0.1587  -0.1049 0.0561  571 HOH A O   
8883 O  O   . HOH AA .   ? 0.5677 0.5287 0.6121 0.1446  -0.1095 0.0639  572 HOH A O   
8884 O  O   . HOH AA .   ? 0.2570 0.2279 0.2712 0.0566  0.0085  0.0519  573 HOH A O   
8885 O  O   . HOH AA .   ? 0.3624 0.2988 0.2830 0.0062  0.0628  0.0820  574 HOH A O   
8886 O  O   . HOH AA .   ? 0.4677 0.3003 0.4923 -0.1073 -0.2080 0.0432  575 HOH A O   
8887 O  O   . HOH AA .   ? 0.5995 0.4008 0.4474 -0.0174 -0.0038 0.0474  576 HOH A O   
8888 O  O   . HOH AA .   ? 0.2887 0.3940 0.2539 -0.0369 -0.0632 -0.0734 577 HOH A O   
8889 O  O   . HOH AA .   ? 0.1710 0.1332 0.2564 -0.0081 -0.0560 0.0602  578 HOH A O   
8890 O  O   . HOH AA .   ? 0.2552 0.3815 0.3692 -0.0750 -0.0048 -0.0461 579 HOH A O   
8891 O  O   . HOH AA .   ? 0.2987 0.3125 0.3511 -0.1134 -0.0302 -0.0482 580 HOH A O   
8892 O  O   . HOH AA .   ? 0.4049 0.3698 0.4446 -0.0348 -0.0502 0.2398  581 HOH A O   
8893 O  O   . HOH AA .   ? 0.4074 0.3169 0.5148 0.0172  0.1278  0.1093  582 HOH A O   
8894 O  O   . HOH AA .   ? 0.3495 0.6275 0.4715 -0.0820 -0.1062 0.2546  583 HOH A O   
8895 O  O   . HOH AA .   ? 0.2548 0.3249 0.3630 -0.0447 -0.0491 -0.0054 584 HOH A O   
8896 O  O   . HOH AA .   ? 0.7398 0.2940 0.7749 0.0932  0.0177  -0.0150 585 HOH A O   
8897 O  O   . HOH AA .   ? 0.3662 0.4081 0.2514 0.0773  0.0533  0.0337  586 HOH A O   
8898 O  O   . HOH AA .   ? 0.5501 0.3896 0.3300 -0.0380 0.0279  -0.0479 587 HOH A O   
8899 O  O   . HOH AA .   ? 0.3862 0.7718 0.3231 0.1219  0.0145  0.0118  588 HOH A O   
8900 O  O   . HOH AA .   ? 0.3258 0.3210 0.3432 0.1316  0.0241  -0.0325 589 HOH A O   
8901 O  O   . HOH AA .   ? 0.4021 0.5802 0.2625 -0.0820 -0.0100 -0.1287 590 HOH A O   
8902 O  O   . HOH AA .   ? 0.4653 0.5134 0.4297 -0.0083 0.0253  -0.0024 591 HOH A O   
8903 O  O   . HOH AA .   ? 0.3739 0.2800 0.4003 0.1186  -0.0726 0.0482  592 HOH A O   
8904 O  O   . HOH AA .   ? 0.4224 1.1594 0.3795 0.0647  0.0683  -0.0593 593 HOH A O   
8905 O  O   . HOH AA .   ? 0.1908 0.1838 0.2402 -0.0037 0.0151  0.0458  594 HOH A O   
8906 O  O   . HOH AA .   ? 0.2699 0.4276 0.3063 0.0074  0.0038  -0.0155 595 HOH A O   
8907 O  O   . HOH AA .   ? 0.4983 0.2661 0.3655 0.0082  -0.0707 0.0572  596 HOH A O   
8908 O  O   . HOH AA .   ? 0.5432 0.2911 0.6178 -0.1521 -0.0304 -0.0066 597 HOH A O   
8909 O  O   . HOH AA .   ? 0.4332 0.4435 0.4772 -0.0299 -0.0055 -0.0068 598 HOH A O   
8910 O  O   . HOH AA .   ? 0.5270 0.4361 0.5654 -0.0531 0.1159  0.0340  599 HOH A O   
8911 O  O   . HOH AA .   ? 0.3972 0.3551 0.4203 0.0633  -0.1138 0.0167  600 HOH A O   
8912 O  O   . HOH AA .   ? 0.2427 0.4799 0.7306 -0.0502 0.0336  -0.0447 601 HOH A O   
8913 O  O   . HOH AA .   ? 0.3380 0.2174 0.3172 -0.0530 -0.0344 0.0001  602 HOH A O   
8914 O  O   . HOH AA .   ? 0.1795 0.2963 0.3001 -0.0220 -0.0273 0.0376  603 HOH A O   
8915 O  O   . HOH AA .   ? 0.3905 0.3351 0.3366 -0.0785 -0.0051 -0.0151 604 HOH A O   
8916 O  O   . HOH AA .   ? 0.5705 1.0922 0.4369 -0.1523 0.1373  -0.1751 605 HOH A O   
8917 O  O   . HOH AA .   ? 0.6156 0.2980 0.3887 0.0461  -0.1254 0.0386  606 HOH A O   
8918 O  O   . HOH AA .   ? 0.4337 0.6063 0.3750 0.0031  0.1617  0.0337  607 HOH A O   
8919 O  O   . HOH AA .   ? 0.6967 0.7658 0.3563 -0.1541 0.0751  -0.0842 608 HOH A O   
8920 O  O   . HOH AA .   ? 0.3659 0.3055 0.5678 -0.0489 0.0009  0.1234  609 HOH A O   
8921 O  O   . HOH AA .   ? 0.3596 0.2816 0.3869 0.0131  -0.0478 0.0111  610 HOH A O   
8922 O  O   . HOH AA .   ? 0.4882 0.4134 0.5391 -0.0555 0.2247  0.0515  611 HOH A O   
8923 O  O   . HOH AA .   ? 0.5510 0.4611 0.7153 0.1839  -0.2673 -0.0078 612 HOH A O   
8924 O  O   . HOH AA .   ? 0.5414 0.4432 0.3518 -0.1082 -0.0552 0.0201  613 HOH A O   
8925 O  O   . HOH AA .   ? 0.2818 0.2102 0.4035 -0.0607 -0.0132 -0.0139 614 HOH A O   
8926 O  O   . HOH AA .   ? 0.6940 0.4765 0.3916 -0.0089 -0.0449 0.0950  615 HOH A O   
8927 O  O   . HOH AA .   ? 0.3558 0.8661 0.4903 0.0449  0.0411  0.2781  616 HOH A O   
8928 O  O   . HOH AA .   ? 0.4477 0.3560 0.2781 0.0237  0.0684  0.0158  617 HOH A O   
8929 O  O   . HOH AA .   ? 0.8301 0.7094 0.3125 -0.2199 0.1303  -0.0380 618 HOH A O   
8930 O  O   . HOH AA .   ? 0.2713 0.4131 0.3581 -0.0379 -0.0877 0.0381  619 HOH A O   
8931 O  O   . HOH AA .   ? 0.5213 0.4677 0.3773 0.0464  0.0902  0.0854  620 HOH A O   
8932 O  O   . HOH AA .   ? 0.9877 0.3849 0.9673 -0.1914 -0.0380 0.2594  621 HOH A O   
8933 O  O   . HOH AA .   ? 0.5069 0.5755 0.3398 -0.2555 -0.0820 -0.0294 622 HOH A O   
8934 O  O   . HOH AA .   ? 0.2732 0.4133 0.3207 0.0839  -0.0062 0.0190  623 HOH A O   
8935 O  O   . HOH AA .   ? 0.3483 0.5263 0.2546 0.1092  -0.0276 0.0012  624 HOH A O   
8936 O  O   . HOH AA .   ? 0.5387 0.4390 0.4989 0.2196  0.1606  0.1515  625 HOH A O   
8937 O  O   . HOH AA .   ? 0.3395 0.5970 0.5604 -0.1715 0.0297  0.0083  626 HOH A O   
8938 O  O   . HOH AA .   ? 0.2427 0.3431 0.6264 -0.0048 -0.0776 0.0296  627 HOH A O   
8939 O  O   . HOH AA .   ? 0.2947 0.3206 0.5333 0.0392  0.0762  0.1490  628 HOH A O   
8940 O  O   . HOH AA .   ? 0.6699 0.4548 0.4058 -0.1203 -0.1053 -0.0298 629 HOH A O   
8941 O  O   . HOH AA .   ? 0.3827 0.3944 0.3827 0.0400  0.0971  -0.0323 630 HOH A O   
8942 O  O   . HOH AA .   ? 0.2347 0.6429 0.3527 0.0026  0.0886  -0.0260 631 HOH A O   
8943 O  O   . HOH AA .   ? 0.5147 0.4899 0.5107 -0.0303 0.0128  0.0106  632 HOH A O   
8944 O  O   . HOH AA .   ? 0.3686 0.4162 0.3273 -0.0159 -0.0041 0.0719  633 HOH A O   
8945 O  O   . HOH AA .   ? 0.5044 0.5230 0.4758 -0.1289 0.0310  0.0176  634 HOH A O   
8946 O  O   . HOH AA .   ? 0.4075 0.3299 0.4868 -0.0722 0.0407  0.0685  635 HOH A O   
8947 O  O   . HOH AA .   ? 0.3788 0.3211 0.4504 -0.0541 -0.0309 0.1203  636 HOH A O   
8948 O  O   . HOH AA .   ? 0.2821 0.5630 0.3085 -0.0590 -0.0888 0.0938  637 HOH A O   
8949 O  O   . HOH AA .   ? 0.3884 0.4439 0.4581 0.1161  0.0750  0.0154  638 HOH A O   
8950 O  O   . HOH AA .   ? 0.3814 0.7196 0.4279 -0.0819 -0.0337 0.0732  639 HOH A O   
8951 O  O   . HOH AA .   ? 0.2374 0.3852 0.5103 0.0172  0.0801  -0.0161 640 HOH A O   
8952 O  O   . HOH AA .   ? 0.4642 0.5407 0.4235 0.0998  0.0206  0.0006  641 HOH A O   
8953 O  O   . HOH AA .   ? 0.3059 0.6492 0.6924 0.1852  -0.0096 0.0534  642 HOH A O   
8954 O  O   . HOH AA .   ? 0.7634 0.3628 0.6821 0.1078  0.3088  0.2178  643 HOH A O   
8955 O  O   . HOH AA .   ? 0.2051 0.1675 0.2395 -0.0166 -0.0351 -0.0114 644 HOH A O   
8956 O  O   . HOH AA .   ? 0.6118 0.6516 0.3675 -0.1646 0.0274  0.1357  645 HOH A O   
8957 O  O   . HOH AA .   ? 0.3630 0.6082 0.5536 0.1318  0.0105  0.1381  646 HOH A O   
8958 O  O   . HOH AA .   ? 0.7328 0.5813 0.4915 -0.1848 0.0971  -0.0348 647 HOH A O   
8959 O  O   . HOH AA .   ? 0.5326 0.4393 0.3940 -0.1304 -0.0752 0.0684  648 HOH A O   
8960 O  O   . HOH AA .   ? 0.4888 0.4512 0.4821 -0.0085 -0.0198 0.0258  649 HOH A O   
8961 O  O   . HOH AA .   ? 0.6021 0.4066 0.3721 0.1435  0.0142  -0.0902 650 HOH A O   
8962 O  O   . HOH AA .   ? 0.3001 0.6715 0.3097 0.1017  0.0219  0.0055  651 HOH A O   
8963 O  O   . HOH AA .   ? 0.3510 0.3831 0.4440 -0.0581 0.0544  -0.0922 652 HOH A O   
8964 O  O   . HOH AA .   ? 0.3454 0.9162 0.6193 -0.2020 -0.1021 -0.0296 653 HOH A O   
8965 O  O   . HOH AA .   ? 0.5836 0.4166 0.6421 0.0679  -0.1541 -0.1110 654 HOH A O   
8966 O  O   . HOH AA .   ? 0.2913 0.4266 0.5851 -0.0534 0.0153  0.1923  655 HOH A O   
8967 O  O   . HOH AA .   ? 0.3915 0.4974 0.5193 0.0011  -0.0879 -0.1801 656 HOH A O   
8968 O  O   . HOH AA .   ? 0.4660 0.3968 0.5908 0.0370  0.1495  0.0736  657 HOH A O   
8969 O  O   . HOH AA .   ? 0.3953 0.5601 0.3542 -0.0842 -0.0020 0.0736  658 HOH A O   
8970 O  O   . HOH AA .   ? 0.3801 0.4976 0.3173 -0.1357 -0.0789 0.1107  659 HOH A O   
8971 O  O   . HOH AA .   ? 0.6016 0.7358 0.4877 -0.1217 0.0205  -0.1588 660 HOH A O   
8972 O  O   . HOH AA .   ? 0.4768 0.4681 0.4799 -0.0072 0.0058  -0.0165 661 HOH A O   
8973 O  O   . HOH AA .   ? 0.6169 0.1888 0.7588 -0.0215 0.0757  0.0366  662 HOH A O   
8974 O  O   . HOH AA .   ? 0.3657 0.3371 0.3316 -0.1132 0.0614  -0.0444 663 HOH A O   
8975 O  O   . HOH AA .   ? 0.5159 0.5796 0.3828 0.0543  -0.1236 0.0816  664 HOH A O   
8976 O  O   . HOH AA .   ? 0.5422 0.5628 0.3834 -0.2657 0.0999  -0.0421 665 HOH A O   
8977 O  O   . HOH AA .   ? 0.3561 0.3422 0.5374 -0.1368 0.0588  -0.0392 666 HOH A O   
8978 O  O   . HOH AA .   ? 0.2334 0.2814 0.2286 0.0285  0.0395  0.0468  667 HOH A O   
8979 O  O   . HOH AA .   ? 0.3177 0.4111 0.2522 0.0151  0.0958  0.0412  668 HOH A O   
8980 O  O   . HOH AA .   ? 0.4734 0.4580 0.4571 0.0095  -0.0222 0.0237  669 HOH A O   
8981 O  O   . HOH AA .   ? 0.2438 0.2195 0.5097 -0.0939 -0.0093 0.0421  670 HOH A O   
8982 O  O   . HOH AA .   ? 0.4888 0.6731 0.5962 0.0823  -0.1150 0.1615  671 HOH A O   
8983 O  O   . HOH AA .   ? 0.3658 0.2285 0.4355 -0.0109 0.0350  0.0272  672 HOH A O   
8984 O  O   . HOH AA .   ? 0.3349 0.4368 0.3791 0.0584  0.0026  -0.0389 673 HOH A O   
8985 O  O   . HOH AA .   ? 0.5538 0.3365 0.7314 0.1433  0.0670  -0.0574 674 HOH A O   
8986 O  O   . HOH AA .   ? 0.6029 0.3540 0.4317 0.0323  -0.0399 0.0749  675 HOH A O   
8987 O  O   . HOH AA .   ? 0.3083 0.2815 0.5501 0.0033  0.0658  0.0842  676 HOH A O   
8988 O  O   . HOH AA .   ? 0.4277 0.4284 0.3869 0.0055  0.0075  0.0876  677 HOH A O   
8989 O  O   . HOH AA .   ? 0.7876 0.4676 0.2909 0.0333  0.0834  0.0869  678 HOH A O   
8990 O  O   . HOH AA .   ? 0.4827 0.3817 0.2823 -0.1366 0.0042  0.0669  679 HOH A O   
8991 O  O   . HOH AA .   ? 0.5999 0.3416 0.7180 -0.1228 0.0427  -0.0813 680 HOH A O   
8992 O  O   . HOH AA .   ? 0.7170 0.8053 0.3326 -0.0882 0.1534  -0.1229 681 HOH A O   
8993 O  O   . HOH AA .   ? 0.7113 0.3905 0.5636 0.1537  -0.0491 -0.0625 682 HOH A O   
8994 O  O   . HOH AA .   ? 0.4230 0.3523 0.2741 -0.0234 0.1013  0.0653  683 HOH A O   
8995 O  O   . HOH AA .   ? 0.3825 0.5998 0.2360 0.0795  0.0707  0.0451  684 HOH A O   
8996 O  O   . HOH BA .   ? 0.3632 0.2181 0.4692 -0.0201 0.0259  0.0754  401 HOH B O   
8997 O  O   . HOH BA .   ? 0.2236 0.4828 0.4014 -0.0827 -0.1049 0.0990  402 HOH B O   
8998 O  O   . HOH BA .   ? 0.7012 0.3467 0.3315 -0.0315 0.0888  -0.0061 403 HOH B O   
8999 O  O   . HOH BA .   ? 0.2555 0.1949 0.2262 -0.0359 -0.0135 0.0182  404 HOH B O   
9000 O  O   . HOH BA .   ? 0.3790 0.7295 0.3986 -0.2467 0.1676  -0.2170 405 HOH B O   
9001 O  O   . HOH BA .   ? 0.3994 0.2802 0.5277 -0.1174 0.0839  -0.0128 406 HOH B O   
9002 O  O   . HOH BA .   ? 0.3138 0.4393 0.4567 -0.0891 -0.0528 0.0917  407 HOH B O   
9003 O  O   . HOH BA .   ? 0.3561 0.2676 0.3633 -0.0722 -0.1194 0.0447  408 HOH B O   
9004 O  O   . HOH BA .   ? 0.5155 0.4887 0.5753 0.1113  -0.1514 -0.1128 409 HOH B O   
9005 O  O   . HOH BA .   ? 0.2629 0.8698 0.5067 -0.0087 0.0111  0.1298  410 HOH B O   
9006 O  O   . HOH BA .   ? 0.9733 0.2395 0.6258 -0.0812 0.0019  0.1763  411 HOH B O   
9007 O  O   . HOH BA .   ? 0.3378 0.4422 0.3773 -0.0574 -0.0788 -0.0033 412 HOH B O   
9008 O  O   . HOH BA .   ? 0.2309 0.3019 0.4425 0.1045  0.0737  0.0995  413 HOH B O   
9009 O  O   . HOH BA .   ? 0.2455 0.2362 0.2955 -0.0631 0.0535  -0.0293 414 HOH B O   
9010 O  O   . HOH BA .   ? 0.2952 0.4120 0.3129 0.0000  -0.0292 0.0343  415 HOH B O   
9011 O  O   . HOH BA .   ? 0.4237 0.6585 0.5264 0.0886  -0.0657 -0.0945 416 HOH B O   
9012 O  O   . HOH BA .   ? 0.1371 0.1312 0.1529 0.0013  0.0110  0.0155  417 HOH B O   
9013 O  O   . HOH BA .   ? 0.4854 0.2896 0.2998 -0.0837 0.0070  0.0149  418 HOH B O   
9014 O  O   . HOH BA .   ? 0.4521 0.3406 0.6944 0.1500  0.1735  0.0296  419 HOH B O   
9015 O  O   . HOH BA .   ? 0.5730 0.2794 0.3356 -0.1358 -0.0894 -0.0149 420 HOH B O   
9016 O  O   . HOH BA .   ? 0.5134 0.6442 0.3867 -0.0925 0.0527  0.1149  421 HOH B O   
9017 O  O   . HOH BA .   ? 0.5080 0.4066 0.1762 0.2414  0.0351  0.0321  422 HOH B O   
9018 O  O   . HOH BA .   ? 0.4335 0.2451 0.2597 -0.0530 0.0362  0.0098  423 HOH B O   
9019 O  O   . HOH BA .   ? 0.2518 0.2674 0.2755 -0.0697 -0.0336 0.0451  424 HOH B O   
9020 O  O   . HOH BA .   ? 0.3519 0.3704 0.3676 -0.0336 0.0768  0.0756  425 HOH B O   
9021 O  O   . HOH BA .   ? 0.2736 0.4036 0.2409 0.0688  0.0022  0.0456  426 HOH B O   
9022 O  O   . HOH BA .   ? 0.1869 0.2112 0.2798 0.0070  0.0523  0.0263  427 HOH B O   
9023 O  O   . HOH BA .   ? 0.2558 0.2303 0.4598 -0.0515 -0.0015 0.0780  428 HOH B O   
9024 O  O   . HOH BA .   ? 0.3901 0.6348 0.5243 0.1920  -0.1646 -0.2088 429 HOH B O   
9025 O  O   . HOH BA .   ? 0.1583 0.2369 0.3211 0.0189  -0.0102 -0.0302 430 HOH B O   
9026 O  O   . HOH BA .   ? 0.1877 0.1788 0.2490 0.0041  -0.0077 0.0285  431 HOH B O   
9027 O  O   . HOH BA .   ? 0.1328 0.1281 0.1473 0.0275  0.0065  0.0261  432 HOH B O   
9028 O  O   . HOH BA .   ? 0.6662 1.0130 0.2699 -0.3385 0.3768  -0.0141 433 HOH B O   
9029 O  O   . HOH BA .   ? 0.4343 0.3457 0.3529 -0.0013 0.0457  0.0157  434 HOH B O   
9030 O  O   . HOH BA .   ? 0.4254 0.5285 0.5090 -0.0134 -0.2174 -0.0229 435 HOH B O   
9031 O  O   . HOH BA .   ? 0.1848 0.1300 0.1755 -0.0141 -0.0142 0.0207  436 HOH B O   
9032 O  O   . HOH BA .   ? 0.2715 0.4722 0.3343 0.0444  0.0804  -0.0469 437 HOH B O   
9033 O  O   . HOH BA .   ? 0.4708 0.3554 0.3961 -0.0251 0.0779  0.0578  438 HOH B O   
9034 O  O   . HOH BA .   ? 0.3958 0.3862 0.4976 -0.0258 0.0827  -0.0221 439 HOH B O   
9035 O  O   . HOH BA .   ? 0.9544 0.3893 0.4973 -0.2828 -0.1028 0.1940  440 HOH B O   
9036 O  O   . HOH BA .   ? 0.4317 0.2808 0.3744 0.0427  -0.0480 -0.0059 441 HOH B O   
9037 O  O   . HOH BA .   ? 0.3028 0.2157 0.2440 -0.0040 0.0285  -0.0357 442 HOH B O   
9038 O  O   . HOH BA .   ? 0.5782 0.2206 0.2597 0.0719  0.0483  -0.0234 443 HOH B O   
9039 O  O   . HOH BA .   ? 0.3620 0.5424 0.2840 0.0228  -0.0111 -0.0161 444 HOH B O   
9040 O  O   . HOH BA .   ? 0.3455 0.3088 0.4931 0.0320  -0.0162 -0.1091 445 HOH B O   
9041 O  O   . HOH BA .   ? 0.3520 0.2149 0.2834 -0.0163 -0.0383 0.0037  446 HOH B O   
9042 O  O   . HOH BA .   ? 0.4970 0.3406 0.3010 0.1087  0.0073  -0.0311 447 HOH B O   
9043 O  O   . HOH BA .   ? 0.1829 0.2219 0.2763 0.0236  -0.0263 -0.0086 448 HOH B O   
9044 O  O   . HOH BA .   ? 0.1430 0.1604 0.1702 0.0026  -0.0062 0.0051  449 HOH B O   
9045 O  O   . HOH BA .   ? 0.1374 0.1172 0.1939 -0.0021 -0.0253 -0.0065 450 HOH B O   
9046 O  O   . HOH BA .   ? 0.3149 0.3102 0.4041 -0.1244 0.0335  -0.0485 451 HOH B O   
9047 O  O   . HOH BA .   ? 0.4980 0.3850 0.3797 -0.1802 -0.0196 -0.0556 452 HOH B O   
9048 O  O   . HOH BA .   ? 0.3300 0.3339 0.3545 0.0445  -0.0010 0.0834  453 HOH B O   
9049 O  O   . HOH BA .   ? 0.3097 0.3416 0.4041 -0.0400 0.0109  -0.0032 454 HOH B O   
9050 O  O   . HOH BA .   ? 0.3334 0.3202 0.2846 0.0184  0.0290  0.0662  455 HOH B O   
9051 O  O   . HOH BA .   ? 0.3347 0.2685 0.2465 0.0640  -0.1072 0.0137  456 HOH B O   
9052 O  O   . HOH BA .   ? 0.2064 0.3265 0.3415 -0.0383 -0.0236 -0.0364 457 HOH B O   
9053 O  O   . HOH BA .   ? 0.2869 0.7302 0.4114 0.0505  -0.0236 0.0000  458 HOH B O   
9054 O  O   . HOH BA .   ? 0.3080 0.2284 0.2303 0.0418  -0.0845 -0.0215 459 HOH B O   
9055 O  O   . HOH BA .   ? 0.2721 0.2563 0.2260 -0.0297 0.0068  -0.0107 460 HOH B O   
9056 O  O   . HOH BA .   ? 0.4077 0.3449 0.9250 -0.0612 -0.1364 0.2206  461 HOH B O   
9057 O  O   . HOH BA .   ? 0.5585 0.4220 0.2813 -0.1114 -0.0366 0.1020  462 HOH B O   
9058 O  O   . HOH BA .   ? 0.4726 0.4144 0.4362 -0.0174 0.0449  0.0611  463 HOH B O   
9059 O  O   . HOH BA .   ? 0.2297 0.3118 0.2236 0.0232  0.0207  0.0502  464 HOH B O   
9060 O  O   . HOH BA .   ? 0.3384 0.1664 0.4234 -0.0535 -0.1014 0.0736  465 HOH B O   
9061 O  O   . HOH BA .   ? 0.2842 0.2739 0.2868 -0.0337 -0.0030 0.0460  466 HOH B O   
9062 O  O   . HOH BA .   ? 0.2074 0.1464 0.1634 -0.0220 0.0279  0.0065  467 HOH B O   
9063 O  O   . HOH BA .   ? 0.8965 0.3811 0.3777 -0.0443 -0.0504 0.0988  468 HOH B O   
9064 O  O   . HOH BA .   ? 0.2720 0.2440 0.1915 0.0032  -0.0647 -0.0451 469 HOH B O   
9065 O  O   . HOH BA .   ? 0.1482 0.1401 0.2925 -0.0130 -0.0135 0.0035  470 HOH B O   
9066 O  O   . HOH BA .   ? 0.4797 0.2725 0.2730 -0.1476 0.0752  -0.0419 471 HOH B O   
9067 O  O   . HOH BA .   ? 0.1773 0.2944 0.4203 -0.0082 0.0223  0.0225  472 HOH B O   
9068 O  O   . HOH BA .   ? 0.4209 0.3600 0.2992 0.1112  0.0741  0.0013  473 HOH B O   
9069 O  O   . HOH BA .   ? 0.1839 0.3342 0.2528 0.0239  0.0182  0.0329  474 HOH B O   
9070 O  O   . HOH BA .   ? 0.2852 0.2075 0.3427 -0.0403 0.0104  -0.0494 475 HOH B O   
9071 O  O   . HOH BA .   ? 0.2225 0.2889 0.2425 0.0731  0.0212  0.0296  476 HOH B O   
9072 O  O   . HOH BA .   ? 0.3714 0.2908 0.3802 0.0210  0.0092  -0.0401 477 HOH B O   
9073 O  O   . HOH BA .   ? 0.1893 0.2074 0.2364 -0.0311 0.0040  0.0288  478 HOH B O   
9074 O  O   . HOH BA .   ? 0.4072 0.7569 0.5478 0.0854  -0.0097 -0.2468 479 HOH B O   
9075 O  O   . HOH BA .   ? 0.1552 0.1976 0.1831 -0.0230 -0.0075 0.0274  480 HOH B O   
9076 O  O   . HOH BA .   ? 0.2101 0.2221 0.2606 0.0255  -0.0444 0.0212  481 HOH B O   
9077 O  O   . HOH BA .   ? 0.4656 0.5775 0.2622 0.0199  -0.0317 0.1917  482 HOH B O   
9078 O  O   . HOH BA .   ? 0.1876 0.1166 0.2132 0.0381  0.0124  0.0027  483 HOH B O   
9079 O  O   . HOH BA .   ? 0.3677 0.2965 0.5382 0.0695  0.0208  -0.0752 484 HOH B O   
9080 O  O   . HOH BA .   ? 0.2133 0.2180 0.2744 0.0595  -0.0043 0.0320  485 HOH B O   
9081 O  O   . HOH BA .   ? 0.2333 0.1460 0.1922 -0.0159 0.0095  0.0609  486 HOH B O   
9082 O  O   . HOH BA .   ? 0.6788 0.5306 0.3309 0.1149  -0.1477 0.0823  487 HOH B O   
9083 O  O   . HOH BA .   ? 0.3942 0.2379 0.2657 -0.0126 -0.0620 0.0040  488 HOH B O   
9084 O  O   . HOH BA .   ? 0.6125 0.6711 0.1841 -0.1284 0.0270  0.0271  489 HOH B O   
9085 O  O   . HOH BA .   ? 0.3195 0.3044 0.3604 0.0126  0.0941  -0.0476 490 HOH B O   
9086 O  O   . HOH BA .   ? 0.5125 0.6809 0.5391 0.1089  -0.1560 0.0624  491 HOH B O   
9087 O  O   . HOH BA .   ? 0.1925 0.1146 0.2147 -0.0118 -0.0222 -0.0054 492 HOH B O   
9088 O  O   . HOH BA .   ? 0.2591 0.2053 0.2422 0.0452  -0.0293 0.0339  493 HOH B O   
9089 O  O   . HOH BA .   ? 0.1249 0.1121 0.1762 0.0034  0.0111  0.0189  494 HOH B O   
9090 O  O   . HOH BA .   ? 0.3598 0.2761 0.3928 -0.0639 0.0208  -0.0430 495 HOH B O   
9091 O  O   . HOH BA .   ? 0.1668 0.2121 0.2414 -0.0208 0.0237  0.0433  496 HOH B O   
9092 O  O   . HOH BA .   ? 0.3914 0.4093 0.2924 0.0494  0.0387  -0.1100 497 HOH B O   
9093 O  O   . HOH BA .   ? 0.4128 0.7097 0.6965 -0.1419 0.0717  -0.0148 498 HOH B O   
9094 O  O   . HOH BA .   ? 0.3265 0.3359 0.3876 -0.0174 0.1059  0.0833  499 HOH B O   
9095 O  O   . HOH BA .   ? 0.3142 0.1824 0.6528 -0.0409 0.1020  -0.1008 500 HOH B O   
9096 O  O   . HOH BA .   ? 0.2965 0.1746 0.2429 0.0027  0.0796  0.0155  501 HOH B O   
9097 O  O   . HOH BA .   ? 0.1898 0.1757 0.1898 0.0190  0.0164  0.0117  502 HOH B O   
9098 O  O   . HOH BA .   ? 0.3626 0.2916 0.4424 -0.0240 0.0113  0.0256  503 HOH B O   
9099 O  O   . HOH BA .   ? 0.6682 0.3766 0.3140 0.1276  -0.0688 0.0100  504 HOH B O   
9100 O  O   . HOH BA .   ? 0.4684 0.4062 0.6590 0.1617  0.2114  0.2922  505 HOH B O   
9101 O  O   . HOH BA .   ? 0.1455 0.0958 0.2070 -0.0012 -0.0139 0.0222  506 HOH B O   
9102 O  O   . HOH BA .   ? 0.1279 0.1259 0.1855 0.0087  -0.0127 0.0204  507 HOH B O   
9103 O  O   . HOH BA .   ? 0.4563 0.2922 0.7016 0.0605  0.0286  -0.1319 508 HOH B O   
9104 O  O   . HOH BA .   ? 0.1437 0.1136 0.1283 -0.0004 0.0159  0.0198  509 HOH B O   
9105 O  O   . HOH BA .   ? 0.3565 0.2991 0.3925 -0.0315 -0.1307 0.0387  510 HOH B O   
9106 O  O   . HOH BA .   ? 0.5962 0.4262 0.5317 -0.0325 -0.1073 -0.0399 511 HOH B O   
9107 O  O   . HOH BA .   ? 0.3161 0.2597 0.2863 0.0031  0.0004  0.0155  512 HOH B O   
9108 O  O   . HOH BA .   ? 0.3121 0.2499 0.1483 0.0151  0.0223  0.0170  513 HOH B O   
9109 O  O   . HOH BA .   ? 0.2257 0.1819 0.3074 -0.0167 0.0497  -0.0199 514 HOH B O   
9110 O  O   . HOH BA .   ? 0.4757 0.6372 0.2451 -0.1101 0.0020  0.0130  515 HOH B O   
9111 O  O   . HOH BA .   ? 0.1136 0.1003 0.1699 0.0016  -0.0083 0.0131  516 HOH B O   
9112 O  O   . HOH BA .   ? 0.1751 0.2245 0.2151 0.0139  0.0333  0.0255  517 HOH B O   
9113 O  O   . HOH BA .   ? 0.2846 0.3051 0.2528 -0.0016 0.0573  -0.0308 518 HOH B O   
9114 O  O   . HOH BA .   ? 0.4596 0.3292 0.3457 0.0995  0.0005  -0.0260 519 HOH B O   
9115 O  O   . HOH BA .   ? 0.5199 0.2152 0.7188 -0.0086 0.0345  -0.0523 520 HOH B O   
9116 O  O   . HOH BA .   ? 0.4251 0.3350 0.4795 -0.0228 -0.0225 -0.0346 521 HOH B O   
9117 O  O   . HOH BA .   ? 0.3995 0.3106 0.4392 0.0072  -0.1145 -0.0335 522 HOH B O   
9118 O  O   . HOH BA .   ? 0.4397 0.2081 0.2842 -0.0614 0.0037  -0.0674 523 HOH B O   
9119 O  O   . HOH BA .   ? 0.3802 0.3096 0.4517 0.0264  0.0601  -0.0163 524 HOH B O   
9120 O  O   . HOH BA .   ? 0.5558 0.5370 0.3960 0.0740  0.1458  -0.0389 525 HOH B O   
9121 O  O   . HOH BA .   ? 0.3901 0.3875 0.2733 -0.0450 0.0115  0.0871  526 HOH B O   
9122 O  O   . HOH BA .   ? 0.2847 0.1962 0.3068 -0.0071 0.0694  -0.0167 527 HOH B O   
9123 O  O   . HOH BA .   ? 0.3463 0.5807 0.2004 -0.0133 -0.0469 -0.0355 528 HOH B O   
9124 O  O   . HOH BA .   ? 0.5743 0.3334 0.4173 0.0416  0.0647  0.0480  529 HOH B O   
9125 O  O   . HOH BA .   ? 0.2892 0.2700 0.3384 -0.0086 0.0119  -0.0591 530 HOH B O   
9126 O  O   . HOH BA .   ? 0.2653 0.2003 0.2748 -0.0010 0.0772  -0.0027 531 HOH B O   
9127 O  O   . HOH BA .   ? 0.3259 0.1870 0.2710 -0.0631 -0.0668 0.0529  532 HOH B O   
9128 O  O   . HOH BA .   ? 0.2919 0.5611 0.4447 -0.0766 0.0928  0.1259  533 HOH B O   
9129 O  O   . HOH BA .   ? 0.2262 0.1698 0.1824 -0.0184 -0.0159 -0.0047 534 HOH B O   
9130 O  O   . HOH BA .   ? 0.3440 0.2864 0.6922 -0.0673 0.0251  -0.1512 535 HOH B O   
9131 O  O   . HOH BA .   ? 0.4039 0.3355 0.1807 -0.0089 -0.0615 0.0595  536 HOH B O   
9132 O  O   . HOH BA .   ? 0.1900 0.2587 0.2534 0.0179  0.0022  -0.0118 537 HOH B O   
9133 O  O   . HOH BA .   ? 0.6758 0.3319 0.4712 0.1092  0.2344  0.1046  538 HOH B O   
9134 O  O   . HOH BA .   ? 0.2799 0.2188 0.3252 0.0320  -0.0261 0.0188  539 HOH B O   
9135 O  O   . HOH BA .   ? 0.3063 0.3426 0.2098 0.0695  -0.0228 -0.0692 540 HOH B O   
9136 O  O   . HOH BA .   ? 0.3163 0.3579 0.4494 -0.1225 0.1336  -0.0718 541 HOH B O   
9137 O  O   . HOH BA .   ? 0.5820 0.3722 0.3039 -0.0778 0.0288  -0.0851 542 HOH B O   
9138 O  O   . HOH BA .   ? 0.3130 0.3790 0.6966 -0.0049 -0.1975 0.1099  543 HOH B O   
9139 O  O   . HOH BA .   ? 0.1736 0.2298 0.2945 -0.0566 0.0195  -0.0428 544 HOH B O   
9140 O  O   . HOH BA .   ? 0.6524 0.4926 0.3283 -0.3017 -0.0612 0.0523  545 HOH B O   
9141 O  O   . HOH BA .   ? 0.1408 0.1458 0.1636 -0.0137 -0.0003 0.0097  546 HOH B O   
9142 O  O   . HOH BA .   ? 0.4045 0.4724 0.4030 0.1395  0.0672  0.0671  547 HOH B O   
9143 O  O   . HOH BA .   ? 0.5270 0.5630 0.3389 -0.2167 -0.0703 0.0022  548 HOH B O   
9144 O  O   . HOH BA .   ? 0.4234 0.3034 0.3153 0.0143  0.0102  0.0004  549 HOH B O   
9145 O  O   . HOH BA .   ? 0.4375 0.5608 0.3524 -0.1963 0.0190  -0.0527 550 HOH B O   
9146 O  O   . HOH BA .   ? 0.3978 0.2564 0.2706 -0.0097 -0.0364 0.0374  551 HOH B O   
9147 O  O   . HOH BA .   ? 0.1414 0.1615 0.1670 -0.0159 0.0116  0.0352  552 HOH B O   
9148 O  O   . HOH BA .   ? 0.3579 0.5284 0.4940 0.2216  0.0219  0.0889  553 HOH B O   
9149 O  O   . HOH BA .   ? 0.1967 0.1341 0.3297 -0.0080 -0.0861 0.0144  554 HOH B O   
9150 O  O   . HOH BA .   ? 0.3231 0.4485 0.6950 0.1747  0.2286  0.2160  555 HOH B O   
9151 O  O   . HOH BA .   ? 0.2116 0.3506 0.3567 0.0898  0.0428  0.1766  556 HOH B O   
9152 O  O   . HOH BA .   ? 0.1373 0.1575 0.2007 -0.0126 -0.0162 0.0168  557 HOH B O   
9153 O  O   . HOH BA .   ? 0.3116 0.3633 0.3177 -0.1187 -0.0851 0.0493  558 HOH B O   
9154 O  O   . HOH BA .   ? 0.2364 0.5197 0.3428 -0.1568 0.1270  -0.1179 559 HOH B O   
9155 O  O   . HOH BA .   ? 0.4258 0.2565 0.2273 -0.1621 -0.0515 0.0249  560 HOH B O   
9156 O  O   . HOH BA .   ? 0.3234 0.3262 0.4557 -0.0952 0.1008  0.0552  561 HOH B O   
9157 O  O   . HOH BA .   ? 0.4691 0.3794 0.3856 -0.0049 -0.0304 0.0634  562 HOH B O   
9158 O  O   . HOH BA .   ? 0.5134 0.3067 0.2087 0.0185  0.0186  -0.0617 563 HOH B O   
9159 O  O   . HOH BA .   ? 0.3656 0.2813 0.2382 -0.0370 -0.1520 0.0535  564 HOH B O   
9160 O  O   . HOH BA .   ? 0.4201 1.0096 0.4640 -0.1571 -0.0286 0.4632  565 HOH B O   
9161 O  O   . HOH BA .   ? 0.3808 0.3348 0.7228 -0.0025 0.1377  0.1751  566 HOH B O   
9162 O  O   . HOH BA .   ? 0.2629 0.1683 0.2385 0.0127  0.0454  -0.0164 567 HOH B O   
9163 O  O   . HOH BA .   ? 0.3184 0.2632 0.4223 -0.0242 -0.0149 0.0649  568 HOH B O   
9164 O  O   . HOH BA .   ? 0.3000 0.4325 0.4349 -0.0375 -0.0348 0.1324  569 HOH B O   
9165 O  O   . HOH BA .   ? 0.3506 0.2628 0.3160 -0.0348 -0.0196 0.0866  570 HOH B O   
9166 O  O   . HOH BA .   ? 0.4391 0.3143 0.4354 -0.0204 0.0392  -0.0279 571 HOH B O   
9167 O  O   . HOH BA .   ? 0.2714 0.3034 0.3225 0.0871  -0.0390 -0.0303 572 HOH B O   
9168 O  O   . HOH BA .   ? 0.2576 0.3476 0.2866 0.1028  0.0453  0.0406  573 HOH B O   
9169 O  O   . HOH BA .   ? 0.6912 0.2613 0.4977 0.1417  0.1988  0.0378  574 HOH B O   
9170 O  O   . HOH BA .   ? 0.1956 0.2622 0.2741 0.0087  -0.0034 -0.0413 575 HOH B O   
9171 O  O   . HOH BA .   ? 0.2532 0.3385 0.4351 0.0124  -0.0139 0.0605  576 HOH B O   
9172 O  O   . HOH BA .   ? 0.3643 0.3228 0.4444 -0.1233 -0.0408 0.0716  577 HOH B O   
9173 O  O   . HOH BA .   ? 0.4331 0.4586 0.4702 -0.0012 0.0930  -0.1176 578 HOH B O   
9174 O  O   . HOH BA .   ? 0.3195 0.2407 0.3658 -0.0560 -0.0806 0.0680  579 HOH B O   
9175 O  O   . HOH BA .   ? 0.3116 0.3402 0.2028 0.0624  0.0195  0.0254  580 HOH B O   
9176 O  O   . HOH BA .   ? 0.3086 0.2693 0.3103 -0.0800 0.0205  0.0545  581 HOH B O   
9177 O  O   . HOH BA .   ? 0.2540 0.2511 0.3970 0.0153  0.0981  -0.0184 582 HOH B O   
9178 O  O   . HOH BA .   ? 0.5195 0.4585 0.3714 0.0587  -0.0759 -0.1291 583 HOH B O   
9179 O  O   . HOH BA .   ? 0.3319 0.7113 0.1661 -0.0288 -0.0669 -0.0092 584 HOH B O   
9180 O  O   . HOH BA .   ? 0.3723 0.6084 0.4686 -0.2478 0.0178  0.0308  585 HOH B O   
9181 O  O   . HOH BA .   ? 0.5044 0.3336 0.3055 0.0603  -0.0377 -0.0583 586 HOH B O   
9182 O  O   . HOH BA .   ? 0.2647 0.5410 0.3827 0.0471  0.0284  -0.0129 587 HOH B O   
9183 O  O   . HOH BA .   ? 0.3007 0.7975 0.4030 -0.1819 -0.0133 -0.2366 588 HOH B O   
9184 O  O   . HOH BA .   ? 0.3222 0.7941 0.3698 0.0317  -0.1198 -0.1038 589 HOH B O   
9185 O  O   . HOH BA .   ? 0.2201 0.2269 0.2781 0.0036  0.0185  0.0239  590 HOH B O   
9186 O  O   . HOH BA .   ? 0.3794 0.3995 0.2843 0.0310  -0.1093 0.0070  591 HOH B O   
9187 O  O   . HOH BA .   ? 0.2499 0.3940 0.4778 -0.0025 -0.0087 0.1328  592 HOH B O   
9188 O  O   . HOH BA .   ? 0.2764 0.3622 0.3637 -0.1153 0.0522  0.0148  593 HOH B O   
9189 O  O   . HOH BA .   ? 0.2326 0.2902 0.2576 0.0203  0.0165  -0.0118 594 HOH B O   
9190 O  O   . HOH BA .   ? 0.4074 0.4563 0.3547 -0.0683 0.0347  -0.0784 595 HOH B O   
9191 O  O   . HOH BA .   ? 0.4867 0.3693 0.3669 0.0819  -0.0914 -0.0300 596 HOH B O   
9192 O  O   . HOH BA .   ? 0.2834 0.4581 0.4787 -0.0506 -0.0085 -0.0960 597 HOH B O   
9193 O  O   . HOH BA .   ? 0.2129 0.1719 0.2518 -0.0223 -0.0171 -0.0141 598 HOH B O   
9194 O  O   . HOH BA .   ? 0.4930 0.3062 0.3611 -0.0254 -0.1620 0.0418  599 HOH B O   
9195 O  O   . HOH BA .   ? 0.2021 0.3989 0.4109 -0.0334 0.0807  0.0359  600 HOH B O   
9196 O  O   . HOH BA .   ? 0.4022 0.3010 0.6032 -0.0531 0.1114  -0.1825 601 HOH B O   
9197 O  O   . HOH BA .   ? 0.5612 0.4988 0.3959 0.1087  -0.1388 0.1460  602 HOH B O   
9198 O  O   . HOH BA .   ? 0.4064 0.6518 0.4038 0.1954  -0.0647 -0.1362 603 HOH B O   
9199 O  O   . HOH BA .   ? 0.4387 0.2876 0.7210 -0.0194 -0.0304 0.0806  604 HOH B O   
9200 O  O   . HOH BA .   ? 0.5187 0.7047 0.8628 0.1639  -0.2998 -0.1772 605 HOH B O   
9201 O  O   . HOH BA .   ? 0.4177 0.3288 0.4740 0.0428  -0.0289 0.0263  606 HOH B O   
9202 O  O   . HOH BA .   ? 0.4029 0.2595 0.2559 -0.0166 0.0370  0.0403  607 HOH B O   
9203 O  O   . HOH BA .   ? 0.3084 0.5582 0.2360 -0.1321 -0.0458 0.0532  608 HOH B O   
9204 O  O   . HOH BA .   ? 0.7799 0.3209 0.3884 0.1949  0.1875  0.0802  609 HOH B O   
9205 O  O   . HOH BA .   ? 0.7859 0.5572 0.3765 -0.3065 0.1848  0.0065  610 HOH B O   
9206 O  O   . HOH BA .   ? 0.6077 0.5144 0.6221 -0.1091 -0.0791 -0.1456 611 HOH B O   
9207 O  O   . HOH BA .   ? 0.4148 0.3993 0.4692 -0.0606 -0.1650 0.0034  612 HOH B O   
9208 O  O   . HOH BA .   ? 0.5328 0.4670 0.3070 0.0413  0.0006  0.1644  613 HOH B O   
9209 O  O   . HOH BA .   ? 0.5270 0.5892 0.5636 -0.0706 0.0780  0.0172  614 HOH B O   
9210 O  O   . HOH BA .   ? 0.5184 0.8608 0.2901 0.0126  0.0063  -0.0252 615 HOH B O   
9211 O  O   . HOH BA .   ? 0.6873 0.2517 0.3121 0.0195  -0.0900 -0.0573 616 HOH B O   
9212 O  O   . HOH BA .   ? 0.7985 0.4841 0.6548 -0.2090 0.2726  -0.1018 617 HOH B O   
9213 O  O   . HOH BA .   ? 0.4209 0.5435 0.3599 0.1050  0.0153  0.2144  618 HOH B O   
9214 O  O   . HOH BA .   ? 0.4037 0.3520 0.3376 -0.1429 0.0216  0.0520  619 HOH B O   
9215 O  O   . HOH BA .   ? 0.4843 0.5177 0.2724 0.0839  -0.0465 0.0536  620 HOH B O   
9216 O  O   . HOH BA .   ? 0.5971 0.7173 0.6126 0.2337  -0.0784 0.0657  621 HOH B O   
9217 O  O   . HOH BA .   ? 0.3506 0.3362 0.3083 0.0695  -0.0342 0.0502  622 HOH B O   
9218 O  O   . HOH BA .   ? 0.4376 0.2351 0.8984 0.0355  0.0696  0.2688  623 HOH B O   
9219 O  O   . HOH BA .   ? 0.4351 0.4187 0.9154 0.1405  -0.1126 -0.0664 624 HOH B O   
9220 O  O   . HOH BA .   ? 0.7967 0.4043 0.3894 -0.0644 0.0669  0.0251  625 HOH B O   
9221 O  O   . HOH BA .   ? 0.4041 0.4575 0.4270 0.0150  -0.0387 0.1276  626 HOH B O   
9222 O  O   . HOH BA .   ? 0.5314 0.4218 0.5631 0.1398  -0.0317 -0.2379 627 HOH B O   
9223 O  O   . HOH BA .   ? 0.5842 0.4159 0.3538 0.0851  0.0877  -0.0421 628 HOH B O   
9224 O  O   . HOH BA .   ? 0.5000 0.3811 0.3294 0.1014  -0.0273 0.0318  629 HOH B O   
9225 O  O   . HOH BA .   ? 0.5457 0.3262 0.4218 0.0914  -0.0787 0.0214  630 HOH B O   
9226 O  O   . HOH BA .   ? 0.4586 0.5404 0.4565 -0.0008 -0.0908 0.0032  631 HOH B O   
9227 O  O   . HOH BA .   ? 0.2878 0.4179 0.3125 0.0673  0.0498  0.0307  632 HOH B O   
9228 O  O   . HOH BA .   ? 0.2078 0.3546 0.5910 -0.0135 0.0181  0.0986  633 HOH B O   
9229 O  O   . HOH BA .   ? 0.2015 0.2294 0.2568 0.0153  -0.0097 0.0290  634 HOH B O   
9230 O  O   . HOH BA .   ? 0.3001 0.3198 0.2755 0.0080  0.0444  0.0479  635 HOH B O   
9231 O  O   . HOH BA .   ? 0.2724 0.3653 0.3634 -0.0201 -0.0394 0.0236  636 HOH B O   
9232 O  O   . HOH BA .   ? 0.4151 0.2572 0.3856 -0.0458 0.0039  0.0536  637 HOH B O   
9233 O  O   . HOH BA .   ? 0.4451 0.5134 0.5094 0.1375  -0.0342 -0.1133 638 HOH B O   
9234 O  O   . HOH BA .   ? 0.2929 0.5414 0.4579 -0.0309 0.0647  -0.0658 639 HOH B O   
9235 O  O   . HOH BA .   ? 0.5219 0.4908 0.4211 0.0370  -0.0058 0.0606  640 HOH B O   
9236 O  O   . HOH BA .   ? 0.4632 0.5280 0.6767 0.0406  -0.1395 -0.1453 641 HOH B O   
9237 O  O   . HOH BA .   ? 0.4265 0.2863 0.7203 0.0779  0.1278  0.1074  642 HOH B O   
9238 O  O   . HOH BA .   ? 0.4680 0.3267 0.2948 0.0501  0.1119  0.0077  643 HOH B O   
9239 O  O   . HOH BA .   ? 0.3759 0.4028 0.2407 0.0162  0.0334  0.0003  644 HOH B O   
9240 O  O   . HOH BA .   ? 0.4787 0.3044 0.5773 0.0688  0.0690  -0.0199 645 HOH B O   
9241 O  O   . HOH BA .   ? 0.5603 0.6449 0.4771 -0.1093 -0.0315 0.2775  646 HOH B O   
9242 O  O   . HOH BA .   ? 0.2070 0.3139 0.2610 0.0219  0.0161  0.0158  647 HOH B O   
9243 O  O   . HOH BA .   ? 0.7425 0.3479 0.3894 0.0925  -0.1733 -0.0237 648 HOH B O   
9244 O  O   . HOH BA .   ? 0.4401 0.3599 0.3242 0.0138  0.0027  0.0732  649 HOH B O   
9245 O  O   . HOH BA .   ? 0.4678 0.4725 0.4032 -0.0176 0.0127  0.0040  650 HOH B O   
9246 O  O   . HOH BA .   ? 0.4621 0.4532 0.3317 0.0102  0.0763  0.0125  651 HOH B O   
9247 O  O   . HOH BA .   ? 0.1973 0.3307 0.3351 0.0245  -0.0296 0.0607  652 HOH B O   
9248 O  O   . HOH BA .   ? 0.4683 0.4620 0.4075 0.0218  -0.0634 -0.1105 653 HOH B O   
9249 O  O   . HOH BA .   ? 0.3893 0.2974 0.3353 -0.0321 -0.0239 0.0881  654 HOH B O   
9250 O  O   . HOH BA .   ? 0.3606 0.2549 0.3163 0.0428  0.1091  0.0635  655 HOH B O   
9251 O  O   . HOH BA .   ? 0.3952 0.5633 0.4640 0.1189  0.0270  0.1419  656 HOH B O   
9252 O  O   . HOH BA .   ? 0.4064 0.4639 0.4365 -0.0304 0.1632  0.0747  657 HOH B O   
9253 O  O   . HOH BA .   ? 0.5554 0.3272 0.5745 -0.1018 0.0787  -0.1495 658 HOH B O   
9254 O  O   . HOH BA .   ? 0.3529 0.3553 0.3456 0.1180  -0.0603 -0.0374 659 HOH B O   
9255 O  O   . HOH BA .   ? 0.4716 0.3120 0.4546 -0.0023 0.0365  -0.0444 660 HOH B O   
9256 O  O   . HOH BA .   ? 0.4002 0.2402 0.4129 -0.0586 -0.0502 -0.0133 661 HOH B O   
9257 O  O   . HOH BA .   ? 0.4744 0.3729 0.4946 0.1172  0.0614  0.1060  662 HOH B O   
9258 O  O   . HOH BA .   ? 0.5223 0.2048 0.7036 0.1010  -0.0903 0.0204  663 HOH B O   
9259 O  O   . HOH BA .   ? 0.3578 0.3722 0.2834 0.0490  -0.0814 0.0557  664 HOH B O   
9260 O  O   . HOH BA .   ? 0.3285 0.4308 0.4987 0.0908  -0.0666 -0.0118 665 HOH B O   
9261 O  O   . HOH BA .   ? 0.3625 0.6585 0.4269 -0.0775 0.0263  0.1995  666 HOH B O   
9262 O  O   . HOH BA .   ? 0.4722 0.2751 0.7988 -0.0573 -0.0895 -0.0460 667 HOH B O   
9263 O  O   . HOH BA .   ? 0.7429 0.2708 0.5464 -0.2297 -0.0285 0.1060  668 HOH B O   
9264 O  O   . HOH BA .   ? 0.7352 0.2494 0.3983 0.1105  0.0036  -0.0192 669 HOH B O   
9265 O  O   . HOH BA .   ? 0.6904 0.3581 0.4600 0.1602  0.0500  0.1277  670 HOH B O   
9266 O  O   . HOH BA .   ? 0.3176 0.2739 0.2428 -0.0016 0.0718  0.0032  671 HOH B O   
9267 O  O   . HOH BA .   ? 0.3341 0.3865 0.4005 -0.0972 -0.0174 -0.0628 672 HOH B O   
9268 O  O   . HOH BA .   ? 0.3385 0.3227 0.2717 -0.0422 -0.0258 0.0737  673 HOH B O   
9269 O  O   . HOH BA .   ? 0.1988 1.0942 0.4484 0.0298  0.1921  -0.1380 674 HOH B O   
9270 O  O   . HOH BA .   ? 0.7698 0.2810 0.8308 0.1160  -0.2313 -0.0362 675 HOH B O   
9271 O  O   . HOH BA .   ? 0.3991 0.2226 0.6989 -0.0163 0.1447  -0.0776 676 HOH B O   
9272 O  O   . HOH BA .   ? 0.5842 0.5161 0.6776 -0.0596 -0.1611 -0.1662 677 HOH B O   
9273 O  O   . HOH BA .   ? 0.5329 0.6074 0.5852 -0.2492 0.2599  -0.1539 678 HOH B O   
9274 O  O   . HOH CA .   ? 0.3248 0.3946 0.3753 -0.0559 0.0706  -0.0144 401 HOH C O   
9275 O  O   . HOH CA .   ? 0.4008 0.9167 0.6946 -0.1041 0.2303  -0.2843 402 HOH C O   
9276 O  O   . HOH CA .   ? 0.5315 0.7397 0.2657 -0.1544 0.0370  0.0120  403 HOH C O   
9277 O  O   . HOH CA .   ? 0.3103 0.2692 0.2242 0.0363  -0.0463 0.0445  404 HOH C O   
9278 O  O   . HOH CA .   ? 0.2298 0.4781 0.9266 0.0515  0.0758  0.1512  405 HOH C O   
9279 O  O   . HOH CA .   ? 0.2117 0.3816 0.4080 -0.0611 0.0314  -0.1437 406 HOH C O   
9280 O  O   . HOH CA .   ? 0.3277 0.3991 0.4503 -0.0395 -0.0247 -0.0820 407 HOH C O   
9281 O  O   . HOH CA .   ? 0.3231 0.2133 0.2610 -0.0247 -0.0244 -0.0121 408 HOH C O   
9282 O  O   . HOH CA .   ? 0.2491 0.6632 0.4300 -0.0192 0.0127  -0.0930 409 HOH C O   
9283 O  O   . HOH CA .   ? 0.2745 0.5180 0.3316 -0.0258 -0.0537 0.0262  410 HOH C O   
9284 O  O   . HOH CA .   ? 0.3158 0.3552 0.2667 -0.0326 0.0680  -0.0767 411 HOH C O   
9285 O  O   . HOH CA .   ? 0.3517 0.4449 0.3483 -0.1941 -0.0548 0.0575  412 HOH C O   
9286 O  O   . HOH CA .   ? 0.4031 0.2966 0.2824 -0.1088 -0.0471 0.0850  413 HOH C O   
9287 O  O   . HOH CA .   ? 0.2010 0.2604 0.1427 -0.0348 -0.0037 -0.0190 414 HOH C O   
9288 O  O   . HOH CA .   ? 0.5243 0.4284 0.3119 -0.1676 -0.0482 0.0621  415 HOH C O   
9289 O  O   . HOH CA .   ? 0.2870 0.5041 0.4099 -0.0681 0.0761  0.1685  416 HOH C O   
9290 O  O   . HOH CA .   ? 0.4292 0.3819 0.3328 -0.0398 -0.1245 0.0043  417 HOH C O   
9291 O  O   . HOH CA .   ? 0.4913 0.4492 0.7122 -0.0577 -0.2416 -0.1949 418 HOH C O   
9292 O  O   . HOH CA .   ? 0.7549 0.4371 0.5563 -0.0851 0.3272  0.0210  419 HOH C O   
9293 O  O   . HOH CA .   ? 0.2099 0.3453 0.2539 0.0315  0.0614  -0.0182 420 HOH C O   
9294 O  O   . HOH CA .   ? 0.3583 0.3865 0.3046 -0.0307 0.0319  0.0179  421 HOH C O   
9295 O  O   . HOH CA .   ? 0.5147 0.3068 0.3415 0.0458  -0.0657 -0.0280 422 HOH C O   
9296 O  O   . HOH CA .   ? 0.2673 0.4902 0.4746 0.0463  -0.0357 -0.1272 423 HOH C O   
9297 O  O   . HOH CA .   ? 0.2426 0.3948 0.3544 -0.0346 -0.0725 -0.0315 424 HOH C O   
9298 O  O   . HOH CA .   ? 0.2193 0.2732 0.2609 0.0161  0.0114  -0.0500 425 HOH C O   
9299 O  O   . HOH CA .   ? 0.4717 0.5314 0.3963 0.0653  -0.1580 -0.0441 426 HOH C O   
9300 O  O   . HOH CA .   ? 0.3941 0.4852 0.2207 0.0042  -0.0038 0.0784  427 HOH C O   
9301 O  O   . HOH CA .   ? 0.3189 0.4975 0.2576 0.0113  0.0313  0.0729  428 HOH C O   
9302 O  O   . HOH CA .   ? 0.2545 0.2404 0.2746 -0.0030 0.0073  -0.0120 429 HOH C O   
9303 O  O   . HOH CA .   ? 0.2666 0.3065 0.1581 -0.0212 0.0162  0.0462  430 HOH C O   
9304 O  O   . HOH CA .   ? 0.5836 0.4482 0.4210 -0.0890 -0.1222 -0.0322 431 HOH C O   
9305 O  O   . HOH CA .   ? 0.6001 0.3981 0.4191 -0.0041 0.1305  0.0489  432 HOH C O   
9306 O  O   . HOH CA .   ? 0.2290 0.2065 0.2205 0.0156  0.0148  -0.0302 433 HOH C O   
9307 O  O   . HOH CA .   ? 0.5998 0.3085 0.6060 -0.0395 0.0829  -0.0732 434 HOH C O   
9308 O  O   . HOH CA .   ? 0.3078 0.4692 0.6362 0.0663  0.1210  0.2578  435 HOH C O   
9309 O  O   . HOH CA .   ? 0.1698 0.1932 0.1461 0.0098  -0.0022 -0.0018 436 HOH C O   
9310 O  O   . HOH CA .   ? 0.2044 0.4409 0.2632 0.0223  -0.0236 0.0140  437 HOH C O   
9311 O  O   . HOH CA .   ? 0.6993 1.5487 0.4697 0.1506  -0.0260 -0.4585 438 HOH C O   
9312 O  O   . HOH CA .   ? 0.4034 0.3633 0.2934 -0.0574 0.0125  -0.0070 439 HOH C O   
9313 O  O   . HOH CA .   ? 0.3292 0.2537 0.1220 -0.0489 -0.0243 -0.0227 440 HOH C O   
9314 O  O   . HOH CA .   ? 0.3373 0.5572 0.4158 0.0530  -0.0150 0.0397  441 HOH C O   
9315 O  O   . HOH CA .   ? 0.1828 0.1479 0.1554 -0.0082 -0.0013 -0.0057 442 HOH C O   
9316 O  O   . HOH CA .   ? 0.3332 0.5972 0.2920 0.1430  0.0296  0.0296  443 HOH C O   
9317 O  O   . HOH CA .   ? 0.5118 0.2925 0.5578 -0.1140 0.0401  0.0409  444 HOH C O   
9318 O  O   . HOH CA .   ? 0.4144 0.3324 0.2462 0.0527  -0.0044 -0.0159 445 HOH C O   
9319 O  O   . HOH CA .   ? 0.6616 0.3554 0.4471 -0.0093 -0.2099 -0.0065 446 HOH C O   
9320 O  O   . HOH CA .   ? 0.6190 0.5401 0.2635 0.0368  -0.0394 -0.0046 447 HOH C O   
9321 O  O   . HOH CA .   ? 0.3092 0.5151 0.3581 -0.0337 0.0200  0.0839  448 HOH C O   
9322 O  O   . HOH CA .   ? 0.3677 0.4916 0.6055 -0.1514 0.1231  0.0569  449 HOH C O   
9323 O  O   . HOH CA .   ? 0.2372 0.2437 0.2702 -0.0029 0.0422  -0.0044 450 HOH C O   
9324 O  O   . HOH CA .   ? 0.2771 0.3797 0.2936 0.0310  0.0280  0.1158  451 HOH C O   
9325 O  O   . HOH CA .   ? 0.3258 0.4887 0.3318 -0.1180 0.0681  -0.0728 452 HOH C O   
9326 O  O   . HOH CA .   ? 0.3865 0.4768 0.8907 0.0479  0.0608  -0.0951 453 HOH C O   
9327 O  O   . HOH CA .   ? 0.2762 0.4696 0.5039 0.0247  -0.0900 0.0636  454 HOH C O   
9328 O  O   . HOH CA .   ? 0.1585 0.2369 0.1680 0.0140  -0.0173 0.0173  455 HOH C O   
9329 O  O   . HOH CA .   ? 0.1802 0.1787 0.1874 0.0205  -0.0385 0.0083  456 HOH C O   
9330 O  O   . HOH CA .   ? 0.2377 0.2425 0.2330 0.0333  -0.0069 0.0033  457 HOH C O   
9331 O  O   . HOH CA .   ? 0.3197 0.3999 0.1709 -0.0291 -0.0542 -0.0097 458 HOH C O   
9332 O  O   . HOH CA .   ? 0.3436 0.4756 0.2917 0.0508  -0.0500 -0.0937 459 HOH C O   
9333 O  O   . HOH CA .   ? 0.4008 0.4280 0.3265 -0.0179 -0.1074 0.0171  460 HOH C O   
9334 O  O   . HOH CA .   ? 0.1782 0.2559 0.1333 -0.0293 -0.0343 0.0229  461 HOH C O   
9335 O  O   . HOH CA .   ? 0.2784 0.2158 0.2295 -0.0812 -0.0355 -0.0292 462 HOH C O   
9336 O  O   . HOH CA .   ? 0.3732 0.4779 0.6102 -0.0084 -0.1552 0.1025  463 HOH C O   
9337 O  O   . HOH CA .   ? 0.2762 0.2095 0.2075 0.0291  -0.0227 0.0153  464 HOH C O   
9338 O  O   . HOH CA .   ? 0.2143 0.2025 0.3258 0.0220  0.0107  -0.0089 465 HOH C O   
9339 O  O   . HOH CA .   ? 0.1650 0.1584 0.1345 0.0074  -0.0060 0.0129  466 HOH C O   
9340 O  O   . HOH CA .   ? 0.2128 0.2033 0.2025 -0.0557 -0.0137 -0.0300 467 HOH C O   
9341 O  O   . HOH CA .   ? 0.3367 0.5015 0.3207 -0.0308 -0.0001 0.1322  468 HOH C O   
9342 O  O   . HOH CA .   ? 0.3462 0.3655 0.3707 -0.0944 -0.0770 -0.0100 469 HOH C O   
9343 O  O   . HOH CA .   ? 0.5838 0.3925 0.2588 -0.0638 0.0083  0.0002  470 HOH C O   
9344 O  O   . HOH CA .   ? 0.3899 0.4516 0.7043 0.1935  -0.1513 -0.0285 471 HOH C O   
9345 O  O   . HOH CA .   ? 0.5780 0.5217 0.6567 -0.0271 -0.1040 -0.1595 472 HOH C O   
9346 O  O   . HOH CA .   ? 0.3155 0.2462 0.2297 -0.0190 0.0308  0.0102  473 HOH C O   
9347 O  O   . HOH CA .   ? 0.4148 0.4621 0.3428 -0.0253 0.0605  0.0001  474 HOH C O   
9348 O  O   . HOH CA .   ? 0.4805 0.5267 0.4118 0.0469  -0.0834 -0.1218 475 HOH C O   
9349 O  O   . HOH CA .   ? 0.2934 0.3895 0.3536 0.0197  0.0533  0.1043  476 HOH C O   
9350 O  O   . HOH CA .   ? 0.4041 0.7295 0.4014 0.0505  -0.1395 0.1981  477 HOH C O   
9351 O  O   . HOH CA .   ? 0.1360 0.8423 1.4949 -0.2400 -0.3827 0.4181  478 HOH C O   
9352 O  O   . HOH CA .   ? 0.2525 0.3262 0.2056 0.0498  0.0356  0.0422  479 HOH C O   
9353 O  O   . HOH CA .   ? 0.4371 0.3494 0.5876 0.0140  -0.2423 -0.0620 480 HOH C O   
9354 O  O   . HOH CA .   ? 0.2581 0.3665 0.2383 0.1166  0.0359  0.0376  481 HOH C O   
9355 O  O   . HOH CA .   ? 0.2547 0.5787 0.4666 -0.0269 0.1178  0.0230  482 HOH C O   
9356 O  O   . HOH CA .   ? 0.5250 0.4016 0.3670 0.1040  0.1082  -0.0529 483 HOH C O   
9357 O  O   . HOH CA .   ? 0.3459 0.2816 0.1841 -0.0658 0.0076  0.0204  484 HOH C O   
9358 O  O   . HOH CA .   ? 0.4014 1.0258 0.2672 0.0573  -0.0083 0.2235  485 HOH C O   
9359 O  O   . HOH CA .   ? 0.2350 0.3690 0.3313 -0.0475 -0.0469 -0.0104 486 HOH C O   
9360 O  O   . HOH CA .   ? 0.4841 0.3904 0.6909 -0.1078 -0.0741 0.0110  487 HOH C O   
9361 O  O   . HOH CA .   ? 0.2775 0.2942 0.2655 -0.0154 0.0137  0.0480  488 HOH C O   
9362 O  O   . HOH CA .   ? 0.3369 0.3831 0.1621 -0.0187 -0.0549 0.0060  489 HOH C O   
9363 O  O   . HOH CA .   ? 0.3332 0.3703 0.3131 -0.0160 -0.0096 0.0542  490 HOH C O   
9364 O  O   . HOH CA .   ? 0.1743 0.1591 0.1562 -0.0081 -0.0124 0.0021  491 HOH C O   
9365 O  O   . HOH CA .   ? 0.3893 0.4115 0.5392 0.1546  0.0947  0.2023  492 HOH C O   
9366 O  O   . HOH CA .   ? 0.2622 0.5588 0.3512 -0.1346 0.0018  0.0348  493 HOH C O   
9367 O  O   . HOH CA .   ? 0.3699 0.3933 0.4357 0.0718  0.0982  0.0855  494 HOH C O   
9368 O  O   . HOH CA .   ? 0.1864 0.1380 0.1829 -0.0149 -0.0095 -0.0026 495 HOH C O   
9369 O  O   . HOH CA .   ? 0.7682 0.2420 0.4544 -0.0269 0.0965  -0.0278 496 HOH C O   
9370 O  O   . HOH CA .   ? 0.4924 0.5184 0.3067 0.0671  0.0484  0.0621  497 HOH C O   
9371 O  O   . HOH CA .   ? 0.2335 0.2609 0.1770 0.0288  0.0229  0.0367  498 HOH C O   
9372 O  O   . HOH CA .   ? 0.3474 0.4952 0.2763 0.0184  0.0460  0.0637  499 HOH C O   
9373 O  O   . HOH CA .   ? 0.1951 0.4058 0.4407 -0.0489 -0.0043 0.0103  500 HOH C O   
9374 O  O   . HOH CA .   ? 0.4109 0.2502 0.3358 0.1002  0.0968  0.0899  501 HOH C O   
9375 O  O   . HOH CA .   ? 0.2334 0.2907 0.4421 -0.0197 -0.1346 0.0659  502 HOH C O   
9376 O  O   . HOH CA .   ? 0.3849 0.3662 0.3712 0.1058  -0.0630 -0.0576 503 HOH C O   
9377 O  O   . HOH CA .   ? 0.2304 0.4362 0.3971 0.0450  -0.1023 0.0186  504 HOH C O   
9378 O  O   . HOH CA .   ? 0.1879 0.2046 0.1840 -0.0008 -0.0416 -0.0039 505 HOH C O   
9379 O  O   . HOH CA .   ? 0.2896 0.2438 0.2094 -0.0463 0.0159  0.0381  506 HOH C O   
9380 O  O   . HOH CA .   ? 0.1421 0.1398 0.1246 -0.0097 -0.0072 0.0053  507 HOH C O   
9381 O  O   . HOH CA .   ? 0.5041 0.3488 0.6030 -0.1544 0.1080  -0.0136 508 HOH C O   
9382 O  O   . HOH CA .   ? 0.2717 0.5985 0.4685 -0.0895 -0.0487 -0.0553 509 HOH C O   
9383 O  O   . HOH CA .   ? 0.2946 0.2811 0.4727 -0.1185 0.0031  0.0117  510 HOH C O   
9384 O  O   . HOH CA .   ? 0.4624 0.4073 0.4459 -0.0196 -0.0536 0.0489  511 HOH C O   
9385 O  O   . HOH CA .   ? 0.7458 0.3729 0.3978 -0.0611 0.1930  -0.0403 512 HOH C O   
9386 O  O   . HOH CA .   ? 0.1752 0.1824 0.1648 -0.0141 0.0109  -0.0078 513 HOH C O   
9387 O  O   . HOH CA .   ? 0.4549 0.8867 0.6116 -0.2383 0.0066  -0.1005 514 HOH C O   
9388 O  O   . HOH CA .   ? 0.1904 0.1795 0.1702 -0.0304 0.0148  0.0087  515 HOH C O   
9389 O  O   . HOH CA .   ? 0.3035 0.3127 0.1404 -0.0626 -0.0592 -0.0072 516 HOH C O   
9390 O  O   . HOH CA .   ? 0.4383 0.5716 0.2570 -0.2320 0.0208  0.0294  517 HOH C O   
9391 O  O   . HOH CA .   ? 0.6190 0.3633 0.5560 0.1516  -0.0903 -0.0802 518 HOH C O   
9392 O  O   . HOH CA .   ? 0.3503 0.5378 0.2527 -0.0390 -0.0200 0.0658  519 HOH C O   
9393 O  O   . HOH CA .   ? 0.2073 0.2896 0.1936 -0.0443 -0.0041 0.0188  520 HOH C O   
9394 O  O   . HOH CA .   ? 0.6534 0.3939 0.1873 -0.0093 -0.0142 0.0111  521 HOH C O   
9395 O  O   . HOH CA .   ? 0.3670 0.6314 0.5791 -0.1180 0.0472  -0.1617 522 HOH C O   
9396 O  O   . HOH CA .   ? 0.3747 0.5741 0.2860 -0.0675 0.1363  -0.0157 523 HOH C O   
9397 O  O   . HOH CA .   ? 0.3353 0.7541 0.5265 -0.1198 0.0226  0.0661  524 HOH C O   
9398 O  O   . HOH CA .   ? 0.4590 0.6161 0.2618 -0.0131 0.0080  0.0311  525 HOH C O   
9399 O  O   . HOH CA .   ? 0.2857 0.2679 0.1526 -0.0307 0.0166  0.0006  526 HOH C O   
9400 O  O   . HOH CA .   ? 0.7210 0.3620 0.3946 0.0719  -0.2116 -0.0017 527 HOH C O   
9401 O  O   . HOH CA .   ? 0.2428 0.2649 0.3446 -0.0756 0.0011  -0.0489 528 HOH C O   
9402 O  O   . HOH CA .   ? 0.7109 0.9695 0.3070 -0.1303 -0.0509 0.1377  529 HOH C O   
9403 O  O   . HOH CA .   ? 0.3978 0.4614 0.4750 -0.0016 -0.1017 -0.1031 530 HOH C O   
9404 O  O   . HOH CA .   ? 0.4348 0.2608 0.3064 -0.0762 0.0937  -0.0062 531 HOH C O   
9405 O  O   . HOH CA .   ? 0.4127 0.6264 0.4336 0.0967  -0.0079 0.0743  532 HOH C O   
9406 O  O   . HOH CA .   ? 0.2800 0.2165 0.2475 0.0135  -0.1142 -0.0238 533 HOH C O   
9407 O  O   . HOH CA .   ? 0.2799 0.2518 0.1894 -0.0249 -0.0807 0.0000  534 HOH C O   
9408 O  O   . HOH CA .   ? 0.2338 0.5665 0.2372 -0.0419 0.0248  0.0526  535 HOH C O   
9409 O  O   . HOH CA .   ? 0.3687 0.3758 0.4820 0.1386  -0.0175 0.0971  536 HOH C O   
9410 O  O   . HOH CA .   ? 0.3471 0.3908 0.3271 0.0323  0.0220  0.1524  537 HOH C O   
9411 O  O   . HOH CA .   ? 0.3789 0.5128 0.3405 0.0585  0.0861  0.0350  538 HOH C O   
9412 O  O   . HOH CA .   ? 0.3356 0.4176 0.2070 0.0163  0.0274  0.0664  539 HOH C O   
9413 O  O   . HOH CA .   ? 0.2956 0.2089 0.1810 -0.0269 -0.0137 0.0094  540 HOH C O   
9414 O  O   . HOH CA .   ? 0.4678 0.4497 0.4558 0.1740  -0.0951 0.0267  541 HOH C O   
9415 O  O   . HOH CA .   ? 0.6380 0.3651 0.3819 -0.0408 -0.1315 0.0194  542 HOH C O   
9416 O  O   . HOH CA .   ? 0.4651 0.4591 0.4306 0.1031  -0.1079 -0.1681 543 HOH C O   
9417 O  O   . HOH CA .   ? 0.4238 0.4532 0.3651 -0.0355 0.0656  0.1646  544 HOH C O   
9418 O  O   . HOH CA .   ? 0.1747 0.1734 0.1789 0.0033  -0.0154 -0.0337 545 HOH C O   
9419 O  O   . HOH CA .   ? 0.4341 0.2631 0.6988 0.0215  0.1185  -0.0104 546 HOH C O   
9420 O  O   . HOH CA .   ? 0.3111 0.4486 0.3195 -0.0486 -0.0325 0.0142  547 HOH C O   
9421 O  O   . HOH CA .   ? 0.2333 0.1456 0.2329 -0.0163 -0.0644 0.0231  548 HOH C O   
9422 O  O   . HOH CA .   ? 0.3908 0.5155 0.5155 0.0512  0.0391  0.0824  549 HOH C O   
9423 O  O   . HOH CA .   ? 0.3608 0.3962 0.4459 0.1056  -0.0144 -0.0557 550 HOH C O   
9424 O  O   . HOH CA .   ? 0.6634 0.3617 0.3334 0.0851  0.0490  0.0109  551 HOH C O   
9425 O  O   . HOH CA .   ? 0.2929 0.5468 0.3021 -0.0152 -0.0419 0.0086  552 HOH C O   
9426 O  O   . HOH CA .   ? 0.2906 0.3383 0.4249 -0.0076 -0.0647 -0.0096 553 HOH C O   
9427 O  O   . HOH CA .   ? 0.2881 0.5306 0.3200 0.0011  -0.0092 0.2150  554 HOH C O   
9428 O  O   . HOH CA .   ? 0.5075 0.4792 0.5445 -0.0562 0.0661  0.0114  555 HOH C O   
9429 O  O   . HOH CA .   ? 0.3757 0.3208 0.3142 0.0183  -0.0536 -0.0004 556 HOH C O   
9430 O  O   . HOH CA .   ? 0.4202 0.4321 0.3693 0.0163  -0.0143 -0.0254 557 HOH C O   
9431 O  O   . HOH CA .   ? 0.4238 0.4733 0.3872 0.0158  -0.0118 -0.0015 558 HOH C O   
9432 O  O   . HOH CA .   ? 0.2543 0.2302 0.2737 0.0752  0.0270  0.0656  559 HOH C O   
9433 O  O   . HOH CA .   ? 0.6581 0.3518 0.2845 -0.0675 -0.0670 0.0034  560 HOH C O   
9434 O  O   . HOH CA .   ? 0.4366 0.3569 0.3315 0.0701  0.0339  -0.0064 561 HOH C O   
9435 O  O   . HOH CA .   ? 0.6645 0.6233 0.3043 -0.2053 -0.1895 0.0397  562 HOH C O   
9436 O  O   . HOH CA .   ? 0.6267 0.3534 0.3621 0.0863  0.1257  0.0200  563 HOH C O   
9437 O  O   . HOH CA .   ? 0.3994 0.9974 0.5426 0.1029  0.0464  0.3957  564 HOH C O   
9438 O  O   . HOH CA .   ? 0.3995 0.2676 0.3304 -0.0803 0.0774  0.0108  565 HOH C O   
9439 O  O   . HOH CA .   ? 0.4929 0.3653 0.5284 0.2212  0.2085  0.0759  566 HOH C O   
9440 O  O   . HOH CA .   ? 0.4009 0.3884 0.2852 -0.0292 -0.0480 0.0292  567 HOH C O   
9441 O  O   . HOH CA .   ? 0.3310 0.2819 0.2653 0.0080  0.0281  0.1004  568 HOH C O   
9442 O  O   . HOH CA .   ? 0.4428 0.3808 0.4009 -0.0395 -0.1034 -0.0215 569 HOH C O   
9443 O  O   . HOH CA .   ? 0.5975 0.3107 0.4009 0.0626  -0.0846 0.0565  570 HOH C O   
9444 O  O   . HOH CA .   ? 0.3353 0.7081 0.3638 0.0824  -0.0528 -0.0118 571 HOH C O   
9445 O  O   . HOH CA .   ? 0.2903 0.3332 0.2724 -0.0098 -0.0227 0.0924  572 HOH C O   
9446 O  O   . HOH CA .   ? 0.5583 0.4635 0.7931 -0.0818 -0.1953 0.0122  573 HOH C O   
9447 O  O   . HOH CA .   ? 0.5328 0.6117 0.5365 -0.1638 -0.0967 -0.0114 574 HOH C O   
9448 O  O   . HOH CA .   ? 0.5052 0.3477 0.4872 -0.1655 -0.0519 -0.0980 575 HOH C O   
9449 O  O   . HOH CA .   ? 0.3726 0.5231 0.3308 -0.0621 -0.0521 -0.0016 576 HOH C O   
9450 O  O   . HOH CA .   ? 0.3184 0.5782 0.3921 0.1169  0.0089  0.0323  577 HOH C O   
9451 O  O   . HOH CA .   ? 0.3721 0.5062 0.3871 -0.0696 -0.0757 -0.0038 578 HOH C O   
9452 O  O   . HOH CA .   ? 0.3859 0.7895 0.3306 -0.1770 0.0290  -0.0782 579 HOH C O   
9453 O  O   . HOH CA .   ? 0.5908 0.5384 0.4461 0.0920  0.1154  0.0954  580 HOH C O   
9454 O  O   . HOH CA .   ? 0.3508 0.4619 0.2225 0.0326  -0.0105 0.0325  581 HOH C O   
9455 O  O   . HOH CA .   ? 0.4278 0.7087 0.6795 0.0380  -0.2847 0.0245  582 HOH C O   
9456 O  O   . HOH CA .   ? 0.4334 0.4125 0.3695 -0.0233 0.0068  -0.0043 583 HOH C O   
9457 O  O   . HOH CA .   ? 0.4151 0.8806 0.4876 -0.2469 0.1397  0.0099  584 HOH C O   
9458 O  O   . HOH CA .   ? 0.4706 0.5017 1.0239 0.0116  -0.1745 -0.3615 585 HOH C O   
9459 O  O   . HOH CA .   ? 0.5504 0.4506 0.2798 0.0274  -0.0292 -0.0027 586 HOH C O   
9460 O  O   . HOH CA .   ? 0.4750 0.3545 0.5061 0.0740  -0.1147 -0.0034 587 HOH C O   
9461 O  O   . HOH CA .   ? 0.2207 0.3898 0.4487 -0.0451 -0.0387 0.0153  588 HOH C O   
9462 O  O   . HOH CA .   ? 0.4533 0.3150 0.3929 0.0050  0.0183  0.0365  589 HOH C O   
9463 O  O   . HOH CA .   ? 0.6393 0.3874 0.3337 -0.0650 0.0315  0.0402  590 HOH C O   
9464 O  O   . HOH CA .   ? 0.4153 0.6163 0.5502 -0.0828 -0.1450 0.0685  591 HOH C O   
9465 O  O   . HOH CA .   ? 0.4985 0.4707 0.4322 0.1421  -0.0597 0.0818  592 HOH C O   
9466 O  O   . HOH CA .   ? 0.6628 1.7522 0.6485 0.0748  -0.0744 -0.0308 593 HOH C O   
9467 O  O   . HOH CA .   ? 0.3495 0.4446 0.4481 -0.0756 -0.0173 0.0439  594 HOH C O   
9468 O  O   . HOH CA .   ? 0.4325 0.2502 0.4417 -0.0368 0.1263  -0.0453 595 HOH C O   
9469 O  O   . HOH CA .   ? 0.3005 0.2436 0.2078 -0.0241 0.0098  -0.0069 596 HOH C O   
9470 O  O   . HOH CA .   ? 0.2518 0.3889 0.3748 0.0337  -0.0149 -0.0096 597 HOH C O   
9471 O  O   . HOH CA .   ? 0.3493 0.4483 0.5035 0.0682  0.0260  0.0142  598 HOH C O   
9472 O  O   . HOH CA .   ? 0.6827 0.5995 0.4175 0.1881  0.0715  0.1548  599 HOH C O   
9473 O  O   . HOH CA .   ? 0.5628 0.5328 0.3768 0.3018  -0.0245 -0.0059 600 HOH C O   
9474 O  O   . HOH CA .   ? 0.4680 0.4386 0.4389 0.0033  -0.0150 -0.0078 601 HOH C O   
9475 O  O   . HOH CA .   ? 0.7305 0.3428 0.7489 0.0147  0.4730  0.1367  602 HOH C O   
9476 O  O   . HOH CA .   ? 0.4232 0.5561 0.6335 -0.0183 0.1243  0.2590  603 HOH C O   
9477 O  O   . HOH CA .   ? 0.5123 0.3404 0.5207 0.0323  -0.0675 -0.0814 604 HOH C O   
9478 O  O   . HOH CA .   ? 0.4929 0.5517 0.5189 0.1060  -0.0562 0.0232  605 HOH C O   
9479 O  O   . HOH CA .   ? 0.8151 0.2366 0.6565 0.0019  0.0189  0.0378  606 HOH C O   
9480 O  O   . HOH CA .   ? 0.2809 0.4248 0.4019 0.0436  -0.0435 -0.0190 607 HOH C O   
9481 O  O   . HOH CA .   ? 0.4086 0.4692 0.3603 0.0834  0.0784  0.1013  608 HOH C O   
9482 O  O   . HOH CA .   ? 0.4527 0.4281 0.3464 0.0357  0.0160  -0.0163 609 HOH C O   
9483 O  O   . HOH CA .   ? 0.4604 0.3783 0.5000 0.0642  0.0568  0.0012  610 HOH C O   
9484 O  O   . HOH CA .   ? 0.5703 0.6299 0.3095 0.1251  -0.0581 0.0365  611 HOH C O   
9485 O  O   . HOH CA .   ? 0.5808 0.5861 0.3825 0.1052  -0.0741 0.0993  612 HOH C O   
9486 O  O   . HOH DA .   ? 0.2617 0.2837 0.4186 0.0648  0.0515  0.0299  401 HOH D O   
9487 O  O   . HOH DA .   ? 0.3264 0.4586 0.2987 -0.1324 -0.0730 0.1712  402 HOH D O   
9488 O  O   . HOH DA .   ? 0.3780 0.4171 0.4140 0.0761  0.1543  0.1206  403 HOH D O   
9489 O  O   . HOH DA .   ? 0.4074 0.3231 0.3173 0.0599  0.0836  0.0138  404 HOH D O   
9490 O  O   . HOH DA .   ? 0.3260 0.3008 0.5141 -0.0304 -0.1473 0.0928  405 HOH D O   
9491 O  O   . HOH DA .   ? 0.4368 0.5285 0.3335 -0.0276 0.0425  -0.0163 406 HOH D O   
9492 O  O   . HOH DA .   ? 0.3586 0.3682 0.4976 -0.0280 -0.1186 0.0620  407 HOH D O   
9493 O  O   . HOH DA .   ? 0.2971 0.2732 0.2308 -0.0477 0.0355  -0.0209 408 HOH D O   
9494 O  O   . HOH DA .   ? 0.4811 0.4229 0.5420 -0.0624 0.1210  -0.1009 409 HOH D O   
9495 O  O   . HOH DA .   ? 0.7670 0.6725 0.6506 0.1045  -0.1291 0.2978  410 HOH D O   
9496 O  O   . HOH DA .   ? 0.3890 0.3573 0.4029 0.0532  0.0839  0.1172  411 HOH D O   
9497 O  O   . HOH DA .   ? 0.3610 0.3738 0.2632 0.0596  0.0291  0.0093  412 HOH D O   
9498 O  O   . HOH DA .   ? 0.4102 0.3023 0.8351 -0.0542 0.0450  -0.0494 413 HOH D O   
9499 O  O   . HOH DA .   ? 0.3377 0.2804 0.4010 -0.1029 -0.0363 -0.0500 414 HOH D O   
9500 O  O   . HOH DA .   ? 0.5945 0.3932 0.3771 0.1826  -0.0027 0.0125  415 HOH D O   
9501 O  O   . HOH DA .   ? 0.1641 0.1540 0.1316 0.0111  0.0111  -0.0073 416 HOH D O   
9502 O  O   . HOH DA .   ? 0.3574 0.3142 0.5335 -0.0866 0.1131  -0.0490 417 HOH D O   
9503 O  O   . HOH DA .   ? 0.3962 0.2516 0.5375 -0.0478 0.1177  -0.0788 418 HOH D O   
9504 O  O   . HOH DA .   ? 0.4137 0.4890 0.3146 -0.1059 0.0416  -0.0520 419 HOH D O   
9505 O  O   . HOH DA .   ? 0.6332 0.5217 0.3176 0.0080  -0.1241 0.0625  420 HOH D O   
9506 O  O   . HOH DA .   ? 0.3592 0.3058 0.2585 0.0632  -0.0081 0.0539  421 HOH D O   
9507 O  O   . HOH DA .   ? 0.3102 0.7033 0.4526 0.0807  0.0175  -0.0046 422 HOH D O   
9508 O  O   . HOH DA .   ? 0.3322 0.2601 0.3378 0.0666  -0.0496 -0.0536 423 HOH D O   
9509 O  O   . HOH DA .   ? 0.3628 0.3926 0.3597 -0.0178 -0.0784 0.0591  424 HOH D O   
9510 O  O   . HOH DA .   ? 0.3294 0.4056 0.3572 -0.0583 -0.0307 -0.0097 425 HOH D O   
9511 O  O   . HOH DA .   ? 0.7167 0.2552 0.3425 -0.0122 -0.1775 0.0027  426 HOH D O   
9512 O  O   . HOH DA .   ? 0.2863 0.2648 0.2637 0.0467  0.0190  0.0140  427 HOH D O   
9513 O  O   . HOH DA .   ? 0.5863 0.6010 0.2967 -0.2854 0.1973  -0.2082 428 HOH D O   
9514 O  O   . HOH DA .   ? 0.4433 0.2262 0.2554 0.0835  0.0731  0.0245  429 HOH D O   
9515 O  O   . HOH DA .   ? 0.3456 0.4253 0.2156 0.0279  0.0458  -0.0663 430 HOH D O   
9516 O  O   . HOH DA .   ? 0.5429 0.3013 0.3659 -0.0058 0.0473  0.0850  431 HOH D O   
9517 O  O   . HOH DA .   ? 0.5316 0.4402 0.5683 0.1314  0.0018  0.0137  432 HOH D O   
9518 O  O   . HOH DA .   ? 0.3727 0.4848 0.2983 0.0423  -0.0032 0.0284  433 HOH D O   
9519 O  O   . HOH DA .   ? 0.2838 0.2547 0.3410 -0.0102 0.0346  -0.0268 434 HOH D O   
9520 O  O   . HOH DA .   ? 0.3028 0.3582 0.3019 -0.0761 -0.0029 -0.0403 435 HOH D O   
9521 O  O   . HOH DA .   ? 0.3899 0.4691 0.3433 0.0422  -0.0322 0.0228  436 HOH D O   
9522 O  O   . HOH DA .   ? 0.2301 0.2949 0.3824 -0.0006 0.1192  0.0800  437 HOH D O   
9523 O  O   . HOH DA .   ? 0.2225 0.2800 0.2276 0.0350  0.0086  0.0030  438 HOH D O   
9524 O  O   . HOH DA .   ? 0.4826 0.8312 0.2713 -0.3051 -0.0998 0.2148  439 HOH D O   
9525 O  O   . HOH DA .   ? 0.2997 0.3083 0.2017 -0.0577 -0.0128 0.0396  440 HOH D O   
9526 O  O   . HOH DA .   ? 0.3398 0.2699 0.3201 -0.0142 0.0571  -0.0416 441 HOH D O   
9527 O  O   . HOH DA .   ? 0.3673 0.4576 0.4005 0.0227  0.1085  0.0264  442 HOH D O   
9528 O  O   . HOH DA .   ? 0.4612 0.3037 0.3764 0.0634  0.0700  -0.0314 443 HOH D O   
9529 O  O   . HOH DA .   ? 0.4815 0.3402 0.3500 0.0828  0.2371  0.0267  444 HOH D O   
9530 O  O   . HOH DA .   ? 0.2228 0.1588 0.1490 -0.0136 -0.0208 0.0000  445 HOH D O   
9531 O  O   . HOH DA .   ? 0.2145 0.2200 0.2713 -0.0100 0.0184  -0.0336 446 HOH D O   
9532 O  O   . HOH DA .   ? 0.3611 0.4258 0.4920 -0.1136 0.0822  -0.0598 447 HOH D O   
9533 O  O   . HOH DA .   ? 0.3328 0.3271 0.3736 0.0362  -0.1307 -0.0314 448 HOH D O   
9534 O  O   . HOH DA .   ? 0.8046 0.5296 0.2111 0.2091  -0.1035 -0.0773 449 HOH D O   
9535 O  O   . HOH DA .   ? 0.2303 0.2157 0.1750 0.0100  -0.0115 -0.0115 450 HOH D O   
9536 O  O   . HOH DA .   ? 0.2174 0.1849 0.1667 -0.0221 -0.0102 -0.0174 451 HOH D O   
9537 O  O   . HOH DA .   ? 0.3889 0.3048 0.3851 -0.0731 -0.0480 -0.0540 452 HOH D O   
9538 O  O   . HOH DA .   ? 0.4425 0.3407 0.3134 -0.0111 -0.0253 0.0326  453 HOH D O   
9539 O  O   . HOH DA .   ? 0.2078 0.2958 0.2618 0.0094  0.0326  -0.0326 454 HOH D O   
9540 O  O   . HOH DA .   ? 0.2719 0.2723 0.2581 0.0185  0.0217  0.0073  455 HOH D O   
9541 O  O   . HOH DA .   ? 0.4296 0.2667 0.3097 0.0050  -0.0429 0.0053  456 HOH D O   
9542 O  O   . HOH DA .   ? 0.4951 0.1995 0.8128 -0.0753 0.0022  0.1517  457 HOH D O   
9543 O  O   . HOH DA .   ? 0.3013 0.2887 0.2499 0.0587  0.0403  0.0236  458 HOH D O   
9544 O  O   . HOH DA .   ? 0.2332 0.1708 0.1969 -0.0375 -0.0525 0.0417  459 HOH D O   
9545 O  O   . HOH DA .   ? 0.2470 0.1946 0.3012 -0.0537 0.0713  -0.0504 460 HOH D O   
9546 O  O   . HOH DA .   ? 0.5095 0.5590 0.2180 0.0314  -0.1027 0.0034  461 HOH D O   
9547 O  O   . HOH DA .   ? 0.2187 0.1434 0.1693 0.0372  0.0568  0.0159  462 HOH D O   
9548 O  O   . HOH DA .   ? 0.4249 0.2390 0.3318 -0.0108 0.0023  -0.0480 463 HOH D O   
9549 O  O   . HOH DA .   ? 0.6381 0.2840 0.7016 0.0826  0.1767  0.1729  464 HOH D O   
9550 O  O   . HOH DA .   ? 0.5525 0.5827 0.4700 0.0899  -0.0487 -0.0825 465 HOH D O   
9551 O  O   . HOH DA .   ? 0.2269 0.1499 0.1604 -0.0231 0.0406  -0.0161 466 HOH D O   
9552 O  O   . HOH DA .   ? 0.2124 0.3457 0.3534 0.0531  0.0750  0.0650  467 HOH D O   
9553 O  O   . HOH DA .   ? 0.3019 0.3057 0.2416 -0.0615 -0.0253 -0.0306 468 HOH D O   
9554 O  O   . HOH DA .   ? 0.3703 0.3251 0.5184 0.0916  0.1130  0.0345  469 HOH D O   
9555 O  O   . HOH DA .   ? 0.4812 0.8100 0.5272 -0.0302 0.0241  0.2940  470 HOH D O   
9556 O  O   . HOH DA .   ? 0.2952 0.4266 0.3186 0.0217  0.0403  0.0881  471 HOH D O   
9557 O  O   . HOH DA .   ? 0.1753 0.1830 0.1542 -0.0083 -0.0013 -0.0055 472 HOH D O   
9558 O  O   . HOH DA .   ? 0.3949 0.3595 0.4393 -0.0429 0.0986  -0.0512 473 HOH D O   
9559 O  O   . HOH DA .   ? 0.2025 0.3465 0.3789 -0.0041 -0.0025 -0.1054 474 HOH D O   
9560 O  O   . HOH DA .   ? 0.6777 0.3573 0.4615 -0.0091 -0.0252 -0.0141 475 HOH D O   
9561 O  O   . HOH DA .   ? 0.2624 0.2800 0.1542 -0.0025 -0.0027 0.0079  476 HOH D O   
9562 O  O   . HOH DA .   ? 0.1456 0.1479 0.1434 -0.0025 0.0008  0.0012  477 HOH D O   
9563 O  O   . HOH DA .   ? 0.1810 0.2213 0.1585 -0.0031 0.0002  0.0079  478 HOH D O   
9564 O  O   . HOH DA .   ? 0.2980 0.2888 0.4282 -0.0199 0.1383  0.0823  479 HOH D O   
9565 O  O   . HOH DA .   ? 0.4189 0.2939 0.2337 0.0233  -0.0247 0.0111  480 HOH D O   
9566 O  O   . HOH DA .   ? 0.3926 0.7059 0.5996 -0.1478 0.1399  -0.1054 481 HOH D O   
9567 O  O   . HOH DA .   ? 0.4066 0.1983 0.3925 -0.0688 -0.1241 0.0750  482 HOH D O   
9568 O  O   . HOH DA .   ? 0.2105 0.1531 0.1909 0.0471  0.0390  0.0100  483 HOH D O   
9569 O  O   . HOH DA .   ? 0.4885 0.7216 0.2025 0.1918  -0.0519 -0.0772 484 HOH D O   
9570 O  O   . HOH DA .   ? 0.3545 0.4194 0.2864 0.0813  -0.0310 -0.0136 485 HOH D O   
9571 O  O   . HOH DA .   ? 0.2852 0.2445 0.5560 -0.0652 0.0363  -0.0968 486 HOH D O   
9572 O  O   . HOH DA .   ? 0.2724 0.2787 0.2935 0.1007  0.0215  0.0079  487 HOH D O   
9573 O  O   . HOH DA .   ? 0.2696 0.4357 0.5116 -0.0655 -0.0267 -0.0469 488 HOH D O   
9574 O  O   . HOH DA .   ? 0.2870 0.2691 0.2700 -0.0479 0.0208  -0.0397 489 HOH D O   
9575 O  O   . HOH DA .   ? 0.4301 0.2992 0.5510 -0.0444 0.0995  -0.0668 490 HOH D O   
9576 O  O   . HOH DA .   ? 0.1367 0.1509 0.1369 -0.0016 -0.0119 -0.0164 491 HOH D O   
9577 O  O   . HOH DA .   ? 0.2824 0.4749 0.8746 0.0941  0.2426  0.2192  492 HOH D O   
9578 O  O   . HOH DA .   ? 0.3395 0.5679 0.3881 0.1371  0.0106  0.0000  493 HOH D O   
9579 O  O   . HOH DA .   ? 0.4459 0.3750 0.6384 -0.1213 -0.0723 -0.0129 494 HOH D O   
9580 O  O   . HOH DA .   ? 0.2989 0.3801 0.3351 0.0835  0.0531  0.0204  495 HOH D O   
9581 O  O   . HOH DA .   ? 0.1847 0.1799 0.2162 0.0055  -0.0215 0.0139  496 HOH D O   
9582 O  O   . HOH DA .   ? 0.5590 0.4136 0.2948 0.0003  0.0881  -0.0873 497 HOH D O   
9583 O  O   . HOH DA .   ? 0.2840 0.2546 0.2780 0.0807  0.0471  0.0281  498 HOH D O   
9584 O  O   . HOH DA .   ? 0.8507 0.6980 0.5976 0.3881  -0.0672 -0.0353 499 HOH D O   
9585 O  O   . HOH DA .   ? 0.2133 0.2209 0.2278 0.0348  0.0416  -0.0167 500 HOH D O   
9586 O  O   . HOH DA .   ? 0.2577 0.2518 0.2955 0.0030  0.0443  0.0020  501 HOH D O   
9587 O  O   . HOH DA .   ? 0.1685 0.1368 0.1700 0.0073  0.0451  0.0271  502 HOH D O   
9588 O  O   . HOH DA .   ? 0.1674 0.1561 0.1434 -0.0049 -0.0115 -0.0069 503 HOH D O   
9589 O  O   . HOH DA .   ? 0.5388 0.2583 0.2389 -0.1599 0.0631  -0.0517 504 HOH D O   
9590 O  O   . HOH DA .   ? 0.3698 0.2902 0.2974 -0.0057 -0.0166 -0.1015 505 HOH D O   
9591 O  O   . HOH DA .   ? 0.5595 0.3893 0.5284 -0.1279 0.2449  0.0370  506 HOH D O   
9592 O  O   . HOH DA .   ? 0.2593 0.6883 0.3995 -0.0849 0.0131  -0.0797 507 HOH D O   
9593 O  O   . HOH DA .   ? 0.2457 0.1606 0.2812 -0.0005 -0.0405 -0.0271 508 HOH D O   
9594 O  O   . HOH DA .   ? 0.4695 0.3788 0.4264 0.0412  -0.0453 0.1054  509 HOH D O   
9595 O  O   . HOH DA .   ? 0.4439 0.3017 0.2754 0.0441  -0.0659 -0.0215 510 HOH D O   
9596 O  O   . HOH DA .   ? 0.5159 0.2150 0.3854 0.0586  0.0072  0.0027  511 HOH D O   
9597 O  O   . HOH DA .   ? 0.2089 0.1303 0.1786 -0.0142 0.0068  -0.0064 512 HOH D O   
9598 O  O   . HOH DA .   ? 0.4242 0.2782 0.7511 0.0311  -0.0740 -0.0911 513 HOH D O   
9599 O  O   . HOH DA .   ? 0.2429 0.3310 0.2590 0.0629  0.0955  0.0816  514 HOH D O   
9600 O  O   . HOH DA .   ? 0.3486 0.4504 0.3416 0.2029  -0.0204 -0.0778 515 HOH D O   
9601 O  O   . HOH DA .   ? 0.4748 0.2732 0.4153 -0.0461 0.0754  -0.1357 516 HOH D O   
9602 O  O   . HOH DA .   ? 0.4382 0.6254 0.4637 -0.2041 -0.0995 0.0732  517 HOH D O   
9603 O  O   . HOH DA .   ? 0.1828 0.1604 0.1766 -0.0331 -0.0244 -0.0087 518 HOH D O   
9604 O  O   . HOH DA .   ? 0.2984 0.3148 0.2412 0.0776  0.0510  0.0166  519 HOH D O   
9605 O  O   . HOH DA .   ? 0.3542 0.2269 0.3037 -0.0262 0.0867  -0.0122 520 HOH D O   
9606 O  O   . HOH DA .   ? 0.4630 0.2439 0.5108 -0.0500 0.1170  -0.0851 521 HOH D O   
9607 O  O   . HOH DA .   ? 0.5756 0.7103 0.5518 0.0116  -0.0453 0.3269  522 HOH D O   
9608 O  O   . HOH DA .   ? 0.5051 0.2933 0.3775 0.0835  -0.0545 -0.0641 523 HOH D O   
9609 O  O   . HOH DA .   ? 0.3735 0.5115 0.4536 0.0218  0.0220  -0.0025 524 HOH D O   
9610 O  O   . HOH DA .   ? 0.3433 0.4252 0.3966 0.0483  -0.0104 -0.1236 525 HOH D O   
9611 O  O   . HOH DA .   ? 0.3280 0.9429 0.4721 0.0110  0.0390  0.3249  526 HOH D O   
9612 O  O   . HOH DA .   ? 0.4478 0.1742 0.1903 0.0801  0.0335  -0.0388 527 HOH D O   
9613 O  O   . HOH DA .   ? 0.4403 0.2823 0.2829 -0.0400 -0.0627 0.0200  528 HOH D O   
9614 O  O   . HOH DA .   ? 0.3323 0.3278 0.5218 -0.0209 0.0162  -0.0838 529 HOH D O   
9615 O  O   . HOH DA .   ? 0.4403 0.4353 0.4123 0.0700  0.1021  0.0442  530 HOH D O   
9616 O  O   . HOH DA .   ? 0.3753 0.2135 0.2366 0.0822  0.0140  0.0200  531 HOH D O   
9617 O  O   . HOH DA .   ? 0.5988 0.4622 0.3878 -0.0019 -0.1857 0.0316  532 HOH D O   
9618 O  O   . HOH DA .   ? 0.4265 0.2235 0.2306 -0.0871 -0.0580 0.0465  533 HOH D O   
9619 O  O   . HOH DA .   ? 0.4146 0.3652 0.4130 0.0588  0.0625  0.0168  534 HOH D O   
9620 O  O   . HOH DA .   ? 0.3529 0.5987 0.3978 -0.0234 0.0554  -0.1182 535 HOH D O   
9621 O  O   . HOH DA .   ? 0.4967 0.3791 0.4679 0.0795  0.1476  0.0454  536 HOH D O   
9622 O  O   . HOH DA .   ? 0.3203 0.2077 0.1484 -0.0433 0.0033  -0.0321 537 HOH D O   
9623 O  O   . HOH DA .   ? 0.3364 0.3155 0.7910 -0.0701 -0.0539 0.2121  538 HOH D O   
9624 O  O   . HOH DA .   ? 0.3422 0.2232 0.3339 -0.0555 -0.0630 0.0410  539 HOH D O   
9625 O  O   . HOH DA .   ? 0.3759 0.4463 0.4803 0.0465  0.1227  -0.0388 540 HOH D O   
9626 O  O   . HOH DA .   ? 0.2301 0.2301 0.3025 -0.0043 0.0462  0.0080  541 HOH D O   
9627 O  O   . HOH DA .   ? 0.2934 0.3574 0.3215 0.0024  0.0436  0.0518  542 HOH D O   
9628 O  O   . HOH DA .   ? 0.2591 0.1823 0.3463 -0.0302 0.0374  -0.0170 543 HOH D O   
9629 O  O   . HOH DA .   ? 0.3177 0.4880 0.3687 0.1636  0.0010  0.0065  544 HOH D O   
9630 O  O   . HOH DA .   ? 0.4005 0.3143 0.2034 -0.1550 -0.0653 0.0289  545 HOH D O   
9631 O  O   . HOH DA .   ? 0.3986 0.3111 0.4163 -0.1564 0.0230  -0.0552 546 HOH D O   
9632 O  O   . HOH DA .   ? 0.4363 0.2967 0.5094 0.0442  0.0592  -0.0003 547 HOH D O   
9633 O  O   . HOH DA .   ? 0.5087 0.6204 0.6789 0.0290  -0.2829 -0.1234 548 HOH D O   
9634 O  O   . HOH DA .   ? 0.5498 0.4375 0.8368 0.0082  0.3233  0.0805  549 HOH D O   
9635 O  O   . HOH DA .   ? 0.2407 0.1965 0.2260 0.0119  0.0074  -0.0402 550 HOH D O   
9636 O  O   . HOH DA .   ? 0.2188 0.2006 0.3300 -0.0514 0.0261  -0.0253 551 HOH D O   
9637 O  O   . HOH DA .   ? 0.3974 0.4048 0.5074 0.0216  0.1227  0.1743  552 HOH D O   
9638 O  O   . HOH DA .   ? 0.3436 0.6057 0.6808 0.0429  0.1621  0.1175  553 HOH D O   
9639 O  O   . HOH DA .   ? 0.2851 0.4969 0.2477 -0.1094 0.0310  -0.0818 554 HOH D O   
9640 O  O   . HOH DA .   ? 0.3843 0.4629 0.3759 0.0452  -0.1055 -0.0602 555 HOH D O   
9641 O  O   . HOH DA .   ? 0.4290 0.2846 0.1728 0.0030  0.0352  -0.0231 556 HOH D O   
9642 O  O   . HOH DA .   ? 0.2196 0.3448 0.2063 -0.0020 -0.0055 -0.0761 557 HOH D O   
9643 O  O   . HOH DA .   ? 0.4334 0.5157 0.3105 0.1050  0.0889  0.1120  558 HOH D O   
9644 O  O   . HOH DA .   ? 0.6773 0.2370 0.6136 0.0346  -0.0670 0.1462  559 HOH D O   
9645 O  O   . HOH DA .   ? 0.2385 1.7678 0.7425 -0.1323 0.3796  -0.6144 560 HOH D O   
9646 O  O   . HOH DA .   ? 0.2064 0.3620 0.4039 -0.0008 -0.0201 0.0626  561 HOH D O   
9647 O  O   . HOH DA .   ? 0.1784 0.1542 0.1509 -0.0111 0.0200  -0.0129 562 HOH D O   
9648 O  O   . HOH DA .   ? 0.5832 0.3822 0.3694 0.0378  -0.0833 -0.0774 563 HOH D O   
9649 O  O   . HOH DA .   ? 0.2041 0.1781 0.1681 -0.0171 0.0005  0.0064  564 HOH D O   
9650 O  O   . HOH DA .   ? 0.4928 0.5526 0.3603 0.0648  0.0758  0.0542  565 HOH D O   
9651 O  O   . HOH DA .   ? 0.5764 0.3450 0.7222 0.0047  0.1169  -0.0749 566 HOH D O   
9652 O  O   . HOH DA .   ? 0.3671 0.7288 0.2667 0.0205  0.0425  0.0342  567 HOH D O   
9653 O  O   . HOH DA .   ? 0.5453 0.6784 0.5305 -0.3281 0.2513  -0.2019 568 HOH D O   
9654 O  O   . HOH DA .   ? 0.1703 0.1751 0.2122 -0.0148 0.0406  0.0184  569 HOH D O   
9655 O  O   . HOH DA .   ? 0.2781 0.3504 0.2609 0.1039  0.0586  -0.0153 570 HOH D O   
9656 O  O   . HOH DA .   ? 0.3009 0.2998 0.3820 0.0168  0.0273  -0.0677 571 HOH D O   
9657 O  O   . HOH DA .   ? 0.4716 0.2687 0.2642 -0.0429 0.0423  -0.0624 572 HOH D O   
9658 O  O   . HOH DA .   ? 0.4281 0.4955 0.3621 -0.0715 -0.0868 -0.0153 573 HOH D O   
9659 O  O   . HOH DA .   ? 0.2960 0.3824 0.4725 -0.0933 -0.0218 0.0772  574 HOH D O   
9660 O  O   . HOH DA .   ? 0.2222 0.3010 0.3186 0.0295  -0.0012 -0.0626 575 HOH D O   
9661 O  O   . HOH DA .   ? 0.5632 0.4858 0.3454 0.0141  -0.0353 -0.0761 576 HOH D O   
9662 O  O   . HOH DA .   ? 0.4295 0.3853 0.2184 0.1507  0.0081  -0.0541 577 HOH D O   
9663 O  O   . HOH DA .   ? 0.2676 0.2050 0.3305 -0.0038 -0.0265 0.0683  578 HOH D O   
9664 O  O   . HOH DA .   ? 0.4531 0.3267 0.4030 0.0652  -0.0466 -0.0034 579 HOH D O   
9665 O  O   . HOH DA .   ? 0.3652 0.4259 0.2750 0.0908  0.0084  0.0124  580 HOH D O   
9666 O  O   . HOH DA .   ? 0.4220 0.4164 0.3776 0.0911  -0.1268 -0.1370 581 HOH D O   
9667 O  O   . HOH DA .   ? 0.4755 0.2931 0.5984 0.1447  -0.0100 0.0961  582 HOH D O   
9668 O  O   . HOH DA .   ? 0.3428 0.3525 0.6521 0.0718  -0.0306 0.2364  583 HOH D O   
9669 O  O   . HOH DA .   ? 0.3652 0.4044 0.3510 -0.0280 -0.0640 0.1623  584 HOH D O   
9670 O  O   . HOH DA .   ? 0.3250 0.3323 0.3805 -0.1078 0.1171  0.0458  585 HOH D O   
9671 O  O   . HOH DA .   ? 0.4428 0.4572 0.3905 0.0532  -0.0685 0.0260  586 HOH D O   
9672 O  O   . HOH DA .   ? 0.5134 0.2614 0.3420 -0.0725 -0.1054 -0.0666 587 HOH D O   
9673 O  O   . HOH DA .   ? 0.2308 0.1890 0.2601 -0.0157 0.0089  -0.0145 588 HOH D O   
9674 O  O   . HOH DA .   ? 0.4606 0.2621 0.2728 0.0122  0.0352  -0.0480 589 HOH D O   
9675 O  O   . HOH DA .   ? 0.4070 0.4487 0.3443 -0.0748 0.0926  -0.0374 590 HOH D O   
9676 O  O   . HOH DA .   ? 0.4049 0.4574 0.3600 -0.0176 0.0344  -0.0222 591 HOH D O   
9677 O  O   . HOH DA .   ? 0.4044 0.3603 0.3497 -0.0697 -0.0282 0.0880  592 HOH D O   
9678 O  O   . HOH DA .   ? 0.4749 0.2139 0.9773 0.0605  -0.1025 -0.0048 593 HOH D O   
9679 O  O   . HOH DA .   ? 0.3215 0.3793 0.7366 0.0103  -0.0528 -0.0431 594 HOH D O   
9680 O  O   . HOH DA .   ? 0.4002 0.2037 0.3263 -0.0171 -0.0458 -0.0195 595 HOH D O   
9681 O  O   . HOH DA .   ? 0.5470 0.9031 0.4887 -0.0314 -0.1260 0.1253  596 HOH D O   
9682 O  O   . HOH DA .   ? 0.6980 0.4647 0.3347 -0.1928 0.0113  -0.0452 597 HOH D O   
9683 O  O   . HOH DA .   ? 0.2755 0.2748 0.3312 0.0257  -0.0397 0.0085  598 HOH D O   
9684 O  O   . HOH DA .   ? 0.5199 0.3432 0.5056 -0.1346 -0.0507 0.1198  599 HOH D O   
9685 O  O   . HOH DA .   ? 0.4354 0.1597 0.4436 0.0517  0.0262  -0.0583 600 HOH D O   
9686 O  O   . HOH DA .   ? 0.5259 0.3798 0.4803 0.0218  0.0708  -0.0925 601 HOH D O   
9687 O  O   . HOH DA .   ? 0.3260 0.2309 0.2700 -0.0190 -0.0216 -0.0080 602 HOH D O   
9688 O  O   . HOH DA .   ? 0.7439 0.7968 0.2850 -0.1517 -0.0766 0.1426  603 HOH D O   
9689 O  O   . HOH DA .   ? 0.2106 0.3660 0.2994 0.0069  -0.0142 -0.0477 604 HOH D O   
9690 O  O   . HOH DA .   ? 0.6576 0.3255 0.5726 0.0076  -0.1455 0.0441  605 HOH D O   
9691 O  O   . HOH DA .   ? 0.2657 0.3321 0.5281 -0.1585 0.0539  0.0479  606 HOH D O   
9692 O  O   . HOH DA .   ? 0.3943 0.6208 0.7034 0.0728  -0.1212 0.0754  607 HOH D O   
9693 O  O   . HOH DA .   ? 0.7975 0.3301 0.5145 -0.0096 -0.1596 0.0972  608 HOH D O   
9694 O  O   . HOH DA .   ? 0.4793 0.5044 0.4504 0.0137  0.1489  -0.1263 609 HOH D O   
9695 O  O   . HOH DA .   ? 0.5037 0.4851 0.4867 -0.0205 -0.0297 -0.0024 610 HOH D O   
9696 O  O   . HOH DA .   ? 0.2611 0.5295 0.4108 0.0107  -0.0414 0.1843  611 HOH D O   
9697 O  O   . HOH DA .   ? 0.3421 0.4636 0.5310 -0.0779 0.0324  -0.1612 612 HOH D O   
9698 O  O   . HOH DA .   ? 0.2679 0.1941 0.2069 -0.0458 -0.0027 -0.0068 613 HOH D O   
9699 O  O   . HOH DA .   ? 0.8241 0.5292 0.4818 0.2369  0.0193  -0.0631 614 HOH D O   
9700 O  O   . HOH DA .   ? 0.2708 0.2815 0.3244 0.0277  0.0672  0.0375  615 HOH D O   
9701 O  O   . HOH DA .   ? 0.3679 0.6752 0.8144 0.0068  -0.1129 -0.0825 616 HOH D O   
9702 O  O   . HOH DA .   ? 0.4170 0.3264 0.3629 -0.1021 0.0117  0.0100  617 HOH D O   
9703 O  O   . HOH DA .   ? 0.6594 0.6828 0.5116 0.2113  0.0402  0.2191  618 HOH D O   
9704 O  O   . HOH DA .   ? 0.4581 0.3212 0.3332 -0.0675 0.0480  0.0743  619 HOH D O   
9705 O  O   . HOH DA .   ? 0.5723 0.3874 0.4630 0.0141  0.0674  0.0879  620 HOH D O   
9706 O  O   . HOH DA .   ? 0.4648 0.4850 1.1423 0.0037  0.0346  0.0739  621 HOH D O   
9707 O  O   . HOH DA .   ? 0.4636 0.3401 0.4426 0.0943  0.2400  0.0792  622 HOH D O   
9708 O  O   . HOH DA .   ? 0.3264 0.3441 0.3816 0.0558  0.1146  0.0181  623 HOH D O   
9709 O  O   . HOH DA .   ? 0.2687 0.5189 0.2099 0.0266  -0.0004 0.0040  624 HOH D O   
9710 O  O   . HOH DA .   ? 0.6516 0.6131 0.5197 -0.1110 0.1866  0.0824  625 HOH D O   
9711 O  O   . HOH DA .   ? 0.5819 0.6849 0.5330 -0.0272 -0.1205 -0.2173 626 HOH D O   
9712 O  O   . HOH DA .   ? 0.3646 0.6447 0.4077 0.0178  -0.0029 0.0411  627 HOH D O   
9713 O  O   . HOH DA .   ? 0.2305 0.2319 0.2268 -0.0089 -0.0192 0.0435  628 HOH D O   
9714 O  O   . HOH DA .   ? 0.5384 0.7495 0.4289 0.1485  0.0290  0.1311  629 HOH D O   
9715 O  O   . HOH DA .   ? 0.2822 0.3257 0.3274 0.0153  -0.0333 0.0214  630 HOH D O   
9716 O  O   . HOH DA .   ? 0.5842 0.3985 0.4340 0.0705  -0.0911 0.0086  631 HOH D O   
9717 O  O   . HOH DA .   ? 0.5432 0.3638 0.7005 0.1267  -0.0300 -0.2198 632 HOH D O   
9718 O  O   . HOH DA .   ? 0.4730 0.6377 0.3933 -0.0976 -0.0054 0.1353  633 HOH D O   
9719 O  O   . HOH DA .   ? 0.2709 0.4778 0.4807 -0.0304 0.0403  0.1016  634 HOH D O   
9720 O  O   . HOH DA .   ? 0.6893 0.2933 0.6189 0.1441  -0.0274 0.0434  635 HOH D O   
9721 O  O   . HOH DA .   ? 0.3947 0.3164 0.4089 -0.0098 -0.0206 -0.0051 636 HOH D O   
9722 O  O   . HOH DA .   ? 0.2843 0.3352 0.4331 0.0653  0.0139  -0.0313 637 HOH D O   
9723 O  O   . HOH DA .   ? 0.4723 0.3677 0.3328 0.0864  -0.0867 -0.0323 638 HOH D O   
9724 O  O   . HOH DA .   ? 0.3647 0.3493 0.2858 -0.0029 0.0612  0.0506  639 HOH D O   
9725 O  O   . HOH DA .   ? 0.3264 0.4185 0.2938 0.0517  0.0691  0.0595  640 HOH D O   
9726 O  O   . HOH DA .   ? 0.3525 0.4415 0.5031 0.0523  0.0115  -0.0696 641 HOH D O   
9727 O  O   . HOH DA .   ? 0.3953 0.4175 0.4373 -0.0589 0.1187  -0.0400 642 HOH D O   
9728 O  O   . HOH DA .   ? 0.2437 0.3674 0.3134 0.0359  -0.0586 0.0192  643 HOH D O   
9729 O  O   . HOH DA .   ? 0.3454 0.3771 0.2464 0.0185  -0.0550 0.0057  644 HOH D O   
9730 O  O   . HOH DA .   ? 0.3689 0.3651 0.4499 0.0987  -0.0718 -0.0035 645 HOH D O   
9731 O  O   . HOH DA .   ? 0.4714 0.5858 0.3285 0.0049  0.0357  0.0558  646 HOH D O   
9732 O  O   . HOH DA .   ? 0.8975 0.2451 0.5844 0.0659  -0.0681 -0.0226 647 HOH D O   
9733 O  O   . HOH DA .   ? 0.6154 0.1906 0.4945 0.0473  0.1927  0.0816  648 HOH D O   
9734 O  O   . HOH DA .   ? 0.5772 0.4238 0.4907 0.1277  0.0629  0.0635  649 HOH D O   
9735 O  O   . HOH DA .   ? 0.3316 0.3034 0.3125 0.1034  0.1177  0.0423  650 HOH D O   
9736 O  O   . HOH DA .   ? 0.3868 0.5195 0.5475 0.0238  -0.0095 -0.1521 651 HOH D O   
9737 O  O   . HOH DA .   ? 0.4044 0.5395 0.3806 0.0034  -0.1219 -0.0566 652 HOH D O   
9738 O  O   . HOH DA .   ? 0.3783 0.3569 0.3166 0.0879  0.0027  -0.1495 653 HOH D O   
9739 O  O   . HOH DA .   ? 0.3143 0.3591 0.2682 0.0241  0.0596  -0.0100 654 HOH D O   
9740 O  O   . HOH DA .   ? 0.6573 0.2955 0.8490 0.0194  -0.0026 -0.1895 655 HOH D O   
9741 O  O   . HOH DA .   ? 0.3717 0.4714 0.2652 -0.0857 0.0512  0.1084  656 HOH D O   
9742 O  O   . HOH DA .   ? 0.4718 0.3424 0.3219 0.1298  0.1106  -0.0049 657 HOH D O   
9743 O  O   . HOH DA .   ? 0.5328 0.6093 0.4861 -0.1544 0.1571  0.0358  658 HOH D O   
9744 O  O   . HOH DA .   ? 0.5341 0.2935 0.7355 -0.0928 0.0046  0.0587  659 HOH D O   
9745 O  O   . HOH DA .   ? 0.7673 0.6955 0.4833 -0.3464 0.0925  -0.1939 660 HOH D O   
9746 O  O   . HOH DA .   ? 0.3547 0.4885 0.5167 0.0686  -0.1009 -0.1213 661 HOH D O   
9747 O  O   . HOH DA .   ? 0.6793 0.4100 0.5299 0.0066  -0.0985 0.0298  662 HOH D O   
# 
